data_9BXW
# 
_entry.id   9BXW 
# 
_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   9BXW         pdb_00009bxw 10.2210/pdb9bxw/pdb 
WWPDB D_1000284353 ?            ?                   
# 
_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                        9BXW 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marzena.pazgier@usuhs.edu 
_pdbx_contact_author.name_first         Marzena 
_pdbx_contact_author.name_last          Pazgier 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0594-5057 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tolbert, W.D.' 1 ? 
'Niu, L.'       2 ? 
'Pazgier, M.'   3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1961 
_citation.page_last                 1969 
_citation.title                     
'Optimization of a Piperidine CD4-Mimetic Scaffold Sensitizing HIV-1 Infected Cells to Antibody-Dependent Cellular Cytotoxicity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00403 
_citation.pdbx_database_id_PubMed   39563795 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, D.'                1  ?                   
primary 'Niu, L.'                2  ?                   
primary 'Ding, S.'               3  ?                   
primary 'Zhu, H.'                4  ?                   
primary 'Tolbert, W.D.'          5  ?                   
primary 'Medjahed, H.'           6  ?                   
primary 'Beaudoin-Bussieres, G.' 7  ?                   
primary 'Abrams, C.'             8  0000-0002-1240-0816 
primary 'Finzi, A.'              9  ?                   
primary 'Pazgier, M.'            10 ?                   
primary 'Smith 3rd, A.B.'        11 0000-0002-1712-8567 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'HIV-1 LM/HS clade A/E CRF01 gp120 core' 39452.723 1  ? 'H61Y, Q105H, V108I, H375S, N474D, I475M, K476R' ? ? 
2 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   9  ? ?                                                ? ? 
3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   1  ? ? ? ? 
4 non-polymer syn 
'(3S,5R)-1-[4-(2-carbamimidamidoethyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)-5-(hydroxymethyl)piperidine-3-carboxamide' 
483.967   1  ? ?                                                ? ? 
5 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL' 118.174   2  ? ?                                                ? ? 
6 water       nat water 18.015    83 ? ?                                                ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
3 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE   
4 
'(3S,5R)-1-[4-(2-carbamimidamidoethyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)-5-(hydroxymethyl)piperidine-3-carboxamide' 
A1ATD 
5 '(4S)-2-METHYL-2,4-PENTANEDIOL' MPD   
6 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 
A1ATD non-polymer                  . 
'(3S,5R)-1-[4-(2-carbamimidamidoethyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)-5-(hydroxymethyl)piperidine-3-carboxamide' 
? 'C21 H31 Cl F N7 O3' 483.967 
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 
MPD   non-polymer                  . '(4S)-2-METHYL-2,4-PENTANEDIOL' ? 'C6 H14 O2'          118.174 
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  122 122 LEU LEU A . n 
A 1 82  THR 82  123 123 THR THR A . n 
A 1 83  GLY 83  124 124 GLY GLY A . n 
A 1 84  GLY 84  198 198 GLY GLY A . n 
A 1 85  SER 85  199 199 SER SER A . n 
A 1 86  VAL 86  200 200 VAL VAL A . n 
A 1 87  ILE 87  201 201 ILE ILE A . n 
A 1 88  LYS 88  202 202 LYS LYS A . n 
A 1 89  GLN 89  203 203 GLN GLN A . n 
A 1 90  ALA 90  204 204 ALA ALA A . n 
A 1 91  CYS 91  205 205 CYS CYS A . n 
A 1 92  PRO 92  206 206 PRO PRO A . n 
A 1 93  LYS 93  207 207 LYS LYS A . n 
A 1 94  ILE 94  208 208 ILE ILE A . n 
A 1 95  SER 95  209 209 SER SER A . n 
A 1 96  PHE 96  210 210 PHE PHE A . n 
A 1 97  ASP 97  211 211 ASP ASP A . n 
A 1 98  PRO 98  212 212 PRO PRO A . n 
A 1 99  ILE 99  213 213 ILE ILE A . n 
A 1 100 PRO 100 214 214 PRO PRO A . n 
A 1 101 ILE 101 215 215 ILE ILE A . n 
A 1 102 HIS 102 216 216 HIS HIS A . n 
A 1 103 TYR 103 217 217 TYR TYR A . n 
A 1 104 CYS 104 218 218 CYS CYS A . n 
A 1 105 THR 105 219 219 THR THR A . n 
A 1 106 PRO 106 220 220 PRO PRO A . n 
A 1 107 ALA 107 221 221 ALA ALA A . n 
A 1 108 GLY 108 222 222 GLY GLY A . n 
A 1 109 TYR 109 223 223 TYR TYR A . n 
A 1 110 VAL 110 224 224 VAL VAL A . n 
A 1 111 ILE 111 225 225 ILE ILE A . n 
A 1 112 LEU 112 226 226 LEU LEU A . n 
A 1 113 LYS 113 227 227 LYS LYS A . n 
A 1 114 CYS 114 228 228 CYS CYS A . n 
A 1 115 ASN 115 229 229 ASN ASN A . n 
A 1 116 ASP 116 230 230 ASP ASP A . n 
A 1 117 LYS 117 231 231 LYS LYS A . n 
A 1 118 ASN 118 232 232 ASN ASN A . n 
A 1 119 PHE 119 233 233 PHE PHE A . n 
A 1 120 ASN 120 234 234 ASN ASN A . n 
A 1 121 GLY 121 235 235 GLY GLY A . n 
A 1 122 THR 122 236 236 THR THR A . n 
A 1 123 GLY 123 237 237 GLY GLY A . n 
A 1 124 PRO 124 238 238 PRO PRO A . n 
A 1 125 CYS 125 239 239 CYS CYS A . n 
A 1 126 LYS 126 240 240 LYS LYS A . n 
A 1 127 ASN 127 241 241 ASN ASN A . n 
A 1 128 VAL 128 242 242 VAL VAL A . n 
A 1 129 SER 129 243 243 SER SER A . n 
A 1 130 SER 130 244 244 SER SER A . n 
A 1 131 VAL 131 245 245 VAL VAL A . n 
A 1 132 GLN 132 246 246 GLN GLN A . n 
A 1 133 CYS 133 247 247 CYS CYS A . n 
A 1 134 THR 134 248 248 THR THR A . n 
A 1 135 HIS 135 249 249 HIS HIS A . n 
A 1 136 GLY 136 250 250 GLY GLY A . n 
A 1 137 ILE 137 251 251 ILE ILE A . n 
A 1 138 LYS 138 252 252 LYS LYS A . n 
A 1 139 PRO 139 253 253 PRO PRO A . n 
A 1 140 VAL 140 254 254 VAL VAL A . n 
A 1 141 VAL 141 255 255 VAL VAL A . n 
A 1 142 SER 142 256 256 SER SER A . n 
A 1 143 THR 143 257 257 THR THR A . n 
A 1 144 GLN 144 258 258 GLN GLN A . n 
A 1 145 LEU 145 259 259 LEU LEU A . n 
A 1 146 LEU 146 260 260 LEU LEU A . n 
A 1 147 LEU 147 261 261 LEU LEU A . n 
A 1 148 ASN 148 262 262 ASN ASN A . n 
A 1 149 GLY 149 263 263 GLY GLY A . n 
A 1 150 SER 150 264 264 SER SER A . n 
A 1 151 LEU 151 265 265 LEU LEU A . n 
A 1 152 ALA 152 266 266 ALA ALA A . n 
A 1 153 GLU 153 267 267 GLU GLU A . n 
A 1 154 GLU 154 268 268 GLU GLU A . n 
A 1 155 GLU 155 269 269 GLU GLU A . n 
A 1 156 ILE 156 270 270 ILE ILE A . n 
A 1 157 ILE 157 271 271 ILE ILE A . n 
A 1 158 ILE 158 272 272 ILE ILE A . n 
A 1 159 ARG 159 273 273 ARG ARG A . n 
A 1 160 SER 160 274 274 SER SER A . n 
A 1 161 GLU 161 275 275 GLU GLU A . n 
A 1 162 ASN 162 276 276 ASN ASN A . n 
A 1 163 LEU 163 277 277 LEU LEU A . n 
A 1 164 THR 164 278 278 THR THR A . n 
A 1 165 ASN 165 279 279 ASN ASN A . n 
A 1 166 ASN 166 280 280 ASN ASN A . n 
A 1 167 ALA 167 281 281 ALA ALA A . n 
A 1 168 LYS 168 282 282 LYS LYS A . n 
A 1 169 THR 169 283 283 THR THR A . n 
A 1 170 ILE 170 284 284 ILE ILE A . n 
A 1 171 ILE 171 285 285 ILE ILE A . n 
A 1 172 VAL 172 286 286 VAL VAL A . n 
A 1 173 HIS 173 287 287 HIS HIS A . n 
A 1 174 LEU 174 288 288 LEU LEU A . n 
A 1 175 ASN 175 289 289 ASN ASN A . n 
A 1 176 LYS 176 290 290 LYS LYS A . n 
A 1 177 SER 177 291 291 SER SER A . n 
A 1 178 VAL 178 292 292 VAL VAL A . n 
A 1 179 GLU 179 293 293 GLU GLU A . n 
A 1 180 ILE 180 294 294 ILE ILE A . n 
A 1 181 ASN 181 295 295 ASN ASN A . n 
A 1 182 CYS 182 296 296 CYS CYS A . n 
A 1 183 THR 183 297 297 THR THR A . n 
A 1 184 ARG 184 298 298 ARG ARG A . n 
A 1 185 PRO 185 299 299 PRO PRO A . n 
A 1 186 SER 186 300 300 SER SER A . n 
A 1 187 ASN 187 301 301 ASN ASN A . n 
A 1 188 GLY 188 318 ?   ?   ?   A . n 
A 1 189 GLY 189 319 ?   ?   ?   A . n 
A 1 190 SER 190 320 ?   ?   ?   A . n 
A 1 191 GLY 191 321 ?   ?   ?   A . n 
A 1 192 SER 192 322 ?   ?   ?   A . n 
A 1 193 GLY 193 323 ?   ?   ?   A . n 
A 1 194 GLY 194 324 ?   ?   ?   A . n 
A 1 195 ASP 195 325 325 ASP ASP A . n 
A 1 196 ILE 196 326 326 ILE ILE A . n 
A 1 197 ARG 197 327 327 ARG ARG A . n 
A 1 198 LYS 198 328 328 LYS LYS A . n 
A 1 199 ALA 199 329 329 ALA ALA A . n 
A 1 200 TYR 200 330 330 TYR TYR A . n 
A 1 201 CYS 201 331 331 CYS CYS A . n 
A 1 202 GLU 202 332 332 GLU GLU A . n 
A 1 203 ILE 203 333 333 ILE ILE A . n 
A 1 204 ASN 204 334 334 ASN ASN A . n 
A 1 205 GLY 205 335 335 GLY GLY A . n 
A 1 206 THR 206 336 336 THR THR A . n 
A 1 207 LYS 207 337 337 LYS LYS A . n 
A 1 208 TRP 208 338 338 TRP TRP A . n 
A 1 209 ASN 209 339 339 ASN ASN A . n 
A 1 210 LYS 210 340 340 LYS LYS A . n 
A 1 211 VAL 211 341 341 VAL VAL A . n 
A 1 212 LEU 212 342 342 LEU LEU A . n 
A 1 213 LYS 213 343 343 LYS LYS A . n 
A 1 214 GLN 214 344 344 GLN GLN A . n 
A 1 215 VAL 215 345 345 VAL VAL A . n 
A 1 216 THR 216 346 346 THR THR A . n 
A 1 217 GLU 217 347 347 GLU GLU A . n 
A 1 218 LYS 218 348 348 LYS LYS A . n 
A 1 219 LEU 219 349 349 LEU LEU A . n 
A 1 220 LYS 220 350 350 LYS LYS A . n 
A 1 221 GLU 221 351 351 GLU GLU A . n 
A 1 222 HIS 222 352 352 HIS HIS A . n 
A 1 223 PHE 223 353 353 PHE PHE A . n 
A 1 224 ASN 224 354 354 ASN ASN A . n 
A 1 225 ASN 225 355 355 ASN ASN A . n 
A 1 226 LYS 226 357 357 LYS LYS A . n 
A 1 227 THR 227 358 358 THR THR A . n 
A 1 228 ILE 228 359 359 ILE ILE A . n 
A 1 229 ILE 229 360 360 ILE ILE A . n 
A 1 230 PHE 230 361 361 PHE PHE A . n 
A 1 231 GLN 231 362 362 GLN GLN A . n 
A 1 232 PRO 232 363 363 PRO PRO A . n 
A 1 233 PRO 233 364 364 PRO PRO A . n 
A 1 234 SER 234 365 365 SER SER A . n 
A 1 235 GLY 235 366 366 GLY GLY A . n 
A 1 236 GLY 236 367 367 GLY GLY A . n 
A 1 237 ASP 237 368 368 ASP ASP A . n 
A 1 238 LEU 238 369 369 LEU LEU A . n 
A 1 239 GLU 239 370 370 GLU GLU A . n 
A 1 240 ILE 240 371 371 ILE ILE A . n 
A 1 241 THR 241 372 372 THR THR A . n 
A 1 242 MET 242 373 373 MET MET A . n 
A 1 243 HIS 243 374 374 HIS HIS A . n 
A 1 244 SER 244 375 375 SER SER A . n 
A 1 245 PHE 245 376 376 PHE PHE A . n 
A 1 246 ASN 246 377 377 ASN ASN A . n 
A 1 247 CYS 247 378 378 CYS CYS A . n 
A 1 248 ARG 248 379 379 ARG ARG A . n 
A 1 249 GLY 249 380 380 GLY GLY A . n 
A 1 250 GLU 250 381 381 GLU GLU A . n 
A 1 251 PHE 251 382 382 PHE PHE A . n 
A 1 252 PHE 252 383 383 PHE PHE A . n 
A 1 253 TYR 253 384 384 TYR TYR A . n 
A 1 254 CYS 254 385 385 CYS CYS A . n 
A 1 255 ASN 255 386 386 ASN ASN A . n 
A 1 256 THR 256 387 387 THR THR A . n 
A 1 257 THR 257 388 388 THR THR A . n 
A 1 258 GLN 258 389 389 GLN GLN A . n 
A 1 259 LEU 259 390 390 LEU LEU A . n 
A 1 260 PHE 260 391 391 PHE PHE A . n 
A 1 261 ASN 261 392 392 ASN ASN A . n 
A 1 262 ASN 262 393 393 ASN ASN A . n 
A 1 263 THR 263 394 394 THR THR A . n 
A 1 264 CYS 264 395 395 CYS CYS A . n 
A 1 265 ILE 265 402 ?   ?   ?   A . n 
A 1 266 GLY 266 403 ?   ?   ?   A . n 
A 1 267 ASN 267 404 ?   ?   ?   A . n 
A 1 268 GLU 268 405 ?   ?   ?   A . n 
A 1 269 THR 269 406 ?   ?   ?   A . n 
A 1 270 MET 270 407 ?   ?   ?   A . n 
A 1 271 LYS 271 408 408 LYS LYS A . n 
A 1 272 GLY 272 409 409 GLY GLY A . n 
A 1 273 CYS 273 410 410 CYS CYS A . n 
A 1 274 ASN 274 411 411 ASN ASN A . n 
A 1 275 GLY 275 412 412 GLY GLY A . n 
A 1 276 THR 276 413 413 THR THR A . n 
A 1 277 ILE 277 414 414 ILE ILE A . n 
A 1 278 THR 278 415 415 THR THR A . n 
A 1 279 LEU 279 416 416 LEU LEU A . n 
A 1 280 PRO 280 417 417 PRO PRO A . n 
A 1 281 CYS 281 418 418 CYS CYS A . n 
A 1 282 LYS 282 419 419 LYS LYS A . n 
A 1 283 ILE 283 420 420 ILE ILE A . n 
A 1 284 LYS 284 421 421 LYS LYS A . n 
A 1 285 GLN 285 422 422 GLN GLN A . n 
A 1 286 ILE 286 423 423 ILE ILE A . n 
A 1 287 ILE 287 424 424 ILE ILE A . n 
A 1 288 ASN 288 425 425 ASN ASN A . n 
A 1 289 MET 289 426 426 MET MET A . n 
A 1 290 TRP 290 427 427 TRP TRP A . n 
A 1 291 GLN 291 428 428 GLN GLN A . n 
A 1 292 GLY 292 429 429 GLY GLY A . n 
A 1 293 THR 293 430 430 THR THR A . n 
A 1 294 GLY 294 431 431 GLY GLY A . n 
A 1 295 GLN 295 432 432 GLN GLN A . n 
A 1 296 ALA 296 433 433 ALA ALA A . n 
A 1 297 MET 297 434 434 MET MET A . n 
A 1 298 TYR 298 435 435 TYR TYR A . n 
A 1 299 ALA 299 436 436 ALA ALA A . n 
A 1 300 PRO 300 437 437 PRO PRO A . n 
A 1 301 PRO 301 438 438 PRO PRO A . n 
A 1 302 ILE 302 439 439 ILE ILE A . n 
A 1 303 ASP 303 440 440 ASP ASP A . n 
A 1 304 GLY 304 441 441 GLY GLY A . n 
A 1 305 LYS 305 442 442 LYS LYS A . n 
A 1 306 ILE 306 443 443 ILE ILE A . n 
A 1 307 ASN 307 444 444 ASN ASN A . n 
A 1 308 CYS 308 445 445 CYS CYS A . n 
A 1 309 VAL 309 446 446 VAL VAL A . n 
A 1 310 SER 310 447 447 SER SER A . n 
A 1 311 ASN 311 448 448 ASN ASN A . n 
A 1 312 ILE 312 449 449 ILE ILE A . n 
A 1 313 THR 313 450 450 THR THR A . n 
A 1 314 GLY 314 451 451 GLY GLY A . n 
A 1 315 ILE 315 452 452 ILE ILE A . n 
A 1 316 LEU 316 453 453 LEU LEU A . n 
A 1 317 LEU 317 454 454 LEU LEU A . n 
A 1 318 THR 318 455 455 THR THR A . n 
A 1 319 ARG 319 456 456 ARG ARG A . n 
A 1 320 ASP 320 457 457 ASP ASP A . n 
A 1 321 GLY 321 458 458 GLY GLY A . n 
A 1 322 GLY 322 459 459 GLY GLY A . n 
A 1 323 ALA 323 460 460 ALA ALA A . n 
A 1 324 ASN 324 461 461 ASN ASN A . n 
A 1 325 ASN 325 462 462 ASN ASN A . n 
A 1 326 THR 326 463 463 THR THR A . n 
A 1 327 SER 327 464 464 SER SER A . n 
A 1 328 ASN 328 465 465 ASN ASN A . n 
A 1 329 GLU 329 466 466 GLU GLU A . n 
A 1 330 THR 330 467 467 THR THR A . n 
A 1 331 PHE 331 468 468 PHE PHE A . n 
A 1 332 ARG 332 469 469 ARG ARG A . n 
A 1 333 PRO 333 470 470 PRO PRO A . n 
A 1 334 GLY 334 471 471 GLY GLY A . n 
A 1 335 GLY 335 472 472 GLY GLY A . n 
A 1 336 GLY 336 473 473 GLY GLY A . n 
A 1 337 ASP 337 474 474 ASP ASP A . n 
A 1 338 MET 338 475 475 MET MET A . n 
A 1 339 ARG 339 476 476 ARG ARG A . n 
A 1 340 ASP 340 477 477 ASP ASP A . n 
A 1 341 ASN 341 478 478 ASN ASN A . n 
A 1 342 TRP 342 479 479 TRP TRP A . n 
A 1 343 ARG 343 480 480 ARG ARG A . n 
A 1 344 SER 344 481 481 SER SER A . n 
A 1 345 GLU 345 482 482 GLU GLU A . n 
A 1 346 LEU 346 483 483 LEU LEU A . n 
A 1 347 TYR 347 484 484 TYR TYR A . n 
A 1 348 LYS 348 485 485 LYS LYS A . n 
A 1 349 TYR 349 486 486 TYR TYR A . n 
A 1 350 LYS 350 487 487 LYS LYS A . n 
A 1 351 VAL 351 488 488 VAL VAL A . n 
A 1 352 VAL 352 489 489 VAL VAL A . n 
A 1 353 GLN 353 490 490 GLN GLN A . n 
A 1 354 ILE 354 491 491 ILE ILE A . n 
A 1 355 GLU 355 492 492 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ATD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ATD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG   1  501 501 NAG   NAG A . 
C 2 NAG   1  502 502 NAG   NAG A . 
D 2 NAG   1  503 503 NAG   NAG A . 
E 2 NAG   1  504 504 NAG   NAG A . 
F 2 NAG   1  505 505 NAG   NAG A . 
G 2 NAG   1  506 506 NAG   NAG A . 
H 2 NAG   1  507 507 NAG   NAG A . 
I 2 NAG   1  508 508 NAG   NAG A . 
J 2 NAG   1  509 510 NAG   NAG A . 
K 3 EPE   1  510 512 EPE   EPE A . 
L 4 A1ATD 1  511 1   A1ATD MW5 A . 
M 5 MPD   1  512 1   MPD   MPD A . 
N 5 MPD   1  513 2   MPD   MPD A . 
O 6 HOH   1  601 40  HOH   HOH A . 
O 6 HOH   2  602 66  HOH   HOH A . 
O 6 HOH   3  603 16  HOH   HOH A . 
O 6 HOH   4  604 42  HOH   HOH A . 
O 6 HOH   5  605 23  HOH   HOH A . 
O 6 HOH   6  606 30  HOH   HOH A . 
O 6 HOH   7  607 80  HOH   HOH A . 
O 6 HOH   8  608 52  HOH   HOH A . 
O 6 HOH   9  609 71  HOH   HOH A . 
O 6 HOH   10 610 29  HOH   HOH A . 
O 6 HOH   11 611 3   HOH   HOH A . 
O 6 HOH   12 612 49  HOH   HOH A . 
O 6 HOH   13 613 43  HOH   HOH A . 
O 6 HOH   14 614 14  HOH   HOH A . 
O 6 HOH   15 615 37  HOH   HOH A . 
O 6 HOH   16 616 22  HOH   HOH A . 
O 6 HOH   17 617 44  HOH   HOH A . 
O 6 HOH   18 618 84  HOH   HOH A . 
O 6 HOH   19 619 55  HOH   HOH A . 
O 6 HOH   20 620 13  HOH   HOH A . 
O 6 HOH   21 621 46  HOH   HOH A . 
O 6 HOH   22 622 79  HOH   HOH A . 
O 6 HOH   23 623 33  HOH   HOH A . 
O 6 HOH   24 624 4   HOH   HOH A . 
O 6 HOH   25 625 57  HOH   HOH A . 
O 6 HOH   26 626 41  HOH   HOH A . 
O 6 HOH   27 627 50  HOH   HOH A . 
O 6 HOH   28 628 24  HOH   HOH A . 
O 6 HOH   29 629 28  HOH   HOH A . 
O 6 HOH   30 630 34  HOH   HOH A . 
O 6 HOH   31 631 9   HOH   HOH A . 
O 6 HOH   32 632 11  HOH   HOH A . 
O 6 HOH   33 633 12  HOH   HOH A . 
O 6 HOH   34 634 69  HOH   HOH A . 
O 6 HOH   35 635 45  HOH   HOH A . 
O 6 HOH   36 636 6   HOH   HOH A . 
O 6 HOH   37 637 59  HOH   HOH A . 
O 6 HOH   38 638 1   HOH   HOH A . 
O 6 HOH   39 639 60  HOH   HOH A . 
O 6 HOH   40 640 68  HOH   HOH A . 
O 6 HOH   41 641 2   HOH   HOH A . 
O 6 HOH   42 642 20  HOH   HOH A . 
O 6 HOH   43 643 19  HOH   HOH A . 
O 6 HOH   44 644 61  HOH   HOH A . 
O 6 HOH   45 645 62  HOH   HOH A . 
O 6 HOH   46 646 65  HOH   HOH A . 
O 6 HOH   47 647 27  HOH   HOH A . 
O 6 HOH   48 648 35  HOH   HOH A . 
O 6 HOH   49 649 78  HOH   HOH A . 
O 6 HOH   50 650 39  HOH   HOH A . 
O 6 HOH   51 651 8   HOH   HOH A . 
O 6 HOH   52 652 51  HOH   HOH A . 
O 6 HOH   53 653 15  HOH   HOH A . 
O 6 HOH   54 654 54  HOH   HOH A . 
O 6 HOH   55 655 32  HOH   HOH A . 
O 6 HOH   56 656 25  HOH   HOH A . 
O 6 HOH   57 657 5   HOH   HOH A . 
O 6 HOH   58 658 7   HOH   HOH A . 
O 6 HOH   59 659 74  HOH   HOH A . 
O 6 HOH   60 660 92  HOH   HOH A . 
O 6 HOH   61 661 26  HOH   HOH A . 
O 6 HOH   62 662 21  HOH   HOH A . 
O 6 HOH   63 663 85  HOH   HOH A . 
O 6 HOH   64 664 38  HOH   HOH A . 
O 6 HOH   65 665 36  HOH   HOH A . 
O 6 HOH   66 666 10  HOH   HOH A . 
O 6 HOH   67 667 17  HOH   HOH A . 
O 6 HOH   68 668 18  HOH   HOH A . 
O 6 HOH   69 669 82  HOH   HOH A . 
O 6 HOH   70 670 76  HOH   HOH A . 
O 6 HOH   71 671 77  HOH   HOH A . 
O 6 HOH   72 672 64  HOH   HOH A . 
O 6 HOH   73 673 31  HOH   HOH A . 
O 6 HOH   74 674 47  HOH   HOH A . 
O 6 HOH   75 675 72  HOH   HOH A . 
O 6 HOH   76 676 58  HOH   HOH A . 
O 6 HOH   77 677 53  HOH   HOH A . 
O 6 HOH   78 678 83  HOH   HOH A . 
O 6 HOH   79 679 73  HOH   HOH A . 
O 6 HOH   80 680 48  HOH   HOH A . 
O 6 HOH   81 681 63  HOH   HOH A . 
O 6 HOH   82 682 70  HOH   HOH A . 
O 6 HOH   83 683 91  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                     9BXW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.701 
_cell.length_a_esd                 ? 
_cell.length_b                     66.827 
_cell.length_b_esd                 ? 
_cell.length_c                     92.457 
_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                         9BXW 
_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                   9BXW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.90 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;10% PEG 3350
5% PEG 400
0.1 M HEPES pH 7.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Si(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97946 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BXW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     19892 
_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                           84.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.5 
_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                                0.058 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.113 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.1 
_reflns_shell.d_res_low                                     2.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             840 
_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                               3.4 
_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                               0.445 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.53 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          74.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.79 
_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                                 9BXW 
_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                            2.10 
_refine.ls_d_res_low                             38.02 
_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                     19859 
_refine.ls_number_reflns_R_free                  981 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    84.93 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2170 
_refine.ls_R_factor_R_free                       0.2680 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2145 
_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                          1.36 
_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                 26.80 
_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                            0.30 
_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        2668 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         190 
_refine_hist.number_atoms_solvent             83 
_refine_hist.number_atoms_total               2941 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        38.02 
# 
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' ? 0.004  ? 2914 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.769  ? 3956 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.946 ? 434  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.048  ? 464  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 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' 2.10 2.21  . . 125 2388 77.00 . . . . 0.2962 . . . . . . . . . . . 0.3108 
'X-RAY DIFFRACTION' 2.21 2.35  . . 147 2686 86.00 . . . . 0.2752 . . . . . . . . . . . 0.3293 
'X-RAY DIFFRACTION' 2.35 2.53  . . 162 2661 86.00 . . . . 0.2773 . . . . . . . . . . . 0.3397 
'X-RAY DIFFRACTION' 2.53 2.78  . . 142 2853 90.00 . . . . 0.2661 . . . . . . . . . . . 0.3033 
'X-RAY DIFFRACTION' 2.78 3.18  . . 118 2843 89.00 . . . . 0.2391 . . . . . . . . . . . 0.2858 
'X-RAY DIFFRACTION' 3.18 4.01  . . 152 2713 86.00 . . . . 0.1985 . . . . . . . . . . . 0.2346 
'X-RAY DIFFRACTION' 4.01 38.02 . . 135 2734 81.00 . . . . 0.1753 . . . . . . . . . . . 0.2488 
# 
_struct.entry_id                     9BXW 
_struct.title                        'CRYSTAL STRUCTURE OF HIV-1 LM/HS CLADE A/E CRF01 GP120 CORE IN COMPLEX WITH DL-III-115' 
_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        9BXW 
_struct_keywords.text            'HIV-1 GP120, CLADE A/E CF01, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 6 ? 
# 
_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              9BXW 
_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 9BXW VAL A 1   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      42  1 
1 9BXW PRO A 2   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      43  2 
1 9BXW TYR A 20  ? UNP A0A0M3KKW9 HIS 18  'engineered mutation' 61  3 
1 9BXW HIS A 64  ? UNP A0A0M3KKW9 GLN 62  'engineered mutation' 105 4 
1 9BXW ILE A 67  ? UNP A0A0M3KKW9 VAL 65  'engineered mutation' 108 5 
1 9BXW SER A 244 ? UNP A0A0M3KKW9 HIS 242 'engineered mutation' 375 6 
1 9BXW ASP A 337 ? UNP A0A0M3KKW9 ASN 335 'engineered mutation' 474 7 
1 9BXW MET A 338 ? UNP A0A0M3KKW9 ILE 336 'engineered mutation' 475 8 
1 9BXW 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,O 
# 
_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 ? ? ? ? ? ? ? 2.041 ? ?               
disulf2 disulf ?   ? A CYS 78  SG  ? ? ? 1_555 A CYS 91  SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf3 disulf ?   ? A CYS 104 SG  ? ? ? 1_555 A CYS 133 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf4 disulf ?   ? A CYS 114 SG  ? ? ? 1_555 A CYS 125 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf5 disulf ?   ? A CYS 182 SG  ? ? ? 1_555 A CYS 201 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf6 disulf ?   ? A CYS 247 SG  ? ? ? 1_555 A CYS 308 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf7 disulf ?   ? A CYS 254 SG  ? ? ? 1_555 A CYS 281 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf8 disulf ?   ? A CYS 264 SG  ? ? ? 1_555 A CYS 273 SG ? ? A CYS 395 A CYS 410 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
covale1 covale one ? A ASN 120 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 234 A NAG 501 1_555 ? ? ? ? ? ? ? 1.437 ? N-Glycosylation 
covale2 covale one ? A ASN 127 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 241 A NAG 502 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale3 covale one ? A ASN 148 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 262 A NAG 503 1_555 ? ? ? ? ? ? ? 1.430 ? N-Glycosylation 
covale4 covale one ? A ASN 162 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 276 A NAG 504 1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
covale5 covale one ? A ASN 175 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 289 A NAG 505 1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale6 covale one ? A ASN 181 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 295 A NAG 506 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale7 covale one ? A ASN 204 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 334 A NAG 507 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale8 covale one ? A ASN 255 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 386 A NAG 508 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale9 covale one ? A ASN 311 ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 448 A NAG 509 1_555 ? ? ? ? ? ? ? 1.428 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG B .   ? ASN A 120 ? NAG A 501 ? 1_555 ASN A 234 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG C .   ? ASN A 127 ? NAG A 502 ? 1_555 ASN A 241 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG D .   ? ASN A 148 ? NAG A 503 ? 1_555 ASN A 262 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG E .   ? ASN A 162 ? NAG A 504 ? 1_555 ASN A 276 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG F .   ? ASN A 175 ? NAG A 505 ? 1_555 ASN A 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG G .   ? ASN A 181 ? NAG A 506 ? 1_555 ASN A 295 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG H .   ? ASN A 204 ? NAG A 507 ? 1_555 ASN A 334 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG I .   ? ASN A 255 ? NAG A 508 ? 1_555 ASN A 386 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG J .   ? ASN A 311 ? NAG A 509 ? 1_555 ASN A 448 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 CYS A 13  ? CYS A 33  ? CYS A 54  ? 1_555 CYS A 74  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS A 78  ? CYS A 91  ? CYS A 119 ? 1_555 CYS A 205 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 104 ? CYS A 133 ? CYS A 218 ? 1_555 CYS A 247 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 114 ? CYS A 125 ? CYS A 228 ? 1_555 CYS A 239 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 182 ? CYS A 201 ? CYS A 296 ? 1_555 CYS A 331 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 247 ? CYS A 308 ? CYS A 378 ? 1_555 CYS A 445 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS A 254 ? CYS A 281 ? CYS A 385 ? 1_555 CYS A 418 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS A 264 ? CYS A 273 ? CYS A 395 ? 1_555 CYS A 410 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 5 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 4 5 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TRP A 4   ? ASP A 6   ? TRP A 45  ASP A 47  
AA1 2 TYR A 349 ? ILE A 354 ? TYR A 486 ILE A 491 
AA1 3 TYR A 109 ? CYS A 114 ? TYR A 223 CYS A 228 
AA1 4 VAL A 128 ? VAL A 131 ? VAL A 242 VAL A 245 
AA1 5 ILE A 43  ? HIS A 44  ? ILE A 84  HIS A 85  
AA2 1 VAL A 34  ? PRO A 35  ? VAL A 75  PRO A 76  
AA2 2 PHE A 12  ? SER A 15  ? PHE A 53  SER A 56  
AA2 3 ILE A 101 ? CYS A 104 ? ILE A 215 CYS A 218 
AA3 1 GLU A 50  ? ASN A 53  ? GLU A 91  ASN A 94  
AA3 2 THR A 122 ? CYS A 125 ? THR A 236 CYS A 239 
AA4 1 VAL A 79  ? LEU A 81  ? VAL A 120 LEU A 122 
AA4 2 GLN A 295 ? MET A 297 ? GLN A 432 MET A 434 
AA4 3 ILE A 286 ? ASN A 288 ? ILE A 423 ASN A 425 
AA5 1 LEU A 145 ? LEU A 147 ? LEU A 259 LEU A 261 
AA5 2 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA5 3 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA5 4 ASN A 328 ? PRO A 333 ? ASN A 465 PRO A 470 
AA5 5 THR A 227 ? PHE A 230 ? THR A 358 PHE A 361 
AA6 1 ILE A 157 ? ARG A 159 ? ILE A 271 ARG A 273 
AA6 2 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA6 3 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA6 4 LYS A 198 ? ASN A 204 ? LYS A 328 ASN A 334 
AA6 5 THR A 276 ? LYS A 284 ? THR A 413 LYS A 421 
AA6 6 GLU A 250 ? CYS A 254 ? GLU A 381 CYS A 385 
AA6 7 HIS A 243 ? CYS A 247 ? HIS A 374 CYS A 378 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 5   ? N LYS A 46  O GLN A 353 ? O GLN A 490 
AA1 2 3 O LYS A 350 ? O LYS A 487 N LEU A 112 ? N LEU A 226 
AA1 3 4 N LYS A 113 ? N LYS A 227 O SER A 129 ? O SER A 243 
AA1 4 5 O SER A 130 ? O SER A 244 N ILE A 43  ? N ILE A 84  
AA2 1 2 O VAL A 34  ? O VAL A 75  N CYS A 13  ? N CYS A 54  
AA2 2 3 N PHE A 12  ? N PHE A 53  O CYS A 104 ? O CYS A 218 
AA3 1 2 N GLU A 50  ? N GLU A 91  O CYS A 125 ? O CYS A 239 
AA4 1 2 N VAL A 79  ? N VAL A 120 O MET A 297 ? O MET A 434 
AA4 2 3 O ALA A 296 ? O ALA A 433 N ILE A 287 ? N ILE A 424 
AA5 1 2 N LEU A 146 ? N LEU A 260 O THR A 313 ? O THR A 450 
AA5 2 3 O LEU A 317 ? O LEU A 454 N ILE A 170 ? N ILE A 284 
AA5 4 5 O PHE A 331 ? O PHE A 468 N ILE A 229 ? N ILE A 360 
AA6 1 2 N ARG A 159 ? N ARG A 273 O ILE A 171 ? O ILE A 285 
AA6 2 3 N ILE A 170 ? N ILE A 284 O LEU A 317 ? O LEU A 454 
AA6 4 5 N ILE A 203 ? N ILE A 333 O ILE A 277 ? O ILE A 414 
AA6 5 6 O LYS A 282 ? O LYS A 419 N TYR A 253 ? N TYR A 384 
AA6 6 7 O CYS A 254 ? O CYS A 385 N HIS A 243 ? N HIS A 374 
# 
_pdbx_entry_details.entry_id                   9BXW 
_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 ASP A 57  ? ? -96.58  38.27  
2 1 TYR A 61  ? ? 75.46   -15.14 
3 1 THR A 123 ? ? -95.50  35.65  
4 1 GLN A 258 ? ? 67.05   -60.16 
5 1 GLU A 268 ? ? -125.69 -92.79 
6 1 ASN A 276 ? ? -170.81 95.02  
7 1 ASN A 354 ? ? 18.40   63.02  
8 1 PHE A 391 ? ? -104.70 43.80  
9 1 ASN A 411 ? ? -162.99 8.32   
# 
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 GLY 318 ? A GLY 188 
4  1 Y 1 A GLY 319 ? A GLY 189 
5  1 Y 1 A SER 320 ? A SER 190 
6  1 Y 1 A GLY 321 ? A GLY 191 
7  1 Y 1 A SER 322 ? A SER 192 
8  1 Y 1 A GLY 323 ? A GLY 193 
9  1 Y 1 A GLY 324 ? A GLY 194 
10 1 Y 1 A ILE 402 ? A ILE 265 
11 1 Y 1 A GLY 403 ? A GLY 266 
12 1 Y 1 A ASN 404 ? A ASN 267 
13 1 Y 1 A GLU 405 ? A GLU 268 
14 1 Y 1 A THR 406 ? A THR 269 
15 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 
A1ATD C10  C  N N 1   
A1ATD CD   C  N N 2   
A1ATD NE   N  N N 3   
A1ATD CZ   C  N N 4   
A1ATD NH1  N  N N 5   
A1ATD NH2  N  N N 6   
A1ATD C01  C  N N 7   
A1ATD C03  C  N N 8   
A1ATD C04  C  N N 9   
A1ATD C06  C  N N 10  
A1ATD C08  C  N N 11  
A1ATD C09  C  N S 12  
A1ATD C13  C  Y N 13  
A1ATD C14  C  Y N 14  
A1ATD C15  C  Y N 15  
A1ATD C17  C  Y N 16  
A1ATD C19  C  Y N 17  
A1ATD C20  C  Y N 18  
A1ATD C21  C  N N 19  
A1ATD C22  C  N R 20  
A1ATD C23  C  N N 21  
A1ATD C25  C  N N 22  
A1ATD C26  C  N N 23  
A1ATD C27  C  N N 24  
A1ATD F16  F  N N 25  
A1ATD N02  N  N N 26  
A1ATD N05  N  N N 27  
A1ATD N07  N  N N 28  
A1ATD N12  N  N N 29  
A1ATD O11  O  N N 30  
A1ATD O24  O  N N 31  
A1ATD O28  O  N N 32  
A1ATD CL1  CL N N 33  
A1ATD H1   H  N N 34  
A1ATD H2   H  N N 35  
A1ATD H3   H  N N 36  
A1ATD H4   H  N N 37  
A1ATD H5   H  N N 38  
A1ATD H6   H  N N 39  
A1ATD H7   H  N N 40  
A1ATD H8   H  N N 41  
A1ATD H9   H  N N 42  
A1ATD H10  H  N N 43  
A1ATD H11  H  N N 44  
A1ATD H12  H  N N 45  
A1ATD H13  H  N N 46  
A1ATD H14  H  N N 47  
A1ATD H15  H  N N 48  
A1ATD H16  H  N N 49  
A1ATD H17  H  N N 50  
A1ATD H18  H  N N 51  
A1ATD H19  H  N N 52  
A1ATD H20  H  N N 53  
A1ATD H21  H  N N 54  
A1ATD H22  H  N N 55  
A1ATD H23  H  N N 56  
A1ATD H24  H  N N 57  
A1ATD H25  H  N N 58  
A1ATD H26  H  N N 59  
A1ATD H27  H  N N 60  
A1ATD H28  H  N N 61  
A1ATD H29  H  N N 62  
A1ATD H31  H  N N 63  
A1ATD H32  H  N N 64  
ALA   N    N  N N 65  
ALA   CA   C  N S 66  
ALA   C    C  N N 67  
ALA   O    O  N N 68  
ALA   CB   C  N N 69  
ALA   OXT  O  N N 70  
ALA   H    H  N N 71  
ALA   H2   H  N N 72  
ALA   HA   H  N N 73  
ALA   HB1  H  N N 74  
ALA   HB2  H  N N 75  
ALA   HB3  H  N N 76  
ALA   HXT  H  N N 77  
ARG   N    N  N N 78  
ARG   CA   C  N S 79  
ARG   C    C  N N 80  
ARG   O    O  N N 81  
ARG   CB   C  N N 82  
ARG   CG   C  N N 83  
ARG   CD   C  N N 84  
ARG   NE   N  N N 85  
ARG   CZ   C  N N 86  
ARG   NH1  N  N N 87  
ARG   NH2  N  N N 88  
ARG   OXT  O  N N 89  
ARG   H    H  N N 90  
ARG   H2   H  N N 91  
ARG   HA   H  N N 92  
ARG   HB2  H  N N 93  
ARG   HB3  H  N N 94  
ARG   HG2  H  N N 95  
ARG   HG3  H  N N 96  
ARG   HD2  H  N N 97  
ARG   HD3  H  N N 98  
ARG   HE   H  N N 99  
ARG   HH11 H  N N 100 
ARG   HH12 H  N N 101 
ARG   HH21 H  N N 102 
ARG   HH22 H  N N 103 
ARG   HXT  H  N N 104 
ASN   N    N  N N 105 
ASN   CA   C  N S 106 
ASN   C    C  N N 107 
ASN   O    O  N N 108 
ASN   CB   C  N N 109 
ASN   CG   C  N N 110 
ASN   OD1  O  N N 111 
ASN   ND2  N  N N 112 
ASN   OXT  O  N N 113 
ASN   H    H  N N 114 
ASN   H2   H  N N 115 
ASN   HA   H  N N 116 
ASN   HB2  H  N N 117 
ASN   HB3  H  N N 118 
ASN   HD21 H  N N 119 
ASN   HD22 H  N N 120 
ASN   HXT  H  N N 121 
ASP   N    N  N N 122 
ASP   CA   C  N S 123 
ASP   C    C  N N 124 
ASP   O    O  N N 125 
ASP   CB   C  N N 126 
ASP   CG   C  N N 127 
ASP   OD1  O  N N 128 
ASP   OD2  O  N N 129 
ASP   OXT  O  N N 130 
ASP   H    H  N N 131 
ASP   H2   H  N N 132 
ASP   HA   H  N N 133 
ASP   HB2  H  N N 134 
ASP   HB3  H  N N 135 
ASP   HD2  H  N N 136 
ASP   HXT  H  N N 137 
CYS   N    N  N N 138 
CYS   CA   C  N R 139 
CYS   C    C  N N 140 
CYS   O    O  N N 141 
CYS   CB   C  N N 142 
CYS   SG   S  N N 143 
CYS   OXT  O  N N 144 
CYS   H    H  N N 145 
CYS   H2   H  N N 146 
CYS   HA   H  N N 147 
CYS   HB2  H  N N 148 
CYS   HB3  H  N N 149 
CYS   HG   H  N N 150 
CYS   HXT  H  N N 151 
EPE   N1   N  N N 152 
EPE   C2   C  N N 153 
EPE   C3   C  N N 154 
EPE   N4   N  N N 155 
EPE   C5   C  N N 156 
EPE   C6   C  N N 157 
EPE   C7   C  N N 158 
EPE   C8   C  N N 159 
EPE   O8   O  N N 160 
EPE   C9   C  N N 161 
EPE   C10  C  N N 162 
EPE   S    S  N N 163 
EPE   O1S  O  N N 164 
EPE   O2S  O  N N 165 
EPE   O3S  O  N N 166 
EPE   H21  H  N N 167 
EPE   H22  H  N N 168 
EPE   H31  H  N N 169 
EPE   H32  H  N N 170 
EPE   H51  H  N N 171 
EPE   H52  H  N N 172 
EPE   H61  H  N N 173 
EPE   H62  H  N N 174 
EPE   H71  H  N N 175 
EPE   H72  H  N N 176 
EPE   H81  H  N N 177 
EPE   H82  H  N N 178 
EPE   HO8  H  N N 179 
EPE   H91  H  N N 180 
EPE   H92  H  N N 181 
EPE   H101 H  N N 182 
EPE   H102 H  N N 183 
EPE   HOS3 H  N N 184 
GLN   N    N  N N 185 
GLN   CA   C  N S 186 
GLN   C    C  N N 187 
GLN   O    O  N N 188 
GLN   CB   C  N N 189 
GLN   CG   C  N N 190 
GLN   CD   C  N N 191 
GLN   OE1  O  N N 192 
GLN   NE2  N  N N 193 
GLN   OXT  O  N N 194 
GLN   H    H  N N 195 
GLN   H2   H  N N 196 
GLN   HA   H  N N 197 
GLN   HB2  H  N N 198 
GLN   HB3  H  N N 199 
GLN   HG2  H  N N 200 
GLN   HG3  H  N N 201 
GLN   HE21 H  N N 202 
GLN   HE22 H  N N 203 
GLN   HXT  H  N N 204 
GLU   N    N  N N 205 
GLU   CA   C  N S 206 
GLU   C    C  N N 207 
GLU   O    O  N N 208 
GLU   CB   C  N N 209 
GLU   CG   C  N N 210 
GLU   CD   C  N N 211 
GLU   OE1  O  N N 212 
GLU   OE2  O  N N 213 
GLU   OXT  O  N N 214 
GLU   H    H  N N 215 
GLU   H2   H  N N 216 
GLU   HA   H  N N 217 
GLU   HB2  H  N N 218 
GLU   HB3  H  N N 219 
GLU   HG2  H  N N 220 
GLU   HG3  H  N N 221 
GLU   HE2  H  N N 222 
GLU   HXT  H  N N 223 
GLY   N    N  N N 224 
GLY   CA   C  N N 225 
GLY   C    C  N N 226 
GLY   O    O  N N 227 
GLY   OXT  O  N N 228 
GLY   H    H  N N 229 
GLY   H2   H  N N 230 
GLY   HA2  H  N N 231 
GLY   HA3  H  N N 232 
GLY   HXT  H  N N 233 
HIS   N    N  N N 234 
HIS   CA   C  N S 235 
HIS   C    C  N N 236 
HIS   O    O  N N 237 
HIS   CB   C  N N 238 
HIS   CG   C  Y N 239 
HIS   ND1  N  Y N 240 
HIS   CD2  C  Y N 241 
HIS   CE1  C  Y N 242 
HIS   NE2  N  Y N 243 
HIS   OXT  O  N N 244 
HIS   H    H  N N 245 
HIS   H2   H  N N 246 
HIS   HA   H  N N 247 
HIS   HB2  H  N N 248 
HIS   HB3  H  N N 249 
HIS   HD1  H  N N 250 
HIS   HD2  H  N N 251 
HIS   HE1  H  N N 252 
HIS   HE2  H  N N 253 
HIS   HXT  H  N N 254 
HOH   O    O  N N 255 
HOH   H1   H  N N 256 
HOH   H2   H  N N 257 
ILE   N    N  N N 258 
ILE   CA   C  N S 259 
ILE   C    C  N N 260 
ILE   O    O  N N 261 
ILE   CB   C  N S 262 
ILE   CG1  C  N N 263 
ILE   CG2  C  N N 264 
ILE   CD1  C  N N 265 
ILE   OXT  O  N N 266 
ILE   H    H  N N 267 
ILE   H2   H  N N 268 
ILE   HA   H  N N 269 
ILE   HB   H  N N 270 
ILE   HG12 H  N N 271 
ILE   HG13 H  N N 272 
ILE   HG21 H  N N 273 
ILE   HG22 H  N N 274 
ILE   HG23 H  N N 275 
ILE   HD11 H  N N 276 
ILE   HD12 H  N N 277 
ILE   HD13 H  N N 278 
ILE   HXT  H  N N 279 
LEU   N    N  N N 280 
LEU   CA   C  N S 281 
LEU   C    C  N N 282 
LEU   O    O  N N 283 
LEU   CB   C  N N 284 
LEU   CG   C  N N 285 
LEU   CD1  C  N N 286 
LEU   CD2  C  N N 287 
LEU   OXT  O  N N 288 
LEU   H    H  N N 289 
LEU   H2   H  N N 290 
LEU   HA   H  N N 291 
LEU   HB2  H  N N 292 
LEU   HB3  H  N N 293 
LEU   HG   H  N N 294 
LEU   HD11 H  N N 295 
LEU   HD12 H  N N 296 
LEU   HD13 H  N N 297 
LEU   HD21 H  N N 298 
LEU   HD22 H  N N 299 
LEU   HD23 H  N N 300 
LEU   HXT  H  N N 301 
LYS   N    N  N N 302 
LYS   CA   C  N S 303 
LYS   C    C  N N 304 
LYS   O    O  N N 305 
LYS   CB   C  N N 306 
LYS   CG   C  N N 307 
LYS   CD   C  N N 308 
LYS   CE   C  N N 309 
LYS   NZ   N  N N 310 
LYS   OXT  O  N N 311 
LYS   H    H  N N 312 
LYS   H2   H  N N 313 
LYS   HA   H  N N 314 
LYS   HB2  H  N N 315 
LYS   HB3  H  N N 316 
LYS   HG2  H  N N 317 
LYS   HG3  H  N N 318 
LYS   HD2  H  N N 319 
LYS   HD3  H  N N 320 
LYS   HE2  H  N N 321 
LYS   HE3  H  N N 322 
LYS   HZ1  H  N N 323 
LYS   HZ2  H  N N 324 
LYS   HZ3  H  N N 325 
LYS   HXT  H  N N 326 
MET   N    N  N N 327 
MET   CA   C  N S 328 
MET   C    C  N N 329 
MET   O    O  N N 330 
MET   CB   C  N N 331 
MET   CG   C  N N 332 
MET   SD   S  N N 333 
MET   CE   C  N N 334 
MET   OXT  O  N N 335 
MET   H    H  N N 336 
MET   H2   H  N N 337 
MET   HA   H  N N 338 
MET   HB2  H  N N 339 
MET   HB3  H  N N 340 
MET   HG2  H  N N 341 
MET   HG3  H  N N 342 
MET   HE1  H  N N 343 
MET   HE2  H  N N 344 
MET   HE3  H  N N 345 
MET   HXT  H  N N 346 
MPD   C1   C  N N 347 
MPD   C2   C  N N 348 
MPD   O2   O  N N 349 
MPD   CM   C  N N 350 
MPD   C3   C  N N 351 
MPD   C4   C  N S 352 
MPD   O4   O  N N 353 
MPD   C5   C  N N 354 
MPD   H11  H  N N 355 
MPD   H12  H  N N 356 
MPD   H13  H  N N 357 
MPD   HO2  H  N N 358 
MPD   HM1  H  N N 359 
MPD   HM2  H  N N 360 
MPD   HM3  H  N N 361 
MPD   H31  H  N N 362 
MPD   H32  H  N N 363 
MPD   H4   H  N N 364 
MPD   HO4  H  N N 365 
MPD   H51  H  N N 366 
MPD   H52  H  N N 367 
MPD   H53  H  N N 368 
NAG   C1   C  N R 369 
NAG   C2   C  N R 370 
NAG   C3   C  N R 371 
NAG   C4   C  N S 372 
NAG   C5   C  N R 373 
NAG   C6   C  N N 374 
NAG   C7   C  N N 375 
NAG   C8   C  N N 376 
NAG   N2   N  N N 377 
NAG   O1   O  N N 378 
NAG   O3   O  N N 379 
NAG   O4   O  N N 380 
NAG   O5   O  N N 381 
NAG   O6   O  N N 382 
NAG   O7   O  N N 383 
NAG   H1   H  N N 384 
NAG   H2   H  N N 385 
NAG   H3   H  N N 386 
NAG   H4   H  N N 387 
NAG   H5   H  N N 388 
NAG   H61  H  N N 389 
NAG   H62  H  N N 390 
NAG   H81  H  N N 391 
NAG   H82  H  N N 392 
NAG   H83  H  N N 393 
NAG   HN2  H  N N 394 
NAG   HO1  H  N N 395 
NAG   HO3  H  N N 396 
NAG   HO4  H  N N 397 
NAG   HO6  H  N N 398 
PHE   N    N  N N 399 
PHE   CA   C  N S 400 
PHE   C    C  N N 401 
PHE   O    O  N N 402 
PHE   CB   C  N N 403 
PHE   CG   C  Y N 404 
PHE   CD1  C  Y N 405 
PHE   CD2  C  Y N 406 
PHE   CE1  C  Y N 407 
PHE   CE2  C  Y N 408 
PHE   CZ   C  Y N 409 
PHE   OXT  O  N N 410 
PHE   H    H  N N 411 
PHE   H2   H  N N 412 
PHE   HA   H  N N 413 
PHE   HB2  H  N N 414 
PHE   HB3  H  N N 415 
PHE   HD1  H  N N 416 
PHE   HD2  H  N N 417 
PHE   HE1  H  N N 418 
PHE   HE2  H  N N 419 
PHE   HZ   H  N N 420 
PHE   HXT  H  N N 421 
PRO   N    N  N N 422 
PRO   CA   C  N S 423 
PRO   C    C  N N 424 
PRO   O    O  N N 425 
PRO   CB   C  N N 426 
PRO   CG   C  N N 427 
PRO   CD   C  N N 428 
PRO   OXT  O  N N 429 
PRO   H    H  N N 430 
PRO   HA   H  N N 431 
PRO   HB2  H  N N 432 
PRO   HB3  H  N N 433 
PRO   HG2  H  N N 434 
PRO   HG3  H  N N 435 
PRO   HD2  H  N N 436 
PRO   HD3  H  N N 437 
PRO   HXT  H  N N 438 
SER   N    N  N N 439 
SER   CA   C  N S 440 
SER   C    C  N N 441 
SER   O    O  N N 442 
SER   CB   C  N N 443 
SER   OG   O  N N 444 
SER   OXT  O  N N 445 
SER   H    H  N N 446 
SER   H2   H  N N 447 
SER   HA   H  N N 448 
SER   HB2  H  N N 449 
SER   HB3  H  N N 450 
SER   HG   H  N N 451 
SER   HXT  H  N N 452 
THR   N    N  N N 453 
THR   CA   C  N S 454 
THR   C    C  N N 455 
THR   O    O  N N 456 
THR   CB   C  N R 457 
THR   OG1  O  N N 458 
THR   CG2  C  N N 459 
THR   OXT  O  N N 460 
THR   H    H  N N 461 
THR   H2   H  N N 462 
THR   HA   H  N N 463 
THR   HB   H  N N 464 
THR   HG1  H  N N 465 
THR   HG21 H  N N 466 
THR   HG22 H  N N 467 
THR   HG23 H  N N 468 
THR   HXT  H  N N 469 
TRP   N    N  N N 470 
TRP   CA   C  N S 471 
TRP   C    C  N N 472 
TRP   O    O  N N 473 
TRP   CB   C  N N 474 
TRP   CG   C  Y N 475 
TRP   CD1  C  Y N 476 
TRP   CD2  C  Y N 477 
TRP   NE1  N  Y N 478 
TRP   CE2  C  Y N 479 
TRP   CE3  C  Y N 480 
TRP   CZ2  C  Y N 481 
TRP   CZ3  C  Y N 482 
TRP   CH2  C  Y N 483 
TRP   OXT  O  N N 484 
TRP   H    H  N N 485 
TRP   H2   H  N N 486 
TRP   HA   H  N N 487 
TRP   HB2  H  N N 488 
TRP   HB3  H  N N 489 
TRP   HD1  H  N N 490 
TRP   HE1  H  N N 491 
TRP   HE3  H  N N 492 
TRP   HZ2  H  N N 493 
TRP   HZ3  H  N N 494 
TRP   HH2  H  N N 495 
TRP   HXT  H  N N 496 
TYR   N    N  N N 497 
TYR   CA   C  N S 498 
TYR   C    C  N N 499 
TYR   O    O  N N 500 
TYR   CB   C  N N 501 
TYR   CG   C  Y N 502 
