data_9BXG
# 
_entry.id   9BXG 
# 
_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   9BXG         pdb_00009bxg 10.2210/pdb9bxg/pdb 
WWPDB D_1000284340 ?            ?                   
# 
_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                        9BXG 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marzena.pazgier@usuhs.edu 
_pdbx_contact_author.name_first         Marzena 
_pdbx_contact_author.name_last          Pazgier 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0594-5057 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'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)-1-[4-(5-carbamimidamidopentanoyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' 507.989   1   ? 
?                                                 ? ? 
5 water       nat water 18.015    215 ? ?                                                 ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 2-acetamido-2-deoxy-beta-D-glucopyranose                                                                           NAG   
3 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'                                                              EPE   
4 '(3S)-1-[4-(5-carbamimidamidopentanoyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' A1ATA 
5 water                                                                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   PRO n 
1 3   VAL n 
1 4   TRP n 
1 5   LYS n 
1 6   ASP n 
1 7   ALA n 
1 8   ASP n 
1 9   THR n 
1 10  THR n 
1 11  LEU n 
1 12  PHE n 
1 13  CYS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  ALA n 
1 18  LYS n 
1 19  ALA n 
1 20  TYR n 
1 21  GLU n 
1 22  THR n 
1 23  GLU n 
1 24  VAL n 
1 25  HIS n 
1 26  ASN n 
1 27  VAL n 
1 28  TRP n 
1 29  ALA n 
1 30  THR n 
1 31  HIS n 
1 32  ALA n 
1 33  CYS n 
1 34  VAL n 
1 35  PRO n 
1 36  THR n 
1 37  ASP n 
1 38  PRO n 
1 39  ASN n 
1 40  PRO n 
1 41  GLN n 
1 42  GLU n 
1 43  ILE n 
1 44  HIS n 
1 45  LEU n 
1 46  GLU n 
1 47  ASN n 
1 48  VAL n 
1 49  THR n 
1 50  GLU n 
1 51  ASN n 
1 52  PHE n 
1 53  ASN n 
1 54  MET n 
1 55  TRP n 
1 56  LYS n 
1 57  ASN n 
1 58  ASN n 
1 59  MET n 
1 60  VAL n 
1 61  GLU n 
1 62  GLN n 
1 63  MET n 
1 64  HIS n 
1 65  GLU n 
1 66  ASP n 
1 67  ILE n 
1 68  ILE n 
1 69  SER n 
1 70  LEU n 
1 71  TRP n 
1 72  ASP n 
1 73  GLN n 
1 74  SER n 
1 75  LEU n 
1 76  GLN n 
1 77  PRO n 
1 78  CYS n 
1 79  VAL n 
1 80  LYS n 
1 81  LEU n 
1 82  THR n 
1 83  GLY n 
1 84  GLY n 
1 85  SER n 
1 86  VAL n 
1 87  ILE n 
1 88  LYS n 
1 89  GLN n 
1 90  ALA n 
1 91  CYS n 
1 92  PRO n 
1 93  LYS n 
1 94  ILE n 
1 95  SER n 
1 96  PHE n 
1 97  ASP n 
1 98  PRO n 
1 99  ILE n 
1 100 PRO n 
1 101 ILE n 
1 102 HIS n 
1 103 TYR n 
1 104 CYS n 
1 105 THR n 
1 106 PRO n 
1 107 ALA n 
1 108 GLY n 
1 109 TYR n 
1 110 VAL n 
1 111 ILE n 
1 112 LEU n 
1 113 LYS n 
1 114 CYS n 
1 115 ASN n 
1 116 ASP n 
1 117 LYS n 
1 118 ASN n 
1 119 PHE n 
1 120 ASN n 
1 121 GLY n 
1 122 THR n 
1 123 GLY n 
1 124 PRO n 
1 125 CYS n 
1 126 LYS n 
1 127 ASN n 
1 128 VAL n 
1 129 SER n 
1 130 SER n 
1 131 VAL n 
1 132 GLN n 
1 133 CYS n 
1 134 THR n 
1 135 HIS n 
1 136 GLY n 
1 137 ILE n 
1 138 LYS n 
1 139 PRO n 
1 140 VAL n 
1 141 VAL n 
1 142 SER n 
1 143 THR n 
1 144 GLN n 
1 145 LEU n 
1 146 LEU n 
1 147 LEU n 
1 148 ASN n 
1 149 GLY n 
1 150 SER n 
1 151 LEU n 
1 152 ALA n 
1 153 GLU n 
1 154 GLU n 
1 155 GLU n 
1 156 ILE n 
1 157 ILE n 
1 158 ILE n 
1 159 ARG n 
1 160 SER n 
1 161 GLU n 
1 162 ASN n 
1 163 LEU n 
1 164 THR n 
1 165 ASN n 
1 166 ASN n 
1 167 ALA n 
1 168 LYS n 
1 169 THR n 
1 170 ILE n 
1 171 ILE n 
1 172 VAL n 
1 173 HIS n 
1 174 LEU n 
1 175 ASN n 
1 176 LYS n 
1 177 SER n 
1 178 VAL n 
1 179 GLU n 
1 180 ILE n 
1 181 ASN n 
1 182 CYS n 
1 183 THR n 
1 184 ARG n 
1 185 PRO n 
1 186 SER n 
1 187 ASN n 
1 188 GLY n 
1 189 GLY n 
1 190 SER n 
1 191 GLY n 
1 192 SER n 
1 193 GLY n 
1 194 GLY n 
1 195 ASP n 
1 196 ILE n 
1 197 ARG n 
1 198 LYS n 
1 199 ALA n 
1 200 TYR n 
1 201 CYS n 
1 202 GLU n 
1 203 ILE n 
1 204 ASN n 
1 205 GLY n 
1 206 THR n 
1 207 LYS n 
1 208 TRP n 
1 209 ASN n 
1 210 LYS n 
1 211 VAL n 
1 212 LEU n 
1 213 LYS n 
1 214 GLN n 
1 215 VAL n 
1 216 THR n 
1 217 GLU n 
1 218 LYS n 
1 219 LEU n 
1 220 LYS n 
1 221 GLU n 
1 222 HIS n 
1 223 PHE n 
1 224 ASN n 
1 225 ASN n 
1 226 LYS n 
1 227 THR n 
1 228 ILE n 
1 229 ILE n 
1 230 PHE n 
1 231 GLN n 
1 232 PRO n 
1 233 PRO n 
1 234 SER n 
1 235 GLY n 
1 236 GLY n 
1 237 ASP n 
1 238 LEU n 
1 239 GLU n 
1 240 ILE n 
1 241 THR n 
1 242 MET n 
1 243 HIS n 
1 244 SER n 
1 245 PHE n 
1 246 ASN n 
1 247 CYS n 
1 248 ARG n 
1 249 GLY n 
1 250 GLU n 
1 251 PHE n 
1 252 PHE n 
1 253 TYR n 
1 254 CYS n 
1 255 ASN n 
1 256 THR n 
1 257 THR n 
1 258 GLN n 
1 259 LEU n 
1 260 PHE n 
1 261 ASN n 
1 262 ASN n 
1 263 THR n 
1 264 CYS n 
1 265 ILE n 
1 266 GLY n 
1 267 ASN n 
1 268 GLU n 
1 269 THR n 
1 270 MET n 
1 271 LYS n 
1 272 GLY n 
1 273 CYS n 
1 274 ASN n 
1 275 GLY n 
1 276 THR n 
1 277 ILE n 
1 278 THR n 
1 279 LEU n 
1 280 PRO n 
1 281 CYS n 
1 282 LYS n 
1 283 ILE n 
1 284 LYS n 
1 285 GLN n 
1 286 ILE n 
1 287 ILE n 
1 288 ASN n 
1 289 MET n 
1 290 TRP n 
1 291 GLN n 
1 292 GLY n 
1 293 THR n 
1 294 GLY n 
1 295 GLN n 
1 296 ALA n 
1 297 MET n 
1 298 TYR n 
1 299 ALA n 
1 300 PRO n 
1 301 PRO n 
1 302 ILE n 
1 303 ASP n 
1 304 GLY n 
1 305 LYS n 
1 306 ILE n 
1 307 ASN n 
1 308 CYS n 
1 309 VAL n 
1 310 SER n 
1 311 ASN n 
1 312 ILE n 
1 313 THR n 
1 314 GLY n 
1 315 ILE n 
1 316 LEU n 
1 317 LEU n 
1 318 THR n 
1 319 ARG n 
1 320 ASP n 
1 321 GLY n 
1 322 GLY n 
1 323 ALA n 
1 324 ASN n 
1 325 ASN n 
1 326 THR n 
1 327 SER n 
1 328 ASN n 
1 329 GLU n 
1 330 THR n 
1 331 PHE n 
1 332 ARG n 
1 333 PRO n 
1 334 GLY n 
1 335 GLY n 
1 336 GLY n 
1 337 ASP n 
1 338 MET n 
1 339 ARG n 
1 340 ASP n 
1 341 ASN n 
1 342 TRP n 
1 343 ARG n 
1 344 SER n 
1 345 GLU n 
1 346 LEU n 
1 347 TYR n 
1 348 LYS n 
1 349 TYR n 
1 350 LYS n 
1 351 VAL n 
1 352 VAL n 
1 353 GLN n 
1 354 ILE n 
1 355 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   355 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HIV-1 Env' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Human immunodeficiency virus 1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11676 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            'HEK 293 GNT1-' 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ATA non-polymer                  . 
'(3S)-1-[4-(5-carbamimidamidopentanoyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' ? 
'C23 H31 Cl F N7 O3' 507.989 
ALA   'L-peptide linking'          y ALANINE ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking'          y ARGININE ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking'          y ASPARAGINE ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking'          y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking'          y CYSTEINE ? 'C3 H7 N O2 S'       121.158 
EPE   non-polymer                  . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S'     238.305 
GLN   'L-peptide linking'          y GLUTAMINE ? 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking'          y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129 
GLY   'peptide linking'            y GLYCINE ? 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking'          y HISTIDINE ? 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer                  . WATER ? 'H2 O'               18.015  
ILE   'L-peptide linking'          y ISOLEUCINE ? 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking'          y LEUCINE ? 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking'          y LYSINE ? 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking'          y METHIONINE ? 'C5 H11 N O2 S'      149.211 
NAG   'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'        221.208 
PHE   'L-peptide linking'          y PHENYLALANINE ? 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking'          y PROLINE ? 'C5 H9 N O2'         115.130 
SER   'L-peptide linking'          y SERINE ? 'C3 H7 N O3'         105.093 
THR   'L-peptide linking'          y THREONINE ? 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking'          y TRYPTOPHAN ? 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking'          y TYROSINE ? 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking'          y VALINE ? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   VAL 1   42  ?   ?   ?   A . n 
A 1 2   PRO 2   43  ?   ?   ?   A . n 
A 1 3   VAL 3   44  44  VAL VAL A . n 
A 1 4   TRP 4   45  45  TRP TRP A . n 
A 1 5   LYS 5   46  46  LYS LYS A . n 
A 1 6   ASP 6   47  47  ASP ASP A . n 
A 1 7   ALA 7   48  48  ALA ALA A . n 
A 1 8   ASP 8   49  49  ASP ASP A . n 
A 1 9   THR 9   50  50  THR THR A . n 
A 1 10  THR 10  51  51  THR THR A . n 
A 1 11  LEU 11  52  52  LEU LEU A . n 
A 1 12  PHE 12  53  53  PHE PHE A . n 
A 1 13  CYS 13  54  54  CYS CYS A . n 
A 1 14  ALA 14  55  55  ALA ALA A . n 
A 1 15  SER 15  56  56  SER SER A . n 
A 1 16  ASP 16  57  57  ASP ASP A . n 
A 1 17  ALA 17  58  58  ALA ALA A . n 
A 1 18  LYS 18  59  59  LYS LYS A . n 
A 1 19  ALA 19  60  60  ALA ALA A . n 
A 1 20  TYR 20  61  61  TYR TYR A . n 
A 1 21  GLU 21  62  62  GLU GLU A . n 
A 1 22  THR 22  63  63  THR THR A . n 
A 1 23  GLU 23  64  64  GLU GLU A . n 
A 1 24  VAL 24  65  65  VAL VAL A . n 
A 1 25  HIS 25  66  66  HIS HIS A . n 
A 1 26  ASN 26  67  67  ASN ASN A . n 
A 1 27  VAL 27  68  68  VAL VAL A . n 
A 1 28  TRP 28  69  69  TRP TRP A . n 
A 1 29  ALA 29  70  70  ALA ALA A . n 
A 1 30  THR 30  71  71  THR THR A . n 
A 1 31  HIS 31  72  72  HIS HIS A . n 
A 1 32  ALA 32  73  73  ALA ALA A . n 
A 1 33  CYS 33  74  74  CYS CYS A . n 
A 1 34  VAL 34  75  75  VAL VAL A . n 
A 1 35  PRO 35  76  76  PRO PRO A . n 
A 1 36  THR 36  77  77  THR THR A . n 
A 1 37  ASP 37  78  78  ASP ASP A . n 
A 1 38  PRO 38  79  79  PRO PRO A . n 
A 1 39  ASN 39  80  80  ASN ASN A . n 
A 1 40  PRO 40  81  81  PRO PRO A . n 
A 1 41  GLN 41  82  82  GLN GLN A . n 
A 1 42  GLU 42  83  83  GLU GLU A . n 
A 1 43  ILE 43  84  84  ILE ILE A . n 
A 1 44  HIS 44  85  85  HIS HIS A . n 
A 1 45  LEU 45  86  86  LEU LEU A . n 
A 1 46  GLU 46  87  87  GLU GLU A . n 
A 1 47  ASN 47  88  88  ASN ASN A . n 
A 1 48  VAL 48  89  89  VAL VAL A . n 
A 1 49  THR 49  90  90  THR THR A . n 
A 1 50  GLU 50  91  91  GLU GLU A . n 
A 1 51  ASN 51  92  92  ASN ASN A . n 
A 1 52  PHE 52  93  93  PHE PHE A . n 
A 1 53  ASN 53  94  94  ASN ASN A . n 
A 1 54  MET 54  95  95  MET MET A . n 
A 1 55  TRP 55  96  96  TRP TRP A . n 
A 1 56  LYS 56  97  97  LYS LYS A . n 
A 1 57  ASN 57  98  98  ASN ASN A . n 
A 1 58  ASN 58  99  99  ASN ASN A . n 
A 1 59  MET 59  100 100 MET MET A . n 
A 1 60  VAL 60  101 101 VAL VAL A . n 
A 1 61  GLU 61  102 102 GLU GLU A . n 
A 1 62  GLN 62  103 103 GLN GLN A . n 
A 1 63  MET 63  104 104 MET MET A . n 
A 1 64  HIS 64  105 105 HIS HIS A . n 
A 1 65  GLU 65  106 106 GLU GLU A . n 
A 1 66  ASP 66  107 107 ASP ASP A . n 
A 1 67  ILE 67  108 108 ILE ILE A . n 
A 1 68  ILE 68  109 109 ILE ILE A . n 
A 1 69  SER 69  110 110 SER SER A . n 
A 1 70  LEU 70  111 111 LEU LEU A . n 
A 1 71  TRP 71  112 112 TRP TRP A . n 
A 1 72  ASP 72  113 113 ASP ASP A . n 
A 1 73  GLN 73  114 114 GLN GLN A . n 
A 1 74  SER 74  115 115 SER SER A . n 
A 1 75  LEU 75  116 116 LEU LEU A . n 
A 1 76  GLN 76  117 117 GLN GLN A . n 
A 1 77  PRO 77  118 118 PRO PRO A . n 
A 1 78  CYS 78  119 119 CYS CYS A . n 
A 1 79  VAL 79  120 120 VAL VAL A . n 
A 1 80  LYS 80  121 121 LYS LYS A . n 
A 1 81  LEU 81  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 187 317 ?   ?   ?   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 ?   ?   ?   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        A1ATA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ATA 
_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 A1ATA 1   511 513 A1ATA MW5 A . 
M 5 HOH   1   601 162 HOH   HOH A . 
M 5 HOH   2   602 157 HOH   HOH A . 
M 5 HOH   3   603 134 HOH   HOH A . 
M 5 HOH   4   604 148 HOH   HOH A . 
M 5 HOH   5   605 26  HOH   HOH A . 
M 5 HOH   6   606 66  HOH   HOH A . 
M 5 HOH   7   607 152 HOH   HOH A . 
M 5 HOH   8   608 229 HOH   HOH A . 
M 5 HOH   9   609 22  HOH   HOH A . 
M 5 HOH   10  610 116 HOH   HOH A . 
M 5 HOH   11  611 119 HOH   HOH A . 
M 5 HOH   12  612 29  HOH   HOH A . 
M 5 HOH   13  613 142 HOH   HOH A . 
M 5 HOH   14  614 103 HOH   HOH A . 
M 5 HOH   15  615 191 HOH   HOH A . 
M 5 HOH   16  616 16  HOH   HOH A . 