TYR   CD1  C  Y N 503 
TYR   CD2  C  Y N 504 
TYR   CE1  C  Y N 505 
TYR   CE2  C  Y N 506 
TYR   CZ   C  Y N 507 
TYR   OH   O  N N 508 
TYR   OXT  O  N N 509 
TYR   H    H  N N 510 
TYR   H2   H  N N 511 
TYR   HA   H  N N 512 
TYR   HB2  H  N N 513 
TYR   HB3  H  N N 514 
TYR   HD1  H  N N 515 
TYR   HD2  H  N N 516 
TYR   HE1  H  N N 517 
TYR   HE2  H  N N 518 
TYR   HH   H  N N 519 
TYR   HXT  H  N N 520 
VAL   N    N  N N 521 
VAL   CA   C  N S 522 
VAL   C    C  N N 523 
VAL   O    O  N N 524 
VAL   CB   C  N N 525 
VAL   CG1  C  N N 526 
VAL   CG2  C  N N 527 
VAL   OXT  O  N N 528 
VAL   H    H  N N 529 
VAL   H2   H  N N 530 
VAL   HA   H  N N 531 
VAL   HB   H  N N 532 
VAL   HG11 H  N N 533 
VAL   HG12 H  N N 534 
VAL   HG13 H  N N 535 
VAL   HG21 H  N N 536 
VAL   HG22 H  N N 537 
VAL   HG23 H  N N 538 
VAL   HXT  H  N N 539 
# 
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 
A1ATD CL1 C17  sing N N 1   
A1ATD C19 C17  doub Y N 2   
A1ATD C19 C20  sing Y N 3   
A1ATD C17 C15  sing Y N 4   
A1ATD C20 C13  doub Y N 5   
A1ATD C15 F16  sing N N 6   
A1ATD C15 C14  doub Y N 7   
A1ATD C13 C14  sing Y N 8   
A1ATD C13 N12  sing N N 9   
A1ATD N12 C10  sing N N 10  
A1ATD C10 O11  doub N N 11  
A1ATD C10 C09  sing N N 12  
A1ATD C21 C09  sing N N 13  
A1ATD C21 C22  sing N N 14  
A1ATD C09 C08  sing N N 15  
A1ATD C22 C27  sing N N 16  
A1ATD C22 C23  sing N N 17  
A1ATD C27 O28  sing N N 18  
A1ATD C08 N07  sing N N 19  
A1ATD C23 N07  sing N N 20  
A1ATD N07 C06  sing N N 21  
A1ATD C25 C26  sing N N 22  
A1ATD C25 N05  sing N N 23  
A1ATD C26 N02  sing N N 24  
A1ATD C06 N05  sing N N 25  
A1ATD C06 O24  doub N N 26  
A1ATD N05 C04  sing N N 27  
A1ATD C04 C03  sing N N 28  
A1ATD N02 C03  sing N N 29  
A1ATD N02 C01  sing N N 30  
A1ATD C01 CD   sing N N 31  
A1ATD CD  NE   sing N N 32  
A1ATD NH2 CZ   doub N N 33  
A1ATD NE  CZ   sing N N 34  
A1ATD CZ  NH1  sing N N 35  
A1ATD CD  H1   sing N N 36  
A1ATD CD  H2   sing N N 37  
A1ATD NE  H3   sing N N 38  
A1ATD NH1 H4   sing N N 39  
A1ATD NH1 H5   sing N N 40  
A1ATD NH2 H6   sing N N 41  
A1ATD C01 H7   sing N N 42  
A1ATD C01 H8   sing N N 43  
A1ATD C03 H9   sing N N 44  
A1ATD C03 H10  sing N N 45  
A1ATD C04 H11  sing N N 46  
A1ATD C04 H12  sing N N 47  
A1ATD C08 H13  sing N N 48  
A1ATD C08 H14  sing N N 49  
A1ATD C09 H15  sing N N 50  
A1ATD C14 H16  sing N N 51  
A1ATD C19 H17  sing N N 52  
A1ATD C20 H18  sing N N 53  
A1ATD C21 H19  sing N N 54  
A1ATD C21 H20  sing N N 55  
A1ATD C22 H21  sing N N 56  
A1ATD C23 H22  sing N N 57  
A1ATD C23 H23  sing N N 58  
A1ATD C25 H24  sing N N 59  
A1ATD C25 H25  sing N N 60  
A1ATD C26 H26  sing N N 61  
A1ATD C26 H27  sing N N 62  
A1ATD C27 H28  sing N N 63  
A1ATD C27 H29  sing N N 64  
A1ATD N12 H31  sing N N 65  
A1ATD O28 H32  sing N N 66  
ALA   N   CA   sing N N 67  
ALA   N   H    sing N N 68  
ALA   N   H2   sing N N 69  
ALA   CA  C    sing N N 70  
ALA   CA  CB   sing N N 71  
ALA   CA  HA   sing N N 72  
ALA   C   O    doub N N 73  
ALA   C   OXT  sing N N 74  
ALA   CB  HB1  sing N N 75  
ALA   CB  HB2  sing N N 76  
ALA   CB  HB3  sing N N 77  
ALA   OXT HXT  sing N N 78  
ARG   N   CA   sing N N 79  
ARG   N   H    sing N N 80  
ARG   N   H2   sing N N 81  
ARG   CA  C    sing N N 82  
ARG   CA  CB   sing N N 83  
ARG   CA  HA   sing N N 84  
ARG   C   O    doub N N 85  
ARG   C   OXT  sing N N 86  
ARG   CB  CG   sing N N 87  
ARG   CB  HB2  sing N N 88  
ARG   CB  HB3  sing N N 89  
ARG   CG  CD   sing N N 90  
ARG   CG  HG2  sing N N 91  
ARG   CG  HG3  sing N N 92  
ARG   CD  NE   sing N N 93  
ARG   CD  HD2  sing N N 94  
ARG   CD  HD3  sing N N 95  
ARG   NE  CZ   sing N N 96  
ARG   NE  HE   sing N N 97  
ARG   CZ  NH1  sing N N 98  
ARG   CZ  NH2  doub N N 99  
ARG   NH1 HH11 sing N N 100 
ARG   NH1 HH12 sing N N 101 
ARG   NH2 HH21 sing N N 102 
ARG   NH2 HH22 sing N N 103 
ARG   OXT HXT  sing N N 104 
ASN   N   CA   sing N N 105 
ASN   N   H    sing N N 106 
ASN   N   H2   sing N N 107 
ASN   CA  C    sing N N 108 
ASN   CA  CB   sing N N 109 
ASN   CA  HA   sing N N 110 
ASN   C   O    doub N N 111 
ASN   C   OXT  sing N N 112 
ASN   CB  CG   sing N N 113 
ASN   CB  HB2  sing N N 114 
ASN   CB  HB3  sing N N 115 
ASN   CG  OD1  doub N N 116 
ASN   CG  ND2  sing N N 117 
ASN   ND2 HD21 sing N N 118 
ASN   ND2 HD22 sing N N 119 
ASN   OXT HXT  sing N N 120 
ASP   N   CA   sing N N 121 
ASP   N   H    sing N N 122 
ASP   N   H2   sing N N 123 
ASP   CA  C    sing N N 124 
ASP   CA  CB   sing N N 125 
ASP   CA  HA   sing N N 126 
ASP   C   O    doub N N 127 
ASP   C   OXT  sing N N 128 
ASP   CB  CG   sing N N 129 
ASP   CB  HB2  sing N N 130 
ASP   CB  HB3  sing N N 131 
ASP   CG  OD1  doub N N 132 
ASP   CG  OD2  sing N N 133 
ASP   OD2 HD2  sing N N 134 
ASP   OXT HXT  sing N N 135 
CYS   N   CA   sing N N 136 
CYS   N   H    sing N N 137 
CYS   N   H2   sing N N 138 
CYS   CA  C    sing N N 139 
CYS   CA  CB   sing N N 140 
CYS   CA  HA   sing N N 141 
CYS   C   O    doub N N 142 
CYS   C   OXT  sing N N 143 
CYS   CB  SG   sing N N 144 
CYS   CB  HB2  sing N N 145 
CYS   CB  HB3  sing N N 146 
CYS   SG  HG   sing N N 147 
CYS   OXT HXT  sing N N 148 
EPE   N1  C2   sing N N 149 
EPE   N1  C6   sing N N 150 
EPE   N1  C9   sing N N 151 
EPE   C2  C3   sing N N 152 
EPE   C2  H21  sing N N 153 
EPE   C2  H22  sing N N 154 
EPE   C3  N4   sing N N 155 
EPE   C3  H31  sing N N 156 
EPE   C3  H32  sing N N 157 
EPE   N4  C5   sing N N 158 
EPE   N4  C7   sing N N 159 
EPE   C5  C6   sing N N 160 
EPE   C5  H51  sing N N 161 
EPE   C5  H52  sing N N 162 
EPE   C6  H61  sing N N 163 
EPE   C6  H62  sing N N 164 
EPE   C7  C8   sing N N 165 
EPE   C7  H71  sing N N 166 
EPE   C7  H72  sing N N 167 
EPE   C8  O8   sing N N 168 
EPE   C8  H81  sing N N 169 
EPE   C8  H82  sing N N 170 
EPE   O8  HO8  sing N N 171 
EPE   C9  C10  sing N N 172 
EPE   C9  H91  sing N N 173 
EPE   C9  H92  sing N N 174 
EPE   C10 S    sing N N 175 
EPE   C10 H101 sing N N 176 
EPE   C10 H102 sing N N 177 
EPE   S   O1S  doub N N 178 
EPE   S   O2S  doub N N 179 
EPE   S   O3S  sing N N 180 
EPE   O3S HOS3 sing N N 181 
GLN   N   CA   sing N N 182 
GLN   N   H    sing N N 183 
GLN   N   H2   sing N N 184 
GLN   CA  C    sing N N 185 
GLN   CA  CB   sing N N 186 
GLN   CA  HA   sing N N 187 
GLN   C   O    doub N N 188 
GLN   C   OXT  sing N N 189 
GLN   CB  CG   sing N N 190 
GLN   CB  HB2  sing N N 191 
GLN   CB  HB3  sing N N 192 
GLN   CG  CD   sing N N 193 
GLN   CG  HG2  sing N N 194 
GLN   CG  HG3  sing N N 195 
GLN   CD  OE1  doub N N 196 
GLN   CD  NE2  sing N N 197 
GLN   NE2 HE21 sing N N 198 
GLN   NE2 HE22 sing N N 199 
GLN   OXT HXT  sing N N 200 
GLU   N   CA   sing N N 201 
GLU   N   H    sing N N 202 
GLU   N   H2   sing N N 203 
GLU   CA  C    sing N N 204 
GLU   CA  CB   sing N N 205 
GLU   CA  HA   sing N N 206 
GLU   C   O    doub N N 207 
GLU   C   OXT  sing N N 208 
GLU   CB  CG   sing N N 209 
GLU   CB  HB2  sing N N 210 
GLU   CB  HB3  sing N N 211 
GLU   CG  CD   sing N N 212 
GLU   CG  HG2  sing N N 213 
GLU   CG  HG3  sing N N 214 
GLU   CD  OE1  doub N N 215 
GLU   CD  OE2  sing N N 216 
GLU   OE2 HE2  sing N N 217 
GLU   OXT HXT  sing N N 218 
GLY   N   CA   sing N N 219 
GLY   N   H    sing N N 220 
GLY   N   H2   sing N N 221 
GLY   CA  C    sing N N 222 
GLY   CA  HA2  sing N N 223 
GLY   CA  HA3  sing N N 224 
GLY   C   O    doub N N 225 
GLY   C   OXT  sing N N 226 
GLY   OXT HXT  sing N N 227 
HIS   N   CA   sing N N 228 
HIS   N   H    sing N N 229 
HIS   N   H2   sing N N 230 
HIS   CA  C    sing N N 231 
HIS   CA  CB   sing N N 232 
HIS   CA  HA   sing N N 233 
HIS   C   O    doub N N 234 
HIS   C   OXT  sing N N 235 
HIS   CB  CG   sing N N 236 
HIS   CB  HB2  sing N N 237 
HIS   CB  HB3  sing N N 238 
HIS   CG  ND1  sing Y N 239 
HIS   CG  CD2  doub Y N 240 
HIS   ND1 CE1  doub Y N 241 
HIS   ND1 HD1  sing N N 242 
HIS   CD2 NE2  sing Y N 243 
HIS   CD2 HD2  sing N N 244 
HIS   CE1 NE2  sing Y N 245 
HIS   CE1 HE1  sing N N 246 
HIS   NE2 HE2  sing N N 247 
HIS   OXT HXT  sing N N 248 
HOH   O   H1   sing N N 249 
HOH   O   H2   sing N N 250 
ILE   N   CA   sing N N 251 
ILE   N   H    sing N N 252 
ILE   N   H2   sing N N 253 
ILE   CA  C    sing N N 254 
ILE   CA  CB   sing N N 255 
ILE   CA  HA   sing N N 256 
ILE   C   O    doub N N 257 
ILE   C   OXT  sing N N 258 
ILE   CB  CG1  sing N N 259 
ILE   CB  CG2  sing N N 260 
ILE   CB  HB   sing N N 261 
ILE   CG1 CD1  sing N N 262 
ILE   CG1 HG12 sing N N 263 
ILE   CG1 HG13 sing N N 264 
ILE   CG2 HG21 sing N N 265 
ILE   CG2 HG22 sing N N 266 
ILE   CG2 HG23 sing N N 267 
ILE   CD1 HD11 sing N N 268 
ILE   CD1 HD12 sing N N 269 
ILE   CD1 HD13 sing N N 270 
ILE   OXT HXT  sing N N 271 
LEU   N   CA   sing N N 272 
LEU   N   H    sing N N 273 
LEU   N   H2   sing N N 274 
LEU   CA  C    sing N N 275 
LEU   CA  CB   sing N N 276 
LEU   CA  HA   sing N N 277 
LEU   C   O    doub N N 278 
LEU   C   OXT  sing N N 279 
LEU   CB  CG   sing N N 280 
LEU   CB  HB2  sing N N 281 
LEU   CB  HB3  sing N N 282 
LEU   CG  CD1  sing N N 283 
LEU   CG  CD2  sing N N 284 
LEU   CG  HG   sing N N 285 
LEU   CD1 HD11 sing N N 286 
LEU   CD1 HD12 sing N N 287 
LEU   CD1 HD13 sing N N 288 
LEU   CD2 HD21 sing N N 289 
LEU   CD2 HD22 sing N N 290 
LEU   CD2 HD23 sing N N 291 
LEU   OXT HXT  sing N N 292 
LYS   N   CA   sing N N 293 
LYS   N   H    sing N N 294 
LYS   N   H2   sing N N 295 
LYS   CA  C    sing N N 296 
LYS   CA  CB   sing N N 297 
LYS   CA  HA   sing N N 298 
LYS   C   O    doub N N 299 
LYS   C   OXT  sing N N 300 
LYS   CB  CG   sing N N 301 
LYS   CB  HB2  sing N N 302 
LYS   CB  HB3  sing N N 303 
LYS   CG  CD   sing N N 304 
LYS   CG  HG2  sing N N 305 
LYS   CG  HG3  sing N N 306 
LYS   CD  CE   sing N N 307 
LYS   CD  HD2  sing N N 308 
LYS   CD  HD3  sing N N 309 
LYS   CE  NZ   sing N N 310 
LYS   CE  HE2  sing N N 311 
LYS   CE  HE3  sing N N 312 
LYS   NZ  HZ1  sing N N 313 
LYS   NZ  HZ2  sing N N 314 
LYS   NZ  HZ3  sing N N 315 
LYS   OXT HXT  sing N N 316 
MET   N   CA   sing N N 317 
MET   N   H    sing N N 318 
MET   N   H2   sing N N 319 
MET   CA  C    sing N N 320 
MET   CA  CB   sing N N 321 
MET   CA  HA   sing N N 322 
MET   C   O    doub N N 323 
MET   C   OXT  sing N N 324 
MET   CB  CG   sing N N 325 
MET   CB  HB2  sing N N 326 
MET   CB  HB3  sing N N 327 
MET   CG  SD   sing N N 328 
MET   CG  HG2  sing N N 329 
MET   CG  HG3  sing N N 330 
MET   SD  CE   sing N N 331 
MET   CE  HE1  sing N N 332 
MET   CE  HE2  sing N N 333 
MET   CE  HE3  sing N N 334 
MET   OXT HXT  sing N N 335 
MPD   C1  C2   sing N N 336 
MPD   C1  H11  sing N N 337 
MPD   C1  H12  sing N N 338 
MPD   C1  H13  sing N N 339 
MPD   C2  O2   sing N N 340 
MPD   C2  CM   sing N N 341 
MPD   C2  C3   sing N N 342 
MPD   O2  HO2  sing N N 343 
MPD   CM  HM1  sing N N 344 
MPD   CM  HM2  sing N N 345 
MPD   CM  HM3  sing N N 346 
MPD   C3  C4   sing N N 347 
MPD   C3  H31  sing N N 348 
MPD   C3  H32  sing N N 349 
MPD   C4  O4   sing N N 350 
MPD   C4  C5   sing N N 351 
MPD   C4  H4   sing N N 352 
MPD   O4  HO4  sing N N 353 
MPD   C5  H51  sing N N 354 
MPD   C5  H52  sing N N 355 
MPD   C5  H53  sing N N 356 
NAG   C1  C2   sing N N 357 
NAG   C1  O1   sing N N 358 
NAG   C1  O5   sing N N 359 
NAG   C1  H1   sing N N 360 
NAG   C2  C3   sing N N 361 
NAG   C2  N2   sing N N 362 
NAG   C2  H2   sing N N 363 
NAG   C3  C4   sing N N 364 
NAG   C3  O3   sing N N 365 
NAG   C3  H3   sing N N 366 
NAG   C4  C5   sing N N 367 
NAG   C4  O4   sing N N 368 
NAG   C4  H4   sing N N 369 
NAG   C5  C6   sing N N 370 
NAG   C5  O5   sing N N 371 
NAG   C5  H5   sing N N 372 
NAG   C6  O6   sing N N 373 
NAG   C6  H61  sing N N 374 
NAG   C6  H62  sing N N 375 
NAG   C7  C8   sing N N 376 
NAG   C7  N2   sing N N 377 
NAG   C7  O7   doub N N 378 
NAG   C8  H81  sing N N 379 
NAG   C8  H82  sing N N 380 
NAG   C8  H83  sing N N 381 
NAG   N2  HN2  sing N N 382 
NAG   O1  HO1  sing N N 383 
NAG   O3  HO3  sing N N 384 
NAG   O4  HO4  sing N N 385 
NAG   O6  HO6  sing N N 386 
PHE   N   CA   sing N N 387 
PHE   N   H    sing N N 388 
PHE   N   H2   sing N N 389 
PHE   CA  C    sing N N 390 
PHE   CA  CB   sing N N 391 
PHE   CA  HA   sing N N 392 
PHE   C   O    doub N N 393 
PHE   C   OXT  sing N N 394 
PHE   CB  CG   sing N N 395 
PHE   CB  HB2  sing N N 396 
PHE   CB  HB3  sing N N 397 
PHE   CG  CD1  doub Y N 398 
PHE   CG  CD2  sing Y N 399 
PHE   CD1 CE1  sing Y N 400 
PHE   CD1 HD1  sing N N 401 
PHE   CD2 CE2  doub Y N 402 
PHE   CD2 HD2  sing N N 403 
PHE   CE1 CZ   doub Y N 404 
PHE   CE1 HE1  sing N N 405 
PHE   CE2 CZ   sing Y N 406 
PHE   CE2 HE2  sing N N 407 
PHE   CZ  HZ   sing N N 408 
PHE   OXT HXT  sing N N 409 
PRO   N   CA   sing N N 410 
PRO   N   CD   sing N N 411 
PRO   N   H    sing N N 412 
PRO   CA  C    sing N N 413 
PRO   CA  CB   sing N N 414 
PRO   CA  HA   sing N N 415 
PRO   C   O    doub N N 416 
PRO   C   OXT  sing N N 417 
PRO   CB  CG   sing N N 418 
PRO   CB  HB2  sing N N 419 
PRO   CB  HB3  sing N N 420 
PRO   CG  CD   sing N N 421 
PRO   CG  HG2  sing N N 422 
PRO   CG  HG3  sing N N 423 
PRO   CD  HD2  sing N N 424 
PRO   CD  HD3  sing N N 425 
PRO   OXT HXT  sing N N 426 
SER   N   CA   sing N N 427 
SER   N   H    sing N N 428 
SER   N   H2   sing N N 429 
SER   CA  C    sing N N 430 
SER   CA  CB   sing N N 431 
SER   CA  HA   sing N N 432 
SER   C   O    doub N N 433 
SER   C   OXT  sing N N 434 
SER   CB  OG   sing N N 435 
SER   CB  HB2  sing N N 436 
SER   CB  HB3  sing N N 437 
SER   OG  HG   sing N N 438 
SER   OXT HXT  sing N N 439 
THR   N   CA   sing N N 440 
THR   N   H    sing N N 441 
THR   N   H2   sing N N 442 
THR   CA  C    sing N N 443 
THR   CA  CB   sing N N 444 
THR   CA  HA   sing N N 445 
THR   C   O    doub N N 446 
THR   C   OXT  sing N N 447 
THR   CB  OG1  sing N N 448 
THR   CB  CG2  sing N N 449 
THR   CB  HB   sing N N 450 
THR   OG1 HG1  sing N N 451 
THR   CG2 HG21 sing N N 452 
THR   CG2 HG22 sing N N 453 
THR   CG2 HG23 sing N N 454 
THR   OXT HXT  sing N N 455 
TRP   N   CA   sing N N 456 
TRP   N   H    sing N N 457 
TRP   N   H2   sing N N 458 
TRP   CA  C    sing N N 459 
TRP   CA  CB   sing N N 460 
TRP   CA  HA   sing N N 461 
TRP   C   O    doub N N 462 
TRP   C   OXT  sing N N 463 
TRP   CB  CG   sing N N 464 
TRP   CB  HB2  sing N N 465 
TRP   CB  HB3  sing N N 466 
TRP   CG  CD1  doub Y N 467 
TRP   CG  CD2  sing Y N 468 
TRP   CD1 NE1  sing Y N 469 
TRP   CD1 HD1  sing N N 470 
TRP   CD2 CE2  doub Y N 471 
TRP   CD2 CE3  sing Y N 472 
TRP   NE1 CE2  sing Y N 473 
TRP   NE1 HE1  sing N N 474 
TRP   CE2 CZ2  sing Y N 475 
TRP   CE3 CZ3  doub Y N 476 
TRP   CE3 HE3  sing N N 477 
TRP   CZ2 CH2  doub Y N 478 
TRP   CZ2 HZ2  sing N N 479 
TRP   CZ3 CH2  sing Y N 480 
TRP   CZ3 HZ3  sing N N 481 
TRP   CH2 HH2  sing N N 482 
TRP   OXT HXT  sing N N 483 
TYR   N   CA   sing N N 484 
TYR   N   H    sing N N 485 
TYR   N   H2   sing N N 486 
TYR   CA  C    sing N N 487 
TYR   CA  CB   sing N N 488 
TYR   CA  HA   sing N N 489 
TYR   C   O    doub N N 490 
TYR   C   OXT  sing N N 491 
TYR   CB  CG   sing N N 492 
TYR   CB  HB2  sing N N 493 
TYR   CB  HB3  sing N N 494 
TYR   CG  CD1  doub Y N 495 
TYR   CG  CD2  sing Y N 496 
TYR   CD1 CE1  sing Y N 497 
TYR   CD1 HD1  sing N N 498 
TYR   CD2 CE2  doub Y N 499 
TYR   CD2 HD2  sing N N 500 
TYR   CE1 CZ   doub Y N 501 
TYR   CE1 HE1  sing N N 502 
TYR   CE2 CZ   sing Y N 503 
TYR   CE2 HE2  sing N N 504 
TYR   CZ  OH   sing N N 505 
TYR   OH  HH   sing N N 506 
TYR   OXT HXT  sing N N 507 
VAL   N   CA   sing N N 508 
VAL   N   H    sing N N 509 
VAL   N   H2   sing N N 510 
VAL   CA  C    sing N N 511 
VAL   CA  CB   sing N N 512 
VAL   CA  HA   sing N N 513 
VAL   C   O    doub N N 514 
VAL   C   OXT  sing N N 515 
VAL   CB  CG1  sing N N 516 
VAL   CB  CG2  sing N N 517 
VAL   CB  HB   sing N N 518 
VAL   CG1 HG11 sing N N 519 
VAL   CG1 HG12 sing N N 520 
VAL   CG1 HG13 sing N N 521 
VAL   CG2 HG21 sing N N 522 
VAL   CG2 HG22 sing N N 523 
VAL   CG2 HG23 sing N N 524 
VAL   OXT HXT  sing N N 525 
# 
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                    9BXW 
_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]   0.015949 
_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]   0.014964 
_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]   0.010816 
_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   ? -23.919 -15.049 -0.118  1.00 61.41 ? 44  VAL   A N   1 
ATOM   2    C  CA  . VAL   A 1 3   ? -23.252 -14.311 0.946   1.00 60.73 ? 44  VAL   A CA  1 
ATOM   3    C  C   . VAL   A 1 3   ? -21.954 -13.725 0.401   1.00 60.91 ? 44  VAL   A C   1 
ATOM   4    O  O   . VAL   A 1 3   ? -21.346 -14.291 -0.512  1.00 63.31 ? 44  VAL   A O   1 
ATOM   5    C  CB  . VAL   A 1 3   ? -22.987 -15.203 2.170   1.00 64.32 ? 44  VAL   A CB  1 
ATOM   6    C  CG1 . VAL   A 1 3   ? -22.587 -14.352 3.362   1.00 61.76 ? 44  VAL   A CG1 1 
ATOM   7    C  CG2 . VAL   A 1 3   ? -24.208 -16.046 2.494   1.00 63.12 ? 44  VAL   A CG2 1 
ATOM   8    N  N   . TRP   A 1 4   ? -21.523 -12.597 0.965   1.00 59.02 ? 45  TRP   A N   1 
ATOM   9    C  CA  . TRP   A 1 4   ? -20.381 -11.876 0.421   1.00 57.64 ? 45  TRP   A CA  1 
ATOM   10   C  C   . TRP   A 1 4   ? -19.819 -10.941 1.480   1.00 58.81 ? 45  TRP   A C   1 
ATOM   11   O  O   . TRP   A 1 4   ? -20.469 -10.639 2.485   1.00 58.79 ? 45  TRP   A O   1 
ATOM   12   C  CB  . TRP   A 1 4   ? -20.770 -11.079 -0.830  1.00 55.31 ? 45  TRP   A CB  1 
ATOM   13   C  CG  . TRP   A 1 4   ? -21.612 -9.880  -0.500  1.00 56.38 ? 45  TRP   A CG  1 
ATOM   14   C  CD1 . TRP   A 1 4   ? -21.177 -8.662  -0.045  1.00 55.48 ? 45  TRP   A CD1 1 
ATOM   15   C  CD2 . TRP   A 1 4   ? -23.038 -9.794  -0.566  1.00 56.01 ? 45  TRP   A CD2 1 
ATOM   16   N  NE1 . TRP   A 1 4   ? -22.246 -7.822  0.159   1.00 54.63 ? 45  TRP   A NE1 1 
ATOM   17   C  CE2 . TRP   A 1 4   ? -23.399 -8.493  -0.154  1.00 55.83 ? 45  TRP   A CE2 1 
ATOM   18   C  CE3 . TRP   A 1 4   ? -24.045 -10.686 -0.943  1.00 56.49 ? 45  TRP   A CE3 1 
ATOM   19   C  CZ2 . TRP   A 1 4   ? -24.725 -8.065  -0.110  1.00 56.13 ? 45  TRP   A CZ2 1 
ATOM   20   C  CZ3 . TRP   A 1 4   ? -25.361 -10.259 -0.900  1.00 57.32 ? 45  TRP   A CZ3 1 
ATOM   21   C  CH2 . TRP   A 1 4   ? -25.689 -8.961  -0.486  1.00 57.17 ? 45  TRP   A CH2 1 
ATOM   22   N  N   . LYS   A 1 5   ? -18.607 -10.461 1.215   1.00 56.76 ? 46  LYS   A N   1 
ATOM   23   C  CA  . LYS   A 1 5   ? -17.951 -9.477  2.059   1.00 57.85 ? 46  LYS   A CA  1 
ATOM   24   C  C   . LYS   A 1 5   ? -17.174 -8.515  1.173   1.00 56.01 ? 46  LYS   A C   1 
ATOM   25   O  O   . LYS   A 1 5   ? -16.719 -8.877  0.085   1.00 53.02 ? 46  LYS   A O   1 
ATOM   26   C  CB  . LYS   A 1 5   ? -17.007 -10.137 3.077   1.00 59.10 ? 46  LYS   A CB  1 
ATOM   27   C  CG  . LYS   A 1 5   ? -16.172 -11.276 2.503   1.00 61.07 ? 46  LYS   A CG  1 
ATOM   28   C  CD  . LYS   A 1 5   ? -14.983 -11.619 3.393   1.00 66.30 ? 46  LYS   A CD  1 
ATOM   29   C  CE  . LYS   A 1 5   ? -13.801 -12.120 2.568   1.00 64.65 ? 46  LYS   A CE  1 
ATOM   30   N  NZ  . LYS   A 1 5   ? -12.670 -12.568 3.427   1.00 64.65 ? 46  LYS   A NZ  1 
ATOM   31   N  N   . ASP   A 1 6   ? -17.038 -7.279  1.642   1.00 56.84 ? 47  ASP   A N   1 
ATOM   32   C  CA  . ASP   A 1 6   ? -16.245 -6.296  0.921   1.00 56.16 ? 47  ASP   A CA  1 
ATOM   33   C  C   . ASP   A 1 6   ? -14.853 -6.849  0.650   1.00 56.37 ? 47  ASP   A C   1 
ATOM   34   O  O   . ASP   A 1 6   ? -14.202 -7.397  1.544   1.00 57.36 ? 47  ASP   A O   1 
ATOM   35   C  CB  . ASP   A 1 6   ? -16.153 -5.000  1.729   1.00 59.43 ? 47  ASP   A CB  1 
ATOM   36   C  CG  . ASP   A 1 6   ? -17.331 -4.079  1.494   1.00 61.86 ? 47  ASP   A CG  1 
ATOM   37   O  OD1 . ASP   A 1 6   ? -18.115 -4.338  0.556   1.00 60.19 ? 47  ASP   A OD1 1 
ATOM   38   O  OD2 . ASP   A 1 6   ? -17.465 -3.093  2.247   1.00 65.20 ? 47  ASP   A OD2 1 
ATOM   39   N  N   . ALA   A 1 7   ? -14.396 -6.702  -0.589  1.00 52.58 ? 48  ALA   A N   1 
ATOM   40   C  CA  . ALA   A 1 7   ? -13.109 -7.266  -0.960  1.00 50.71 ? 48  ALA   A CA  1 
ATOM   41   C  C   . ALA   A 1 7   ? -12.565 -6.536  -2.178  1.00 53.39 ? 48  ALA   A C   1 
ATOM   42   O  O   . ALA   A 1 7   ? -13.309 -5.903  -2.936  1.00 46.20 ? 48  ALA   A O   1 
ATOM   43   C  CB  . ALA   A 1 7   ? -13.219 -8.770  -1.238  1.00 52.94 ? 48  ALA   A CB  1 
ATOM   44   N  N   . ASP   A 1 8   ? -11.247 -6.624  -2.343  1.00 50.19 ? 49  ASP   A N   1 
ATOM   45   C  CA  . ASP   A 1 8   ? -10.565 -6.173  -3.545  1.00 47.97 ? 49  ASP   A CA  1 
ATOM   46   C  C   . ASP   A 1 8   ? -9.963  -7.374  -4.257  1.00 49.80 ? 49  ASP   A C   1 
ATOM   47   O  O   . ASP   A 1 8   ? -9.533  -8.338  -3.613  1.00 48.65 ? 49  ASP   A O   1 
ATOM   48   C  CB  . ASP   A 1 8   ? -9.465  -5.162  -3.221  1.00 49.93 ? 49  ASP   A CB  1 
ATOM   49   C  CG  . ASP   A 1 8   ? -10.004 -3.884  -2.624  1.00 49.49 ? 49  ASP   A CG  1 
ATOM   50   O  OD1 . ASP   A 1 8   ? -11.227 -3.658  -2.719  1.00 49.36 ? 49  ASP   A OD1 1 
ATOM   51   O  OD2 . ASP   A 1 8   ? -9.196  -3.113  -2.063  1.00 55.72 ? 49  ASP   A OD2 1 
ATOM   52   N  N   . THR   A 1 9   ? -9.946  -7.313  -5.587  1.00 44.87 ? 50  THR   A N   1 
ATOM   53   C  CA  . THR   A 1 9   ? -9.301  -8.326  -6.409  1.00 46.11 ? 50  THR   A CA  1 
ATOM   54   C  C   . THR   A 1 9   ? -8.916  -7.670  -7.725  1.00 42.98 ? 50  THR   A C   1 
ATOM   55   O  O   . THR   A 1 9   ? -9.334  -6.549  -8.023  1.00 42.36 ? 50  THR   A O   1 
ATOM   56   C  CB  . THR   A 1 9   ? -10.207 -9.550  -6.635  1.00 46.29 ? 50  THR   A CB  1 
ATOM   57   O  OG1 . THR   A 1 9   ? -9.439  -10.632 -7.185  1.00 49.27 ? 50  THR   A OG1 1 
ATOM   58   C  CG2 . THR   A 1 9   ? -11.352 -9.212  -7.584  1.00 45.71 ? 50  THR   A CG2 1 
ATOM   59   N  N   . THR   A 1 10  ? -8.101  -8.368  -8.512  1.00 43.27 ? 51  THR   A N   1 
ATOM   60   C  CA  . THR   A 1 10  ? -7.688  -7.846  -9.810  1.00 44.13 ? 51  THR   A CA  1 
ATOM   61   C  C   . THR   A 1 10  ? -8.825  -7.998  -10.815 1.00 40.24 ? 51  THR   A C   1 
ATOM   62   O  O   . THR   A 1 10  ? -9.341  -9.099  -11.020 1.00 41.12 ? 51  THR   A O   1 
ATOM   63   C  CB  . THR   A 1 10  ? -6.432  -8.563  -10.310 1.00 41.92 ? 51  THR   A CB  1 
ATOM   64   O  OG1 . THR   A 1 10  ? -5.386  -8.426  -9.340  1.00 48.84 ? 51  THR   A OG1 1 
ATOM   65   C  CG2 . THR   A 1 10  ? -5.963  -7.953  -11.620 1.00 48.58 ? 51  THR   A CG2 1 
ATOM   66   N  N   . LEU   A 1 11  ? -9.221  -6.892  -11.436 1.00 39.73 ? 52  LEU   A N   1 
ATOM   67   C  CA  . LEU   A 1 11  ? -10.289 -6.923  -12.422 1.00 39.65 ? 52  LEU   A CA  1 
ATOM   68   C  C   . LEU   A 1 11  ? -9.715  -7.206  -13.809 1.00 36.91 ? 52  LEU   A C   1 
ATOM   69   O  O   . LEU   A 1 11  ? -8.505  -7.146  -14.029 1.00 38.29 ? 52  LEU   A O   1 
ATOM   70   C  CB  . LEU   A 1 11  ? -11.057 -5.600  -12.407 1.00 39.31 ? 52  LEU   A CB  1 
ATOM   71   C  CG  . LEU   A 1 11  ? -11.794 -5.281  -11.100 1.00 39.71 ? 52  LEU   A CG  1 
ATOM   72   C  CD1 . LEU   A 1 11  ? -12.296 -3.852  -11.117 1.00 40.81 ? 52  LEU   A CD1 1 
ATOM   73   C  CD2 . LEU   A 1 11  ? -12.934 -6.250  -10.860 1.00 40.40 ? 52  LEU   A CD2 1 
ATOM   74   N  N   . PHE   A 1 12  ? -10.599 -7.542  -14.748 1.00 35.93 ? 53  PHE   A N   1 
ATOM   75   C  CA  . PHE   A 1 12  ? -10.248 -7.614  -16.161 1.00 38.02 ? 53  PHE   A CA  1 
ATOM   76   C  C   . PHE   A 1 12  ? -11.230 -6.761  -16.959 1.00 38.81 ? 53  PHE   A C   1 
ATOM   77   O  O   . PHE   A 1 12  ? -12.339 -6.472  -16.499 1.00 38.39 ? 53  PHE   A O   1 
ATOM   78   C  CB  . PHE   A 1 12  ? -10.187 -9.090  -16.655 1.00 37.76 ? 53  PHE   A CB  1 
ATOM   79   C  CG  . PHE   A 1 12  ? -11.535 -9.762  -16.821 1.00 40.73 ? 53  PHE   A CG  1 
ATOM   80   C  CD1 . PHE   A 1 12  ? -12.210 -9.708  -18.030 1.00 39.96 ? 53  PHE   A CD1 1 
ATOM   81   C  CD2 . PHE   A 1 12  ? -12.107 -10.481 -15.774 1.00 41.18 ? 53  PHE   A CD2 1 
ATOM   82   C  CE1 . PHE   A 1 12  ? -13.434 -10.338 -18.192 1.00 38.45 ? 53  PHE   A CE1 1 
ATOM   83   C  CE2 . PHE   A 1 12  ? -13.336 -11.112 -15.931 1.00 41.65 ? 53  PHE   A CE2 1 
ATOM   84   C  CZ  . PHE   A 1 12  ? -13.996 -11.039 -17.143 1.00 41.36 ? 53  PHE   A CZ  1 
ATOM   85   N  N   . CYS   A 1 13  ? -10.798 -6.305  -18.134 1.00 36.95 ? 54  CYS   A N   1 
ATOM   86   C  CA  . CYS   A 1 13  ? -11.565 -5.355  -18.931 1.00 40.96 ? 54  CYS   A CA  1 
ATOM   87   C  C   . CYS   A 1 13  ? -12.153 -6.028  -20.165 1.00 38.85 ? 54  CYS   A C   1 
ATOM   88   O  O   . CYS   A 1 13  ? -11.604 -7.006  -20.681 1.00 41.16 ? 54  CYS   A O   1 
ATOM   89   C  CB  . CYS   A 1 13  ? -10.704 -4.153  -19.361 1.00 41.00 ? 54  CYS   A CB  1 
ATOM   90   S  SG  . CYS   A 1 13  ? -9.215  -4.544  -20.347 1.00 46.99 ? 54  CYS   A SG  1 
ATOM   91   N  N   . ALA   A 1 14  ? -13.280 -5.487  -20.634 1.00 36.89 ? 55  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 14  ? -13.953 -5.974  -21.831 1.00 42.37 ? 55  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 14  ? -14.432 -4.785  -22.655 1.00 40.87 ? 55  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 14  ? -14.904 -3.789  -22.099 1.00 38.66 ? 55  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 14  ? -15.136 -6.888  -21.475 1.00 40.77 ? 55  ALA   A CB  1 
ATOM   96   N  N   . SER   A 1 15  ? -14.311 -4.891  -23.979 1.00 42.77 ? 56  SER   A N   1 
ATOM   97   C  CA  . SER   A 1 15  ? -14.689 -3.800  -24.869 1.00 47.84 ? 56  SER   A CA  1 
ATOM   98   C  C   . SER   A 1 15  ? -15.129 -4.356  -26.218 1.00 48.65 ? 56  SER   A C   1 
ATOM   99   O  O   . SER   A 1 15  ? -14.941 -5.537  -26.527 1.00 47.14 ? 56  SER   A O   1 
ATOM   100  C  CB  . SER   A 1 15  ? -13.538 -2.805  -25.062 1.00 45.93 ? 56  SER   A CB  1 
ATOM   101  O  OG  . SER   A 1 15  ? -12.444 -3.425  -25.719 1.00 51.39 ? 56  SER   A OG  1 
ATOM   102  N  N   . ASP   A 1 16  ? -15.722 -3.476  -27.022 1.00 49.66 ? 57  ASP   A N   1 
ATOM   103  C  CA  . ASP   A 1 16  ? -16.180 -3.782  -28.376 1.00 51.36 ? 57  ASP   A CA  1 
ATOM   104  C  C   . ASP   A 1 16  ? -15.151 -3.366  -29.422 1.00 53.75 ? 57  ASP   A C   1 
ATOM   105  O  O   . ASP   A 1 16  ? -15.505 -2.872  -30.497 1.00 55.69 ? 57  ASP   A O   1 
ATOM   106  C  CB  . ASP   A 1 16  ? -17.519 -3.099  -28.644 1.00 52.73 ? 57  ASP   A CB  1 
ATOM   107  C  CG  . ASP   A 1 16  ? -18.717 -3.970  -28.278 1.00 58.54 ? 57  ASP   A CG  1 
ATOM   108  O  OD1 . ASP   A 1 16  ? -18.716 -4.568  -27.183 1.00 56.75 ? 57  ASP   A OD1 1 
ATOM   109  O  OD2 . ASP   A 1 16  ? -19.667 -4.050  -29.090 1.00 65.88 ? 57  ASP   A OD2 1 
ATOM   110  N  N   . ALA   A 1 17  ? -13.866 -3.550  -29.128 1.00 49.44 ? 58  ALA   A N   1 
ATOM   111  C  CA  . ALA   A 1 17  ? -12.822 -3.102  -30.038 1.00 49.93 ? 58  ALA   A CA  1 
ATOM   112  C  C   . ALA   A 1 17  ? -12.934 -3.807  -31.383 1.00 54.33 ? 58  ALA   A C   1 
ATOM   113  O  O   . ALA   A 1 17  ? -13.394 -4.950  -31.480 1.00 55.84 ? 58  ALA   A O   1 
ATOM   114  C  CB  . ALA   A 1 17  ? -11.440 -3.351  -29.435 1.00 50.31 ? 58  ALA   A CB  1 
ATOM   115  N  N   . LYS   A 1 18  ? -12.490 -3.111  -32.426 1.00 55.52 ? 59  LYS   A N   1 
ATOM   116  C  CA  . LYS   A 1 18  ? -12.556 -3.588  -33.798 1.00 58.81 ? 59  LYS   A CA  1 
ATOM   117  C  C   . LYS   A 1 18  ? -11.174 -4.005  -34.286 1.00 58.80 ? 59  LYS   A C   1 
ATOM   118  O  O   . LYS   A 1 18  ? -10.145 -3.568  -33.764 1.00 55.51 ? 59  LYS   A O   1 
ATOM   119  C  CB  . LYS   A 1 18  ? -13.128 -2.508  -34.721 1.00 59.28 ? 59  LYS   A CB  1 
ATOM   120  C  CG  . LYS   A 1 18  ? -14.549 -2.087  -34.385 1.00 64.30 ? 59  LYS   A CG  1 
ATOM   121  C  CD  . LYS   A 1 18  ? -15.498 -3.276  -34.409 1.00 66.70 ? 59  LYS   A CD  1 
ATOM   122  C  CE  . LYS   A 1 18  ? -16.668 -3.021  -35.346 1.00 71.44 ? 59  LYS   A CE  1 
ATOM   123  N  NZ  . LYS   A 1 18  ? -17.976 -3.169  -34.643 1.00 71.89 ? 59  LYS   A NZ  1 
ATOM   124  N  N   . ALA   A 1 19  ? -11.164 -4.850  -35.316 1.00 64.13 ? 60  ALA   A N   1 
ATOM   125  C  CA  . ALA   A 1 19  ? -9.926  -5.339  -35.910 1.00 63.35 ? 60  ALA   A CA  1 
ATOM   126  C  C   . ALA   A 1 19  ? -9.436  -4.397  -37.010 1.00 60.33 ? 60  ALA   A C   1 
ATOM   127  O  O   . ALA   A 1 19  ? -10.235 -3.842  -37.771 1.00 59.63 ? 60  ALA   A O   1 
ATOM   128  C  CB  . ALA   A 1 19  ? -10.130 -6.751  -36.466 1.00 65.26 ? 60  ALA   A CB  1 
ATOM   129  N  N   . TYR   A 1 20  ? -8.112  -4.217  -37.077 1.00 59.11 ? 61  TYR   A N   1 
ATOM   130  C  CA  . TYR   A 1 20  ? -7.435  -3.379  -38.064 1.00 57.07 ? 61  TYR   A CA  1 
ATOM   131  C  C   . TYR   A 1 20  ? -7.556  -1.881  -37.800 1.00 51.72 ? 61  TYR   A C   1 
ATOM   132  O  O   . TYR   A 1 20  ? -6.811  -1.092  -38.391 1.00 47.51 ? 61  TYR   A O   1 
ATOM   133  C  CB  . TYR   A 1 20  ? -7.934  -3.671  -39.480 1.00 60.21 ? 61  TYR   A CB  1 
ATOM   134  C  CG  . TYR   A 1 20  ? -8.021  -5.129  -39.874 1.00 63.51 ? 61  TYR   A CG  1 
ATOM   135  C  CD1 . TYR   A 1 20  ? -6.915  -5.966  -39.781 1.00 62.78 ? 61  TYR   A CD1 1 
ATOM   136  C  CD2 . TYR   A 1 20  ? -9.192  -5.650  -40.407 1.00 66.80 ? 61  TYR   A CD2 1 
ATOM   137  C  CE1 . TYR   A 1 20  ? -6.987  -7.298  -40.173 1.00 70.69 ? 61  TYR   A CE1 1 
ATOM   138  C  CE2 . TYR   A 1 20  ? -9.273  -6.971  -40.803 1.00 65.36 ? 61  TYR   A CE2 1 
ATOM   139  C  CZ  . TYR   A 1 20  ? -8.170  -7.792  -40.686 1.00 71.42 ? 61  TYR   A CZ  1 
ATOM   140  O  OH  . TYR   A 1 20  ? -8.278  -9.104  -41.089 1.00 63.55 ? 61  TYR   A OH  1 
ATOM   141  N  N   . GLU   A 1 21  ? -8.473  -1.461  -36.936 1.00 51.92 ? 62  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 21  ? -8.588  -0.039  -36.651 1.00 52.26 ? 62  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 21  ? -7.350  0.426   -35.896 1.00 47.44 ? 62  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 21  ? -6.908  -0.226  -34.946 1.00 46.91 ? 62  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 21  ? -9.856  0.247   -35.850 1.00 52.04 ? 62  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 21  ? -9.851  1.592   -35.138 1.00 50.51 ? 62  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 21  ? -10.283 2.746   -36.039 1.00 53.41 ? 62  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 21  ? -9.405  3.368   -36.681 1.00 55.38 ? 62  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 21  ? -11.499 3.038   -36.097 1.00 61.90 ? 62  GLU   A OE2 1 
ATOM   150  N  N   . THR   A 1 22  ? -6.775  1.541   -36.336 1.00 45.73 ? 63  THR   A N   1 
ATOM   151  C  CA  . THR   A 1 22  ? -5.539  2.041   -35.755 1.00 43.68 ? 63  THR   A CA  1 
ATOM   152  C  C   . THR   A 1 22  ? -5.766  3.018   -34.608 1.00 42.98 ? 63  THR   A C   1 
ATOM   153  O  O   . THR   A 1 22  ? -4.796  3.398   -33.945 1.00 40.95 ? 63  THR   A O   1 
ATOM   154  C  CB  . THR   A 1 22  ? -4.685  2.713   -36.836 1.00 46.16 ? 63  THR   A CB  1 
ATOM   155  O  OG1 . THR   A 1 22  ? -5.427  3.775   -37.449 1.00 48.14 ? 63  THR   A OG1 1 
ATOM   156  C  CG2 . THR   A 1 22  ? -4.272  1.701   -37.902 1.00 45.11 ? 63  THR   A CG2 1 
ATOM   157  N  N   . GLU   A 1 23  ? -7.006  3.442   -34.365 1.00 39.66 ? 64  GLU   A N   1 
ATOM   158  C  CA  . GLU   A 1 23  ? -7.291  4.304   -33.225 1.00 41.15 ? 64  GLU   A CA  1 
ATOM   159  C  C   . GLU   A 1 23  ? -6.730  3.682   -31.949 1.00 38.51 ? 64  GLU   A C   1 
ATOM   160  O  O   . GLU   A 1 23  ? -6.857  2.477   -31.718 1.00 37.43 ? 64  GLU   A O   1 
ATOM   161  C  CB  . GLU   A 1 23  ? -8.801  4.532   -33.113 1.00 42.31 ? 64  GLU   A CB  1 
ATOM   162  C  CG  . GLU   A 1 23  ? -9.204  5.674   -32.196 1.00 40.31 ? 64  GLU   A CG  1 
ATOM   163  C  CD  . GLU   A 1 23  ? -9.149  5.281   -30.734 1.00 39.40 ? 64  GLU   A CD  1 
ATOM   164  O  OE1 . GLU   A 1 23  ? -9.558  4.139   -30.435 1.00 38.30 ? 64  GLU   A OE1 1 
ATOM   165  O  OE2 . GLU   A 1 23  ? -8.705  6.103   -29.895 1.00 38.51 ? 64  GLU   A OE2 1 
ATOM   166  N  N   . VAL   A 1 24  ? -6.092  4.514   -31.122 1.00 36.34 ? 65  VAL   A N   1 
ATOM   167  C  CA  . VAL   A 1 24  ? -5.253  3.983   -30.050 1.00 36.78 ? 65  VAL   A CA  1 
ATOM   168  C  C   . VAL   A 1 24  ? -6.088  3.249   -29.005 1.00 35.27 ? 65  VAL   A C   1 
ATOM   169  O  O   . VAL   A 1 24  ? -5.664  2.216   -28.481 1.00 35.91 ? 65  VAL   A O   1 
ATOM   170  C  CB  . VAL   A 1 24  ? -4.395  5.104   -29.427 1.00 37.25 ? 65  VAL   A CB  1 
ATOM   171  C  CG1 . VAL   A 1 24  ? -3.401  5.652   -30.453 1.00 38.19 ? 65  VAL   A CG1 1 
ATOM   172  C  CG2 . VAL   A 1 24  ? -5.270  6.220   -28.869 1.00 33.73 ? 65  VAL   A CG2 1 
ATOM   173  N  N   . HIS   A 1 25  ? -7.281  3.754   -28.682 1.00 35.45 ? 66  HIS   A N   1 
ATOM   174  C  CA  . HIS   A 1 25  ? -8.116  3.058   -27.705 1.00 37.06 ? 66  HIS   A CA  1 
ATOM   175  C  C   . HIS   A 1 25  ? -8.523  1.682   -28.218 1.00 40.17 ? 66  HIS   A C   1 
ATOM   176  O  O   . HIS   A 1 25  ? -8.550  0.708   -27.454 1.00 38.48 ? 66  HIS   A O   1 
ATOM   177  C  CB  . HIS   A 1 25  ? -9.347  3.897   -27.364 1.00 34.45 ? 66  HIS   A CB  1 
ATOM   178  C  CG  . HIS   A 1 25  ? -9.022  5.222   -26.745 1.00 37.26 ? 66  HIS   A CG  1 
ATOM   179  N  ND1 . HIS   A 1 25  ? -8.661  6.326   -27.487 1.00 35.49 ? 66  HIS   A ND1 1 
ATOM   180  C  CD2 . HIS   A 1 25  ? -9.004  5.617   -25.450 1.00 36.84 ? 66  HIS   A CD2 1 
ATOM   181  C  CE1 . HIS   A 1 25  ? -8.433  7.343   -26.676 1.00 37.63 ? 66  HIS   A CE1 1 
ATOM   182  N  NE2 . HIS   A 1 25  ? -8.633  6.939   -25.434 1.00 37.91 ? 66  HIS   A NE2 1 
ATOM   183  N  N   . ASN   A 1 26  ? -8.842  1.584   -29.512 1.00 38.79 ? 67  ASN   A N   1 
ATOM   184  C  CA  . ASN   A 1 26  ? -9.124  0.288   -30.119 1.00 37.60 ? 67  ASN   A CA  1 
ATOM   185  C  C   . ASN   A 1 26  ? -7.916  -0.636  -30.025 1.00 36.58 ? 67  ASN   A C   1 
ATOM   186  O  O   . ASN   A 1 26  ? -8.036  -1.794  -29.607 1.00 33.61 ? 67  ASN   A O   1 
ATOM   187  C  CB  . ASN   A 1 26  ? -9.539  0.478   -31.579 1.00 37.81 ? 67  ASN   A CB  1 
ATOM   188  C  CG  . ASN   A 1 26  ? -11.026 0.745   -31.739 1.00 45.26 ? 67  ASN   A CG  1 
ATOM   189  O  OD1 . ASN   A 1 26  ? -11.825 -0.187  -31.876 1.00 49.96 ? 67  ASN   A OD1 1 
ATOM   190  N  ND2 . ASN   A 1 26  ? -11.405 2.021   -31.740 1.00 43.80 ? 67  ASN   A ND2 1 
ATOM   191  N  N   . VAL   A 1 27  ? -6.741  -0.143  -30.432 1.00 35.89 ? 68  VAL   A N   1 
ATOM   192  C  CA  . VAL   A 1 27  ? -5.534  -0.965  -30.400 1.00 34.34 ? 68  VAL   A CA  1 
ATOM   193  C  C   . VAL   A 1 27  ? -5.261  -1.459  -28.985 1.00 37.86 ? 68  VAL   A C   1 
ATOM   194  O  O   . VAL   A 1 27  ? -4.936  -2.634  -28.775 1.00 35.08 ? 68  VAL   A O   1 
ATOM   195  C  CB  . VAL   A 1 27  ? -4.335  -0.180  -30.966 1.00 38.40 ? 68  VAL   A CB  1 
ATOM   196  C  CG1 . VAL   A 1 27  ? -3.022  -0.849  -30.566 1.00 39.47 ? 68  VAL   A CG1 1 
ATOM   197  C  CG2 . VAL   A 1 27  ? -4.438  -0.037  -32.498 1.00 38.53 ? 68  VAL   A CG2 1 
ATOM   198  N  N   . TRP   A 1 28  ? -5.391  -0.575  -27.991 1.00 36.82 ? 69  TRP   A N   1 
ATOM   199  C  CA  . TRP   A 1 28  ? -5.111  -0.977  -26.616 1.00 34.94 ? 69  TRP   A CA  1 
ATOM   200  C  C   . TRP   A 1 28  ? -6.113  -2.016  -26.124 1.00 36.70 ? 69  TRP   A C   1 
ATOM   201  O  O   . TRP   A 1 28  ? -5.729  -2.999  -25.479 1.00 37.62 ? 69  TRP   A O   1 
ATOM   202  C  CB  . TRP   A 1 28  ? -5.113  0.246   -25.698 1.00 35.10 ? 69  TRP   A CB  1 
ATOM   203  C  CG  . TRP   A 1 28  ? -4.839  -0.099  -24.265 1.00 36.47 ? 69  TRP   A CG  1 
ATOM   204  C  CD1 . TRP   A 1 28  ? -3.618  -0.199  -23.660 1.00 36.27 ? 69  TRP   A CD1 1 
ATOM   205  C  CD2 . TRP   A 1 28  ? -5.811  -0.400  -23.259 1.00 34.73 ? 69  TRP   A CD2 1 
ATOM   206  N  NE1 . TRP   A 1 28  ? -3.770  -0.537  -22.339 1.00 35.17 ? 69  TRP   A NE1 1 
ATOM   207  C  CE2 . TRP   A 1 28  ? -5.107  -0.668  -22.066 1.00 35.62 ? 69  TRP   A CE2 1 
ATOM   208  C  CE3 . TRP   A 1 28  ? -7.208  -0.467  -23.250 1.00 36.21 ? 69  TRP   A CE3 1 
ATOM   209  C  CZ2 . TRP   A 1 28  ? -5.752  -0.996  -20.876 1.00 36.51 ? 69  TRP   A CZ2 1 
ATOM   210  C  CZ3 . TRP   A 1 28  ? -7.848  -0.796  -22.071 1.00 37.68 ? 69  TRP   A CZ3 1 
ATOM   211  C  CH2 . TRP   A 1 28  ? -7.120  -1.057  -20.898 1.00 36.24 ? 69  TRP   A CH2 1 
ATOM   212  N  N   . ALA   A 1 29  ? -7.402  -1.813  -26.406 1.00 37.56 ? 70  ALA   A N   1 
ATOM   213  C  CA  . ALA   A 1 29  ? -8.413  -2.774  -25.975 1.00 38.52 ? 70  ALA   A CA  1 
ATOM   214  C  C   . ALA   A 1 29  ? -8.273  -4.102  -26.705 1.00 38.95 ? 70  ALA   A C   1 
ATOM   215  O  O   . ALA   A 1 29  ? -8.674  -5.145  -26.176 1.00 41.16 ? 70  ALA   A O   1 
ATOM   216  C  CB  . ALA   A 1 29  ? -9.813  -2.201  -26.195 1.00 40.43 ? 70  ALA   A CB  1 
ATOM   217  N  N   . THR   A 1 30  ? -7.713  -4.082  -27.916 1.00 38.70 ? 71  THR   A N   1 
ATOM   218  C  CA  . THR   A 1 30  ? -7.570  -5.310  -28.690 1.00 40.10 ? 71  THR   A CA  1 
ATOM   219  C  C   . THR   A 1 30  ? -6.618  -6.283  -28.007 1.00 41.60 ? 71  THR   A C   1 
ATOM   220  O  O   . THR   A 1 30  ? -6.878  -7.490  -27.971 1.00 46.80 ? 71  THR   A O   1 
ATOM   221  C  CB  . THR   A 1 30  ? -7.092  -4.981  -30.108 1.00 40.61 ? 71  THR   A CB  1 
ATOM   222  O  OG1 . THR   A 1 30  ? -8.206  -4.550  -30.903 1.00 45.33 ? 71  THR   A OG1 1 
ATOM   223  C  CG2 . THR   A 1 30  ? -6.456  -6.198  -30.759 1.00 40.54 ? 71  THR   A CG2 1 
ATOM   224  N  N   . HIS   A 1 31  ? -5.520  -5.787  -27.443 1.00 40.74 ? 72  HIS   A N   1 
ATOM   225  C  CA  . HIS   A 1 31  ? -4.553  -6.677  -26.814 1.00 41.81 ? 72  HIS   A CA  1 
ATOM   226  C  C   . HIS   A 1 31  ? -4.677  -6.744  -25.296 1.00 40.62 ? 72  HIS   A C   1 
ATOM   227  O  O   . HIS   A 1 31  ? -4.085  -7.641  -24.686 1.00 42.25 ? 72  HIS   A O   1 
ATOM   228  C  CB  . HIS   A 1 31  ? -3.121  -6.270  -27.206 1.00 41.92 ? 72  HIS   A CB  1 
ATOM   229  C  CG  . HIS   A 1 31  ? -2.643  -4.996  -26.572 1.00 42.70 ? 72  HIS   A CG  1 
ATOM   230  N  ND1 . HIS   A 1 31  ? -2.753  -4.742  -25.221 1.00 45.67 ? 72  HIS   A ND1 1 
ATOM   231  C  CD2 . HIS   A 1 31  ? -2.041  -3.907  -27.109 1.00 43.36 ? 72  HIS   A CD2 1 
ATOM   232  C  CE1 . HIS   A 1 31  ? -2.247  -3.551  -24.953 1.00 42.07 ? 72  HIS   A CE1 1 
ATOM   233  N  NE2 . HIS   A 1 31  ? -1.807  -3.023  -26.081 1.00 44.59 ? 72  HIS   A NE2 1 
ATOM   234  N  N   . ALA   A 1 32  ? -5.420  -5.828  -24.668 1.00 41.53 ? 73  ALA   A N   1 
ATOM   235  C  CA  . ALA   A 1 32  ? -5.489  -5.764  -23.214 1.00 38.08 ? 73  ALA   A CA  1 
ATOM   236  C  C   . ALA   A 1 32  ? -6.839  -6.162  -22.632 1.00 36.35 ? 73  ALA   A C   1 
ATOM   237  O  O   . ALA   A 1 32  ? -6.930  -6.356  -21.415 1.00 38.03 ? 73  ALA   A O   1 
ATOM   238  C  CB  . ALA   A 1 32  ? -5.132  -4.352  -22.728 1.00 37.78 ? 73  ALA   A CB  1 
ATOM   239  N  N   . CYS   A 1 33  ? -7.877  -6.306  -23.452 1.00 37.82 ? 74  CYS   A N   1 
ATOM   240  C  CA  . CYS   A 1 33  ? -9.222  -6.607  -22.985 1.00 38.34 ? 74  CYS   A CA  1 
ATOM   241  C  C   . CYS   A 1 33  ? -9.794  -7.787  -23.762 1.00 39.96 ? 74  CYS   A C   1 
ATOM   242  O  O   . CYS   A 1 33  ? -9.280  -8.182  -24.812 1.00 40.83 ? 74  CYS   A O   1 
ATOM   243  C  CB  . CYS   A 1 33  ? -10.145 -5.387  -23.127 1.00 41.82 ? 74  CYS   A CB  1 
ATOM   244  S  SG  . CYS   A 1 33  ? -9.601  -3.895  -22.243 1.00 40.86 ? 74  CYS   A SG  1 
ATOM   245  N  N   . VAL   A 1 34  ? -10.874 -8.352  -23.228 1.00 39.11 ? 75  VAL   A N   1 
ATOM   246  C  CA  . VAL   A 1 34  ? -11.597 -9.442  -23.882 1.00 43.53 ? 75  VAL   A CA  1 
ATOM   247  C  C   . VAL   A 1 34  ? -12.802 -8.857  -24.614 1.00 43.58 ? 75  VAL   A C   1 
ATOM   248  O  O   . VAL   A 1 34  ? -13.110 -7.670  -24.439 1.00 43.92 ? 75  VAL   A O   1 
ATOM   249  C  CB  . VAL   A 1 34  ? -12.028 -10.515 -22.869 1.00 42.30 ? 75  VAL   A CB  1 
ATOM   250  C  CG1 . VAL   A 1 34  ? -10.829 -11.004 -22.063 1.00 44.19 ? 75  VAL   A CG1 1 
ATOM   251  C  CG2 . VAL   A 1 34  ? -13.107 -9.978  -21.958 1.00 38.04 ? 75  VAL   A CG2 1 
ATOM   252  N  N   . PRO   A 1 35  ? -13.495 -9.631  -25.448 1.00 44.63 ? 76  PRO   A N   1 
ATOM   253  C  CA  . PRO   A 1 35  ? -14.733 -9.132  -26.055 1.00 46.34 ? 76  PRO   A CA  1 
ATOM   254  C  C   . PRO   A 1 35  ? -15.816 -8.910  -25.008 1.00 48.28 ? 76  PRO   A C   1 
ATOM   255  O  O   . PRO   A 1 35  ? -15.858 -9.572  -23.969 1.00 45.68 ? 76  PRO   A O   1 
ATOM   256  C  CB  . PRO   A 1 35  ? -15.120 -10.251 -27.030 1.00 48.40 ? 76  PRO   A CB  1 
ATOM   257  C  CG  . PRO   A 1 35  ? -13.804 -10.947 -27.325 1.00 50.10 ? 76  PRO   A CG  1 
ATOM   258  C  CD  . PRO   A 1 35  ? -13.115 -10.944 -25.995 1.00 45.82 ? 76  PRO   A CD  1 
ATOM   259  N  N   . THR   A 1 36  ? -16.700 -7.958  -25.299 1.00 46.70 ? 77  THR   A N   1 
ATOM   260  C  CA  . THR   A 1 36  ? -17.775 -7.619  -24.376 1.00 47.81 ? 77  THR   A CA  1 
ATOM   261  C  C   . THR   A 1 36  ? -18.695 -8.819  -24.167 1.00 54.06 ? 77  THR   A C   1 
ATOM   262  O  O   . THR   A 1 36  ? -18.874 -9.657  -25.054 1.00 55.17 ? 77  THR   A O   1 
ATOM   263  C  CB  . THR   A 1 36  ? -18.568 -6.421  -24.909 1.00 50.20 ? 77  THR   A CB  1 
ATOM   264  O  OG1 . THR   A 1 36  ? -17.697 -5.287  -25.011 1.00 49.28 ? 77  THR   A OG1 1 
ATOM   265  C  CG2 . THR   A 1 36  ? -19.721 -6.074  -23.981 1.00 50.51 ? 77  THR   A CG2 1 
ATOM   266  N  N   . ASP   A 1 37  ? -19.269 -8.905  -22.971 1.00 56.31 ? 78  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 37  ? -20.176 -9.997  -22.641 1.00 59.38 ? 78  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 37  ? -21.337 -10.040 -23.631 1.00 58.09 ? 78  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 37  ? -22.183 -9.136  -23.637 1.00 53.84 ? 78  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 37  ? -20.694 -9.843  -21.209 1.00 56.96 ? 78  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 37  ? -21.320 -11.119 -20.670 1.00 60.63 ? 78  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 37  ? -21.762 -11.960 -21.483 1.00 60.61 ? 78  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 37  ? -21.375 -11.275 -19.430 1.00 63.85 ? 78  ASP   A OD2 1 
ATOM   274  N  N   . PRO   A 1 38  ? -21.418 -11.078 -24.469 1.00 61.44 ? 79  PRO   A N   1 
ATOM   275  C  CA  . PRO   A 1 38  ? -22.511 -11.140 -25.454 1.00 59.92 ? 79  PRO   A CA  1 
ATOM   276  C  C   . PRO   A 1 38  ? -23.890 -11.207 -24.823 1.00 60.52 ? 79  PRO   A C   1 
ATOM   277  O  O   . PRO   A 1 38  ? -24.858 -10.712 -25.414 1.00 61.06 ? 79  PRO   A O   1 
ATOM   278  C  CB  . PRO   A 1 38  ? -22.193 -12.419 -26.243 1.00 57.67 ? 79  PRO   A CB  1 
ATOM   279  C  CG  . PRO   A 1 38  ? -21.385 -13.248 -25.293 1.00 58.69 ? 79  PRO   A CG  1 
ATOM   280  C  CD  . PRO   A 1 38  ? -20.545 -12.262 -24.538 1.00 59.65 ? 79  PRO   A CD  1 
ATOM   281  N  N   . ASN   A 1 39  ? -24.017 -11.805 -23.640 1.00 58.44 ? 80  ASN   A N   1 
ATOM   282  C  CA  . ASN   A 1 39  ? -25.309 -11.954 -22.969 1.00 62.23 ? 80  ASN   A CA  1 
ATOM   283  C  C   . ASN   A 1 39  ? -25.168 -11.581 -21.503 1.00 59.73 ? 80  ASN   A C   1 
ATOM   284  O  O   . ASN   A 1 39  ? -25.078 -12.449 -20.627 1.00 60.90 ? 80  ASN   A O   1 
ATOM   285  C  CB  . ASN   A 1 39  ? -25.847 -13.380 -23.123 1.00 62.77 ? 80  ASN   A CB  1 
ATOM   286  C  CG  . ASN   A 1 39  ? -27.303 -13.502 -22.709 1.00 66.01 ? 80  ASN   A CG  1 
ATOM   287  O  OD1 . ASN   A 1 39  ? -27.700 -14.484 -22.078 1.00 66.50 ? 80  ASN   A OD1 1 
ATOM   288  N  ND2 . ASN   A 1 39  ? -28.106 -12.495 -23.052 1.00 66.92 ? 80  ASN   A ND2 1 
ATOM   289  N  N   . PRO   A 1 40  ? -25.153 -10.288 -21.193 1.00 60.01 ? 81  PRO   A N   1 
ATOM   290  C  CA  . PRO   A 1 40  ? -25.102 -9.867  -19.791 1.00 61.77 ? 81  PRO   A CA  1 
ATOM   291  C  C   . PRO   A 1 40  ? -26.481 -9.895  -19.148 1.00 58.07 ? 81  PRO   A C   1 
ATOM   292  O  O   . PRO   A 1 40  ? -27.499 -9.617  -19.785 1.00 58.95 ? 81  PRO   A O   1 
ATOM   293  C  CB  . PRO   A 1 40  ? -24.568 -8.433  -19.879 1.00 58.30 ? 81  PRO   A CB  1 
ATOM   294  C  CG  . PRO   A 1 40  ? -25.090 -7.945  -21.188 1.00 60.86 ? 81  PRO   A CG  1 
ATOM   295  C  CD  . PRO   A 1 40  ? -25.076 -9.140  -22.115 1.00 61.02 ? 81  PRO   A CD  1 
ATOM   296  N  N   . GLN   A 1 41  ? -26.505 -10.239 -17.860 1.00 59.23 ? 82  GLN   A N   1 
ATOM   297  C  CA  . GLN   A 1 41  ? -27.768 -10.267 -17.121 1.00 59.10 ? 82  GLN   A CA  1 
ATOM   298  C  C   . GLN   A 1 41  ? -27.489 -10.073 -15.636 1.00 58.27 ? 82  GLN   A C   1 
ATOM   299  O  O   . GLN   A 1 41  ? -26.864 -10.931 -15.005 1.00 59.99 ? 82  GLN   A O   1 
ATOM   300  C  CB  . GLN   A 1 41  ? -28.514 -11.573 -17.372 1.00 61.95 ? 82  GLN   A CB  1 
ATOM   301  C  CG  . GLN   A 1 41  ? -29.768 -11.725 -16.530 1.00 58.96 ? 82  GLN   A CG  1 
ATOM   302  C  CD  . GLN   A 1 41  ? -30.774 -10.613 -16.782 1.00 58.04 ? 82  GLN   A CD  1 
ATOM   303  O  OE1 . GLN   A 1 41  ? -31.456 -10.595 -17.810 1.00 59.74 ? 82  GLN   A OE1 1 
ATOM   304  N  NE2 . GLN   A 1 41  ? -30.866 -9.675  -15.846 1.00 56.72 ? 82  GLN   A NE2 1 
ATOM   305  N  N   . GLU   A 1 42  ? -27.972 -8.965  -15.081 1.00 56.97 ? 83  GLU   A N   1 
ATOM   306  C  CA  . GLU   A 1 42  ? -27.836 -8.689  -13.659 1.00 54.18 ? 83  GLU   A CA  1 
ATOM   307  C  C   . GLU   A 1 42  ? -28.846 -9.496  -12.845 1.00 55.19 ? 83  GLU   A C   1 
ATOM   308  O  O   . GLU   A 1 42  ? -29.934 -9.833  -13.319 1.00 53.52 ? 83  GLU   A O   1 
ATOM   309  C  CB  . GLU   A 1 42  ? -28.035 -7.199  -13.397 1.00 52.17 ? 83  GLU   A CB  1 
ATOM   310  C  CG  . GLU   A 1 42  ? -29.498 -6.797  -13.324 1.00 55.03 ? 83  GLU   A CG  1 
ATOM   311  C  CD  . GLU   A 1 42  ? -29.701 -5.292  -13.358 1.00 61.02 ? 83  GLU   A CD  1 
ATOM   312  O  OE1 . GLU   A 1 42  ? -29.274 -4.651  -14.346 1.00 60.90 ? 83  GLU   A OE1 1 
ATOM   313  O  OE2 . GLU   A 1 42  ? -30.296 -4.752  -12.399 1.00 63.02 ? 83  GLU   A OE2 1 
ATOM   314  N  N   . ILE   A 1 43  ? -28.476 -9.803  -11.605 1.00 52.59 ? 84  ILE   A N   1 
ATOM   315  C  CA  . ILE   A 1 43  ? -29.352 -10.499 -10.667 1.00 53.34 ? 84  ILE   A CA  1 
ATOM   316  C  C   . ILE   A 1 43  ? -29.757 -9.501  -9.594  1.00 52.42 ? 84  ILE   A C   1 
ATOM   317  O  O   . ILE   A 1 43  ? -28.895 -8.898  -8.943  1.00 51.19 ? 84  ILE   A O   1 
ATOM   318  C  CB  . ILE   A 1 43  ? -28.669 -11.725 -10.043 1.00 50.07 ? 84  ILE   A CB  1 
ATOM   319  C  CG1 . ILE   A 1 43  ? -28.153 -12.679 -11.127 1.00 51.65 ? 84  ILE   A CG1 1 
ATOM   320  C  CG2 . ILE   A 1 43  ? -29.620 -12.437 -9.088  1.00 52.31 ? 84  ILE   A CG2 1 
ATOM   321  C  CD1 . ILE   A 1 43  ? -27.183 -13.735 -10.591 1.00 45.68 ? 84  ILE   A CD1 1 
ATOM   322  N  N   . HIS   A 1 44  ? -31.061 -9.315  -9.413  1.00 54.16 ? 85  HIS   A N   1 
ATOM   323  C  CA  . HIS   A 1 44  ? -31.540 -8.426  -8.366  1.00 54.89 ? 85  HIS   A CA  1 
ATOM   324  C  C   . HIS   A 1 44  ? -31.496 -9.128  -7.015  1.00 52.35 ? 85  HIS   A C   1 
ATOM   325  O  O   . HIS   A 1 44  ? -31.817 -10.315 -6.903  1.00 52.94 ? 85  HIS   A O   1 
ATOM   326  C  CB  . HIS   A 1 44  ? -32.962 -7.947  -8.654  1.00 54.14 ? 85  HIS   A CB  1 
ATOM   327  C  CG  . HIS   A 1 44  ? -33.497 -7.017  -7.610  1.00 56.31 ? 85  HIS   A CG  1 
ATOM   328  N  ND1 . HIS   A 1 44  ? -34.474 -7.386  -6.710  1.00 60.29 ? 85  HIS   A ND1 1 
ATOM   329  C  CD2 . HIS   A 1 44  ? -33.171 -5.738  -7.307  1.00 55.36 ? 85  HIS   A CD2 1 
ATOM   330  C  CE1 . HIS   A 1 44  ? -34.731 -6.371  -5.904  1.00 58.46 ? 85  HIS   A CE1 1 
ATOM   331  N  NE2 . HIS   A 1 44  ? -33.955 -5.358  -6.246  1.00 55.79 ? 85  HIS   A NE2 1 
ATOM   332  N  N   . LEU   A 1 45  ? -31.091 -8.384  -5.988  1.00 53.88 ? 86  LEU   A N   1 
ATOM   333  C  CA  . LEU   A 1 45  ? -30.979 -8.882  -4.616  1.00 53.17 ? 86  LEU   A CA  1 
ATOM   334  C  C   . LEU   A 1 45  ? -32.128 -8.285  -3.812  1.00 56.33 ? 86  LEU   A C   1 
ATOM   335  O  O   . LEU   A 1 45  ? -32.039 -7.149  -3.334  1.00 52.45 ? 86  LEU   A O   1 
ATOM   336  C  CB  . LEU   A 1 45  ? -29.632 -8.508  -4.007  1.00 51.95 ? 86  LEU   A CB  1 
ATOM   337  C  CG  . LEU   A 1 45  ? -28.415 -8.663  -4.916  1.00 51.82 ? 86  LEU   A CG  1 
ATOM   338  C  CD1 . LEU   A 1 45  ? -27.203 -7.987  -4.301  1.00 53.54 ? 86  LEU   A CD1 1 
ATOM   339  C  CD2 . LEU   A 1 45  ? -28.136 -10.132 -5.197  1.00 51.79 ? 86  LEU   A CD2 1 
ATOM   340  N  N   . GLU   A 1 46  ? -33.199 -9.059  -3.655  1.00 60.19 ? 87  GLU   A N   1 
ATOM   341  C  CA  . GLU   A 1 46  ? -34.422 -8.539  -3.058  1.00 63.10 ? 87  GLU   A CA  1 
ATOM   342  C  C   . GLU   A 1 46  ? -34.207 -8.193  -1.587  1.00 61.16 ? 87  GLU   A C   1 
ATOM   343  O  O   . GLU   A 1 46  ? -33.617 -8.970  -0.831  1.00 58.46 ? 87  GLU   A O   1 
ATOM   344  C  CB  . GLU   A 1 46  ? -35.553 -9.557  -3.208  1.00 63.85 ? 87  GLU   A CB  1 
ATOM   345  C  CG  . GLU   A 1 46  ? -35.903 -9.876  -4.657  1.00 68.81 ? 87  GLU   A CG  1 
ATOM   346  C  CD  . GLU   A 1 46  ? -37.143 -9.139  -5.137  1.00 74.42 ? 87  GLU   A CD  1 
ATOM   347  O  OE1 . GLU   A 1 46  ? -37.004 -8.011  -5.656  1.00 72.93 ? 87  GLU   A OE1 1 
ATOM   348  O  OE2 . GLU   A 1 46  ? -38.258 -9.687  -5.000  1.00 77.90 ? 87  GLU   A OE2 1 
ATOM   349  N  N   . ASN   A 1 47  ? -34.686 -7.014  -1.191  1.00 62.82 ? 88  ASN   A N   1 
ATOM   350  C  CA  . ASN   A 1 47  ? -34.644 -6.531  0.188   1.00 62.77 ? 88  ASN   A CA  1 
ATOM   351  C  C   . ASN   A 1 47  ? -33.223 -6.410  0.731   1.00 61.66 ? 88  ASN   A C   1 
ATOM   352  O  O   . ASN   A 1 47  ? -33.021 -6.452  1.950   1.00 61.61 ? 88  ASN   A O   1 
ATOM   353  C  CB  . ASN   A 1 47  ? -35.478 -7.427  1.110   1.00 67.22 ? 88  ASN   A CB  1 
ATOM   354  C  CG  . ASN   A 1 47  ? -36.958 -7.112  1.050   1.00 74.00 ? 88  ASN   A CG  1 
ATOM   355  O  OD1 . ASN   A 1 47  ? -37.371 -5.971  1.264   1.00 74.80 ? 88  ASN   A OD1 1 
ATOM   356  N  ND2 . ASN   A 1 47  ? -37.768 -8.127  0.752   1.00 73.31 ? 88  ASN   A ND2 1 
ATOM   357  N  N   . VAL   A 1 48  ? -32.233 -6.239  -0.142  1.00 59.09 ? 89  VAL   A N   1 
ATOM   358  C  CA  . VAL   A 1 48  ? -30.835 -6.139  0.266   1.00 56.47 ? 89  VAL   A CA  1 
ATOM   359  C  C   . VAL   A 1 48  ? -30.427 -4.671  0.267   1.00 55.77 ? 89  VAL   A C   1 
ATOM   360  O  O   . VAL   A 1 48  ? -30.559 -3.979  -0.750  1.00 55.87 ? 89  VAL   A O   1 
ATOM   361  C  CB  . VAL   A 1 48  ? -29.920 -6.960  -0.655  1.00 55.47 ? 89  VAL   A CB  1 
ATOM   362  C  CG1 . VAL   A 1 48  ? -28.452 -6.687  -0.332  1.00 54.08 ? 89  VAL   A CG1 1 
ATOM   363  C  CG2 . VAL   A 1 48  ? -30.221 -8.446  -0.527  1.00 57.29 ? 89  VAL   A CG2 1 
ATOM   364  N  N   . THR   A 1 49  ? -29.933 -4.194  1.405   1.00 53.80 ? 90  THR   A N   1 
ATOM   365  C  CA  . THR   A 1 49  ? -29.324 -2.876  1.513   1.00 55.32 ? 90  THR   A CA  1 
ATOM   366  C  C   . THR   A 1 49  ? -27.826 -3.049  1.714   1.00 56.21 ? 90  THR   A C   1 
ATOM   367  O  O   . THR   A 1 49  ? -27.397 -3.878  2.525   1.00 51.41 ? 90  THR   A O   1 
ATOM   368  C  CB  . THR   A 1 49  ? -29.932 -2.073  2.666   1.00 56.96 ? 90  THR   A CB  1 
ATOM   369  O  OG1 . THR   A 1 49  ? -31.217 -1.571  2.271   1.00 61.49 ? 90  THR   A OG1 1 
ATOM   370  C  CG2 . THR   A 1 49  ? -29.027 -0.905  3.042   1.00 53.61 ? 90  THR   A CG2 1 
ATOM   371  N  N   . GLU   A 1 50  ? -27.037 -2.280  0.964   1.00 55.18 ? 91  GLU   A N   1 
ATOM   372  C  CA  . GLU   A 1 50  ? -25.586 -2.372  1.006   1.00 52.61 ? 91  GLU   A CA  1 
ATOM   373  C  C   . GLU   A 1 50  ? -25.002 -0.970  1.087   1.00 50.64 ? 91  GLU   A C   1 
ATOM   374  O  O   . GLU   A 1 50  ? -25.611 -0.000  0.626   1.00 52.19 ? 91  GLU   A O   1 
ATOM   375  C  CB  . GLU   A 1 50  ? -25.038 -3.104  -0.227  1.00 52.40 ? 91  GLU   A CB  1 
ATOM   376  C  CG  . GLU   A 1 50  ? -24.793 -4.588  -0.019  1.00 57.43 ? 91  GLU   A CG  1 
ATOM   377  C  CD  . GLU   A 1 50  ? -23.504 -4.875  0.725   1.00 59.05 ? 91  GLU   A CD  1 
ATOM   378  O  OE1 . GLU   A 1 50  ? -22.509 -4.170  0.463   1.00 58.42 ? 91  GLU   A OE1 1 
ATOM   379  O  OE2 . GLU   A 1 50  ? -23.486 -5.808  1.559   1.00 61.85 ? 91  GLU   A OE2 1 
ATOM   380  N  N   . ASN   A 1 51  ? -23.815 -0.872  1.679   1.00 47.89 ? 92  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? -23.115 0.395   1.824   1.00 47.86 ? 92  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? -22.058 0.530   0.735   1.00 47.87 ? 92  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? -21.285 -0.403  0.488   1.00 46.05 ? 92  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? -22.470 0.513   3.206   1.00 49.57 ? 92  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? -23.487 0.554   4.326   1.00 52.95 ? 92  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? -24.580 1.093   4.163   1.00 54.47 ? 92  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? -23.125 -0.004  5.480   1.00 53.37 ? 92  ASN   A ND2 1 
ATOM   388  N  N   . PHE   A 1 52  ? -22.037 1.693   0.086   1.00 45.48 ? 93  PHE   A N   1 
ATOM   389  C  CA  . PHE   A 1 52  ? -21.084 2.018   -0.963  1.00 44.66 ? 93  PHE   A CA  1 
ATOM   390  C  C   . PHE   A 1 52  ? -20.231 3.205   -0.531  1.00 44.25 ? 93  PHE   A C   1 
ATOM   391  O  O   . PHE   A 1 52  ? -20.633 4.007   0.317   1.00 44.96 ? 93  PHE   A O   1 
ATOM   392  C  CB  . PHE   A 1 52  ? -21.802 2.352   -2.281  1.00 46.88 ? 93  PHE   A CB  1 
ATOM   393  C  CG  . PHE   A 1 52  ? -22.528 1.189   -2.888  1.00 45.63 ? 93  PHE   A CG  1 
ATOM   394  C  CD1 . PHE   A 1 52  ? -23.736 0.771   -2.366  1.00 50.66 ? 93  PHE   A CD1 1 
ATOM   395  C  CD2 . PHE   A 1 52  ? -22.007 0.516   -3.979  1.00 42.84 ? 93  PHE   A CD2 1 
ATOM   396  C  CE1 . PHE   A 1 52  ? -24.414 -0.302  -2.912  1.00 50.23 ? 93  PHE   A CE1 1 
ATOM   397  C  CE2 . PHE   A 1 52  ? -22.682 -0.557  -4.535  1.00 45.96 ? 93  PHE   A CE2 1 
ATOM   398  C  CZ  . PHE   A 1 52  ? -23.889 -0.967  -3.998  1.00 49.26 ? 93  PHE   A CZ  1 
ATOM   399  N  N   . ASN   A 1 53  ? -19.040 3.313   -1.122  1.00 40.61 ? 94  ASN   A N   1 
ATOM   400  C  CA  . ASN   A 1 53  ? -18.188 4.482   -0.895  1.00 39.02 ? 94  ASN   A CA  1 
ATOM   401  C  C   . ASN   A 1 53  ? -17.389 4.745   -2.170  1.00 39.13 ? 94  ASN   A C   1 
ATOM   402  O  O   . ASN   A 1 53  ? -16.321 4.158   -2.371  1.00 38.73 ? 94  ASN   A O   1 
ATOM   403  C  CB  . ASN   A 1 53  ? -17.271 4.279   0.301   1.00 39.18 ? 94  ASN   A CB  1 
ATOM   404  C  CG  . ASN   A 1 53  ? -16.602 5.564   0.737   1.00 42.03 ? 94  ASN   A CG  1 
ATOM   405  O  OD1 . ASN   A 1 53  ? -16.606 6.561   0.006   1.00 39.84 ? 94  ASN   A OD1 1 
ATOM   406  N  ND2 . ASN   A 1 53  ? -16.030 5.557   1.938   1.00 39.71 ? 94  ASN   A ND2 1 
ATOM   407  N  N   . MET   A 1 54  ? -17.909 5.639   -3.014  1.00 36.85 ? 95  MET   A N   1 
ATOM   408  C  CA  . MET   A 1 54  ? -17.260 5.969   -4.279  1.00 37.03 ? 95  MET   A CA  1 
ATOM   409  C  C   . MET   A 1 54  ? -15.909 6.644   -4.085  1.00 37.53 ? 95  MET   A C   1 
ATOM   410  O  O   . MET   A 1 54  ? -15.100 6.666   -5.020  1.00 38.18 ? 95  MET   A O   1 
ATOM   411  C  CB  . MET   A 1 54  ? -18.175 6.873   -5.104  1.00 35.13 ? 95  MET   A CB  1 
ATOM   412  C  CG  . MET   A 1 54  ? -18.280 8.289   -4.550  1.00 36.18 ? 95  MET   A CG  1 
ATOM   413  S  SD  . MET   A 1 54  ? -19.343 9.366   -5.526  1.00 40.72 ? 95  MET   A SD  1 
ATOM   414  C  CE  . MET   A 1 54  ? -18.184 9.927   -6.774  1.00 38.78 ? 95  MET   A CE  1 
ATOM   415  N  N   . TRP   A 1 55  ? -15.655 7.197   -2.900  1.00 35.43 ? 96  TRP   A N   1 
ATOM   416  C  CA  . TRP   A 1 55  ? -14.391 7.841   -2.560  1.00 35.53 ? 96  TRP   A CA  1 
ATOM   417  C  C   . TRP   A 1 55  ? -13.365 6.867   -1.996  1.00 36.79 ? 96  TRP   A C   1 
ATOM   418  O  O   . TRP   A 1 55  ? -12.215 7.257   -1.773  1.00 41.30 ? 96  TRP   A O   1 
ATOM   419  C  CB  . TRP   A 1 55  ? -14.651 8.991   -1.575  1.00 37.44 ? 96  TRP   A CB  1 
ATOM   420  C  CG  . TRP   A 1 55  ? -15.673 9.917   -2.152  1.00 37.90 ? 96  TRP   A CG  1 
ATOM   421  C  CD1 . TRP   A 1 55  ? -17.009 9.942   -1.873  1.00 35.65 ? 96  TRP   A CD1 1 
ATOM   422  C  CD2 . TRP   A 1 55  ? -15.457 10.893  -3.180  1.00 36.98 ? 96  TRP   A CD2 1 
ATOM   423  N  NE1 . TRP   A 1 55  ? -17.635 10.891  -2.645  1.00 36.51 ? 96  TRP   A NE1 1 
ATOM   424  C  CE2 . TRP   A 1 55  ? -16.705 11.490  -3.455  1.00 37.48 ? 96  TRP   A CE2 1 
ATOM   425  C  CE3 . TRP   A 1 55  ? -14.329 11.331  -3.883  1.00 33.41 ? 96  TRP   A CE3 1 
ATOM   426  C  CZ2 . TRP   A 1 55  ? -16.857 12.501  -4.402  1.00 36.83 ? 96  TRP   A CZ2 1 
ATOM   427  C  CZ3 . TRP   A 1 55  ? -14.483 12.336  -4.827  1.00 36.52 ? 96  TRP   A CZ3 1 
ATOM   428  C  CH2 . TRP   A 1 55  ? -15.738 12.910  -5.076  1.00 35.81 ? 96  TRP   A CH2 1 
ATOM   429  N  N   . LYS   A 1 56  ? -13.747 5.601   -1.789  1.00 38.55 ? 97  LYS   A N   1 
ATOM   430  C  CA  . LYS   A 1 56  ? -12.861 4.544   -1.291  1.00 40.84 ? 97  LYS   A CA  1 
ATOM   431  C  C   . LYS   A 1 56  ? -13.214 3.290   -2.083  1.00 40.18 ? 97  LYS   A C   1 
ATOM   432  O  O   . LYS   A 1 56  ? -13.862 2.375   -1.572  1.00 44.37 ? 97  LYS   A O   1 
ATOM   433  C  CB  . LYS   A 1 56  ? -13.032 4.321   0.210   1.00 41.12 ? 97  LYS   A CB  1 
ATOM   434  C  CG  . LYS   A 1 56  ? -12.744 5.530   1.072   1.00 45.83 ? 97  LYS   A CG  1 
ATOM   435  C  CD  . LYS   A 1 56  ? -11.263 5.873   1.081   1.00 48.39 ? 97  LYS   A CD  1 
ATOM   436  C  CE  . LYS   A 1 56  ? -10.815 6.312   2.471   1.00 50.34 ? 97  LYS   A CE  1 
ATOM   437  N  NZ  . LYS   A 1 56  ? -9.354  6.083   2.687   1.00 60.25 ? 97  LYS   A NZ  1 
ATOM   438  N  N   . ASN   A 1 57  ? -12.795 3.262   -3.347  1.00 39.37 ? 98  ASN   A N   1 
ATOM   439  C  CA  . ASN   A 1 57  ? -13.177 2.197   -4.266  1.00 41.20 ? 98  ASN   A CA  1 
ATOM   440  C  C   . ASN   A 1 57  ? -11.960 1.773   -5.076  1.00 39.41 ? 98  ASN   A C   1 
ATOM   441  O  O   . ASN   A 1 57  ? -11.453 2.547   -5.895  1.00 40.11 ? 98  ASN   A O   1 
ATOM   442  C  CB  . ASN   A 1 57  ? -14.311 2.645   -5.196  1.00 39.68 ? 98  ASN   A CB  1 
ATOM   443  C  CG  . ASN   A 1 57  ? -14.808 1.521   -6.087  1.00 39.43 ? 98  ASN   A CG  1 
ATOM   444  O  OD1 . ASN   A 1 57  ? -14.128 0.509   -6.262  1.00 41.21 ? 98  ASN   A OD1 1 
ATOM   445  N  ND2 . ASN   A 1 57  ? -16.004 1.687   -6.645  1.00 39.85 ? 98  ASN   A ND2 1 
ATOM   446  N  N   . ASN   A 1 58  ? -11.504 0.540   -4.857  1.00 36.09 ? 99  ASN   A N   1 
ATOM   447  C  CA  . ASN   A 1 58  ? -10.320 0.052   -5.551  1.00 39.87 ? 99  ASN   A CA  1 
ATOM   448  C  C   . ASN   A 1 58  ? -10.510 -0.031  -7.065  1.00 37.53 ? 99  ASN   A C   1 
ATOM   449  O  O   . ASN   A 1 58  ? -9.515  -0.005  -7.797  1.00 35.73 ? 99  ASN   A O   1 
ATOM   450  C  CB  . ASN   A 1 58  ? -9.912  -1.316  -5.001  1.00 43.52 ? 99  ASN   A CB  1 
ATOM   451  C  CG  . ASN   A 1 58  ? -8.561  -1.760  -5.515  1.00 42.54 ? 99  ASN   A CG  1 
ATOM   452  O  OD1 . ASN   A 1 58  ? -8.419  -2.848  -6.075  1.00 45.01 ? 99  ASN   A OD1 1 
ATOM   453  N  ND2 . ASN   A 1 58  ? -7.560  -0.897  -5.355  1.00 40.53 ? 99  ASN   A ND2 1 
ATOM   454  N  N   . MET   A 1 59  ? -11.750 -0.149  -7.554  1.00 35.27 ? 100 MET   A N   1 
ATOM   455  C  CA  . MET   A 1 59  ? -11.974 -0.080  -8.998  1.00 34.98 ? 100 MET   A CA  1 
ATOM   456  C  C   . MET   A 1 59  ? -11.399 1.206   -9.584  1.00 34.64 ? 100 MET   A C   1 
ATOM   457  O  O   . MET   A 1 59  ? -10.770 1.184   -10.649 1.00 37.39 ? 100 MET   A O   1 
ATOM   458  C  CB  . MET   A 1 59  ? -13.467 -0.184  -9.319  1.00 36.90 ? 100 MET   A CB  1 
ATOM   459  C  CG  . MET   A 1 59  ? -14.089 -1.537  -9.032  1.00 40.96 ? 100 MET   A CG  1 
ATOM   460  S  SD  . MET   A 1 59  ? -15.877 -1.449  -8.807  1.00 40.56 ? 100 MET   A SD  1 
ATOM   461  C  CE  . MET   A 1 59  ? -16.446 -1.578  -10.502 1.00 40.26 ? 100 MET   A CE  1 
ATOM   462  N  N   . VAL   A 1 60  ? -11.608 2.340   -8.907  1.00 35.21 ? 101 VAL   A N   1 
ATOM   463  C  CA  . VAL   A 1 60  ? -11.068 3.611   -9.392  1.00 37.42 ? 101 VAL   A CA  1 
ATOM   464  C  C   . VAL   A 1 60  ? -9.559  3.509   -9.590  1.00 37.14 ? 101 VAL   A C   1 
ATOM   465  O  O   . VAL   A 1 60  ? -9.021  3.900   -10.632 1.00 32.04 ? 101 VAL   A O   1 
ATOM   466  C  CB  . VAL   A 1 60  ? -11.428 4.752   -8.423  1.00 38.56 ? 101 VAL   A CB  1 
ATOM   467  C  CG1 . VAL   A 1 60  ? -10.709 6.051   -8.813  1.00 37.05 ? 101 VAL   A CG1 1 
ATOM   468  C  CG2 . VAL   A 1 60  ? -12.939 4.952   -8.369  1.00 38.50 ? 101 VAL   A CG2 1 
ATOM   469  N  N   . GLU   A 1 61  ? -8.853  2.991   -8.583  1.00 38.17 ? 102 GLU   A N   1 
ATOM   470  C  CA  . GLU   A 1 61  ? -7.405  2.852   -8.691  1.00 40.51 ? 102 GLU   A CA  1 
ATOM   471  C  C   . GLU   A 1 61  ? -7.020  1.968   -9.868  1.00 34.70 ? 102 GLU   A C   1 
ATOM   472  O  O   . GLU   A 1 61  ? -6.030  2.233   -10.555 1.00 33.84 ? 102 GLU   A O   1 
ATOM   473  C  CB  . GLU   A 1 61  ? -6.830  2.274   -7.399  1.00 39.68 ? 102 GLU   A CB  1 
ATOM   474  C  CG  . GLU   A 1 61  ? -7.286  2.956   -6.126  1.00 43.28 ? 102 GLU   A CG  1 
ATOM   475  C  CD  . GLU   A 1 61  ? -7.070  4.455   -6.154  1.00 50.30 ? 102 GLU   A CD  1 
ATOM   476  O  OE1 . GLU   A 1 61  ? -7.961  5.185   -5.665  1.00 52.88 ? 102 GLU   A OE1 1 
ATOM   477  O  OE2 . GLU   A 1 61  ? -6.021  4.901   -6.676  1.00 53.86 ? 102 GLU   A OE2 1 
ATOM   478  N  N   . GLN   A 1 62  ? -7.782  0.902   -10.109 1.00 34.90 ? 103 GLN   A N   1 
ATOM   479  C  CA  . GLN   A 1 62  ? -7.437  -0.017  -11.188 1.00 36.78 ? 103 GLN   A CA  1 
ATOM   480  C  C   . GLN   A 1 62  ? -7.700  0.604   -12.557 1.00 35.05 ? 103 GLN   A C   1 
ATOM   481  O  O   . GLN   A 1 62  ? -6.909  0.419   -13.489 1.00 33.78 ? 103 GLN   A O   1 
ATOM   482  C  CB  . GLN   A 1 62  ? -8.212  -1.324  -11.025 1.00 37.44 ? 103 GLN   A CB  1 
ATOM   483  C  CG  . GLN   A 1 62  ? -7.620  -2.254  -9.991  1.00 40.34 ? 103 GLN   A CG  1 
ATOM   484  C  CD  . GLN   A 1 62  ? -8.331  -3.592  -9.937  1.00 43.46 ? 103 GLN   A CD  1 
ATOM   485  O  OE1 . GLN   A 1 62  ? -8.298  -4.365  -10.898 1.00 42.19 ? 103 GLN   A OE1 1 
ATOM   486  N  NE2 . GLN   A 1 62  ? -8.968  -3.879  -8.806  1.00 42.68 ? 103 GLN   A NE2 1 
ATOM   487  N  N   . MET   A 1 63  ? -8.809  1.338   -12.703 1.00 36.48 ? 104 MET   A N   1 
ATOM   488  C  CA  . MET   A 1 63  ? -9.064  2.043   -13.957 1.00 36.11 ? 104 MET   A CA  1 
ATOM   489  C  C   . MET   A 1 63  ? -7.988  3.083   -14.223 1.00 34.46 ? 104 MET   A C   1 
ATOM   490  O  O   . MET   A 1 63  ? -7.517  3.231   -15.357 1.00 33.38 ? 104 MET   A O   1 
ATOM   491  C  CB  . MET   A 1 63  ? -10.433 2.723   -13.931 1.00 35.21 ? 104 MET   A CB  1 
ATOM   492  C  CG  . MET   A 1 63  ? -10.905 3.174   -15.313 1.00 39.79 ? 104 MET   A CG  1 
ATOM   493  S  SD  . MET   A 1 63  ? -12.590 3.805   -15.347 1.00 41.11 ? 104 MET   A SD  1 
ATOM   494  C  CE  . MET   A 1 63  ? -12.765 4.227   -17.078 1.00 42.16 ? 104 MET   A CE  1 
ATOM   495  N  N   . HIS   A 1 64  ? -7.601  3.828   -13.189 1.00 32.92 ? 105 HIS   A N   1 
ATOM   496  C  CA  . HIS   A 1 64  ? -6.508  4.784   -13.325 1.00 33.17 ? 105 HIS   A CA  1 
ATOM   497  C  C   . HIS   A 1 64  ? -5.261  4.115   -13.895 1.00 33.02 ? 105 HIS   A C   1 
ATOM   498  O  O   . HIS   A 1 64  ? -4.640  4.629   -14.833 1.00 33.15 ? 105 HIS   A O   1 
ATOM   499  C  CB  . HIS   A 1 64  ? -6.211  5.417   -11.965 1.00 34.51 ? 105 HIS   A CB  1 
ATOM   500  C  CG  . HIS   A 1 64  ? -5.536  6.746   -12.059 1.00 35.39 ? 105 HIS   A CG  1 
ATOM   501  N  ND1 . HIS   A 1 64  ? -6.089  7.807   -12.741 1.00 34.23 ? 105 HIS   A ND1 1 
ATOM   502  C  CD2 . HIS   A 1 64  ? -4.351  7.183   -11.574 1.00 36.44 ? 105 HIS   A CD2 1 
ATOM   503  C  CE1 . HIS   A 1 64  ? -5.276  8.844   -12.667 1.00 36.50 ? 105 HIS   A CE1 1 
ATOM   504  N  NE2 . HIS   A 1 64  ? -4.215  8.493   -11.963 1.00 39.07 ? 105 HIS   A NE2 1 
ATOM   505  N  N   . GLU   A 1 65  ? -4.877  2.969   -13.320 1.00 31.91 ? 106 GLU   A N   1 
ATOM   506  C  CA  . GLU   A 1 65  ? -3.749  2.183   -13.818 1.00 35.49 ? 106 GLU   A CA  1 
ATOM   507  C  C   . GLU   A 1 65  ? -3.868  1.878   -15.305 1.00 34.32 ? 106 GLU   A C   1 
ATOM   508  O  O   . GLU   A 1 65  ? -2.871  1.899   -16.037 1.00 34.39 ? 106 GLU   A O   1 
ATOM   509  C  CB  . GLU   A 1 65  ? -3.659  0.868   -13.041 1.00 39.43 ? 106 GLU   A CB  1 
ATOM   510  C  CG  . GLU   A 1 65  ? -2.502  0.770   -12.071 1.00 48.77 ? 106 GLU   A CG  1 
ATOM   511  C  CD  . GLU   A 1 65  ? -2.527  -0.526  -11.273 1.00 51.36 ? 106 GLU   A CD  1 
ATOM   512  O  OE1 . GLU   A 1 65  ? -3.027  -0.512  -10.127 1.00 51.50 ? 106 GLU   A OE1 1 
ATOM   513  O  OE2 . GLU   A 1 65  ? -2.052  -1.557  -11.797 1.00 52.26 ? 106 GLU   A OE2 1 
ATOM   514  N  N   . ASP   A 1 66  ? -5.076  1.539   -15.755 1.00 33.40 ? 107 ASP   A N   1 
ATOM   515  C  CA  . ASP   A 1 66  ? -5.278  1.165   -17.150 1.00 32.90 ? 107 ASP   A CA  1 
ATOM   516  C  C   . ASP   A 1 66  ? -5.104  2.363   -18.077 1.00 34.33 ? 107 ASP   A C   1 
ATOM   517  O  O   . ASP   A 1 66  ? -4.418  2.267   -19.103 1.00 35.23 ? 107 ASP   A O   1 
ATOM   518  C  CB  . ASP   A 1 66  ? -6.669  0.552   -17.331 1.00 34.11 ? 107 ASP   A CB  1 
ATOM   519  C  CG  . ASP   A 1 66  ? -6.726  -0.922  -16.932 1.00 38.53 ? 107 ASP   A CG  1 
ATOM   520  O  OD1 . ASP   A 1 66  ? -5.666  -1.498  -16.593 1.00 36.65 ? 107 ASP   A OD1 1 
ATOM   521  O  OD2 . ASP   A 1 66  ? -7.840  -1.490  -16.950 1.00 40.24 ? 107 ASP   A OD2 1 
ATOM   522  N  N   . ILE   A 1 67  ? -5.741  3.495   -17.751 1.00 33.01 ? 108 ILE   A N   1 
ATOM   523  C  CA  . ILE   A 1 67  ? -5.664  4.660   -18.633 1.00 32.39 ? 108 ILE   A CA  1 
ATOM   524  C  C   . ILE   A 1 67  ? -4.237  5.189   -18.684 1.00 33.77 ? 108 ILE   A C   1 
ATOM   525  O  O   . ILE   A 1 67  ? -3.766  5.645   -19.733 1.00 34.17 ? 108 ILE   A O   1 
ATOM   526  C  CB  . ILE   A 1 67  ? -6.666  5.749   -18.197 1.00 33.51 ? 108 ILE   A CB  1 
ATOM   527  C  CG1 . ILE   A 1 67  ? -8.044  5.136   -17.922 1.00 33.77 ? 108 ILE   A CG1 1 
ATOM   528  C  CG2 . ILE   A 1 67  ? -6.787  6.843   -19.266 1.00 31.36 ? 108 ILE   A CG2 1 
ATOM   529  C  CD1 . ILE   A 1 67  ? -8.516  4.203   -19.025 1.00 33.41 ? 108 ILE   A CD1 1 
ATOM   530  N  N   . ILE   A 1 68  ? -3.521  5.128   -17.558 1.00 33.86 ? 109 ILE   A N   1 
ATOM   531  C  CA  . ILE   A 1 68  ? -2.107  5.493   -17.568 1.00 34.96 ? 109 ILE   A CA  1 
ATOM   532  C  C   . ILE   A 1 68  ? -1.348  4.594   -18.539 1.00 36.83 ? 109 ILE   A C   1 
ATOM   533  O  O   . ILE   A 1 68  ? -0.575  5.066   -19.383 1.00 34.74 ? 109 ILE   A O   1 
ATOM   534  C  CB  . ILE   A 1 68  ? -1.515  5.415   -16.147 1.00 35.86 ? 109 ILE   A CB  1 
ATOM   535  C  CG1 . ILE   A 1 68  ? -2.057  6.543   -15.255 1.00 36.33 ? 109 ILE   A CG1 1 
ATOM   536  C  CG2 . ILE   A 1 68  ? 0.002   5.475   -16.202 1.00 37.59 ? 109 ILE   A CG2 1 
ATOM   537  C  CD1 . ILE   A 1 68  ? -1.562  6.479   -13.816 1.00 36.46 ? 109 ILE   A CD1 1 
ATOM   538  N  N   . SER   A 1 69  ? -1.570  3.281   -18.437 1.00 33.76 ? 110 SER   A N   1 
ATOM   539  C  CA  . SER   A 1 69  ? -0.958  2.346   -19.377 1.00 36.05 ? 110 SER   A CA  1 
ATOM   540  C  C   . SER   A 1 69  ? -1.402  2.626   -20.808 1.00 35.77 ? 110 SER   A C   1 
ATOM   541  O  O   . SER   A 1 69  ? -0.585  2.608   -21.736 1.00 37.21 ? 110 SER   A O   1 
ATOM   542  C  CB  . SER   A 1 69  ? -1.298  0.910   -18.979 1.00 33.66 ? 110 SER   A CB  1 
ATOM   543  O  OG  . SER   A 1 69  ? -0.801  -0.001  -19.936 1.00 40.85 ? 110 SER   A OG  1 
ATOM   544  N  N   . LEU   A 1 70  ? -2.696  2.888   -21.006 1.00 35.84 ? 111 LEU   A N   1 
ATOM   545  C  CA  . LEU   A 1 70  ? -3.195  3.198   -22.343 1.00 36.76 ? 111 LEU   A CA  1 
ATOM   546  C  C   . LEU   A 1 70  ? -2.507  4.431   -22.919 1.00 36.63 ? 111 LEU   A C   1 
ATOM   547  O  O   . LEU   A 1 70  ? -1.962  4.394   -24.028 1.00 35.84 ? 111 LEU   A O   1 
ATOM   548  C  CB  . LEU   A 1 70  ? -4.711  3.396   -22.299 1.00 36.26 ? 111 LEU   A CB  1 
ATOM   549  C  CG  . LEU   A 1 70  ? -5.459  3.385   -23.635 1.00 37.59 ? 111 LEU   A CG  1 
ATOM   550  C  CD1 . LEU   A 1 70  ? -6.936  3.108   -23.403 1.00 40.05 ? 111 LEU   A CD1 1 
ATOM   551  C  CD2 . LEU   A 1 70  ? -5.264  4.706   -24.368 1.00 38.04 ? 111 LEU   A CD2 1 
ATOM   552  N  N   . TRP   A 1 71  ? -2.521  5.539   -22.176 1.00 34.43 ? 112 TRP   A N   1 
ATOM   553  C  CA  . TRP   A 1 71  ? -1.916  6.766   -22.685 1.00 36.20 ? 112 TRP   A CA  1 
ATOM   554  C  C   . TRP   A 1 71  ? -0.421  6.593   -22.908 1.00 38.64 ? 112 TRP   A C   1 
ATOM   555  O  O   . TRP   A 1 71  ? 0.142   7.141   -23.863 1.00 37.52 ? 112 TRP   A O   1 
ATOM   556  C  CB  . TRP   A 1 71  ? -2.185  7.917   -21.721 1.00 35.12 ? 112 TRP   A CB  1 
ATOM   557  C  CG  . TRP   A 1 71  ? -3.483  8.590   -21.973 1.00 32.38 ? 112 TRP   A CG  1 
ATOM   558  C  CD1 . TRP   A 1 71  ? -4.696  7.993   -22.121 1.00 32.82 ? 112 TRP   A CD1 1 
ATOM   559  C  CD2 . TRP   A 1 71  ? -3.701  9.994   -22.117 1.00 32.80 ? 112 TRP   A CD2 1 
ATOM   560  N  NE1 . TRP   A 1 71  ? -5.664  8.942   -22.346 1.00 33.36 ? 112 TRP   A NE1 1 
ATOM   561  C  CE2 . TRP   A 1 71  ? -5.076  10.180  -22.348 1.00 33.02 ? 112 TRP   A CE2 1 
ATOM   562  C  CE3 . TRP   A 1 71  ? -2.865  11.116  -22.068 1.00 35.26 ? 112 TRP   A CE3 1 
ATOM   563  C  CZ2 . TRP   A 1 71  ? -5.637  11.438  -22.528 1.00 34.12 ? 112 TRP   A CZ2 1 
ATOM   564  C  CZ3 . TRP   A 1 71  ? -3.421  12.362  -22.248 1.00 35.43 ? 112 TRP   A CZ3 1 
ATOM   565  C  CH2 . TRP   A 1 71  ? -4.795  12.515  -22.475 1.00 36.21 ? 112 TRP   A CH2 1 
ATOM   566  N  N   . ASP   A 1 72  ? 0.239   5.826   -22.040 1.00 37.93 ? 113 ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 72  ? 1.671   5.614   -22.189 1.00 41.17 ? 113 ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 72  ? 2.006   4.735   -23.390 1.00 39.94 ? 113 ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 72  ? 3.120   4.827   -23.913 1.00 41.68 ? 113 ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 72  ? 2.245   5.008   -20.904 1.00 38.80 ? 113 ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 72  ? 2.361   6.027   -19.775 1.00 50.06 ? 113 ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 72  ? 1.580   7.006   -19.771 1.00 49.31 ? 113 ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 72  ? 3.238   5.853   -18.900 1.00 54.61 ? 113 ASP   A OD2 1 
ATOM   574  N  N   . GLN   A 1 73  ? 1.077   3.887   -23.833 1.00 38.27 ? 114 GLN   A N   1 
ATOM   575  C  CA  . GLN   A 1 73  ? 1.277   3.064   -25.019 1.00 41.60 ? 114 GLN   A CA  1 
ATOM   576  C  C   . GLN   A 1 73  ? 0.862   3.759   -26.311 1.00 43.38 ? 114 GLN   A C   1 
ATOM   577  O  O   . GLN   A 1 73  ? 1.160   3.247   -27.398 1.00 47.21 ? 114 GLN   A O   1 
ATOM   578  C  CB  . GLN   A 1 73  ? 0.481   1.763   -24.903 1.00 39.64 ? 114 GLN   A CB  1 
ATOM   579  C  CG  . GLN   A 1 73  ? 1.108   0.700   -24.030 1.00 44.54 ? 114 GLN   A CG  1 
ATOM   580  C  CD  . GLN   A 1 73  ? 0.122   -0.398  -23.702 1.00 44.07 ? 114 GLN   A CD  1 
ATOM   581  O  OE1 . GLN   A 1 73  ? -0.401  -1.057  -24.600 1.00 47.95 ? 114 GLN   A OE1 1 
ATOM   582  N  NE2 . GLN   A 1 73  ? -0.149  -0.594  -22.413 1.00 44.90 ? 114 GLN   A NE2 1 
ATOM   583  N  N   . SER   A 1 74  ? 0.177   4.900   -26.227 1.00 40.40 ? 115 SER   A N   1 
ATOM   584  C  CA  . SER   A 1 74  ? -0.485  5.451   -27.401 1.00 38.58 ? 115 SER   A CA  1 
ATOM   585  C  C   . SER   A 1 74  ? -0.072  6.892   -27.656 1.00 45.17 ? 115 SER   A C   1 
ATOM   586  O  O   . SER   A 1 74  ? 0.272   7.251   -28.787 1.00 47.44 ? 115 SER   A O   1 
ATOM   587  C  CB  . SER   A 1 74  ? -2.001  5.358   -27.234 1.00 37.76 ? 115 SER   A CB  1 
ATOM   588  O  OG  . SER   A 1 74  ? -2.385  4.108   -26.682 1.00 38.34 ? 115 SER   A OG  1 
ATOM   589  N  N   . LEU   A 1 75  ? -0.122  7.725   -26.615 1.00 44.80 ? 116 LEU   A N   1 
ATOM   590  C  CA  . LEU   A 1 75  ? 0.221   9.142   -26.722 1.00 48.32 ? 116 LEU   A CA  1 
ATOM   591  C  C   . LEU   A 1 75  ? 1.675   9.315   -26.302 1.00 51.13 ? 116 LEU   A C   1 
ATOM   592  O  O   . LEU   A 1 75  ? 1.997   9.756   -25.191 1.00 51.82 ? 116 LEU   A O   1 
ATOM   593  C  CB  . LEU   A 1 75  ? -0.713  9.988   -25.868 1.00 47.33 ? 116 LEU   A CB  1 
ATOM   594  C  CG  . LEU   A 1 75  ? -1.762  10.813  -26.612 1.00 43.90 ? 116 LEU   A CG  1 
ATOM   595  C  CD1 . LEU   A 1 75  ? -2.817  11.345  -25.652 1.00 43.75 ? 116 LEU   A CD1 1 
ATOM   596  C  CD2 . LEU   A 1 75  ? -1.105  11.945  -27.367 1.00 52.03 ? 116 LEU   A CD2 1 
ATOM   597  N  N   . GLN   A 1 76  ? 2.571   8.964   -27.225 1.00 52.38 ? 117 GLN   A N   1 
ATOM   598  C  CA  . GLN   A 1 76  ? 4.000   9.063   -26.964 1.00 57.85 ? 117 GLN   A CA  1 
ATOM   599  C  C   . GLN   A 1 76  ? 4.487   10.482  -27.234 1.00 56.38 ? 117 GLN   A C   1 
ATOM   600  O  O   . GLN   A 1 76  ? 4.551   10.903  -28.405 1.00 59.14 ? 117 GLN   A O   1 
ATOM   601  C  CB  . GLN   A 1 76  ? 4.773   8.048   -27.799 1.00 62.10 ? 117 GLN   A CB  1 
ATOM   602  C  CG  . GLN   A 1 76  ? 4.574   6.618   -27.316 1.00 59.02 ? 117 GLN   A CG  1 
ATOM   603  C  CD  . GLN   A 1 76  ? 5.776   5.731   -27.573 1.00 63.72 ? 117 GLN   A CD  1 
ATOM   604  O  OE1 . GLN   A 1 76  ? 6.777   6.163   -28.152 1.00 63.69 ? 117 GLN   A OE1 1 
ATOM   605  N  NE2 . GLN   A 1 76  ? 5.700   4.492   -27.099 1.00 59.95 ? 117 GLN   A NE2 1 
ATOM   606  N  N   . PRO   A 1 77  ? 4.820   11.259  -26.209 1.00 56.59 ? 118 PRO   A N   1 
ATOM   607  C  CA  . PRO   A 1 77  ? 5.332   12.608  -26.436 1.00 54.26 ? 118 PRO   A CA  1 
ATOM   608  C  C   . PRO   A 1 77  ? 6.696   12.591  -27.105 1.00 58.90 ? 118 PRO   A C   1 
ATOM   609  O  O   . PRO   A 1 77  ? 7.520   11.700  -26.880 1.00 61.63 ? 118 PRO   A O   1 
ATOM   610  C  CB  . PRO   A 1 77  ? 5.429   13.187  -25.024 1.00 51.92 ? 118 PRO   A CB  1 
ATOM   611  C  CG  . PRO   A 1 77  ? 5.568   11.988  -24.145 1.00 56.15 ? 118 PRO   A CG  1 
ATOM   612  C  CD  . PRO   A 1 77  ? 4.655   10.980  -24.771 1.00 55.57 ? 118 PRO   A CD  1 
ATOM   613  N  N   . CYS   A 1 78  ? 6.935   13.613  -27.927 1.00 57.80 ? 119 CYS   A N   1 
ATOM   614  C  CA  . CYS   A 1 78  ? 8.252   13.786  -28.529 1.00 59.37 ? 119 CYS   A CA  1 
ATOM   615  C  C   . CYS   A 1 78  ? 9.334   13.845  -27.460 1.00 63.21 ? 119 CYS   A C   1 
ATOM   616  O  O   . CYS   A 1 78  ? 10.339  13.128  -27.533 1.00 65.38 ? 119 CYS   A O   1 
ATOM   617  C  CB  . CYS   A 1 78  ? 8.268   15.049  -29.389 1.00 59.23 ? 119 CYS   A CB  1 
ATOM   618  S  SG  . CYS   A 1 78  ? 6.857   15.142  -30.514 1.00 77.31 ? 119 CYS   A SG  1 
ATOM   619  N  N   . VAL   A 1 79  ? 9.134   14.684  -26.448 1.00 59.79 ? 120 VAL   A N   1 
ATOM   620  C  CA  . VAL   A 1 79  ? 10.066  14.828  -25.340 1.00 59.24 ? 120 VAL   A CA  1 
ATOM   621  C  C   . VAL   A 1 79  ? 9.280   14.718  -24.045 1.00 58.83 ? 120 VAL   A C   1 
ATOM   622  O  O   . VAL   A 1 79  ? 8.204   15.312  -23.915 1.00 55.20 ? 120 VAL   A O   1 
ATOM   623  C  CB  . VAL   A 1 79  ? 10.821  16.169  -25.399 1.00 57.68 ? 120 VAL   A CB  1 
ATOM   624  C  CG1 . VAL   A 1 79  ? 12.089  16.099  -24.573 1.00 63.51 ? 120 VAL   A CG1 1 
ATOM   625  C  CG2 . VAL   A 1 79  ? 11.128  16.544  -26.844 1.00 62.20 ? 120 VAL   A CG2 1 
ATOM   626  N  N   . LYS   A 1 80  ? 9.807   13.954  -23.098 1.00 62.17 ? 121 LYS   A N   1 
ATOM   627  C  CA  . LYS   A 1 80  ? 9.218   13.845  -21.768 1.00 62.12 ? 121 LYS   A CA  1 
ATOM   628  C  C   . LYS   A 1 80  ? 10.259  14.312  -20.757 1.00 67.82 ? 121 LYS   A C   1 
ATOM   629  O  O   . LYS   A 1 80  ? 11.147  13.547  -20.367 1.00 73.18 ? 121 LYS   A O   1 
ATOM   630  C  CB  . LYS   A 1 80  ? 8.750   12.423  -21.477 1.00 63.06 ? 121 LYS   A CB  1 
ATOM   631  C  CG  . LYS   A 1 80  ? 7.620   12.375  -20.460 1.00 63.05 ? 121 LYS   A CG  1 
ATOM   632  C  CD  . LYS   A 1 80  ? 6.836   11.076  -20.542 1.00 67.71 ? 121 LYS   A CD  1 
ATOM   633  C  CE  . LYS   A 1 80  ? 7.614   9.928   -19.934 1.00 69.80 ? 121 LYS   A CE  1 
ATOM   634  N  NZ  . LYS   A 1 80  ? 6.964   9.434   -18.689 1.00 75.69 ? 121 LYS   A NZ  1 
ATOM   635  N  N   . LEU   A 1 81  ? 10.144  15.573  -20.337 1.00 66.37 ? 122 LEU   A N   1 
ATOM   636  C  CA  . LEU   A 1 81  ? 11.021  16.149  -19.320 1.00 67.79 ? 122 LEU   A CA  1 
ATOM   637  C  C   . LEU   A 1 81  ? 10.507  15.695  -17.957 1.00 69.17 ? 122 LEU   A C   1 
ATOM   638  O  O   . LEU   A 1 81  ? 9.797   16.415  -17.251 1.00 68.32 ? 122 LEU   A O   1 
ATOM   639  C  CB  . LEU   A 1 81  ? 11.052  17.670  -19.434 1.00 63.85 ? 122 LEU   A CB  1 
ATOM   640  C  CG  . LEU   A 1 81  ? 11.108  18.288  -20.832 1.00 61.48 ? 122 LEU   A CG  1 
ATOM   641  C  CD1 . LEU   A 1 81  ? 9.793   18.998  -21.132 1.00 60.50 ? 122 LEU   A CD1 1 
ATOM   642  C  CD2 . LEU   A 1 81  ? 12.260  19.260  -20.926 1.00 58.91 ? 122 LEU   A CD2 1 
ATOM   643  N  N   . THR   A 1 82  ? 10.870  14.467  -17.588 1.00 73.38 ? 123 THR   A N   1 
ATOM   644  C  CA  . THR   A 1 82  ? 10.395  13.842  -16.354 1.00 77.26 ? 123 THR   A CA  1 
ATOM   645  C  C   . THR   A 1 82  ? 11.377  14.016  -15.200 1.00 82.69 ? 123 THR   A C   1 
ATOM   646  O  O   . THR   A 1 82  ? 11.526  13.130  -14.352 1.00 82.60 ? 123 THR   A O   1 
ATOM   647  C  CB  . THR   A 1 82  ? 10.092  12.365  -16.593 1.00 76.62 ? 123 THR   A CB  1 
ATOM   648  O  OG1 . THR   A 1 82  ? 9.178   11.899  -15.594 1.00 79.22 ? 123 THR   A OG1 1 
ATOM   649  C  CG2 . THR   A 1 82  ? 11.370  11.524  -16.556 1.00 78.63 ? 123 THR   A CG2 1 
ATOM   650  N  N   . GLY   A 1 83  ? 12.048  15.164  -15.141 1.00 85.33 ? 124 GLY   A N   1 
ATOM   651  C  CA  . GLY   A 1 83  ? 12.961  15.465  -14.054 1.00 86.65 ? 124 GLY   A CA  1 
ATOM   652  C  C   . GLY   A 1 83  ? 14.346  14.887  -14.255 1.00 87.96 ? 124 GLY   A C   1 
ATOM   653  O  O   . GLY   A 1 83  ? 14.517  13.664  -14.276 1.00 89.29 ? 124 GLY   A O   1 
ATOM   654  N  N   . GLY   A 1 84  ? 15.341  15.750  -14.408 1.00 85.98 ? 198 GLY   A N   1 
ATOM   655  C  CA  . GLY   A 1 84  ? 16.719  15.300  -14.612 1.00 87.49 ? 198 GLY   A CA  1 
ATOM   656  C  C   . GLY   A 1 84  ? 17.057  15.170  -16.099 1.00 90.49 ? 198 GLY   A C   1 
ATOM   657  O  O   . GLY   A 1 84  ? 17.171  16.176  -16.798 1.00 89.37 ? 198 GLY   A O   1 
ATOM   658  N  N   . SER   A 1 85  ? 17.225  13.932  -16.560 1.00 90.82 ? 199 SER   A N   1 
ATOM   659  C  CA  . SER   A 1 85  ? 17.495  13.667  -17.964 1.00 91.28 ? 199 SER   A CA  1 
ATOM   660  C  C   . SER   A 1 85  ? 16.190  13.620  -18.756 1.00 90.13 ? 199 SER   A C   1 
ATOM   661  O  O   . SER   A 1 85  ? 15.106  13.397  -18.209 1.00 88.35 ? 199 SER   A O   1 
ATOM   662  C  CB  . SER   A 1 85  ? 18.268  12.355  -18.125 1.00 90.46 ? 199 SER   A CB  1 
ATOM   663  O  OG  . SER   A 1 85  ? 17.393  11.243  -18.212 1.00 89.87 ? 199 SER   A OG  1 
ATOM   664  N  N   . VAL   A 1 86  ? 16.304  13.834  -20.064 1.00 86.29 ? 200 VAL   A N   1 
ATOM   665  C  CA  . VAL   A 1 86  ? 15.147  13.953  -20.940 1.00 82.97 ? 200 VAL   A CA  1 
ATOM   666  C  C   . VAL   A 1 86  ? 15.255  12.918  -22.050 1.00 82.62 ? 200 VAL   A C   1 
ATOM   667  O  O   . VAL   A 1 86  ? 16.354  12.620  -22.533 1.00 80.64 ? 200 VAL   A O   1 
ATOM   668  C  CB  . VAL   A 1 86  ? 15.031  15.374  -21.525 1.00 80.63 ? 200 VAL   A CB  1 
ATOM   669  C  CG1 . VAL   A 1 86  ? 14.207  16.257  -20.602 1.00 79.88 ? 200 VAL   A CG1 1 
ATOM   670  C  CG2 . VAL   A 1 86  ? 16.413  15.967  -21.729 1.00 84.22 ? 200 VAL   A CG2 1 
ATOM   671  N  N   . ILE   A 1 87  ? 14.108  12.383  -22.461 1.00 80.76 ? 201 ILE   A N   1 
ATOM   672  C  CA  . ILE   A 1 87  ? 14.029  11.349  -23.486 1.00 76.65 ? 201 ILE   A CA  1 
ATOM   673  C  C   . ILE   A 1 87  ? 13.181  11.871  -24.640 1.00 73.43 ? 201 ILE   A C   1 
ATOM   674  O  O   . ILE   A 1 87  ? 12.053  12.334  -24.428 1.00 72.30 ? 201 ILE   A O   1 
ATOM   675  C  CB  . ILE   A 1 87  ? 13.452  10.042  -22.912 1.00 76.33 ? 201 ILE   A CB  1 
ATOM   676  C  CG1 . ILE   A 1 87  ? 12.005  10.246  -22.458 1.00 74.98 ? 201 ILE   A CG1 1 
ATOM   677  C  CG2 . ILE   A 1 87  ? 14.289  9.564   -21.743 1.00 74.47 ? 201 ILE   A CG2 1 
ATOM   678  C  CD1 . ILE   A 1 87  ? 11.291  8.966   -22.046 1.00 72.66 ? 201 ILE   A CD1 1 
ATOM   679  N  N   . LYS   A 1 88  ? 13.722  11.798  -25.857 1.00 73.51 ? 202 LYS   A N   1 
ATOM   680  C  CA  . LYS   A 1 88  ? 13.066  12.304  -27.065 1.00 72.85 ? 202 LYS   A CA  1 
ATOM   681  C  C   . LYS   A 1 88  ? 12.724  11.121  -27.969 1.00 71.02 ? 202 LYS   A C   1 
ATOM   682  O  O   . LYS   A 1 88  ? 13.429  10.831  -28.935 1.00 70.96 ? 202 LYS   A O   1 
ATOM   683  C  CB  . LYS   A 1 88  ? 13.973  13.319  -27.797 1.00 69.67 ? 202 LYS   A CB  1 
ATOM   684  C  CG  . LYS   A 1 88  ? 15.344  13.512  -27.153 1.00 72.14 ? 202 LYS   A CG  1 
ATOM   685  C  CD  . LYS   A 1 88  ? 16.111  14.663  -27.790 1.00 72.43 ? 202 LYS   A CD  1 
ATOM   686  C  CE  . LYS   A 1 88  ? 15.248  15.425  -28.782 1.00 68.80 ? 202 LYS   A CE  1 
ATOM   687  N  NZ  . LYS   A 1 88  ? 15.653  16.852  -28.882 1.00 65.63 ? 202 LYS   A NZ  1 
ATOM   688  N  N   . GLN   A 1 89  ? 11.618  10.446  -27.661 1.00 72.39 ? 203 GLN   A N   1 
ATOM   689  C  CA  . GLN   A 1 89  ? 11.229  9.240   -28.381 1.00 71.45 ? 203 GLN   A CA  1 
ATOM   690  C  C   . GLN   A 1 89  ? 10.399  9.615   -29.612 1.00 70.47 ? 203 GLN   A C   1 
ATOM   691  O  O   . GLN   A 1 89  ? 10.409  10.764  -30.061 1.00 70.43 ? 203 GLN   A O   1 
ATOM   692  C  CB  . GLN   A 1 89  ? 10.484  8.286   -27.443 1.00 68.41 ? 203 GLN   A CB  1 
ATOM   693  C  CG  . GLN   A 1 89  ? 9.605   8.975   -26.414 1.00 70.01 ? 203 GLN   A CG  1 
ATOM   694  C  CD  . GLN   A 1 89  ? 8.850   7.989   -25.543 1.00 71.02 ? 203 GLN   A CD  1 
ATOM   695  O  OE1 . GLN   A 1 89  ? 9.097   6.782   -25.598 1.00 67.99 ? 203 GLN   A OE1 1 
ATOM   696  N  NE2 . GLN   A 1 89  ? 7.922   8.498   -24.733 1.00 66.71 ? 203 GLN   A NE2 1 
ATOM   697  N  N   . ALA   A 1 90  ? 9.678   8.645   -30.173 1.00 71.78 ? 204 ALA   A N   1 
ATOM   698  C  CA  . ALA   A 1 90  ? 8.880   8.860   -31.372 1.00 73.41 ? 204 ALA   A CA  1 
ATOM   699  C  C   . ALA   A 1 90  ? 7.511   9.409   -31.005 1.00 70.45 ? 204 ALA   A C   1 
ATOM   700  O  O   . ALA   A 1 90  ? 6.895   8.983   -30.025 1.00 75.44 ? 204 ALA   A O   1 
ATOM   701  C  CB  . ALA   A 1 90  ? 8.719   7.561   -32.166 1.00 70.99 ? 204 ALA   A CB  1 
ATOM   702  N  N   . CYS   A 1 91  ? 7.040   10.351  -31.805 1.00 68.37 ? 205 CYS   A N   1 
ATOM   703  C  CA  . CYS   A 1 91  ? 5.748   10.971  -31.566 1.00 65.44 ? 205 CYS   A CA  1 
ATOM   704  C  C   . CYS   A 1 91  ? 5.037   11.244  -32.887 1.00 63.30 ? 205 CYS   A C   1 
ATOM   705  O  O   . CYS   A 1 91  ? 4.798   12.408  -33.231 1.00 61.55 ? 205 CYS   A O   1 
ATOM   706  C  CB  . CYS   A 1 91  ? 5.925   12.270  -30.780 1.00 66.49 ? 205 CYS   A CB  1 
ATOM   707  S  SG  . CYS   A 1 91  ? 7.023   13.447  -31.618 1.00 75.05 ? 205 CYS   A SG  1 
ATOM   708  N  N   . PRO   A 1 92  ? 4.694   10.217  -33.659 1.00 61.16 ? 206 PRO   A N   1 
ATOM   709  C  CA  . PRO   A 1 92  ? 3.842   10.448  -34.829 1.00 57.20 ? 206 PRO   A CA  1 
ATOM   710  C  C   . PRO   A 1 92  ? 2.434   10.828  -34.397 1.00 53.88 ? 206 PRO   A C   1 
ATOM   711  O  O   . PRO   A 1 92  ? 1.978   10.470  -33.308 1.00 53.89 ? 206 PRO   A O   1 
ATOM   712  C  CB  . PRO   A 1 92  ? 3.864   9.100   -35.558 1.00 54.43 ? 206 PRO   A CB  1 