M 5 HOH   17  617 102 HOH   HOH A . 
M 5 HOH   18  618 64  HOH   HOH A . 
M 5 HOH   19  619 117 HOH   HOH A . 
M 5 HOH   20  620 25  HOH   HOH A . 
M 5 HOH   21  621 24  HOH   HOH A . 
M 5 HOH   22  622 83  HOH   HOH A . 
M 5 HOH   23  623 158 HOH   HOH A . 
M 5 HOH   24  624 88  HOH   HOH A . 
M 5 HOH   25  625 144 HOH   HOH A . 
M 5 HOH   26  626 195 HOH   HOH A . 
M 5 HOH   27  627 47  HOH   HOH A . 
M 5 HOH   28  628 173 HOH   HOH A . 
M 5 HOH   29  629 91  HOH   HOH A . 
M 5 HOH   30  630 192 HOH   HOH A . 
M 5 HOH   31  631 132 HOH   HOH A . 
M 5 HOH   32  632 155 HOH   HOH A . 
M 5 HOH   33  633 5   HOH   HOH A . 
M 5 HOH   34  634 85  HOH   HOH A . 
M 5 HOH   35  635 9   HOH   HOH A . 
M 5 HOH   36  636 161 HOH   HOH A . 
M 5 HOH   37  637 82  HOH   HOH A . 
M 5 HOH   38  638 100 HOH   HOH A . 
M 5 HOH   39  639 60  HOH   HOH A . 
M 5 HOH   40  640 120 HOH   HOH A . 
M 5 HOH   41  641 79  HOH   HOH A . 
M 5 HOH   42  642 139 HOH   HOH A . 
M 5 HOH   43  643 125 HOH   HOH A . 
M 5 HOH   44  644 70  HOH   HOH A . 
M 5 HOH   45  645 45  HOH   HOH A . 
M 5 HOH   46  646 12  HOH   HOH A . 
M 5 HOH   47  647 210 HOH   HOH A . 
M 5 HOH   48  648 164 HOH   HOH A . 
M 5 HOH   49  649 213 HOH   HOH A . 
M 5 HOH   50  650 18  HOH   HOH A . 
M 5 HOH   51  651 98  HOH   HOH A . 
M 5 HOH   52  652 146 HOH   HOH A . 
M 5 HOH   53  653 167 HOH   HOH A . 
M 5 HOH   54  654 89  HOH   HOH A . 
M 5 HOH   55  655 113 HOH   HOH A . 
M 5 HOH   56  656 8   HOH   HOH A . 
M 5 HOH   57  657 59  HOH   HOH A . 
M 5 HOH   58  658 143 HOH   HOH A . 
M 5 HOH   59  659 54  HOH   HOH A . 
M 5 HOH   60  660 36  HOH   HOH A . 
M 5 HOH   61  661 73  HOH   HOH A . 
M 5 HOH   62  662 101 HOH   HOH A . 
M 5 HOH   63  663 21  HOH   HOH A . 
M 5 HOH   64  664 169 HOH   HOH A . 
M 5 HOH   65  665 49  HOH   HOH A . 
M 5 HOH   66  666 14  HOH   HOH A . 
M 5 HOH   67  667 150 HOH   HOH A . 
M 5 HOH   68  668 115 HOH   HOH A . 
M 5 HOH   69  669 33  HOH   HOH A . 
M 5 HOH   70  670 10  HOH   HOH A . 
M 5 HOH   71  671 188 HOH   HOH A . 
M 5 HOH   72  672 182 HOH   HOH A . 
M 5 HOH   73  673 200 HOH   HOH A . 
M 5 HOH   74  674 51  HOH   HOH A . 
M 5 HOH   75  675 4   HOH   HOH A . 
M 5 HOH   76  676 184 HOH   HOH A . 
M 5 HOH   77  677 19  HOH   HOH A . 
M 5 HOH   78  678 50  HOH   HOH A . 
M 5 HOH   79  679 27  HOH   HOH A . 
M 5 HOH   80  680 44  HOH   HOH A . 
M 5 HOH   81  681 130 HOH   HOH A . 
M 5 HOH   82  682 3   HOH   HOH A . 
M 5 HOH   83  683 209 HOH   HOH A . 
M 5 HOH   84  684 135 HOH   HOH A . 
M 5 HOH   85  685 217 HOH   HOH A . 
M 5 HOH   86  686 68  HOH   HOH A . 
M 5 HOH   87  687 58  HOH   HOH A . 
M 5 HOH   88  688 32  HOH   HOH A . 
M 5 HOH   89  689 61  HOH   HOH A . 
M 5 HOH   90  690 43  HOH   HOH A . 
M 5 HOH   91  691 69  HOH   HOH A . 
M 5 HOH   92  692 1   HOH   HOH A . 
M 5 HOH   93  693 38  HOH   HOH A . 
M 5 HOH   94  694 28  HOH   HOH A . 
M 5 HOH   95  695 140 HOH   HOH A . 
M 5 HOH   96  696 199 HOH   HOH A . 
M 5 HOH   97  697 2   HOH   HOH A . 
M 5 HOH   98  698 52  HOH   HOH A . 
M 5 HOH   99  699 11  HOH   HOH A . 
M 5 HOH   100 700 95  HOH   HOH A . 
M 5 HOH   101 701 41  HOH   HOH A . 
M 5 HOH   102 702 13  HOH   HOH A . 
M 5 HOH   103 703 34  HOH   HOH A . 
M 5 HOH   104 704 78  HOH   HOH A . 
M 5 HOH   105 705 108 HOH   HOH A . 
M 5 HOH   106 706 31  HOH   HOH A . 
M 5 HOH   107 707 186 HOH   HOH A . 
M 5 HOH   108 708 225 HOH   HOH A . 
M 5 HOH   109 709 171 HOH   HOH A . 
M 5 HOH   110 710 17  HOH   HOH A . 
M 5 HOH   111 711 99  HOH   HOH A . 
M 5 HOH   112 712 7   HOH   HOH A . 
M 5 HOH   113 713 133 HOH   HOH A . 
M 5 HOH   114 714 136 HOH   HOH A . 
M 5 HOH   115 715 23  HOH   HOH A . 
M 5 HOH   116 716 92  HOH   HOH A . 
M 5 HOH   117 717 109 HOH   HOH A . 
M 5 HOH   118 718 65  HOH   HOH A . 
M 5 HOH   119 719 35  HOH   HOH A . 
M 5 HOH   120 720 138 HOH   HOH A . 
M 5 HOH   121 721 214 HOH   HOH A . 
M 5 HOH   122 722 118 HOH   HOH A . 
M 5 HOH   123 723 30  HOH   HOH A . 
M 5 HOH   124 724 114 HOH   HOH A . 
M 5 HOH   125 725 71  HOH   HOH A . 
M 5 HOH   126 726 39  HOH   HOH A . 
M 5 HOH   127 727 40  HOH   HOH A . 
M 5 HOH   128 728 185 HOH   HOH A . 
M 5 HOH   129 729 105 HOH   HOH A . 
M 5 HOH   130 730 112 HOH   HOH A . 
M 5 HOH   131 731 76  HOH   HOH A . 
M 5 HOH   132 732 77  HOH   HOH A . 
M 5 HOH   133 733 147 HOH   HOH A . 
M 5 HOH   134 734 215 HOH   HOH A . 
M 5 HOH   135 735 172 HOH   HOH A . 
M 5 HOH   136 736 67  HOH   HOH A . 
M 5 HOH   137 737 180 HOH   HOH A . 
M 5 HOH   138 738 189 HOH   HOH A . 
M 5 HOH   139 739 93  HOH   HOH A . 
M 5 HOH   140 740 90  HOH   HOH A . 
M 5 HOH   141 741 15  HOH   HOH A . 
M 5 HOH   142 742 55  HOH   HOH A . 
M 5 HOH   143 743 159 HOH   HOH A . 
M 5 HOH   144 744 106 HOH   HOH A . 
M 5 HOH   145 745 154 HOH   HOH A . 
M 5 HOH   146 746 104 HOH   HOH A . 
M 5 HOH   147 747 175 HOH   HOH A . 
M 5 HOH   148 748 128 HOH   HOH A . 
M 5 HOH   149 749 181 HOH   HOH A . 
M 5 HOH   150 750 111 HOH   HOH A . 
M 5 HOH   151 751 216 HOH   HOH A . 
M 5 HOH   152 752 151 HOH   HOH A . 
M 5 HOH   153 753 208 HOH   HOH A . 
M 5 HOH   154 754 87  HOH   HOH A . 
M 5 HOH   155 755 203 HOH   HOH A . 
M 5 HOH   156 756 196 HOH   HOH A . 
M 5 HOH   157 757 123 HOH   HOH A . 
M 5 HOH   158 758 56  HOH   HOH A . 
M 5 HOH   159 759 165 HOH   HOH A . 
M 5 HOH   160 760 212 HOH   HOH A . 
M 5 HOH   161 761 84  HOH   HOH A . 
M 5 HOH   162 762 42  HOH   HOH A . 
M 5 HOH   163 763 228 HOH   HOH A . 
M 5 HOH   164 764 121 HOH   HOH A . 
M 5 HOH   165 765 129 HOH   HOH A . 
M 5 HOH   166 766 6   HOH   HOH A . 
M 5 HOH   167 767 57  HOH   HOH A . 
M 5 HOH   168 768 86  HOH   HOH A . 
M 5 HOH   169 769 46  HOH   HOH A . 
M 5 HOH   170 770 174 HOH   HOH A . 
M 5 HOH   171 771 37  HOH   HOH A . 
M 5 HOH   172 772 227 HOH   HOH A . 
M 5 HOH   173 773 219 HOH   HOH A . 
M 5 HOH   174 774 20  HOH   HOH A . 
M 5 HOH   175 775 193 HOH   HOH A . 
M 5 HOH   176 776 97  HOH   HOH A . 
M 5 HOH   177 777 96  HOH   HOH A . 
M 5 HOH   178 778 131 HOH   HOH A . 
M 5 HOH   179 779 220 HOH   HOH A . 
M 5 HOH   180 780 80  HOH   HOH A . 
M 5 HOH   181 781 75  HOH   HOH A . 
M 5 HOH   182 782 205 HOH   HOH A . 
M 5 HOH   183 783 183 HOH   HOH A . 
M 5 HOH   184 784 81  HOH   HOH A . 
M 5 HOH   185 785 149 HOH   HOH A . 
M 5 HOH   186 786 94  HOH   HOH A . 
M 5 HOH   187 787 187 HOH   HOH A . 
M 5 HOH   188 788 178 HOH   HOH A . 
M 5 HOH   189 789 137 HOH   HOH A . 
M 5 HOH   190 790 170 HOH   HOH A . 
M 5 HOH   191 791 160 HOH   HOH A . 
M 5 HOH   192 792 166 HOH   HOH A . 
M 5 HOH   193 793 74  HOH   HOH A . 
M 5 HOH   194 794 72  HOH   HOH A . 
M 5 HOH   195 795 122 HOH   HOH A . 
M 5 HOH   196 796 107 HOH   HOH A . 
M 5 HOH   197 797 177 HOH   HOH A . 
M 5 HOH   198 798 179 HOH   HOH A . 
M 5 HOH   199 799 168 HOH   HOH A . 
M 5 HOH   200 800 226 HOH   HOH A . 
M 5 HOH   201 801 207 HOH   HOH A . 
M 5 HOH   202 802 163 HOH   HOH A . 
M 5 HOH   203 803 48  HOH   HOH A . 
M 5 HOH   204 804 62  HOH   HOH A . 
M 5 HOH   205 805 126 HOH   HOH A . 
M 5 HOH   206 806 197 HOH   HOH A . 
M 5 HOH   207 807 218 HOH   HOH A . 
M 5 HOH   208 808 110 HOH   HOH A . 
M 5 HOH   209 809 127 HOH   HOH A . 
M 5 HOH   210 810 156 HOH   HOH A . 
M 5 HOH   211 811 224 HOH   HOH A . 
M 5 HOH   212 812 222 HOH   HOH A . 
M 5 HOH   213 813 211 HOH   HOH A . 
M 5 HOH   214 814 63  HOH   HOH A . 
M 5 HOH   215 815 153 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                     9BXG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.329 
_cell.length_a_esd                 ? 
_cell.length_b                     67.511 
_cell.length_b_esd                 ? 
_cell.length_c                     87.747 
_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                         9BXG 
_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                   9BXG 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.60 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;10% PEG 3350
5% PEG 400
0.1 M HEPES pH 7.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'SI(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97946 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BXG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.79 
_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                                     36738 
_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                           93.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          27.6 
_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                                0.063 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.96 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.107 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.79 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2056 
_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                               0.615 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.46 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          95.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BXG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.79 
_refine.ls_d_res_low                             36.79 
_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                     36738 
_refine.ls_number_reflns_R_free                  1861 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.17 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2273 
_refine.ls_R_factor_R_free                       0.2598 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2256 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.28 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.29 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2651 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         176 
_refine_hist.number_atoms_solvent             215 
_refine_hist.number_atoms_total               3042 
_refine_hist.d_res_high                       1.79 
_refine_hist.d_res_low                        36.79 
# 
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  ? 2896 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.067  ? 3935 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.306 ? 432  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060  ? 461  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 494  ? 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' 1.79 1.84  . . 159 2558 96.00  . . . . 0.3991 . . . . . . . . . . . 0.3947 
'X-RAY DIFFRACTION' 1.84 1.89  . . 147 2668 98.00  . . . . 0.3829 . . . . . . . . . . . 0.4046 
'X-RAY DIFFRACTION' 1.89 1.95  . . 144 2663 98.00  . . . . 0.3355 . . . . . . . . . . . 0.3088 
'X-RAY DIFFRACTION' 1.95 2.02  . . 127 2654 98.00  . . . . 0.2819 . . . . . . . . . . . 0.3193 
'X-RAY DIFFRACTION' 2.02 2.10  . . 153 2666 97.00  . . . . 0.2654 . . . . . . . . . . . 0.2720 
'X-RAY DIFFRACTION' 2.10 2.20  . . 121 2533 92.00  . . . . 0.2694 . . . . . . . . . . . 0.2712 
'X-RAY DIFFRACTION' 2.20 2.32  . . 142 2706 99.00  . . . . 0.2733 . . . . . . . . . . . 0.2823 
'X-RAY DIFFRACTION' 2.32 2.46  . . 164 2686 99.00  . . . . 0.2527 . . . . . . . . . . . 0.3335 
'X-RAY DIFFRACTION' 2.46 2.65  . . 153 2722 99.00  . . . . 0.2544 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 2.65 2.92  . . 130 2743 99.00  . . . . 0.2480 . . . . . . . . . . . 0.2805 
'X-RAY DIFFRACTION' 2.92 3.34  . . 114 2639 94.00  . . . . 0.2148 . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 3.34 4.21  . . 160 2796 100.00 . . . . 0.1854 . . . . . . . . . . . 0.2290 
'X-RAY DIFFRACTION' 4.21 36.79 . . 147 2843 96.00  . . . . 0.1811 . . . . . . . . . . . 0.2350 
# 
_struct.entry_id                     9BXG 
_struct.title                        'CRYSTAL STRUCTURE OF HIV-1 LM/HS CLADE A/E CRF01 GP120 CORE IN COMPLEX WITH HZ-IV-242' 
_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        9BXG 
_struct_keywords.text            'HIV-1 GP120, CLADE A/E CF01, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0M3KKW9_9HIV1 
_struct_ref.pdbx_db_accession          A0A0M3KKW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VWKDADTTLFCASDAKAHETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMQEDVISLWDQSLQPCVKLT
GGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEN
LTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEITM
HHFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG
ANNTSNETFRPGGGNIKDNWRSELYKYKVVQIE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BXG 
_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 9BXG VAL A 1   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      42  1 
1 9BXG PRO A 2   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      43  2 
1 9BXG TYR A 20  ? UNP A0A0M3KKW9 HIS 18  'engineered mutation' 61  3 
1 9BXG HIS A 64  ? UNP A0A0M3KKW9 GLN 62  'engineered mutation' 105 4 
1 9BXG ILE A 67  ? UNP A0A0M3KKW9 VAL 65  'engineered mutation' 108 5 
1 9BXG SER A 244 ? UNP A0A0M3KKW9 HIS 242 'engineered mutation' 375 6 
1 9BXG ASP A 337 ? UNP A0A0M3KKW9 ASN 335 'engineered mutation' 474 7 
1 9BXG MET A 338 ? UNP A0A0M3KKW9 ILE 336 'engineered mutation' 475 8 
1 9BXG ARG A 339 ? UNP A0A0M3KKW9 LYS 337 'engineered mutation' 476 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLU A 23  ? CYS A 33  ? GLU A 64  CYS A 74  1 ? 11 
HELX_P HELX_P2 AA2 ASN A 57  ? GLN A 73  ? ASN A 98  GLN A 114 1 ? 17 
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 ASP A 337 ? TYR A 347 ? ASP A 474 TYR A 484 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? A CYS 13  SG  ? ? ? 1_555 A CYS 33  SG ? ? A CYS 54  A CYS 74  1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf2 disulf ?   ? A CYS 78  SG  ? ? ? 1_555 A CYS 91  SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf3 disulf ?   ? A CYS 104 SG  ? ? ? 1_555 A CYS 133 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.050 ? ?               
disulf4 disulf ?   ? A CYS 114 SG  ? ? ? 1_555 A CYS 125 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.047 ? ?               
disulf5 disulf ?   ? A CYS 182 SG  ? ? ? 1_555 A CYS 201 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf6 disulf ?   ? A CYS 247 SG  ? ? ? 1_555 A CYS 308 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf7 disulf ?   ? A CYS 254 SG  ? ? ? 1_555 A CYS 281 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.044 ? ?               
disulf8 disulf ?   ? A CYS 264 SG  ? ? ? 1_555 A CYS 273 SG ? ? A CYS 395 A CYS 410 1_555 ? ? ? ? ? ? ? 2.037 ? ?               
covale1 covale one ? A ASN 120 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 234 A NAG 501 1_555 ? ? ? ? ? ? ? 1.434 ? N-Glycosylation 
covale2 covale one ? A ASN 127 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 241 A NAG 502 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale3 covale one ? A ASN 148 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 262 A NAG 503 1_555 ? ? ? ? ? ? ? 1.434 ? N-Glycosylation 
covale4 covale one ? A ASN 162 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 276 A NAG 504 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale5 covale one ? A ASN 175 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 289 A NAG 505 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale6 covale one ? A ASN 181 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 295 A NAG 506 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale7 covale one ? A ASN 204 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 334 A NAG 507 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
covale8 covale one ? A ASN 255 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 386 A NAG 508 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale9 covale one ? A ASN 311 ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 448 A NAG 509 1_555 ? ? ? ? ? ? ? 1.429 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG B .   ? ASN A 120 ? NAG A 501 ? 1_555 ASN A 234 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG C .   ? ASN A 127 ? NAG A 502 ? 1_555 ASN A 241 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG D .   ? ASN A 148 ? NAG A 503 ? 1_555 ASN A 262 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG E .   ? ASN A 162 ? NAG A 504 ? 1_555 ASN A 276 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG F .   ? ASN A 175 ? NAG A 505 ? 1_555 ASN A 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG G .   ? ASN A 181 ? NAG A 506 ? 1_555 ASN A 295 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG H .   ? ASN A 204 ? NAG A 507 ? 1_555 ASN A 334 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG I .   ? ASN A 255 ? NAG A 508 ? 1_555 ASN A 386 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG J .   ? ASN A 311 ? NAG A 509 ? 1_555 ASN A 448 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 CYS A 13  ? CYS A 33  ? CYS A 54  ? 1_555 CYS A 74  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS A 78  ? CYS A 91  ? CYS A 119 ? 1_555 CYS A 205 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 104 ? CYS A 133 ? CYS A 218 ? 1_555 CYS A 247 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 114 ? CYS A 125 ? CYS A 228 ? 1_555 CYS A 239 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 182 ? CYS A 201 ? CYS A 296 ? 1_555 CYS A 331 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 247 ? CYS A 308 ? CYS A 378 ? 1_555 CYS A 445 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS A 254 ? CYS A 281 ? CYS A 385 ? 1_555 CYS A 418 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS A 264 ? CYS A 273 ? CYS A 395 ? 1_555 CYS A 410 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 4 5 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TRP A 4   ? ASP A 6   ? TRP A 45  ASP A 47  
AA1 2 TYR A 349 ? ILE A 354 ? TYR A 486 ILE A 491 
AA1 3 TYR A 109 ? CYS A 114 ? TYR A 223 CYS A 228 
AA1 4 VAL A 128 ? VAL A 131 ? VAL A 242 VAL A 245 
AA1 5 GLU A 42  ? HIS A 44  ? GLU A 83  HIS A 85  
AA2 1 VAL A 34  ? PRO A 35  ? VAL A 75  PRO A 76  
AA2 2 PHE A 12  ? SER A 15  ? PHE A 53  SER A 56  
AA2 3 HIS A 102 ? CYS A 104 ? HIS A 216 CYS A 218 
AA3 1 GLU A 50  ? ASN A 53  ? GLU A 91  ASN A 94  
AA3 2 THR A 122 ? CYS A 125 ? THR A 236 CYS A 239 
AA4 1 SER A 85  ? LYS A 88  ? SER A 199 LYS A 202 
AA4 2 VAL A 79  ? THR A 82  ? VAL A 120 THR A 123 
AA4 3 GLN A 295 ? MET A 297 ? GLN A 432 MET A 434 
AA4 4 ILE A 286 ? ASN A 288 ? ILE A 423 ASN A 425 
AA5 1 LEU A 145 ? LEU A 147 ? LEU A 259 LEU A 261 
AA5 2 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA5 3 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA5 4 ASN A 328 ? PRO A 333 ? ASN A 465 PRO A 470 
AA5 5 THR A 227 ? PHE A 230 ? THR A 358 PHE A 361 
AA6 1 ILE A 157 ? ARG A 159 ? ILE A 271 ARG A 273 
AA6 2 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA6 3 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA6 4 LYS A 198 ? ASN A 204 ? LYS A 328 ASN A 334 
AA6 5 THR A 276 ? LYS A 284 ? THR A 413 LYS A 421 
AA6 6 GLU A 250 ? CYS A 254 ? GLU A 381 CYS A 385 
AA6 7 HIS A 243 ? CYS A 247 ? HIS A 374 CYS A 378 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 5   ? N LYS A 46  O GLN A 353 ? O GLN A 490 
AA1 2 3 O LYS A 350 ? O LYS A 487 N LEU A 112 ? N LEU A 226 
AA1 3 4 N LYS A 113 ? N LYS A 227 O SER A 129 ? O SER A 243 
AA1 4 5 O SER A 130 ? O SER A 244 N ILE A 43  ? N ILE A 84  
AA2 1 2 O VAL A 34  ? O VAL A 75  N CYS A 13  ? N CYS A 54  
AA2 2 3 N ALA A 14  ? N ALA A 55  O HIS A 102 ? O HIS A 216 
AA3 1 2 N PHE A 52  ? N PHE A 93  O GLY A 123 ? O GLY A 237 
AA4 1 2 O SER A 85  ? O SER A 199 N THR A 82  ? N THR A 123 
AA4 2 3 N LEU A 81  ? N LEU A 122 O GLN A 295 ? O GLN A 432 
AA4 3 4 O ALA A 296 ? O ALA A 433 N ILE A 287 ? N ILE A 424 
AA5 1 2 N LEU A 146 ? N LEU A 260 O THR A 313 ? O THR A 450 
AA5 2 3 O LEU A 317 ? O LEU A 454 N ILE A 170 ? N ILE A 284 
AA5 4 5 O GLU A 329 ? O GLU A 466 N 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 284 ? O LYS A 421 N PHE A 251 ? N PHE A 382 
AA6 6 7 O CYS A 254 ? O CYS A 385 N HIS A 243 ? N HIS A 374 
# 
_pdbx_entry_details.entry_id                   9BXG 
_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 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              410 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              410 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             SG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              410 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                122.40 
_pdbx_validate_rmsd_angle.angle_target_value         114.20 
_pdbx_validate_rmsd_angle.angle_deviation            8.20 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 115 ? ? -130.40 -43.12 
2  1 LEU A 116 ? ? -109.24 76.56  
3  1 ASP A 211 ? ? -166.35 105.22 
4  1 GLN A 258 ? ? 68.50   -54.81 
5  1 GLU A 268 ? ? -117.22 -97.12 
6  1 ASN A 276 ? ? -169.20 95.65  
7  1 SER A 365 ? ? -93.39  48.72  
8  1 PHE A 391 ? ? -117.94 53.35  
9  1 CYS A 410 ? ? -120.25 -82.42 
10 1 ASN A 411 ? ? -25.19  26.67  
# 
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 ASN 317 ? A ASN 187 
4  1 Y 1 A GLY 318 ? A GLY 188 
5  1 Y 1 A GLY 319 ? A GLY 189 
6  1 Y 1 A SER 320 ? A SER 190 
7  1 Y 1 A GLY 321 ? A GLY 191 
8  1 Y 1 A SER 322 ? A SER 192 
9  1 Y 1 A GLY 323 ? A GLY 193 
10 1 Y 1 A GLY 324 ? A GLY 194 
11 1 Y 1 A ILE 402 ? A ILE 265 
12 1 Y 1 A GLY 403 ? A GLY 266 
13 1 Y 1 A ASN 404 ? A ASN 267 
14 1 Y 1 A GLU 405 ? A GLU 268 
15 1 Y 1 A THR 406 ? A THR 269 
16 1 Y 1 A MET 407 ? A MET 270 
17 1 Y 1 A LYS 408 ? A LYS 271 
# 
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 
A1ATA C10  C  N N 1   
A1ATA CG   C  N S 2   
A1ATA ND1  N  N N 3   
A1ATA CD2  C  N N 4   
A1ATA CE1  C  N N 5   
A1ATA CE2  C  N N 6   
A1ATA CZ   C  N N 7   
A1ATA NH1  N  N N 8   
A1ATA NH2  N  N N 9   
A1ATA C01  C  N N 10  
A1ATA C03  C  N N 11  
A1ATA C04  C  N N 12  
A1ATA C06  C  N N 13  
A1ATA C08  C  N N 14  
A1ATA C09  C  N S 15  
A1ATA C13  C  Y N 16  
A1ATA C14  C  Y N 17  
A1ATA C15  C  Y N 18  
A1ATA C17  C  Y N 19  
A1ATA C19  C  Y N 20  
A1ATA C20  C  Y N 21  
A1ATA C21  C  N N 22  
A1ATA C22  C  N N 23  
A1ATA C23  C  N N 24  
A1ATA C25  C  N N 25  
A1ATA C26  C  N N 26  
A1ATA F16  F  N N 27  
A1ATA N02  N  N N 28  
A1ATA N05  N  N N 29  
A1ATA N07  N  N N 30  
A1ATA N12  N  N N 31  
A1ATA O11  O  N N 32  
A1ATA O24  O  N N 33  
A1ATA O27  O  N N 34  
A1ATA CL1  CL N N 35  
A1ATA H1   H  N N 36  
A1ATA H4   H  N N 37  
A1ATA H5   H  N N 38  
A1ATA H6   H  N N 39  
A1ATA H7   H  N N 40  
A1ATA H8   H  N N 41  
A1ATA H9   H  N N 42  
A1ATA H10  H  N N 43  
A1ATA H11  H  N N 44  
A1ATA H12  H  N N 45  
A1ATA H13  H  N N 46  
A1ATA H14  H  N N 47  
A1ATA H15  H  N N 48  
A1ATA H16  H  N N 49  
A1ATA H17  H  N N 50  
A1ATA H18  H  N N 51  
A1ATA H19  H  N N 52  
A1ATA H20  H  N N 53  
A1ATA H21  H  N N 54  
A1ATA H22  H  N N 55  
A1ATA H23  H  N N 56  
A1ATA H24  H  N N 57  
A1ATA H25  H  N N 58  
A1ATA H26  H  N N 59  
A1ATA H27  H  N N 60  
A1ATA H28  H  N N 61  
A1ATA H29  H  N N 62  
A1ATA H30  H  N N 63  
A1ATA H31  H  N N 64  
A1ATA H32  H  N N 65  
A1ATA H33  H  N N 66  
ALA   N    N  N N 67  
ALA   CA   C  N S 68  
ALA   C    C  N N 69  
ALA   O    O  N N 70  
ALA   CB   C  N N 71  
ALA   OXT  O  N N 72  
ALA   H    H  N N 73  
ALA   H2   H  N N 74  
ALA   HA   H  N N 75  
ALA   HB1  H  N N 76  
ALA   HB2  H  N N 77  
ALA   HB3  H  N N 78  
ALA   HXT  H  N N 79  
ARG   N    N  N N 80  
ARG   CA   C  N S 81  
ARG   C    C  N N 82  
ARG   O    O  N N 83  
ARG   CB   C  N N 84  
ARG   CG   C  N N 85  
ARG   CD   C  N N 86  
ARG   NE   N  N N 87  
ARG   CZ   C  N N 88  
ARG   NH1  N  N N 89  
ARG   NH2  N  N N 90  
ARG   OXT  O  N N 91  
ARG   H    H  N N 92  
ARG   H2   H  N N 93  
ARG   HA   H  N N 94  
ARG   HB2  H  N N 95  
ARG   HB3  H  N N 96  
ARG   HG2  H  N N 97  
ARG   HG3  H  N N 98  
ARG   HD2  H  N N 99  
ARG   HD3  H  N N 100 
ARG   HE   H  N N 101 
ARG   HH11 H  N N 102 
ARG   HH12 H  N N 103 
ARG   HH21 H  N N 104 
ARG   HH22 H  N N 105 
ARG   HXT  H  N N 106 
ASN   N    N  N N 107 
ASN   CA   C  N S 108 
ASN   C    C  N N 109 
ASN   O    O  N N 110 
ASN   CB   C  N N 111 
ASN   CG   C  N N 112 
ASN   OD1  O  N N 113 
ASN   ND2  N  N N 114 
ASN   OXT  O  N N 115 
ASN   H    H  N N 116 
ASN   H2   H  N N 117 
ASN   HA   H  N N 118 
ASN   HB2  H  N N 119 
ASN   HB3  H  N N 120 
ASN   HD21 H  N N 121 
ASN   HD22 H  N N 122 
ASN   HXT  H  N N 123 
ASP   N    N  N N 124 
ASP   CA   C  N S 125 
ASP   C    C  N N 126 
ASP   O    O  N N 127 
ASP   CB   C  N N 128 
ASP   CG   C  N N 129 
ASP   OD1  O  N N 130 
ASP   OD2  O  N N 131 
ASP   OXT  O  N N 132 
ASP   H    H  N N 133 
ASP   H2   H  N N 134 
ASP   HA   H  N N 135 
ASP   HB2  H  N N 136 
ASP   HB3  H  N N 137 
ASP   HD2  H  N N 138 
ASP   HXT  H  N N 139 
CYS   N    N  N N 140 
CYS   CA   C  N R 141 
CYS   C    C  N N 142 
CYS   O    O  N N 143 
CYS   CB   C  N N 144 
CYS   SG   S  N N 145 
CYS   OXT  O  N N 146 
CYS   H    H  N N 147 
CYS   H2   H  N N 148 
CYS   HA   H  N N 149 
CYS   HB2  H  N N 150 
CYS   HB3  H  N N 151 
CYS   HG   H  N N 152 
CYS   HXT  H  N N 153 