ATOM   713  C  CG  . PRO   A 1 92  ? 4.199   8.095   -34.487 1.00 56.75 ? 206 PRO   A CG  1 
ATOM   714  C  CD  . PRO   A 1 92  ? 5.131   8.812   -33.556 1.00 59.50 ? 206 PRO   A CD  1 
ATOM   715  N  N   . LYS   A 1 93  ? 1.750   11.580  -35.257 1.00 49.18 ? 207 LYS   A N   1 
ATOM   716  C  CA  . LYS   A 1 93  ? 0.344   11.870  -35.016 1.00 48.02 ? 207 LYS   A CA  1 
ATOM   717  C  C   . LYS   A 1 93  ? -0.452  10.571  -35.061 1.00 46.09 ? 207 LYS   A C   1 
ATOM   718  O  O   . LYS   A 1 93  ? -0.188  9.690   -35.881 1.00 51.46 ? 207 LYS   A O   1 
ATOM   719  C  CB  . LYS   A 1 93  ? -0.185  12.865  -36.048 1.00 48.85 ? 207 LYS   A CB  1 
ATOM   720  C  CG  . LYS   A 1 93  ? 0.310   14.295  -35.850 1.00 42.93 ? 207 LYS   A CG  1 
ATOM   721  C  CD  . LYS   A 1 93  ? 0.153   14.757  -34.412 1.00 43.51 ? 207 LYS   A CD  1 
ATOM   722  C  CE  . LYS   A 1 93  ? 0.479   16.240  -34.274 1.00 45.95 ? 207 LYS   A CE  1 
ATOM   723  N  NZ  . LYS   A 1 93  ? 0.367   16.740  -32.868 1.00 48.75 ? 207 LYS   A NZ  1 
ATOM   724  N  N   . ILE   A 1 94  ? -1.418  10.443  -34.155 1.00 44.05 ? 208 ILE   A N   1 
ATOM   725  C  CA  . ILE   A 1 94  ? -2.173  9.210   -33.984 1.00 42.14 ? 208 ILE   A CA  1 
ATOM   726  C  C   . ILE   A 1 94  ? -3.664  9.518   -34.117 1.00 42.31 ? 208 ILE   A C   1 
ATOM   727  O  O   . ILE   A 1 94  ? -4.080  10.672  -34.218 1.00 42.33 ? 208 ILE   A O   1 
ATOM   728  C  CB  . ILE   A 1 94  ? -1.867  8.517   -32.634 1.00 45.41 ? 208 ILE   A CB  1 
ATOM   729  C  CG1 . ILE   A 1 94  ? -2.330  9.371   -31.450 1.00 44.54 ? 208 ILE   A CG1 1 
ATOM   730  C  CG2 . ILE   A 1 94  ? -0.374  8.242   -32.489 1.00 44.40 ? 208 ILE   A CG2 1 
ATOM   731  C  CD1 . ILE   A 1 94  ? -3.623  8.905   -30.819 1.00 46.51 ? 208 ILE   A CD1 1 
ATOM   732  N  N   . SER   A 1 95  ? -4.464  8.455   -34.135 1.00 40.68 ? 209 SER   A N   1 
ATOM   733  C  CA  . SER   A 1 95  ? -5.921  8.540   -34.147 1.00 39.79 ? 209 SER   A CA  1 
ATOM   734  C  C   . SER   A 1 95  ? -6.425  8.299   -32.725 1.00 39.93 ? 209 SER   A C   1 
ATOM   735  O  O   . SER   A 1 95  ? -6.177  7.234   -32.150 1.00 36.50 ? 209 SER   A O   1 
ATOM   736  C  CB  . SER   A 1 95  ? -6.507  7.513   -35.119 1.00 39.44 ? 209 SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 95  ? -7.919  7.490   -35.075 1.00 39.77 ? 209 SER   A OG  1 
ATOM   738  N  N   . PHE   A 1 96  ? -7.122  9.285   -32.161 1.00 39.20 ? 210 PHE   A N   1 
ATOM   739  C  CA  . PHE   A 1 96  ? -7.495  9.269   -30.749 1.00 39.29 ? 210 PHE   A CA  1 
ATOM   740  C  C   . PHE   A 1 96  ? -8.989  9.544   -30.613 1.00 42.29 ? 210 PHE   A C   1 
ATOM   741  O  O   . PHE   A 1 96  ? -9.458  10.640  -30.939 1.00 44.52 ? 210 PHE   A O   1 
ATOM   742  C  CB  . PHE   A 1 96  ? -6.666  10.293  -29.968 1.00 41.13 ? 210 PHE   A CB  1 
ATOM   743  C  CG  . PHE   A 1 96  ? -6.981  10.350  -28.497 1.00 39.59 ? 210 PHE   A CG  1 
ATOM   744  C  CD1 . PHE   A 1 96  ? -8.146  10.951  -28.040 1.00 39.16 ? 210 PHE   A CD1 1 
ATOM   745  C  CD2 . PHE   A 1 96  ? -6.102  9.812   -27.568 1.00 40.11 ? 210 PHE   A CD2 1 
ATOM   746  C  CE1 . PHE   A 1 96  ? -8.428  11.012  -26.684 1.00 39.41 ? 210 PHE   A CE1 1 
ATOM   747  C  CE2 . PHE   A 1 96  ? -6.379  9.866   -26.212 1.00 39.75 ? 210 PHE   A CE2 1 
ATOM   748  C  CZ  . PHE   A 1 96  ? -7.542  10.467  -25.770 1.00 38.99 ? 210 PHE   A CZ  1 
ATOM   749  N  N   . ASP   A 1 97  ? -9.729  8.553   -30.110 1.00 42.09 ? 211 ASP   A N   1 
ATOM   750  C  CA  . ASP   A 1 97  ? -11.152 8.688   -29.824 1.00 40.77 ? 211 ASP   A CA  1 
ATOM   751  C  C   . ASP   A 1 97  ? -11.572 7.626   -28.808 1.00 40.74 ? 211 ASP   A C   1 
ATOM   752  O  O   . ASP   A 1 97  ? -11.706 6.446   -29.158 1.00 38.00 ? 211 ASP   A O   1 
ATOM   753  C  CB  . ASP   A 1 97  ? -11.973 8.568   -31.109 1.00 45.50 ? 211 ASP   A CB  1 
ATOM   754  C  CG  . ASP   A 1 97  ? -13.445 8.909   -30.901 1.00 50.43 ? 211 ASP   A CG  1 
ATOM   755  O  OD1 . ASP   A 1 97  ? -13.796 9.433   -29.819 1.00 47.30 ? 211 ASP   A OD1 1 
ATOM   756  O  OD2 . ASP   A 1 97  ? -14.251 8.640   -31.822 1.00 56.05 ? 211 ASP   A OD2 1 
ATOM   757  N  N   . PRO   A 1 98  ? -11.781 8.007   -27.545 1.00 35.99 ? 212 PRO   A N   1 
ATOM   758  C  CA  . PRO   A 1 98  ? -12.064 7.014   -26.500 1.00 34.87 ? 212 PRO   A CA  1 
ATOM   759  C  C   . PRO   A 1 98  ? -13.274 6.143   -26.814 1.00 36.33 ? 212 PRO   A C   1 
ATOM   760  O  O   . PRO   A 1 98  ? -14.256 6.590   -27.412 1.00 36.46 ? 212 PRO   A O   1 
ATOM   761  C  CB  . PRO   A 1 98  ? -12.317 7.873   -25.258 1.00 38.32 ? 212 PRO   A CB  1 
ATOM   762  C  CG  . PRO   A 1 98  ? -11.551 9.140   -25.495 1.00 40.49 ? 212 PRO   A CG  1 
ATOM   763  C  CD  . PRO   A 1 98  ? -11.470 9.336   -26.991 1.00 37.15 ? 212 PRO   A CD  1 
ATOM   764  N  N   . ILE   A 1 99  ? -13.196 4.896   -26.367 1.00 36.40 ? 213 ILE   A N   1 
ATOM   765  C  CA  . ILE   A 1 99  ? -14.253 3.905   -26.557 1.00 37.79 ? 213 ILE   A CA  1 
ATOM   766  C  C   . ILE   A 1 99  ? -14.652 3.381   -25.183 1.00 37.84 ? 213 ILE   A C   1 
ATOM   767  O  O   . ILE   A 1 99  ? -13.892 3.505   -24.209 1.00 37.78 ? 213 ILE   A O   1 
ATOM   768  C  CB  . ILE   A 1 99  ? -13.803 2.753   -27.486 1.00 36.58 ? 213 ILE   A CB  1 
ATOM   769  C  CG1 . ILE   A 1 99  ? -12.770 1.874   -26.783 1.00 37.24 ? 213 ILE   A CG1 1 
ATOM   770  C  CG2 . ILE   A 1 99  ? -13.254 3.297   -28.816 1.00 39.74 ? 213 ILE   A CG2 1 
ATOM   771  C  CD1 . ILE   A 1 99  ? -12.141 0.826   -27.682 1.00 41.54 ? 213 ILE   A CD1 1 
ATOM   772  N  N   . PRO   A 1 100 ? -15.839 2.790   -25.067 1.00 38.05 ? 214 PRO   A N   1 
ATOM   773  C  CA  . PRO   A 1 100 ? -16.270 2.258   -23.768 1.00 36.96 ? 214 PRO   A CA  1 
ATOM   774  C  C   . PRO   A 1 100 ? -15.471 1.023   -23.365 1.00 41.06 ? 214 PRO   A C   1 
ATOM   775  O  O   . PRO   A 1 100 ? -15.229 0.121   -24.171 1.00 37.92 ? 214 PRO   A O   1 
ATOM   776  C  CB  . PRO   A 1 100 ? -17.748 1.912   -23.998 1.00 38.24 ? 214 PRO   A CB  1 
ATOM   777  C  CG  . PRO   A 1 100 ? -18.151 2.718   -25.198 1.00 40.47 ? 214 PRO   A CG  1 
ATOM   778  C  CD  . PRO   A 1 100 ? -16.921 2.736   -26.063 1.00 38.11 ? 214 PRO   A CD  1 
ATOM   779  N  N   . ILE   A 1 101 ? -15.072 0.996   -22.092 1.00 40.44 ? 215 ILE   A N   1 
ATOM   780  C  CA  . ILE   A 1 101 ? -14.368 -0.124  -21.477 1.00 37.88 ? 215 ILE   A CA  1 
ATOM   781  C  C   . ILE   A 1 101 ? -15.232 -0.651  -20.341 1.00 37.42 ? 215 ILE   A C   1 
ATOM   782  O  O   . ILE   A 1 101 ? -15.708 0.129   -19.508 1.00 38.47 ? 215 ILE   A O   1 
ATOM   783  C  CB  . ILE   A 1 101 ? -12.988 0.299   -20.937 1.00 38.96 ? 215 ILE   A CB  1 
ATOM   784  C  CG1 . ILE   A 1 101 ? -12.199 1.055   -22.005 1.00 39.61 ? 215 ILE   A CG1 1 
ATOM   785  C  CG2 . ILE   A 1 101 ? -12.210 -0.905  -20.404 1.00 32.98 ? 215 ILE   A CG2 1 
ATOM   786  C  CD1 . ILE   A 1 101 ? -11.533 0.156   -23.011 1.00 41.17 ? 215 ILE   A CD1 1 
ATOM   787  N  N   . HIS   A 1 102 ? -15.429 -1.964  -20.302 1.00 34.33 ? 216 HIS   A N   1 
ATOM   788  C  CA  . HIS   A 1 102 ? -16.112 -2.616  -19.193 1.00 39.79 ? 216 HIS   A CA  1 
ATOM   789  C  C   . HIS   A 1 102 ? -15.083 -3.197  -18.231 1.00 37.24 ? 216 HIS   A C   1 
ATOM   790  O  O   . HIS   A 1 102 ? -14.066 -3.753  -18.657 1.00 37.37 ? 216 HIS   A O   1 
ATOM   791  C  CB  . HIS   A 1 102 ? -17.036 -3.736  -19.683 1.00 38.29 ? 216 HIS   A CB  1 
ATOM   792  C  CG  . HIS   A 1 102 ? -18.034 -3.304  -20.710 1.00 40.80 ? 216 HIS   A CG  1 
ATOM   793  N  ND1 . HIS   A 1 102 ? -19.387 -3.233  -20.453 1.00 41.81 ? 216 HIS   A ND1 1 
ATOM   794  C  CD2 . HIS   A 1 102 ? -17.879 -2.949  -22.008 1.00 43.47 ? 216 HIS   A CD2 1 
ATOM   795  C  CE1 . HIS   A 1 102 ? -20.020 -2.840  -21.544 1.00 43.78 ? 216 HIS   A CE1 1 
ATOM   796  N  NE2 . HIS   A 1 102 ? -19.128 -2.660  -22.501 1.00 44.14 ? 216 HIS   A NE2 1 
ATOM   797  N  N   . TYR   A 1 103 ? -15.350 -3.075  -16.937 1.00 38.90 ? 217 TYR   A N   1 
ATOM   798  C  CA  . TYR   A 1 103 ? -14.521 -3.703  -15.919 1.00 39.36 ? 217 TYR   A CA  1 
ATOM   799  C  C   . TYR   A 1 103 ? -15.277 -4.889  -15.336 1.00 37.50 ? 217 TYR   A C   1 
ATOM   800  O  O   . TYR   A 1 103 ? -16.452 -4.768  -14.976 1.00 35.39 ? 217 TYR   A O   1 
ATOM   801  C  CB  . TYR   A 1 103 ? -14.111 -2.690  -14.847 1.00 36.65 ? 217 TYR   A CB  1 
ATOM   802  C  CG  . TYR   A 1 103 ? -13.035 -1.768  -15.374 1.00 36.95 ? 217 TYR   A CG  1 
ATOM   803  C  CD1 . TYR   A 1 103 ? -11.708 -2.176  -15.408 1.00 40.14 ? 217 TYR   A CD1 1 
ATOM   804  C  CD2 . TYR   A 1 103 ? -13.349 -0.519  -15.897 1.00 37.62 ? 217 TYR   A CD2 1 
ATOM   805  C  CE1 . TYR   A 1 103 ? -10.718 -1.356  -15.915 1.00 39.90 ? 217 TYR   A CE1 1 
ATOM   806  C  CE2 . TYR   A 1 103 ? -12.362 0.312   -16.410 1.00 36.85 ? 217 TYR   A CE2 1 
ATOM   807  C  CZ  . TYR   A 1 103 ? -11.046 -0.119  -16.415 1.00 37.40 ? 217 TYR   A CZ  1 
ATOM   808  O  OH  . TYR   A 1 103 ? -10.045 0.684   -16.917 1.00 44.29 ? 217 TYR   A OH  1 
ATOM   809  N  N   . CYS   A 1 104 ? -14.611 -6.041  -15.283 1.00 39.25 ? 218 CYS   A N   1 
ATOM   810  C  CA  . CYS   A 1 104 ? -15.251 -7.308  -14.966 1.00 41.55 ? 218 CYS   A CA  1 
ATOM   811  C  C   . CYS   A 1 104 ? -14.475 -8.030  -13.872 1.00 40.90 ? 218 CYS   A C   1 
ATOM   812  O  O   . CYS   A 1 104 ? -13.252 -7.911  -13.773 1.00 40.01 ? 218 CYS   A O   1 
ATOM   813  C  CB  . CYS   A 1 104 ? -15.348 -8.197  -16.213 1.00 41.71 ? 218 CYS   A CB  1 
ATOM   814  S  SG  . CYS   A 1 104 ? -16.106 -7.372  -17.634 1.00 47.27 ? 218 CYS   A SG  1 
ATOM   815  N  N   . THR   A 1 105 ? -15.208 -8.798  -13.046 1.00 41.91 ? 219 THR   A N   1 
ATOM   816  C  CA  . THR   A 1 105 ? -14.619 -9.548  -11.944 1.00 42.22 ? 219 THR   A CA  1 
ATOM   817  C  C   . THR   A 1 105 ? -14.260 -10.969 -12.375 1.00 43.62 ? 219 THR   A C   1 
ATOM   818  O  O   . THR   A 1 105 ? -14.914 -11.542 -13.255 1.00 42.37 ? 219 THR   A O   1 
ATOM   819  C  CB  . THR   A 1 105 ? -15.590 -9.621  -10.770 1.00 41.30 ? 219 THR   A CB  1 
ATOM   820  O  OG1 . THR   A 1 105 ? -16.901 -9.911  -11.264 1.00 42.98 ? 219 THR   A OG1 1 
ATOM   821  C  CG2 . THR   A 1 105 ? -15.622 -8.306  -9.995  1.00 41.95 ? 219 THR   A CG2 1 
ATOM   822  N  N   . PRO   A 1 106 ? -13.232 -11.553 -11.767 1.00 41.60 ? 220 PRO   A N   1 
ATOM   823  C  CA  . PRO   A 1 106 ? -12.890 -12.956 -12.029 1.00 44.28 ? 220 PRO   A CA  1 
ATOM   824  C  C   . PRO   A 1 106 ? -13.782 -13.890 -11.211 1.00 43.39 ? 220 PRO   A C   1 
ATOM   825  O  O   . PRO   A 1 106 ? -14.598 -13.455 -10.401 1.00 44.44 ? 220 PRO   A O   1 
ATOM   826  C  CB  . PRO   A 1 106 ? -11.430 -13.032 -11.587 1.00 44.91 ? 220 PRO   A CB  1 
ATOM   827  C  CG  . PRO   A 1 106 ? -11.359 -12.046 -10.451 1.00 41.28 ? 220 PRO   A CG  1 
ATOM   828  C  CD  . PRO   A 1 106 ? -12.277 -10.912 -10.841 1.00 42.72 ? 220 PRO   A CD  1 
ATOM   829  N  N   . ALA   A 1 107 ? -13.625 -15.196 -11.447 1.00 46.41 ? 221 ALA   A N   1 
ATOM   830  C  CA  . ALA   A 1 107 ? -14.398 -16.195 -10.710 1.00 45.73 ? 221 ALA   A CA  1 
ATOM   831  C  C   . ALA   A 1 107 ? -14.245 -16.013 -9.201  1.00 44.66 ? 221 ALA   A C   1 
ATOM   832  O  O   . ALA   A 1 107 ? -13.155 -15.725 -8.696  1.00 44.29 ? 221 ALA   A O   1 
ATOM   833  C  CB  . ALA   A 1 107 ? -13.965 -17.612 -11.103 1.00 43.27 ? 221 ALA   A CB  1 
ATOM   834  N  N   . GLY   A 1 108 ? -15.346 -16.203 -8.475  1.00 44.82 ? 222 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 108 ? -15.357 -16.048 -7.034  1.00 46.44 ? 222 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 108 ? -15.733 -14.668 -6.542  1.00 47.34 ? 222 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 108 ? -15.805 -14.460 -5.323  1.00 50.55 ? 222 GLY   A O   1 
ATOM   838  N  N   . TYR   A 1 109 ? -15.983 -13.726 -7.448  1.00 48.77 ? 223 TYR   A N   1 
ATOM   839  C  CA  . TYR   A 1 109 ? -16.295 -12.347 -7.108  1.00 47.39 ? 223 TYR   A CA  1 
ATOM   840  C  C   . TYR   A 1 109 ? -17.464 -11.874 -7.961  1.00 46.03 ? 223 TYR   A C   1 
ATOM   841  O  O   . TYR   A 1 109 ? -17.757 -12.439 -9.019  1.00 50.44 ? 223 TYR   A O   1 
ATOM   842  C  CB  . TYR   A 1 109 ? -15.081 -11.428 -7.330  1.00 46.14 ? 223 TYR   A CB  1 
ATOM   843  C  CG  . TYR   A 1 109 ? -13.906 -11.733 -6.433  1.00 47.16 ? 223 TYR   A CG  1 
ATOM   844  C  CD1 . TYR   A 1 109 ? -13.647 -10.961 -5.310  1.00 46.61 ? 223 TYR   A CD1 1 
ATOM   845  C  CD2 . TYR   A 1 109 ? -13.046 -12.783 -6.719  1.00 47.73 ? 223 TYR   A CD2 1 
ATOM   846  C  CE1 . TYR   A 1 109 ? -12.576 -11.235 -4.488  1.00 49.50 ? 223 TYR   A CE1 1 
ATOM   847  C  CE2 . TYR   A 1 109 ? -11.967 -13.067 -5.902  1.00 48.40 ? 223 TYR   A CE2 1 
ATOM   848  C  CZ  . TYR   A 1 109 ? -11.738 -12.288 -4.783  1.00 54.33 ? 223 TYR   A CZ  1 
ATOM   849  O  OH  . TYR   A 1 109 ? -10.669 -12.549 -3.948  1.00 49.56 ? 223 TYR   A OH  1 
ATOM   850  N  N   . VAL   A 1 110 ? -18.135 -10.820 -7.492  1.00 44.38 ? 224 VAL   A N   1 
ATOM   851  C  CA  . VAL   A 1 110 ? -19.187 -10.166 -8.259  1.00 45.25 ? 224 VAL   A CA  1 
ATOM   852  C  C   . VAL   A 1 110 ? -19.123 -8.668  -8.000  1.00 42.21 ? 224 VAL   A C   1 
ATOM   853  O  O   . VAL   A 1 110 ? -18.525 -8.200  -7.029  1.00 41.78 ? 224 VAL   A O   1 
ATOM   854  C  CB  . VAL   A 1 110 ? -20.605 -10.697 -7.933  1.00 44.81 ? 224 VAL   A CB  1 
ATOM   855  C  CG1 . VAL   A 1 110 ? -20.818 -12.082 -8.531  1.00 47.69 ? 224 VAL   A CG1 1 
ATOM   856  C  CG2 . VAL   A 1 110 ? -20.863 -10.693 -6.430  1.00 43.11 ? 224 VAL   A CG2 1 
ATOM   857  N  N   . ILE   A 1 111 ? -19.751 -7.917  -8.894  1.00 42.12 ? 225 ILE   A N   1 
ATOM   858  C  CA  . ILE   A 1 111 ? -19.857 -6.471  -8.775  1.00 42.21 ? 225 ILE   A CA  1 
ATOM   859  C  C   . ILE   A 1 111 ? -21.260 -6.151  -8.279  1.00 43.39 ? 225 ILE   A C   1 
ATOM   860  O  O   . ILE   A 1 111 ? -22.252 -6.535  -8.910  1.00 44.26 ? 225 ILE   A O   1 
ATOM   861  C  CB  . ILE   A 1 111 ? -19.563 -5.778  -10.116 1.00 40.13 ? 225 ILE   A CB  1 
ATOM   862  C  CG1 . ILE   A 1 111 ? -18.134 -6.099  -10.577 1.00 41.20 ? 225 ILE   A CG1 1 
ATOM   863  C  CG2 . ILE   A 1 111 ? -19.776 -4.277  -10.001 1.00 38.18 ? 225 ILE   A CG2 1 
ATOM   864  C  CD1 . ILE   A 1 111 ? -17.809 -5.639  -11.995 1.00 44.34 ? 225 ILE   A CD1 1 
ATOM   865  N  N   . LEU   A 1 112 ? -21.352 -5.474  -7.140  1.00 39.55 ? 226 LEU   A N   1 
ATOM   866  C  CA  . LEU   A 1 112 ? -22.631 -4.982  -6.651  1.00 43.59 ? 226 LEU   A CA  1 
ATOM   867  C  C   . LEU   A 1 112 ? -22.922 -3.635  -7.299  1.00 42.46 ? 226 LEU   A C   1 
ATOM   868  O  O   . LEU   A 1 112 ? -22.017 -2.812  -7.476  1.00 39.55 ? 226 LEU   A O   1 
ATOM   869  C  CB  . LEU   A 1 112 ? -22.623 -4.855  -5.127  1.00 41.74 ? 226 LEU   A CB  1 
ATOM   870  C  CG  . LEU   A 1 112 ? -22.635 -6.184  -4.364  1.00 47.22 ? 226 LEU   A CG  1 
ATOM   871  C  CD1 . LEU   A 1 112 ? -22.988 -5.982  -2.900  1.00 46.68 ? 226 LEU   A CD1 1 
ATOM   872  C  CD2 . LEU   A 1 112 ? -23.583 -7.170  -5.022  1.00 48.16 ? 226 LEU   A CD2 1 
ATOM   873  N  N   . LYS   A 1 113 ? -24.186 -3.423  -7.667  1.00 43.63 ? 227 LYS   A N   1 
ATOM   874  C  CA  . LYS   A 1 113 ? -24.592 -2.257  -8.444  1.00 43.81 ? 227 LYS   A CA  1 
ATOM   875  C  C   . LYS   A 1 113 ? -25.699 -1.516  -7.710  1.00 44.49 ? 227 LYS   A C   1 
ATOM   876  O  O   . LYS   A 1 113 ? -26.744 -2.098  -7.402  1.00 45.08 ? 227 LYS   A O   1 
ATOM   877  C  CB  . LYS   A 1 113 ? -25.054 -2.674  -9.844  1.00 44.79 ? 227 LYS   A CB  1 
ATOM   878  C  CG  . LYS   A 1 113 ? -25.291 -1.522  -10.799 1.00 44.01 ? 227 LYS   A CG  1 
ATOM   879  C  CD  . LYS   A 1 113 ? -26.088 -1.972  -12.008 1.00 45.02 ? 227 LYS   A CD  1 
ATOM   880  C  CE  . LYS   A 1 113 ? -26.319 -0.815  -12.967 1.00 46.32 ? 227 LYS   A CE  1 
ATOM   881  N  NZ  . LYS   A 1 113 ? -26.945 -1.268  -14.239 1.00 49.25 ? 227 LYS   A NZ  1 
ATOM   882  N  N   . CYS   A 1 114 ? -25.467 -0.233  -7.442  1.00 44.50 ? 228 CYS   A N   1 
ATOM   883  C  CA  . CYS   A 1 114 ? -26.446 0.621   -6.784  1.00 49.35 ? 228 CYS   A CA  1 
ATOM   884  C  C   . CYS   A 1 114 ? -27.410 1.157   -7.835  1.00 50.44 ? 228 CYS   A C   1 
ATOM   885  O  O   . CYS   A 1 114 ? -27.019 1.965   -8.685  1.00 48.61 ? 228 CYS   A O   1 
ATOM   886  C  CB  . CYS   A 1 114 ? -25.752 1.777   -6.074  1.00 52.42 ? 228 CYS   A CB  1 
ATOM   887  S  SG  . CYS   A 1 114 ? -26.925 2.657   -5.087  1.00 59.06 ? 228 CYS   A SG  1 
ATOM   888  N  N   . ASN   A 1 115 ? -28.667 0.719   -7.784  1.00 48.09 ? 229 ASN   A N   1 
ATOM   889  C  CA  . ASN   A 1 115 ? -29.694 1.190   -8.703  1.00 49.66 ? 229 ASN   A CA  1 
ATOM   890  C  C   . ASN   A 1 115 ? -30.591 2.255   -8.081  1.00 53.21 ? 229 ASN   A C   1 
ATOM   891  O  O   . ASN   A 1 115 ? -31.668 2.536   -8.616  1.00 56.04 ? 229 ASN   A O   1 
ATOM   892  C  CB  . ASN   A 1 115 ? -30.532 0.014   -9.200  1.00 52.98 ? 229 ASN   A CB  1 
ATOM   893  C  CG  . ASN   A 1 115 ? -29.689 -1.066  -9.826  1.00 53.32 ? 229 ASN   A CG  1 
ATOM   894  O  OD1 . ASN   A 1 115 ? -29.668 -2.201  -9.355  1.00 54.28 ? 229 ASN   A OD1 1 
ATOM   895  N  ND2 . ASN   A 1 115 ? -28.982 -0.719  -10.896 1.00 48.74 ? 229 ASN   A ND2 1 
ATOM   896  N  N   . ASP   A 1 116 ? -30.177 2.844   -6.959  1.00 55.35 ? 230 ASP   A N   1 
ATOM   897  C  CA  . ASP   A 1 116 ? -30.911 3.973   -6.395  1.00 53.96 ? 230 ASP   A CA  1 
ATOM   898  C  C   . ASP   A 1 116 ? -30.706 5.211   -7.268  1.00 52.92 ? 230 ASP   A C   1 
ATOM   899  O  O   . ASP   A 1 116 ? -29.572 5.648   -7.500  1.00 52.02 ? 230 ASP   A O   1 
ATOM   900  C  CB  . ASP   A 1 116 ? -30.480 4.257   -4.947  1.00 55.15 ? 230 ASP   A CB  1 
ATOM   901  C  CG  . ASP   A 1 116 ? -30.994 3.203   -3.933  1.00 58.56 ? 230 ASP   A CG  1 
ATOM   902  O  OD1 . ASP   A 1 116 ? -32.239 3.260   -3.651  1.00 61.57 ? 230 ASP   A OD1 1 
ATOM   903  O  OD2 . ASP   A 1 116 ? -30.149 2.402   -3.433  1.00 60.97 ? 230 ASP   A OD2 1 
ATOM   904  N  N   . LYS   A 1 117 ? -31.814 5.798   -7.718  1.00 53.81 ? 231 LYS   A N   1 
ATOM   905  C  CA  . LYS   A 1 117 ? -31.740 6.908   -8.657  1.00 56.43 ? 231 LYS   A CA  1 
ATOM   906  C  C   . LYS   A 1 117 ? -31.287 8.206   -8.002  1.00 53.12 ? 231 LYS   A C   1 
ATOM   907  O  O   . LYS   A 1 117 ? -30.866 9.121   -8.714  1.00 55.05 ? 231 LYS   A O   1 
ATOM   908  C  CB  . LYS   A 1 117 ? -33.092 7.110   -9.339  1.00 57.72 ? 231 LYS   A CB  1 
ATOM   909  C  CG  . LYS   A 1 117 ? -33.285 6.254   -10.575 1.00 59.32 ? 231 LYS   A CG  1 
ATOM   910  C  CD  . LYS   A 1 117 ? -34.491 6.708   -11.376 1.00 61.72 ? 231 LYS   A CD  1 
ATOM   911  C  CE  . LYS   A 1 117 ? -35.340 5.525   -11.797 1.00 62.00 ? 231 LYS   A CE  1 
ATOM   912  N  NZ  . LYS   A 1 117 ? -34.509 4.436   -12.378 1.00 63.96 ? 231 LYS   A NZ  1 
ATOM   913  N  N   . ASN   A 1 118 ? -31.357 8.314   -6.678  1.00 49.83 ? 232 ASN   A N   1 
ATOM   914  C  CA  . ASN   A 1 118 ? -30.836 9.477   -5.973  1.00 49.39 ? 232 ASN   A CA  1 
ATOM   915  C  C   . ASN   A 1 118 ? -29.512 9.191   -5.276  1.00 47.34 ? 232 ASN   A C   1 
ATOM   916  O  O   . ASN   A 1 118 ? -29.071 10.001  -4.455  1.00 46.26 ? 232 ASN   A O   1 
ATOM   917  C  CB  . ASN   A 1 118 ? -31.855 9.988   -4.950  1.00 52.12 ? 232 ASN   A CB  1 
ATOM   918  C  CG  . ASN   A 1 118 ? -32.478 8.870   -4.132  1.00 53.83 ? 232 ASN   A CG  1 
ATOM   919  O  OD1 . ASN   A 1 118 ? -32.149 7.693   -4.307  1.00 49.57 ? 232 ASN   A OD1 1 
ATOM   920  N  ND2 . ASN   A 1 118 ? -33.377 9.237   -3.224  1.00 56.23 ? 232 ASN   A ND2 1 
ATOM   921  N  N   . PHE   A 1 119 ? -28.879 8.059   -5.571  1.00 45.90 ? 233 PHE   A N   1 
ATOM   922  C  CA  . PHE   A 1 119 ? -27.645 7.693   -4.887  1.00 48.31 ? 233 PHE   A CA  1 
ATOM   923  C  C   . PHE   A 1 119 ? -26.583 8.769   -5.082  1.00 46.39 ? 233 PHE   A C   1 
ATOM   924  O  O   . PHE   A 1 119 ? -26.266 9.144   -6.214  1.00 40.74 ? 233 PHE   A O   1 
ATOM   925  C  CB  . PHE   A 1 119 ? -27.135 6.347   -5.396  1.00 47.59 ? 233 PHE   A CB  1 
ATOM   926  C  CG  . PHE   A 1 119 ? -25.917 5.860   -4.671  1.00 44.85 ? 233 PHE   A CG  1 
ATOM   927  C  CD1 . PHE   A 1 119 ? -25.834 5.965   -3.291  1.00 48.07 ? 233 PHE   A CD1 1 
ATOM   928  C  CD2 . PHE   A 1 119 ? -24.851 5.317   -5.364  1.00 44.30 ? 233 PHE   A CD2 1 
ATOM   929  C  CE1 . PHE   A 1 119 ? -24.714 5.529   -2.616  1.00 47.25 ? 233 PHE   A CE1 1 
ATOM   930  C  CE2 . PHE   A 1 119 ? -23.727 4.876   -4.695  1.00 43.98 ? 233 PHE   A CE2 1 
ATOM   931  C  CZ  . PHE   A 1 119 ? -23.659 4.980   -3.321  1.00 44.84 ? 233 PHE   A CZ  1 
ATOM   932  N  N   . ASN   A 1 120 ? -26.026 9.267   -3.979  1.00 43.16 ? 234 ASN   A N   1 
ATOM   933  C  CA  . ASN   A 1 120 ? -25.013 10.309  -4.072  1.00 42.78 ? 234 ASN   A CA  1 
ATOM   934  C  C   . ASN   A 1 120 ? -23.590 9.764   -4.065  1.00 41.11 ? 234 ASN   A C   1 
ATOM   935  O  O   . ASN   A 1 120 ? -22.645 10.554  -4.139  1.00 36.99 ? 234 ASN   A O   1 
ATOM   936  C  CB  . ASN   A 1 120 ? -25.204 11.342  -2.952  1.00 44.92 ? 234 ASN   A CB  1 
ATOM   937  C  CG  . ASN   A 1 120 ? -24.872 10.804  -1.576  1.00 45.01 ? 234 ASN   A CG  1 
ATOM   938  O  OD1 . ASN   A 1 120 ? -24.226 9.770   -1.425  1.00 45.18 ? 234 ASN   A OD1 1 
ATOM   939  N  ND2 . ASN   A 1 120 ? -25.325 11.512  -0.555  1.00 47.22 ? 234 ASN   A ND2 1 
ATOM   940  N  N   . GLY   A 1 121 ? -23.415 8.444   -3.986  1.00 40.70 ? 235 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? -22.113 7.816   -4.042  1.00 40.20 ? 235 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? -21.589 7.295   -2.717  1.00 41.83 ? 235 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? -20.656 6.479   -2.720  1.00 37.74 ? 235 GLY   A O   1 
ATOM   944  N  N   . THR   A 1 122 ? -22.148 7.732   -1.587  1.00 40.36 ? 236 THR   A N   1 
ATOM   945  C  CA  . THR   A 1 122 ? -21.694 7.248   -0.290  1.00 46.11 ? 236 THR   A CA  1 
ATOM   946  C  C   . THR   A 1 122 ? -22.892 6.943   0.598   1.00 45.82 ? 236 THR   A C   1 
ATOM   947  O  O   . THR   A 1 122 ? -23.924 7.615   0.536   1.00 45.59 ? 236 THR   A O   1 
ATOM   948  C  CB  . THR   A 1 122 ? -20.768 8.254   0.408   1.00 43.84 ? 236 THR   A CB  1 
ATOM   949  O  OG1 . THR   A 1 122 ? -21.393 8.743   1.601   1.00 51.21 ? 236 THR   A OG1 1 
ATOM   950  C  CG2 . THR   A 1 122 ? -20.448 9.420   -0.510  1.00 42.17 ? 236 THR   A CG2 1 
ATOM   951  N  N   . GLY   A 1 123 ? -22.740 5.922   1.434   1.00 48.42 ? 237 GLY   A N   1 
ATOM   952  C  CA  . GLY   A 1 123 ? -23.793 5.519   2.334   1.00 54.68 ? 237 GLY   A CA  1 
ATOM   953  C  C   . GLY   A 1 123 ? -24.587 4.339   1.811   1.00 49.16 ? 237 GLY   A C   1 
ATOM   954  O  O   . GLY   A 1 123 ? -24.179 3.657   0.866   1.00 46.72 ? 237 GLY   A O   1 
ATOM   955  N  N   . PRO   A 1 124 ? -25.744 4.077   2.415   1.00 50.40 ? 238 PRO   A N   1 
ATOM   956  C  CA  . PRO   A 1 124 ? -26.511 2.886   2.040   1.00 52.29 ? 238 PRO   A CA  1 
ATOM   957  C  C   . PRO   A 1 124 ? -27.237 3.039   0.711   1.00 54.97 ? 238 PRO   A C   1 
ATOM   958  O  O   . PRO   A 1 124 ? -27.647 4.131   0.306   1.00 50.83 ? 238 PRO   A O   1 
ATOM   959  C  CB  . PRO   A 1 124 ? -27.508 2.727   3.193   1.00 53.79 ? 238 PRO   A CB  1 
ATOM   960  C  CG  . PRO   A 1 124 ? -27.657 4.094   3.760   1.00 53.77 ? 238 PRO   A CG  1 
ATOM   961  C  CD  . PRO   A 1 124 ? -26.338 4.784   3.565   1.00 54.23 ? 238 PRO   A CD  1 
ATOM   962  N  N   . CYS   A 1 125 ? -27.405 1.899   0.050   1.00 50.97 ? 239 CYS   A N   1 
ATOM   963  C  CA  . CYS   A 1 125 ? -28.095 1.763   -1.224  1.00 57.23 ? 239 CYS   A CA  1 
ATOM   964  C  C   . CYS   A 1 125 ? -29.216 0.742   -1.041  1.00 56.23 ? 239 CYS   A C   1 
ATOM   965  O  O   . CYS   A 1 125 ? -28.980 -0.356  -0.523  1.00 58.35 ? 239 CYS   A O   1 
ATOM   966  C  CB  . CYS   A 1 125 ? -27.090 1.345   -2.316  1.00 52.84 ? 239 CYS   A CB  1 
ATOM   967  S  SG  . CYS   A 1 125 ? -27.710 1.120   -4.017  1.00 73.60 ? 239 CYS   A SG  1 
ATOM   968  N  N   . LYS   A 1 126 ? -30.441 1.117   -1.418  1.00 52.85 ? 240 LYS   A N   1 
ATOM   969  C  CA  . LYS   A 1 126 ? -31.618 0.299   -1.138  1.00 54.10 ? 240 LYS   A CA  1 
ATOM   970  C  C   . LYS   A 1 126 ? -31.996 -0.638  -2.281  1.00 56.57 ? 240 LYS   A C   1 
ATOM   971  O  O   . LYS   A 1 126 ? -32.683 -1.639  -2.043  1.00 54.68 ? 240 LYS   A O   1 
ATOM   972  C  CB  . LYS   A 1 126 ? -32.810 1.207   -0.809  1.00 58.01 ? 240 LYS   A CB  1 
ATOM   973  C  CG  . LYS   A 1 126 ? -33.969 0.527   -0.106  1.00 61.37 ? 240 LYS   A CG  1 
ATOM   974  C  CD  . LYS   A 1 126 ? -35.290 1.099   -0.608  1.00 64.16 ? 240 LYS   A CD  1 
ATOM   975  C  CE  . LYS   A 1 126 ? -35.308 2.617   -0.516  1.00 59.11 ? 240 LYS   A CE  1 
ATOM   976  N  NZ  . LYS   A 1 126 ? -36.623 3.117   -0.035  1.00 57.51 ? 240 LYS   A NZ  1 
ATOM   977  N  N   . ASN   A 1 127 ? -31.571 -0.343  -3.506  1.00 55.85 ? 241 ASN   A N   1 
ATOM   978  C  CA  . ASN   A 1 127 ? -31.907 -1.133  -4.691  1.00 55.43 ? 241 ASN   A CA  1 
ATOM   979  C  C   . ASN   A 1 127 ? -30.606 -1.683  -5.273  1.00 52.80 ? 241 ASN   A C   1 
ATOM   980  O  O   . ASN   A 1 127 ? -29.999 -1.070  -6.155  1.00 50.62 ? 241 ASN   A O   1 
ATOM   981  C  CB  . ASN   A 1 127 ? -32.664 -0.285  -5.713  1.00 54.44 ? 241 ASN   A CB  1 
ATOM   982  C  CG  . ASN   A 1 127 ? -33.190 -1.100  -6.876  1.00 58.38 ? 241 ASN   A CG  1 
ATOM   983  O  OD1 . ASN   A 1 127 ? -33.050 -2.322  -6.914  1.00 56.63 ? 241 ASN   A OD1 1 
ATOM   984  N  ND2 . ASN   A 1 127 ? -33.796 -0.415  -7.839  1.00 60.19 ? 241 ASN   A ND2 1 
ATOM   985  N  N   . VAL   A 1 128 ? -30.185 -2.844  -4.782  1.00 49.89 ? 242 VAL   A N   1 
ATOM   986  C  CA  . VAL   A 1 128 ? -28.895 -3.424  -5.133  1.00 47.86 ? 242 VAL   A CA  1 
ATOM   987  C  C   . VAL   A 1 128 ? -29.104 -4.554  -6.128  1.00 49.71 ? 242 VAL   A C   1 
ATOM   988  O  O   . VAL   A 1 128 ? -30.001 -5.392  -5.967  1.00 49.64 ? 242 VAL   A O   1 
ATOM   989  C  CB  . VAL   A 1 128 ? -28.143 -3.927  -3.885  1.00 50.16 ? 242 VAL   A CB  1 
ATOM   990  C  CG1 . VAL   A 1 128 ? -26.762 -4.456  -4.270  1.00 48.40 ? 242 VAL   A CG1 1 
ATOM   991  C  CG2 . VAL   A 1 128 ? -28.027 -2.814  -2.856  1.00 52.46 ? 242 VAL   A CG2 1 
ATOM   992  N  N   . SER   A 1 129 ? -28.271 -4.569  -7.162  1.00 48.48 ? 243 SER   A N   1 
ATOM   993  C  CA  . SER   A 1 129 ? -28.208 -5.656  -8.120  1.00 49.51 ? 243 SER   A CA  1 
ATOM   994  C  C   . SER   A 1 129 ? -26.758 -6.097  -8.241  1.00 46.78 ? 243 SER   A C   1 
ATOM   995  O  O   . SER   A 1 129 ? -25.830 -5.337  -7.953  1.00 47.96 ? 243 SER   A O   1 
ATOM   996  C  CB  . SER   A 1 129 ? -28.758 -5.238  -9.494  1.00 51.11 ? 243 SER   A CB  1 
ATOM   997  O  OG  . SER   A 1 129 ? -27.725 -4.780  -10.351 1.00 52.04 ? 243 SER   A OG  1 
ATOM   998  N  N   . SER   A 1 130 ? -26.570 -7.341  -8.656  1.00 46.13 ? 244 SER   A N   1 
ATOM   999  C  CA  . SER   A 1 130 ? -25.248 -7.896  -8.891  1.00 47.84 ? 244 SER   A CA  1 
ATOM   1000 C  C   . SER   A 1 130 ? -25.056 -8.127  -10.383 1.00 48.21 ? 244 SER   A C   1 
ATOM   1001 O  O   . SER   A 1 130 ? -25.964 -8.612  -11.067 1.00 46.85 ? 244 SER   A O   1 
ATOM   1002 C  CB  . SER   A 1 130 ? -25.053 -9.205  -8.120  1.00 44.59 ? 244 SER   A CB  1 
ATOM   1003 O  OG  . SER   A 1 130 ? -25.333 -10.325 -8.940  1.00 51.10 ? 244 SER   A OG  1 
ATOM   1004 N  N   . VAL   A 1 131 ? -23.876 -7.762  -10.886 1.00 45.36 ? 245 VAL   A N   1 
ATOM   1005 C  CA  . VAL   A 1 131 ? -23.535 -7.919  -12.292 1.00 45.38 ? 245 VAL   A CA  1 
ATOM   1006 C  C   . VAL   A 1 131 ? -22.141 -8.526  -12.390 1.00 44.90 ? 245 VAL   A C   1 
ATOM   1007 O  O   . VAL   A 1 131 ? -21.404 -8.618  -11.407 1.00 44.09 ? 245 VAL   A O   1 
ATOM   1008 C  CB  . VAL   A 1 131 ? -23.600 -6.586  -13.071 1.00 46.03 ? 245 VAL   A CB  1 
ATOM   1009 C  CG1 . VAL   A 1 131 ? -24.996 -5.977  -12.989 1.00 46.36 ? 245 VAL   A CG1 1 
ATOM   1010 C  CG2 . VAL   A 1 131 ? -22.546 -5.611  -12.555 1.00 42.89 ? 245 VAL   A CG2 1 
ATOM   1011 N  N   . GLN   A 1 132 ? -21.790 -8.948  -13.603 1.00 42.21 ? 246 GLN   A N   1 
ATOM   1012 C  CA  . GLN   A 1 132 ? -20.465 -9.483  -13.889 1.00 45.75 ? 246 GLN   A CA  1 
ATOM   1013 C  C   . GLN   A 1 132 ? -19.511 -8.440  -14.446 1.00 43.73 ? 246 GLN   A C   1 
ATOM   1014 O  O   . GLN   A 1 132 ? -18.300 -8.542  -14.230 1.00 43.86 ? 246 GLN   A O   1 
ATOM   1015 C  CB  . GLN   A 1 132 ? -20.568 -10.648 -14.880 1.00 49.68 ? 246 GLN   A CB  1 
ATOM   1016 C  CG  . GLN   A 1 132 ? -21.470 -11.763 -14.415 1.00 51.64 ? 246 GLN   A CG  1 
ATOM   1017 C  CD  . GLN   A 1 132 ? -20.715 -12.839 -13.667 1.00 58.09 ? 246 GLN   A CD  1 
ATOM   1018 O  OE1 . GLN   A 1 132 ? -19.886 -12.545 -12.803 1.00 57.68 ? 246 GLN   A OE1 1 
ATOM   1019 N  NE2 . GLN   A 1 132 ? -20.993 -14.099 -13.999 1.00 65.95 ? 246 GLN   A NE2 1 
ATOM   1020 N  N   . CYS   A 1 133 ? -20.031 -7.443  -15.152 1.00 42.16 ? 247 CYS   A N   1 
ATOM   1021 C  CA  . CYS   A 1 133 ? -19.232 -6.364  -15.700 1.00 43.07 ? 247 CYS   A CA  1 
ATOM   1022 C  C   . CYS   A 1 133 ? -19.961 -5.052  -15.471 1.00 40.25 ? 247 CYS   A C   1 
ATOM   1023 O  O   . CYS   A 1 133 ? -21.194 -5.013  -15.437 1.00 39.26 ? 247 CYS   A O   1 
ATOM   1024 C  CB  . CYS   A 1 133 ? -18.975 -6.565  -17.200 1.00 39.55 ? 247 CYS   A CB  1 
ATOM   1025 S  SG  . CYS   A 1 133 ? -18.027 -8.045  -17.591 1.00 52.85 ? 247 CYS   A SG  1 
ATOM   1026 N  N   . THR   A 1 134 ? -19.192 -3.982  -15.287 1.00 36.82 ? 248 THR   A N   1 
ATOM   1027 C  CA  . THR   A 1 134 ? -19.779 -2.655  -15.321 1.00 38.98 ? 248 THR   A CA  1 
ATOM   1028 C  C   . THR   A 1 134 ? -20.266 -2.351  -16.739 1.00 37.33 ? 248 THR   A C   1 
ATOM   1029 O  O   . THR   A 1 134 ? -19.990 -3.089  -17.688 1.00 33.89 ? 248 THR   A O   1 
ATOM   1030 C  CB  . THR   A 1 134 ? -18.763 -1.602  -14.881 1.00 38.30 ? 248 THR   A CB  1 
ATOM   1031 O  OG1 . THR   A 1 134 ? -17.842 -1.366  -15.952 1.00 37.69 ? 248 THR   A OG1 1 
ATOM   1032 C  CG2 . THR   A 1 134 ? -17.985 -2.070  -13.650 1.00 38.91 ? 248 THR   A CG2 1 
ATOM   1033 N  N   . HIS   A 1 135 ? -21.003 -1.250  -16.881 1.00 38.36 ? 249 HIS   A N   1 
ATOM   1034 C  CA  . HIS   A 1 135 ? -21.356 -0.777  -18.211 1.00 40.24 ? 249 HIS   A CA  1 
ATOM   1035 C  C   . HIS   A 1 135 ? -20.111 -0.228  -18.909 1.00 40.57 ? 249 HIS   A C   1 
ATOM   1036 O  O   . HIS   A 1 135 ? -19.023 -0.143  -18.330 1.00 39.56 ? 249 HIS   A O   1 
ATOM   1037 C  CB  . HIS   A 1 135 ? -22.451 0.284   -18.133 1.00 39.22 ? 249 HIS   A CB  1 
ATOM   1038 C  CG  . HIS   A 1 135 ? -22.006 1.565   -17.499 1.00 43.52 ? 249 HIS   A CG  1 
ATOM   1039 N  ND1 . HIS   A 1 135 ? -22.152 1.816   -16.152 1.00 40.77 ? 249 HIS   A ND1 1 
ATOM   1040 C  CD2 . HIS   A 1 135 ? -21.430 2.671   -18.028 1.00 43.06 ? 249 HIS   A CD2 1 
ATOM   1041 C  CE1 . HIS   A 1 135 ? -21.671 3.015   -15.876 1.00 41.89 ? 249 HIS   A CE1 1 
ATOM   1042 N  NE2 . HIS   A 1 135 ? -21.229 3.556   -16.997 1.00 42.34 ? 249 HIS   A NE2 1 
ATOM   1043 N  N   . GLY   A 1 136 ? -20.274 0.142   -20.178 1.00 40.19 ? 250 GLY   A N   1 
ATOM   1044 C  CA  . GLY   A 1 136 ? -19.193 0.741   -20.935 1.00 39.25 ? 250 GLY   A CA  1 
ATOM   1045 C  C   . GLY   A 1 136 ? -18.875 2.152   -20.485 1.00 37.04 ? 250 GLY   A C   1 
ATOM   1046 O  O   . GLY   A 1 136 ? -19.708 3.054   -20.611 1.00 38.93 ? 250 GLY   A O   1 
ATOM   1047 N  N   . ILE   A 1 137 ? -17.676 2.350   -19.944 1.00 36.61 ? 251 ILE   A N   1 
ATOM   1048 C  CA  . ILE   A 1 137 ? -17.226 3.644   -19.443 1.00 36.28 ? 251 ILE   A CA  1 
ATOM   1049 C  C   . ILE   A 1 137 ? -16.158 4.180   -20.384 1.00 37.90 ? 251 ILE   A C   1 
ATOM   1050 O  O   . ILE   A 1 137 ? -15.155 3.505   -20.645 1.00 37.52 ? 251 ILE   A O   1 
ATOM   1051 C  CB  . ILE   A 1 137 ? -16.683 3.533   -18.008 1.00 39.46 ? 251 ILE   A CB  1 
ATOM   1052 C  CG1 . ILE   A 1 137 ? -17.764 3.007   -17.059 1.00 39.67 ? 251 ILE   A CG1 1 
ATOM   1053 C  CG2 . ILE   A 1 137 ? -16.123 4.874   -17.527 1.00 36.20 ? 251 ILE   A CG2 1 
ATOM   1054 C  CD1 . ILE   A 1 137 ? -17.227 2.624   -15.699 1.00 39.62 ? 251 ILE   A CD1 1 
ATOM   1055 N  N   . LYS   A 1 138 ? -16.374 5.393   -20.891 1.00 36.92 ? 252 LYS   A N   1 
ATOM   1056 C  CA  . LYS   A 1 138 ? -15.390 6.061   -21.736 1.00 35.80 ? 252 LYS   A CA  1 
ATOM   1057 C  C   . LYS   A 1 138 ? -14.346 6.749   -20.867 1.00 37.11 ? 252 LYS   A C   1 
ATOM   1058 O  O   . LYS   A 1 138 ? -14.708 7.554   -20.002 1.00 35.93 ? 252 LYS   A O   1 
ATOM   1059 C  CB  . LYS   A 1 138 ? -16.064 7.089   -22.634 1.00 38.35 ? 252 LYS   A CB  1 
ATOM   1060 C  CG  . LYS   A 1 138 ? -16.823 6.492   -23.813 1.00 37.46 ? 252 LYS   A CG  1 
ATOM   1061 C  CD  . LYS   A 1 138 ? -16.866 7.463   -24.982 1.00 39.01 ? 252 LYS   A CD  1 
ATOM   1062 C  CE  . LYS   A 1 138 ? -17.790 6.975   -26.083 1.00 41.54 ? 252 LYS   A CE  1 
ATOM   1063 N  NZ  . LYS   A 1 138 ? -18.463 8.137   -26.753 1.00 47.22 ? 252 LYS   A NZ  1 
ATOM   1064 N  N   . PRO   A 1 139 ? -13.057 6.466   -21.053 1.00 34.32 ? 253 PRO   A N   1 
ATOM   1065 C  CA  . PRO   A 1 139 ? -12.007 7.119   -20.235 1.00 36.10 ? 253 PRO   A CA  1 
ATOM   1066 C  C   . PRO   A 1 139 ? -11.608 8.501   -20.762 1.00 36.31 ? 253 PRO   A C   1 
ATOM   1067 O  O   . PRO   A 1 139 ? -10.561 8.707   -21.384 1.00 39.51 ? 253 PRO   A O   1 
ATOM   1068 C  CB  . PRO   A 1 139 ? -10.855 6.116   -20.319 1.00 32.44 ? 253 PRO   A CB  1 
ATOM   1069 C  CG  . PRO   A 1 139 ? -11.006 5.528   -21.714 1.00 38.92 ? 253 PRO   A CG  1 
ATOM   1070 C  CD  . PRO   A 1 139 ? -12.498 5.430   -21.940 1.00 34.56 ? 253 PRO   A CD  1 
ATOM   1071 N  N   . VAL   A 1 140 ? -12.464 9.492   -20.512 1.00 35.03 ? 254 VAL   A N   1 
ATOM   1072 C  CA  . VAL   A 1 140 ? -12.263 10.847  -21.029 1.00 35.06 ? 254 VAL   A CA  1 
ATOM   1073 C  C   . VAL   A 1 140 ? -11.439 11.639  -20.022 1.00 34.37 ? 254 VAL   A C   1 
ATOM   1074 O  O   . VAL   A 1 140 ? -11.876 11.865  -18.890 1.00 34.68 ? 254 VAL   A O   1 
ATOM   1075 C  CB  . VAL   A 1 140 ? -13.601 11.552  -21.317 1.00 37.46 ? 254 VAL   A CB  1 
ATOM   1076 C  CG1 . VAL   A 1 140 ? -13.365 12.888  -22.023 1.00 32.47 ? 254 VAL   A CG1 1 
ATOM   1077 C  CG2 . VAL   A 1 140 ? -14.524 10.659  -22.149 1.00 36.03 ? 254 VAL   A CG2 1 
ATOM   1078 N  N   . VAL   A 1 141 ? -10.249 12.066  -20.437 1.00 36.02 ? 255 VAL   A N   1 
ATOM   1079 C  CA  . VAL   A 1 141 ? -9.360  12.855  -19.591 1.00 38.61 ? 255 VAL   A CA  1 
ATOM   1080 C  C   . VAL   A 1 141 ? -9.702  14.329  -19.778 1.00 37.95 ? 255 VAL   A C   1 
ATOM   1081 O  O   . VAL   A 1 141 ? -9.695  14.837  -20.904 1.00 35.13 ? 255 VAL   A O   1 
ATOM   1082 C  CB  . VAL   A 1 141 ? -7.887  12.585  -19.934 1.00 38.87 ? 255 VAL   A CB  1 
ATOM   1083 C  CG1 . VAL   A 1 141 ? -6.989  13.703  -19.374 1.00 36.67 ? 255 VAL   A CG1 1 
ATOM   1084 C  CG2 . VAL   A 1 141 ? -7.462  11.199  -19.439 1.00 37.47 ? 255 VAL   A CG2 1 
ATOM   1085 N  N   . SER   A 1 142 ? -9.986  15.021  -18.677 1.00 34.35 ? 256 SER   A N   1 
ATOM   1086 C  CA  . SER   A 1 142 ? -10.303 16.442  -18.742 1.00 35.16 ? 256 SER   A CA  1 
ATOM   1087 C  C   . SER   A 1 142 ? -10.136 17.061  -17.361 1.00 37.94 ? 256 SER   A C   1 
ATOM   1088 O  O   . SER   A 1 142 ? -9.946  16.363  -16.360 1.00 34.95 ? 256 SER   A O   1 
ATOM   1089 C  CB  . SER   A 1 142 ? -11.726 16.677  -19.262 1.00 36.96 ? 256 SER   A CB  1 
ATOM   1090 O  OG  . SER   A 1 142 ? -12.698 16.107  -18.397 1.00 36.00 ? 256 SER   A OG  1 
ATOM   1091 N  N   . THR   A 1 143 ? -10.206 18.394  -17.328 1.00 33.99 ? 257 THR   A N   1 
ATOM   1092 C  CA  . THR   A 1 143 ? -10.301 19.173  -16.102 1.00 34.32 ? 257 THR   A CA  1 
ATOM   1093 C  C   . THR   A 1 143 ? -11.522 20.087  -16.171 1.00 33.81 ? 257 THR   A C   1 
ATOM   1094 O  O   . THR   A 1 143 ? -12.019 20.420  -17.250 1.00 32.74 ? 257 THR   A O   1 
ATOM   1095 C  CB  . THR   A 1 143 ? -9.034  20.015  -15.852 1.00 36.51 ? 257 THR   A CB  1 
ATOM   1096 O  OG1 . THR   A 1 143 ? -8.891  21.000  -16.884 1.00 36.95 ? 257 THR   A OG1 1 
ATOM   1097 C  CG2 . THR   A 1 143 ? -7.791  19.137  -15.824 1.00 39.43 ? 257 THR   A CG2 1 
ATOM   1098 N  N   . GLN   A 1 144 ? -11.990 20.498  -14.991 1.00 33.43 ? 258 GLN   A N   1 
ATOM   1099 C  CA  . GLN   A 1 144 ? -13.145 21.379  -14.817 1.00 36.55 ? 258 GLN   A CA  1 
ATOM   1100 C  C   . GLN   A 1 144 ? -14.466 20.740  -15.236 1.00 33.75 ? 258 GLN   A C   1 
ATOM   1101 O  O   . GLN   A 1 144 ? -15.381 20.621  -14.414 1.00 36.25 ? 258 GLN   A O   1 
ATOM   1102 C  CB  . GLN   A 1 144 ? -12.956 22.705  -15.558 1.00 32.69 ? 258 GLN   A CB  1 
ATOM   1103 C  CG  . GLN   A 1 144 ? -11.658 23.428  -15.251 1.00 33.56 ? 258 GLN   A CG  1 
ATOM   1104 C  CD  . GLN   A 1 144 ? -11.751 24.920  -15.565 1.00 36.12 ? 258 GLN   A CD  1 
ATOM   1105 O  OE1 . GLN   A 1 144 ? -12.725 25.379  -16.171 1.00 32.58 ? 258 GLN   A OE1 1 
ATOM   1106 N  NE2 . GLN   A 1 144 ? -10.733 25.677  -15.165 1.00 36.96 ? 258 GLN   A NE2 1 
ATOM   1107 N  N   . LEU   A 1 145 ? -14.594 20.344  -16.499 1.00 34.92 ? 259 LEU   A N   1 
ATOM   1108 C  CA  . LEU   A 1 145 ? -15.830 19.770  -17.019 1.00 34.96 ? 259 LEU   A CA  1 
ATOM   1109 C  C   . LEU   A 1 145 ? -15.643 18.290  -17.318 1.00 36.44 ? 259 LEU   A C   1 
ATOM   1110 O  O   . LEU   A 1 145 ? -14.675 17.899  -17.983 1.00 35.38 ? 259 LEU   A O   1 
ATOM   1111 C  CB  . LEU   A 1 145 ? -16.296 20.507  -18.277 1.00 33.03 ? 259 LEU   A CB  1 
ATOM   1112 C  CG  . LEU   A 1 145 ? -16.315 22.035  -18.231 1.00 34.27 ? 259 LEU   A CG  1 
ATOM   1113 C  CD1 . LEU   A 1 145 ? -16.338 22.623  -19.628 1.00 38.94 ? 259 LEU   A CD1 1 
ATOM   1114 C  CD2 . LEU   A 1 145 ? -17.506 22.534  -17.407 1.00 37.61 ? 259 LEU   A CD2 1 
ATOM   1115 N  N   . LEU   A 1 146 ? -16.579 17.477  -16.832 1.00 33.78 ? 260 LEU   A N   1 
ATOM   1116 C  CA  . LEU   A 1 146 ? -16.607 16.061  -17.157 1.00 32.85 ? 260 LEU   A CA  1 
ATOM   1117 C  C   . LEU   A 1 146 ? -17.345 15.886  -18.475 1.00 34.65 ? 260 LEU   A C   1 
ATOM   1118 O  O   . LEU   A 1 146 ? -18.447 16.415  -18.654 1.00 33.74 ? 260 LEU   A O   1 
ATOM   1119 C  CB  . LEU   A 1 146 ? -17.294 15.275  -16.043 1.00 32.79 ? 260 LEU   A CB  1 
ATOM   1120 C  CG  . LEU   A 1 146 ? -16.539 15.238  -14.707 1.00 35.15 ? 260 LEU   A CG  1 
ATOM   1121 C  CD1 . LEU   A 1 146 ? -17.286 14.431  -13.657 1.00 36.56 ? 260 LEU   A CD1 1 
ATOM   1122 C  CD2 . LEU   A 1 146 ? -15.143 14.679  -14.909 1.00 38.38 ? 260 LEU   A CD2 1 
ATOM   1123 N  N   . LEU   A 1 147 ? -16.738 15.152  -19.399 1.00 33.88 ? 261 LEU   A N   1 
ATOM   1124 C  CA  . LEU   A 1 147 ? -17.203 15.114  -20.776 1.00 35.90 ? 261 LEU   A CA  1 
ATOM   1125 C  C   . LEU   A 1 147 ? -17.597 13.703  -21.177 1.00 34.53 ? 261 LEU   A C   1 
ATOM   1126 O  O   . LEU   A 1 147 ? -16.922 12.732  -20.823 1.00 34.24 ? 261 LEU   A O   1 
ATOM   1127 C  CB  . LEU   A 1 147 ? -16.128 15.633  -21.736 1.00 33.93 ? 261 LEU   A CB  1 
ATOM   1128 C  CG  . LEU   A 1 147 ? -15.559 17.013  -21.437 1.00 34.39 ? 261 LEU   A CG  1 
ATOM   1129 C  CD1 . LEU   A 1 147 ? -14.456 17.340  -22.427 1.00 37.08 ? 261 LEU   A CD1 1 
ATOM   1130 C  CD2 . LEU   A 1 147 ? -16.665 18.050  -21.497 1.00 34.43 ? 261 LEU   A CD2 1 
ATOM   1131 N  N   . ASN   A 1 148 ? -18.698 13.602  -21.916 1.00 36.07 ? 262 ASN   A N   1 
ATOM   1132 C  CA  . ASN   A 1 148 ? -19.075 12.368  -22.590 1.00 35.39 ? 262 ASN   A CA  1 
ATOM   1133 C  C   . ASN   A 1 148 ? -19.384 11.243  -21.607 1.00 38.93 ? 262 ASN   A C   1 
ATOM   1134 O  O   . ASN   A 1 148 ? -19.178 10.066  -21.918 1.00 38.53 ? 262 ASN   A O   1 
ATOM   1135 C  CB  . ASN   A 1 148 ? -17.979 11.935  -23.567 1.00 35.04 ? 262 ASN   A CB  1 
ATOM   1136 C  CG  . ASN   A 1 148 ? -18.075 12.644  -24.898 1.00 39.02 ? 262 ASN   A CG  1 
ATOM   1137 O  OD1 . ASN   A 1 148 ? -18.946 13.485  -25.109 1.00 35.39 ? 262 ASN   A OD1 1 
ATOM   1138 N  ND2 . ASN   A 1 148 ? -17.175 12.312  -25.803 1.00 39.86 ? 262 ASN   A ND2 1 
ATOM   1139 N  N   . GLY   A 1 149 ? -19.876 11.586  -20.416 1.00 40.17 ? 263 GLY   A N   1 
ATOM   1140 C  CA  . GLY   A 1 149 ? -20.226 10.607  -19.414 1.00 39.70 ? 263 GLY   A CA  1 
ATOM   1141 C  C   . GLY   A 1 149 ? -21.715 10.303  -19.392 1.00 40.78 ? 263 GLY   A C   1 
ATOM   1142 O  O   . GLY   A 1 149 ? -22.471 10.627  -20.312 1.00 36.67 ? 263 GLY   A O   1 
ATOM   1143 N  N   . SER   A 1 150 ? -22.129 9.639   -18.318 1.00 37.55 ? 264 SER   A N   1 
ATOM   1144 C  CA  . SER   A 1 150 ? -23.537 9.382   -18.073 1.00 41.23 ? 264 SER   A CA  1 
ATOM   1145 C  C   . SER   A 1 150 ? -24.141 10.556  -17.309 1.00 41.53 ? 264 SER   A C   1 
ATOM   1146 O  O   . SER   A 1 150 ? -23.437 11.441  -16.819 1.00 40.52 ? 264 SER   A O   1 
ATOM   1147 C  CB  . SER   A 1 150 ? -23.715 8.076   -17.301 1.00 41.18 ? 264 SER   A CB  1 
ATOM   1148 O  OG  . SER   A 1 150 ? -23.126 8.169   -16.013 1.00 47.40 ? 264 SER   A OG  1 
ATOM   1149 N  N   . LEU   A 1 151 ? -25.464 10.566  -17.216 1.00 41.89 ? 265 LEU   A N   1 
ATOM   1150 C  CA  . LEU   A 1 151 ? -26.170 11.652  -16.557 1.00 44.03 ? 265 LEU   A CA  1 
ATOM   1151 C  C   . LEU   A 1 151 ? -26.940 11.130  -15.353 1.00 45.60 ? 265 LEU   A C   1 
ATOM   1152 O  O   . LEU   A 1 151 ? -27.350 9.964   -15.311 1.00 47.04 ? 265 LEU   A O   1 
ATOM   1153 C  CB  . LEU   A 1 151 ? -27.132 12.359  -17.521 1.00 44.90 ? 265 LEU   A CB  1 
ATOM   1154 C  CG  . LEU   A 1 151 ? -26.530 12.991  -18.772 1.00 42.45 ? 265 LEU   A CG  1 
ATOM   1155 C  CD1 . LEU   A 1 151 ? -27.560 13.030  -19.886 1.00 46.63 ? 265 LEU   A CD1 1 
ATOM   1156 C  CD2 . LEU   A 1 151 ? -26.013 14.386  -18.452 1.00 42.10 ? 265 LEU   A CD2 1 
ATOM   1157 N  N   . ALA   A 1 152 ? -27.121 12.005  -14.363 1.00 46.51 ? 266 ALA   A N   1 
ATOM   1158 C  CA  . ALA   A 1 152 ? -28.005 11.680  -13.251 1.00 46.33 ? 266 ALA   A CA  1 