EPE   N1   N  N N 154 
EPE   C2   C  N N 155 
EPE   C3   C  N N 156 
EPE   N4   N  N N 157 
EPE   C5   C  N N 158 
EPE   C6   C  N N 159 
EPE   C7   C  N N 160 
EPE   C8   C  N N 161 
EPE   O8   O  N N 162 
EPE   C9   C  N N 163 
EPE   C10  C  N N 164 
EPE   S    S  N N 165 
EPE   O1S  O  N N 166 
EPE   O2S  O  N N 167 
EPE   O3S  O  N N 168 
EPE   H21  H  N N 169 
EPE   H22  H  N N 170 
EPE   H31  H  N N 171 
EPE   H32  H  N N 172 
EPE   H51  H  N N 173 
EPE   H52  H  N N 174 
EPE   H61  H  N N 175 
EPE   H62  H  N N 176 
EPE   H71  H  N N 177 
EPE   H72  H  N N 178 
EPE   H81  H  N N 179 
EPE   H82  H  N N 180 
EPE   HO8  H  N N 181 
EPE   H91  H  N N 182 
EPE   H92  H  N N 183 
EPE   H101 H  N N 184 
EPE   H102 H  N N 185 
EPE   HOS3 H  N N 186 
GLN   N    N  N N 187 
GLN   CA   C  N S 188 
GLN   C    C  N N 189 
GLN   O    O  N N 190 
GLN   CB   C  N N 191 
GLN   CG   C  N N 192 
GLN   CD   C  N N 193 
GLN   OE1  O  N N 194 
GLN   NE2  N  N N 195 
GLN   OXT  O  N N 196 
GLN   H    H  N N 197 
GLN   H2   H  N N 198 
GLN   HA   H  N N 199 
GLN   HB2  H  N N 200 
GLN   HB3  H  N N 201 
GLN   HG2  H  N N 202 
GLN   HG3  H  N N 203 
GLN   HE21 H  N N 204 
GLN   HE22 H  N N 205 
GLN   HXT  H  N N 206 
GLU   N    N  N N 207 
GLU   CA   C  N S 208 
GLU   C    C  N N 209 
GLU   O    O  N N 210 
GLU   CB   C  N N 211 
GLU   CG   C  N N 212 
GLU   CD   C  N N 213 
GLU   OE1  O  N N 214 
GLU   OE2  O  N N 215 
GLU   OXT  O  N N 216 
GLU   H    H  N N 217 
GLU   H2   H  N N 218 
GLU   HA   H  N N 219 
GLU   HB2  H  N N 220 
GLU   HB3  H  N N 221 
GLU   HG2  H  N N 222 
GLU   HG3  H  N N 223 
GLU   HE2  H  N N 224 
GLU   HXT  H  N N 225 
GLY   N    N  N N 226 
GLY   CA   C  N N 227 
GLY   C    C  N N 228 
GLY   O    O  N N 229 
GLY   OXT  O  N N 230 
GLY   H    H  N N 231 
GLY   H2   H  N N 232 
GLY   HA2  H  N N 233 
GLY   HA3  H  N N 234 
GLY   HXT  H  N N 235 
HIS   N    N  N N 236 
HIS   CA   C  N S 237 
HIS   C    C  N N 238 
HIS   O    O  N N 239 
HIS   CB   C  N N 240 
HIS   CG   C  Y N 241 
HIS   ND1  N  Y N 242 
HIS   CD2  C  Y N 243 
HIS   CE1  C  Y N 244 
HIS   NE2  N  Y N 245 
HIS   OXT  O  N N 246 
HIS   H    H  N N 247 
HIS   H2   H  N N 248 
HIS   HA   H  N N 249 
HIS   HB2  H  N N 250 
HIS   HB3  H  N N 251 
HIS   HD1  H  N N 252 
HIS   HD2  H  N N 253 
HIS   HE1  H  N N 254 
HIS   HE2  H  N N 255 
HIS   HXT  H  N N 256 
HOH   O    O  N N 257 
HOH   H1   H  N N 258 
HOH   H2   H  N N 259 
ILE   N    N  N N 260 
ILE   CA   C  N S 261 
ILE   C    C  N N 262 
ILE   O    O  N N 263 
ILE   CB   C  N S 264 
ILE   CG1  C  N N 265 
ILE   CG2  C  N N 266 
ILE   CD1  C  N N 267 
ILE   OXT  O  N N 268 
ILE   H    H  N N 269 
ILE   H2   H  N N 270 
ILE   HA   H  N N 271 
ILE   HB   H  N N 272 
ILE   HG12 H  N N 273 
ILE   HG13 H  N N 274 
ILE   HG21 H  N N 275 
ILE   HG22 H  N N 276 
ILE   HG23 H  N N 277 
ILE   HD11 H  N N 278 
ILE   HD12 H  N N 279 
ILE   HD13 H  N N 280 
ILE   HXT  H  N N 281 
LEU   N    N  N N 282 
LEU   CA   C  N S 283 
LEU   C    C  N N 284 
LEU   O    O  N N 285 
LEU   CB   C  N N 286 
LEU   CG   C  N N 287 
LEU   CD1  C  N N 288 
LEU   CD2  C  N N 289 
LEU   OXT  O  N N 290 
LEU   H    H  N N 291 
LEU   H2   H  N N 292 
LEU   HA   H  N N 293 
LEU   HB2  H  N N 294 
LEU   HB3  H  N N 295 
LEU   HG   H  N N 296 
LEU   HD11 H  N N 297 
LEU   HD12 H  N N 298 
LEU   HD13 H  N N 299 
LEU   HD21 H  N N 300 
LEU   HD22 H  N N 301 
LEU   HD23 H  N N 302 
LEU   HXT  H  N N 303 
LYS   N    N  N N 304 
LYS   CA   C  N S 305 
LYS   C    C  N N 306 
LYS   O    O  N N 307 
LYS   CB   C  N N 308 
LYS   CG   C  N N 309 
LYS   CD   C  N N 310 
LYS   CE   C  N N 311 
LYS   NZ   N  N N 312 
LYS   OXT  O  N N 313 
LYS   H    H  N N 314 
LYS   H2   H  N N 315 
LYS   HA   H  N N 316 
LYS   HB2  H  N N 317 
LYS   HB3  H  N N 318 
LYS   HG2  H  N N 319 
LYS   HG3  H  N N 320 
LYS   HD2  H  N N 321 
LYS   HD3  H  N N 322 
LYS   HE2  H  N N 323 
LYS   HE3  H  N N 324 
LYS   HZ1  H  N N 325 
LYS   HZ2  H  N N 326 
LYS   HZ3  H  N N 327 
LYS   HXT  H  N N 328 
MET   N    N  N N 329 
MET   CA   C  N S 330 
MET   C    C  N N 331 
MET   O    O  N N 332 
MET   CB   C  N N 333 
MET   CG   C  N N 334 
MET   SD   S  N N 335 
MET   CE   C  N N 336 
MET   OXT  O  N N 337 
MET   H    H  N N 338 
MET   H2   H  N N 339 
MET   HA   H  N N 340 
MET   HB2  H  N N 341 
MET   HB3  H  N N 342 
MET   HG2  H  N N 343 
MET   HG3  H  N N 344 
MET   HE1  H  N N 345 
MET   HE2  H  N N 346 
MET   HE3  H  N N 347 
MET   HXT  H  N N 348 
NAG   C1   C  N R 349 
NAG   C2   C  N R 350 
NAG   C3   C  N R 351 
NAG   C4   C  N S 352 
NAG   C5   C  N R 353 
NAG   C6   C  N N 354 
NAG   C7   C  N N 355 
NAG   C8   C  N N 356 
NAG   N2   N  N N 357 
NAG   O1   O  N N 358 
NAG   O3   O  N N 359 
NAG   O4   O  N N 360 
NAG   O5   O  N N 361 
NAG   O6   O  N N 362 
NAG   O7   O  N N 363 
NAG   H1   H  N N 364 
NAG   H2   H  N N 365 
NAG   H3   H  N N 366 
NAG   H4   H  N N 367 
NAG   H5   H  N N 368 
NAG   H61  H  N N 369 
NAG   H62  H  N N 370 
NAG   H81  H  N N 371 
NAG   H82  H  N N 372 
NAG   H83  H  N N 373 
NAG   HN2  H  N N 374 
NAG   HO1  H  N N 375 
NAG   HO3  H  N N 376 
NAG   HO4  H  N N 377 
NAG   HO6  H  N N 378 
PHE   N    N  N N 379 
PHE   CA   C  N S 380 
PHE   C    C  N N 381 
PHE   O    O  N N 382 
PHE   CB   C  N N 383 
PHE   CG   C  Y N 384 
PHE   CD1  C  Y N 385 
PHE   CD2  C  Y N 386 
PHE   CE1  C  Y N 387 
PHE   CE2  C  Y N 388 
PHE   CZ   C  Y N 389 
PHE   OXT  O  N N 390 
PHE   H    H  N N 391 
PHE   H2   H  N N 392 
PHE   HA   H  N N 393 
PHE   HB2  H  N N 394 
PHE   HB3  H  N N 395 
PHE   HD1  H  N N 396 
PHE   HD2  H  N N 397 
PHE   HE1  H  N N 398 
PHE   HE2  H  N N 399 
PHE   HZ   H  N N 400 
PHE   HXT  H  N N 401 
PRO   N    N  N N 402 
PRO   CA   C  N S 403 
PRO   C    C  N N 404 
PRO   O    O  N N 405 
PRO   CB   C  N N 406 
PRO   CG   C  N N 407 
PRO   CD   C  N N 408 
PRO   OXT  O  N N 409 
PRO   H    H  N N 410 
PRO   HA   H  N N 411 
PRO   HB2  H  N N 412 
PRO   HB3  H  N N 413 
PRO   HG2  H  N N 414 
PRO   HG3  H  N N 415 
PRO   HD2  H  N N 416 
PRO   HD3  H  N N 417 
PRO   HXT  H  N N 418 
SER   N    N  N N 419 
SER   CA   C  N S 420 
SER   C    C  N N 421 
SER   O    O  N N 422 
SER   CB   C  N N 423 
SER   OG   O  N N 424 
SER   OXT  O  N N 425 
SER   H    H  N N 426 
SER   H2   H  N N 427 
SER   HA   H  N N 428 
SER   HB2  H  N N 429 
SER   HB3  H  N N 430 
SER   HG   H  N N 431 
SER   HXT  H  N N 432 
THR   N    N  N N 433 
THR   CA   C  N S 434 
THR   C    C  N N 435 
THR   O    O  N N 436 
THR   CB   C  N R 437 
THR   OG1  O  N N 438 
THR   CG2  C  N N 439 
THR   OXT  O  N N 440 
THR   H    H  N N 441 
THR   H2   H  N N 442 
THR   HA   H  N N 443 
THR   HB   H  N N 444 
THR   HG1  H  N N 445 
THR   HG21 H  N N 446 
THR   HG22 H  N N 447 
THR   HG23 H  N N 448 
THR   HXT  H  N N 449 
TRP   N    N  N N 450 
TRP   CA   C  N S 451 
TRP   C    C  N N 452 
TRP   O    O  N N 453 
TRP   CB   C  N N 454 
TRP   CG   C  Y N 455 
TRP   CD1  C  Y N 456 
TRP   CD2  C  Y N 457 
TRP   NE1  N  Y N 458 
TRP   CE2  C  Y N 459 
TRP   CE3  C  Y N 460 
TRP   CZ2  C  Y N 461 
TRP   CZ3  C  Y N 462 
TRP   CH2  C  Y N 463 
TRP   OXT  O  N N 464 
TRP   H    H  N N 465 
TRP   H2   H  N N 466 
TRP   HA   H  N N 467 
TRP   HB2  H  N N 468 
TRP   HB3  H  N N 469 
TRP   HD1  H  N N 470 
TRP   HE1  H  N N 471 
TRP   HE3  H  N N 472 
TRP   HZ2  H  N N 473 
TRP   HZ3  H  N N 474 
TRP   HH2  H  N N 475 
TRP   HXT  H  N N 476 
TYR   N    N  N N 477 
TYR   CA   C  N S 478 
TYR   C    C  N N 479 
TYR   O    O  N N 480 
TYR   CB   C  N N 481 
TYR   CG   C  Y N 482 
TYR   CD1  C  Y N 483 
TYR   CD2  C  Y N 484 
TYR   CE1  C  Y N 485 
TYR   CE2  C  Y N 486 
TYR   CZ   C  Y N 487 
TYR   OH   O  N N 488 
TYR   OXT  O  N N 489 
TYR   H    H  N N 490 
TYR   H2   H  N N 491 
TYR   HA   H  N N 492 
TYR   HB2  H  N N 493 
TYR   HB3  H  N N 494 
TYR   HD1  H  N N 495 
TYR   HD2  H  N N 496 
TYR   HE1  H  N N 497 
TYR   HE2  H  N N 498 
TYR   HH   H  N N 499 
TYR   HXT  H  N N 500 
VAL   N    N  N N 501 
VAL   CA   C  N S 502 
VAL   C    C  N N 503 
VAL   O    O  N N 504 
VAL   CB   C  N N 505 
VAL   CG1  C  N N 506 
VAL   CG2  C  N N 507 
VAL   OXT  O  N N 508 
VAL   H    H  N N 509 
VAL   H2   H  N N 510 
VAL   HA   H  N N 511 
VAL   HB   H  N N 512 
VAL   HG11 H  N N 513 
VAL   HG12 H  N N 514 
VAL   HG13 H  N N 515 
VAL   HG21 H  N N 516 
VAL   HG22 H  N N 517 
VAL   HG23 H  N N 518 
VAL   HXT  H  N N 519 
# 
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 
A1ATA C10 C09  sing N N 1   
A1ATA C10 N12  sing N N 2   
A1ATA C10 O11  doub N N 3   
A1ATA CG  CD2  sing N N 4   
A1ATA CG  C01  sing N N 5   
A1ATA ND1 CE2  sing N N 6   
A1ATA ND1 CZ   sing N N 7   
A1ATA CD2 CE1  sing N N 8   
A1ATA CE1 CE2  sing N N 9   
A1ATA CZ  NH1  doub N N 10  
A1ATA CZ  NH2  sing N N 11  
A1ATA C01 N02  sing N N 12  
A1ATA C01 O27  doub N N 13  
A1ATA C03 C04  sing N N 14  
A1ATA C03 N02  sing N N 15  
A1ATA C04 N05  sing N N 16  
A1ATA C06 N05  sing N N 17  
A1ATA C06 N07  sing N N 18  
A1ATA C06 O24  doub N N 19  
A1ATA C08 C09  sing N N 20  
A1ATA C08 N07  sing N N 21  
A1ATA C09 C21  sing N N 22  
A1ATA C13 C14  doub Y N 23  
A1ATA C13 C20  sing Y N 24  
A1ATA C13 N12  sing N N 25  
A1ATA C14 C15  sing Y N 26  
A1ATA C15 C17  doub Y N 27  
A1ATA C15 F16  sing N N 28  
A1ATA C17 C19  sing Y N 29  
A1ATA C17 CL1  sing N N 30  
A1ATA C19 C20  doub Y N 31  
A1ATA C21 C22  sing N N 32  
A1ATA C22 C23  sing N N 33  
A1ATA C23 N07  sing N N 34  
A1ATA C25 C26  sing N N 35  
A1ATA C25 N05  sing N N 36  
A1ATA C26 N02  sing N N 37  
A1ATA CG  H1   sing N N 38  
A1ATA CD2 H4   sing N N 39  
A1ATA CD2 H5   sing N N 40  
A1ATA CE1 H6   sing N N 41  
A1ATA CE1 H7   sing N N 42  
A1ATA CE2 H8   sing N N 43  
A1ATA CE2 H9   sing N N 44  
A1ATA NH1 H10  sing N N 45  
A1ATA NH2 H11  sing N N 46  
A1ATA NH2 H12  sing N N 47  
A1ATA C03 H13  sing N N 48  
A1ATA C03 H14  sing N N 49  
A1ATA C04 H15  sing N N 50  
A1ATA C04 H16  sing N N 51  
A1ATA C08 H17  sing N N 52  
A1ATA C08 H18  sing N N 53  
A1ATA C09 H19  sing N N 54  
A1ATA C14 H20  sing N N 55  
A1ATA C19 H21  sing N N 56  
A1ATA C20 H22  sing N N 57  
A1ATA C21 H23  sing N N 58  
A1ATA C21 H24  sing N N 59  
A1ATA C22 H25  sing N N 60  
A1ATA C22 H26  sing N N 61  
A1ATA C23 H27  sing N N 62  
A1ATA C23 H28  sing N N 63  
A1ATA C25 H29  sing N N 64  
A1ATA C25 H30  sing N N 65  
A1ATA C26 H31  sing N N 66  
A1ATA C26 H32  sing N N 67  
A1ATA N12 H33  sing N N 68  
A1ATA ND1 CG   sing N N 69  
ALA   N   CA   sing N N 70  
ALA   N   H    sing N N 71  
ALA   N   H2   sing N N 72  
ALA   CA  C    sing N N 73  
ALA   CA  CB   sing N N 74  
ALA   CA  HA   sing N N 75  
ALA   C   O    doub N N 76  
ALA   C   OXT  sing N N 77  
ALA   CB  HB1  sing N N 78  
ALA   CB  HB2  sing N N 79  
ALA   CB  HB3  sing N N 80  
ALA   OXT HXT  sing N N 81  
ARG   N   CA   sing N N 82  
ARG   N   H    sing N N 83  
ARG   N   H2   sing N N 84  
ARG   CA  C    sing N N 85  
ARG   CA  CB   sing N N 86  
ARG   CA  HA   sing N N 87  
ARG   C   O    doub N N 88  
ARG   C   OXT  sing N N 89  
ARG   CB  CG   sing N N 90  
ARG   CB  HB2  sing N N 91  
ARG   CB  HB3  sing N N 92  
ARG   CG  CD   sing N N 93  