ATOM   1159 C  C   . ALA   A 1 152 ? -29.403 11.381  -13.780 1.00 50.70 ? 266 ALA   A C   1 
ATOM   1160 O  O   . ALA   A 1 152 ? -29.915 12.087  -14.654 1.00 50.15 ? 266 ALA   A O   1 
ATOM   1161 C  CB  . ALA   A 1 152 ? -28.051 12.823  -12.237 1.00 43.95 ? 266 ALA   A CB  1 
ATOM   1162 N  N   . GLU   A 1 153 ? -30.022 10.327  -13.248 1.00 57.79 ? 267 GLU   A N   1 
ATOM   1163 C  CA  . GLU   A 1 153 ? -31.304 9.873   -13.776 1.00 58.72 ? 267 GLU   A CA  1 
ATOM   1164 C  C   . GLU   A 1 153 ? -32.486 10.689  -13.262 1.00 57.80 ? 267 GLU   A C   1 
ATOM   1165 O  O   . GLU   A 1 153 ? -33.551 10.673  -13.889 1.00 56.59 ? 267 GLU   A O   1 
ATOM   1166 C  CB  . GLU   A 1 153 ? -31.511 8.387   -13.456 1.00 58.99 ? 267 GLU   A CB  1 
ATOM   1167 C  CG  . GLU   A 1 153 ? -30.760 7.449   -14.403 1.00 63.70 ? 267 GLU   A CG  1 
ATOM   1168 C  CD  . GLU   A 1 153 ? -29.680 6.624   -13.717 1.00 70.14 ? 267 GLU   A CD  1 
ATOM   1169 O  OE1 . GLU   A 1 153 ? -28.689 6.268   -14.394 1.00 72.17 ? 267 GLU   A OE1 1 
ATOM   1170 O  OE2 . GLU   A 1 153 ? -29.823 6.330   -12.510 1.00 69.33 ? 267 GLU   A OE2 1 
ATOM   1171 N  N   . GLU   A 1 154 ? -32.328 11.414  -12.155 1.00 55.80 ? 268 GLU   A N   1 
ATOM   1172 C  CA  . GLU   A 1 154 ? -33.426 12.224  -11.640 1.00 54.64 ? 268 GLU   A CA  1 
ATOM   1173 C  C   . GLU   A 1 154 ? -33.005 13.674  -11.454 1.00 53.09 ? 268 GLU   A C   1 
ATOM   1174 O  O   . GLU   A 1 154 ? -33.106 14.478  -12.386 1.00 50.48 ? 268 GLU   A O   1 
ATOM   1175 C  CB  . GLU   A 1 154 ? -33.944 11.651  -10.322 1.00 58.96 ? 268 GLU   A CB  1 
ATOM   1176 C  CG  . GLU   A 1 154 ? -35.043 10.618  -10.485 1.00 61.35 ? 268 GLU   A CG  1 
ATOM   1177 C  CD  . GLU   A 1 154 ? -35.547 10.092  -9.156  1.00 67.87 ? 268 GLU   A CD  1 
ATOM   1178 O  OE1 . GLU   A 1 154 ? -35.065 9.026   -8.722  1.00 68.71 ? 268 GLU   A OE1 1 
ATOM   1179 O  OE2 . GLU   A 1 154 ? -36.425 10.741  -8.547  1.00 72.39 ? 268 GLU   A OE2 1 
ATOM   1180 N  N   . GLU   A 1 155 ? -32.550 14.021  -10.256 1.00 48.21 ? 269 GLU   A N   1 
ATOM   1181 C  CA  . GLU   A 1 155 ? -32.109 15.375  -9.969  1.00 50.41 ? 269 GLU   A CA  1 
ATOM   1182 C  C   . GLU   A 1 155 ? -30.599 15.493  -10.148 1.00 45.49 ? 269 GLU   A C   1 
ATOM   1183 O  O   . GLU   A 1 155 ? -29.876 14.501  -10.263 1.00 44.71 ? 269 GLU   A O   1 
ATOM   1184 C  CB  . GLU   A 1 155 ? -32.499 15.770  -8.544  1.00 51.89 ? 269 GLU   A CB  1 
ATOM   1185 C  CG  . GLU   A 1 155 ? -33.959 15.536  -8.207  1.00 56.58 ? 269 GLU   A CG  1 
ATOM   1186 C  CD  . GLU   A 1 155 ? -34.427 16.355  -7.013  1.00 61.66 ? 269 GLU   A CD  1 
ATOM   1187 O  OE1 . GLU   A 1 155 ? -33.721 17.312  -6.622  1.00 61.21 ? 269 GLU   A OE1 1 
ATOM   1188 O  OE2 . GLU   A 1 155 ? -35.509 16.038  -6.469  1.00 64.19 ? 269 GLU   A OE2 1 
ATOM   1189 N  N   . ILE   A 1 156 ? -30.120 16.737  -10.165 1.00 46.31 ? 270 ILE   A N   1 
ATOM   1190 C  CA  . ILE   A 1 156 ? -28.685 16.973  -10.108 1.00 45.53 ? 270 ILE   A CA  1 
ATOM   1191 C  C   . ILE   A 1 156 ? -28.161 16.457  -8.778  1.00 42.32 ? 270 ILE   A C   1 
ATOM   1192 O  O   . ILE   A 1 156 ? -28.669 16.816  -7.709  1.00 42.25 ? 270 ILE   A O   1 
ATOM   1193 C  CB  . ILE   A 1 156 ? -28.379 18.466  -10.299 1.00 44.12 ? 270 ILE   A CB  1 
ATOM   1194 C  CG1 . ILE   A 1 156 ? -28.852 18.930  -11.678 1.00 46.87 ? 270 ILE   A CG1 1 
ATOM   1195 C  CG2 . ILE   A 1 156 ? -26.889 18.741  -10.112 1.00 39.92 ? 270 ILE   A CG2 1 
ATOM   1196 C  CD1 . ILE   A 1 156 ? -28.085 20.109  -12.216 1.00 45.18 ? 270 ILE   A CD1 1 
ATOM   1197 N  N   . ILE   A 1 157 ? -27.153 15.602  -8.834  1.00 43.61 ? 271 ILE   A N   1 
ATOM   1198 C  CA  . ILE   A 1 157 ? -26.591 14.992  -7.636  1.00 39.79 ? 271 ILE   A CA  1 
ATOM   1199 C  C   . ILE   A 1 157 ? -25.297 15.702  -7.268  1.00 39.46 ? 271 ILE   A C   1 
ATOM   1200 O  O   . ILE   A 1 157 ? -24.473 16.013  -8.140  1.00 37.42 ? 271 ILE   A O   1 
ATOM   1201 C  CB  . ILE   A 1 157 ? -26.358 13.484  -7.839  1.00 40.11 ? 271 ILE   A CB  1 
ATOM   1202 C  CG1 . ILE   A 1 157 ? -27.633 12.814  -8.364  1.00 40.38 ? 271 ILE   A CG1 1 
ATOM   1203 C  CG2 . ILE   A 1 157 ? -25.908 12.841  -6.535  1.00 41.64 ? 271 ILE   A CG2 1 
ATOM   1204 C  CD1 . ILE   A 1 157 ? -28.869 13.135  -7.546  1.00 43.04 ? 271 ILE   A CD1 1 
ATOM   1205 N  N   . ILE   A 1 158 ? -25.124 15.971  -5.975  1.00 39.85 ? 272 ILE   A N   1 
ATOM   1206 C  CA  . ILE   A 1 158 ? -23.886 16.527  -5.434  1.00 40.12 ? 272 ILE   A CA  1 
ATOM   1207 C  C   . ILE   A 1 158 ? -23.097 15.381  -4.814  1.00 42.09 ? 272 ILE   A C   1 
ATOM   1208 O  O   . ILE   A 1 158 ? -23.610 14.671  -3.940  1.00 44.66 ? 272 ILE   A O   1 
ATOM   1209 C  CB  . ILE   A 1 158 ? -24.166 17.626  -4.395  1.00 44.00 ? 272 ILE   A CB  1 
ATOM   1210 C  CG1 . ILE   A 1 158 ? -24.937 18.789  -5.027  1.00 44.96 ? 272 ILE   A CG1 1 
ATOM   1211 C  CG2 . ILE   A 1 158 ? -22.864 18.119  -3.759  1.00 43.68 ? 272 ILE   A CG2 1 
ATOM   1212 C  CD1 . ILE   A 1 158 ? -24.368 19.283  -6.351  1.00 41.43 ? 272 ILE   A CD1 1 
ATOM   1213 N  N   . ARG   A 1 159 ? -21.849 15.200  -5.247  1.00 35.73 ? 273 ARG   A N   1 
ATOM   1214 C  CA  . ARG   A 1 159 ? -21.010 14.107  -4.767  1.00 37.78 ? 273 ARG   A CA  1 
ATOM   1215 C  C   . ARG   A 1 159 ? -19.758 14.662  -4.098  1.00 38.63 ? 273 ARG   A C   1 
ATOM   1216 O  O   . ARG   A 1 159 ? -19.055 15.495  -4.679  1.00 38.35 ? 273 ARG   A O   1 
ATOM   1217 C  CB  . ARG   A 1 159 ? -20.621 13.166  -5.911  1.00 35.79 ? 273 ARG   A CB  1 
ATOM   1218 C  CG  . ARG   A 1 159 ? -21.783 12.717  -6.788  1.00 34.60 ? 273 ARG   A CG  1 
ATOM   1219 C  CD  . ARG   A 1 159 ? -21.380 11.550  -7.673  1.00 37.55 ? 273 ARG   A CD  1 
ATOM   1220 N  NE  . ARG   A 1 159 ? -22.424 11.220  -8.634  1.00 38.42 ? 273 ARG   A NE  1 
ATOM   1221 C  CZ  . ARG   A 1 159 ? -23.492 10.494  -8.341  1.00 37.42 ? 273 ARG   A CZ  1 
ATOM   1222 N  NH1 . ARG   A 1 159 ? -23.680 10.004  -7.127  1.00 38.92 ? 273 ARG   A NH1 1 
ATOM   1223 N  NH2 . ARG   A 1 159 ? -24.403 10.271  -9.282  1.00 35.77 ? 273 ARG   A NH2 1 
ATOM   1224 N  N   . SER   A 1 160 ? -19.480 14.193  -2.882  1.00 38.50 ? 274 SER   A N   1 
ATOM   1225 C  CA  . SER   A 1 160 ? -18.304 14.618  -2.131  1.00 39.55 ? 274 SER   A CA  1 
ATOM   1226 C  C   . SER   A 1 160 ? -18.068 13.638  -0.991  1.00 38.95 ? 274 SER   A C   1 
ATOM   1227 O  O   . SER   A 1 160 ? -19.020 13.150  -0.378  1.00 38.57 ? 274 SER   A O   1 
ATOM   1228 C  CB  . SER   A 1 160 ? -18.464 16.040  -1.576  1.00 41.64 ? 274 SER   A CB  1 
ATOM   1229 O  OG  . SER   A 1 160 ? -17.436 16.354  -0.640  1.00 42.20 ? 274 SER   A OG  1 
ATOM   1230 N  N   . GLU   A 1 161 ? -16.793 13.353  -0.718  1.00 37.65 ? 275 GLU   A N   1 
ATOM   1231 C  CA  . GLU   A 1 161 ? -16.450 12.492  0.409   1.00 37.42 ? 275 GLU   A CA  1 
ATOM   1232 C  C   . GLU   A 1 161 ? -16.885 13.106  1.734   1.00 42.22 ? 275 GLU   A C   1 
ATOM   1233 O  O   . GLU   A 1 161 ? -17.132 12.384  2.707   1.00 39.59 ? 275 GLU   A O   1 
ATOM   1234 C  CB  . GLU   A 1 161 ? -14.947 12.230  0.417   1.00 38.94 ? 275 GLU   A CB  1 
ATOM   1235 C  CG  . GLU   A 1 161 ? -14.524 11.130  1.357   1.00 39.16 ? 275 GLU   A CG  1 
ATOM   1236 C  CD  . GLU   A 1 161 ? -13.041 10.814  1.261   1.00 41.66 ? 275 GLU   A CD  1 
ATOM   1237 O  OE1 . GLU   A 1 161 ? -12.273 11.670  0.764   1.00 47.28 ? 275 GLU   A OE1 1 
ATOM   1238 O  OE2 . GLU   A 1 161 ? -12.645 9.708   1.690   1.00 47.28 ? 275 GLU   A OE2 1 
ATOM   1239 N  N   . ASN   A 1 162 ? -16.987 14.430  1.786   1.00 43.86 ? 276 ASN   A N   1 
ATOM   1240 C  CA  . ASN   A 1 162 ? -17.356 15.144  2.999   1.00 42.85 ? 276 ASN   A CA  1 
ATOM   1241 C  C   . ASN   A 1 162 ? -17.599 16.608  2.644   1.00 43.49 ? 276 ASN   A C   1 
ATOM   1242 O  O   . ASN   A 1 162 ? -16.661 17.410  2.577   1.00 41.64 ? 276 ASN   A O   1 
ATOM   1243 C  CB  . ASN   A 1 162 ? -16.267 14.984  4.066   1.00 47.88 ? 276 ASN   A CB  1 
ATOM   1244 C  CG  . ASN   A 1 162 ? -16.555 15.780  5.324   1.00 47.31 ? 276 ASN   A CG  1 
ATOM   1245 O  OD1 . ASN   A 1 162 ? -17.626 16.366  5.465   1.00 49.74 ? 276 ASN   A OD1 1 
ATOM   1246 N  ND2 . ASN   A 1 162 ? -15.592 15.803  6.246   1.00 52.16 ? 276 ASN   A ND2 1 
ATOM   1247 N  N   . LEU   A 1 163 ? -18.865 16.955  2.399   1.00 40.32 ? 277 LEU   A N   1 
ATOM   1248 C  CA  . LEU   A 1 163 ? -19.203 18.300  1.942   1.00 45.13 ? 277 LEU   A CA  1 
ATOM   1249 C  C   . LEU   A 1 163 ? -18.717 19.368  2.910   1.00 47.80 ? 277 LEU   A C   1 
ATOM   1250 O  O   . LEU   A 1 163 ? -18.432 20.500  2.497   1.00 46.70 ? 277 LEU   A O   1 
ATOM   1251 C  CB  . LEU   A 1 163 ? -20.716 18.414  1.754   1.00 48.69 ? 277 LEU   A CB  1 
ATOM   1252 C  CG  . LEU   A 1 163 ? -21.304 18.208  0.359   1.00 50.79 ? 277 LEU   A CG  1 
ATOM   1253 C  CD1 . LEU   A 1 163 ? -22.770 18.627  0.334   1.00 49.21 ? 277 LEU   A CD1 1 
ATOM   1254 C  CD2 . LEU   A 1 163 ? -20.502 18.973  -0.696  1.00 46.68 ? 277 LEU   A CD2 1 
ATOM   1255 N  N   . THR   A 1 164 ? -18.630 19.032  4.200   1.00 47.42 ? 278 THR   A N   1 
ATOM   1256 C  CA  . THR   A 1 164 ? -18.248 19.999  5.223   1.00 49.17 ? 278 THR   A CA  1 
ATOM   1257 C  C   . THR   A 1 164 ? -16.766 20.355  5.164   1.00 47.69 ? 278 THR   A C   1 
ATOM   1258 O  O   . THR   A 1 164 ? -16.375 21.420  5.653   1.00 47.35 ? 278 THR   A O   1 
ATOM   1259 C  CB  . THR   A 1 164 ? -18.597 19.453  6.613   1.00 49.74 ? 278 THR   A CB  1 
ATOM   1260 O  OG1 . THR   A 1 164 ? -20.004 19.590  6.847   1.00 54.76 ? 278 THR   A OG1 1 
ATOM   1261 C  CG2 . THR   A 1 164 ? -17.840 20.211  7.695   1.00 55.36 ? 278 THR   A CG2 1 
ATOM   1262 N  N   . ASN   A 1 165 ? -15.939 19.490  4.588   1.00 46.71 ? 279 ASN   A N   1 
ATOM   1263 C  CA  . ASN   A 1 165 ? -14.511 19.733  4.434   1.00 46.73 ? 279 ASN   A CA  1 
ATOM   1264 C  C   . ASN   A 1 165 ? -14.263 20.336  3.054   1.00 46.01 ? 279 ASN   A C   1 
ATOM   1265 O  O   . ASN   A 1 165 ? -14.502 19.680  2.033   1.00 46.03 ? 279 ASN   A O   1 
ATOM   1266 C  CB  . ASN   A 1 165 ? -13.730 18.430  4.618   1.00 44.94 ? 279 ASN   A CB  1 
ATOM   1267 C  CG  . ASN   A 1 165 ? -12.240 18.597  4.380   1.00 45.73 ? 279 ASN   A CG  1 
ATOM   1268 O  OD1 . ASN   A 1 165 ? -11.781 19.651  3.935   1.00 49.05 ? 279 ASN   A OD1 1 
ATOM   1269 N  ND2 . ASN   A 1 165 ? -11.477 17.549  4.670   1.00 44.33 ? 279 ASN   A ND2 1 
ATOM   1270 N  N   . ASN   A 1 166 ? -13.778 21.578  3.023   1.00 45.77 ? 280 ASN   A N   1 
ATOM   1271 C  CA  . ASN   A 1 166 ? -13.582 22.290  1.763   1.00 48.70 ? 280 ASN   A CA  1 
ATOM   1272 C  C   . ASN   A 1 166 ? -12.397 21.776  0.954   1.00 45.11 ? 280 ASN   A C   1 
ATOM   1273 O  O   . ASN   A 1 166 ? -12.239 22.179  -0.203  1.00 45.85 ? 280 ASN   A O   1 
ATOM   1274 C  CB  . ASN   A 1 166 ? -13.416 23.794  2.019   1.00 46.77 ? 280 ASN   A CB  1 
ATOM   1275 C  CG  . ASN   A 1 166 ? -12.161 24.124  2.799   1.00 46.36 ? 280 ASN   A CG  1 
ATOM   1276 O  OD1 . ASN   A 1 166 ? -12.073 23.847  3.991   1.00 50.27 ? 280 ASN   A OD1 1 
ATOM   1277 N  ND2 . ASN   A 1 166 ? -11.190 24.741  2.133   1.00 50.84 ? 280 ASN   A ND2 1 
ATOM   1278 N  N   . ALA   A 1 167 ? -11.566 20.903  1.521   1.00 48.06 ? 281 ALA   A N   1 
ATOM   1279 C  CA  . ALA   A 1 167 ? -10.472 20.301  0.768   1.00 48.05 ? 281 ALA   A CA  1 
ATOM   1280 C  C   . ALA   A 1 167 ? -10.911 19.105  -0.070  1.00 46.42 ? 281 ALA   A C   1 
ATOM   1281 O  O   . ALA   A 1 167 ? -10.102 18.579  -0.841  1.00 47.94 ? 281 ALA   A O   1 
ATOM   1282 C  CB  . ALA   A 1 167 ? -9.346  19.880  1.718   1.00 48.59 ? 281 ALA   A CB  1 
ATOM   1283 N  N   . LYS   A 1 168 ? -12.164 18.677  0.052   1.00 45.24 ? 282 LYS   A N   1 
ATOM   1284 C  CA  . LYS   A 1 168 ? -12.691 17.528  -0.672  1.00 43.53 ? 282 LYS   A CA  1 
ATOM   1285 C  C   . LYS   A 1 168 ? -13.380 17.990  -1.952  1.00 44.05 ? 282 LYS   A C   1 
ATOM   1286 O  O   . LYS   A 1 168 ? -14.287 18.828  -1.905  1.00 44.83 ? 282 LYS   A O   1 
ATOM   1287 C  CB  . LYS   A 1 168 ? -13.679 16.755  0.203   1.00 44.36 ? 282 LYS   A CB  1 
ATOM   1288 C  CG  . LYS   A 1 168 ? -13.045 15.965  1.337   1.00 42.91 ? 282 LYS   A CG  1 
ATOM   1289 C  CD  . LYS   A 1 168 ? -11.970 15.017  0.824   1.00 45.51 ? 282 LYS   A CD  1 
ATOM   1290 C  CE  . LYS   A 1 168 ? -10.980 14.660  1.923   1.00 47.97 ? 282 LYS   A CE  1 
ATOM   1291 N  NZ  . LYS   A 1 168 ? -10.917 13.180  2.137   1.00 43.83 ? 282 LYS   A NZ  1 
ATOM   1292 N  N   . THR   A 1 169 ? -12.956 17.436  -3.090  1.00 42.75 ? 283 THR   A N   1 
ATOM   1293 C  CA  . THR   A 1 169 ? -13.530 17.823  -4.373  1.00 41.75 ? 283 THR   A CA  1 
ATOM   1294 C  C   . THR   A 1 169 ? -15.008 17.461  -4.423  1.00 40.88 ? 283 THR   A C   1 
ATOM   1295 O  O   . THR   A 1 169 ? -15.433 16.427  -3.897  1.00 41.68 ? 283 THR   A O   1 
ATOM   1296 C  CB  . THR   A 1 169 ? -12.791 17.132  -5.527  1.00 45.98 ? 283 THR   A CB  1 
ATOM   1297 O  OG1 . THR   A 1 169 ? -11.376 17.292  -5.364  1.00 44.95 ? 283 THR   A OG1 1 
ATOM   1298 C  CG2 . THR   A 1 169 ? -13.224 17.705  -6.893  1.00 36.69 ? 283 THR   A CG2 1 
ATOM   1299 N  N   . ILE   A 1 170 ? -15.793 18.318  -5.061  1.00 36.72 ? 284 ILE   A N   1 
ATOM   1300 C  CA  . ILE   A 1 170 ? -17.205 18.055  -5.289  1.00 36.23 ? 284 ILE   A CA  1 
ATOM   1301 C  C   . ILE   A 1 170 ? -17.383 17.670  -6.747  1.00 36.43 ? 284 ILE   A C   1 
ATOM   1302 O  O   . ILE   A 1 170 ? -16.827 18.322  -7.639  1.00 35.58 ? 284 ILE   A O   1 
ATOM   1303 C  CB  . ILE   A 1 170 ? -18.070 19.276  -4.939  1.00 37.38 ? 284 ILE   A CB  1 
ATOM   1304 C  CG1 . ILE   A 1 170 ? -18.034 19.567  -3.430  1.00 37.76 ? 284 ILE   A CG1 1 
ATOM   1305 C  CG2 . ILE   A 1 170 ? -19.491 19.056  -5.425  1.00 37.39 ? 284 ILE   A CG2 1 
ATOM   1306 C  CD1 . ILE   A 1 170 ? -18.567 20.945  -3.062  1.00 36.64 ? 284 ILE   A CD1 1 
ATOM   1307 N  N   . ILE   A 1 171 ? -18.135 16.606  -6.993  1.00 34.41 ? 285 ILE   A N   1 
ATOM   1308 C  CA  . ILE   A 1 171 ? -18.539 16.232  -8.341  1.00 34.87 ? 285 ILE   A CA  1 
ATOM   1309 C  C   . ILE   A 1 171 ? -20.012 16.591  -8.487  1.00 36.54 ? 285 ILE   A C   1 
ATOM   1310 O  O   . ILE   A 1 171 ? -20.860 16.094  -7.735  1.00 36.31 ? 285 ILE   A O   1 
ATOM   1311 C  CB  . ILE   A 1 171 ? -18.295 14.739  -8.615  1.00 33.32 ? 285 ILE   A CB  1 
ATOM   1312 C  CG1 . ILE   A 1 171 ? -16.797 14.420  -8.635  1.00 34.48 ? 285 ILE   A CG1 1 
ATOM   1313 C  CG2 . ILE   A 1 171 ? -18.938 14.321  -9.936  1.00 34.46 ? 285 ILE   A CG2 1 
ATOM   1314 C  CD1 . ILE   A 1 171 ? -16.496 12.929  -8.671  1.00 36.28 ? 285 ILE   A CD1 1 
ATOM   1315 N  N   . VAL   A 1 172 ? -20.314 17.482  -9.422  1.00 32.35 ? 286 VAL   A N   1 
ATOM   1316 C  CA  . VAL   A 1 172 ? -21.692 17.782  -9.789  1.00 34.35 ? 286 VAL   A CA  1 
ATOM   1317 C  C   . VAL   A 1 172 ? -22.075 16.848  -10.931 1.00 36.64 ? 286 VAL   A C   1 
ATOM   1318 O  O   . VAL   A 1 172 ? -21.414 16.827  -11.974 1.00 34.45 ? 286 VAL   A O   1 
ATOM   1319 C  CB  . VAL   A 1 172 ? -21.858 19.256  -10.193 1.00 36.02 ? 286 VAL   A CB  1 
ATOM   1320 C  CG1 . VAL   A 1 172 ? -23.242 19.500  -10.767 1.00 36.85 ? 286 VAL   A CG1 1 
ATOM   1321 C  CG2 . VAL   A 1 172 ? -21.609 20.168  -8.999  1.00 35.72 ? 286 VAL   A CG2 1 
ATOM   1322 N  N   . HIS   A 1 173 ? -23.121 16.053  -10.723 1.00 37.16 ? 287 HIS   A N   1 
ATOM   1323 C  CA  . HIS   A 1 173 ? -23.624 15.137  -11.739 1.00 35.08 ? 287 HIS   A CA  1 
ATOM   1324 C  C   . HIS   A 1 173 ? -24.884 15.745  -12.344 1.00 39.41 ? 287 HIS   A C   1 
ATOM   1325 O  O   . HIS   A 1 173 ? -25.932 15.793  -11.692 1.00 41.23 ? 287 HIS   A O   1 
ATOM   1326 C  CB  . HIS   A 1 173 ? -23.908 13.760  -11.145 1.00 36.44 ? 287 HIS   A CB  1 
ATOM   1327 C  CG  . HIS   A 1 173 ? -23.934 12.658  -12.161 1.00 37.72 ? 287 HIS   A CG  1 
ATOM   1328 N  ND1 . HIS   A 1 173 ? -24.058 11.328  -11.819 1.00 40.54 ? 287 HIS   A ND1 1 
ATOM   1329 C  CD2 . HIS   A 1 173 ? -23.843 12.690  -13.512 1.00 39.05 ? 287 HIS   A CD2 1 
ATOM   1330 C  CE1 . HIS   A 1 173 ? -24.038 10.589  -12.915 1.00 42.42 ? 287 HIS   A CE1 1 
ATOM   1331 N  NE2 . HIS   A 1 173 ? -23.911 11.392  -13.956 1.00 39.78 ? 287 HIS   A NE2 1 
ATOM   1332 N  N   . LEU   A 1 174 ? -24.784 16.202  -13.589 1.00 40.07 ? 288 LEU   A N   1 
ATOM   1333 C  CA  . LEU   A 1 174 ? -25.927 16.820  -14.243 1.00 38.81 ? 288 LEU   A CA  1 
ATOM   1334 C  C   . LEU   A 1 174 ? -26.945 15.763  -14.653 1.00 43.64 ? 288 LEU   A C   1 
ATOM   1335 O  O   . LEU   A 1 174 ? -26.610 14.594  -14.864 1.00 42.18 ? 288 LEU   A O   1 
ATOM   1336 C  CB  . LEU   A 1 174 ? -25.473 17.613  -15.468 1.00 38.80 ? 288 LEU   A CB  1 
ATOM   1337 C  CG  . LEU   A 1 174 ? -24.510 18.773  -15.193 1.00 38.35 ? 288 LEU   A CG  1 
ATOM   1338 C  CD1 . LEU   A 1 174 ? -24.169 19.514  -16.486 1.00 36.89 ? 288 LEU   A CD1 1 
ATOM   1339 C  CD2 . LEU   A 1 174 ? -25.098 19.719  -14.158 1.00 36.54 ? 288 LEU   A CD2 1 
ATOM   1340 N  N   . ASN   A 1 175 ? -28.207 16.183  -14.749 1.00 42.46 ? 289 ASN   A N   1 
ATOM   1341 C  CA  . ASN   A 1 175 ? -29.263 15.350  -15.308 1.00 46.63 ? 289 ASN   A CA  1 
ATOM   1342 C  C   . ASN   A 1 175 ? -29.629 15.747  -16.734 1.00 44.98 ? 289 ASN   A C   1 
ATOM   1343 O  O   . ASN   A 1 175 ? -30.452 15.073  -17.360 1.00 45.80 ? 289 ASN   A O   1 
ATOM   1344 C  CB  . ASN   A 1 175 ? -30.512 15.390  -14.416 1.00 45.05 ? 289 ASN   A CB  1 
ATOM   1345 C  CG  . ASN   A 1 175 ? -31.036 16.797  -14.193 1.00 46.89 ? 289 ASN   A CG  1 
ATOM   1346 O  OD1 . ASN   A 1 175 ? -30.557 17.764  -14.781 1.00 45.83 ? 289 ASN   A OD1 1 
ATOM   1347 N  ND2 . ASN   A 1 175 ? -32.031 16.910  -13.328 1.00 53.08 ? 289 ASN   A ND2 1 
ATOM   1348 N  N   . LYS   A 1 176 ? -29.035 16.817  -17.258 1.00 44.20 ? 290 LYS   A N   1 
ATOM   1349 C  CA  . LYS   A 1 176 ? -29.245 17.260  -18.630 1.00 45.35 ? 290 LYS   A CA  1 
ATOM   1350 C  C   . LYS   A 1 176 ? -27.898 17.688  -19.193 1.00 44.00 ? 290 LYS   A C   1 
ATOM   1351 O  O   . LYS   A 1 176 ? -27.209 18.516  -18.592 1.00 45.56 ? 290 LYS   A O   1 
ATOM   1352 C  CB  . LYS   A 1 176 ? -30.248 18.423  -18.695 1.00 47.42 ? 290 LYS   A CB  1 
ATOM   1353 C  CG  . LYS   A 1 176 ? -31.254 18.370  -19.857 1.00 50.27 ? 290 LYS   A CG  1 
ATOM   1354 C  CD  . LYS   A 1 176 ? -31.780 16.957  -20.111 1.00 56.08 ? 290 LYS   A CD  1 
ATOM   1355 C  CE  . LYS   A 1 176 ? -33.082 16.983  -20.916 1.00 61.78 ? 290 LYS   A CE  1 
ATOM   1356 N  NZ  . LYS   A 1 176 ? -32.870 17.337  -22.355 1.00 62.12 ? 290 LYS   A NZ  1 
ATOM   1357 N  N   . SER   A 1 177 ? -27.520 17.130  -20.336 1.00 45.83 ? 291 SER   A N   1 
ATOM   1358 C  CA  . SER   A 1 177 ? -26.202 17.425  -20.877 1.00 46.32 ? 291 SER   A CA  1 
ATOM   1359 C  C   . SER   A 1 177 ? -26.193 18.778  -21.576 1.00 43.46 ? 291 SER   A C   1 
ATOM   1360 O  O   . SER   A 1 177 ? -27.218 19.254  -22.071 1.00 47.28 ? 291 SER   A O   1 
ATOM   1361 C  CB  . SER   A 1 177 ? -25.764 16.336  -21.850 1.00 43.53 ? 291 SER   A CB  1 
ATOM   1362 O  OG  . SER   A 1 177 ? -26.374 16.537  -23.107 1.00 52.71 ? 291 SER   A OG  1 
ATOM   1363 N  N   . VAL   A 1 178 ? -25.017 19.402  -21.607 1.00 39.95 ? 292 VAL   A N   1 
ATOM   1364 C  CA  . VAL   A 1 178 ? -24.819 20.680  -22.282 1.00 42.09 ? 292 VAL   A CA  1 
ATOM   1365 C  C   . VAL   A 1 178 ? -23.742 20.487  -23.340 1.00 41.72 ? 292 VAL   A C   1 
ATOM   1366 O  O   . VAL   A 1 178 ? -22.605 20.116  -23.020 1.00 40.06 ? 292 VAL   A O   1 
ATOM   1367 C  CB  . VAL   A 1 178 ? -24.438 21.799  -21.299 1.00 40.30 ? 292 VAL   A CB  1 
ATOM   1368 C  CG1 . VAL   A 1 178 ? -23.989 23.053  -22.059 1.00 41.82 ? 292 VAL   A CG1 1 
ATOM   1369 C  CG2 . VAL   A 1 178 ? -25.607 22.111  -20.376 1.00 40.82 ? 292 VAL   A CG2 1 
ATOM   1370 N  N   . GLU   A 1 179 ? -24.103 20.723  -24.596 1.00 40.58 ? 293 GLU   A N   1 
ATOM   1371 C  CA  . GLU   A 1 179 ? -23.169 20.517  -25.692 1.00 43.42 ? 293 GLU   A CA  1 
ATOM   1372 C  C   . GLU   A 1 179 ? -22.072 21.575  -25.671 1.00 38.58 ? 293 GLU   A C   1 
ATOM   1373 O  O   . GLU   A 1 179 ? -22.330 22.754  -25.413 1.00 37.72 ? 293 GLU   A O   1 
ATOM   1374 C  CB  . GLU   A 1 179 ? -23.909 20.556  -27.029 1.00 47.46 ? 293 GLU   A CB  1 
ATOM   1375 C  CG  . GLU   A 1 179 ? -23.377 19.580  -28.067 1.00 54.12 ? 293 GLU   A CG  1 
ATOM   1376 C  CD  . GLU   A 1 179 ? -24.333 19.405  -29.240 1.00 64.00 ? 293 GLU   A CD  1 
ATOM   1377 O  OE1 . GLU   A 1 179 ? -24.972 20.402  -29.641 1.00 66.57 ? 293 GLU   A OE1 1 
ATOM   1378 O  OE2 . GLU   A 1 179 ? -24.442 18.273  -29.759 1.00 68.51 ? 293 GLU   A OE2 1 
ATOM   1379 N  N   . ILE   A 1 180 ? -20.839 21.144  -25.931 1.00 35.35 ? 294 ILE   A N   1 
ATOM   1380 C  CA  . ILE   A 1 180 ? -19.699 22.041  -26.090 1.00 35.92 ? 294 ILE   A CA  1 
ATOM   1381 C  C   . ILE   A 1 180 ? -18.990 21.661  -27.384 1.00 41.38 ? 294 ILE   A C   1 
ATOM   1382 O  O   . ILE   A 1 180 ? -18.496 20.536  -27.521 1.00 38.19 ? 294 ILE   A O   1 
ATOM   1383 C  CB  . ILE   A 1 180 ? -18.735 21.981  -24.892 1.00 41.64 ? 294 ILE   A CB  1 
ATOM   1384 C  CG1 . ILE   A 1 180 ? -17.582 22.972  -25.078 1.00 40.40 ? 294 ILE   A CG1 1 
ATOM   1385 C  CG2 . ILE   A 1 180 ? -18.206 20.562  -24.687 1.00 40.28 ? 294 ILE   A CG2 1 
ATOM   1386 C  CD1 . ILE   A 1 180 ? -16.479 22.820  -24.048 1.00 46.91 ? 294 ILE   A CD1 1 
ATOM   1387 N  N   . ASN   A 1 181 ? -18.942 22.594  -28.329 1.00 39.60 ? 295 ASN   A N   1 
ATOM   1388 C  CA  . ASN   A 1 181 ? -18.478 22.327  -29.686 1.00 42.69 ? 295 ASN   A CA  1 
ATOM   1389 C  C   . ASN   A 1 181 ? -17.206 23.134  -29.928 1.00 42.25 ? 295 ASN   A C   1 
ATOM   1390 O  O   . ASN   A 1 181 ? -17.247 24.367  -29.986 1.00 42.29 ? 295 ASN   A O   1 
ATOM   1391 C  CB  . ASN   A 1 181 ? -19.591 22.667  -30.679 1.00 43.97 ? 295 ASN   A CB  1 
ATOM   1392 C  CG  . ASN   A 1 181 ? -19.131 22.661  -32.118 1.00 46.03 ? 295 ASN   A CG  1 
ATOM   1393 O  OD1 . ASN   A 1 181 ? -18.023 22.234  -32.437 1.00 44.58 ? 295 ASN   A OD1 1 
ATOM   1394 N  ND2 . ASN   A 1 181 ? -19.999 23.136  -33.005 1.00 53.31 ? 295 ASN   A ND2 1 
ATOM   1395 N  N   . CYS   A 1 182 ? -16.081 22.435  -30.070 1.00 42.17 ? 296 CYS   A N   1 
ATOM   1396 C  CA  . CYS   A 1 182 ? -14.759 23.047  -30.102 1.00 42.75 ? 296 CYS   A CA  1 
ATOM   1397 C  C   . CYS   A 1 182 ? -14.114 22.839  -31.467 1.00 44.60 ? 296 CYS   A C   1 
ATOM   1398 O  O   . CYS   A 1 182 ? -14.132 21.725  -32.004 1.00 44.03 ? 296 CYS   A O   1 
ATOM   1399 C  CB  . CYS   A 1 182 ? -13.871 22.457  -29.006 1.00 44.34 ? 296 CYS   A CB  1 
ATOM   1400 S  SG  . CYS   A 1 182 ? -14.542 22.689  -27.336 1.00 52.28 ? 296 CYS   A SG  1 
ATOM   1401 N  N   . THR   A 1 183 ? -13.529 23.904  -32.015 1.00 40.95 ? 297 THR   A N   1 
ATOM   1402 C  CA  . THR   A 1 183 ? -12.973 23.860  -33.358 1.00 44.17 ? 297 THR   A CA  1 
ATOM   1403 C  C   . THR   A 1 183 ? -11.648 24.602  -33.428 1.00 42.37 ? 297 THR   A C   1 
ATOM   1404 O  O   . THR   A 1 183 ? -11.485 25.676  -32.841 1.00 41.52 ? 297 THR   A O   1 
ATOM   1405 C  CB  . THR   A 1 183 ? -13.942 24.462  -34.382 1.00 45.32 ? 297 THR   A CB  1 
ATOM   1406 O  OG1 . THR   A 1 183 ? -15.230 23.853  -34.241 1.00 45.78 ? 297 THR   A OG1 1 
ATOM   1407 C  CG2 . THR   A 1 183 ? -13.428 24.237  -35.798 1.00 47.27 ? 297 THR   A CG2 1 
ATOM   1408 N  N   . ARG   A 1 184 ? -10.705 24.004  -34.151 1.00 43.33 ? 298 ARG   A N   1 
ATOM   1409 C  CA  . ARG   A 1 184 ? -9.505  24.678  -34.633 1.00 41.64 ? 298 ARG   A CA  1 
ATOM   1410 C  C   . ARG   A 1 184 ? -9.633  24.766  -36.150 1.00 44.13 ? 298 ARG   A C   1 
ATOM   1411 O  O   . ARG   A 1 184 ? -9.298  23.803  -36.857 1.00 45.05 ? 298 ARG   A O   1 
ATOM   1412 C  CB  . ARG   A 1 184 ? -8.240  23.907  -34.234 1.00 41.35 ? 298 ARG   A CB  1 
ATOM   1413 C  CG  . ARG   A 1 184 ? -6.916  24.654  -34.417 1.00 39.54 ? 298 ARG   A CG  1 
ATOM   1414 C  CD  . ARG   A 1 184 ? -6.663  25.068  -35.863 1.00 41.79 ? 298 ARG   A CD  1 
ATOM   1415 N  NE  . ARG   A 1 184 ? -6.392  23.929  -36.731 1.00 38.03 ? 298 ARG   A NE  1 
ATOM   1416 C  CZ  . ARG   A 1 184 ? -5.189  23.406  -36.926 1.00 44.45 ? 298 ARG   A CZ  1 
ATOM   1417 N  NH1 . ARG   A 1 184 ? -4.119  23.883  -36.310 1.00 43.20 ? 298 ARG   A NH1 1 
ATOM   1418 N  NH2 . ARG   A 1 184 ? -5.056  22.379  -37.762 1.00 42.69 ? 298 ARG   A NH2 1 
ATOM   1419 N  N   . PRO   A 1 185 ? -10.122 25.878  -36.700 1.00 45.11 ? 299 PRO   A N   1 
ATOM   1420 C  CA  . PRO   A 1 185 ? -10.351 25.946  -38.148 1.00 46.85 ? 299 PRO   A CA  1 
ATOM   1421 C  C   . PRO   A 1 185 ? -9.065  25.745  -38.942 1.00 48.71 ? 299 PRO   A C   1 
ATOM   1422 O  O   . PRO   A 1 185 ? -7.954  25.974  -38.459 1.00 47.86 ? 299 PRO   A O   1 
ATOM   1423 C  CB  . PRO   A 1 185 ? -10.924 27.354  -38.353 1.00 46.58 ? 299 PRO   A CB  1 
ATOM   1424 C  CG  . PRO   A 1 185 ? -10.565 28.118  -37.112 1.00 47.53 ? 299 PRO   A CG  1 
ATOM   1425 C  CD  . PRO   A 1 185 ? -10.546 27.108  -36.010 1.00 45.47 ? 299 PRO   A CD  1 
ATOM   1426 N  N   . SER   A 1 186 ? -9.239  25.321  -40.192 1.00 51.18 ? 300 SER   A N   1 
ATOM   1427 C  CA  . SER   A 1 186 ? -8.131  24.888  -41.034 1.00 54.70 ? 300 SER   A CA  1 
ATOM   1428 C  C   . SER   A 1 186 ? -7.279  26.065  -41.513 1.00 59.27 ? 300 SER   A C   1 
ATOM   1429 O  O   . SER   A 1 186 ? -7.679  27.233  -41.463 1.00 60.11 ? 300 SER   A O   1 
ATOM   1430 C  CB  . SER   A 1 186 ? -8.656  24.109  -42.243 1.00 55.80 ? 300 SER   A CB  1 
ATOM   1431 O  OG  . SER   A 1 186 ? -9.884  24.651  -42.700 1.00 57.16 ? 300 SER   A OG  1 
ATOM   1432 N  N   . ASN   A 1 187 ? -6.085  25.725  -41.994 1.00 65.14 ? 301 ASN   A N   1 
ATOM   1433 C  CA  . ASN   A 1 187 ? -5.143  26.676  -42.576 1.00 65.77 ? 301 ASN   A CA  1 
ATOM   1434 C  C   . ASN   A 1 187 ? -4.922  27.885  -41.672 1.00 65.59 ? 301 ASN   A C   1 
ATOM   1435 O  O   . ASN   A 1 187 ? -3.911  28.580  -41.792 1.00 67.51 ? 301 ASN   A O   1 
ATOM   1436 C  CB  . ASN   A 1 187 ? -5.622  27.128  -43.960 1.00 65.53 ? 301 ASN   A CB  1 
ATOM   1437 C  CG  . ASN   A 1 187 ? -5.709  25.980  -44.956 1.00 69.89 ? 301 ASN   A CG  1 
ATOM   1438 O  OD1 . ASN   A 1 187 ? -6.788  25.445  -45.220 1.00 71.99 ? 301 ASN   A OD1 1 
ATOM   1439 N  ND2 . ASN   A 1 187 ? -4.564  25.598  -45.516 1.00 73.10 ? 301 ASN   A ND2 1 
ATOM   1440 N  N   . ASP   A 1 195 ? -2.865  31.910  -36.524 1.00 60.39 ? 325 ASP   A N   1 
ATOM   1441 C  CA  . ASP   A 1 195 ? -2.370  31.037  -35.462 1.00 51.33 ? 325 ASP   A CA  1 
ATOM   1442 C  C   . ASP   A 1 195 ? -2.967  29.644  -35.586 1.00 48.44 ? 325 ASP   A C   1 
ATOM   1443 O  O   . ASP   A 1 195 ? -4.174  29.467  -35.441 1.00 52.33 ? 325 ASP   A O   1 
ATOM   1444 C  CB  . ASP   A 1 195 ? -2.696  31.622  -34.085 1.00 52.24 ? 325 ASP   A CB  1 
ATOM   1445 C  CG  . ASP   A 1 195 ? -1.616  31.326  -33.049 1.00 56.55 ? 325 ASP   A CG  1 
ATOM   1446 O  OD1 . ASP   A 1 195 ? -1.275  30.138  -32.848 1.00 54.17 ? 325 ASP   A OD1 1 
ATOM   1447 O  OD2 . ASP   A 1 195 ? -1.111  32.290  -32.436 1.00 60.57 ? 325 ASP   A OD2 1 
ATOM   1448 N  N   . ILE   A 1 196 ? -2.114  28.653  -35.857 1.00 47.76 ? 326 ILE   A N   1 
ATOM   1449 C  CA  . ILE   A 1 196 ? -2.579  27.273  -35.933 1.00 49.67 ? 326 ILE   A CA  1 
ATOM   1450 C  C   . ILE   A 1 196 ? -2.986  26.732  -34.568 1.00 46.25 ? 326 ILE   A C   1 
ATOM   1451 O  O   . ILE   A 1 196 ? -3.684  25.713  -34.494 1.00 45.32 ? 326 ILE   A O   1 
ATOM   1452 C  CB  . ILE   A 1 196 ? -1.497  26.373  -36.556 1.00 48.48 ? 326 ILE   A CB  1 
ATOM   1453 C  CG1 . ILE   A 1 196 ? -0.125  26.722  -35.974 1.00 49.53 ? 326 ILE   A CG1 1 
ATOM   1454 C  CG2 . ILE   A 1 196 ? -1.499  26.499  -38.084 1.00 50.56 ? 326 ILE   A CG2 1 
ATOM   1455 C  CD1 . ILE   A 1 196 ? 0.862   25.557  -35.971 1.00 51.86 ? 326 ILE   A CD1 1 
ATOM   1456 N  N   . ARG   A 1 197 ? -2.573  27.386  -33.485 1.00 45.68 ? 327 ARG   A N   1 
ATOM   1457 C  CA  . ARG   A 1 197 ? -2.870  26.917  -32.141 1.00 43.82 ? 327 ARG   A CA  1 
ATOM   1458 C  C   . ARG   A 1 197 ? -4.128  27.544  -31.553 1.00 40.86 ? 327 ARG   A C   1 
ATOM   1459 O  O   . ARG   A 1 197 ? -4.562  27.127  -30.478 1.00 37.74 ? 327 ARG   A O   1 
ATOM   1460 C  CB  . ARG   A 1 197 ? -1.678  27.190  -31.223 1.00 41.51 ? 327 ARG   A CB  1 
ATOM   1461 C  CG  . ARG   A 1 197 ? -0.375  26.584  -31.719 1.00 45.46 ? 327 ARG   A CG  1 
ATOM   1462 C  CD  . ARG   A 1 197 ? 0.709   26.630  -30.653 1.00 45.53 ? 327 ARG   A CD  1 
ATOM   1463 N  NE  . ARG   A 1 197 ? 1.837   25.771  -30.993 1.00 46.71 ? 327 ARG   A NE  1 
ATOM   1464 C  CZ  . ARG   A 1 197 ? 2.693   26.016  -31.977 1.00 49.92 ? 327 ARG   A CZ  1 
ATOM   1465 N  NH1 . ARG   A 1 197 ? 2.568   27.083  -32.754 1.00 48.22 ? 327 ARG   A NH1 1 
ATOM   1466 N  NH2 . ARG   A 1 197 ? 3.694   25.168  -32.193 1.00 46.41 ? 327 ARG   A NH2 1 
ATOM   1467 N  N   . LYS   A 1 198 ? -4.728  28.526  -32.220 1.00 40.77 ? 328 LYS   A N   1 
ATOM   1468 C  CA  . LYS   A 1 198 ? -5.928  29.172  -31.701 1.00 42.65 ? 328 LYS   A CA  1 
ATOM   1469 C  C   . LYS   A 1 198 ? -7.173  28.371  -32.080 1.00 43.28 ? 328 LYS   A C   1 
ATOM   1470 O  O   . LYS   A 1 198 ? -7.310  27.907  -33.220 1.00 39.46 ? 328 LYS   A O   1 
ATOM   1471 C  CB  . LYS   A 1 198 ? -6.035  30.598  -32.236 1.00 45.76 ? 328 LYS   A CB  1 
ATOM   1472 C  CG  . LYS   A 1 198 ? -7.164  31.422  -31.637 1.00 47.01 ? 328 LYS   A CG  1 
ATOM   1473 C  CD  . LYS   A 1 198 ? -6.824  31.928  -30.251 1.00 49.07 ? 328 LYS   A CD  1 
ATOM   1474 C  CE  . LYS   A 1 198 ? -7.995  31.740  -29.276 1.00 46.04 ? 328 LYS   A CE  1 
ATOM   1475 N  NZ  . LYS   A 1 198 ? -9.253  32.417  -29.716 1.00 46.91 ? 328 LYS   A NZ  1 
ATOM   1476 N  N   . ALA   A 1 199 ? -8.077  28.206  -31.115 1.00 37.14 ? 329 ALA   A N   1 
ATOM   1477 C  CA  . ALA   A 1 199 ? -9.334  27.497  -31.322 1.00 40.62 ? 329 ALA   A CA  1 
ATOM   1478 C  C   . ALA   A 1 199 ? -10.414 28.224  -30.531 1.00 39.88 ? 329 ALA   A C   1 
ATOM   1479 O  O   . ALA   A 1 199 ? -10.167 29.271  -29.925 1.00 41.95 ? 329 ALA   A O   1 
ATOM   1480 C  CB  . ALA   A 1 199 ? -9.213  26.022  -30.914 1.00 39.69 ? 329 ALA   A CB  1 
ATOM   1481 N  N   . TYR   A 1 200 ? -11.623 27.672  -30.540 1.00 38.63 ? 330 TYR   A N   1 
ATOM   1482 C  CA  . TYR   A 1 200 ? -12.730 28.266  -29.807 1.00 42.86 ? 330 TYR   A CA  1 
ATOM   1483 C  C   . TYR   A 1 200 ? -13.770 27.185  -29.564 1.00 43.47 ? 330 TYR   A C   1 
ATOM   1484 O  O   . TYR   A 1 200 ? -13.975 26.318  -30.417 1.00 43.74 ? 330 TYR   A O   1 
ATOM   1485 C  CB  . TYR   A 1 200 ? -13.336 29.446  -30.578 1.00 43.07 ? 330 TYR   A CB  1 
ATOM   1486 C  CG  . TYR   A 1 200 ? -13.934 29.046  -31.904 1.00 45.53 ? 330 TYR   A CG  1 
ATOM   1487 C  CD1 . TYR   A 1 200 ? -13.157 28.998  -33.056 1.00 47.00 ? 330 TYR   A CD1 1 
ATOM   1488 C  CD2 . TYR   A 1 200 ? -15.275 28.700  -32.000 1.00 50.85 ? 330 TYR   A CD2 1 
ATOM   1489 C  CE1 . TYR   A 1 200 ? -13.704 28.620  -34.268 1.00 51.34 ? 330 TYR   A CE1 1 
ATOM   1490 C  CE2 . TYR   A 1 200 ? -15.830 28.322  -33.202 1.00 51.87 ? 330 TYR   A CE2 1 
ATOM   1491 C  CZ  . TYR   A 1 200 ? -15.043 28.283  -34.333 1.00 52.26 ? 330 TYR   A CZ  1 
ATOM   1492 O  OH  . TYR   A 1 200 ? -15.605 27.905  -35.532 1.00 57.53 ? 330 TYR   A OH  1 
ATOM   1493 N  N   . CYS   A 1 201 ? -14.409 27.229  -28.400 1.00 41.79 ? 331 CYS   A N   1 
ATOM   1494 C  CA  . CYS   A 1 201 ? -15.475 26.301  -28.054 1.00 42.60 ? 331 CYS   A CA  1 
ATOM   1495 C  C   . CYS   A 1 201 ? -16.789 27.063  -27.997 1.00 43.99 ? 331 CYS   A C   1 
ATOM   1496 O  O   . CYS   A 1 201 ? -16.871 28.117  -27.358 1.00 45.78 ? 331 CYS   A O   1 
ATOM   1497 C  CB  . CYS   A 1 201 ? -15.200 25.611  -26.717 1.00 46.27 ? 331 CYS   A CB  1 
ATOM   1498 S  SG  . CYS   A 1 201 ? -13.787 24.484  -26.740 1.00 62.33 ? 331 CYS   A SG  1 
ATOM   1499 N  N   . GLU   A 1 202 ? -17.802 26.537  -28.672 1.00 42.03 ? 332 GLU   A N   1 
ATOM   1500 C  CA  . GLU   A 1 202 ? -19.121 27.146  -28.711 1.00 44.01 ? 332 GLU   A CA  1 
ATOM   1501 C  C   . GLU   A 1 202 ? -20.038 26.426  -27.734 1.00 43.79 ? 332 GLU   A C   1 
ATOM   1502 O  O   . GLU   A 1 202 ? -20.139 25.194  -27.757 1.00 40.86 ? 332 GLU   A O   1 
ATOM   1503 C  CB  . GLU   A 1 202 ? -19.698 27.087  -30.124 1.00 44.47 ? 332 GLU   A CB  1 
ATOM   1504 C  CG  . GLU   A 1 202 ? -19.112 28.127  -31.061 1.00 53.57 ? 332 GLU   A CG  1 
ATOM   1505 C  CD  . GLU   A 1 202 ? -20.042 28.485  -32.205 1.00 58.39 ? 332 GLU   A CD  1 
ATOM   1506 O  OE1 . GLU   A 1 202 ? -20.810 27.605  -32.645 1.00 61.62 ? 332 GLU   A OE1 1 
ATOM   1507 O  OE2 . GLU   A 1 202 ? -19.995 29.648  -32.664 1.00 61.57 ? 332 GLU   A OE2 1 
ATOM   1508 N  N   . ILE   A 1 203 ? -20.696 27.193  -26.879 1.00 39.89 ? 333 ILE   A N   1 
ATOM   1509 C  CA  . ILE   A 1 203 ? -21.682 26.660  -25.955 1.00 42.74 ? 333 ILE   A CA  1 
ATOM   1510 C  C   . ILE   A 1 203 ? -22.925 27.532  -26.023 1.00 46.58 ? 333 ILE   A C   1 
ATOM   1511 O  O   . ILE   A 1 203 ? -22.833 28.763  -26.103 1.00 44.51 ? 333 ILE   A O   1 
ATOM   1512 C  CB  . ILE   A 1 203 ? -21.141 26.592  -24.514 1.00 44.87 ? 333 ILE   A CB  1 
ATOM   1513 C  CG1 . ILE   A 1 203 ? -19.930 25.659  -24.449 1.00 41.12 ? 333 ILE   A CG1 1 
ATOM   1514 C  CG2 . ILE   A 1 203 ? -22.239 26.131  -23.569 1.00 43.12 ? 333 ILE   A CG2 1 
ATOM   1515 C  CD1 . ILE   A 1 203 ? -18.746 26.240  -23.718 1.00 41.58 ? 333 ILE   A CD1 1 
ATOM   1516 N  N   . ASN   A 1 204 ? -24.086 26.892  -26.001 1.00 43.07 ? 334 ASN   A N   1 
ATOM   1517 C  CA  . ASN   A 1 204 ? -25.344 27.620  -25.953 1.00 46.88 ? 334 ASN   A CA  1 
ATOM   1518 C  C   . ASN   A 1 204 ? -25.516 28.238  -24.568 1.00 48.58 ? 334 ASN   A C   1 
ATOM   1519 O  O   . ASN   A 1 204 ? -25.635 27.520  -23.568 1.00 43.51 ? 334 ASN   A O   1 
ATOM   1520 C  CB  . ASN   A 1 204 ? -26.489 26.673  -26.295 1.00 45.76 ? 334 ASN   A CB  1 
ATOM   1521 C  CG  . ASN   A 1 204 ? -27.852 27.330  -26.224 1.00 51.00 ? 334 ASN   A CG  1 
ATOM   1522 O  OD1 . ASN   A 1 204 ? -28.051 28.342  -25.553 1.00 49.30 ? 334 ASN   A OD1 1 
ATOM   1523 N  ND2 . ASN   A 1 204 ? -28.807 26.741  -26.925 1.00 53.57 ? 334 ASN   A ND2 1 
ATOM   1524 N  N   . GLY   A 1 205 ? -25.524 29.572  -24.516 1.00 47.46 ? 335 GLY   A N   1 
ATOM   1525 C  CA  . GLY   A 1 205 ? -25.569 30.256  -23.235 1.00 50.12 ? 335 GLY   A CA  1 
ATOM   1526 C  C   . GLY   A 1 205 ? -26.876 30.051  -22.493 1.00 49.90 ? 335 GLY   A C   1 
ATOM   1527 O  O   . GLY   A 1 205 ? -26.884 29.888  -21.270 1.00 48.42 ? 335 GLY   A O   1 
ATOM   1528 N  N   . THR   A 1 206 ? -27.999 30.072  -23.217 1.00 52.93 ? 336 THR   A N   1 
ATOM   1529 C  CA  . THR   A 1 206 ? -29.292 29.800  -22.597 1.00 51.14 ? 336 THR   A CA  1 
ATOM   1530 C  C   . THR   A 1 206 ? -29.256 28.487  -21.825 1.00 52.08 ? 336 THR   A C   1 
ATOM   1531 O  O   . THR   A 1 206 ? -29.623 28.431  -20.645 1.00 49.69 ? 336 THR   A O   1 
ATOM   1532 C  CB  . THR   A 1 206 ? -30.387 29.764  -23.666 1.00 52.52 ? 336 THR   A CB  1 
ATOM   1533 O  OG1 . THR   A 1 206 ? -30.317 30.953  -24.463 1.00 55.77 ? 336 THR   A OG1 1 
ATOM   1534 C  CG2 . THR   A 1 206 ? -31.766 29.658  -23.025 1.00 53.18 ? 336 THR   A CG2 1 
ATOM   1535 N  N   . LYS   A 1 207 ? -28.800 27.420  -22.482 1.00 49.27 ? 337 LYS   A N   1 
ATOM   1536 C  CA  . LYS   A 1 207 ? -28.715 26.119  -21.830 1.00 51.40 ? 337 LYS   A CA  1 
ATOM   1537 C  C   . LYS   A 1 207 ? -27.771 26.162  -20.636 1.00 48.22 ? 337 LYS   A C   1 
ATOM   1538 O  O   . LYS   A 1 207 ? -28.146 25.789  -19.519 1.00 49.03 ? 337 LYS   A O   1 
ATOM   1539 C  CB  . LYS   A 1 207 ? -28.256 25.066  -22.835 1.00 49.40 ? 337 LYS   A CB  1 
ATOM   1540 C  CG  . LYS   A 1 207 ? -29.359 24.163  -23.348 1.00 53.31 ? 337 LYS   A CG  1 
ATOM   1541 C  CD  . LYS   A 1 207 ? -29.019 23.646  -24.737 1.00 55.72 ? 337 LYS   A CD  1 
ATOM   1542 C  CE  . LYS   A 1 207 ? -30.249 23.158  -25.483 1.00 55.08 ? 337 LYS   A CE  1 
ATOM   1543 N  NZ  . LYS   A 1 207 ? -30.988 22.099  -24.735 1.00 59.30 ? 337 LYS   A NZ  1 
ATOM   1544 N  N   . TRP   A 1 208 ? -26.534 26.617  -20.856 1.00 44.54 ? 338 TRP   A N   1 
ATOM   1545 C  CA  . TRP   A 1 208 ? -25.539 26.599  -19.788 1.00 46.89 ? 338 TRP   A CA  1 
ATOM   1546 C  C   . TRP   A 1 208 ? -26.027 27.355  -18.561 1.00 48.97 ? 338 TRP   A C   1 
ATOM   1547 O  O   . TRP   A 1 208 ? -25.852 26.896  -17.425 1.00 46.53 ? 338 TRP   A O   1 
ATOM   1548 C  CB  . TRP   A 1 208 ? -24.221 27.197  -20.281 1.00 47.08 ? 338 TRP   A CB  1 
ATOM   1549 C  CG  . TRP   A 1 208 ? -23.241 27.395  -19.173 1.00 45.73 ? 338 TRP   A CG  1 
ATOM   1550 C  CD1 . TRP   A 1 208 ? -22.851 28.580  -18.620 1.00 44.99 ? 338 TRP   A CD1 1 
ATOM   1551 C  CD2 . TRP   A 1 208 ? -22.543 26.370  -18.462 1.00 45.03 ? 338 TRP   A CD2 1 
ATOM   1552 N  NE1 . TRP   A 1 208 ? -21.944 28.355  -17.614 1.00 43.11 ? 338 TRP   A NE1 1 
ATOM   1553 C  CE2 . TRP   A 1 208 ? -21.738 27.006  -17.496 1.00 45.30 ? 338 TRP   A CE2 1 
ATOM   1554 C  CE3 . TRP   A 1 208 ? -22.516 24.975  -18.551 1.00 46.01 ? 338 TRP   A CE3 1 
ATOM   1555 C  CZ2 . TRP   A 1 208 ? -20.913 26.295  -16.625 1.00 45.79 ? 338 TRP   A CZ2 1 
ATOM   1556 C  CZ3 . TRP   A 1 208 ? -21.696 24.270  -17.684 1.00 42.70 ? 338 TRP   A CZ3 1 
ATOM   1557 C  CH2 . TRP   A 1 208 ? -20.908 24.932  -16.733 1.00 42.71 ? 338 TRP   A CH2 1 
ATOM   1558 N  N   . ASN   A 1 209 ? -26.629 28.526  -18.769 1.00 50.63 ? 339 ASN   A N   1 
ATOM   1559 C  CA  . ASN   A 1 209 ? -27.060 29.331  -17.636 1.00 51.46 ? 339 ASN   A CA  1 
ATOM   1560 C  C   . ASN   A 1 209 ? -28.274 28.724  -16.947 1.00 51.20 ? 339 ASN   A C   1 
ATOM   1561 O  O   . ASN   A 1 209 ? -28.464 28.932  -15.743 1.00 49.27 ? 339 ASN   A O   1 
ATOM   1562 C  CB  . ASN   A 1 209 ? -27.343 30.762  -18.090 1.00 52.50 ? 339 ASN   A CB  1 
ATOM   1563 C  CG  . ASN   A 1 209 ? -26.071 31.542  -18.359 1.00 58.86 ? 339 ASN   A CG  1 
ATOM   1564 O  OD1 . ASN   A 1 209 ? -25.157 31.553  -17.532 1.00 59.99 ? 339 ASN   A OD1 1 
ATOM   1565 N  ND2 . ASN   A 1 209 ? -25.999 32.189  -19.518 1.00 57.39 ? 339 ASN   A ND2 1 
ATOM   1566 N  N   . LYS   A 1 210 ? -29.096 27.965  -17.676 1.00 47.46 ? 340 LYS   A N   1 
ATOM   1567 C  CA  . LYS   A 1 210 ? -30.204 27.277  -17.023 1.00 49.11 ? 340 LYS   A CA  1 
ATOM   1568 C  C   . LYS   A 1 210 ? -29.696 26.144  -16.142 1.00 49.39 ? 340 LYS   A C   1 
ATOM   1569 O  O   . LYS   A 1 210 ? -30.189 25.955  -15.023 1.00 44.96 ? 340 LYS   A O   1 
ATOM   1570 C  CB  . LYS   A 1 210 ? -31.202 26.749  -18.058 1.00 51.31 ? 340 LYS   A CB  1 
ATOM   1571 C  CG  . LYS   A 1 210 ? -31.789 27.805  -19.007 1.00 57.19 ? 340 LYS   A CG  1 
ATOM   1572 C  CD  . LYS   A 1 210 ? -32.004 29.180  -18.363 1.00 59.00 ? 340 LYS   A CD  1 
ATOM   1573 C  CE  . LYS   A 1 210 ? -32.484 29.094  -16.925 1.00 58.53 ? 340 LYS   A CE  1 
ATOM   1574 N  NZ  . LYS   A 1 210 ? -32.926 30.420  -16.425 1.00 63.83 ? 340 LYS   A NZ  1 
ATOM   1575 N  N   . VAL   A 1 211 ? -28.710 25.381  -16.625 1.00 46.07 ? 341 VAL   A N   1 
ATOM   1576 C  CA  . VAL   A 1 211 ? -28.145 24.310  -15.811 1.00 46.51 ? 341 VAL   A CA  1 
ATOM   1577 C  C   . VAL   A 1 211 ? -27.351 24.890  -14.648 1.00 47.05 ? 341 VAL   A C   1 
ATOM   1578 O  O   . VAL   A 1 211 ? -27.440 24.404  -13.514 1.00 43.83 ? 341 VAL   A O   1 
ATOM   1579 C  CB  . VAL   A 1 211 ? -27.282 23.371  -16.678 1.00 50.21 ? 341 VAL   A CB  1 
ATOM   1580 C  CG1 . VAL   A 1 211 ? -26.494 22.399  -15.801 1.00 47.53 ? 341 VAL   A CG1 1 
ATOM   1581 C  CG2 . VAL   A 1 211 ? -28.147 22.620  -17.684 1.00 45.45 ? 341 VAL   A CG2 1 
ATOM   1582 N  N   . LEU   A 1 212 ? -26.570 25.944  -14.902 1.00 44.27 ? 342 LEU   A N   1 
ATOM   1583 C  CA  . LEU   A 1 212 ? -25.759 26.525  -13.836 1.00 45.88 ? 342 LEU   A CA  1 
ATOM   1584 C  C   . LEU   A 1 212 ? -26.630 27.096  -12.722 1.00 49.61 ? 342 LEU   A C   1 
ATOM   1585 O  O   . LEU   A 1 212 ? -26.279 26.994  -11.539 1.00 47.45 ? 342 LEU   A O   1 
ATOM   1586 C  CB  . LEU   A 1 212 ? -24.831 27.600  -14.400 1.00 48.08 ? 342 LEU   A CB  1 
ATOM   1587 C  CG  . LEU   A 1 212 ? -23.723 28.007  -13.428 1.00 47.73 ? 342 LEU   A CG  1 
ATOM   1588 C  CD1 . LEU   A 1 212 ? -22.791 26.836  -13.170 1.00 46.35 ? 342 LEU   A CD1 1 
ATOM   1589 C  CD2 . LEU   A 1 212 ? -22.962 29.235  -13.920 1.00 49.65 ? 342 LEU   A CD2 1 
ATOM   1590 N  N   . LYS   A 1 213 ? -27.761 27.713  -13.079 1.00 44.91 ? 343 LYS   A N   1 
ATOM   1591 C  CA  . LYS   A 1 213 ? -28.711 28.154  -12.063 1.00 48.06 ? 343 LYS   A CA  1 
ATOM   1592 C  C   . LYS   A 1 213 ? -29.213 26.973  -11.243 1.00 47.99 ? 343 LYS   A C   1 
ATOM   1593 O  O   . LYS   A 1 213 ? -29.295 27.047  -10.011 1.00 48.07 ? 343 LYS   A O   1 
ATOM   1594 C  CB  . LYS   A 1 213 ? -29.883 28.886  -12.721 1.00 52.19 ? 343 LYS   A CB  1 
ATOM   1595 C  CG  . LYS   A 1 213 ? -29.711 30.393  -12.836 1.00 60.69 ? 343 LYS   A CG  1 
ATOM   1596 C  CD  . LYS   A 1 213 ? -30.733 31.000  -13.791 1.00 63.62 ? 343 LYS   A CD  1 
ATOM   1597 C  CE  . LYS   A 1 213 ? -30.290 32.370  -14.276 1.00 67.53 ? 343 LYS   A CE  1 
ATOM   1598 N  NZ  . LYS   A 1 213 ? -31.228 33.438  -13.838 1.00 72.06 ? 343 LYS   A NZ  1 
ATOM   1599 N  N   . GLN   A 1 214 ? -29.548 25.871  -11.912 1.00 46.91 ? 344 GLN   A N   1 
ATOM   1600 C  CA  . GLN   A 1 214 ? -30.016 24.688  -11.203 1.00 48.14 ? 344 GLN   A CA  1 
ATOM   1601 C  C   . GLN   A 1 214 ? -28.933 24.097  -10.305 1.00 50.03 ? 344 GLN   A C   1 
ATOM   1602 O  O   . GLN   A 1 214 ? -29.248 23.518  -9.257  1.00 51.15 ? 344 GLN   A O   1 
ATOM   1603 C  CB  . GLN   A 1 214 ? -30.522 23.653  -12.209 1.00 48.15 ? 344 GLN   A CB  1 
ATOM   1604 C  CG  . GLN   A 1 214 ? -31.937 23.924  -12.680 1.00 46.99 ? 344 GLN   A CG  1 
ATOM   1605 C  CD  . GLN   A 1 214 ? -32.342 23.067  -13.856 1.00 46.98 ? 344 GLN   A CD  1 
ATOM   1606 O  OE1 . GLN   A 1 214 ? -31.582 22.216  -14.314 1.00 47.66 ? 344 GLN   A OE1 1 
ATOM   1607 N  NE2 . GLN   A 1 214 ? -33.547 23.294  -14.360 1.00 49.25 ? 344 GLN   A NE2 1 
ATOM   1608 N  N   . VAL   A 1 215 ? -27.661 24.227  -10.692 1.00 46.49 ? 345 VAL   A N   1 
ATOM   1609 C  CA  . VAL   A 1 215 ? -26.577 23.767  -9.828  1.00 45.24 ? 345 VAL   A CA  1 
ATOM   1610 C  C   . VAL   A 1 215 ? -26.510 24.613  -8.559  1.00 46.86 ? 345 VAL   A C   1 
ATOM   1611 O  O   . VAL   A 1 215 ? -26.240 24.098  -7.466  1.00 47.65 ? 345 VAL   A O   1 
ATOM   1612 C  CB  . VAL   A 1 215 ? -25.239 23.775  -10.595 1.00 44.85 ? 345 VAL   A CB  1 
ATOM   1613 C  CG1 . VAL   A 1 215 ? -24.073 23.407  -9.669  1.00 41.59 ? 345 VAL   A CG1 1 
ATOM   1614 C  CG2 . VAL   A 1 215 ? -25.289 22.822  -11.800 1.00 42.17 ? 345 VAL   A CG2 1 
ATOM   1615 N  N   . THR   A 1 216 ? -26.753 25.923  -8.676  1.00 46.20 ? 346 THR   A N   1 
ATOM   1616 C  CA  . THR   A 1 216 ? -26.748 26.778  -7.491  1.00 49.92 ? 346 THR   A CA  1 
ATOM   1617 C  C   . THR   A 1 216 ? -27.934 26.467  -6.586  1.00 48.72 ? 346 THR   A C   1 
ATOM   1618 O  O   . THR   A 1 216 ? -27.793 26.432  -5.359  1.00 51.95 ? 346 THR   A O   1 
ATOM   1619 C  CB  . THR   A 1 216 ? -26.748 28.257  -7.893  1.00 50.22 ? 346 THR   A CB  1 
ATOM   1620 O  OG1 . THR   A 1 216 ? -27.992 28.596  -8.519  1.00 52.74 ? 346 THR   A OG1 1 
ATOM   1621 C  CG2 . THR   A 1 216 ? -25.616 28.553  -8.860  1.00 45.81 ? 346 THR   A CG2 1 
ATOM   1622 N  N   . GLU   A 1 217 ? -29.109 26.232  -7.173  1.00 50.31 ? 347 GLU   A N   1 
ATOM   1623 C  CA  . GLU   A 1 217 ? -30.265 25.816  -6.387  1.00 52.20 ? 347 GLU   A CA  1 
ATOM   1624 C  C   . GLU   A 1 217 ? -29.946 24.574  -5.561  1.00 52.31 ? 347 GLU   A C   1 
ATOM   1625 O  O   . GLU   A 1 217 ? -30.262 24.507  -4.368  1.00 52.60 ? 347 GLU   A O   1 
ATOM   1626 C  CB  . GLU   A 1 217 ? -31.460 25.563  -7.312  1.00 54.71 ? 347 GLU   A CB  1 
ATOM   1627 C  CG  . GLU   A 1 217 ? -32.454 24.534  -6.783  1.00 62.60 ? 347 GLU   A CG  1 
ATOM   1628 C  CD  . GLU   A 1 217 ? -33.528 24.159  -7.799  1.00 69.44 ? 347 GLU   A CD  1 
ATOM   1629 O  OE1 . GLU   A 1 217 ? -33.398 24.536  -8.986  1.00 68.90 ? 347 GLU   A OE1 1 
ATOM   1630 O  OE2 . GLU   A 1 217 ? -34.500 23.477  -7.404  1.00 72.16 ? 347 GLU   A OE2 1 
ATOM   1631 N  N   . LYS   A 1 218 ? -29.308 23.580  -6.185  1.00 51.45 ? 348 LYS   A N   1 
ATOM   1632 C  CA  . LYS   A 1 218 ? -28.979 22.341  -5.484  1.00 49.48 ? 348 LYS   A CA  1 
ATOM   1633 C  C   . LYS   A 1 218 ? -27.939 22.578  -4.396  1.00 47.97 ? 348 LYS   A C   1 
ATOM   1634 O  O   . LYS   A 1 218 ? -28.091 22.110  -3.262  1.00 49.51 ? 348 LYS   A O   1 
ATOM   1635 C  CB  . LYS   A 1 218 ? -28.481 21.293  -6.483  1.00 49.94 ? 348 LYS   A CB  1 
ATOM   1636 C  CG  . LYS   A 1 218 ? -28.483 19.866  -5.957  1.00 48.72 ? 348 LYS   A CG  1 
ATOM   1637 C  CD  . LYS   A 1 218 ? -29.774 19.543  -5.228  1.00 52.18 ? 348 LYS   A CD  1 
ATOM   1638 C  CE  . LYS   A 1 218 ? -30.751 18.803  -6.133  1.00 53.63 ? 348 LYS   A CE  1 
ATOM   1639 N  NZ  . LYS   A 1 218 ? -31.583 17.834  -5.362  1.00 52.83 ? 348 LYS   A NZ  1 
ATOM   1640 N  N   . LEU   A 1 219 ? -26.860 23.289  -4.727  1.00 48.47 ? 349 LEU   A N   1 
ATOM   1641 C  CA  . LEU   A 1 219 ? -25.837 23.580  -3.728  1.00 47.66 ? 349 LEU   A CA  1 
ATOM   1642 C  C   . LEU   A 1 219 ? -26.408 24.367  -2.557  1.00 49.75 ? 349 LEU   A C   1 
ATOM   1643 O  O   . LEU   A 1 219 ? -25.955 24.201  -1.419  1.00 48.98 ? 349 LEU   A O   1 
ATOM   1644 C  CB  . LEU   A 1 219 ? -24.681 24.343  -4.374  1.00 48.56 ? 349 LEU   A CB  1 
ATOM   1645 C  CG  . LEU   A 1 219 ? -23.744 23.502  -5.249  1.00 49.16 ? 349 LEU   A CG  1 
ATOM   1646 C  CD1 . LEU   A 1 219 ? -22.750 24.380  -6.000  1.00 45.07 ? 349 LEU   A CD1 1 
ATOM   1647 C  CD2 . LEU   A 1 219 ? -23.018 22.456  -4.418  1.00 45.07 ? 349 LEU   A CD2 1 
ATOM   1648 N  N   . LYS   A 1 220 ? -27.396 25.228  -2.813  1.00 49.37 ? 350 LYS   A N   1 
ATOM   1649 C  CA  . LYS   A 1 220 ? -28.084 25.908  -1.719  1.00 51.16 ? 350 LYS   A CA  1 
ATOM   1650 C  C   . LYS   A 1 220 ? -28.666 24.905  -0.731  1.00 51.80 ? 350 LYS   A C   1 
ATOM   1651 O  O   . LYS   A 1 220 ? -28.680 25.148  0.482   1.00 52.56 ? 350 LYS   A O   1 
ATOM   1652 C  CB  . LYS   A 1 220 ? -29.191 26.805  -2.275  1.00 50.61 ? 350 LYS   A CB  1 
ATOM   1653 C  CG  . LYS   A 1 220 ? -28.879 28.292  -2.264  1.00 56.11 ? 350 LYS   A CG  1 
ATOM   1654 C  CD  . LYS   A 1 220 ? -29.978 29.082  -2.963  1.00 55.54 ? 350 LYS   A CD  1 
ATOM   1655 C  CE  . LYS   A 1 220 ? -29.643 30.561  -3.025  1.00 59.93 ? 350 LYS   A CE  1 
ATOM   1656 N  NZ  . LYS   A 1 220 ? -30.064 31.264  -1.780  1.00 59.58 ? 350 LYS   A NZ  1 
ATOM   1657 N  N   . GLU   A 1 221 ? -29.152 23.770  -1.234  1.00 52.66 ? 351 GLU   A N   1 
ATOM   1658 C  CA  . GLU   A 1 221 ? -29.770 22.769  -0.373  1.00 51.29 ? 351 GLU   A CA  1 
ATOM   1659 C  C   . GLU   A 1 221 ? -28.771 22.161  0.599   1.00 51.62 ? 351 GLU   A C   1 
ATOM   1660 O  O   . GLU   A 1 221 ? -29.161 21.733  1.692   1.00 53.75 ? 351 GLU   A O   1 
ATOM   1661 C  CB  . GLU   A 1 221 ? -30.412 21.673  -1.224  1.00 50.82 ? 351 GLU   A CB  1 
ATOM   1662 C  CG  . GLU   A 1 221 ? -31.575 22.154  -2.083  1.00 55.60 ? 351 GLU   A CG  1 
ATOM   1663 C  CD  . GLU   A 1 221 ? -32.165 21.046  -2.949  1.00 66.29 ? 351 GLU   A CD  1 
ATOM   1664 O  OE1 . GLU   A 1 221 ? -32.940 21.367  -3.879  1.00 63.63 ? 351 GLU   A OE1 1 
ATOM   1665 O  OE2 . GLU   A 1 221 ? -31.865 19.857  -2.690  1.00 69.51 ? 351 GLU   A OE2 1 
ATOM   1666 N  N   . HIS   A 1 222 ? -27.491 22.106  0.225   1.00 51.02 ? 352 HIS   A N   1 
ATOM   1667 C  CA  . HIS   A 1 222 ? -26.459 21.525  1.076   1.00 51.23 ? 352 HIS   A CA  1 
ATOM   1668 C  C   . HIS   A 1 222 ? -25.729 22.548  1.936   1.00 49.77 ? 352 HIS   A C   1 
ATOM   1669 O  O   . HIS   A 1 222 ? -24.953 22.152  2.813   1.00 47.22 ? 352 HIS   A O   1 
ATOM   1670 C  CB  . HIS   A 1 222 ? -25.420 20.777  0.235   1.00 52.13 ? 352 HIS   A CB  1 
ATOM   1671 C  CG  . HIS   A 1 222 ? -25.980 19.625  -0.537  1.00 50.00 ? 352 HIS   A CG  1 
ATOM   1672 N  ND1 . HIS   A 1 222 ? -25.763 18.313  -0.178  1.00 45.65 ? 352 HIS   A ND1 1 
ATOM   1673 C  CD2 . HIS   A 1 222 ? -26.742 19.589  -1.656  1.00 48.62 ? 352 HIS   A CD2 1 
ATOM   1674 C  CE1 . HIS   A 1 222 ? -26.375 17.517  -1.036  1.00 49.50 ? 352 HIS   A CE1 1 
ATOM   1675 N  NE2 . HIS   A 1 222 ? -26.975 18.266  -1.945  1.00 51.85 ? 352 HIS   A NE2 1 
ATOM   1676 N  N   . PHE   A 1 223 ? -25.934 23.843  1.701   1.00 50.45 ? 353 PHE   A N   1 
ATOM   1677 C  CA  . PHE   A 1 223 ? -25.230 24.890  2.436   1.00 52.83 ? 353 PHE   A CA  1 
ATOM   1678 C  C   . PHE   A 1 223 ? -26.250 25.876  3.006   1.00 54.35 ? 353 PHE   A C   1 
ATOM   1679 O  O   . PHE   A 1 223 ? -26.209 27.081  2.754   1.00 55.71 ? 353 PHE   A O   1 
ATOM   1680 C  CB  . PHE   A 1 223 ? -24.198 25.558  1.534   1.00 50.34 ? 353 PHE   A CB  1 
ATOM   1681 C  CG  . PHE   A 1 223 ? -23.044 24.662  1.185   1.00 52.04 ? 353 PHE   A CG  1 
ATOM   1682 C  CD1 . PHE   A 1 223 ? -21.951 24.549  2.033   1.00 50.75 ? 353 PHE   A CD1 1 
ATOM   1683 C  CD2 . PHE   A 1 223 ? -23.067 23.906  0.025   1.00 48.83 ? 353 PHE   A CD2 1 
ATOM   1684 C  CE1 . PHE   A 1 223 ? -20.899 23.713  1.718   1.00 52.00 ? 353 PHE   A CE1 1 
ATOM   1685 C  CE2 . PHE   A 1 223 ? -22.018 23.070  -0.295  1.00 49.31 ? 353 PHE   A CE2 1 
ATOM   1686 C  CZ  . PHE   A 1 223 ? -20.932 22.971  0.550   1.00 49.63 ? 353 PHE   A CZ  1 
ATOM   1687 N  N   . ASN   A 1 224 ? -27.162 25.326  3.815   1.00 54.99 ? 354 ASN   A N   1 
ATOM   1688 C  CA  . ASN   A 1 224 ? -28.317 26.003  4.405   1.00 58.68 ? 354 ASN   A CA  1 
ATOM   1689 C  C   . ASN   A 1 224 ? -28.687 27.299  3.698   1.00 59.96 ? 354 ASN   A C   1 
ATOM   1690 O  O   . ASN   A 1 224 ? -28.636 28.384  4.287   1.00 55.16 ? 354 ASN   A O   1 
ATOM   1691 C  CB  . ASN   A 1 224 ? -28.086 26.259  5.898   1.00 63.02 ? 354 ASN   A CB  1 
ATOM   1692 C  CG  . ASN   A 1 224 ? -26.956 27.240  6.164   1.00 66.93 ? 354 ASN   A CG  1 
ATOM   1693 O  OD1 . ASN   A 1 224 ? -25.835 26.829  6.454   1.00 72.64 ? 354 ASN   A OD1 1 
ATOM   1694 N  ND2 . ASN   A 1 224 ? -27.250 28.538  6.092   1.00 66.49 ? 354 ASN   A ND2 1 
ATOM   1695 N  N   . ASN   A 1 225 ? -29.068 27.181  2.428   1.00 56.77 ? 355 ASN   A N   1 
ATOM   1696 C  CA  . ASN   A 1 225 ? -29.620 28.294  1.664   1.00 58.75 ? 355 ASN   A CA  1 
ATOM   1697 C  C   . ASN   A 1 225 ? -28.694 29.512  1.655   1.00 56.11 ? 355 ASN   A C   1 
ATOM   1698 O  O   . ASN   A 1 225 ? -29.158 30.654  1.609   1.00 57.26 ? 355 ASN   A O   1 
ATOM   1699 C  CB  . ASN   A 1 225 ? -31.006 28.677  2.193   1.00 63.53 ? 355 ASN   A CB  1 
ATOM   1700 C  CG  . ASN   A 1 225 ? -31.961 29.078  1.085   1.00 62.56 ? 355 ASN   A CG  1 
ATOM   1701 O  OD1 . ASN   A 1 225 ? -31.895 30.190  0.553   1.00 65.55 ? 355 ASN   A OD1 1 
ATOM   1702 N  ND2 . ASN   A 1 225 ? -32.851 28.164  0.722   1.00 60.28 ? 355 ASN   A ND2 1 
ATOM   1703 N  N   . LYS   A 1 226 ? -27.382 29.292  1.696   1.00 55.49 ? 357 LYS   A N   1 
ATOM   1704 C  CA  . LYS   A 1 226 ? -26.442 30.403  1.654   1.00 53.40 ? 357 LYS   A CA  1 
ATOM   1705 C  C   . LYS   A 1 226 ? -26.360 30.973  0.236   1.00 51.71 ? 357 LYS   A C   1 
ATOM   1706 O  O   . LYS   A 1 226 ? -26.924 30.430  -0.717  1.00 53.06 ? 357 LYS   A O   1 
ATOM   1707 C  CB  . LYS   A 1 226 ? -25.060 29.954  2.125   1.00 53.30 ? 357 LYS   A CB  1 
ATOM   1708 C  CG  . LYS   A 1 226 ? -24.925 29.810  3.633   1.00 56.72 ? 357 LYS   A CG  1 
ATOM   1709 C  CD  . LYS   A 1 226 ? -23.517 29.399  4.031   1.00 53.69 ? 357 LYS   A CD  1 
ATOM   1710 C  CE  . LYS   A 1 226 ? -22.565 30.579  3.976   1.00 54.97 ? 357 LYS   A CE  1 
ATOM   1711 N  NZ  . LYS   A 1 226 ? -21.312 30.307  4.737   1.00 52.93 ? 357 LYS   A NZ  1 
ATOM   1712 N  N   . THR   A 1 227 ? -25.653 32.092  0.097   1.00 49.58 ? 358 THR   A N   1 
ATOM   1713 C  CA  . THR   A 1 227 ? -25.436 32.691  -1.216  1.00 51.84 ? 358 THR   A CA  1 
ATOM   1714 C  C   . THR   A 1 227 ? -24.351 31.907  -1.949  1.00 50.01 ? 358 THR   A C   1 
ATOM   1715 O  O   . THR   A 1 227 ? -23.218 31.801  -1.466  1.00 51.15 ? 358 THR   A O   1 
ATOM   1716 C  CB  . THR   A 1 227 ? -25.055 34.168  -1.087  1.00 50.79 ? 358 THR   A CB  1 
ATOM   1717 O  OG1 . THR   A 1 227 ? -26.064 34.863  -0.345  1.00 50.62 ? 358 THR   A OG1 1 
ATOM   1718 C  CG2 . THR   A 1 227 ? -24.901 34.820  -2.462  1.00 48.72 ? 358 THR   A CG2 1 
ATOM   1719 N  N   . ILE   A 1 228 ? -24.700 31.347  -3.104  1.00 50.45 ? 359 ILE   A N   1 
ATOM   1720 C  CA  . ILE   A 1 228 ? -23.795 30.507  -3.882  1.00 49.73 ? 359 ILE   A CA  1 
ATOM   1721 C  C   . ILE   A 1 228 ? -23.134 31.376  -4.944  1.00 50.37 ? 359 ILE   A C   1 
ATOM   1722 O  O   . ILE   A 1 228 ? -23.818 31.977  -5.780  1.00 49.00 ? 359 ILE   A O   1 
ATOM   1723 C  CB  . ILE   A 1 228 ? -24.538 29.324  -4.522  1.00 48.42 ? 359 ILE   A CB  1 
ATOM   1724 C  CG1 . ILE   A 1 228 ? -25.223 28.477  -3.448  1.00 47.86 ? 359 ILE   A CG1 1 
ATOM   1725 C  CG2 . ILE   A 1 228 ? -23.579 28.479  -5.364  1.00 47.19 ? 359 ILE   A CG2 1 
ATOM   1726 C  CD1 . ILE   A 1 228 ? -24.319 28.096  -2.295  1.00 48.46 ? 359 ILE   A CD1 1 
ATOM   1727 N  N   . ILE   A 1 229 ? -21.805 31.438  -4.922  1.00 49.64 ? 360 ILE   A N   1 
ATOM   1728 C  CA  . ILE   A 1 229 ? -21.043 32.247  -5.865  1.00 49.81 ? 360 ILE   A CA  1 
ATOM   1729 C  C   . ILE   A 1 229 ? -20.075 31.345  -6.614  1.00 48.37 ? 360 ILE   A C   1 
ATOM   1730 O  O   . ILE   A 1 229 ? -19.428 30.480  -6.013  1.00 45.11 ? 360 ILE   A O   1 
ATOM   1731 C  CB  . ILE   A 1 229 ? -20.286 33.386  -5.152  1.00 51.11 ? 360 ILE   A CB  1 
ATOM   1732 C  CG1 . ILE   A 1 229 ? -21.268 34.444  -4.641  1.00 50.86 ? 360 ILE   A CG1 1 
ATOM   1733 C  CG2 . ILE   A 1 229 ? -19.239 34.008  -6.074  1.00 48.13 ? 360 ILE   A CG2 1 
ATOM   1734 C  CD1 . ILE   A 1 229 ? -20.883 35.008  -3.292  1.00 49.44 ? 360 ILE   A CD1 1 
ATOM   1735 N  N   . PHE   A 1 230 ? -19.988 31.540  -7.928  1.00 50.52 ? 361 PHE   A N   1 
ATOM   1736 C  CA  . PHE   A 1 230 ? -19.006 30.867  -8.767  1.00 49.16 ? 361 PHE   A CA  1 
ATOM   1737 C  C   . PHE   A 1 230 ? -17.903 31.848  -9.141  1.00 48.26 ? 361 PHE   A C   1 
ATOM   1738 O  O   . PHE   A 1 230 ? -18.173 33.019  -9.424  1.00 52.18 ? 361 PHE   A O   1 
ATOM   1739 C  CB  . PHE   A 1 230 ? -19.651 30.286  -10.033 1.00 46.10 ? 361 PHE   A CB  1 
ATOM   1740 C  CG  . PHE   A 1 230 ? -20.479 29.061  -9.776  1.00 44.02 ? 361 PHE   A CG  1 
ATOM   1741 C  CD1 . PHE   A 1 230 ? -19.880 27.823  -9.609  1.00 45.70 ? 361 PHE   A CD1 1 
ATOM   1742 C  CD2 . PHE   A 1 230 ? -21.855 29.147  -9.690  1.00 44.27 ? 361 PHE   A CD2 1 
ATOM   1743 C  CE1 . PHE   A 1 230 ? -20.641 26.693  -9.361  1.00 44.52 ? 361 PHE   A CE1 1 
ATOM   1744 C  CE2 . PHE   A 1 230 ? -22.620 28.023  -9.447  1.00 44.93 ? 361 PHE   A CE2 1 
ATOM   1745 C  CZ  . PHE   A 1 230 ? -22.013 26.794  -9.280  1.00 46.15 ? 361 PHE   A CZ  1 
ATOM   1746 N  N   . GLN   A 1 231 ? -16.662 31.372  -9.118  1.00 47.39 ? 362 GLN   A N   1 
ATOM   1747 C  CA  . GLN   A 1 231 ? -15.509 32.185  -9.470  1.00 50.34 ? 362 GLN   A CA  1 
ATOM   1748 C  C   . GLN   A 1 231 ? -14.495 31.329  -10.213 1.00 51.20 ? 362 GLN   A C   1 
ATOM   1749 O  O   . GLN   A 1 231 ? -14.438 30.110  -10.008 1.00 47.33 ? 362 GLN   A O   1 
ATOM   1750 C  CB  . GLN   A 1 231 ? -14.858 32.812  -8.225  1.00 49.22 ? 362 GLN   A CB  1 
ATOM   1751 C  CG  . GLN   A 1 231 ? -15.518 34.112  -7.771  1.00 50.75 ? 362 GLN   A CG  1 
ATOM   1752 C  CD  . GLN   A 1 231 ? -15.791 35.061  -8.924  1.00 53.56 ? 362 GLN   A CD  1 
ATOM   1753 O  OE1 . GLN   A 1 231 ? -14.892 35.762  -9.393  1.00 56.65 ? 362 GLN   A OE1 1 
ATOM   1754 N  NE2 . GLN   A 1 231 ? -17.037 35.087  -9.388  1.00 51.40 ? 362 GLN   A NE2 1 
ATOM   1755 N  N   . PRO   A 1 232 ? -13.708 31.928  -11.103 1.00 52.06 ? 363 PRO   A N   1 
ATOM   1756 C  CA  . PRO   A 1 232 ? -12.668 31.169  -11.806 1.00 49.73 ? 363 PRO   A CA  1 
ATOM   1757 C  C   . PRO   A 1 232 ? -11.616 30.676  -10.832 1.00 51.56 ? 363 PRO   A C   1 
ATOM   1758 O  O   . PRO   A 1 232 ? -11.502 31.203  -9.714  1.00 50.54 ? 363 PRO   A O   1 
ATOM   1759 C  CB  . PRO   A 1 232 ? -12.079 32.199  -12.785 1.00 47.53 ? 363 PRO   A CB  1 
ATOM   1760 C  CG  . PRO   A 1 232 ? -13.162 33.212  -12.952 1.00 51.06 ? 363 PRO   A CG  1 
ATOM   1761 C  CD  . PRO   A 1 232 ? -13.780 33.317  -11.585 1.00 52.72 ? 363 PRO   A CD  1 
ATOM   1762 N  N   . PRO   A 1 233 ? -10.827 29.672  -11.214 1.00 50.10 ? 364 PRO   A N   1 
ATOM   1763 C  CA  . PRO   A 1 233 ? -9.791  29.161  -10.309 1.00 51.19 ? 364 PRO   A CA  1 
ATOM   1764 C  C   . PRO   A 1 233 ? -8.892  30.276  -9.797  1.00 50.69 ? 364 PRO   A C   1 
ATOM   1765 O  O   . PRO   A 1 233 ? -8.555  31.213  -10.523 1.00 49.89 ? 364 PRO   A O   1 
ATOM   1766 C  CB  . PRO   A 1 233 ? -9.018  28.175  -11.190 1.00 45.39 ? 364 PRO   A CB  1 
ATOM   1767 C  CG  . PRO   A 1 233 ? -10.044 27.702  -12.162 1.00 45.12 ? 364 PRO   A CG  1 
ATOM   1768 C  CD  . PRO   A 1 233 ? -10.830 28.941  -12.492 1.00 48.02 ? 364 PRO   A CD  1 
ATOM   1769 N  N   . SER   A 1 234 ? -8.494  30.166  -8.533  1.00 54.54 ? 365 SER   A N   1 
ATOM   1770 C  CA  . SER   A 1 234 ? -7.626  31.165  -7.912  1.00 57.07 ? 365 SER   A CA  1 
ATOM   1771 C  C   . SER   A 1 234 ? -6.174  30.684  -7.941  1.00 56.98 ? 365 SER   A C   1 
ATOM   1772 O  O   . SER   A 1 234 ? -5.568  30.365  -6.920  1.00 61.64 ? 365 SER   A O   1 
ATOM   1773 C  CB  . SER   A 1 234 ? -8.091  31.462  -6.488  1.00 59.62 ? 365 SER   A CB  1 
ATOM   1774 O  OG  . SER   A 1 234 ? -9.478  31.747  -6.451  1.00 59.40 ? 365 SER   A OG  1 
ATOM   1775 N  N   . GLY   A 1 235 ? -5.618  30.645  -9.147  1.00 60.06 ? 366 GLY   A N   1 
ATOM   1776 C  CA  . GLY   A 1 235 ? -4.219  30.320  -9.326  1.00 56.53 ? 366 GLY   A CA  1 
ATOM   1777 C  C   . GLY   A 1 235 ? -3.994  28.859  -9.693  1.00 58.02 ? 366 GLY   A C   1 
ATOM   1778 O  O   . GLY   A 1 235 ? -4.868  27.998  -9.548  1.00 56.16 ? 366 GLY   A O   1 
ATOM   1779 N  N   . GLY   A 1 236 ? -2.786  28.581  -10.174 1.00 54.96 ? 367 GLY   A N   1 
ATOM   1780 C  CA  . GLY   A 1 236 ? -2.386  27.254  -10.585 1.00 54.27 ? 367 GLY   A CA  1 
ATOM   1781 C  C   . GLY   A 1 236 ? -1.863  27.241  -12.006 1.00 53.50 ? 367 GLY   A C   1 
ATOM   1782 O  O   . GLY   A 1 236 ? -1.755  28.268  -12.674 1.00 49.03 ? 367 GLY   A O   1 
ATOM   1783 N  N   . ASP   A 1 237 ? -1.525  26.039  -12.464 1.00 54.41 ? 368 ASP   A N   1 
ATOM   1784 C  CA  . ASP   A 1 237 ? -1.046  25.868  -13.825 1.00 52.96 ? 368 ASP   A CA  1 
ATOM   1785 C  C   . ASP   A 1 237 ? -2.221  25.845  -14.803 1.00 48.78 ? 368 ASP   A C   1 
ATOM   1786 O  O   . ASP   A 1 237 ? -3.385  25.693  -14.417 1.00 45.53 ? 368 ASP   A O   1 
ATOM   1787 C  CB  . ASP   A 1 237 ? -0.214  24.589  -13.940 1.00 59.63 ? 368 ASP   A CB  1 
ATOM   1788 C  CG  . ASP   A 1 237 ? 1.112   24.691  -13.201 1.00 66.14 ? 368 ASP   A CG  1 
ATOM   1789 O  OD1 . ASP   A 1 237 ? 1.739   25.769  -13.257 1.00 68.04 ? 368 ASP   A OD1 1 
ATOM   1790 O  OD2 . ASP   A 1 237 ? 1.522   23.700  -12.560 1.00 86.85 ? 368 ASP   A OD2 1 
ATOM   1791 N  N   . LEU   A 1 238 ? -1.896  26.007  -16.091 1.00 43.80 ? 369 LEU   A N   1 
ATOM   1792 C  CA  . LEU   A 1 238 ? -2.928  26.147  -17.115 1.00 40.53 ? 369 LEU   A CA  1 
ATOM   1793 C  C   . LEU   A 1 238 ? -3.878  24.961  -17.133 1.00 40.21 ? 369 LEU   A C   1 
ATOM   1794 O  O   . LEU   A 1 238 ? -5.047  25.112  -17.506 1.00 39.30 ? 369 LEU   A O   1 
ATOM   1795 C  CB  . LEU   A 1 238 ? -2.286  26.316  -18.495 1.00 39.27 ? 369 LEU   A CB  1 
ATOM   1796 C  CG  . LEU   A 1 238 ? -1.547  27.627  -18.750 1.00 45.39 ? 369 LEU   A CG  1 
ATOM   1797 C  CD1 . LEU   A 1 238 ? -0.590  27.497  -19.932 1.00 42.72 ? 369 LEU   A CD1 1 
ATOM   1798 C  CD2 . LEU   A 1 238 ? -2.539  28.768  -18.964 1.00 47.74 ? 369 LEU   A CD2 1 
ATOM   1799 N  N   . GLU   A 1 239 ? -3.399  23.775  -16.745 1.00 40.24 ? 370 GLU   A N   1 
ATOM   1800 C  CA  . GLU   A 1 239 ? -4.235  22.580  -16.825 1.00 42.98 ? 370 GLU   A CA  1 
ATOM   1801 C  C   . GLU   A 1 239 ? -5.477  22.687  -15.949 1.00 43.15 ? 370 GLU   A C   1 
ATOM   1802 O  O   . GLU   A 1 239 ? -6.513  22.097  -16.275 1.00 45.62 ? 370 GLU   A O   1 
ATOM   1803 C  CB  . GLU   A 1 239 ? -3.433  21.331  -16.442 1.00 42.82 ? 370 GLU   A CB  1 
ATOM   1804 C  CG  . GLU   A 1 239 ? -2.499  20.835  -17.530 1.00 42.41 ? 370 GLU   A CG  1 
ATOM   1805 C  CD  . GLU   A 1 239 ? -1.256  21.692  -17.652 1.00 44.06 ? 370 GLU   A CD  1 
ATOM   1806 O  OE1 . GLU   A 1 239 ? -0.979  22.447  -16.700 1.00 42.28 ? 370 GLU   A OE1 1 
ATOM   1807 O  OE2 . GLU   A 1 239 ? -0.567  21.614  -18.693 1.00 39.72 ? 370 GLU   A OE2 1 
ATOM   1808 N  N   . ILE   A 1 240 ? -5.408  23.421  -14.844 1.00 40.37 ? 371 ILE   A N   1 
ATOM   1809 C  CA  . ILE   A 1 240 ? -6.541  23.500  -13.934 1.00 42.28 ? 371 ILE   A CA  1 
ATOM   1810 C  C   . ILE   A 1 240 ? -7.181  24.884  -13.891 1.00 40.87 ? 371 ILE   A C   1 
ATOM   1811 O  O   . ILE   A 1 240 ? -8.357  24.989  -13.511 1.00 41.74 ? 371 ILE   A O   1 
ATOM   1812 C  CB  . ILE   A 1 240 ? -6.153  23.029  -12.517 1.00 46.73 ? 371 ILE   A CB  1 
ATOM   1813 C  CG1 . ILE   A 1 240 ? -4.888  23.737  -12.021 1.00 45.23 ? 371 ILE   A CG1 1 
ATOM   1814 C  CG2 . ILE   A 1 240 ? -5.954  21.515  -12.507 1.00 43.29 ? 371 ILE   A CG2 1 
ATOM   1815 C  CD1 . ILE   A 1 240 ? -5.106  25.154  -11.565 1.00 47.07 ? 371 ILE   A CD1 1 
ATOM   1816 N  N   . THR   A 1 241 ? -6.471  25.942  -14.273 1.00 41.60 ? 372 THR   A N   1 
ATOM   1817 C  CA  . THR   A 1 241 ? -7.151  27.216  -14.476 1.00 41.62 ? 372 THR   A CA  1 
ATOM   1818 C  C   . THR   A 1 241 ? -7.912  27.265  -15.796 1.00 39.68 ? 372 THR   A C   1 
ATOM   1819 O  O   . THR   A 1 241 ? -8.725  28.175  -15.993 1.00 38.17 ? 372 THR   A O   1 
ATOM   1820 C  CB  . THR   A 1 241 ? -6.153  28.373  -14.422 1.00 40.44 ? 372 THR   A CB  1 
ATOM   1821 O  OG1 . THR   A 1 241 ? -5.324  28.334  -15.590 1.00 41.37 ? 372 THR   A OG1 1 
ATOM   1822 C  CG2 . THR   A 1 241 ? -5.287  28.281  -13.160 1.00 44.60 ? 372 THR   A CG2 1 
ATOM   1823 N  N   . MET   A 1 242 ? -7.661  26.320  -16.699 1.00 38.54 ? 373 MET   A N   1 
ATOM   1824 C  CA  . MET   A 1 242 ? -8.398  26.186  -17.944 1.00 36.76 ? 373 MET   A CA  1 
ATOM   1825 C  C   . MET   A 1 242 ? -9.128  24.849  -17.984 1.00 36.55 ? 373 MET   A C   1 
ATOM   1826 O  O   . MET   A 1 242 ? -8.820  23.921  -17.230 1.00 35.61 ? 373 MET   A O   1 
ATOM   1827 C  CB  . MET   A 1 242 ? -7.467  26.296  -19.158 1.00 38.61 ? 373 MET   A CB  1 
ATOM   1828 C  CG  . MET   A 1 242 ? -6.487  27.445  -19.079 1.00 43.06 ? 373 MET   A CG  1 
ATOM   1829 S  SD  . MET   A 1 242 ? -7.077  28.863  -20.000 1.00 52.41 ? 373 MET   A SD  1 
ATOM   1830 C  CE  . MET   A 1 242 ? -5.513  29.620  -20.432 1.00 54.20 ? 373 MET   A CE  1 
ATOM   1831 N  N   . HIS   A 1 243 ? -10.115 24.765  -18.871 1.00 36.40 ? 374 HIS   A N   1 
ATOM   1832 C  CA  . HIS   A 1 243 ? -10.761 23.494  -19.173 1.00 37.33 ? 374 HIS   A CA  1 
ATOM   1833 C  C   . HIS   A 1 243 ? -9.887  22.762  -20.184 1.00 36.51 ? 374 HIS   A C   1 
ATOM   1834 O  O   . HIS   A 1 243 ? -9.810  23.160  -21.350 1.00 36.33 ? 374 HIS   A O   1 
ATOM   1835 C  CB  . HIS   A 1 243 ? -12.176 23.719  -19.702 1.00 34.85 ? 374 HIS   A CB  1 
ATOM   1836 C  CG  . HIS   A 1 243 ? -12.776 22.516  -20.363 1.00 36.48 ? 374 HIS   A CG  1 
ATOM   1837 N  ND1 . HIS   A 1 243 ? -12.767 21.268  -19.780 1.00 35.95 ? 374 HIS   A ND1 1 
ATOM   1838 C  CD2 . HIS   A 1 243 ? -13.415 22.373  -21.549 1.00 36.93 ? 374 HIS   A CD2 1 
ATOM   1839 C  CE1 . HIS   A 1 243 ? -13.363 20.405  -20.582 1.00 35.97 ? 374 HIS   A CE1 1 
ATOM   1840 N  NE2 . HIS   A 1 243 ? -13.768 21.050  -21.661 1.00 37.18 ? 374 HIS   A NE2 1 
ATOM   1841 N  N   . SER   A 1 244 ? -9.206  21.714  -19.733 1.00 37.04 ? 375 SER   A N   1 
ATOM   1842 C  CA  . SER   A 1 244 ? -8.278  20.970  -20.571 1.00 36.27 ? 375 SER   A CA  1 
ATOM   1843 C  C   . SER   A 1 244 ? -8.892  19.644  -20.991 1.00 40.20 ? 375 SER   A C   1 
ATOM   1844 O  O   . SER   A 1 244 ? -9.605  19.002  -20.211 1.00 39.15 ? 375 SER   A O   1 
ATOM   1845 C  CB  . SER   A 1 244 ? -6.963  20.719  -19.834 1.00 40.58 ? 375 SER   A CB  1 
ATOM   1846 O  OG  . SER   A 1 244 ? -6.262  21.934  -19.622 1.00 44.53 ? 375 SER   A OG  1 
ATOM   1847 N  N   . PHE   A 1 245 ? -8.605  19.235  -22.224 1.00 34.92 ? 376 PHE   A N   1 
ATOM   1848 C  CA  . PHE   A 1 245 ? -9.077  17.962  -22.747 1.00 37.41 ? 376 PHE   A CA  1 
ATOM   1849 C  C   . PHE   A 1 245 ? -8.255  17.641  -23.987 1.00 37.95 ? 376 PHE   A C   1 
ATOM   1850 O  O   . PHE   A 1 245 ? -7.469  18.466  -24.459 1.00 36.43 ? 376 PHE   A O   1 
ATOM   1851 C  CB  . PHE   A 1 245 ? -10.578 18.007  -23.053 1.00 35.24 ? 376 PHE   A CB  1 
ATOM   1852 C  CG  . PHE   A 1 245 ? -10.978 19.135  -23.970 1.00 38.13 ? 376 PHE   A CG  1 
ATOM   1853 C  CD1 . PHE   A 1 245 ? -11.079 20.434  -23.493 1.00 40.33 ? 376 PHE   A CD1 1 
ATOM   1854 C  CD2 . PHE   A 1 245 ? -11.252 18.895  -25.311 1.00 37.46 ? 376 PHE   A CD2 1 
ATOM   1855 C  CE1 . PHE   A 1 245 ? -11.446 21.474  -24.333 1.00 41.00 ? 376 PHE   A CE1 1 
ATOM   1856 C  CE2 . PHE   A 1 245 ? -11.620 19.934  -26.158 1.00 38.96 ? 376 PHE   A CE2 1 
ATOM   1857 C  CZ  . PHE   A 1 245 ? -11.718 21.223  -25.668 1.00 41.37 ? 376 PHE   A CZ  1 
ATOM   1858 N  N   . ASN   A 1 246 ? -8.425  16.428  -24.504 1.00 36.43 ? 377 ASN   A N   1 
ATOM   1859 C  CA  . ASN   A 1 246 ? -7.723  16.010  -25.710 1.00 36.57 ? 377 ASN   A CA  1 
ATOM   1860 C  C   . ASN   A 1 246 ? -8.731  15.730  -26.815 1.00 38.85 ? 377 ASN   A C   1 
ATOM   1861 O  O   . ASN   A 1 246 ? -9.648  14.922  -26.636 1.00 39.63 ? 377 ASN   A O   1 
ATOM   1862 C  CB  . ASN   A 1 246 ? -6.848  14.777  -25.469 1.00 39.26 ? 377 ASN   A CB  1 
ATOM   1863 C  CG  . ASN   A 1 246 ? -5.974  14.449  -26.672 1.00 40.70 ? 377 ASN   A CG  1 
ATOM   1864 O  OD1 . ASN   A 1 246 ? -6.483  14.116  -27.743 1.00 40.13 ? 377 ASN   A OD1 1 
ATOM   1865 N  ND2 . ASN   A 1 246 ? -4.658  14.582  -26.512 1.00 40.71 ? 377 ASN   A ND2 1 
ATOM   1866 N  N   . CYS   A 1 247 ? -8.543  16.390  -27.955 1.00 40.38 ? 378 CYS   A N   1 
ATOM   1867 C  CA  . CYS   A 1 247 ? -9.429  16.279  -29.107 1.00 39.95 ? 378 CYS   A CA  1 
ATOM   1868 C  C   . CYS   A 1 247 ? -8.607  15.844  -30.315 1.00 40.25 ? 378 CYS   A C   1 
ATOM   1869 O  O   . CYS   A 1 247 ? -7.706  16.570  -30.750 1.00 40.36 ? 378 CYS   A O   1 
ATOM   1870 C  CB  . CYS   A 1 247 ? -10.131 17.615  -29.374 1.00 45.29 ? 378 CYS   A CB  1 
ATOM   1871 S  SG  . CYS   A 1 247 ? -11.097 17.677  -30.897 1.00 51.81 ? 378 CYS   A SG  1 
ATOM   1872 N  N   . ARG   A 1 248 ? -8.924  14.667  -30.859 1.00 42.05 ? 379 ARG   A N   1 
ATOM   1873 C  CA  . ARG   A 1 248 ? -8.190  14.102  -31.996 1.00 42.54 ? 379 ARG   A CA  1 
ATOM   1874 C  C   . ARG   A 1 248 ? -6.694  14.015  -31.707 1.00 40.63 ? 379 ARG   A C   1 
ATOM   1875 O  O   . ARG   A 1 248 ? -5.864  14.182  -32.604 1.00 40.25 ? 379 ARG   A O   1 
ATOM   1876 C  CB  . ARG   A 1 248 ? -8.419  14.907  -33.282 1.00 43.77 ? 379 ARG   A CB  1 
ATOM   1877 C  CG  . ARG   A 1 248 ? -9.860  15.271  -33.616 1.00 49.25 ? 379 ARG   A CG  1 
ATOM   1878 C  CD  . ARG   A 1 248 ? -10.790 14.079  -33.690 1.00 50.07 ? 379 ARG   A CD  1 
ATOM   1879 N  NE  . ARG   A 1 248 ? -12.170 14.518  -33.870 1.00 56.12 ? 379 ARG   A NE  1 
ATOM   1880 C  CZ  . ARG   A 1 248 ? -13.221 13.971  -33.274 1.00 59.39 ? 379 ARG   A CZ  1 
ATOM   1881 N  NH1 . ARG   A 1 248 ? -13.095 12.925  -32.471 1.00 57.27 ? 379 ARG   A NH1 1 
ATOM   1882 N  NH2 . ARG   A 1 248 ? -14.429 14.488  -33.484 1.00 55.42 ? 379 ARG   A NH2 1 
ATOM   1883 N  N   . GLY   A 1 249 ? -6.333  13.771  -30.449 1.00 38.95 ? 380 GLY   A N   1 
ATOM   1884 C  CA  . GLY   A 1 249 ? -4.942  13.691  -30.061 1.00 38.17 ? 380 GLY   A CA  1 
ATOM   1885 C  C   . GLY   A 1 249 ? -4.256  15.015  -29.792 1.00 40.53 ? 380 GLY   A C   1 
ATOM   1886 O  O   . GLY   A 1 249 ? -3.071  15.014  -29.437 1.00 40.26 ? 380 GLY   A O   1 
ATOM   1887 N  N   . GLU   A 1 250 ? -4.950  16.139  -29.946 1.00 37.15 ? 381 GLU   A N   1 
ATOM   1888 C  CA  . GLU   A 1 250 ? -4.395  17.449  -29.633 1.00 38.61 ? 381 GLU   A CA  1 
ATOM   1889 C  C   . GLU   A 1 250 ? -4.936  17.935  -28.293 1.00 36.18 ? 381 GLU   A C   1 
ATOM   1890 O  O   . GLU   A 1 250 ? -6.106  17.716  -27.968 1.00 36.63 ? 381 GLU   A O   1 
ATOM   1891 C  CB  . GLU   A 1 250 ? -4.730  18.457  -30.733 1.00 38.33 ? 381 GLU   A CB  1 
ATOM   1892 C  CG  . GLU   A 1 250 ? -4.299  18.017  -32.132 1.00 42.45 ? 381 GLU   A CG  1 
ATOM   1893 C  CD  . GLU   A 1 250 ? -2.793  18.098  -32.331 1.00 46.53 ? 381 GLU   A CD  1 
ATOM   1894 O  OE1 . GLU   A 1 250 ? -2.214  17.184  -32.969 1.00 49.70 ? 381 GLU   A OE1 1 
ATOM   1895 O  OE2 . GLU   A 1 250 ? -2.191  19.079  -31.847 1.00 45.73 ? 381 GLU   A OE2 1 
ATOM   1896 N  N   . PHE   A 1 251 ? -4.082  18.603  -27.521 1.00 36.19 ? 382 PHE   A N   1 
ATOM   1897 C  CA  . PHE   A 1 251 ? -4.433  19.057  -26.177 1.00 34.98 ? 382 PHE   A CA  1 
ATOM   1898 C  C   . PHE   A 1 251 ? -5.025  20.463  -26.242 1.00 37.14 ? 382 PHE   A C   1 
ATOM   1899 O  O   . PHE   A 1 251 ? -4.309  21.440  -26.496 1.00 36.19 ? 382 PHE   A O   1 
ATOM   1900 C  CB  . PHE   A 1 251 ? -3.209  19.015  -25.267 1.00 35.63 ? 382 PHE   A CB  1 
ATOM   1901 C  CG  . PHE   A 1 251 ? -2.739  17.623  -24.964 1.00 35.83 ? 382 PHE   A CG  1 
ATOM   1902 C  CD1 . PHE   A 1 251 ? -3.270  16.912  -23.899 1.00 38.23 ? 382 PHE   A CD1 1 
ATOM   1903 C  CD2 . PHE   A 1 251 ? -1.789  17.011  -25.764 1.00 38.02 ? 382 PHE   A CD2 1 
ATOM   1904 C  CE1 . PHE   A 1 251 ? -2.848  15.622  -23.626 1.00 39.86 ? 382 PHE   A CE1 1 
ATOM   1905 C  CE2 . PHE   A 1 251 ? -1.362  15.722  -25.498 1.00 38.16 ? 382 PHE   A CE2 1 
ATOM   1906 C  CZ  . PHE   A 1 251 ? -1.891  15.026  -24.428 1.00 39.53 ? 382 PHE   A CZ  1 
ATOM   1907 N  N   . PHE   A 1 252 ? -6.327  20.568  -25.982 1.00 36.22 ? 383 PHE   A N   1 
ATOM   1908 C  CA  . PHE   A 1 252 ? -7.017  21.851  -25.936 1.00 34.76 ? 383 PHE   A CA  1 
ATOM   1909 C  C   . PHE   A 1 252 ? -7.013  22.416  -24.519 1.00 38.64 ? 383 PHE   A C   1 
ATOM   1910 O  O   . PHE   A 1 252 ? -7.256  21.694  -23.544 1.00 35.68 ? 383 PHE   A O   1 
ATOM   1911 C  CB  . PHE   A 1 252 ? -8.462  21.706  -26.416 1.00 38.52 ? 383 PHE   A CB  1 
ATOM   1912 C  CG  . PHE   A 1 252 ? -8.617  21.692  -27.920 1.00 37.72 ? 383 PHE   A CG  1 
ATOM   1913 C  CD1 . PHE   A 1 252 ? -7.990  20.723  -28.686 1.00 35.47 ? 383 PHE   A CD1 1 
ATOM   1914 C  CD2 . PHE   A 1 252 ? -9.398  22.640  -28.560 1.00 39.70 ? 383 PHE   A CD2 1 
ATOM   1915 C  CE1 . PHE   A 1 252 ? -8.136  20.700  -30.069 1.00 41.13 ? 383 PHE   A CE1 1 
ATOM   1916 C  CE2 . PHE   A 1 252 ? -9.547  22.626  -29.941 1.00 39.53 ? 383 PHE   A CE2 1 
ATOM   1917 C  CZ  . PHE   A 1 252 ? -8.915  21.656  -30.693 1.00 41.14 ? 383 PHE   A CZ  1 
ATOM   1918 N  N   . TYR   A 1 253 ? -6.744  23.718  -24.419 1.00 37.47 ? 384 TYR   A N   1 
ATOM   1919 C  CA  . TYR   A 1 253 ? -6.855  24.483  -23.181 1.00 36.59 ? 384 TYR   A CA  1 
ATOM   1920 C  C   . TYR   A 1 253 ? -7.845  25.612  -23.429 1.00 37.49 ? 384 TYR   A C   1 
ATOM   1921 O  O   . TYR   A 1 253 ? -7.612  26.468  -24.290 1.00 39.04 ? 384 TYR   A O   1 
ATOM   1922 C  CB  . TYR   A 1 253 ? -5.497  25.040  -22.741 1.00 37.85 ? 384 TYR   A CB  1 
ATOM   1923 C  CG  . TYR   A 1 253 ? -4.521  23.993  -22.238 1.00 39.42 ? 384 TYR   A CG  1 
ATOM   1924 C  CD1 . TYR   A 1 253 ? -4.097  22.956  -23.060 1.00 37.23 ? 384 TYR   A CD1 1 
ATOM   1925 C  CD2 . TYR   A 1 253 ? -4.018  24.047  -20.943 1.00 37.53 ? 384 TYR   A CD2 1 
ATOM   1926 C  CE1 . TYR   A 1 253 ? -3.206  21.997  -22.607 1.00 39.70 ? 384 TYR   A CE1 1 
ATOM   1927 C  CE2 . TYR   A 1 253 ? -3.119  23.085  -20.478 1.00 39.04 ? 384 TYR   A CE2 1 
ATOM   1928 C  CZ  . TYR   A 1 253 ? -2.719  22.061  -21.322 1.00 37.33 ? 384 TYR   A CZ  1 
ATOM   1929 O  OH  . TYR   A 1 253 ? -1.835  21.091  -20.903 1.00 40.72 ? 384 TYR   A OH  1 
ATOM   1930 N  N   . CYS   A 1 254 ? -8.953  25.606  -22.695 1.00 37.47 ? 385 CYS   A N   1 
ATOM   1931 C  CA  . CYS   A 1 254 ? -10.059 26.513  -22.964 1.00 39.22 ? 385 CYS   A CA  1 
ATOM   1932 C  C   . CYS   A 1 254 ? -10.365 27.355  -21.733 1.00 39.81 ? 385 CYS   A C   1 
ATOM   1933 O  O   . CYS   A 1 254 ? -10.467 26.832  -20.615 1.00 35.77 ? 385 CYS   A O   1 
ATOM   1934 C  CB  . CYS   A 1 254 ? -11.292 25.733  -23.424 1.00 38.86 ? 385 CYS   A CB  1 
ATOM   1935 S  SG  . CYS   A 1 254 ? -11.076 25.012  -25.061 1.00 45.53 ? 385 CYS   A SG  1 
ATOM   1936 N  N   . ASN   A 1 255 ? -10.491 28.660  -21.949 1.00 39.36 ? 386 ASN   A N   1 
ATOM   1937 C  CA  . ASN   A 1 255 ? -10.780 29.610  -20.883 1.00 40.59 ? 386 ASN   A CA  1 
ATOM   1938 C  C   . ASN   A 1 255 ? -12.267 29.562  -20.558 1.00 37.56 ? 386 ASN   A C   1 
ATOM   1939 O  O   . ASN   A 1 255 ? -13.106 29.852  -21.418 1.00 39.93 ? 386 ASN   A O   1 
ATOM   1940 C  CB  . ASN   A 1 255 ? -10.354 31.007  -21.325 1.00 44.17 ? 386 ASN   A CB  1 
ATOM   1941 C  CG  . ASN   A 1 255 ? -10.472 32.042  -20.225 1.00 45.98 ? 386 ASN   A CG  1 
ATOM   1942 O  OD1 . ASN   A 1 255 ? -11.407 32.022  -19.422 1.00 46.29 ? 386 ASN   A OD1 1 
ATOM   1943 N  ND2 . ASN   A 1 255 ? -9.518  32.962  -20.190 1.00 45.54 ? 386 ASN   A ND2 1 
ATOM   1944 N  N   . THR   A 1 256 ? -12.595 29.194  -19.322 1.00 40.32 ? 387 THR   A N   1 
ATOM   1945 C  CA  . THR   A 1 256 ? -13.976 29.018  -18.896 1.00 41.04 ? 387 THR   A CA  1 
ATOM   1946 C  C   . THR   A 1 256 ? -14.482 30.187  -18.054 1.00 40.75 ? 387 THR   A C   1 
ATOM   1947 O  O   . THR   A 1 256 ? -15.487 30.043  -17.352 1.00 41.76 ? 387 THR   A O   1 
ATOM   1948 C  CB  . THR   A 1 256 ? -14.122 27.714  -18.109 1.00 39.15 ? 387 THR   A CB  1 
ATOM   1949 O  OG1 . THR   A 1 256 ? -13.170 27.706  -17.037 1.00 36.80 ? 387 THR   A OG1 1 
ATOM   1950 C  CG2 . THR   A 1 256 ? -13.898 26.489  -19.010 1.00 37.57 ? 387 THR   A CG2 1 
ATOM   1951 N  N   . THR   A 1 257 ? -13.793 31.331  -18.090 1.00 38.59 ? 388 THR   A N   1 
ATOM   1952 C  CA  . THR   A 1 257 ? -14.237 32.485  -17.309 1.00 47.17 ? 388 THR   A CA  1 
ATOM   1953 C  C   . THR   A 1 257 ? -15.680 32.852  -17.636 1.00 46.04 ? 388 THR   A C   1 
ATOM   1954 O  O   . THR   A 1 257 ? -16.455 33.209  -16.742 1.00 45.28 ? 388 THR   A O   1 
ATOM   1955 C  CB  . THR   A 1 257 ? -13.312 33.683  -17.556 1.00 47.32 ? 388 THR   A CB  1 
ATOM   1956 O  OG1 . THR   A 1 257 ? -12.024 33.430  -16.975 1.00 51.73 ? 388 THR   A OG1 1 
ATOM   1957 C  CG2 . THR   A 1 257 ? -13.897 34.951  -16.937 1.00 53.49 ? 388 THR   A CG2 1 
ATOM   1958 N  N   . GLN   A 1 258 ? -16.061 32.764  -18.912 1.00 44.50 ? 389 GLN   A N   1 
ATOM   1959 C  CA  . GLN   A 1 258 ? -17.417 33.110  -19.322 1.00 45.98 ? 389 GLN   A CA  1 
ATOM   1960 C  C   . GLN   A 1 258 ? -18.448 32.104  -18.836 1.00 46.29 ? 389 GLN   A C   1 
ATOM   1961 O  O   . GLN   A 1 258 ? -19.645 32.410  -18.843 1.00 45.28 ? 389 GLN   A O   1 
ATOM   1962 C  CB  . GLN   A 1 258 ? -17.492 33.211  -20.843 1.00 43.98 ? 389 GLN   A CB  1 
ATOM   1963 C  CG  . GLN   A 1 258 ? -16.769 34.404  -21.420 1.00 45.02 ? 389 GLN   A CG  1 
ATOM   1964 C  CD  . GLN   A 1 258 ? -16.893 34.465  -22.923 1.00 45.40 ? 389 GLN   A CD  1 
ATOM   1965 O  OE1 . GLN   A 1 258 ? -17.924 34.876  -23.459 1.00 49.51 ? 389 GLN   A OE1 1 
ATOM   1966 N  NE2 . GLN   A 1 258 ? -15.847 34.034  -23.616 1.00 44.40 ? 389 GLN   A NE2 1 
ATOM   1967 N  N   . LEU   A 1 259 ? -18.016 30.905  -18.445 1.00 44.38 ? 390 LEU   A N   1 
ATOM   1968 C  CA  . LEU   A 1 259 ? -18.945 29.925  -17.897 1.00 42.05 ? 390 LEU   A CA  1 
ATOM   1969 C  C   . LEU   A 1 259 ? -19.161 30.141  -16.404 1.00 47.30 ? 390 LEU   A C   1 
ATOM   1970 O  O   . LEU   A 1 259 ? -20.289 30.030  -15.908 1.00 47.36 ? 390 LEU   A O   1 
ATOM   1971 C  CB  . LEU   A 1 259 ? -18.424 28.510  -18.156 1.00 45.00 ? 390 LEU   A CB  1 
ATOM   1972 C  CG  . LEU   A 1 259 ? -18.528 27.974  -19.586 1.00 43.99 ? 390 LEU   A CG  1 
ATOM   1973 C  CD1 . LEU   A 1 259 ? -18.307 26.473  -19.602 1.00 44.47 ? 390 LEU   A CD1 1 
ATOM   1974 C  CD2 . LEU   A 1 259 ? -19.873 28.336  -20.221 1.00 43.55 ? 390 LEU   A CD2 1 
ATOM   1975 N  N   . PHE   A 1 260 ? -18.096 30.450  -15.670 1.00 46.06 ? 391 PHE   A N   1 
ATOM   1976 C  CA  . PHE   A 1 260 ? -18.171 30.575  -14.218 1.00 48.67 ? 391 PHE   A CA  1 
ATOM   1977 C  C   . PHE   A 1 260 ? -18.146 32.030  -13.784 1.00 55.12 ? 391 PHE   A C   1 
ATOM   1978 O  O   . PHE   A 1 260 ? -17.450 32.431  -12.844 1.00 55.05 ? 391 PHE   A O   1 
ATOM   1979 C  CB  . PHE   A 1 260 ? -17.064 29.751  -13.580 1.00 46.42 ? 391 PHE   A CB  1 
ATOM   1980 C  CG  . PHE   A 1 260 ? -17.214 28.284  -13.855 1.00 46.32 ? 391 PHE   A CG  1 
ATOM   1981 C  CD1 . PHE   A 1 260 ? -18.158 27.537  -13.172 1.00 45.87 ? 391 PHE   A CD1 1 
ATOM   1982 C  CD2 . PHE   A 1 260 ? -16.465 27.667  -14.841 1.00 43.81 ? 391 PHE   A CD2 1 
ATOM   1983 C  CE1 . PHE   A 1 260 ? -18.326 26.192  -13.436 1.00 41.24 ? 391 PHE   A CE1 1 
ATOM   1984 C  CE2 . PHE   A 1 260 ? -16.625 26.320  -15.110 1.00 42.00 ? 391 PHE   A CE2 1 
ATOM   1985 C  CZ  . PHE   A 1 260 ? -17.557 25.583  -14.405 1.00 44.78 ? 391 PHE   A CZ  1 
ATOM   1986 N  N   . ASN   A 1 261 ? -18.919 32.830  -14.509 1.00 59.44 ? 392 ASN   A N   1 
ATOM   1987 C  CA  . ASN   A 1 261 ? -19.339 34.156  -14.093 1.00 64.51 ? 392 ASN   A CA  1 
ATOM   1988 C  C   . ASN   A 1 261 ? -20.775 34.064  -13.590 1.00 70.34 ? 392 ASN   A C   1 
ATOM   1989 O  O   . ASN   A 1 261 ? -21.591 33.323  -14.147 1.00 70.34 ? 392 ASN   A O   1 
ATOM   1990 C  CB  . ASN   A 1 261 ? -19.239 35.145  -15.258 1.00 61.04 ? 392 ASN   A CB  1 
ATOM   1991 C  CG  . ASN   A 1 261 ? -17.967 35.969  -15.212 1.00 63.13 ? 392 ASN   A CG  1 
ATOM   1992 O  OD1 . ASN   A 1 261 ? -17.208 35.907  -14.239 1.00 60.11 ? 392 ASN   A OD1 1 
ATOM   1993 N  ND2 . ASN   A 1 261 ? -17.722 36.744  -16.267 1.00 64.06 ? 392 ASN   A ND2 1 
ATOM   1994 N  N   . ASN   A 1 262 ? -21.074 34.791  -12.519 1.00 72.19 ? 393 ASN   A N   1 
ATOM   1995 C  CA  . ASN   A 1 262 ? -22.426 34.824  -11.982 1.00 75.24 ? 393 ASN   A CA  1 
ATOM   1996 C  C   . ASN   A 1 262 ? -23.283 35.898  -12.636 1.00 79.55 ? 393 ASN   A C   1 
ATOM   1997 O  O   . ASN   A 1 262 ? -24.389 36.172  -12.156 1.00 82.12 ? 393 ASN   A O   1 
ATOM   1998 C  CB  . ASN   A 1 262 ? -22.387 35.027  -10.465 1.00 73.51 ? 393 ASN   A CB  1 
ATOM   1999 C  CG  . ASN   A 1 262 ? -21.760 33.855  -9.744  1.00 65.07 ? 393 ASN   A CG  1 
ATOM   2000 O  OD1 . ASN   A 1 262 ? -22.446 32.906  -9.351  1.00 62.00 ? 393 ASN   A OD1 1 
ATOM   2001 N  ND2 . ASN   A 1 262 ? -20.445 33.911  -9.568  1.00 62.81 ? 393 ASN   A ND2 1 
ATOM   2002 N  N   . THR   A 1 263 ? -22.793 36.501  -13.722 1.00 79.44 ? 394 THR   A N   1 
ATOM   2003 C  CA  . THR   A 1 263 ? -23.515 37.572  -14.401 1.00 81.65 ? 394 THR   A CA  1 
ATOM   2004 C  C   . THR   A 1 263 ? -24.961 37.174  -14.677 1.00 83.24 ? 394 THR   A C   1 
ATOM   2005 O  O   . THR   A 1 263 ? -25.904 37.836  -14.228 1.00 83.17 ? 394 THR   A O   1 
ATOM   2006 C  CB  . THR   A 1 263 ? -22.799 37.935  -15.709 1.00 84.14 ? 394 THR   A CB  1 
ATOM   2007 O  OG1 . THR   A 1 263 ? -22.081 36.796  -16.206 1.00 81.69 ? 394 THR   A OG1 1 
ATOM   2008 C  CG2 . THR   A 1 263 ? -21.832 39.093  -15.500 1.00 80.18 ? 394 THR   A CG2 1 
ATOM   2009 N  N   . CYS   A 1 264 ? -25.151 36.086  -15.417 1.00 84.08 ? 395 CYS   A N   1 
ATOM   2010 C  CA  . CYS   A 1 264 ? -26.488 35.630  -15.778 1.00 82.49 ? 395 CYS   A CA  1 
ATOM   2011 C  C   . CYS   A 1 264 ? -26.963 34.534  -14.834 1.00 81.49 ? 395 CYS   A C   1 
ATOM   2012 O  O   . CYS   A 1 264 ? -28.025 33.950  -15.041 1.00 82.15 ? 395 CYS   A O   1 
ATOM   2013 C  CB  . CYS   A 1 264 ? -26.514 35.125  -17.223 1.00 81.28 ? 395 CYS   A CB  1 
ATOM   2014 S  SG  . CYS   A 1 264 ? -25.259 35.866  -18.303 1.00 88.20 ? 395 CYS   A SG  1 
ATOM   2015 N  N   . LYS   A 1 271 ? -28.513 41.376  -17.476 1.00 68.91 ? 408 LYS   A N   1 
ATOM   2016 C  CA  . LYS   A 1 271 ? -28.634 40.309  -18.462 1.00 74.26 ? 408 LYS   A CA  1 
ATOM   2017 C  C   . LYS   A 1 271 ? -28.265 40.799  -19.861 1.00 78.18 ? 408 LYS   A C   1 
ATOM   2018 O  O   . LYS   A 1 271 ? -27.287 41.532  -20.034 1.00 77.91 ? 408 LYS   A O   1 
ATOM   2019 C  CB  . LYS   A 1 271 ? -30.049 39.722  -18.449 1.00 72.81 ? 408 LYS   A CB  1 
ATOM   2020 C  CG  . LYS   A 1 271 ? -30.282 38.763  -17.288 1.00 68.99 ? 408 LYS   A CG  1 
ATOM   2021 C  CD  . LYS   A 1 271 ? -31.727 38.801  -16.793 1.00 65.41 ? 408 LYS   A CD  1 
ATOM   2022 C  CE  . LYS   A 1 271 ? -32.575 37.754  -17.491 1.00 61.53 ? 408 LYS   A CE  1 
ATOM   2023 N  NZ  . LYS   A 1 271 ? -33.300 38.340  -18.658 1.00 59.15 ? 408 LYS   A NZ  1 
ATOM   2024 N  N   . GLY   A 1 272 ? -29.063 40.421  -20.856 1.00 78.05 ? 409 GLY   A N   1 
ATOM   2025 C  CA  . GLY   A 1 272 ? -28.612 40.597  -22.221 1.00 76.64 ? 409 GLY   A CA  1 
ATOM   2026 C  C   . GLY   A 1 272 ? -27.549 39.599  -22.617 1.00 80.40 ? 409 GLY   A C   1 
ATOM   2027 O  O   . GLY   A 1 272 ? -26.800 39.836  -23.572 1.00 78.24 ? 409 GLY   A O   1 
ATOM   2028 N  N   . CYS   A 1 273 ? -27.472 38.482  -21.892 1.00 82.30 ? 410 CYS   A N   1 
ATOM   2029 C  CA  . CYS   A 1 273 ? -26.456 37.444  -22.055 1.00 80.25 ? 410 CYS   A CA  1 
ATOM   2030 C  C   . CYS   A 1 273 ? -27.181 36.101  -22.118 1.00 78.39 ? 410 CYS   A C   1 
ATOM   2031 O  O   . CYS   A 1 273 ? -27.550 35.537  -21.083 1.00 81.27 ? 410 CYS   A O   1 
ATOM   2032 C  CB  . CYS   A 1 273 ? -25.457 37.484  -20.902 1.00 81.02 ? 410 CYS   A CB  1 
ATOM   2033 S  SG  . CYS   A 1 273 ? -26.236 37.376  -19.254 1.00 88.27 ? 410 CYS   A SG  1 
ATOM   2034 N  N   . ASN   A 1 274 ? -27.384 35.586  -23.329 1.00 75.96 ? 411 ASN   A N   1 
ATOM   2035 C  CA  . ASN   A 1 274 ? -28.130 34.345  -23.492 1.00 70.75 ? 411 ASN   A CA  1 
ATOM   2036 C  C   . ASN   A 1 274 ? -27.896 33.723  -24.864 1.00 67.26 ? 411 ASN   A C   1 
ATOM   2037 O  O   . ASN   A 1 274 ? -28.567 32.753  -25.234 1.00 66.89 ? 411 ASN   A O   1 
ATOM   2038 C  CB  . ASN   A 1 274 ? -29.620 34.603  -23.273 1.00 72.63 ? 411 ASN   A CB  1 
ATOM   2039 C  CG  . ASN   A 1 274 ? -30.320 35.037  -24.543 1.00 78.65 ? 411 ASN   A CG  1 
ATOM   2040 O  OD1 . ASN   A 1 274 ? -29.921 36.015  -25.182 1.00 81.66 ? 411 ASN   A OD1 1 
ATOM   2041 N  ND2 . ASN   A 1 274 ? -31.361 34.308  -24.926 1.00 79.99 ? 411 ASN   A ND2 1 
ATOM   2042 N  N   . GLY   A 1 275 ? -26.954 34.271  -25.624 1.00 65.69 ? 412 GLY   A N   1 
ATOM   2043 C  CA  . GLY   A 1 275 ? -26.603 33.745  -26.926 1.00 59.37 ? 412 GLY   A CA  1 
ATOM   2044 C  C   . GLY   A 1 275 ? -25.520 32.686  -26.853 1.00 55.37 ? 412 GLY   A C   1 
ATOM   2045 O  O   . GLY   A 1 275 ? -25.239 32.114  -25.796 1.00 53.39 ? 412 GLY   A O   1 
ATOM   2046 N  N   . THR   A 1 276 ? -24.906 32.424  -28.006 1.00 53.26 ? 413 THR   A N   1 
ATOM   2047 C  CA  . THR   A 1 276 ? -23.815 31.458  -28.086 1.00 50.78 ? 413 THR   A CA  1 
ATOM   2048 C  C   . THR   A 1 276 ? -22.605 31.984  -27.321 1.00 49.86 ? 413 THR   A C   1 
ATOM   2049 O  O   . THR   A 1 276 ? -22.116 33.082  -27.605 1.00 51.98 ? 413 THR   A O   1 