ARG   CG  HG2  sing N N 94  
ARG   CG  HG3  sing N N 95  
ARG   CD  NE   sing N N 96  
ARG   CD  HD2  sing N N 97  
ARG   CD  HD3  sing N N 98  
ARG   NE  CZ   sing N N 99  
ARG   NE  HE   sing N N 100 
ARG   CZ  NH1  sing N N 101 
ARG   CZ  NH2  doub N N 102 
ARG   NH1 HH11 sing N N 103 
ARG   NH1 HH12 sing N N 104 
ARG   NH2 HH21 sing N N 105 
ARG   NH2 HH22 sing N N 106 
ARG   OXT HXT  sing N N 107 
ASN   N   CA   sing N N 108 
ASN   N   H    sing N N 109 
ASN   N   H2   sing N N 110 
ASN   CA  C    sing N N 111 
ASN   CA  CB   sing N N 112 
ASN   CA  HA   sing N N 113 
ASN   C   O    doub N N 114 
ASN   C   OXT  sing N N 115 
ASN   CB  CG   sing N N 116 
ASN   CB  HB2  sing N N 117 
ASN   CB  HB3  sing N N 118 
ASN   CG  OD1  doub N N 119 
ASN   CG  ND2  sing N N 120 
ASN   ND2 HD21 sing N N 121 
ASN   ND2 HD22 sing N N 122 
ASN   OXT HXT  sing N N 123 
ASP   N   CA   sing N N 124 
ASP   N   H    sing N N 125 
ASP   N   H2   sing N N 126 
ASP   CA  C    sing N N 127 
ASP   CA  CB   sing N N 128 
ASP   CA  HA   sing N N 129 
ASP   C   O    doub N N 130 
ASP   C   OXT  sing N N 131 
ASP   CB  CG   sing N N 132 
ASP   CB  HB2  sing N N 133 
ASP   CB  HB3  sing N N 134 
ASP   CG  OD1  doub N N 135 
ASP   CG  OD2  sing N N 136 
ASP   OD2 HD2  sing N N 137 
ASP   OXT HXT  sing N N 138 
CYS   N   CA   sing N N 139 
CYS   N   H    sing N N 140 
CYS   N   H2   sing N N 141 
CYS   CA  C    sing N N 142 
CYS   CA  CB   sing N N 143 
CYS   CA  HA   sing N N 144 
CYS   C   O    doub N N 145 
CYS   C   OXT  sing N N 146 
CYS   CB  SG   sing N N 147 
CYS   CB  HB2  sing N N 148 
CYS   CB  HB3  sing N N 149 
CYS   SG  HG   sing N N 150 
CYS   OXT HXT  sing N N 151 
EPE   N1  C2   sing N N 152 
EPE   N1  C6   sing N N 153 
EPE   N1  C9   sing N N 154 
EPE   C2  C3   sing N N 155 
EPE   C2  H21  sing N N 156 
EPE   C2  H22  sing N N 157 
EPE   C3  N4   sing N N 158 
EPE   C3  H31  sing N N 159 
EPE   C3  H32  sing N N 160 
EPE   N4  C5   sing N N 161 
EPE   N4  C7   sing N N 162 
EPE   C5  C6   sing N N 163 
EPE   C5  H51  sing N N 164 
EPE   C5  H52  sing N N 165 
EPE   C6  H61  sing N N 166 
EPE   C6  H62  sing N N 167 
EPE   C7  C8   sing N N 168 
EPE   C7  H71  sing N N 169 
EPE   C7  H72  sing N N 170 
EPE   C8  O8   sing N N 171 
EPE   C8  H81  sing N N 172 
EPE   C8  H82  sing N N 173 
EPE   O8  HO8  sing N N 174 
EPE   C9  C10  sing N N 175 
EPE   C9  H91  sing N N 176 
EPE   C9  H92  sing N N 177 
EPE   C10 S    sing N N 178 
EPE   C10 H101 sing N N 179 
EPE   C10 H102 sing N N 180 
EPE   S   O1S  doub N N 181 
EPE   S   O2S  doub N N 182 
EPE   S   O3S  sing N N 183 
EPE   O3S HOS3 sing N N 184 
GLN   N   CA   sing N N 185 
GLN   N   H    sing N N 186 
GLN   N   H2   sing N N 187 
GLN   CA  C    sing N N 188 
GLN   CA  CB   sing N N 189 
GLN   CA  HA   sing N N 190 
GLN   C   O    doub N N 191 
GLN   C   OXT  sing N N 192 
GLN   CB  CG   sing N N 193 
GLN   CB  HB2  sing N N 194 
GLN   CB  HB3  sing N N 195 
GLN   CG  CD   sing N N 196 
GLN   CG  HG2  sing N N 197 
GLN   CG  HG3  sing N N 198 
GLN   CD  OE1  doub N N 199 
GLN   CD  NE2  sing N N 200 
GLN   NE2 HE21 sing N N 201 
GLN   NE2 HE22 sing N N 202 
GLN   OXT HXT  sing N N 203 
GLU   N   CA   sing N N 204 
GLU   N   H    sing N N 205 
GLU   N   H2   sing N N 206 
GLU   CA  C    sing N N 207 
GLU   CA  CB   sing N N 208 
GLU   CA  HA   sing N N 209 
GLU   C   O    doub N N 210 
GLU   C   OXT  sing N N 211 
GLU   CB  CG   sing N N 212 
GLU   CB  HB2  sing N N 213 
GLU   CB  HB3  sing N N 214 
GLU   CG  CD   sing N N 215 
GLU   CG  HG2  sing N N 216 
GLU   CG  HG3  sing N N 217 
GLU   CD  OE1  doub N N 218 
GLU   CD  OE2  sing N N 219 
GLU   OE2 HE2  sing N N 220 
GLU   OXT HXT  sing N N 221 
GLY   N   CA   sing N N 222 
GLY   N   H    sing N N 223 
GLY   N   H2   sing N N 224 
GLY   CA  C    sing N N 225 
GLY   CA  HA2  sing N N 226 
GLY   CA  HA3  sing N N 227 
GLY   C   O    doub N N 228 
GLY   C   OXT  sing N N 229 
GLY   OXT HXT  sing N N 230 
HIS   N   CA   sing N N 231 
HIS   N   H    sing N N 232 
HIS   N   H2   sing N N 233 
HIS   CA  C    sing N N 234 
HIS   CA  CB   sing N N 235 
HIS   CA  HA   sing N N 236 
HIS   C   O    doub N N 237 
HIS   C   OXT  sing N N 238 
HIS   CB  CG   sing N N 239 
HIS   CB  HB2  sing N N 240 
HIS   CB  HB3  sing N N 241 
HIS   CG  ND1  sing Y N 242 
HIS   CG  CD2  doub Y N 243 
HIS   ND1 CE1  doub Y N 244 
HIS   ND1 HD1  sing N N 245 
HIS   CD2 NE2  sing Y N 246 
HIS   CD2 HD2  sing N N 247 
HIS   CE1 NE2  sing Y N 248 
HIS   CE1 HE1  sing N N 249 
HIS   NE2 HE2  sing N N 250 
HIS   OXT HXT  sing N N 251 
HOH   O   H1   sing N N 252 
HOH   O   H2   sing N N 253 
ILE   N   CA   sing N N 254 
ILE   N   H    sing N N 255 
ILE   N   H2   sing N N 256 
ILE   CA  C    sing N N 257 
ILE   CA  CB   sing N N 258 
ILE   CA  HA   sing N N 259 
ILE   C   O    doub N N 260 
ILE   C   OXT  sing N N 261 
ILE   CB  CG1  sing N N 262 
ILE   CB  CG2  sing N N 263 
ILE   CB  HB   sing N N 264 
ILE   CG1 CD1  sing N N 265 
ILE   CG1 HG12 sing N N 266 
ILE   CG1 HG13 sing N N 267 
ILE   CG2 HG21 sing N N 268 
ILE   CG2 HG22 sing N N 269 
ILE   CG2 HG23 sing N N 270 
ILE   CD1 HD11 sing N N 271 
ILE   CD1 HD12 sing N N 272 
ILE   CD1 HD13 sing N N 273 
ILE   OXT HXT  sing N N 274 
LEU   N   CA   sing N N 275 
LEU   N   H    sing N N 276 
LEU   N   H2   sing N N 277 
LEU   CA  C    sing N N 278 
LEU   CA  CB   sing N N 279 
LEU   CA  HA   sing N N 280 
LEU   C   O    doub N N 281 
LEU   C   OXT  sing N N 282 
LEU   CB  CG   sing N N 283 
LEU   CB  HB2  sing N N 284 
LEU   CB  HB3  sing N N 285 
LEU   CG  CD1  sing N N 286 
LEU   CG  CD2  sing N N 287 
LEU   CG  HG   sing N N 288 
LEU   CD1 HD11 sing N N 289 
LEU   CD1 HD12 sing N N 290 
LEU   CD1 HD13 sing N N 291 
LEU   CD2 HD21 sing N N 292 
LEU   CD2 HD22 sing N N 293 
LEU   CD2 HD23 sing N N 294 
LEU   OXT HXT  sing N N 295 
LYS   N   CA   sing N N 296 
LYS   N   H    sing N N 297 
LYS   N   H2   sing N N 298 
LYS   CA  C    sing N N 299 
LYS   CA  CB   sing N N 300 
LYS   CA  HA   sing N N 301 
LYS   C   O    doub N N 302 
LYS   C   OXT  sing N N 303 
LYS   CB  CG   sing N N 304 
LYS   CB  HB2  sing N N 305 
LYS   CB  HB3  sing N N 306 
LYS   CG  CD   sing N N 307 
LYS   CG  HG2  sing N N 308 
LYS   CG  HG3  sing N N 309 
LYS   CD  CE   sing N N 310 
LYS   CD  HD2  sing N N 311 
LYS   CD  HD3  sing N N 312 
LYS   CE  NZ   sing N N 313 
LYS   CE  HE2  sing N N 314 
LYS   CE  HE3  sing N N 315 
LYS   NZ  HZ1  sing N N 316 
LYS   NZ  HZ2  sing N N 317 
LYS   NZ  HZ3  sing N N 318 
LYS   OXT HXT  sing N N 319 
MET   N   CA   sing N N 320 
MET   N   H    sing N N 321 
MET   N   H2   sing N N 322 
MET   CA  C    sing N N 323 
MET   CA  CB   sing N N 324 
MET   CA  HA   sing N N 325 
MET   C   O    doub N N 326 
MET   C   OXT  sing N N 327 
MET   CB  CG   sing N N 328 
MET   CB  HB2  sing N N 329 
MET   CB  HB3  sing N N 330 
MET   CG  SD   sing N N 331 
MET   CG  HG2  sing N N 332 
MET   CG  HG3  sing N N 333 
MET   SD  CE   sing N N 334 
MET   CE  HE1  sing N N 335 
MET   CE  HE2  sing N N 336 
MET   CE  HE3  sing N N 337 
MET   OXT HXT  sing N N 338 
NAG   C1  C2   sing N N 339 
NAG   C1  O1   sing N N 340 
NAG   C1  O5   sing N N 341 
NAG   C1  H1   sing N N 342 
NAG   C2  C3   sing N N 343 
NAG   C2  N2   sing N N 344 
NAG   C2  H2   sing N N 345 
NAG   C3  C4   sing N N 346 
NAG   C3  O3   sing N N 347 
NAG   C3  H3   sing N N 348 
NAG   C4  C5   sing N N 349 
NAG   C4  O4   sing N N 350 
NAG   C4  H4   sing N N 351 
NAG   C5  C6   sing N N 352 
NAG   C5  O5   sing N N 353 
NAG   C5  H5   sing N N 354 
NAG   C6  O6   sing N N 355 
NAG   C6  H61  sing N N 356 
NAG   C6  H62  sing N N 357 
NAG   C7  C8   sing N N 358 
NAG   C7  N2   sing N N 359 
NAG   C7  O7   doub N N 360 
NAG   C8  H81  sing N N 361 
NAG   C8  H82  sing N N 362 
NAG   C8  H83  sing N N 363 
NAG   N2  HN2  sing N N 364 
NAG   O1  HO1  sing N N 365 
NAG   O3  HO3  sing N N 366 
NAG   O4  HO4  sing N N 367 
NAG   O6  HO6  sing N N 368 
PHE   N   CA   sing N N 369 
PHE   N   H    sing N N 370 
PHE   N   H2   sing N N 371 
PHE   CA  C    sing N N 372 
PHE   CA  CB   sing N N 373 
PHE   CA  HA   sing N N 374 
PHE   C   O    doub N N 375 
PHE   C   OXT  sing N N 376 
PHE   CB  CG   sing N N 377 
PHE   CB  HB2  sing N N 378 
PHE   CB  HB3  sing N N 379 
PHE   CG  CD1  doub Y N 380 
PHE   CG  CD2  sing Y N 381 
PHE   CD1 CE1  sing Y N 382 
PHE   CD1 HD1  sing N N 383 
PHE   CD2 CE2  doub Y N 384 
PHE   CD2 HD2  sing N N 385 
PHE   CE1 CZ   doub Y N 386 
PHE   CE1 HE1  sing N N 387 
PHE   CE2 CZ   sing Y N 388 
PHE   CE2 HE2  sing N N 389 
PHE   CZ  HZ   sing N N 390 
PHE   OXT HXT  sing N N 391 
PRO   N   CA   sing N N 392 
PRO   N   CD   sing N N 393 
PRO   N   H    sing N N 394 
PRO   CA  C    sing N N 395 
PRO   CA  CB   sing N N 396 
PRO   CA  HA   sing N N 397 
PRO   C   O    doub N N 398 
PRO   C   OXT  sing N N 399 
PRO   CB  CG   sing N N 400 
PRO   CB  HB2  sing N N 401 
PRO   CB  HB3  sing N N 402 
PRO   CG  CD   sing N N 403 
PRO   CG  HG2  sing N N 404 
PRO   CG  HG3  sing N N 405 
PRO   CD  HD2  sing N N 406 
PRO   CD  HD3  sing N N 407 
PRO   OXT HXT  sing N N 408 
SER   N   CA   sing N N 409 
SER   N   H    sing N N 410 
SER   N   H2   sing N N 411 
SER   CA  C    sing N N 412 
SER   CA  CB   sing N N 413 
SER   CA  HA   sing N N 414 
SER   C   O    doub N N 415 
SER   C   OXT  sing N N 416 
SER   CB  OG   sing N N 417 
SER   CB  HB2  sing N N 418 
SER   CB  HB3  sing N N 419 
SER   OG  HG   sing N N 420 
SER   OXT HXT  sing N N 421 
THR   N   CA   sing N N 422 
THR   N   H    sing N N 423 
THR   N   H2   sing N N 424 
THR   CA  C    sing N N 425 
THR   CA  CB   sing N N 426 
THR   CA  HA   sing N N 427 
THR   C   O    doub N N 428 
THR   C   OXT  sing N N 429 
THR   CB  OG1  sing N N 430 
THR   CB  CG2  sing N N 431 
THR   CB  HB   sing N N 432 
THR   OG1 HG1  sing N N 433 
THR   CG2 HG21 sing N N 434 
THR   CG2 HG22 sing N N 435 
THR   CG2 HG23 sing N N 436 
THR   OXT HXT  sing N N 437 
TRP   N   CA   sing N N 438 
TRP   N   H    sing N N 439 
TRP   N   H2   sing N N 440 
TRP   CA  C    sing N N 441 
TRP   CA  CB   sing N N 442 
TRP   CA  HA   sing N N 443 
TRP   C   O    doub N N 444 
TRP   C   OXT  sing N N 445 
TRP   CB  CG   sing N N 446 
TRP   CB  HB2  sing N N 447 
TRP   CB  HB3  sing N N 448 
TRP   CG  CD1  doub Y N 449 
TRP   CG  CD2  sing Y N 450 
TRP   CD1 NE1  sing Y N 451 
TRP   CD1 HD1  sing N N 452 
TRP   CD2 CE2  doub Y N 453 
TRP   CD2 CE3  sing Y N 454 
TRP   NE1 CE2  sing Y N 455 
TRP   NE1 HE1  sing N N 456 
TRP   CE2 CZ2  sing Y N 457 
TRP   CE3 CZ3  doub Y N 458 
TRP   CE3 HE3  sing N N 459 
TRP   CZ2 CH2  doub Y N 460 
TRP   CZ2 HZ2  sing N N 461 
TRP   CZ3 CH2  sing Y N 462 
TRP   CZ3 HZ3  sing N N 463 
TRP   CH2 HH2  sing N N 464 
TRP   OXT HXT  sing N N 465 
TYR   N   CA   sing N N 466 
TYR   N   H    sing N N 467 
TYR   N   H2   sing N N 468 
TYR   CA  C    sing N N 469 
TYR   CA  CB   sing N N 470 
TYR   CA  HA   sing N N 471 
TYR   C   O    doub N N 472 
TYR   C   OXT  sing N N 473 
TYR   CB  CG   sing N N 474 
TYR   CB  HB2  sing N N 475 
TYR   CB  HB3  sing N N 476 
TYR   CG  CD1  doub Y N 477 
TYR   CG  CD2  sing Y N 478 
TYR   CD1 CE1  sing Y N 479 
TYR   CD1 HD1  sing N N 480 
TYR   CD2 CE2  doub Y N 481 
TYR   CD2 HD2  sing N N 482 
TYR   CE1 CZ   doub Y N 483 
TYR   CE1 HE1  sing N N 484 
TYR   CE2 CZ   sing Y N 485 
TYR   CE2 HE2  sing N N 486 
TYR   CZ  OH   sing N N 487 
TYR   OH  HH   sing N N 488 
TYR   OXT HXT  sing N N 489 
VAL   N   CA   sing N N 490 
VAL   N   H    sing N N 491 
VAL   N   H2   sing N N 492 
VAL   CA  C    sing N N 493 
VAL   CA  CB   sing N N 494 
VAL   CA  HA   sing N N 495 
VAL   C   O    doub N N 496 
VAL   C   OXT  sing N N 497 
VAL   CB  CG1  sing N N 498 
VAL   CB  CG2  sing N N 499 
VAL   CB  HB   sing N N 500 
VAL   CG1 HG11 sing N N 501 
VAL   CG1 HG12 sing N N 502 
VAL   CG1 HG13 sing N N 503 
VAL   CG2 HG21 sing N N 504 
VAL   CG2 HG22 sing N N 505 
VAL   CG2 HG23 sing N N 506 
VAL   OXT HXT  sing N N 507 
# 
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                    9BXG 
_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]   0.015076 
_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]   0.014812 
_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]   0.011396 
_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   ? -24.496 18.099  1.397   1.00 50.24 ? 44  VAL   A N   1 
ATOM   2    C  CA  . VAL   A 1 3   ? -23.715 17.558  0.289   1.00 50.29 ? 44  VAL   A CA  1 
ATOM   3    C  C   . VAL   A 1 3   ? -22.413 16.923  0.790   1.00 49.19 ? 44  VAL   A C   1 
ATOM   4    O  O   . VAL   A 1 3   ? -21.674 17.524  1.576   1.00 49.13 ? 44  VAL   A O   1 
ATOM   5    C  CB  . VAL   A 1 3   ? -23.437 18.652  -0.769  1.00 55.02 ? 44  VAL   A CB  1 
ATOM   6    C  CG1 . VAL   A 1 3   ? -22.123 19.366  -0.486  1.00 52.69 ? 44  VAL   A CG1 1 
ATOM   7    C  CG2 . VAL   A 1 3   ? -23.434 18.050  -2.168  1.00 52.02 ? 44  VAL   A CG2 1 
ATOM   8    N  N   . TRP   A 1 4   ? -22.147 15.698  0.332   1.00 46.69 ? 45  TRP   A N   1 
ATOM   9    C  CA  . TRP   A 1 4   ? -20.970 14.946  0.746   1.00 48.36 ? 45  TRP   A CA  1 
ATOM   10   C  C   . TRP   A 1 4   ? -20.516 14.059  -0.404  1.00 44.11 ? 45  TRP   A C   1 
ATOM   11   O  O   . TRP   A 1 4   ? -21.213 13.900  -1.407  1.00 47.23 ? 45  TRP   A O   1 
ATOM   12   C  CB  . TRP   A 1 4   ? -21.261 14.097  1.988   1.00 42.16 ? 45  TRP   A CB  1 
ATOM   13   C  CG  . TRP   A 1 4   ? -22.261 13.010  1.723   1.00 43.61 ? 45  TRP   A CG  1 
ATOM   14   C  CD1 . TRP   A 1 4   ? -22.027 11.808  1.119   1.00 41.55 ? 45  TRP   A CD1 1 
ATOM   15   C  CD2 . TRP   A 1 4   ? -23.659 13.041  2.025   1.00 42.12 ? 45  TRP   A CD2 1 
ATOM   16   N  NE1 . TRP   A 1 4   ? -23.191 11.085  1.036   1.00 41.87 ? 45  TRP   A NE1 1 
ATOM   17   C  CE2 . TRP   A 1 4   ? -24.209 11.821  1.585   1.00 40.77 ? 45  TRP   A CE2 1 
ATOM   18   C  CE3 . TRP   A 1 4   ? -24.499 13.981  2.630   1.00 41.96 ? 45  TRP   A CE3 1 
ATOM   19   C  CZ2 . TRP   A 1 4   ? -25.559 11.514  1.734   1.00 43.10 ? 45  TRP   A CZ2 1 
ATOM   20   C  CZ3 . TRP   A 1 4   ? -25.839 13.674  2.776   1.00 42.21 ? 45  TRP   A CZ3 1 
ATOM   21   C  CH2 . TRP   A 1 4   ? -26.356 12.453  2.329   1.00 40.99 ? 45  TRP   A CH2 1 
ATOM   22   N  N   . LYS   A 1 5   ? -19.333 13.469  -0.238  1.00 44.84 ? 46  LYS   A N   1 
ATOM   23   C  CA  . LYS   A 1 5   ? -18.779 12.518  -1.190  1.00 45.81 ? 46  LYS   A CA  1 
ATOM   24   C  C   . LYS   A 1 5   ? -18.008 11.447  -0.429  1.00 42.60 ? 46  LYS   A C   1 
ATOM   25   O  O   . LYS   A 1 5   ? -17.486 11.696  0.660   1.00 39.51 ? 46  LYS   A O   1 
ATOM   26   C  CB  . LYS   A 1 5   ? -17.841 13.201  -2.202  1.00 48.50 ? 46  LYS   A CB  1 
ATOM   27   C  CG  . LYS   A 1 5   ? -16.461 13.501  -1.643  1.00 48.21 ? 46  LYS   A CG  1 
ATOM   28   C  CD  . LYS   A 1 5   ? -15.625 14.351  -2.586  1.00 53.94 ? 46  LYS   A CD  1 
ATOM   29   C  CE  . LYS   A 1 5   ? -14.156 14.326  -2.189  1.00 58.68 ? 46  LYS   A CE  1 
ATOM   30   N  NZ  . LYS   A 1 5   ? -13.424 15.546  -2.636  1.00 64.79 ? 46  LYS   A NZ  1 
ATOM   31   N  N   . ASP   A 1 6   ? -17.934 10.254  -1.013  1.00 44.11 ? 47  ASP   A N   1 
ATOM   32   C  CA  . ASP   A 1 6   ? -17.172 9.177   -0.394  1.00 43.57 ? 47  ASP   A CA  1 
ATOM   33   C  C   . ASP   A 1 6   ? -15.705 9.571   -0.269  1.00 44.81 ? 47  ASP   A C   1 
ATOM   34   O  O   . ASP   A 1 6   ? -15.094 10.048  -1.229  1.00 43.63 ? 47  ASP   A O   1 
ATOM   35   C  CB  . ASP   A 1 6   ? -17.307 7.885   -1.204  1.00 47.48 ? 47  ASP   A CB  1 
ATOM   36   C  CG  . ASP   A 1 6   ? -18.674 7.240   -1.054  1.00 46.61 ? 47  ASP   A CG  1 
ATOM   37   O  OD1 . ASP   A 1 6   ? -19.294 7.391   0.020   1.00 47.36 ? 47  ASP   A OD1 1 
ATOM   38   O  OD2 . ASP   A 1 6   ? -19.114 6.564   -2.007  1.00 51.32 ? 47  ASP   A OD2 1 
ATOM   39   N  N   . ALA   A 1 7   ? -15.135 9.354   0.915   1.00 38.87 ? 48  ALA   A N   1 
ATOM   40   C  CA  . ALA   A 1 7   ? -13.765 9.763   1.184   1.00 39.79 ? 48  ALA   A CA  1 
ATOM   41   C  C   . ALA   A 1 7   ? -13.209 8.949   2.343   1.00 41.02 ? 48  ALA   A C   1 
ATOM   42   O  O   . ALA   A 1 7   ? -13.956 8.397   3.156   1.00 40.12 ? 48  ALA   A O   1 
ATOM   43   C  CB  . ALA   A 1 7   ? -13.682 11.261  1.492   1.00 43.22 ? 48  ALA   A CB  1 
ATOM   44   N  N   . ASP   A 1 8   ? -11.882 8.875   2.394   1.00 35.62 ? 49  ASP   A N   1 
ATOM   45   C  CA  . ASP   A 1 8   ? -11.157 8.278   3.504   1.00 37.74 ? 49  ASP   A CA  1 
ATOM   46   C  C   . ASP   A 1 8   ? -10.396 9.369   4.247   1.00 38.09 ? 49  ASP   A C   1 
ATOM   47   O  O   . ASP   A 1 8   ? -9.797  10.254  3.626   1.00 40.67 ? 49  ASP   A O   1 
ATOM   48   C  CB  . ASP   A 1 8   ? -10.159 7.218   3.022   1.00 40.37 ? 49  ASP   A CB  1 
ATOM   49   C  CG  . ASP   A 1 8   ? -10.826 5.994   2.424   1.00 36.70 ? 49  ASP   A CG  1 
ATOM   50   O  OD1 . ASP   A 1 8   ? -12.031 5.776   2.670   1.00 40.82 ? 49  ASP   A OD1 1 
ATOM   51   O  OD2 . ASP   A 1 8   ? -10.127 5.231   1.717   1.00 44.46 ? 49  ASP   A OD2 1 
ATOM   52   N  N   . THR   A 1 9   ? -10.410 9.305   5.576   1.00 36.42 ? 50  THR   A N   1 
ATOM   53   C  CA  . THR   A 1 9   ? -9.596  10.214  6.367   1.00 35.24 ? 50  THR   A CA  1 
ATOM   54   C  C   . THR   A 1 9   ? -9.238  9.539   7.682   1.00 33.88 ? 50  THR   A C   1 
ATOM   55   O  O   . THR   A 1 9   ? -9.833  8.530   8.071   1.00 32.24 ? 50  THR   A O   1 
ATOM   56   C  CB  . THR   A 1 9   ? -10.305 11.556  6.609   1.00 36.65 ? 50  THR   A CB  1 
ATOM   57   O  OG1 . THR   A 1 9   ? -9.331  12.548  6.958   1.00 35.10 ? 50  THR   A OG1 1 
ATOM   58   C  CG2 . THR   A 1 9   ? -11.323 11.431  7.738   1.00 34.56 ? 50  THR   A CG2 1 
ATOM   59   N  N   . THR   A 1 10  ? -8.243  10.102  8.358   1.00 33.06 ? 51  THR   A N   1 
ATOM   60   C  CA  . THR   A 1 10  ? -7.743  9.515   9.595   1.00 32.70 ? 51  THR   A CA  1 
ATOM   61   C  C   . THR   A 1 10  ? -8.728  9.774   10.727  1.00 33.55 ? 51  THR   A C   1 
ATOM   62   O  O   . THR   A 1 10  ? -9.009  10.929  11.064  1.00 30.71 ? 51  THR   A O   1 
ATOM   63   C  CB  . THR   A 1 10  ? -6.363  10.065  9.945   1.00 37.26 ? 51  THR   A CB  1 
ATOM   64   O  OG1 . THR   A 1 10  ? -5.540  10.070  8.772   1.00 39.20 ? 51  THR   A OG1 1 
ATOM   65   C  CG2 . THR   A 1 10  ? -5.711  9.192   11.011  1.00 35.63 ? 51  THR   A CG2 1 
ATOM   66   N  N   . LEU   A 1 11  ? -9.231  8.699   11.325  1.00 28.26 ? 52  LEU   A N   1 
ATOM   67   C  CA  . LEU   A 1 11  ? -10.219 8.783   12.386  1.00 29.25 ? 52  LEU   A CA  1 
ATOM   68   C  C   . LEU   A 1 11  ? -9.519  8.952   13.729  1.00 27.38 ? 52  LEU   A C   1 
ATOM   69   O  O   . LEU   A 1 11  ? -8.308  8.761   13.854  1.00 31.15 ? 52  LEU   A O   1 
ATOM   70   C  CB  . LEU   A 1 11  ? -11.091 7.522   12.385  1.00 28.17 ? 52  LEU   A CB  1 
ATOM   71   C  CG  . LEU   A 1 11  ? -11.867 7.236   11.095  1.00 32.58 ? 52  LEU   A CG  1 
ATOM   72   C  CD1 . LEU   A 1 11  ? -12.437 5.833   11.117  1.00 31.87 ? 52  LEU   A CD1 1 
ATOM   73   C  CD2 . LEU   A 1 11  ? -12.968 8.263   10.877  1.00 30.88 ? 52  LEU   A CD2 1 
ATOM   74   N  N   . PHE   A 1 12  ? -10.293 9.311   14.747  1.00 24.78 ? 53  PHE   A N   1 
ATOM   75   C  CA  . PHE   A 1 12  ? -9.826  9.238   16.122  1.00 26.61 ? 53  PHE   A CA  1 
ATOM   76   C  C   . PHE   A 1 12  ? -10.781 8.364   16.925  1.00 25.75 ? 53  PHE   A C   1 
ATOM   77   O  O   . PHE   A 1 12  ? -11.869 8.012   16.468  1.00 29.76 ? 53  PHE   A O   1 
ATOM   78   C  CB  . PHE   A 1 12  ? -9.657  10.639  16.740  1.00 27.42 ? 53  PHE   A CB  1 
ATOM   79   C  CG  . PHE   A 1 12  ? -10.947 11.368  17.048  1.00 28.53 ? 53  PHE   A CG  1 
ATOM   80   C  CD1 . PHE   A 1 12  ? -11.586 11.193  18.267  1.00 25.67 ? 53  PHE   A CD1 1 
ATOM   81   C  CD2 . PHE   A 1 12  ? -11.477 12.283  16.145  1.00 28.46 ? 53  PHE   A CD2 1 
ATOM   82   C  CE1 . PHE   A 1 12  ? -12.746 11.884  18.562  1.00 29.81 ? 53  PHE   A CE1 1 
ATOM   83   C  CE2 . PHE   A 1 12  ? -12.638 12.978  16.435  1.00 26.39 ? 53  PHE   A CE2 1 
ATOM   84   C  CZ  . PHE   A 1 12  ? -13.275 12.778  17.644  1.00 27.98 ? 53  PHE   A CZ  1 
ATOM   85   N  N   . CYS   A 1 13  ? -10.356 7.982   18.124  1.00 26.36 ? 54  CYS   A N   1 
ATOM   86   C  CA  . CYS   A 1 13  ? -11.111 7.045   18.941  1.00 27.45 ? 54  CYS   A CA  1 
ATOM   87   C  C   . CYS   A 1 13  ? -11.538 7.695   20.247  1.00 25.90 ? 54  CYS   A C   1 
ATOM   88   O  O   . CYS   A 1 13  ? -10.915 8.650   20.725  1.00 26.12 ? 54  CYS   A O   1 
ATOM   89   C  CB  . CYS   A 1 13  ? -10.312 5.757   19.231  1.00 29.52 ? 54  CYS   A CB  1 
ATOM   90   S  SG  . CYS   A 1 13  ? -8.714  5.962   20.069  1.00 31.31 ? 54  CYS   A SG  1 
ATOM   91   N  N   . ALA   A 1 14  ? -12.629 7.171   20.801  1.00 23.88 ? 55  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 14  ? -13.198 7.625   22.061  1.00 28.76 ? 55  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 14  ? -13.590 6.407   22.885  1.00 28.93 ? 55  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 14  ? -13.944 5.357   22.339  1.00 24.30 ? 55  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 14  ? -14.418 8.536   21.847  1.00 30.29 ? 55  ALA   A CB  1 
ATOM   96   N  N   . SER   A 1 15  ? -13.528 6.552   24.208  1.00 29.17 ? 56  SER   A N   1 
ATOM   97   C  CA  . SER   A 1 15  ? -13.838 5.426   25.078  1.00 29.49 ? 56  SER   A CA  1 
ATOM   98   C  C   . SER   A 1 15  ? -14.151 5.926   26.478  1.00 32.49 ? 56  SER   A C   1 
ATOM   99   O  O   . SER   A 1 15  ? -13.873 7.076   26.824  1.00 31.10 ? 56  SER   A O   1 
ATOM   100  C  CB  . SER   A 1 15  ? -12.681 4.423   25.130  1.00 32.24 ? 56  SER   A CB  1 
ATOM   101  O  OG  . SER   A 1 15  ? -11.776 4.752   26.176  1.00 31.79 ? 56  SER   A OG  1 
ATOM   102  N  N   . ASP   A 1 16  ? -14.754 5.037   27.273  1.00 29.98 ? 57  ASP   A N   1 
ATOM   103  C  CA  . ASP   A 1 16  ? -15.010 5.269   28.687  1.00 33.80 ? 57  ASP   A CA  1 
ATOM   104  C  C   . ASP   A 1 16  ? -13.897 4.714   29.572  1.00 33.04 ? 57  ASP   A C   1 
ATOM   105  O  O   . ASP   A 1 16  ? -14.160 4.304   30.710  1.00 35.66 ? 57  ASP   A O   1 
ATOM   106  C  CB  . ASP   A 1 16  ? -16.360 4.661   29.068  1.00 35.92 ? 57  ASP   A CB  1 
ATOM   107  C  CG  . ASP   A 1 16  ? -17.525 5.364   28.393  1.00 36.71 ? 57  ASP   A CG  1 