ATOM   2050 C  CB  . THR   A 1 276 ? -23.444 31.194  -29.548 1.00 52.40 ? 413 THR   A CB  1 
ATOM   2051 O  OG1 . THR   A 1 276 ? -24.419 30.338  -30.160 1.00 52.13 ? 413 THR   A OG1 1 
ATOM   2052 C  CG2 . THR   A 1 276 ? -22.058 30.546  -29.652 1.00 49.70 ? 413 THR   A CG2 1 
ATOM   2053 N  N   . ILE   A 1 277 ? -22.119 31.213  -26.353 1.00 47.69 ? 414 ILE   A N   1 
ATOM   2054 C  CA  . ILE   A 1 277 ? -20.910 31.570  -25.619 1.00 46.71 ? 414 ILE   A CA  1 
ATOM   2055 C  C   . ILE   A 1 277 ? -19.708 31.022  -26.377 1.00 47.79 ? 414 ILE   A C   1 
ATOM   2056 O  O   . ILE   A 1 277 ? -19.648 29.824  -26.678 1.00 45.11 ? 414 ILE   A O   1 
ATOM   2057 C  CB  . ILE   A 1 277 ? -20.945 31.022  -24.183 1.00 48.44 ? 414 ILE   A CB  1 
ATOM   2058 C  CG1 . ILE   A 1 277 ? -22.247 31.415  -23.480 1.00 50.28 ? 414 ILE   A CG1 1 
ATOM   2059 C  CG2 . ILE   A 1 277 ? -19.724 31.510  -23.393 1.00 47.13 ? 414 ILE   A CG2 1 
ATOM   2060 C  CD1 . ILE   A 1 277 ? -22.351 30.909  -22.052 1.00 45.95 ? 414 ILE   A CD1 1 
ATOM   2061 N  N   . THR   A 1 278 ? -18.745 31.890  -26.681 1.00 46.87 ? 415 THR   A N   1 
ATOM   2062 C  CA  . THR   A 1 278 ? -17.545 31.497  -27.413 1.00 45.27 ? 415 THR   A CA  1 
ATOM   2063 C  C   . THR   A 1 278 ? -16.348 31.571  -26.471 1.00 45.06 ? 415 THR   A C   1 
ATOM   2064 O  O   . THR   A 1 278 ? -15.897 32.661  -26.105 1.00 45.58 ? 415 THR   A O   1 
ATOM   2065 C  CB  . THR   A 1 278 ? -17.347 32.371  -28.651 1.00 48.13 ? 415 THR   A CB  1 
ATOM   2066 O  OG1 . THR   A 1 278 ? -18.489 32.238  -29.507 1.00 50.99 ? 415 THR   A OG1 1 
ATOM   2067 C  CG2 . THR   A 1 278 ? -16.099 31.941  -29.421 1.00 47.50 ? 415 THR   A CG2 1 
ATOM   2068 N  N   . LEU   A 1 279 ? -15.845 30.410  -26.077 1.00 43.83 ? 416 LEU   A N   1 
ATOM   2069 C  CA  . LEU   A 1 279 ? -14.680 30.315  -25.211 1.00 42.19 ? 416 LEU   A CA  1 
ATOM   2070 C  C   . LEU   A 1 279 ? -13.416 30.350  -26.060 1.00 42.15 ? 416 LEU   A C   1 
ATOM   2071 O  O   . LEU   A 1 279 ? -13.334 29.627  -27.060 1.00 40.97 ? 416 LEU   A O   1 
ATOM   2072 C  CB  . LEU   A 1 279 ? -14.725 29.029  -24.398 1.00 38.75 ? 416 LEU   A CB  1 
ATOM   2073 C  CG  . LEU   A 1 279 ? -15.969 28.834  -23.522 1.00 42.34 ? 416 LEU   A CG  1 
ATOM   2074 C  CD1 . LEU   A 1 279 ? -15.950 27.472  -22.850 1.00 39.75 ? 416 LEU   A CD1 1 
ATOM   2075 C  CD2 . LEU   A 1 279 ? -16.095 29.939  -22.482 1.00 39.77 ? 416 LEU   A CD2 1 
ATOM   2076 N  N   . PRO   A 1 280 ? -12.429 31.179  -25.718 1.00 39.54 ? 417 PRO   A N   1 
ATOM   2077 C  CA  . PRO   A 1 280 ? -11.155 31.155  -26.450 1.00 40.30 ? 417 PRO   A CA  1 
ATOM   2078 C  C   . PRO   A 1 280 ? -10.289 29.997  -25.970 1.00 39.22 ? 417 PRO   A C   1 
ATOM   2079 O  O   . PRO   A 1 280 ? -10.151 29.765  -24.767 1.00 39.85 ? 417 PRO   A O   1 
ATOM   2080 C  CB  . PRO   A 1 280 ? -10.526 32.507  -26.103 1.00 41.92 ? 417 PRO   A CB  1 
ATOM   2081 C  CG  . PRO   A 1 280 ? -11.040 32.789  -24.712 1.00 42.13 ? 417 PRO   A CG  1 
ATOM   2082 C  CD  . PRO   A 1 280 ? -12.449 32.218  -24.672 1.00 43.54 ? 417 PRO   A CD  1 
ATOM   2083 N  N   . CYS   A 1 281 ? -9.699  29.272  -26.916 1.00 37.03 ? 418 CYS   A N   1 
ATOM   2084 C  CA  . CYS   A 1 281 ? -8.915  28.086  -26.608 1.00 39.81 ? 418 CYS   A CA  1 
ATOM   2085 C  C   . CYS   A 1 281 ? -7.571  28.134  -27.322 1.00 40.97 ? 418 CYS   A C   1 
ATOM   2086 O  O   . CYS   A 1 281 ? -7.380  28.862  -28.300 1.00 39.11 ? 418 CYS   A O   1 
ATOM   2087 C  CB  . CYS   A 1 281 ? -9.653  26.804  -27.011 1.00 45.15 ? 418 CYS   A CB  1 
ATOM   2088 S  SG  . CYS   A 1 281 ? -11.289 26.612  -26.301 1.00 48.71 ? 418 CYS   A SG  1 
ATOM   2089 N  N   . LYS   A 1 282 ? -6.636  27.337  -26.813 1.00 37.66 ? 419 LYS   A N   1 
ATOM   2090 C  CA  . LYS   A 1 282 ? -5.330  27.153  -27.427 1.00 40.12 ? 419 LYS   A CA  1 
ATOM   2091 C  C   . LYS   A 1 282 ? -5.003  25.668  -27.444 1.00 38.94 ? 419 LYS   A C   1 
ATOM   2092 O  O   . LYS   A 1 282 ? -5.326  24.942  -26.498 1.00 36.66 ? 419 LYS   A O   1 
ATOM   2093 C  CB  . LYS   A 1 282 ? -4.227  27.909  -26.668 1.00 39.54 ? 419 LYS   A CB  1 
ATOM   2094 C  CG  . LYS   A 1 282 ? -4.398  29.421  -26.606 1.00 42.10 ? 419 LYS   A CG  1 
ATOM   2095 C  CD  . LYS   A 1 282 ? -3.257  30.063  -25.815 1.00 48.16 ? 419 LYS   A CD  1 
ATOM   2096 C  CE  . LYS   A 1 282 ? -3.550  31.524  -25.487 1.00 46.73 ? 419 LYS   A CE  1 
ATOM   2097 N  NZ  . LYS   A 1 282 ? -3.684  31.756  -24.016 1.00 47.97 ? 419 LYS   A NZ  1 
ATOM   2098 N  N   . ILE   A 1 283 ? -4.377  25.219  -28.525 1.00 35.99 ? 420 ILE   A N   1 
ATOM   2099 C  CA  . ILE   A 1 283 ? -3.781  23.891  -28.570 1.00 37.55 ? 420 ILE   A CA  1 
ATOM   2100 C  C   . ILE   A 1 283 ? -2.366  24.026  -28.028 1.00 34.73 ? 420 ILE   A C   1 
ATOM   2101 O  O   . ILE   A 1 283 ? -1.571  24.819  -28.541 1.00 36.91 ? 420 ILE   A O   1 
ATOM   2102 C  CB  . ILE   A 1 283 ? -3.785  23.320  -29.996 1.00 35.55 ? 420 ILE   A CB  1 
ATOM   2103 C  CG1 . ILE   A 1 283 ? -5.203  23.341  -30.577 1.00 38.69 ? 420 ILE   A CG1 1 
ATOM   2104 C  CG2 . ILE   A 1 283 ? -3.231  21.904  -30.005 1.00 36.14 ? 420 ILE   A CG2 1 
ATOM   2105 C  CD1 . ILE   A 1 283 ? -5.442  22.305  -31.675 1.00 34.36 ? 420 ILE   A CD1 1 
ATOM   2106 N  N   . LYS   A 1 284 ? -2.058  23.283  -26.974 1.00 37.91 ? 421 LYS   A N   1 
ATOM   2107 C  CA  . LYS   A 1 284 ? -0.757  23.362  -26.329 1.00 38.15 ? 421 LYS   A CA  1 
ATOM   2108 C  C   . LYS   A 1 284 ? 0.115   22.188  -26.748 1.00 41.23 ? 421 LYS   A C   1 
ATOM   2109 O  O   . LYS   A 1 284 ? -0.370  21.064  -26.909 1.00 36.87 ? 421 LYS   A O   1 
ATOM   2110 C  CB  . LYS   A 1 284 ? -0.902  23.390  -24.806 1.00 39.65 ? 421 LYS   A CB  1 
ATOM   2111 C  CG  . LYS   A 1 284 ? -0.918  24.793  -24.209 1.00 40.09 ? 421 LYS   A CG  1 
ATOM   2112 C  CD  . LYS   A 1 284 ? -0.512  24.771  -22.739 1.00 39.05 ? 421 LYS   A CD  1 
ATOM   2113 C  CE  . LYS   A 1 284 ? 0.992   24.959  -22.573 1.00 36.45 ? 421 LYS   A CE  1 
ATOM   2114 N  NZ  . LYS   A 1 284 ? 1.361   26.398  -22.618 1.00 42.58 ? 421 LYS   A NZ  1 
ATOM   2115 N  N   . GLN   A 1 285 ? 1.408   22.462  -26.926 1.00 42.94 ? 422 GLN   A N   1 
ATOM   2116 C  CA  . GLN   A 1 285 ? 2.415   21.444  -27.196 1.00 40.94 ? 422 GLN   A CA  1 
ATOM   2117 C  C   . GLN   A 1 285 ? 3.108   20.949  -25.935 1.00 42.90 ? 422 GLN   A C   1 
ATOM   2118 O  O   . GLN   A 1 285 ? 3.465   19.770  -25.853 1.00 44.01 ? 422 GLN   A O   1 
ATOM   2119 C  CB  . GLN   A 1 285 ? 3.468   21.991  -28.161 1.00 40.10 ? 422 GLN   A CB  1 
ATOM   2120 C  CG  . GLN   A 1 285 ? 3.074   21.934  -29.611 1.00 42.98 ? 422 GLN   A CG  1 
ATOM   2121 C  CD  . GLN   A 1 285 ? 4.174   22.429  -30.517 1.00 46.28 ? 422 GLN   A CD  1 
ATOM   2122 O  OE1 . GLN   A 1 285 ? 3.913   23.028  -31.560 1.00 49.58 ? 422 GLN   A OE1 1 
ATOM   2123 N  NE2 . GLN   A 1 285 ? 5.416   22.188  -30.122 1.00 45.18 ? 422 GLN   A NE2 1 
ATOM   2124 N  N   . ILE   A 1 286 ? 3.331   21.828  -24.961 1.00 39.21 ? 423 ILE   A N   1 
ATOM   2125 C  CA  . ILE   A 1 286 ? 3.972   21.471  -23.701 1.00 41.01 ? 423 ILE   A CA  1 
ATOM   2126 C  C   . ILE   A 1 286 ? 2.882   21.286  -22.657 1.00 40.53 ? 423 ILE   A C   1 
ATOM   2127 O  O   . ILE   A 1 286 ? 2.097   22.205  -22.392 1.00 38.91 ? 423 ILE   A O   1 
ATOM   2128 C  CB  . ILE   A 1 286 ? 4.993   22.531  -23.259 1.00 38.65 ? 423 ILE   A CB  1 
ATOM   2129 C  CG1 . ILE   A 1 286 ? 6.125   22.639  -24.293 1.00 42.29 ? 423 ILE   A CG1 1 
ATOM   2130 C  CG2 . ILE   A 1 286 ? 5.545   22.192  -21.887 1.00 38.44 ? 423 ILE   A CG2 1 
ATOM   2131 C  CD1 . ILE   A 1 286 ? 6.977   23.894  -24.184 1.00 37.12 ? 423 ILE   A CD1 1 
ATOM   2132 N  N   . ILE   A 1 287 ? 2.835   20.098  -22.069 1.00 38.21 ? 424 ILE   A N   1 
ATOM   2133 C  CA  . ILE   A 1 287 ? 1.750   19.685  -21.192 1.00 41.67 ? 424 ILE   A CA  1 
ATOM   2134 C  C   . ILE   A 1 287 ? 2.332   19.278  -19.846 1.00 41.59 ? 424 ILE   A C   1 
ATOM   2135 O  O   . ILE   A 1 287 ? 3.396   18.654  -19.786 1.00 38.97 ? 424 ILE   A O   1 
ATOM   2136 C  CB  . ILE   A 1 287 ? 0.950   18.522  -21.821 1.00 42.18 ? 424 ILE   A CB  1 
ATOM   2137 C  CG1 . ILE   A 1 287 ? 0.322   18.960  -23.150 1.00 41.68 ? 424 ILE   A CG1 1 
ATOM   2138 C  CG2 . ILE   A 1 287 ? -0.103  17.995  -20.861 1.00 44.61 ? 424 ILE   A CG2 1 
ATOM   2139 C  CD1 . ILE   A 1 287 ? -0.320  20.319  -23.109 1.00 38.09 ? 424 ILE   A CD1 1 
ATOM   2140 N  N   . ASN   A 1 288 ? 1.646   19.652  -18.767 1.00 40.63 ? 425 ASN   A N   1 
ATOM   2141 C  CA  . ASN   A 1 288 ? 1.900   19.078  -17.451 1.00 45.58 ? 425 ASN   A CA  1 
ATOM   2142 C  C   . ASN   A 1 288 ? 1.071   17.799  -17.355 1.00 42.88 ? 425 ASN   A C   1 
ATOM   2143 O  O   . ASN   A 1 288 ? -0.165  17.848  -17.330 1.00 42.57 ? 425 ASN   A O   1 
ATOM   2144 C  CB  . ASN   A 1 288 ? 1.550   20.064  -16.338 1.00 44.90 ? 425 ASN   A CB  1 
ATOM   2145 C  CG  . ASN   A 1 288 ? 2.435   21.301  -16.339 1.00 49.91 ? 425 ASN   A CG  1 
ATOM   2146 O  OD1 . ASN   A 1 288 ? 3.660   21.206  -16.280 1.00 49.75 ? 425 ASN   A OD1 1 
ATOM   2147 N  ND2 . ASN   A 1 288 ? 1.809   22.474  -16.401 1.00 49.72 ? 425 ASN   A ND2 1 
ATOM   2148 N  N   . MET   A 1 289 ? 1.749   16.657  -17.330 1.00 43.97 ? 426 MET   A N   1 
ATOM   2149 C  CA  . MET   A 1 289 ? 1.072   15.375  -17.452 1.00 44.86 ? 426 MET   A CA  1 
ATOM   2150 C  C   . MET   A 1 289 ? 0.180   15.108  -16.248 1.00 44.15 ? 426 MET   A C   1 
ATOM   2151 O  O   . MET   A 1 289 ? 0.448   15.556  -15.129 1.00 48.08 ? 426 MET   A O   1 
ATOM   2152 C  CB  . MET   A 1 289 ? 2.090   14.245  -17.602 1.00 45.10 ? 426 MET   A CB  1 
ATOM   2153 C  CG  . MET   A 1 289 ? 3.154   14.512  -18.650 1.00 46.01 ? 426 MET   A CG  1 
ATOM   2154 S  SD  . MET   A 1 289 ? 4.210   13.080  -18.924 1.00 60.18 ? 426 MET   A SD  1 
ATOM   2155 C  CE  . MET   A 1 289 ? 5.590   13.484  -17.857 1.00 58.70 ? 426 MET   A CE  1 
ATOM   2156 N  N   . TRP   A 1 290 ? -0.899  14.372  -16.496 1.00 39.34 ? 427 TRP   A N   1 
ATOM   2157 C  CA  . TRP   A 1 290 ? -1.799  13.949  -15.438 1.00 44.88 ? 427 TRP   A CA  1 
ATOM   2158 C  C   . TRP   A 1 290 ? -1.437  12.583  -14.871 1.00 45.43 ? 427 TRP   A C   1 
ATOM   2159 O  O   . TRP   A 1 290 ? -1.911  12.234  -13.785 1.00 43.30 ? 427 TRP   A O   1 
ATOM   2160 C  CB  . TRP   A 1 290 ? -3.238  13.922  -15.962 1.00 42.32 ? 427 TRP   A CB  1 
ATOM   2161 C  CG  . TRP   A 1 290 ? -3.447  12.919  -17.063 1.00 41.00 ? 427 TRP   A CG  1 
ATOM   2162 C  CD1 . TRP   A 1 290 ? -3.354  13.141  -18.406 1.00 41.43 ? 427 TRP   A CD1 1 
ATOM   2163 C  CD2 . TRP   A 1 290 ? -3.788  11.534  -16.911 1.00 38.14 ? 427 TRP   A CD2 1 
ATOM   2164 N  NE1 . TRP   A 1 290 ? -3.613  11.979  -19.099 1.00 37.29 ? 427 TRP   A NE1 1 
ATOM   2165 C  CE2 . TRP   A 1 290 ? -3.883  10.980  -18.202 1.00 36.59 ? 427 TRP   A CE2 1 
ATOM   2166 C  CE3 . TRP   A 1 290 ? -4.023  10.710  -15.806 1.00 38.28 ? 427 TRP   A CE3 1 
ATOM   2167 C  CZ2 . TRP   A 1 290 ? -4.202  9.639   -18.419 1.00 35.16 ? 427 TRP   A CZ2 1 
ATOM   2168 C  CZ3 . TRP   A 1 290 ? -4.339  9.377   -16.025 1.00 36.87 ? 427 TRP   A CZ3 1 
ATOM   2169 C  CH2 . TRP   A 1 290 ? -4.425  8.856   -17.321 1.00 34.54 ? 427 TRP   A CH2 1 
ATOM   2170 N  N   . GLN   A 1 291 ? -0.617  11.804  -15.581 1.00 41.99 ? 428 GLN   A N   1 
ATOM   2171 C  CA  . GLN   A 1 291 ? -0.241  10.480  -15.094 1.00 44.98 ? 428 GLN   A CA  1 
ATOM   2172 C  C   . GLN   A 1 291 ? 0.692   10.587  -13.890 1.00 53.49 ? 428 GLN   A C   1 
ATOM   2173 O  O   . GLN   A 1 291 ? 0.447   9.976   -12.841 1.00 54.24 ? 428 GLN   A O   1 
ATOM   2174 C  CB  . GLN   A 1 291 ? 0.413   9.678   -16.223 1.00 43.42 ? 428 GLN   A CB  1 
ATOM   2175 C  CG  . GLN   A 1 291 ? -0.474  9.485   -17.451 1.00 40.68 ? 428 GLN   A CG  1 
ATOM   2176 C  CD  . GLN   A 1 291 ? -0.322  10.609  -18.467 1.00 42.54 ? 428 GLN   A CD  1 
ATOM   2177 O  OE1 . GLN   A 1 291 ? -0.337  11.789  -18.110 1.00 42.63 ? 428 GLN   A OE1 1 
ATOM   2178 N  NE2 . GLN   A 1 291 ? -0.185  10.247  -19.740 1.00 35.61 ? 428 GLN   A NE2 1 
ATOM   2179 N  N   . GLY   A 1 292 ? 1.763   11.365  -14.025 1.00 53.28 ? 429 GLY   A N   1 
ATOM   2180 C  CA  . GLY   A 1 292 ? 2.684   11.623  -12.935 1.00 56.62 ? 429 GLY   A CA  1 
ATOM   2181 C  C   . GLY   A 1 292 ? 3.400   12.929  -13.183 1.00 59.52 ? 429 GLY   A C   1 
ATOM   2182 O  O   . GLY   A 1 292 ? 3.470   13.412  -14.318 1.00 54.62 ? 429 GLY   A O   1 
ATOM   2183 N  N   . THR   A 1 293 ? 3.929   13.506  -12.106 1.00 62.30 ? 430 THR   A N   1 
ATOM   2184 C  CA  . THR   A 1 293 ? 4.556   14.818  -12.206 1.00 60.55 ? 430 THR   A CA  1 
ATOM   2185 C  C   . THR   A 1 293 ? 5.665   14.788  -13.249 1.00 59.04 ? 430 THR   A C   1 
ATOM   2186 O  O   . THR   A 1 293 ? 6.642   14.042  -13.119 1.00 59.58 ? 430 THR   A O   1 
ATOM   2187 C  CB  . THR   A 1 293 ? 5.102   15.264  -10.847 1.00 65.74 ? 430 THR   A CB  1 
ATOM   2188 O  OG1 . THR   A 1 293 ? 4.040   15.816  -10.058 1.00 68.75 ? 430 THR   A OG1 1 
ATOM   2189 C  CG2 . THR   A 1 293 ? 6.184   16.326  -11.022 1.00 63.38 ? 430 THR   A CG2 1 
ATOM   2190 N  N   . GLY   A 1 294 ? 5.502   15.603  -14.282 1.00 57.14 ? 431 GLY   A N   1 
ATOM   2191 C  CA  . GLY   A 1 294 ? 6.449   15.660  -15.376 1.00 58.76 ? 431 GLY   A CA  1 
ATOM   2192 C  C   . GLY   A 1 294 ? 5.877   16.489  -16.500 1.00 53.29 ? 431 GLY   A C   1 
ATOM   2193 O  O   . GLY   A 1 294 ? 4.714   16.903  -16.475 1.00 47.86 ? 431 GLY   A O   1 
ATOM   2194 N  N   . GLN   A 1 295 ? 6.724   16.731  -17.497 1.00 56.50 ? 432 GLN   A N   1 
ATOM   2195 C  CA  . GLN   A 1 295 ? 6.386   17.573  -18.636 1.00 54.12 ? 432 GLN   A CA  1 
ATOM   2196 C  C   . GLN   A 1 295 ? 6.571   16.788  -19.925 1.00 54.98 ? 432 GLN   A C   1 
ATOM   2197 O  O   . GLN   A 1 295 ? 7.628   16.189  -20.145 1.00 57.13 ? 432 GLN   A O   1 
ATOM   2198 C  CB  . GLN   A 1 295 ? 7.253   18.833  -18.666 1.00 55.22 ? 432 GLN   A CB  1 
ATOM   2199 C  CG  . GLN   A 1 295 ? 6.783   19.937  -17.742 1.00 57.12 ? 432 GLN   A CG  1 
ATOM   2200 C  CD  . GLN   A 1 295 ? 7.379   21.281  -18.106 1.00 55.25 ? 432 GLN   A CD  1 
ATOM   2201 O  OE1 . GLN   A 1 295 ? 8.472   21.355  -18.672 1.00 52.75 ? 432 GLN   A OE1 1 
ATOM   2202 N  NE2 . GLN   A 1 295 ? 6.659   22.353  -17.791 1.00 55.93 ? 432 GLN   A NE2 1 
ATOM   2203 N  N   . ALA   A 1 296 ? 5.548   16.796  -20.775 1.00 51.65 ? 433 ALA   A N   1 
ATOM   2204 C  CA  . ALA   A 1 296 ? 5.603   16.138  -22.073 1.00 51.95 ? 433 ALA   A CA  1 
ATOM   2205 C  C   . ALA   A 1 296 ? 5.417   17.185  -23.161 1.00 47.79 ? 433 ALA   A C   1 
ATOM   2206 O  O   . ALA   A 1 296 ? 4.531   18.041  -23.057 1.00 45.94 ? 433 ALA   A O   1 
ATOM   2207 C  CB  . ALA   A 1 296 ? 4.534   15.045  -22.190 1.00 48.35 ? 433 ALA   A CB  1 
ATOM   2208 N  N   . MET   A 1 297 ? 6.251   17.130  -24.196 1.00 44.99 ? 434 MET   A N   1 
ATOM   2209 C  CA  . MET   A 1 297 ? 6.121   18.028  -25.335 1.00 45.33 ? 434 MET   A CA  1 
ATOM   2210 C  C   . MET   A 1 297 ? 5.740   17.231  -26.573 1.00 47.18 ? 434 MET   A C   1 
ATOM   2211 O  O   . MET   A 1 297 ? 6.391   16.232  -26.898 1.00 46.98 ? 434 MET   A O   1 
ATOM   2212 C  CB  . MET   A 1 297 ? 7.408   18.808  -25.601 1.00 45.65 ? 434 MET   A CB  1 
ATOM   2213 C  CG  . MET   A 1 297 ? 7.234   19.848  -26.702 1.00 45.87 ? 434 MET   A CG  1 
ATOM   2214 S  SD  . MET   A 1 297 ? 8.682   20.865  -27.056 1.00 59.65 ? 434 MET   A SD  1 
ATOM   2215 C  CE  . MET   A 1 297 ? 9.533   19.835  -28.252 1.00 48.83 ? 434 MET   A CE  1 
ATOM   2216 N  N   . TYR   A 1 298 ? 4.699   17.680  -27.261 1.00 43.98 ? 435 TYR   A N   1 
ATOM   2217 C  CA  . TYR   A 1 298 ? 4.225   17.051  -28.483 1.00 47.71 ? 435 TYR   A CA  1 
ATOM   2218 C  C   . TYR   A 1 298 ? 4.527   17.947  -29.677 1.00 47.14 ? 435 TYR   A C   1 
ATOM   2219 O  O   . TYR   A 1 298 ? 4.942   19.100  -29.534 1.00 46.37 ? 435 TYR   A O   1 
ATOM   2220 C  CB  . TYR   A 1 298 ? 2.725   16.756  -28.385 1.00 46.31 ? 435 TYR   A CB  1 
ATOM   2221 C  CG  . TYR   A 1 298 ? 2.389   15.786  -27.276 1.00 46.68 ? 435 TYR   A CG  1 
ATOM   2222 C  CD1 . TYR   A 1 298 ? 2.350   14.420  -27.512 1.00 49.45 ? 435 TYR   A CD1 1 
ATOM   2223 C  CD2 . TYR   A 1 298 ? 2.145   16.236  -25.985 1.00 44.05 ? 435 TYR   A CD2 1 
ATOM   2224 C  CE1 . TYR   A 1 298 ? 2.052   13.532  -26.503 1.00 47.49 ? 435 TYR   A CE1 1 
ATOM   2225 C  CE2 . TYR   A 1 298 ? 1.853   15.357  -24.966 1.00 43.58 ? 435 TYR   A CE2 1 
ATOM   2226 C  CZ  . TYR   A 1 298 ? 1.806   14.002  -25.233 1.00 47.59 ? 435 TYR   A CZ  1 
ATOM   2227 O  OH  . TYR   A 1 298 ? 1.514   13.099  -24.237 1.00 49.86 ? 435 TYR   A OH  1 
ATOM   2228 N  N   . ALA   A 1 299 ? 4.321   17.397  -30.867 1.00 47.32 ? 436 ALA   A N   1 
ATOM   2229 C  CA  . ALA   A 1 299 ? 4.543   18.153  -32.087 1.00 46.83 ? 436 ALA   A CA  1 
ATOM   2230 C  C   . ALA   A 1 299 ? 3.388   19.114  -32.347 1.00 46.20 ? 436 ALA   A C   1 
ATOM   2231 O  O   . ALA   A 1 299 ? 2.301   18.962  -31.785 1.00 47.48 ? 436 ALA   A O   1 
ATOM   2232 C  CB  . ALA   A 1 299 ? 4.710   17.211  -33.275 1.00 46.72 ? 436 ALA   A CB  1 
ATOM   2233 N  N   . PRO   A 1 300 ? 3.600   20.111  -33.201 1.00 47.56 ? 437 PRO   A N   1 
ATOM   2234 C  CA  . PRO   A 1 300 ? 2.528   21.065  -33.526 1.00 44.65 ? 437 PRO   A CA  1 
ATOM   2235 C  C   . PRO   A 1 300 ? 1.302   20.346  -34.060 1.00 46.30 ? 437 PRO   A C   1 
ATOM   2236 O  O   . PRO   A 1 300 ? 1.381   19.173  -34.456 1.00 45.86 ? 437 PRO   A O   1 
ATOM   2237 C  CB  . PRO   A 1 300 ? 3.162   21.959  -34.604 1.00 47.82 ? 437 PRO   A CB  1 
ATOM   2238 C  CG  . PRO   A 1 300 ? 4.641   21.803  -34.425 1.00 46.23 ? 437 PRO   A CG  1 
ATOM   2239 C  CD  . PRO   A 1 300 ? 4.852   20.403  -33.921 1.00 44.83 ? 437 PRO   A CD  1 
ATOM   2240 N  N   . PRO   A 1 301 ? 0.154   21.019  -34.111 1.00 45.23 ? 438 PRO   A N   1 
ATOM   2241 C  CA  . PRO   A 1 301 ? -1.097  20.336  -34.467 1.00 42.55 ? 438 PRO   A CA  1 
ATOM   2242 C  C   . PRO   A 1 301 ? -1.161  19.953  -35.941 1.00 47.96 ? 438 PRO   A C   1 
ATOM   2243 O  O   . PRO   A 1 301 ? -0.423  20.457  -36.790 1.00 43.80 ? 438 PRO   A O   1 
ATOM   2244 C  CB  . PRO   A 1 301 ? -2.177  21.366  -34.122 1.00 44.63 ? 438 PRO   A CB  1 
ATOM   2245 C  CG  . PRO   A 1 301 ? -1.477  22.687  -34.182 1.00 44.36 ? 438 PRO   A CG  1 
ATOM   2246 C  CD  . PRO   A 1 301 ? -0.048  22.445  -33.810 1.00 44.80 ? 438 PRO   A CD  1 
ATOM   2247 N  N   . ILE   A 1 302 ? -2.088  19.042  -36.236 1.00 47.67 ? 439 ILE   A N   1 
ATOM   2248 C  CA  . ILE   A 1 302 ? -2.304  18.534  -37.587 1.00 47.84 ? 439 ILE   A CA  1 
ATOM   2249 C  C   . ILE   A 1 302 ? -3.000  19.592  -38.434 1.00 49.01 ? 439 ILE   A C   1 
ATOM   2250 O  O   . ILE   A 1 302 ? -3.457  20.617  -37.913 1.00 47.39 ? 439 ILE   A O   1 
ATOM   2251 C  CB  . ILE   A 1 302 ? -3.123  17.233  -37.546 1.00 47.65 ? 439 ILE   A CB  1 
ATOM   2252 C  CG1 . ILE   A 1 302 ? -4.458  17.480  -36.842 1.00 48.60 ? 439 ILE   A CG1 1 
ATOM   2253 C  CG2 . ILE   A 1 302 ? -2.357  16.142  -36.840 1.00 45.83 ? 439 ILE   A CG2 1 
ATOM   2254 C  CD1 . ILE   A 1 302 ? -5.359  16.261  -36.775 1.00 50.35 ? 439 ILE   A CD1 1 
ATOM   2255 N  N   . ASP   A 1 303 ? -3.090  19.355  -39.741 1.00 53.12 ? 440 ASP   A N   1 
ATOM   2256 C  CA  . ASP   A 1 303 ? -3.757  20.293  -40.630 1.00 51.14 ? 440 ASP   A CA  1 
ATOM   2257 C  C   . ASP   A 1 303 ? -5.263  20.039  -40.656 1.00 53.33 ? 440 ASP   A C   1 
ATOM   2258 O  O   . ASP   A 1 303 ? -5.757  19.007  -40.194 1.00 52.56 ? 440 ASP   A O   1 
ATOM   2259 C  CB  . ASP   A 1 303 ? -3.184  20.198  -42.047 1.00 58.33 ? 440 ASP   A CB  1 
ATOM   2260 C  CG  . ASP   A 1 303 ? -3.340  18.809  -42.653 1.00 62.91 ? 440 ASP   A CG  1 
ATOM   2261 O  OD1 . ASP   A 1 303 ? -4.167  18.020  -42.145 1.00 66.25 ? 440 ASP   A OD1 1 
ATOM   2262 O  OD2 . ASP   A 1 303 ? -2.638  18.510  -43.646 1.00 65.85 ? 440 ASP   A OD2 1 
ATOM   2263 N  N   . GLY   A 1 304 ? -5.995  21.005  -41.208 1.00 52.24 ? 441 GLY   A N   1 
ATOM   2264 C  CA  . GLY   A 1 304 ? -7.423  20.858  -41.399 1.00 49.65 ? 441 GLY   A CA  1 
ATOM   2265 C  C   . GLY   A 1 304 ? -8.245  21.281  -40.197 1.00 50.23 ? 441 GLY   A C   1 
ATOM   2266 O  O   . GLY   A 1 304 ? -7.741  21.711  -39.155 1.00 48.25 ? 441 GLY   A O   1 
ATOM   2267 N  N   . LYS   A 1 305 ? -9.558  21.152  -40.367 1.00 48.47 ? 442 LYS   A N   1 
ATOM   2268 C  CA  . LYS   A 1 305 ? -10.510 21.485  -39.315 1.00 48.28 ? 442 LYS   A CA  1 
ATOM   2269 C  C   . LYS   A 1 305 ? -10.450 20.436  -38.208 1.00 44.77 ? 442 LYS   A C   1 
ATOM   2270 O  O   . LYS   A 1 305 ? -10.768 19.267  -38.442 1.00 48.97 ? 442 LYS   A O   1 
ATOM   2271 C  CB  . LYS   A 1 305 ? -11.918 21.568  -39.903 1.00 49.77 ? 442 LYS   A CB  1 
ATOM   2272 C  CG  . LYS   A 1 305 ? -12.938 22.278  -39.027 1.00 50.34 ? 442 LYS   A CG  1 
ATOM   2273 C  CD  . LYS   A 1 305 ? -14.356 21.994  -39.507 1.00 53.31 ? 442 LYS   A CD  1 
ATOM   2274 C  CE  . LYS   A 1 305 ? -14.809 23.020  -40.525 1.00 58.11 ? 442 LYS   A CE  1 
ATOM   2275 N  NZ  . LYS   A 1 305 ? -15.664 22.410  -41.588 1.00 60.22 ? 442 LYS   A NZ  1 
ATOM   2276 N  N   . ILE   A 1 306 ? -10.035 20.844  -37.010 1.00 45.36 ? 443 ILE   A N   1 
ATOM   2277 C  CA  . ILE   A 1 306 ? -10.042 19.978  -35.832 1.00 41.37 ? 443 ILE   A CA  1 
ATOM   2278 C  C   . ILE   A 1 306 ? -11.276 20.334  -35.015 1.00 42.42 ? 443 ILE   A C   1 
ATOM   2279 O  O   . ILE   A 1 306 ? -11.426 21.479  -34.571 1.00 41.55 ? 443 ILE   A O   1 
ATOM   2280 C  CB  . ILE   A 1 306 ? -8.759  20.140  -34.998 1.00 42.68 ? 443 ILE   A CB  1 
ATOM   2281 C  CG1 . ILE   A 1 306 ? -7.517  19.864  -35.854 1.00 42.61 ? 443 ILE   A CG1 1 
ATOM   2282 C  CG2 . ILE   A 1 306 ? -8.788  19.231  -33.756 1.00 42.29 ? 443 ILE   A CG2 1 
ATOM   2283 C  CD1 . ILE   A 1 306 ? -6.230  20.386  -35.249 1.00 42.00 ? 443 ILE   A CD1 1 
ATOM   2284 N  N   . ASN   A 1 307 ? -12.172 19.369  -34.828 1.00 45.35 ? 444 ASN   A N   1 
ATOM   2285 C  CA  . ASN   A 1 307 ? -13.462 19.648  -34.213 1.00 45.85 ? 444 ASN   A CA  1 
ATOM   2286 C  C   . ASN   A 1 307 ? -13.879 18.491  -33.321 1.00 46.87 ? 444 ASN   A C   1 
ATOM   2287 O  O   . ASN   A 1 307 ? -13.767 17.327  -33.715 1.00 48.32 ? 444 ASN   A O   1 
ATOM   2288 C  CB  . ASN   A 1 307 ? -14.537 19.905  -35.280 1.00 47.06 ? 444 ASN   A CB  1 
ATOM   2289 C  CG  . ASN   A 1 307 ? -15.935 20.015  -34.691 1.00 46.95 ? 444 ASN   A CG  1 
ATOM   2290 O  OD1 . ASN   A 1 307 ? -16.754 19.106  -34.836 1.00 48.40 ? 444 ASN   A OD1 1 
ATOM   2291 N  ND2 . ASN   A 1 307 ? -16.213 21.126  -34.024 1.00 42.90 ? 444 ASN   A ND2 1 
ATOM   2292 N  N   . CYS   A 1 308 ? -14.362 18.819  -32.124 1.00 46.21 ? 445 CYS   A N   1 
ATOM   2293 C  CA  . CYS   A 1 308 ? -14.931 17.844  -31.205 1.00 46.73 ? 445 CYS   A CA  1 
ATOM   2294 C  C   . CYS   A 1 308 ? -16.227 18.399  -30.643 1.00 45.76 ? 445 CYS   A C   1 
ATOM   2295 O  O   . CYS   A 1 308 ? -16.256 19.524  -30.134 1.00 45.04 ? 445 CYS   A O   1 
ATOM   2296 C  CB  . CYS   A 1 308 ? -13.973 17.509  -30.055 1.00 50.69 ? 445 CYS   A CB  1 
ATOM   2297 S  SG  . CYS   A 1 308 ? -12.626 16.404  -30.510 1.00 58.44 ? 445 CYS   A SG  1 
ATOM   2298 N  N   . VAL   A 1 309 ? -17.294 17.616  -30.741 1.00 44.29 ? 446 VAL   A N   1 
ATOM   2299 C  CA  . VAL   A 1 309 ? -18.574 17.942  -30.129 1.00 42.47 ? 446 VAL   A CA  1 
ATOM   2300 C  C   . VAL   A 1 309 ? -18.768 16.966  -28.973 1.00 42.75 ? 446 VAL   A C   1 
ATOM   2301 O  O   . VAL   A 1 309 ? -18.903 15.755  -29.187 1.00 39.43 ? 446 VAL   A O   1 
ATOM   2302 C  CB  . VAL   A 1 309 ? -19.727 17.868  -31.138 1.00 43.12 ? 446 VAL   A CB  1 
ATOM   2303 C  CG1 . VAL   A 1 309 ? -21.054 18.142  -30.448 1.00 46.88 ? 446 VAL   A CG1 1 
ATOM   2304 C  CG2 . VAL   A 1 309 ? -19.500 18.854  -32.270 1.00 45.22 ? 446 VAL   A CG2 1 
ATOM   2305 N  N   . SER   A 1 310 ? -18.754 17.483  -27.747 1.00 36.93 ? 447 SER   A N   1 
ATOM   2306 C  CA  . SER   A 1 310 ? -18.845 16.656  -26.554 1.00 39.11 ? 447 SER   A CA  1 
ATOM   2307 C  C   . SER   A 1 310 ? -20.018 17.099  -25.689 1.00 38.00 ? 447 SER   A C   1 
ATOM   2308 O  O   . SER   A 1 310 ? -20.491 18.236  -25.772 1.00 40.51 ? 447 SER   A O   1 
ATOM   2309 C  CB  . SER   A 1 310 ? -17.548 16.709  -25.727 1.00 39.66 ? 447 SER   A CB  1 
ATOM   2310 O  OG  . SER   A 1 310 ? -16.397 16.620  -26.551 1.00 40.67 ? 447 SER   A OG  1 
ATOM   2311 N  N   . ASN   A 1 311 ? -20.488 16.177  -24.856 1.00 37.29 ? 448 ASN   A N   1 
ATOM   2312 C  CA  . ASN   A 1 311 ? -21.513 16.473  -23.867 1.00 39.44 ? 448 ASN   A CA  1 
ATOM   2313 C  C   . ASN   A 1 311 ? -20.862 16.832  -22.540 1.00 39.19 ? 448 ASN   A C   1 
ATOM   2314 O  O   . ASN   A 1 311 ? -20.041 16.067  -22.022 1.00 37.58 ? 448 ASN   A O   1 
ATOM   2315 C  CB  . ASN   A 1 311 ? -22.429 15.271  -23.655 1.00 41.44 ? 448 ASN   A CB  1 
ATOM   2316 C  CG  . ASN   A 1 311 ? -23.476 15.132  -24.724 1.00 48.50 ? 448 ASN   A CG  1 
ATOM   2317 O  OD1 . ASN   A 1 311 ? -23.860 16.096  -25.381 1.00 49.32 ? 448 ASN   A OD1 1 
ATOM   2318 N  ND2 . ASN   A 1 311 ? -23.950 13.911  -24.896 1.00 54.57 ? 448 ASN   A ND2 1 
ATOM   2319 N  N   . ILE   A 1 312 ? -21.240 17.982  -21.985 1.00 40.25 ? 449 ILE   A N   1 
ATOM   2320 C  CA  . ILE   A 1 312 ? -20.879 18.308  -20.610 1.00 37.87 ? 449 ILE   A CA  1 
ATOM   2321 C  C   . ILE   A 1 312 ? -21.866 17.583  -19.705 1.00 37.24 ? 449 ILE   A C   1 
ATOM   2322 O  O   . ILE   A 1 312 ? -23.051 17.917  -19.668 1.00 37.79 ? 449 ILE   A O   1 
ATOM   2323 C  CB  . ILE   A 1 312 ? -20.898 19.817  -20.352 1.00 39.62 ? 449 ILE   A CB  1 
ATOM   2324 C  CG1 . ILE   A 1 312 ? -19.775 20.497  -21.140 1.00 38.85 ? 449 ILE   A CG1 1 
ATOM   2325 C  CG2 . ILE   A 1 312 ? -20.779 20.093  -18.842 1.00 34.78 ? 449 ILE   A CG2 1 
ATOM   2326 C  CD1 . ILE   A 1 312 ? -19.912 21.999  -21.245 1.00 37.54 ? 449 ILE   A CD1 1 
ATOM   2327 N  N   . THR   A 1 313 ? -21.385 16.576  -18.986 1.00 34.24 ? 450 THR   A N   1 
ATOM   2328 C  CA  . THR   A 1 313 ? -22.249 15.786  -18.128 1.00 33.00 ? 450 THR   A CA  1 
ATOM   2329 C  C   . THR   A 1 313 ? -21.961 15.969  -16.645 1.00 34.85 ? 450 THR   A C   1 
ATOM   2330 O  O   . THR   A 1 313 ? -22.695 15.418  -15.817 1.00 35.56 ? 450 THR   A O   1 
ATOM   2331 C  CB  . THR   A 1 313 ? -22.132 14.300  -18.495 1.00 38.22 ? 450 THR   A CB  1 
ATOM   2332 O  OG1 . THR   A 1 313 ? -20.785 13.861  -18.279 1.00 35.83 ? 450 THR   A OG1 1 
ATOM   2333 C  CG2 . THR   A 1 313 ? -22.522 14.071  -19.968 1.00 35.99 ? 450 THR   A CG2 1 
ATOM   2334 N  N   . GLY   A 1 314 ? -20.926 16.720  -16.287 1.00 32.01 ? 451 GLY   A N   1 
ATOM   2335 C  CA  . GLY   A 1 314 ? -20.626 16.968  -14.889 1.00 33.89 ? 451 GLY   A CA  1 
ATOM   2336 C  C   . GLY   A 1 314 ? -19.634 18.103  -14.770 1.00 33.58 ? 451 GLY   A C   1 
ATOM   2337 O  O   . GLY   A 1 314 ? -19.017 18.531  -15.751 1.00 33.53 ? 451 GLY   A O   1 
ATOM   2338 N  N   . ILE   A 1 315 ? -19.491 18.588  -13.541 1.00 33.24 ? 452 ILE   A N   1 
ATOM   2339 C  CA  . ILE   A 1 315 ? -18.572 19.670  -13.219 1.00 31.46 ? 452 ILE   A CA  1 
ATOM   2340 C  C   . ILE   A 1 315 ? -17.766 19.282  -11.988 1.00 35.43 ? 452 ILE   A C   1 
ATOM   2341 O  O   . ILE   A 1 315 ? -18.300 18.696  -11.040 1.00 33.00 ? 452 ILE   A O   1 
ATOM   2342 C  CB  . ILE   A 1 315 ? -19.315 21.002  -12.977 1.00 34.17 ? 452 ILE   A CB  1 
ATOM   2343 C  CG1 . ILE   A 1 315 ? -20.284 21.299  -14.124 1.00 37.71 ? 452 ILE   A CG1 1 
ATOM   2344 C  CG2 . ILE   A 1 315 ? -18.323 22.148  -12.797 1.00 33.13 ? 452 ILE   A CG2 1 
ATOM   2345 C  CD1 . ILE   A 1 315 ? -21.286 22.396  -13.797 1.00 38.99 ? 452 ILE   A CD1 1 
ATOM   2346 N  N   . LEU   A 1 316 ? -16.478 19.618  -12.004 1.00 36.40 ? 453 LEU   A N   1 
ATOM   2347 C  CA  . LEU   A 1 316 ? -15.589 19.410  -10.870 1.00 34.98 ? 453 LEU   A CA  1 
ATOM   2348 C  C   . LEU   A 1 316 ? -15.481 20.729  -10.115 1.00 38.03 ? 453 LEU   A C   1 
ATOM   2349 O  O   . LEU   A 1 316 ? -15.091 21.747  -10.698 1.00 35.18 ? 453 LEU   A O   1 
ATOM   2350 C  CB  . LEU   A 1 316 ? -14.216 18.936  -11.343 1.00 38.53 ? 453 LEU   A CB  1 
ATOM   2351 C  CG  . LEU   A 1 316 ? -14.185 17.574  -12.041 1.00 39.50 ? 453 LEU   A CG  1 
ATOM   2352 C  CD1 . LEU   A 1 316 ? -12.801 17.288  -12.611 1.00 41.16 ? 453 LEU   A CD1 1 
ATOM   2353 C  CD2 . LEU   A 1 316 ? -14.606 16.477  -11.078 1.00 37.99 ? 453 LEU   A CD2 1 
ATOM   2354 N  N   . LEU   A 1 317 ? -15.827 20.717  -8.828  1.00 38.21 ? 454 LEU   A N   1 
ATOM   2355 C  CA  . LEU   A 1 317 ? -15.945 21.948  -8.058  1.00 40.31 ? 454 LEU   A CA  1 
ATOM   2356 C  C   . LEU   A 1 317 ? -15.134 21.868  -6.772  1.00 38.03 ? 454 LEU   A C   1 
ATOM   2357 O  O   . LEU   A 1 317 ? -15.131 20.841  -6.088  1.00 38.43 ? 454 LEU   A O   1 
ATOM   2358 C  CB  . LEU   A 1 317 ? -17.413 22.236  -7.723  1.00 39.83 ? 454 LEU   A CB  1 
ATOM   2359 C  CG  . LEU   A 1 317 ? -18.232 22.826  -8.868  1.00 38.32 ? 454 LEU   A CG  1 
ATOM   2360 C  CD1 . LEU   A 1 317 ? -19.616 23.201  -8.379  1.00 38.66 ? 454 LEU   A CD1 1 
ATOM   2361 C  CD2 . LEU   A 1 317 ? -17.519 24.029  -9.473  1.00 40.23 ? 454 LEU   A CD2 1 
ATOM   2362 N  N   . THR   A 1 318 ? -14.448 22.965  -6.456  1.00 38.81 ? 455 THR   A N   1 
ATOM   2363 C  CA  . THR   A 1 318 ? -13.745 23.142  -5.193  1.00 43.70 ? 455 THR   A CA  1 
ATOM   2364 C  C   . THR   A 1 318 ? -14.347 24.341  -4.478  1.00 43.06 ? 455 THR   A C   1 
ATOM   2365 O  O   . THR   A 1 318 ? -14.564 25.390  -5.095  1.00 44.06 ? 455 THR   A O   1 
ATOM   2366 C  CB  . THR   A 1 318 ? -12.242 23.357  -5.406  1.00 43.71 ? 455 THR   A CB  1 
ATOM   2367 O  OG1 . THR   A 1 318 ? -11.651 22.156  -5.922  1.00 45.79 ? 455 THR   A OG1 1 
ATOM   2368 C  CG2 . THR   A 1 318 ? -11.558 23.729  -4.086  1.00 45.85 ? 455 THR   A CG2 1 
ATOM   2369 N  N   . ARG   A 1 319 ? -14.615 24.186  -3.185  1.00 43.86 ? 456 ARG   A N   1 
ATOM   2370 C  CA  . ARG   A 1 319 ? -15.244 25.227  -2.385  1.00 43.44 ? 456 ARG   A CA  1 
ATOM   2371 C  C   . ARG   A 1 319 ? -14.189 26.018  -1.623  1.00 44.98 ? 456 ARG   A C   1 
ATOM   2372 O  O   . ARG   A 1 319 ? -13.233 25.448  -1.087  1.00 44.74 ? 456 ARG   A O   1 
ATOM   2373 C  CB  . ARG   A 1 319 ? -16.254 24.618  -1.410  1.00 43.89 ? 456 ARG   A CB  1 
ATOM   2374 C  CG  . ARG   A 1 319 ? -17.075 25.633  -0.632  1.00 47.12 ? 456 ARG   A CG  1 
ATOM   2375 C  CD  . ARG   A 1 319 ? -18.236 24.961  0.094   1.00 48.11 ? 456 ARG   A CD  1 
ATOM   2376 N  NE  . ARG   A 1 319 ? -17.773 24.006  1.093   1.00 45.22 ? 456 ARG   A NE  1 
ATOM   2377 C  CZ  . ARG   A 1 319 ? -17.615 24.288  2.379   1.00 49.67 ? 456 ARG   A CZ  1 
ATOM   2378 N  NH1 . ARG   A 1 319 ? -17.907 25.484  2.866   1.00 46.97 ? 456 ARG   A NH1 1 
ATOM   2379 N  NH2 . ARG   A 1 319 ? -17.144 23.351  3.197   1.00 44.75 ? 456 ARG   A NH2 1 
ATOM   2380 N  N   . ASP   A 1 320 ? -14.370 27.335  -1.581  1.00 45.54 ? 457 ASP   A N   1 
ATOM   2381 C  CA  . ASP   A 1 320 ? -13.465 28.206  -0.847  1.00 52.02 ? 457 ASP   A CA  1 
ATOM   2382 C  C   . ASP   A 1 320 ? -13.553 27.946  0.655   1.00 52.73 ? 457 ASP   A C   1 
ATOM   2383 O  O   . ASP   A 1 320 ? -14.619 27.639  1.197   1.00 49.58 ? 457 ASP   A O   1 
ATOM   2384 C  CB  . ASP   A 1 320 ? -13.789 29.672  -1.131  1.00 50.35 ? 457 ASP   A CB  1 
ATOM   2385 C  CG  . ASP   A 1 320 ? -13.088 30.194  -2.367  1.00 55.93 ? 457 ASP   A CG  1 
ATOM   2386 O  OD1 . ASP   A 1 320 ? -12.225 29.463  -2.903  1.00 55.86 ? 457 ASP   A OD1 1 
ATOM   2387 O  OD2 . ASP   A 1 320 ? -13.395 31.329  -2.796  1.00 55.40 ? 457 ASP   A OD2 1 
ATOM   2388 N  N   . GLY   A 1 321 ? -12.407 28.077  1.328   1.00 52.92 ? 458 GLY   A N   1 
ATOM   2389 C  CA  . GLY   A 1 321 ? -12.353 27.996  2.771   1.00 55.93 ? 458 GLY   A CA  1 
ATOM   2390 C  C   . GLY   A 1 321 ? -12.443 29.366  3.424   1.00 58.23 ? 458 GLY   A C   1 
ATOM   2391 O  O   . GLY   A 1 321 ? -12.500 30.405  2.766   1.00 58.37 ? 458 GLY   A O   1 
ATOM   2392 N  N   . GLY   A 1 322 ? -12.463 29.351  4.754   1.00 59.29 ? 459 GLY   A N   1 
ATOM   2393 C  CA  . GLY   A 1 322 ? -12.547 30.592  5.511   1.00 59.55 ? 459 GLY   A CA  1 
ATOM   2394 C  C   . GLY   A 1 322 ? -13.800 31.397  5.243   1.00 60.83 ? 459 GLY   A C   1 
ATOM   2395 O  O   . GLY   A 1 322 ? -13.732 32.627  5.118   1.00 61.89 ? 459 GLY   A O   1 
ATOM   2396 N  N   . ALA   A 1 323 ? -14.951 30.729  5.151   1.00 60.20 ? 460 ALA   A N   1 
ATOM   2397 C  CA  . ALA   A 1 323 ? -16.209 31.403  4.872   1.00 60.56 ? 460 ALA   A CA  1 
ATOM   2398 C  C   . ALA   A 1 323 ? -17.309 31.049  5.861   1.00 58.45 ? 460 ALA   A C   1 
ATOM   2399 O  O   . ALA   A 1 323 ? -18.455 31.470  5.659   1.00 53.78 ? 460 ALA   A O   1 
ATOM   2400 C  CB  . ALA   A 1 323 ? -16.682 31.086  3.442   1.00 57.67 ? 460 ALA   A CB  1 
ATOM   2401 N  N   . ASN   A 1 324 ? -17.001 30.286  6.913   1.00 59.15 ? 461 ASN   A N   1 
ATOM   2402 C  CA  . ASN   A 1 324 ? -18.030 29.935  7.884   1.00 59.88 ? 461 ASN   A CA  1 
ATOM   2403 C  C   . ASN   A 1 324 ? -18.667 31.187  8.477   1.00 60.09 ? 461 ASN   A C   1 
ATOM   2404 O  O   . ASN   A 1 324 ? -19.871 31.212  8.755   1.00 59.56 ? 461 ASN   A O   1 
ATOM   2405 C  CB  . ASN   A 1 324 ? -17.435 29.054  8.989   1.00 60.89 ? 461 ASN   A CB  1 
ATOM   2406 C  CG  . ASN   A 1 324 ? -16.710 27.815  8.448   1.00 62.69 ? 461 ASN   A CG  1 
ATOM   2407 O  OD1 . ASN   A 1 324 ? -15.485 27.802  8.337   1.00 62.30 ? 461 ASN   A OD1 1 
ATOM   2408 N  ND2 . ASN   A 1 324 ? -17.462 26.745  8.188   1.00 65.15 ? 461 ASN   A ND2 1 
ATOM   2409 N  N   . ASN   A 1 325 ? -17.882 32.249  8.642   1.00 57.19 ? 462 ASN   A N   1 
ATOM   2410 C  CA  . ASN   A 1 325 ? -18.353 33.479  9.257   1.00 59.25 ? 462 ASN   A CA  1 
ATOM   2411 C  C   . ASN   A 1 325 ? -18.887 34.486  8.252   1.00 58.95 ? 462 ASN   A C   1 
ATOM   2412 O  O   . ASN   A 1 325 ? -19.143 35.632  8.630   1.00 59.00 ? 462 ASN   A O   1 
ATOM   2413 C  CB  . ASN   A 1 325 ? -17.232 34.118  10.075  1.00 58.61 ? 462 ASN   A CB  1 
ATOM   2414 C  CG  . ASN   A 1 325 ? -16.943 33.365  11.351  1.00 61.54 ? 462 ASN   A CG  1 
ATOM   2415 O  OD1 . ASN   A 1 325 ? -17.847 32.799  11.967  1.00 64.66 ? 462 ASN   A OD1 1 
ATOM   2416 N  ND2 . ASN   A 1 325 ? -15.680 33.365  11.767  1.00 65.28 ? 462 ASN   A ND2 1 
ATOM   2417 N  N   . THR   A 1 326 ? -19.060 34.098  6.994   1.00 56.47 ? 463 THR   A N   1 
ATOM   2418 C  CA  . THR   A 1 326 ? -19.679 34.943  5.985   1.00 55.56 ? 463 THR   A CA  1 
ATOM   2419 C  C   . THR   A 1 326 ? -21.028 34.345  5.599   1.00 56.19 ? 463 THR   A C   1 
ATOM   2420 O  O   . THR   A 1 326 ? -21.438 33.293  6.099   1.00 54.66 ? 463 THR   A O   1 
ATOM   2421 C  CB  . THR   A 1 326 ? -18.759 35.101  4.768   1.00 57.99 ? 463 THR   A CB  1 
ATOM   2422 O  OG1 . THR   A 1 326 ? -18.913 33.976  3.890   1.00 56.63 ? 463 THR   A OG1 1 
ATOM   2423 C  CG2 . THR   A 1 326 ? -17.295 35.209  5.205   1.00 58.70 ? 463 THR   A CG2 1 
ATOM   2424 N  N   . SER   A 1 327 ? -21.733 35.028  4.703   1.00 52.81 ? 464 SER   A N   1 
ATOM   2425 C  CA  . SER   A 1 327 ? -23.021 34.542  4.232   1.00 57.75 ? 464 SER   A CA  1 
ATOM   2426 C  C   . SER   A 1 327 ? -22.943 33.924  2.842   1.00 54.65 ? 464 SER   A C   1 
ATOM   2427 O  O   . SER   A 1 327 ? -23.984 33.715  2.211   1.00 53.28 ? 464 SER   A O   1 
ATOM   2428 C  CB  . SER   A 1 327 ? -24.043 35.676  4.237   1.00 57.04 ? 464 SER   A CB  1 
ATOM   2429 O  OG  . SER   A 1 327 ? -23.458 36.874  3.760   1.00 59.67 ? 464 SER   A OG  1 
ATOM   2430 N  N   . ASN   A 1 328 ? -21.744 33.625  2.350   1.00 51.17 ? 465 ASN   A N   1 
ATOM   2431 C  CA  . ASN   A 1 328 ? -21.582 33.089  1.007   1.00 56.73 ? 465 ASN   A CA  1 
ATOM   2432 C  C   . ASN   A 1 328 ? -20.769 31.804  1.028   1.00 53.57 ? 465 ASN   A C   1 
ATOM   2433 O  O   . ASN   A 1 328 ? -20.066 31.493  1.993   1.00 53.22 ? 465 ASN   A O   1 
ATOM   2434 C  CB  . ASN   A 1 328 ? -20.899 34.092  0.068   1.00 52.63 ? 465 ASN   A CB  1 
ATOM   2435 C  CG  . ASN   A 1 328 ? -21.283 35.519  0.362   1.00 56.71 ? 465 ASN   A CG  1 
ATOM   2436 O  OD1 . ASN   A 1 328 ? -22.369 35.970  -0.005  1.00 55.10 ? 465 ASN   A OD1 1 
ATOM   2437 N  ND2 . ASN   A 1 328 ? -20.389 36.248  1.024   1.00 59.98 ? 465 ASN   A ND2 1 
ATOM   2438 N  N   . GLU   A 1 329 ? -20.882 31.063  -0.071  1.00 54.14 ? 466 GLU   A N   1 
ATOM   2439 C  CA  . GLU   A 1 329 ? -20.004 29.942  -0.377  1.00 50.67 ? 466 GLU   A CA  1 
ATOM   2440 C  C   . GLU   A 1 329 ? -19.571 30.094  -1.827  1.00 47.74 ? 466 GLU   A C   1 
ATOM   2441 O  O   . GLU   A 1 329 ? -20.417 30.106  -2.726  1.00 47.38 ? 466 GLU   A O   1 
ATOM   2442 C  CB  . GLU   A 1 329 ? -20.711 28.602  -0.155  1.00 48.66 ? 466 GLU   A CB  1 
ATOM   2443 C  CG  . GLU   A 1 329 ? -21.194 28.372  1.268   1.00 54.90 ? 466 GLU   A CG  1 
ATOM   2444 C  CD  . GLU   A 1 329 ? -20.053 28.166  2.254   1.00 55.64 ? 466 GLU   A CD  1 
ATOM   2445 O  OE1 . GLU   A 1 329 ? -20.338 27.968  3.457   1.00 57.11 ? 466 GLU   A OE1 1 
ATOM   2446 O  OE2 . GLU   A 1 329 ? -18.879 28.174  1.822   1.00 52.75 ? 466 GLU   A OE2 1 
ATOM   2447 N  N   . THR   A 1 330 ? -18.267 30.226  -2.052  1.00 46.24 ? 467 THR   A N   1 
ATOM   2448 C  CA  . THR   A 1 330 ? -17.714 30.424  -3.386  1.00 47.41 ? 467 THR   A CA  1 
ATOM   2449 C  C   . THR   A 1 330 ? -17.201 29.093  -3.924  1.00 45.37 ? 467 THR   A C   1 
ATOM   2450 O  O   . THR   A 1 330 ? -16.499 28.358  -3.221  1.00 45.58 ? 467 THR   A O   1 
ATOM   2451 C  CB  . THR   A 1 330 ? -16.590 31.464  -3.363  1.00 48.89 ? 467 THR   A CB  1 
ATOM   2452 O  OG1 . THR   A 1 330 ? -17.107 32.715  -2.892  1.00 48.59 ? 467 THR   A OG1 1 
ATOM   2453 C  CG2 . THR   A 1 330 ? -15.979 31.655  -4.755  1.00 46.98 ? 467 THR   A CG2 1 
ATOM   2454 N  N   . PHE   A 1 331 ? -17.563 28.785  -5.164  1.00 43.41 ? 468 PHE   A N   1 
ATOM   2455 C  CA  . PHE   A 1 331 ? -17.192 27.531  -5.801  1.00 43.96 ? 468 PHE   A CA  1 
ATOM   2456 C  C   . PHE   A 1 331 ? -16.391 27.815  -7.062  1.00 43.16 ? 468 PHE   A C   1 
ATOM   2457 O  O   . PHE   A 1 331 ? -16.748 28.694  -7.851  1.00 43.29 ? 468 PHE   A O   1 
ATOM   2458 C  CB  . PHE   A 1 331 ? -18.437 26.698  -6.125  1.00 45.20 ? 468 PHE   A CB  1 
ATOM   2459 C  CG  . PHE   A 1 331 ? -19.194 26.263  -4.908  1.00 44.12 ? 468 PHE   A CG  1 
ATOM   2460 C  CD1 . PHE   A 1 331 ? -20.014 27.153  -4.235  1.00 44.10 ? 468 PHE   A CD1 1 
ATOM   2461 C  CD2 . PHE   A 1 331 ? -19.069 24.973  -4.421  1.00 44.83 ? 468 PHE   A CD2 1 
ATOM   2462 C  CE1 . PHE   A 1 331 ? -20.703 26.759  -3.100  1.00 46.66 ? 468 PHE   A CE1 1 
ATOM   2463 C  CE2 . PHE   A 1 331 ? -19.758 24.573  -3.287  1.00 43.17 ? 468 PHE   A CE2 1 
ATOM   2464 C  CZ  . PHE   A 1 331 ? -20.576 25.465  -2.627  1.00 42.64 ? 468 PHE   A CZ  1 
ATOM   2465 N  N   . ARG   A 1 332 ? -15.305 27.063  -7.241  1.00 43.02 ? 469 ARG   A N   1 
ATOM   2466 C  CA  . ARG   A 1 332 ? -14.374 27.242  -8.340  1.00 43.19 ? 469 ARG   A CA  1 
ATOM   2467 C  C   . ARG   A 1 332 ? -14.177 25.922  -9.074  1.00 41.21 ? 469 ARG   A C   1 
ATOM   2468 O  O   . ARG   A 1 332 ? -14.103 24.857  -8.441  1.00 37.35 ? 469 ARG   A O   1 
ATOM   2469 C  CB  . ARG   A 1 332 ? -13.022 27.757  -7.826  1.00 44.07 ? 469 ARG   A CB  1 
ATOM   2470 C  CG  . ARG   A 1 332 ? -13.053 29.214  -7.403  1.00 49.14 ? 469 ARG   A CG  1 
ATOM   2471 C  CD  . ARG   A 1 332 ? -11.816 29.617  -6.609  1.00 50.83 ? 469 ARG   A CD  1 
ATOM   2472 N  NE  . ARG   A 1 332 ? -12.140 30.674  -5.657  1.00 54.95 ? 469 ARG   A NE  1 
ATOM   2473 C  CZ  . ARG   A 1 332 ? -12.112 31.968  -5.946  1.00 54.24 ? 469 ARG   A CZ  1 
ATOM   2474 N  NH1 . ARG   A 1 332 ? -11.765 32.398  -7.149  1.00 47.45 ? 469 ARG   A NH1 1 
ATOM   2475 N  NH2 . ARG   A 1 332 ? -12.440 32.852  -5.007  1.00 52.86 ? 469 ARG   A NH2 1 
ATOM   2476 N  N   . PRO   A 1 333 ? -14.096 25.958  -10.404 1.00 37.89 ? 470 PRO   A N   1 
ATOM   2477 C  CA  . PRO   A 1 333 ? -13.858 24.723  -11.165 1.00 40.67 ? 470 PRO   A CA  1 
ATOM   2478 C  C   . PRO   A 1 333 ? -12.526 24.096  -10.784 1.00 37.08 ? 470 PRO   A C   1 
ATOM   2479 O  O   . PRO   A 1 333 ? -11.503 24.772  -10.703 1.00 46.41 ? 470 PRO   A O   1 
ATOM   2480 C  CB  . PRO   A 1 333 ? -13.858 25.195  -12.627 1.00 40.40 ? 470 PRO   A CB  1 
ATOM   2481 C  CG  . PRO   A 1 333 ? -14.513 26.517  -12.619 1.00 42.98 ? 470 PRO   A CG  1 
ATOM   2482 C  CD  . PRO   A 1 333 ? -14.228 27.133  -11.280 1.00 41.15 ? 470 PRO   A CD  1 
ATOM   2483 N  N   . GLY   A 1 334 ? -12.545 22.784  -10.573 1.00 39.19 ? 471 GLY   A N   1 
ATOM   2484 C  CA  . GLY   A 1 334 ? -11.400 22.039  -10.129 1.00 43.78 ? 471 GLY   A CA  1 
ATOM   2485 C  C   . GLY   A 1 334 ? -10.910 21.054  -11.169 1.00 39.94 ? 471 GLY   A C   1 
ATOM   2486 O  O   . GLY   A 1 334 ? -11.255 21.134  -12.360 1.00 37.89 ? 471 GLY   A O   1 
ATOM   2487 N  N   . GLY   A 1 335 ? -10.083 20.105  -10.723 1.00 42.50 ? 472 GLY   A N   1 
ATOM   2488 C  CA  . GLY   A 1 335 ? -9.568  19.074  -11.606 1.00 40.69 ? 472 GLY   A CA  1 
ATOM   2489 C  C   . GLY   A 1 335 ? -8.100  18.786  -11.376 1.00 42.33 ? 472 GLY   A C   1 
ATOM   2490 O  O   . GLY   A 1 335 ? -7.467  19.417  -10.525 1.00 40.83 ? 472 GLY   A O   1 
ATOM   2491 N  N   . GLY   A 1 336 ? -7.548  17.837  -12.129 1.00 40.30 ? 473 GLY   A N   1 
ATOM   2492 C  CA  . GLY   A 1 336 ? -6.147  17.501  -12.001 1.00 42.34 ? 473 GLY   A CA  1 
ATOM   2493 C  C   . GLY   A 1 336 ? -5.917  16.049  -11.646 1.00 45.49 ? 473 GLY   A C   1 
ATOM   2494 O  O   . GLY   A 1 336 ? -5.069  15.383  -12.247 1.00 45.55 ? 473 GLY   A O   1 
ATOM   2495 N  N   . ASP   A 1 337 ? -6.666  15.546  -10.668 1.00 43.57 ? 474 ASP   A N   1 