ATOM   108  O  OD1 . ASP   A 1 16  ? -17.408 6.577   28.119  1.00 42.73 ? 57  ASP   A OD1 1 
ATOM   109  O  OD2 . ASP   A 1 16  ? -18.552 4.702   28.136  1.00 43.87 ? 57  ASP   A OD2 1 
ATOM   110  N  N   . ALA   A 1 17  ? -12.667 4.675   29.063  1.00 33.79 ? 58  ALA   A N   1 
ATOM   111  C  CA  . ALA   A 1 17  ? -11.547 4.123   29.809  1.00 34.50 ? 58  ALA   A CA  1 
ATOM   112  C  C   . ALA   A 1 17  ? -11.426 4.785   31.175  1.00 38.04 ? 58  ALA   A C   1 
ATOM   113  O  O   . ALA   A 1 17  ? -11.686 5.981   31.332  1.00 31.20 ? 58  ALA   A O   1 
ATOM   114  C  CB  . ALA   A 1 17  ? -10.255 4.311   29.016  1.00 30.28 ? 58  ALA   A CB  1 
ATOM   115  N  N   . LYS   A 1 18  ? -11.031 3.991   32.166  1.00 35.74 ? 59  LYS   A N   1 
ATOM   116  C  CA  . LYS   A 1 18  ? -10.832 4.466   33.529  1.00 39.61 ? 59  LYS   A CA  1 
ATOM   117  C  C   . LYS   A 1 18  ? -9.360  4.804   33.729  1.00 38.94 ? 59  LYS   A C   1 
ATOM   118  O  O   . LYS   A 1 18  ? -8.486  3.970   33.468  1.00 36.14 ? 59  LYS   A O   1 
ATOM   119  C  CB  . LYS   A 1 18  ? -11.280 3.418   34.548  1.00 40.19 ? 59  LYS   A CB  1 
ATOM   120  C  CG  . LYS   A 1 18  ? -12.632 2.796   34.262  1.00 42.45 ? 59  LYS   A CG  1 
ATOM   121  C  CD  . LYS   A 1 18  ? -13.704 3.266   35.231  1.00 48.66 ? 59  LYS   A CD  1 
ATOM   122  C  CE  . LYS   A 1 18  ? -14.907 2.340   35.183  1.00 48.10 ? 59  LYS   A CE  1 
ATOM   123  N  NZ  . LYS   A 1 18  ? -14.469 0.917   35.076  1.00 51.60 ? 59  LYS   A NZ  1 
ATOM   124  N  N   . ALA   A 1 19  ? -9.089  6.026   34.196  1.00 36.88 ? 60  ALA   A N   1 
ATOM   125  C  CA  . ALA   A 1 19  ? -7.706  6.469   34.339  1.00 39.07 ? 60  ALA   A CA  1 
ATOM   126  C  C   . ALA   A 1 19  ? -6.942  5.626   35.353  1.00 38.02 ? 60  ALA   A C   1 
ATOM   127  O  O   . ALA   A 1 19  ? -5.719  5.475   35.241  1.00 37.06 ? 60  ALA   A O   1 
ATOM   128  C  CB  . ALA   A 1 19  ? -7.666  7.945   34.737  1.00 40.41 ? 60  ALA   A CB  1 
ATOM   129  N  N   . TYR   A 1 20  ? -7.635  5.073   36.345  1.00 37.91 ? 61  TYR   A N   1 
ATOM   130  C  CA  . TYR   A 1 20  ? -6.997  4.319   37.417  1.00 42.88 ? 61  TYR   A CA  1 
ATOM   131  C  C   . TYR   A 1 20  ? -6.778  2.850   37.091  1.00 46.03 ? 61  TYR   A C   1 
ATOM   132  O  O   . TYR   A 1 20  ? -6.110  2.152   37.864  1.00 45.08 ? 61  TYR   A O   1 
ATOM   133  C  CB  . TYR   A 1 20  ? -7.829  4.423   38.703  1.00 42.65 ? 61  TYR   A CB  1 
ATOM   134  C  CG  . TYR   A 1 20  ? -9.259  3.924   38.585  1.00 46.87 ? 61  TYR   A CG  1 
ATOM   135  C  CD1 . TYR   A 1 20  ? -9.544  2.564   38.484  1.00 47.25 ? 61  TYR   A CD1 1 
ATOM   136  C  CD2 . TYR   A 1 20  ? -10.324 4.813   38.607  1.00 45.43 ? 61  TYR   A CD2 1 
ATOM   137  C  CE1 . TYR   A 1 20  ? -10.848 2.109   38.383  1.00 46.09 ? 61  TYR   A CE1 1 
ATOM   138  C  CE2 . TYR   A 1 20  ? -11.632 4.368   38.512  1.00 50.54 ? 61  TYR   A CE2 1 
ATOM   139  C  CZ  . TYR   A 1 20  ? -11.888 3.017   38.399  1.00 48.35 ? 61  TYR   A CZ  1 
ATOM   140  O  OH  . TYR   A 1 20  ? -13.191 2.581   38.305  1.00 51.88 ? 61  TYR   A OH  1 
ATOM   141  N  N   . GLU   A 1 21  ? -7.315  2.360   35.981  1.00 40.16 ? 62  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 21  ? -7.265  0.936   35.700  1.00 37.78 ? 62  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 21  ? -5.880  0.526   35.220  1.00 36.87 ? 62  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 21  ? -5.213  1.265   34.494  1.00 38.78 ? 62  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 21  ? -8.316  0.560   34.654  1.00 39.04 ? 62  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 21  ? -9.521  -0.162  35.230  1.00 38.46 ? 62  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 21  ? -9.197  -1.578  35.672  1.00 41.17 ? 62  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 21  ? -8.042  -2.014  35.474  1.00 43.47 ? 62  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 21  ? -10.098 -2.248  36.217  1.00 45.46 ? 62  GLU   A OE2 1 
ATOM   150  N  N   . THR   A 1 22  ? -5.448  -0.662  35.642  1.00 35.78 ? 63  THR   A N   1 
ATOM   151  C  CA  . THR   A 1 22  ? -4.257  -1.287  35.091  1.00 34.37 ? 63  THR   A CA  1 
ATOM   152  C  C   . THR   A 1 22  ? -4.583  -2.192  33.911  1.00 33.94 ? 63  THR   A C   1 
ATOM   153  O  O   . THR   A 1 22  ? -3.683  -2.550  33.145  1.00 31.34 ? 63  THR   A O   1 
ATOM   154  C  CB  . THR   A 1 22  ? -3.538  -2.086  36.180  1.00 35.81 ? 63  THR   A CB  1 
ATOM   155  O  OG1 . THR   A 1 22  ? -4.449  -3.026  36.764  1.00 38.62 ? 63  THR   A OG1 1 
ATOM   156  C  CG2 . THR   A 1 22  ? -3.027  -1.150  37.259  1.00 37.85 ? 63  THR   A CG2 1 
ATOM   157  N  N   . GLU   A 1 23  ? -5.848  -2.577  33.766  1.00 35.53 ? 64  GLU   A N   1 
ATOM   158  C  CA  . GLU   A 1 23  ? -6.305  -3.321  32.600  1.00 34.83 ? 64  GLU   A CA  1 
ATOM   159  C  C   . GLU   A 1 23  ? -5.810  -2.643  31.324  1.00 33.99 ? 64  GLU   A C   1 
ATOM   160  O  O   . GLU   A 1 23  ? -5.927  -1.425  31.168  1.00 35.64 ? 64  GLU   A O   1 
ATOM   161  C  CB  . GLU   A 1 23  ? -7.836  -3.397  32.645  1.00 34.30 ? 64  GLU   A CB  1 
ATOM   162  C  CG  . GLU   A 1 23  ? -8.469  -4.408  31.706  1.00 33.84 ? 64  GLU   A CG  1 
ATOM   163  C  CD  . GLU   A 1 23  ? -8.304  -4.027  30.257  1.00 32.66 ? 64  GLU   A CD  1 
ATOM   164  O  OE1 . GLU   A 1 23  ? -8.473  -2.831  29.933  1.00 34.46 ? 64  GLU   A OE1 1 
ATOM   165  O  OE2 . GLU   A 1 23  ? -8.003  -4.921  29.441  1.00 32.71 ? 64  GLU   A OE2 1 
ATOM   166  N  N   . VAL   A 1 24  ? -5.262  -3.442  30.404  1.00 27.17 ? 65  VAL   A N   1 
ATOM   167  C  CA  . VAL   A 1 24  ? -4.455  -2.884  29.324  1.00 30.91 ? 65  VAL   A CA  1 
ATOM   168  C  C   . VAL   A 1 24  ? -5.291  -2.109  28.312  1.00 33.30 ? 65  VAL   A C   1 
ATOM   169  O  O   . VAL   A 1 24  ? -4.812  -1.123  27.742  1.00 31.83 ? 65  VAL   A O   1 
ATOM   170  C  CB  . VAL   A 1 24  ? -3.642  -3.996  28.637  1.00 33.25 ? 65  VAL   A CB  1 
ATOM   171  C  CG1 . VAL   A 1 24  ? -2.633  -4.599  29.606  1.00 35.70 ? 65  VAL   A CG1 1 
ATOM   172  C  CG2 . VAL   A 1 24  ? -4.570  -5.079  28.106  1.00 32.35 ? 65  VAL   A CG2 1 
ATOM   173  N  N   . HIS   A 1 25  ? -6.526  -2.538  28.040  1.00 28.38 ? 66  HIS   A N   1 
ATOM   174  C  CA  . HIS   A 1 25  ? -7.352  -1.771  27.113  1.00 29.72 ? 66  HIS   A CA  1 
ATOM   175  C  C   . HIS   A 1 25  ? -7.607  -0.374  27.658  1.00 28.32 ? 66  HIS   A C   1 
ATOM   176  O  O   . HIS   A 1 25  ? -7.538  0.614   26.920  1.00 27.89 ? 66  HIS   A O   1 
ATOM   177  C  CB  . HIS   A 1 25  ? -8.673  -2.493  26.848  1.00 29.85 ? 66  HIS   A CB  1 
ATOM   178  C  CG  . HIS   A 1 25  ? -8.531  -3.734  26.022  1.00 26.89 ? 66  HIS   A CG  1 
ATOM   179  N  ND1 . HIS   A 1 25  ? -8.293  -4.973  26.575  1.00 29.84 ? 66  HIS   A ND1 1 
ATOM   180  C  CD2 . HIS   A 1 25  ? -8.596  -3.925  24.683  1.00 27.85 ? 66  HIS   A CD2 1 
ATOM   181  C  CE1 . HIS   A 1 25  ? -8.222  -5.876  25.612  1.00 30.60 ? 66  HIS   A CE1 1 
ATOM   182  N  NE2 . HIS   A 1 25  ? -8.400  -5.266  24.455  1.00 29.93 ? 66  HIS   A NE2 1 
ATOM   183  N  N   . ASN   A 1 26  ? -7.909  -0.276  28.952  1.00 29.01 ? 67  ASN   A N   1 
ATOM   184  C  CA  . ASN   A 1 26  ? -8.114  1.024   29.579  1.00 34.97 ? 67  ASN   A CA  1 
ATOM   185  C  C   . ASN   A 1 26  ? -6.873  1.896   29.444  1.00 33.78 ? 67  ASN   A C   1 
ATOM   186  O  O   . ASN   A 1 26  ? -6.966  3.073   29.081  1.00 30.93 ? 67  ASN   A O   1 
ATOM   187  C  CB  . ASN   A 1 26  ? -8.492  0.828   31.047  1.00 31.97 ? 67  ASN   A CB  1 
ATOM   188  C  CG  . ASN   A 1 26  ? -9.927  0.362   31.228  1.00 32.86 ? 67  ASN   A CG  1 
ATOM   189  O  OD1 . ASN   A 1 26  ? -10.844 1.173   31.375  1.00 30.42 ? 67  ASN   A OD1 1 
ATOM   190  N  ND2 . ASN   A 1 26  ? -10.131 -0.951  31.202  1.00 32.85 ? 67  ASN   A ND2 1 
ATOM   191  N  N   . VAL   A 1 27  ? -5.695  1.329   29.722  1.00 32.93 ? 68  VAL   A N   1 
ATOM   192  C  CA  . VAL   A 1 27  ? -4.458  2.105   29.636  1.00 34.71 ? 68  VAL   A CA  1 
ATOM   193  C  C   . VAL   A 1 27  ? -4.257  2.639   28.226  1.00 35.52 ? 68  VAL   A C   1 
ATOM   194  O  O   . VAL   A 1 27  ? -3.923  3.813   28.030  1.00 33.70 ? 68  VAL   A O   1 
ATOM   195  C  CB  . VAL   A 1 27  ? -3.255  1.259   30.090  1.00 32.34 ? 68  VAL   A CB  1 
ATOM   196  C  CG1 . VAL   A 1 27  ? -1.951  1.953   29.726  1.00 38.60 ? 68  VAL   A CG1 1 
ATOM   197  C  CG2 . VAL   A 1 27  ? -3.322  1.000   31.581  1.00 37.96 ? 68  VAL   A CG2 1 
ATOM   198  N  N   . TRP   A 1 28  ? -4.442  1.781   27.220  1.00 30.70 ? 69  TRP   A N   1 
ATOM   199  C  CA  . TRP   A 1 28  ? -4.264  2.220   25.842  1.00 32.86 ? 69  TRP   A CA  1 
ATOM   200  C  C   . TRP   A 1 28  ? -5.282  3.287   25.461  1.00 31.57 ? 69  TRP   A C   1 
ATOM   201  O  O   . TRP   A 1 28  ? -4.930  4.304   24.849  1.00 31.41 ? 69  TRP   A O   1 
ATOM   202  C  CB  . TRP   A 1 28  ? -4.345  1.025   24.894  1.00 29.23 ? 69  TRP   A CB  1 
ATOM   203  C  CG  . TRP   A 1 28  ? -4.184  1.414   23.461  1.00 28.37 ? 69  TRP   A CG  1 
ATOM   204  C  CD1 . TRP   A 1 28  ? -3.017  1.505   22.759  1.00 32.57 ? 69  TRP   A CD1 1 
ATOM   205  C  CD2 . TRP   A 1 28  ? -5.229  1.774   22.551  1.00 30.24 ? 69  TRP   A CD2 1 
ATOM   206  N  NE1 . TRP   A 1 28  ? -3.271  1.902   21.469  1.00 32.74 ? 69  TRP   A NE1 1 
ATOM   207  C  CE2 . TRP   A 1 28  ? -4.623  2.069   21.315  1.00 31.52 ? 69  TRP   A CE2 1 
ATOM   208  C  CE3 . TRP   A 1 28  ? -6.621  1.870   22.660  1.00 31.55 ? 69  TRP   A CE3 1 
ATOM   209  C  CZ2 . TRP   A 1 28  ? -5.359  2.455   20.196  1.00 27.36 ? 69  TRP   A CZ2 1 
ATOM   210  C  CZ3 . TRP   A 1 28  ? -7.348  2.255   21.550  1.00 28.47 ? 69  TRP   A CZ3 1 
ATOM   211  C  CH2 . TRP   A 1 28  ? -6.716  2.543   20.334  1.00 27.40 ? 69  TRP   A CH2 1 
ATOM   212  N  N   . ALA   A 1 29  ? -6.556  3.070   25.805  1.00 31.25 ? 70  ALA   A N   1 
ATOM   213  C  CA  . ALA   A 1 29  ? -7.584  4.049   25.472  1.00 29.55 ? 70  ALA   A CA  1 
ATOM   214  C  C   . ALA   A 1 29  ? -7.383  5.355   26.228  1.00 31.77 ? 70  ALA   A C   1 
ATOM   215  O  O   . ALA   A 1 29  ? -7.738  6.423   25.720  1.00 30.67 ? 70  ALA   A O   1 
ATOM   216  C  CB  . ALA   A 1 29  ? -8.972  3.478   25.760  1.00 28.74 ? 70  ALA   A CB  1 
ATOM   217  N  N   . THR   A 1 30  ? -6.817  5.290   27.433  1.00 30.68 ? 71  THR   A N   1 
ATOM   218  C  CA  . THR   A 1 30  ? -6.594  6.505   28.208  1.00 32.04 ? 71  THR   A CA  1 
ATOM   219  C  C   . THR   A 1 30  ? -5.653  7.464   27.489  1.00 32.39 ? 71  THR   A C   1 
ATOM   220  O  O   . THR   A 1 30  ? -5.846  8.683   27.539  1.00 32.84 ? 71  THR   A O   1 
ATOM   221  C  CB  . THR   A 1 30  ? -6.047  6.154   29.591  1.00 35.83 ? 71  THR   A CB  1 
ATOM   222  O  OG1 . THR   A 1 30  ? -7.040  5.438   30.336  1.00 34.49 ? 71  THR   A OG1 1 
ATOM   223  C  CG2 . THR   A 1 30  ? -5.650  7.422   30.346  1.00 38.23 ? 71  THR   A CG2 1 
ATOM   224  N  N   . HIS   A 1 31  ? -4.630  6.941   26.809  1.00 29.99 ? 72  HIS   A N   1 
ATOM   225  C  CA  . HIS   A 1 31  ? -3.656  7.814   26.169  1.00 35.00 ? 72  HIS   A CA  1 
ATOM   226  C  C   . HIS   A 1 31  ? -3.819  7.917   24.659  1.00 34.60 ? 72  HIS   A C   1 
ATOM   227  O  O   . HIS   A 1 31  ? -3.271  8.850   24.063  1.00 34.14 ? 72  HIS   A O   1 