ATOM   2496 C  CA  . ASP   A 1 337 ? -6.642  14.131  -10.312 1.00 42.76 ? 474 ASP   A CA  1 
ATOM   2497 C  C   . ASP   A 1 337 ? -7.713  13.415  -11.129 1.00 39.39 ? 474 ASP   A C   1 
ATOM   2498 O  O   . ASP   A 1 337 ? -8.911  13.568  -10.866 1.00 37.44 ? 474 ASP   A O   1 
ATOM   2499 C  CB  . ASP   A 1 337 ? -6.863  13.958  -8.810  1.00 44.13 ? 474 ASP   A CB  1 
ATOM   2500 C  CG  . ASP   A 1 337 ? -7.075  12.506  -8.407  1.00 44.77 ? 474 ASP   A CG  1 
ATOM   2501 O  OD1 . ASP   A 1 337 ? -6.636  11.601  -9.147  1.00 40.63 ? 474 ASP   A OD1 1 
ATOM   2502 O  OD2 . ASP   A 1 337 ? -7.669  12.276  -7.333  1.00 48.36 ? 474 ASP   A OD2 1 
ATOM   2503 N  N   . MET   A 1 338 ? -7.278  12.639  -12.129 1.00 40.70 ? 475 MET   A N   1 
ATOM   2504 C  CA  . MET   A 1 338 ? -8.197  11.995  -13.063 1.00 36.88 ? 475 MET   A CA  1 
ATOM   2505 C  C   . MET   A 1 338 ? -9.034  10.906  -12.407 1.00 37.51 ? 475 MET   A C   1 
ATOM   2506 O  O   . MET   A 1 338 ? -10.008 10.439  -13.010 1.00 37.41 ? 475 MET   A O   1 
ATOM   2507 C  CB  . MET   A 1 338 ? -7.417  11.389  -14.232 1.00 38.68 ? 475 MET   A CB  1 
ATOM   2508 C  CG  . MET   A 1 338 ? -7.094  12.353  -15.374 1.00 39.83 ? 475 MET   A CG  1 
ATOM   2509 S  SD  . MET   A 1 338 ? -8.308  13.661  -15.607 1.00 42.73 ? 475 MET   A SD  1 
ATOM   2510 C  CE  . MET   A 1 338 ? -7.232  15.046  -15.970 1.00 40.43 ? 475 MET   A CE  1 
ATOM   2511 N  N   . ARG   A 1 339 ? -8.669  10.468  -11.201 1.00 37.31 ? 476 ARG   A N   1 
ATOM   2512 C  CA  . ARG   A 1 339 ? -9.462  9.444   -10.531 1.00 36.21 ? 476 ARG   A CA  1 
ATOM   2513 C  C   . ARG   A 1 339 ? -10.878 9.928   -10.242 1.00 35.34 ? 476 ARG   A C   1 
ATOM   2514 O  O   . ARG   A 1 339 ? -11.815 9.125   -10.232 1.00 34.61 ? 476 ARG   A O   1 
ATOM   2515 C  CB  . ARG   A 1 339 ? -8.763  8.994   -9.247  1.00 38.52 ? 476 ARG   A CB  1 
ATOM   2516 C  CG  . ARG   A 1 339 ? -7.434  8.316   -9.483  1.00 37.76 ? 476 ARG   A CG  1 
ATOM   2517 C  CD  . ARG   A 1 339 ? -6.708  8.090   -8.170  1.00 46.48 ? 476 ARG   A CD  1 
ATOM   2518 N  NE  . ARG   A 1 339 ? -6.522  9.333   -7.434  1.00 47.38 ? 476 ARG   A NE  1 
ATOM   2519 C  CZ  . ARG   A 1 339 ? -6.007  9.411   -6.215  1.00 53.63 ? 476 ARG   A CZ  1 
ATOM   2520 N  NH1 . ARG   A 1 339 ? -5.609  8.331   -5.563  1.00 54.39 ? 476 ARG   A NH1 1 
ATOM   2521 N  NH2 . ARG   A 1 339 ? -5.897  10.601  -5.632  1.00 53.00 ? 476 ARG   A NH2 1 
ATOM   2522 N  N   . ASP   A 1 340 ? -11.064 11.230  -10.011 1.00 36.53 ? 477 ASP   A N   1 
ATOM   2523 C  CA  . ASP   A 1 340 ? -12.421 11.739  -9.850  1.00 36.67 ? 477 ASP   A CA  1 
ATOM   2524 C  C   . ASP   A 1 340 ? -13.221 11.603  -11.144 1.00 37.76 ? 477 ASP   A C   1 
ATOM   2525 O  O   . ASP   A 1 340 ? -14.439 11.382  -11.097 1.00 36.74 ? 477 ASP   A O   1 
ATOM   2526 C  CB  . ASP   A 1 340 ? -12.386 13.194  -9.372  1.00 36.63 ? 477 ASP   A CB  1 
ATOM   2527 C  CG  . ASP   A 1 340 ? -11.696 13.354  -8.018  1.00 41.19 ? 477 ASP   A CG  1 
ATOM   2528 O  OD1 . ASP   A 1 340 ? -11.973 12.541  -7.115  1.00 41.17 ? 477 ASP   A OD1 1 
ATOM   2529 O  OD2 . ASP   A 1 340 ? -10.897 14.300  -7.862  1.00 51.18 ? 477 ASP   A OD2 1 
ATOM   2530 N  N   . ASN   A 1 341 ? -12.559 11.706  -12.302 1.00 36.25 ? 478 ASN   A N   1 
ATOM   2531 C  CA  . ASN   A 1 341 ? -13.244 11.441  -13.565 1.00 35.20 ? 478 ASN   A CA  1 
ATOM   2532 C  C   . ASN   A 1 341 ? -13.753 10.000  -13.620 1.00 30.80 ? 478 ASN   A C   1 
ATOM   2533 O  O   . ASN   A 1 341 ? -14.922 9.762   -13.940 1.00 32.87 ? 478 ASN   A O   1 
ATOM   2534 C  CB  . ASN   A 1 341 ? -12.318 11.750  -14.749 1.00 34.01 ? 478 ASN   A CB  1 
ATOM   2535 C  CG  . ASN   A 1 341 ? -11.897 13.223  -14.804 1.00 36.56 ? 478 ASN   A CG  1 
ATOM   2536 O  OD1 . ASN   A 1 341 ? -11.612 13.837  -13.776 1.00 35.53 ? 478 ASN   A OD1 1 
ATOM   2537 N  ND2 . ASN   A 1 341 ? -11.862 13.791  -16.011 1.00 37.38 ? 478 ASN   A ND2 1 
ATOM   2538 N  N   . TRP   A 1 342 ? -12.895 9.019   -13.308 1.00 32.89 ? 479 TRP   A N   1 
ATOM   2539 C  CA  . TRP   A 1 342 ? -13.356 7.627   -13.288 1.00 34.49 ? 479 TRP   A CA  1 
ATOM   2540 C  C   . TRP   A 1 342 ? -14.378 7.407   -12.179 1.00 34.42 ? 479 TRP   A C   1 
ATOM   2541 O  O   . TRP   A 1 342 ? -15.354 6.668   -12.359 1.00 33.38 ? 479 TRP   A O   1 
ATOM   2542 C  CB  . TRP   A 1 342 ? -12.182 6.650   -13.112 1.00 35.09 ? 479 TRP   A CB  1 
ATOM   2543 C  CG  . TRP   A 1 342 ? -10.868 7.109   -13.643 1.00 32.78 ? 479 TRP   A CG  1 
ATOM   2544 C  CD1 . TRP   A 1 342 ? -9.660  7.028   -13.015 1.00 34.70 ? 479 TRP   A CD1 1 
ATOM   2545 C  CD2 . TRP   A 1 342 ? -10.619 7.713   -14.915 1.00 33.25 ? 479 TRP   A CD2 1 
ATOM   2546 N  NE1 . TRP   A 1 342 ? -8.676  7.555   -13.814 1.00 32.77 ? 479 TRP   A NE1 1 
ATOM   2547 C  CE2 . TRP   A 1 342 ? -9.239  7.984   -14.986 1.00 30.90 ? 479 TRP   A CE2 1 
ATOM   2548 C  CE3 . TRP   A 1 342 ? -11.430 8.061   -15.995 1.00 30.81 ? 479 TRP   A CE3 1 
ATOM   2549 C  CZ2 . TRP   A 1 342 ? -8.654  8.580   -16.093 1.00 33.40 ? 479 TRP   A CZ2 1 
ATOM   2550 C  CZ3 . TRP   A 1 342 ? -10.848 8.652   -17.098 1.00 32.49 ? 479 TRP   A CZ3 1 
ATOM   2551 C  CH2 . TRP   A 1 342 ? -9.474  8.904   -17.142 1.00 34.54 ? 479 TRP   A CH2 1 
ATOM   2552 N  N   . ARG   A 1 343 ? -14.157 8.039   -11.022 1.00 31.21 ? 480 ARG   A N   1 
ATOM   2553 C  CA  . ARG   A 1 343 ? -15.105 7.982   -9.913  1.00 33.77 ? 480 ARG   A CA  1 
ATOM   2554 C  C   . ARG   A 1 343 ? -16.513 8.373   -10.342 1.00 32.97 ? 480 ARG   A C   1 
ATOM   2555 O  O   . ARG   A 1 343 ? -17.493 7.745   -9.927  1.00 34.72 ? 480 ARG   A O   1 
ATOM   2556 C  CB  . ARG   A 1 343 ? -14.637 8.912   -8.796  1.00 35.61 ? 480 ARG   A CB  1 
ATOM   2557 C  CG  . ARG   A 1 343 ? -14.603 8.314   -7.425  1.00 37.45 ? 480 ARG   A CG  1 
ATOM   2558 C  CD  . ARG   A 1 343 ? -14.206 9.392   -6.429  1.00 38.43 ? 480 ARG   A CD  1 
ATOM   2559 N  NE  . ARG   A 1 343 ? -12.759 9.543   -6.352  1.00 35.55 ? 480 ARG   A NE  1 
ATOM   2560 C  CZ  . ARG   A 1 343 ? -11.925 8.566   -6.028  1.00 35.22 ? 480 ARG   A CZ  1 
ATOM   2561 N  NH1 . ARG   A 1 343 ? -12.364 7.363   -5.700  1.00 38.53 ? 480 ARG   A NH1 1 
ATOM   2562 N  NH2 . ARG   A 1 343 ? -10.616 8.802   -6.034  1.00 39.49 ? 480 ARG   A NH2 1 
ATOM   2563 N  N   . SER   A 1 344 ? -16.635 9.432   -11.144 1.00 33.34 ? 481 SER   A N   1 
ATOM   2564 C  CA  . SER   A 1 344 ? -17.942 9.930   -11.560 1.00 35.39 ? 481 SER   A CA  1 
ATOM   2565 C  C   . SER   A 1 344 ? -18.732 8.920   -12.387 1.00 36.45 ? 481 SER   A C   1 
ATOM   2566 O  O   . SER   A 1 344 ? -19.938 9.117   -12.578 1.00 38.00 ? 481 SER   A O   1 
ATOM   2567 C  CB  . SER   A 1 344 ? -17.781 11.239  -12.349 1.00 34.07 ? 481 SER   A CB  1 
ATOM   2568 O  OG  . SER   A 1 344 ? -17.387 10.989  -13.686 1.00 37.02 ? 481 SER   A OG  1 
ATOM   2569 N  N   . GLU   A 1 345 ? -18.089 7.867   -12.893 1.00 33.92 ? 482 GLU   A N   1 
ATOM   2570 C  CA  . GLU   A 1 345 ? -18.786 6.783   -13.575 1.00 37.38 ? 482 GLU   A CA  1 
ATOM   2571 C  C   . GLU   A 1 345 ? -18.811 5.482   -12.783 1.00 39.83 ? 482 GLU   A C   1 
ATOM   2572 O  O   . GLU   A 1 345 ? -19.765 4.710   -12.911 1.00 38.84 ? 482 GLU   A O   1 
ATOM   2573 C  CB  . GLU   A 1 345 ? -18.151 6.514   -14.948 1.00 38.65 ? 482 GLU   A CB  1 
ATOM   2574 C  CG  . GLU   A 1 345 ? -18.152 7.715   -15.895 1.00 39.98 ? 482 GLU   A CG  1 
ATOM   2575 C  CD  . GLU   A 1 345 ? -19.556 8.197   -16.218 1.00 41.32 ? 482 GLU   A CD  1 
ATOM   2576 O  OE1 . GLU   A 1 345 ? -20.427 7.338   -16.467 1.00 46.95 ? 482 GLU   A OE1 1 
ATOM   2577 O  OE2 . GLU   A 1 345 ? -19.787 9.427   -16.227 1.00 42.73 ? 482 GLU   A OE2 1 
ATOM   2578 N  N   . LEU   A 1 346 ? -17.798 5.230   -11.961 1.00 37.10 ? 483 LEU   A N   1 
ATOM   2579 C  CA  . LEU   A 1 346 ? -17.704 4.019   -11.157 1.00 37.75 ? 483 LEU   A CA  1 
ATOM   2580 C  C   . LEU   A 1 346 ? -18.450 4.126   -9.830  1.00 35.52 ? 483 LEU   A C   1 
ATOM   2581 O  O   . LEU   A 1 346 ? -18.437 3.171   -9.048  1.00 34.52 ? 483 LEU   A O   1 
ATOM   2582 C  CB  . LEU   A 1 346 ? -16.230 3.694   -10.895 1.00 35.15 ? 483 LEU   A CB  1 
ATOM   2583 C  CG  . LEU   A 1 346 ? -15.462 3.131   -12.095 1.00 35.41 ? 483 LEU   A CG  1 
ATOM   2584 C  CD1 . LEU   A 1 346 ? -14.028 2.788   -11.710 1.00 34.09 ? 483 LEU   A CD1 1 
ATOM   2585 C  CD2 . LEU   A 1 346 ? -16.187 1.922   -12.673 1.00 34.70 ? 483 LEU   A CD2 1 
ATOM   2586 N  N   . TYR   A 1 347 ? -19.115 5.253   -9.571  1.00 37.62 ? 484 TYR   A N   1 
ATOM   2587 C  CA  . TYR   A 1 347 ? -19.659 5.521   -8.240  1.00 36.45 ? 484 TYR   A CA  1 
ATOM   2588 C  C   . TYR   A 1 347 ? -20.691 4.481   -7.802  1.00 36.20 ? 484 TYR   A C   1 
ATOM   2589 O  O   . TYR   A 1 347 ? -20.847 4.233   -6.600  1.00 39.82 ? 484 TYR   A O   1 
ATOM   2590 C  CB  . TYR   A 1 347 ? -20.265 6.930   -8.203  1.00 34.67 ? 484 TYR   A CB  1 
ATOM   2591 C  CG  . TYR   A 1 347 ? -21.551 7.076   -8.982  1.00 38.23 ? 484 TYR   A CG  1 
ATOM   2592 C  CD1 . TYR   A 1 347 ? -21.527 7.331   -10.348 1.00 37.96 ? 484 TYR   A CD1 1 
ATOM   2593 C  CD2 . TYR   A 1 347 ? -22.786 6.957   -8.358  1.00 39.89 ? 484 TYR   A CD2 1 
ATOM   2594 C  CE1 . TYR   A 1 347 ? -22.691 7.461   -11.073 1.00 38.27 ? 484 TYR   A CE1 1 
ATOM   2595 C  CE2 . TYR   A 1 347 ? -23.962 7.085   -9.078  1.00 36.60 ? 484 TYR   A CE2 1 
ATOM   2596 C  CZ  . TYR   A 1 347 ? -23.906 7.338   -10.436 1.00 42.33 ? 484 TYR   A CZ  1 
ATOM   2597 O  OH  . TYR   A 1 347 ? -25.075 7.465   -11.158 1.00 47.34 ? 484 TYR   A OH  1 
ATOM   2598 N  N   . LYS   A 1 348 ? -21.399 3.853   -8.735  1.00 37.84 ? 485 LYS   A N   1 
ATOM   2599 C  CA  . LYS   A 1 348 ? -22.463 2.931   -8.355  1.00 38.86 ? 485 LYS   A CA  1 
ATOM   2600 C  C   . LYS   A 1 348 ? -22.018 1.473   -8.335  1.00 39.73 ? 485 LYS   A C   1 
ATOM   2601 O  O   . LYS   A 1 348 ? -22.866 0.582   -8.237  1.00 41.36 ? 485 LYS   A O   1 
ATOM   2602 C  CB  . LYS   A 1 348 ? -23.672 3.106   -9.277  1.00 39.60 ? 485 LYS   A CB  1 
ATOM   2603 C  CG  . LYS   A 1 348 ? -23.427 2.826   -10.754 1.00 45.79 ? 485 LYS   A CG  1 
ATOM   2604 C  CD  . LYS   A 1 348 ? -24.743 2.584   -11.486 1.00 43.45 ? 485 LYS   A CD  1 
ATOM   2605 C  CE  . LYS   A 1 348 ? -24.651 3.010   -12.939 1.00 50.00 ? 485 LYS   A CE  1 
ATOM   2606 N  NZ  . LYS   A 1 348 ? -25.874 3.755   -13.358 1.00 53.72 ? 485 LYS   A NZ  1 
ATOM   2607 N  N   . TYR   A 1 349 ? -20.719 1.206   -8.398  1.00 35.16 ? 486 TYR   A N   1 
ATOM   2608 C  CA  . TYR   A 1 349 ? -20.213 -0.156  -8.419  1.00 38.27 ? 486 TYR   A CA  1 
ATOM   2609 C  C   . TYR   A 1 349 ? -19.297 -0.399  -7.228  1.00 38.68 ? 486 TYR   A C   1 
ATOM   2610 O  O   . TYR   A 1 349 ? -18.629 0.516   -6.734  1.00 36.90 ? 486 TYR   A O   1 
ATOM   2611 C  CB  . TYR   A 1 349 ? -19.451 -0.453  -9.722  1.00 34.33 ? 486 TYR   A CB  1 
ATOM   2612 C  CG  . TYR   A 1 349 ? -20.280 -0.323  -10.978 1.00 39.31 ? 486 TYR   A CG  1 
ATOM   2613 C  CD1 . TYR   A 1 349 ? -21.293 -1.232  -11.264 1.00 40.36 ? 486 TYR   A CD1 1 
ATOM   2614 C  CD2 . TYR   A 1 349 ? -20.037 0.697   -11.887 1.00 37.97 ? 486 TYR   A CD2 1 
ATOM   2615 C  CE1 . TYR   A 1 349 ? -22.047 -1.119  -12.412 1.00 40.13 ? 486 TYR   A CE1 1 
ATOM   2616 C  CE2 . TYR   A 1 349 ? -20.781 0.817   -13.038 1.00 37.83 ? 486 TYR   A CE2 1 
ATOM   2617 C  CZ  . TYR   A 1 349 ? -21.784 -0.091  -13.297 1.00 39.60 ? 486 TYR   A CZ  1 
ATOM   2618 O  OH  . TYR   A 1 349 ? -22.524 0.035   -14.448 1.00 43.99 ? 486 TYR   A OH  1 
ATOM   2619 N  N   . LYS   A 1 350 ? -19.263 -1.651  -6.782  1.00 37.91 ? 487 LYS   A N   1 
ATOM   2620 C  CA  . LYS   A 1 350 ? -18.359 -2.063  -5.721  1.00 40.94 ? 487 LYS   A CA  1 
ATOM   2621 C  C   . LYS   A 1 350 ? -18.141 -3.564  -5.845  1.00 39.07 ? 487 LYS   A C   1 
ATOM   2622 O  O   . LYS   A 1 350 ? -19.041 -4.291  -6.274  1.00 39.20 ? 487 LYS   A O   1 
ATOM   2623 C  CB  . LYS   A 1 350 ? -18.919 -1.683  -4.344  1.00 40.17 ? 487 LYS   A CB  1 
ATOM   2624 C  CG  . LYS   A 1 350 ? -19.419 -2.844  -3.506  1.00 43.48 ? 487 LYS   A CG  1 
ATOM   2625 C  CD  . LYS   A 1 350 ? -19.387 -2.490  -2.029  1.00 49.02 ? 487 LYS   A CD  1 
ATOM   2626 C  CE  . LYS   A 1 350 ? -20.615 -3.020  -1.303  1.00 50.32 ? 487 LYS   A CE  1 
ATOM   2627 N  NZ  . LYS   A 1 350 ? -20.383 -3.093  0.169   1.00 50.50 ? 487 LYS   A NZ  1 
ATOM   2628 N  N   . VAL   A 1 351 ? -16.940 -4.017  -5.498  1.00 39.02 ? 488 VAL   A N   1 
ATOM   2629 C  CA  . VAL   A 1 351 ? -16.552 -5.411  -5.678  1.00 42.29 ? 488 VAL   A CA  1 
ATOM   2630 C  C   . VAL   A 1 351 ? -16.698 -6.141  -4.349  1.00 44.27 ? 488 VAL   A C   1 
ATOM   2631 O  O   . VAL   A 1 351 ? -16.250 -5.646  -3.305  1.00 43.34 ? 488 VAL   A O   1 
ATOM   2632 C  CB  . VAL   A 1 351 ? -15.116 -5.524  -6.219  1.00 40.81 ? 488 VAL   A CB  1 
ATOM   2633 C  CG1 . VAL   A 1 351 ? -14.608 -6.957  -6.083  1.00 41.36 ? 488 VAL   A CG1 1 
ATOM   2634 C  CG2 . VAL   A 1 351 ? -15.049 -5.057  -7.674  1.00 37.63 ? 488 VAL   A CG2 1 
ATOM   2635 N  N   . VAL   A 1 352 ? -17.329 -7.315  -4.385  1.00 44.14 ? 489 VAL   A N   1 
ATOM   2636 C  CA  . VAL   A 1 352 ? -17.515 -8.151  -3.206  1.00 47.21 ? 489 VAL   A CA  1 
ATOM   2637 C  C   . VAL   A 1 352 ? -17.019 -9.556  -3.513  1.00 49.57 ? 489 VAL   A C   1 
ATOM   2638 O  O   . VAL   A 1 352 ? -17.052 -10.010 -4.662  1.00 46.46 ? 489 VAL   A O   1 
ATOM   2639 C  CB  . VAL   A 1 352 ? -18.988 -8.202  -2.740  1.00 48.76 ? 489 VAL   A CB  1 
ATOM   2640 C  CG1 . VAL   A 1 352 ? -19.444 -6.840  -2.240  1.00 47.22 ? 489 VAL   A CG1 1 
ATOM   2641 C  CG2 . VAL   A 1 352 ? -19.884 -8.708  -3.859  1.00 48.06 ? 489 VAL   A CG2 1 
ATOM   2642 N  N   . GLN   A 1 353 ? -16.565 -10.247 -2.470  1.00 50.50 ? 490 GLN   A N   1 
ATOM   2643 C  CA  . GLN   A 1 353 ? -16.128 -11.631 -2.575  1.00 51.24 ? 490 GLN   A CA  1 
ATOM   2644 C  C   . GLN   A 1 353 ? -17.275 -12.561 -2.203  1.00 51.91 ? 490 GLN   A C   1 
ATOM   2645 O  O   . GLN   A 1 353 ? -18.021 -12.295 -1.256  1.00 54.89 ? 490 GLN   A O   1 
ATOM   2646 C  CB  . GLN   A 1 353 ? -14.926 -11.894 -1.668  1.00 52.83 ? 490 GLN   A CB  1 
ATOM   2647 C  CG  . GLN   A 1 353 ? -14.198 -13.190 -1.975  1.00 55.69 ? 490 GLN   A CG  1 
ATOM   2648 C  CD  . GLN   A 1 353 ? -12.916 -13.348 -1.179  1.00 55.11 ? 490 GLN   A CD  1 
ATOM   2649 O  OE1 . GLN   A 1 353 ? -12.418 -12.392 -0.581  1.00 59.91 ? 490 GLN   A OE1 1 
ATOM   2650 N  NE2 . GLN   A 1 353 ? -12.373 -14.560 -1.171  1.00 57.15 ? 490 GLN   A NE2 1 
ATOM   2651 N  N   . ILE   A 1 354 ? -17.417 -13.649 -2.958  1.00 54.13 ? 491 ILE   A N   1 
ATOM   2652 C  CA  . ILE   A 1 354 ? -18.458 -14.642 -2.695  1.00 57.79 ? 491 ILE   A CA  1 
ATOM   2653 C  C   . ILE   A 1 354 ? -17.923 -15.572 -1.609  1.00 60.44 ? 491 ILE   A C   1 
ATOM   2654 O  O   . ILE   A 1 354 ? -17.094 -16.442 -1.873  1.00 61.33 ? 491 ILE   A O   1 
ATOM   2655 C  CB  . ILE   A 1 354 ? -18.855 -15.407 -3.960  1.00 58.09 ? 491 ILE   A CB  1 
ATOM   2656 C  CG1 . ILE   A 1 354 ? -19.566 -14.477 -4.944  1.00 53.87 ? 491 ILE   A CG1 1 
ATOM   2657 C  CG2 . ILE   A 1 354 ? -19.746 -16.598 -3.618  1.00 60.40 ? 491 ILE   A CG2 1 
ATOM   2658 C  CD1 . ILE   A 1 354 ? -21.084 -14.523 -4.848  1.00 55.76 ? 491 ILE   A CD1 1 
ATOM   2659 N  N   . GLU   A 1 355 ? -18.392 -15.383 -0.379  1.00 64.93 ? 492 GLU   A N   1 
ATOM   2660 C  CA  . GLU   A 1 355 ? -17.877 -16.121 0.766   1.00 68.71 ? 492 GLU   A CA  1 
ATOM   2661 C  C   . GLU   A 1 355 ? -18.100 -17.621 0.619   1.00 73.73 ? 492 GLU   A C   1 
ATOM   2662 O  O   . GLU   A 1 355 ? -17.389 -18.423 1.226   1.00 75.07 ? 492 GLU   A O   1 
ATOM   2663 C  CB  . GLU   A 1 355 ? -18.532 -15.621 2.053   1.00 67.48 ? 492 GLU   A CB  1 
ATOM   2664 C  CG  . GLU   A 1 355 ? -17.764 -14.509 2.739   1.00 69.88 ? 492 GLU   A CG  1 
ATOM   2665 C  CD  . GLU   A 1 355 ? -16.669 -15.018 3.662   1.00 78.01 ? 492 GLU   A CD  1 
ATOM   2666 O  OE1 . GLU   A 1 355 ? -15.652 -15.548 3.161   1.00 78.05 ? 492 GLU   A OE1 1 
ATOM   2667 O  OE2 . GLU   A 1 355 ? -16.821 -14.862 4.892   1.00 81.17 ? 492 GLU   A OE2 1 
ATOM   2668 O  OXT . GLU   A 1 355 ? -19.001 -18.064 -0.097  1.00 74.12 ? 492 GLU   A OXT 1 
HETATM 2669 C  C1  . NAG   B 2 .   ? -25.046 11.082  0.787   1.00 48.50 ? 501 NAG   A C1  1 
HETATM 2670 C  C2  . NAG   B 2 .   ? -24.650 12.275  1.647   1.00 50.29 ? 501 NAG   A C2  1 
HETATM 2671 C  C3  . NAG   B 2 .   ? -24.278 11.810  3.047   1.00 50.79 ? 501 NAG   A C3  1 
HETATM 2672 C  C4  . NAG   B 2 .   ? -25.411 10.984  3.642   1.00 53.85 ? 501 NAG   A C4  1 
HETATM 2673 C  C5  . NAG   B 2 .   ? -25.822 9.860   2.691   1.00 54.25 ? 501 NAG   A C5  1 
HETATM 2674 C  C6  . NAG   B 2 .   ? -27.050 9.114   3.158   1.00 54.99 ? 501 NAG   A C6  1 
HETATM 2675 C  C7  . NAG   B 2 .   ? -23.753 14.120  0.307   1.00 49.76 ? 501 NAG   A C7  1 
HETATM 2676 C  C8  . NAG   B 2 .   ? -22.522 14.769  -0.252  1.00 48.25 ? 501 NAG   A C8  1 
HETATM 2677 N  N2  . NAG   B 2 .   ? -23.557 13.021  1.042   1.00 44.65 ? 501 NAG   A N2  1 
HETATM 2678 O  O3  . NAG   B 2 .   ? -24.029 12.953  3.857   1.00 48.42 ? 501 NAG   A O3  1 
HETATM 2679 O  O4  . NAG   B 2 .   ? -25.007 10.423  4.886   1.00 56.21 ? 501 NAG   A O4  1 
HETATM 2680 O  O5  . NAG   B 2 .   ? -26.138 10.395  1.396   1.00 48.90 ? 501 NAG   A O5  1 
HETATM 2681 O  O6  . NAG   B 2 .   ? -26.716 8.099   4.094   1.00 61.14 ? 501 NAG   A O6  1 
HETATM 2682 O  O7  . NAG   B 2 .   ? -24.876 14.572  0.104   1.00 50.02 ? 501 NAG   A O7  1 
HETATM 2683 C  C1  . NAG   C 2 .   ? -34.373 -0.995  -9.025  1.00 62.05 ? 502 NAG   A C1  1 
HETATM 2684 C  C2  . NAG   C 2 .   ? -35.314 0.025   -9.652  1.00 64.69 ? 502 NAG   A C2  1 
HETATM 2685 C  C3  . NAG   C 2 .   ? -35.985 -0.562  -10.888 1.00 66.69 ? 502 NAG   A C3  1 
HETATM 2686 C  C4  . NAG   C 2 .   ? -34.935 -1.102  -11.850 1.00 64.91 ? 502 NAG   A C4  1 
HETATM 2687 C  C5  . NAG   C 2 .   ? -33.988 -2.058  -11.126 1.00 65.15 ? 502 NAG   A C5  1 
HETATM 2688 C  C6  . NAG   C 2 .   ? -32.843 -2.530  -11.994 1.00 66.21 ? 502 NAG   A C6  1 
HETATM 2689 C  C7  . NAG   C 2 .   ? -36.342 1.713   -8.202  1.00 65.64 ? 502 NAG   A C7  1 
HETATM 2690 C  C8  . NAG   C 2 .   ? -37.449 1.998   -7.232  1.00 63.03 ? 502 NAG   A C8  1 
HETATM 2691 N  N2  . NAG   C 2 .   ? -36.310 0.474   -8.697  1.00 64.75 ? 502 NAG   A N2  1 
HETATM 2692 O  O3  . NAG   C 2 .   ? -36.765 0.450   -11.518 1.00 68.29 ? 502 NAG   A O3  1 
HETATM 2693 O  O4  . NAG   C 2 .   ? -35.563 -1.804  -12.917 1.00 63.70 ? 502 NAG   A O4  1 
HETATM 2694 O  O5  . NAG   C 2 .   ? -33.406 -1.407  -9.986  1.00 66.66 ? 502 NAG   A O5  1 
HETATM 2695 O  O6  . NAG   C 2 .   ? -32.047 -3.513  -11.343 1.00 67.17 ? 502 NAG   A O6  1 
HETATM 2696 O  O7  . NAG   C 2 .   ? -35.519 2.568   -8.528  1.00 67.73 ? 502 NAG   A O7  1 
HETATM 2697 C  C1  . NAG   D 2 .   ? -17.219 12.921  -27.096 1.00 40.96 ? 503 NAG   A C1  1 
HETATM 2698 C  C2  . NAG   D 2 .   ? -15.808 13.126  -27.647 1.00 40.97 ? 503 NAG   A C2  1 
HETATM 2699 C  C3  . NAG   D 2 .   ? -15.862 13.579  -29.104 1.00 44.00 ? 503 NAG   A C3  1 
HETATM 2700 C  C4  . NAG   D 2 .   ? -16.727 12.640  -29.934 1.00 43.80 ? 503 NAG   A C4  1 
HETATM 2701 C  C5  . NAG   D 2 .   ? -18.101 12.506  -29.290 1.00 44.07 ? 503 NAG   A C5  1 
HETATM 2702 C  C6  . NAG   D 2 .   ? -19.004 11.521  -29.999 1.00 42.22 ? 503 NAG   A C6  1 
HETATM 2703 C  C7  . NAG   D 2 .   ? -13.960 13.815  -26.178 1.00 42.59 ? 503 NAG   A C7  1 
HETATM 2704 C  C8  . NAG   D 2 .   ? -13.347 14.952  -25.413 1.00 37.63 ? 503 NAG   A C8  1 
HETATM 2705 N  N2  . NAG   D 2 .   ? -15.082 14.098  -26.847 1.00 40.46 ? 503 NAG   A N2  1 
HETATM 2706 O  O3  . NAG   D 2 .   ? -14.536 13.618  -29.620 1.00 49.10 ? 503 NAG   A O3  1 
HETATM 2707 O  O4  . NAG   D 2 .   ? -16.886 13.163  -31.247 1.00 44.49 ? 503 NAG   A O4  1 
HETATM 2708 O  O5  . NAG   D 2 .   ? -17.948 12.037  -27.946 1.00 37.37 ? 503 NAG   A O5  1 
HETATM 2709 O  O6  . NAG   D 2 .   ? -18.608 10.176  -29.771 1.00 43.82 ? 503 NAG   A O6  1 
HETATM 2710 O  O7  . NAG   D 2 .   ? -13.465 12.694  -26.186 1.00 39.93 ? 503 NAG   A O7  1 
HETATM 2711 C  C1  . NAG   E 2 .   ? -15.698 16.527  7.491   1.00 50.79 ? 504 NAG   A C1  1 
HETATM 2712 C  C2  . NAG   E 2 .   ? -15.414 15.645  8.718   1.00 54.05 ? 504 NAG   A C2  1 
HETATM 2713 C  C3  . NAG   E 2 .   ? -15.433 16.482  10.003  1.00 56.88 ? 504 NAG   A C3  1 
HETATM 2714 C  C4  . NAG   E 2 .   ? -14.532 17.703  9.868   1.00 58.71 ? 504 NAG   A C4  1 
HETATM 2715 C  C5  . NAG   E 2 .   ? -14.927 18.491  8.627   1.00 56.00 ? 504 NAG   A C5  1 
HETATM 2716 C  C6  . NAG   E 2 .   ? -14.063 19.708  8.386   1.00 52.34 ? 504 NAG   A C6  1 
HETATM 2717 C  C7  . NAG   E 2 .   ? -16.036 13.270  8.849   1.00 57.05 ? 504 NAG   A C7  1 
HETATM 2718 C  C8  . NAG   E 2 .   ? -17.170 12.294  8.940   1.00 56.05 ? 504 NAG   A C8  1 
HETATM 2719 N  N2  . NAG   E 2 .   ? -16.379 14.561  8.806   1.00 52.74 ? 504 NAG   A N2  1 
HETATM 2720 O  O3  . NAG   E 2 .   ? -14.999 15.681  11.097  1.00 58.56 ? 504 NAG   A O3  1 
HETATM 2721 O  O4  . NAG   E 2 .   ? -14.646 18.536  11.016  1.00 62.81 ? 504 NAG   A O4  1 
HETATM 2722 O  O5  . NAG   E 2 .   ? -14.795 17.644  7.478   1.00 50.00 ? 504 NAG   A O5  1 
HETATM 2723 O  O6  . NAG   E 2 .   ? -12.683 19.402  8.529   1.00 60.24 ? 504 NAG   A O6  1 
HETATM 2724 O  O7  . NAG   E 2 .   ? -14.863 12.905  8.816   1.00 55.78 ? 504 NAG   A O7  1 
HETATM 2725 C  C1  . NAG   F 2 .   ? -32.645 18.166  -12.991 1.00 49.54 ? 505 NAG   A C1  1 
HETATM 2726 C  C2  . NAG   F 2 .   ? -34.110 18.160  -13.421 1.00 52.63 ? 505 NAG   A C2  1 
HETATM 2727 C  C3  . NAG   F 2 .   ? -34.804 19.442  -12.966 1.00 55.45 ? 505 NAG   A C3  1 
HETATM 2728 C  C4  . NAG   F 2 .   ? -34.591 19.674  -11.476 1.00 53.35 ? 505 NAG   A C4  1 
HETATM 2729 C  C5  . NAG   F 2 .   ? -33.105 19.615  -11.142 1.00 52.54 ? 505 NAG   A C5  1 
HETATM 2730 C  C6  . NAG   F 2 .   ? -32.822 19.706  -9.661  1.00 51.45 ? 505 NAG   A C6  1 
HETATM 2731 C  C7  . NAG   F 2 .   ? -34.635 16.876  -15.450 1.00 55.48 ? 505 NAG   A C7  1 
HETATM 2732 C  C8  . NAG   F 2 .   ? -34.681 16.897  -16.950 1.00 54.87 ? 505 NAG   A C8  1 
HETATM 2733 N  N2  . NAG   F 2 .   ? -34.222 18.004  -14.862 1.00 52.77 ? 505 NAG   A N2  1 
HETATM 2734 O  O3  . NAG   F 2 .   ? -36.196 19.338  -13.239 1.00 56.10 ? 505 NAG   A O3  1 
HETATM 2735 O  O4  . NAG   F 2 .   ? -35.101 20.950  -11.107 1.00 56.77 ? 505 NAG   A O4  1 
HETATM 2736 O  O5  . NAG   F 2 .   ? -32.559 18.366  -11.588 1.00 51.98 ? 505 NAG   A O5  1 
HETATM 2737 O  O6  . NAG   F 2 .   ? -31.429 19.618  -9.396  1.00 51.94 ? 505 NAG   A O6  1 
HETATM 2738 O  O7  . NAG   F 2 .   ? -34.961 15.885  -14.803 1.00 55.80 ? 505 NAG   A O7  1 
HETATM 2739 C  C1  . NAG   G 2 .   ? -19.691 23.211  -34.410 1.00 53.27 ? 506 NAG   A C1  1 
HETATM 2740 C  C2  . NAG   G 2 .   ? -20.927 22.992  -35.281 1.00 54.76 ? 506 NAG   A C2  1 
HETATM 2741 C  C3  . NAG   G 2 .   ? -20.568 23.160  -36.756 1.00 56.97 ? 506 NAG   A C3  1 
HETATM 2742 C  C4  . NAG   G 2 .   ? -19.896 24.506  -36.991 1.00 56.67 ? 506 NAG   A C4  1 
HETATM 2743 C  C5  . NAG   G 2 .   ? -18.700 24.671  -36.058 1.00 55.47 ? 506 NAG   A C5  1 
HETATM 2744 C  C6  . NAG   G 2 .   ? -18.060 26.038  -36.148 1.00 57.64 ? 506 NAG   A C6  1 
HETATM 2745 C  C7  . NAG   G 2 .   ? -22.453 21.452  -34.122 1.00 55.68 ? 506 NAG   A C7  1 
HETATM 2746 C  C8  . NAG   G 2 .   ? -22.940 20.038  -34.022 1.00 55.24 ? 506 NAG   A C8  1 
HETATM 2747 N  N2  . NAG   G 2 .   ? -21.511 21.682  -35.043 1.00 52.27 ? 506 NAG   A N2  1 
HETATM 2748 O  O3  . NAG   G 2 .   ? -21.750 23.062  -37.543 1.00 57.92 ? 506 NAG   A O3  1 
HETATM 2749 O  O4  . NAG   G 2 .   ? -19.448 24.596  -38.338 1.00 62.83 ? 506 NAG   A O4  1 
HETATM 2750 O  O5  . NAG   G 2 .   ? -19.119 24.500  -34.696 1.00 55.02 ? 506 NAG   A O5  1 
HETATM 2751 O  O6  . NAG   G 2 .   ? -18.739 26.991  -35.339 1.00 58.67 ? 506 NAG   A O6  1 
HETATM 2752 O  O7  . NAG   G 2 .   ? -22.892 22.345  -33.402 1.00 58.36 ? 506 NAG   A O7  1 
HETATM 2753 C  C1  . NAG   H 2 .   ? -30.161 27.216  -26.956 1.00 54.48 ? 507 NAG   A C1  1 
HETATM 2754 C  C2  . NAG   H 2 .   ? -30.730 27.084  -28.379 1.00 55.21 ? 507 NAG   A C2  1 
HETATM 2755 C  C3  . NAG   H 2 .   ? -32.232 27.379  -28.396 1.00 55.67 ? 507 NAG   A C3  1 
HETATM 2756 C  C4  . NAG   H 2 .   ? -32.959 26.571  -27.330 1.00 59.95 ? 507 NAG   A C4  1 
HETATM 2757 C  C5  . NAG   H 2 .   ? -32.320 26.841  -25.979 1.00 54.51 ? 507 NAG   A C5  1 
HETATM 2758 C  C6  . NAG   H 2 .   ? -32.968 26.084  -24.841 1.00 56.73 ? 507 NAG   A C6  1 
HETATM 2759 C  C7  . NAG   H 2 .   ? -29.522 27.597  -30.463 1.00 56.77 ? 507 NAG   A C7  1 
HETATM 2760 C  C8  . NAG   H 2 .   ? -28.837 28.668  -31.259 1.00 57.34 ? 507 NAG   A C8  1 
HETATM 2761 N  N2  . NAG   H 2 .   ? -30.031 27.979  -29.288 1.00 55.78 ? 507 NAG   A N2  1 
HETATM 2762 O  O3  . NAG   H 2 .   ? -32.754 27.063  -29.681 1.00 57.37 ? 507 NAG   A O3  1 
HETATM 2763 O  O4  . NAG   H 2 .   ? -34.335 26.930  -27.285 1.00 59.44 ? 507 NAG   A O4  1 
HETATM 2764 O  O5  . NAG   H 2 .   ? -30.948 26.435  -26.039 1.00 54.41 ? 507 NAG   A O5  1 
HETATM 2765 O  O6  . NAG   H 2 .   ? -32.348 24.826  -24.611 1.00 60.92 ? 507 NAG   A O6  1 
HETATM 2766 O  O7  . NAG   H 2 .   ? -29.609 26.440  -30.867 1.00 56.10 ? 507 NAG   A O7  1 
HETATM 2767 C  C1  . NAG   I 2 .   ? -9.530  34.005  -19.205 1.00 51.78 ? 508 NAG   A C1  1 
HETATM 2768 C  C2  . NAG   I 2 .   ? -8.124  34.248  -18.651 1.00 51.59 ? 508 NAG   A C2  1 
HETATM 2769 C  C3  . NAG   I 2 .   ? -8.125  35.436  -17.688 1.00 54.79 ? 508 NAG   A C3  1 
HETATM 2770 C  C4  . NAG   I 2 .   ? -8.791  36.653  -18.318 1.00 56.20 ? 508 NAG   A C4  1 
HETATM 2771 C  C5  . NAG   I 2 .   ? -10.170 36.282  -18.845 1.00 55.45 ? 508 NAG   A C5  1 
HETATM 2772 C  C6  . NAG   I 2 .   ? -10.858 37.419  -19.566 1.00 58.16 ? 508 NAG   A C6  1 
HETATM 2773 C  C7  . NAG   I 2 .   ? -6.340  32.714  -17.926 1.00 55.70 ? 508 NAG   A C7  1 
HETATM 2774 C  C8  . NAG   I 2 .   ? -6.026  31.443  -17.191 1.00 54.35 ? 508 NAG   A C8  1 
HETATM 2775 N  N2  . NAG   I 2 .   ? -7.633  33.053  -17.982 1.00 52.33 ? 508 NAG   A N2  1 
HETATM 2776 O  O3  . NAG   I 2 .   ? -6.784  35.760  -17.342 1.00 57.85 ? 508 NAG   A O3  1 
HETATM 2777 O  O4  . NAG   I 2 .   ? -8.926  37.688  -17.350 1.00 62.31 ? 508 NAG   A O4  1 
HETATM 2778 O  O5  . NAG   I 2 .   ? -10.038 35.211  -19.786 1.00 52.08 ? 508 NAG   A O5  1 
HETATM 2779 O  O6  . NAG   I 2 .   ? -10.326 37.614  -20.869 1.00 56.98 ? 508 NAG   A O6  1 
HETATM 2780 O  O7  . NAG   I 2 .   ? -5.464  33.402  -18.441 1.00 57.21 ? 508 NAG   A O7  1 
HETATM 2781 C  C1  . NAG   J 2 .   ? -24.958 13.508  -25.823 1.00 58.67 ? 509 NAG   A C1  1 
HETATM 2782 C  C2  . NAG   J 2 .   ? -24.747 12.002  -26.034 1.00 62.53 ? 509 NAG   A C2  1 
HETATM 2783 C  C3  . NAG   J 2 .   ? -25.950 11.374  -26.736 1.00 67.76 ? 509 NAG   A C3  1 
HETATM 2784 C  C4  . NAG   J 2 .   ? -27.236 11.718  -26.000 1.00 68.78 ? 509 NAG   A C4  1 
HETATM 2785 C  C5  . NAG   J 2 .   ? -27.358 13.229  -25.879 1.00 66.91 ? 509 NAG   A C5  1 
HETATM 2786 C  C6  . NAG   J 2 .   ? -28.574 13.666  -25.095 1.00 65.66 ? 509 NAG   A C6  1 
HETATM 2787 C  C7  . NAG   J 2 .   ? -22.472 11.105  -26.291 1.00 57.94 ? 509 NAG   A C7  1 
HETATM 2788 C  C8  . NAG   J 2 .   ? -21.303 10.943  -27.215 1.00 55.05 ? 509 NAG   A C8  1 
HETATM 2789 N  N2  . NAG   J 2 .   ? -23.529 11.755  -26.791 1.00 59.91 ? 509 NAG   A N2  1 
HETATM 2790 O  O3  . NAG   J 2 .   ? -25.778 9.961   -26.770 1.00 68.71 ? 509 NAG   A O3  1 
HETATM 2791 O  O4  . NAG   J 2 .   ? -28.364 11.203  -26.698 1.00 74.02 ? 509 NAG   A O4  1 
HETATM 2792 O  O5  . NAG   J 2 .   ? -26.214 13.737  -25.180 1.00 64.10 ? 509 NAG   A O5  1 
HETATM 2793 O  O6  . NAG   J 2 .   ? -28.214 14.126  -23.799 1.00 64.44 ? 509 NAG   A O6  1 
HETATM 2794 O  O7  . NAG   J 2 .   ? -22.460 10.666  -25.144 1.00 59.03 ? 509 NAG   A O7  1 
HETATM 2795 N  N1  . EPE   K 3 .   ? -5.117  -5.495  -17.712 1.00 44.41 ? 510 EPE   A N1  1 
HETATM 2796 C  C2  . EPE   K 3 .   ? -4.614  -4.854  -16.486 1.00 42.15 ? 510 EPE   A C2  1 
HETATM 2797 C  C3  . EPE   K 3 .   ? -5.758  -4.759  -15.487 1.00 44.52 ? 510 EPE   A C3  1 
HETATM 2798 N  N4  . EPE   K 3 .   ? -7.020  -4.314  -16.062 1.00 41.25 ? 510 EPE   A N4  1 
HETATM 2799 C  C5  . EPE   K 3 .   ? -7.338  -4.650  -17.434 1.00 40.74 ? 510 EPE   A C5  1 
HETATM 2800 C  C6  . EPE   K 3 .   ? -6.116  -4.627  -18.335 1.00 40.19 ? 510 EPE   A C6  1 
HETATM 2801 C  C7  . EPE   K 3 .   ? -8.146  -4.132  -15.166 1.00 40.73 ? 510 EPE   A C7  1 
HETATM 2802 C  C8  . EPE   K 3 .   ? -7.878  -3.110  -14.070 1.00 41.19 ? 510 EPE   A C8  1 
HETATM 2803 O  O8  . EPE   K 3 .   ? -6.785  -3.527  -13.283 1.00 48.00 ? 510 EPE   A O8  1 
HETATM 2804 C  C9  . EPE   K 3 .   ? -4.036  -5.714  -18.671 1.00 44.96 ? 510 EPE   A C9  1 
HETATM 2805 C  C10 . EPE   K 3 .   ? -4.175  -7.125  -19.235 1.00 43.78 ? 510 EPE   A C10 1 
HETATM 2806 S  S   . EPE   K 3 .   ? -2.636  -7.649  -20.027 1.00 43.28 ? 510 EPE   A S   1 
HETATM 2807 O  O1S . EPE   K 3 .   ? -2.035  -6.500  -20.691 1.00 43.80 ? 510 EPE   A O1S 1 
HETATM 2808 O  O2S . EPE   K 3 .   ? -1.724  -8.145  -18.992 1.00 41.61 ? 510 EPE   A O2S 1 
HETATM 2809 O  O3S . EPE   K 3 .   ? -2.912  -8.701  -21.004 1.00 40.96 ? 510 EPE   A O3S 1 
HETATM 2810 C  C10 . A1ATD L 4 .   ? -3.231  17.424  -15.154 1.00 44.96 ? 511 A1ATD A C10 1 
HETATM 2811 C  CD  . A1ATD L 4 .   ? -1.371  11.599  -8.867  1.00 78.56 ? 511 A1ATD A CD  1 
HETATM 2812 N  NE  . A1ATD L 4 .   ? -1.641  11.421  -7.459  1.00 81.30 ? 511 A1ATD A NE  1 
HETATM 2813 C  CZ  . A1ATD L 4 .   ? -2.489  10.314  -7.043  1.00 82.26 ? 511 A1ATD A CZ  1 
HETATM 2814 N  NH1 . A1ATD L 4 .   ? -2.732  10.140  -5.823  1.00 82.78 ? 511 A1ATD A NH1 1 
HETATM 2815 N  NH2 . A1ATD L 4 .   ? -2.982  9.536   -7.896  1.00 86.62 ? 511 A1ATD A NH2 1 
HETATM 2816 C  C01 . A1ATD L 4 .   ? -0.800  12.975  -9.188  1.00 79.14 ? 511 A1ATD A C01 1 
HETATM 2817 C  C03 . A1ATD L 4 .   ? 1.143   13.555  -9.888  1.00 78.83 ? 511 A1ATD A C03 1 
HETATM 2818 C  C04 . A1ATD L 4 .   ? 1.276   14.866  -10.654 1.00 80.66 ? 511 A1ATD A C04 1 
HETATM 2819 C  C06 . A1ATD L 4 .   ? 0.029   16.904  -11.356 1.00 66.45 ? 511 A1ATD A C06 1 
HETATM 2820 C  C08 . A1ATD L 4 .   ? -2.367  17.259  -12.612 1.00 55.42 ? 511 A1ATD A C08 1 
HETATM 2821 C  C09 . A1ATD L 4 .   ? -2.099  17.595  -14.086 1.00 48.72 ? 511 A1ATD A C09 1 
HETATM 2822 C  C13 . A1ATD L 4 .   ? -3.696  17.326  -17.699 1.00 44.51 ? 511 A1ATD A C13 1 
HETATM 2823 C  C14 . A1ATD L 4 .   ? -5.075  17.255  -17.585 1.00 42.21 ? 511 A1ATD A C14 1 
HETATM 2824 C  C15 . A1ATD L 4 .   ? -5.857  17.087  -18.726 1.00 46.35 ? 511 A1ATD A C15 1 
HETATM 2825 C  C17 . A1ATD L 4 .   ? -5.265  16.969  -19.972 1.00 47.05 ? 511 A1ATD A C17 1 
HETATM 2826 C  C19 . A1ATD L 4 .   ? -3.890  17.018  -20.083 1.00 47.92 ? 511 A1ATD A C19 1 
HETATM 2827 C  C20 . A1ATD L 4 .   ? -3.111  17.187  -18.953 1.00 49.52 ? 511 A1ATD A C20 1 
HETATM 2828 C  C21 . A1ATD L 4 .   ? -1.734  19.038  -14.315 1.00 49.50 ? 511 A1ATD A C21 1 
HETATM 2829 C  C22 . A1ATD L 4 .   ? -0.705  19.648  -13.436 1.00 55.76 ? 511 A1ATD A C22 1 
HETATM 2830 C  C23 . A1ATD L 4 .   ? -0.951  19.173  -11.965 1.00 60.89 ? 511 A1ATD A C23 1 
HETATM 2831 C  C25 . A1ATD L 4 .   ? -0.830  14.514  -11.726 1.00 62.61 ? 511 A1ATD A C25 1 
HETATM 2832 C  C26 . A1ATD L 4 .   ? -0.617  13.039  -11.373 1.00 78.83 ? 511 A1ATD A C26 1 
HETATM 2833 C  C27 . A1ATD L 4 .   ? -0.611  21.203  -13.406 1.00 58.98 ? 511 A1ATD A C27 1 
HETATM 2834 F  F16 . A1ATD L 4 .   ? -7.213  17.034  -18.639 1.00 41.17 ? 511 A1ATD A F16 1 
HETATM 2835 N  N02 . A1ATD L 4 .   ? -0.004  12.817  -10.141 1.00 78.55 ? 511 A1ATD A N02 1 
HETATM 2836 N  N05 . A1ATD L 4 .   ? 0.123   15.445  -11.247 1.00 68.50 ? 511 A1ATD A N05 1 
HETATM 2837 N  N07 . A1ATD L 4 .   ? -1.076  17.686  -11.932 1.00 59.20 ? 511 A1ATD A N07 1 
HETATM 2838 N  N12 . A1ATD L 4 .   ? -2.810  17.487  -16.550 1.00 42.61 ? 511 A1ATD A N12 1 
HETATM 2839 O  O11 . A1ATD L 4 .   ? -4.359  17.282  -14.848 1.00 48.77 ? 511 A1ATD A O11 1 
HETATM 2840 O  O24 . A1ATD L 4 .   ? 0.929   17.525  -10.905 1.00 76.22 ? 511 A1ATD A O24 1 
HETATM 2841 O  O28 . A1ATD L 4 .   ? 0.655   21.473  -12.835 1.00 60.98 ? 511 A1ATD A O28 1 
HETATM 2842 CL CL1 . A1ATD L 4 .   ? -6.254  16.748  -21.444 1.00 74.67 ? 511 A1ATD A CL1 1 
HETATM 2843 C  C1  . MPD   M 5 .   ? -30.315 7.957   1.814   1.00 57.65 ? 512 MPD   A C1  1 
HETATM 2844 C  C2  . MPD   M 5 .   ? -30.472 7.248   0.472   1.00 62.32 ? 512 MPD   A C2  1 
HETATM 2845 O  O2  . MPD   M 5 .   ? -31.514 7.917   -0.290  1.00 61.57 ? 512 MPD   A O2  1 
HETATM 2846 C  CM  . MPD   M 5 .   ? -30.930 5.797   0.669   1.00 58.76 ? 512 MPD   A CM  1 
HETATM 2847 C  C3  . MPD   M 5 .   ? -29.112 7.301   -0.248  1.00 62.68 ? 512 MPD   A C3  1 
HETATM 2848 C  C4  . MPD   M 5 .   ? -28.684 8.662   -0.820  1.00 55.90 ? 512 MPD   A C4  1 
HETATM 2849 O  O4  . MPD   M 5 .   ? -27.496 8.461   -1.550  1.00 52.95 ? 512 MPD   A O4  1 
HETATM 2850 C  C5  . MPD   M 5 .   ? -29.715 9.264   -1.769  1.00 55.84 ? 512 MPD   A C5  1 
HETATM 2851 C  C1  . MPD   N 5 .   ? -16.643 22.660  10.221  1.00 53.02 ? 513 MPD   A C1  1 
HETATM 2852 C  C2  . MPD   N 5 .   ? -15.954 23.935  9.778   1.00 58.20 ? 513 MPD   A C2  1 
HETATM 2853 O  O2  . MPD   N 5 .   ? -16.954 24.975  9.574   1.00 63.41 ? 513 MPD   A O2  1 
HETATM 2854 C  CM  . MPD   N 5 .   ? -15.254 23.669  8.459   1.00 57.95 ? 513 MPD   A CM  1 
HETATM 2855 C  C3  . MPD   N 5 .   ? -14.958 24.383  10.839  1.00 63.39 ? 513 MPD   A C3  1 
HETATM 2856 C  C4  . MPD   N 5 .   ? -13.816 25.218  10.273  1.00 64.07 ? 513 MPD   A C4  1 
HETATM 2857 O  O4  . MPD   N 5 .   ? -14.259 25.894  9.120   1.00 65.70 ? 513 MPD   A O4  1 
HETATM 2858 C  C5  . MPD   N 5 .   ? -13.355 26.245  11.299  1.00 61.84 ? 513 MPD   A C5  1 
HETATM 2859 O  O   . HOH   O 6 .   ? -31.294 12.479  -16.369 1.00 53.92 ? 601 HOH   A O   1 
HETATM 2860 O  O   . HOH   O 6 .   ? -8.483  28.208  -7.444  1.00 53.89 ? 602 HOH   A O   1 
HETATM 2861 O  O   . HOH   O 6 .   ? -17.115 15.192  -32.175 1.00 45.85 ? 603 HOH   A O   1 
HETATM 2862 O  O   . HOH   O 6 .   ? -18.719 11.404  -16.087 1.00 39.79 ? 604 HOH   A O   1 
HETATM 2863 O  O   . HOH   O 6 .   ? -22.270 11.521  -22.392 1.00 46.81 ? 605 HOH   A O   1 
HETATM 2864 O  O   . HOH   O 6 .   ? -4.386  11.441  -9.491  1.00 51.22 ? 606 HOH   A O   1 
HETATM 2865 O  O   . HOH   O 6 .   ? -4.988  23.761  -41.580 1.00 57.24 ? 607 HOH   A O   1 
HETATM 2866 O  O   . HOH   O 6 .   ? -33.588 4.949   -6.538  1.00 57.43 ? 608 HOH   A O   1 
HETATM 2867 O  O   . HOH   O 6 .   ? -16.235 25.176  -32.626 1.00 49.71 ? 609 HOH   A O   1 
HETATM 2868 O  O   . HOH   O 6 .   ? -16.302 29.059  0.322   1.00 49.34 ? 610 HOH   A O   1 
HETATM 2869 O  O   . HOH   O 6 .   ? -15.423 10.711  -25.792 1.00 35.63 ? 611 HOH   A O   1 
HETATM 2870 O  O   . HOH   O 6 .   ? -20.067 33.956  -29.006 1.00 49.59 ? 612 HOH   A O   1 
HETATM 2871 O  O   . HOH   O 6 .   ? -16.768 -11.285 -14.747 1.00 48.25 ? 613 HOH   A O   1 
HETATM 2872 O  O   . HOH   O 6 .   ? -13.929 14.081  -18.738 1.00 36.77 ? 614 HOH   A O   1 
HETATM 2873 O  O   . HOH   O 6 .   ? -23.708 -2.017  -14.858 1.00 42.32 ? 615 HOH   A O   1 
HETATM 2874 O  O   . HOH   O 6 .   ? -30.703 11.940  -10.371 1.00 48.91 ? 616 HOH   A O   1 
HETATM 2875 O  O   . HOH   O 6 .   ? -19.701 20.058  -35.621 1.00 51.51 ? 617 HOH   A O   1 
HETATM 2876 O  O   . HOH   O 6 .   ? -8.056  16.509  -8.807  1.00 46.78 ? 618 HOH   A O   1 
HETATM 2877 O  O   . HOH   O 6 .   ? -19.007 34.730  -25.736 1.00 47.24 ? 619 HOH   A O   1 
HETATM 2878 O  O   . HOH   O 6 .   ? -20.908 11.102  -11.306 1.00 38.03 ? 620 HOH   A O   1 
HETATM 2879 O  O   . HOH   O 6 .   ? -31.371 22.204  -8.737  1.00 54.12 ? 621 HOH   A O   1 
HETATM 2880 O  O   . HOH   O 6 .   ? -21.063 12.606  1.557   1.00 47.92 ? 622 HOH   A O   1 
HETATM 2881 O  O   . HOH   O 6 .   ? -20.798 12.917  -15.874 1.00 38.48 ? 623 HOH   A O   1 
HETATM 2882 O  O   . HOH   O 6 .   ? -11.020 12.594  -25.327 1.00 36.79 ? 624 HOH   A O   1 
HETATM 2883 O  O   . HOH   O 6 .   ? -10.426 14.744  -23.409 1.00 36.57 ? 625 HOH   A O   1 
HETATM 2884 O  O   . HOH   O 6 .   ? -15.041 -2.339  -4.855  1.00 39.39 ? 626 HOH   A O   1 
HETATM 2885 O  O   . HOH   O 6 .   ? -3.422  12.912  -35.408 1.00 46.54 ? 627 HOH   A O   1 
HETATM 2886 O  O   . HOH   O 6 .   ? -7.838  30.711  -23.977 1.00 41.20 ? 628 HOH   A O   1 
HETATM 2887 O  O   . HOH   O 6 .   ? -16.261 18.703  -0.172  1.00 40.96 ? 629 HOH   A O   1 
HETATM 2888 O  O   . HOH   O 6 .   ? -16.127 19.446  -27.156 1.00 41.27 ? 630 HOH   A O   1 
HETATM 2889 O  O   . HOH   O 6 .   ? -31.840 -4.538  -3.053  1.00 51.64 ? 631 HOH   A O   1 
HETATM 2890 O  O   . HOH   O 6 .   ? -18.008 1.473   -2.706  1.00 45.56 ? 632 HOH   A O   1 
HETATM 2891 O  O   . HOH   O 6 .   ? -2.733  2.079   -28.334 1.00 34.99 ? 633 HOH   A O   1 
HETATM 2892 O  O   . HOH   O 6 .   ? -0.859  16.453  -29.356 1.00 44.05 ? 634 HOH   A O   1 
HETATM 2893 O  O   . HOH   O 6 .   ? -11.193 5.242   -4.552  1.00 41.27 ? 635 HOH   A O   1 
HETATM 2894 O  O   . HOH   O 6 .   ? -1.014  32.082  -38.457 1.00 50.49 ? 636 HOH   A O   1 
HETATM 2895 O  O   . HOH   O 6 .   ? -11.403 -5.835  -26.274 1.00 46.99 ? 637 HOH   A O   1 
HETATM 2896 O  O   . HOH   O 6 .   ? -1.611  19.037  -28.496 1.00 34.75 ? 638 HOH   A O   1 
HETATM 2897 O  O   . HOH   O 6 .   ? -26.007 14.681  -2.355  1.00 44.01 ? 639 HOH   A O   1 
HETATM 2898 O  O   . HOH   O 6 .   ? 6.837   23.876  -31.708 1.00 43.60 ? 640 HOH   A O   1 
HETATM 2899 O  O   . HOH   O 6 .   ? -8.340  8.621   -22.953 1.00 35.75 ? 641 HOH   A O   1 
HETATM 2900 O  O   . HOH   O 6 .   ? -13.280 14.544  5.519   1.00 44.14 ? 642 HOH   A O   1 
HETATM 2901 O  O   . HOH   O 6 .   ? -24.712 23.992  -26.000 1.00 44.67 ? 643 HOH   A O   1 
HETATM 2902 O  O   . HOH   O 6 .   ? -20.336 11.411  -2.541  1.00 37.63 ? 644 HOH   A O   1 
HETATM 2903 O  O   . HOH   O 6 .   ? -18.570 6.909   -20.141 1.00 42.12 ? 645 HOH   A O   1 
HETATM 2904 O  O   . HOH   O 6 .   ? -15.682 36.664  -11.898 1.00 55.72 ? 646 HOH   A O   1 
HETATM 2905 O  O   . HOH   O 6 .   ? -15.642 8.982   -27.723 1.00 41.22 ? 647 HOH   A O   1 
HETATM 2906 O  O   . HOH   O 6 .   ? -17.190 8.620   -19.286 1.00 38.30 ? 648 HOH   A O   1 
HETATM 2907 O  O   . HOH   O 6 .   ? -7.870  32.842  -22.447 1.00 43.93 ? 649 HOH   A O   1 
HETATM 2908 O  O   . HOH   O 6 .   ? -4.390  12.678  -12.488 1.00 43.36 ? 650 HOH   A O   1 
HETATM 2909 O  O   . HOH   O 6 .   ? -14.456 14.414  -2.214  1.00 37.65 ? 651 HOH   A O   1 
HETATM 2910 O  O   . HOH   O 6 .   ? -26.959 0.201   5.347   1.00 49.66 ? 652 HOH   A O   1 
HETATM 2911 O  O   . HOH   O 6 .   ? -12.185 -0.940  -2.566  1.00 41.89 ? 653 HOH   A O   1 
HETATM 2912 O  O   . HOH   O 6 .   ? 3.763   24.455  -15.967 1.00 53.19 ? 654 HOH   A O   1 
HETATM 2913 O  O   . HOH   O 6 .   ? -24.900 2.120   -15.595 1.00 50.28 ? 655 HOH   A O   1 
HETATM 2914 O  O   . HOH   O 6 .   ? -3.132  14.569  -33.511 1.00 43.27 ? 656 HOH   A O   1 
HETATM 2915 O  O   . HOH   O 6 .   ? -14.400 32.533  -21.189 1.00 41.23 ? 657 HOH   A O   1 
HETATM 2916 O  O   . HOH   O 6 .   ? -9.659  16.322  -13.541 1.00 38.22 ? 658 HOH   A O   1 
HETATM 2917 O  O   . HOH   O 6 .   ? -0.933  0.572   -8.524  1.00 56.28 ? 659 HOH   A O   1 
HETATM 2918 O  O   . HOH   O 6 .   ? -18.246 3.028   -5.412  1.00 39.04 ? 660 HOH   A O   1 
HETATM 2919 O  O   . HOH   O 6 .   ? -0.041  1.859   -15.420 1.00 39.70 ? 661 HOH   A O   1 
HETATM 2920 O  O   . HOH   O 6 .   ? -9.516  11.420  -23.176 1.00 33.12 ? 662 HOH   A O   1 
HETATM 2921 O  O   . HOH   O 6 .   ? -15.489 28.056  4.125   1.00 55.86 ? 663 HOH   A O   1 
HETATM 2922 O  O   . HOH   O 6 .   ? -21.080 15.083  2.713   1.00 48.32 ? 664 HOH   A O   1 
HETATM 2923 O  O   . HOH   O 6 .   ? 0.293   -6.048  -18.763 1.00 40.94 ? 665 HOH   A O   1 
HETATM 2924 O  O   . HOH   O 6 .   ? -16.158 11.295  -18.379 1.00 38.25 ? 666 HOH   A O   1 
HETATM 2925 O  O   . HOH   O 6 .   ? -0.883  13.949  -20.083 1.00 36.28 ? 667 HOH   A O   1 
HETATM 2926 O  O   . HOH   O 6 .   ? -12.027 17.033  -36.691 1.00 45.72 ? 668 HOH   A O   1 
HETATM 2927 O  O   . HOH   O 6 .   ? -1.815  0.005   -27.015 1.00 43.30 ? 669 HOH   A O   1 
HETATM 2928 O  O   . HOH   O 6 .   ? -29.543 12.670  -3.176  1.00 51.09 ? 670 HOH   A O   1 
HETATM 2929 O  O   . HOH   O 6 .   ? -3.328  6.571   -7.577  1.00 57.48 ? 671 HOH   A O   1 
HETATM 2930 O  O   . HOH   O 6 .   ? -24.050 -9.213  -15.587 1.00 52.25 ? 672 HOH   A O   1 
HETATM 2931 O  O   . HOH   O 6 .   ? -2.768  5.971   -33.868 1.00 43.23 ? 673 HOH   A O   1 
HETATM 2932 O  O   . HOH   O 6 .   ? -14.593 1.102   1.120   1.00 48.12 ? 674 HOH   A O   1 
HETATM 2933 O  O   . HOH   O 6 .   ? -22.969 -0.273  -21.587 1.00 48.37 ? 675 HOH   A O   1 
HETATM 2934 O  O   . HOH   O 6 .   ? -12.662 34.037  -21.404 1.00 46.45 ? 676 HOH   A O   1 
HETATM 2935 O  O   . HOH   O 6 .   ? -29.577 5.093   -1.977  1.00 55.58 ? 677 HOH   A O   1 
HETATM 2936 O  O   . HOH   O 6 .   ? -27.724 15.768  -4.076  1.00 47.44 ? 678 HOH   A O   1 
HETATM 2937 O  O   . HOH   O 6 .   ? -17.497 0.297   0.729   1.00 49.66 ? 679 HOH   A O   1 
HETATM 2938 O  O   . HOH   O 6 .   ? -1.182  2.343   -30.445 1.00 40.70 ? 680 HOH   A O   1 
HETATM 2939 O  O   . HOH   O 6 .   ? -14.498 38.748  -13.065 1.00 60.36 ? 681 HOH   A O   1 
HETATM 2940 O  O   . HOH   O 6 .   ? -1.633  -2.104  -6.202  1.00 53.41 ? 682 HOH   A O   1 
HETATM 2941 O  O   . HOH   O 6 .   ? -4.273  16.390  -6.880  1.00 58.23 ? 683 HOH   A O   1 
# 