ATOM   228  C  CB  . HIS   A 1 31  ? -2.226  7.356   26.505  1.00 34.60 ? 72  HIS   A CB  1 
ATOM   229  C  CG  . HIS   A 1 31  ? -1.680  6.309   25.585  1.00 36.98 ? 72  HIS   A CG  1 
ATOM   230  N  ND1 . HIS   A 1 31  ? -1.207  6.600   24.324  1.00 35.77 ? 72  HIS   A ND1 1 
ATOM   231  C  CD2 . HIS   A 1 31  ? -1.508  4.977   25.754  1.00 36.07 ? 72  HIS   A CD2 1 
ATOM   232  C  CE1 . HIS   A 1 31  ? -0.781  5.490   23.749  1.00 40.28 ? 72  HIS   A CE1 1 
ATOM   233  N  NE2 . HIS   A 1 31  ? -0.951  4.490   24.597  1.00 37.08 ? 72  HIS   A NE2 1 
ATOM   234  N  N   . ALA   A 1 32  ? -4.558  7.003   24.025  1.00 30.70 ? 73  ALA   A N   1 
ATOM   235  C  CA  . ALA   A 1 32  ? -4.712  7.023   22.577  1.00 31.91 ? 73  ALA   A CA  1 
ATOM   236  C  C   . ALA   A 1 32  ? -6.097  7.452   22.108  1.00 28.60 ? 73  ALA   A C   1 
ATOM   237  O  O   . ALA   A 1 32  ? -6.290  7.636   20.901  1.00 27.75 ? 73  ALA   A O   1 
ATOM   238  C  CB  . ALA   A 1 32  ? -4.386  5.645   21.987  1.00 33.03 ? 73  ALA   A CB  1 
ATOM   239  N  N   . CYS   A 1 33  ? -7.057  7.618   23.013  1.00 28.40 ? 74  CYS   A N   1 
ATOM   240  C  CA  . CYS   A 1 33  ? -8.412  8.031   22.668  1.00 30.74 ? 74  CYS   A CA  1 
ATOM   241  C  C   . CYS   A 1 33  ? -8.802  9.224   23.531  1.00 31.73 ? 74  CYS   A C   1 
ATOM   242  O  O   . CYS   A 1 33  ? -8.133  9.552   24.514  1.00 34.44 ? 74  CYS   A O   1 
ATOM   243  C  CB  . CYS   A 1 33  ? -9.419  6.890   22.876  1.00 30.27 ? 74  CYS   A CB  1 
ATOM   244  S  SG  . CYS   A 1 33  ? -9.026  5.362   21.983  1.00 26.49 ? 74  CYS   A SG  1 
ATOM   245  N  N   . VAL   A 1 34  ? -9.902  9.874   23.159  1.00 30.91 ? 75  VAL   A N   1 
ATOM   246  C  CA  . VAL   A 1 34  ? -10.484 10.933  23.982  1.00 29.82 ? 75  VAL   A CA  1 
ATOM   247  C  C   . VAL   A 1 34  ? -11.675 10.340  24.728  1.00 32.07 ? 75  VAL   A C   1 
ATOM   248  O  O   . VAL   A 1 34  ? -12.058 9.192   24.457  1.00 32.13 ? 75  VAL   A O   1 
ATOM   249  C  CB  . VAL   A 1 34  ? -10.900 12.147  23.134  1.00 36.13 ? 75  VAL   A CB  1 
ATOM   250  C  CG1 . VAL   A 1 34  ? -9.705  12.691  22.363  1.00 30.42 ? 75  VAL   A CG1 1 
ATOM   251  C  CG2 . VAL   A 1 34  ? -12.033 11.791  22.192  1.00 28.37 ? 75  VAL   A CG2 1 
ATOM   252  N  N   . PRO   A 1 35  ? -12.268 11.051  25.683  1.00 34.60 ? 76  PRO   A N   1 
ATOM   253  C  CA  . PRO   A 1 35  ? -13.476 10.536  26.334  1.00 35.23 ? 76  PRO   A CA  1 
ATOM   254  C  C   . PRO   A 1 35  ? -14.628 10.472  25.344  1.00 32.62 ? 76  PRO   A C   1 
ATOM   255  O  O   . PRO   A 1 35  ? -14.686 11.233  24.373  1.00 33.04 ? 76  PRO   A O   1 
ATOM   256  C  CB  . PRO   A 1 35  ? -13.746 11.565  27.438  1.00 35.74 ? 76  PRO   A CB  1 
ATOM   257  C  CG  . PRO   A 1 35  ? -12.416 12.206  27.689  1.00 36.67 ? 76  PRO   A CG  1 
ATOM   258  C  CD  . PRO   A 1 35  ? -11.771 12.274  26.337  1.00 33.95 ? 76  PRO   A CD  1 
ATOM   259  N  N   . THR   A 1 36  ? -15.548 9.540   25.585  1.00 33.24 ? 77  THR   A N   1 
ATOM   260  C  CA  . THR   A 1 36  ? -16.680 9.397   24.680  1.00 35.25 ? 77  THR   A CA  1 
ATOM   261  C  C   . THR   A 1 36  ? -17.560 10.639  24.717  1.00 38.98 ? 77  THR   A C   1 
ATOM   262  O  O   . THR   A 1 36  ? -17.723 11.290  25.751  1.00 37.87 ? 77  THR   A O   1 
ATOM   263  C  CB  . THR   A 1 36  ? -17.518 8.160   25.017  1.00 34.81 ? 77  THR   A CB  1 
ATOM   264  O  OG1 . THR   A 1 36  ? -18.195 8.361   26.263  1.00 41.03 ? 77  THR   A OG1 1 
ATOM   265  C  CG2 . THR   A 1 36  ? -16.644 6.922   25.095  1.00 29.68 ? 77  THR   A CG2 1 
ATOM   266  N  N   . ASP   A 1 37  ? -18.136 10.952  23.567  1.00 41.11 ? 78  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 37  ? -19.046 12.076  23.417  1.00 42.85 ? 78  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 37  ? -20.150 11.960  24.463  1.00 42.35 ? 78  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 37  ? -20.955 11.027  24.408  1.00 40.20 ? 78  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 37  ? -19.627 12.110  22.000  1.00 41.15 ? 78  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 37  ? -20.448 13.349  21.734  1.00 45.68 ? 78  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 37  ? -20.788 14.074  22.695  1.00 45.60 ? 78  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 37  ? -20.765 13.588  20.551  1.00 51.51 ? 78  ASP   A OD2 1 
ATOM   274  N  N   . PRO   A 1 38  ? -20.226 12.874  25.430  1.00 42.61 ? 79  PRO   A N   1 
ATOM   275  C  CA  . PRO   A 1 38  ? -21.302 12.783  26.430  1.00 44.64 ? 79  PRO   A CA  1 
ATOM   276  C  C   . PRO   A 1 38  ? -22.681 13.070  25.857  1.00 48.05 ? 79  PRO   A C   1 
ATOM   277  O  O   . PRO   A 1 38  ? -23.683 12.729  26.501  1.00 49.31 ? 79  PRO   A O   1 
ATOM   278  C  CB  . PRO   A 1 38  ? -20.897 13.832  27.476  1.00 45.59 ? 79  PRO   A CB  1 
ATOM   279  C  CG  . PRO   A 1 38  ? -20.079 14.821  26.715  1.00 43.47 ? 79  PRO   A CG  1 
ATOM   280  C  CD  . PRO   A 1 38  ? -19.349 14.034  25.658  1.00 43.68 ? 79  PRO   A CD  1 
ATOM   281  N  N   . ASN   A 1 39  ? -22.760 13.651  24.655  1.00 47.30 ? 80  ASN   A N   1 
ATOM   282  C  CA  . ASN   A 1 39  ? -24.015 14.138  24.075  1.00 49.48 ? 80  ASN   A CA  1 
ATOM   283  C  C   . ASN   A 1 39  ? -24.108 13.727  22.608  1.00 45.64 ? 80  ASN   A C   1 
ATOM   284  O  O   . ASN   A 1 39  ? -24.215 14.572  21.718  1.00 43.09 ? 80  ASN   A O   1 
ATOM   285  C  CB  . ASN   A 1 39  ? -24.113 15.659  24.223  1.00 51.34 ? 80  ASN   A CB  1 
ATOM   286  C  CG  . ASN   A 1 39  ? -25.512 16.183  23.992  1.00 54.45 ? 80  ASN   A CG  1 
ATOM   287  O  OD1 . ASN   A 1 39  ? -26.489 15.436  24.045  1.00 55.90 ? 80  ASN   A OD1 1 
ATOM   288  N  ND2 . ASN   A 1 39  ? -25.612 17.473  23.699  1.00 55.91 ? 80  ASN   A ND2 1 
ATOM   289  N  N   . PRO   A 1 40  ? -24.101 12.426  22.321  1.00 46.44 ? 81  PRO   A N   1 
ATOM   290  C  CA  . PRO   A 1 40  ? -24.043 11.994  20.915  1.00 42.10 ? 81  PRO   A CA  1 
ATOM   291  C  C   . PRO   A 1 40  ? -25.327 12.313  20.162  1.00 44.60 ? 81  PRO   A C   1 
ATOM   292  O  O   . PRO   A 1 40  ? -26.430 12.045  20.646  1.00 44.32 ? 81  PRO   A O   1 
ATOM   293  C  CB  . PRO   A 1 40  ? -23.804 10.485  21.021  1.00 43.07 ? 81  PRO   A CB  1 
ATOM   294  C  CG  . PRO   A 1 40  ? -24.436 10.115  22.327  1.00 42.67 ? 81  PRO   A CG  1 
ATOM   295  C  CD  . PRO   A 1 40  ? -24.134 11.278  23.243  1.00 45.05 ? 81  PRO   A CD  1 
ATOM   296  N  N   . GLN   A 1 41  ? -25.172 12.887  18.965  1.00 39.53 ? 82  GLN   A N   1 
ATOM   297  C  CA  . GLN   A 1 41  ? -26.281 13.267  18.099  1.00 43.25 ? 82  GLN   A CA  1 
ATOM   298  C  C   . GLN   A 1 41  ? -26.336 12.333  16.893  1.00 40.55 ? 82  GLN   A C   1 
ATOM   299  O  O   . GLN   A 1 41  ? -25.299 12.017  16.300  1.00 36.18 ? 82  GLN   A O   1 
ATOM   300  C  CB  . GLN   A 1 41  ? -26.122 14.706  17.586  1.00 46.63 ? 82  GLN   A CB  1 
ATOM   301  C  CG  . GLN   A 1 41  ? -26.118 15.836  18.623  1.00 51.41 ? 82  GLN   A CG  1 
ATOM   302  C  CD  . GLN   A 1 41  ? -27.105 15.659  19.756  1.00 56.86 ? 82  GLN   A CD  1 
ATOM   303  O  OE1 . GLN   A 1 41  ? -28.239 15.226  19.552  1.00 57.49 ? 82  GLN   A OE1 1 
ATOM   304  N  NE2 . GLN   A 1 41  ? -26.679 16.014  20.964  1.00 57.06 ? 82  GLN   A NE2 1 
ATOM   305  N  N   . GLU   A 1 42  ? -27.543 11.900  16.525  1.00 39.47 ? 83  GLU   A N   1 
ATOM   306  C  CA  . GLU   A 1 42  ? -27.772 11.133  15.301  1.00 38.04 ? 83  GLU   A CA  1 
ATOM   307  C  C   . GLU   A 1 42  ? -28.806 11.864  14.455  1.00 40.13 ? 83  GLU   A C   1 
ATOM   308  O  O   . GLU   A 1 42  ? -29.916 12.131  14.927  1.00 39.86 ? 83  GLU   A O   1 
ATOM   309  C  CB  . GLU   A 1 42  ? -28.258 9.712   15.602  1.00 36.70 ? 83  GLU   A CB  1 
ATOM   310  C  CG  . GLU   A 1 42  ? -28.249 8.791   14.387  1.00 38.73 ? 83  GLU   A CG  1 
ATOM   311  C  CD  . GLU   A 1 42  ? -28.424 7.321   14.744  1.00 40.80 ? 83  GLU   A CD  1 
ATOM   312  O  OE1 . GLU   A 1 42  ? -28.058 6.926   15.874  1.00 43.48 ? 83  GLU   A OE1 1 
ATOM   313  O  OE2 . GLU   A 1 42  ? -28.915 6.557   13.884  1.00 42.48 ? 83  GLU   A OE2 1 
ATOM   314  N  N   . ILE   A 1 43  ? -28.453 12.177  13.209  1.00 35.38 ? 84  ILE   A N   1 
ATOM   315  C  CA  . ILE   A 1 43  ? -29.344 12.891  12.298  1.00 41.10 ? 84  ILE   A CA  1 
ATOM   316  C  C   . ILE   A 1 43  ? -29.831 11.925  11.227  1.00 39.16 ? 84  ILE   A C   1 
ATOM   317  O  O   . ILE   A 1 43  ? -29.025 11.310  10.518  1.00 34.77 ? 84  ILE   A O   1 
ATOM   318  C  CB  . ILE   A 1 43  ? -28.663 14.110  11.656  1.00 37.79 ? 84  ILE   A CB  1 
ATOM   319  C  CG1 . ILE   A 1 43  ? -28.238 15.106  12.732  1.00 40.13 ? 84  ILE   A CG1 1 
ATOM   320  C  CG2 . ILE   A 1 43  ? -29.611 14.769  10.664  1.00 35.12 ? 84  ILE   A CG2 1 
ATOM   321  C  CD1 . ILE   A 1 43  ? -29.218 15.202  13.879  1.00 44.34 ? 84  ILE   A CD1 1 
ATOM   322  N  N   . HIS   A 1 44  ? -31.152 11.810  11.094  1.00 40.15 ? 85  HIS   A N   1 
ATOM   323  C  CA  . HIS   A 1 44  ? -31.746 11.012  10.031  1.00 39.39 ? 85  HIS   A CA  1 
ATOM   324  C  C   . HIS   A 1 44  ? -31.751 11.816  8.734   1.00 44.46 ? 85  HIS   A C   1 
ATOM   325  O  O   . HIS   A 1 44  ? -32.107 12.998  8.728   1.00 41.84 ? 85  HIS   A O   1 
ATOM   326  C  CB  . HIS   A 1 44  ? -33.169 10.596  10.411  1.00 44.44 ? 85  HIS   A CB  1 
ATOM   327  C  CG  . HIS   A 1 44  ? -33.943 9.976   9.290   1.00 48.40 ? 85  HIS   A CG  1 
ATOM   328  N  ND1 . HIS   A 1 44  ? -34.584 10.719  8.322   1.00 51.93 ? 85  HIS   A ND1 1 
ATOM   329  C  CD2 . HIS   A 1 44  ? -34.191 8.679   8.993   1.00 50.99 ? 85  HIS   A CD2 1 
ATOM   330  C  CE1 . HIS   A 1 44  ? -35.182 9.905   7.470   1.00 54.47 ? 85  HIS   A CE1 1 
ATOM   331  N  NE2 . HIS   A 1 44  ? -34.959 8.661   7.854   1.00 53.47 ? 85  HIS   A NE2 1 
ATOM   332  N  N   . LEU   A 1 45  ? -31.359 11.176  7.636   1.00 39.56 ? 86  LEU   A N   1 
ATOM   333  C  CA  . LEU   A 1 45  ? -31.233 11.840  6.339   1.00 42.48 ? 86  LEU   A CA  1 
ATOM   334  C  C   . LEU   A 1 45  ? -32.496 11.582  5.526   1.00 45.15 ? 86  LEU   A C   1 
ATOM   335  O  O   . LEU   A 1 45  ? -32.670 10.507  4.945   1.00 45.08 ? 86  LEU   A O   1 
ATOM   336  C  CB  . LEU   A 1 45  ? -29.978 11.366  5.612   1.00 40.65 ? 86  LEU   A CB  1 
ATOM   337  C  CG  . LEU   A 1 45  ? -28.671 11.658  6.357   1.00 42.36 ? 86  LEU   A CG  1 
ATOM   338  C  CD1 . LEU   A 1 45  ? -27.457 11.249  5.533   1.00 37.24 ? 86  LEU   A CD1 1 
ATOM   339  C  CD2 . LEU   A 1 45  ? -28.598 13.130  6.735   1.00 39.56 ? 86  LEU   A CD2 1 
ATOM   340  N  N   . GLU   A 1 46  ? -33.366 12.589  5.470   1.00 46.36 ? 87  GLU   A N   1 
ATOM   341  C  CA  . GLU   A 1 46  ? -34.660 12.462  4.807   1.00 51.18 ? 87  GLU   A CA  1 
ATOM   342  C  C   . GLU   A 1 46  ? -34.503 12.095  3.335   1.00 48.38 ? 87  GLU   A C   1 
ATOM   343  O  O   . GLU   A 1 46  ? -33.870 12.824  2.567   1.00 45.67 ? 87  GLU   A O   1 
ATOM   344  C  CB  . GLU   A 1 46  ? -35.440 13.771  4.951   1.00 50.70 ? 87  GLU   A CB  1 
ATOM   345  C  CG  . GLU   A 1 46  ? -36.135 13.961  6.300   1.00 55.42 ? 87  GLU   A CG  1 
ATOM   346  C  CD  . GLU   A 1 46  ? -36.715 12.672  6.856   1.00 56.96 ? 87  GLU   A CD  1 
ATOM   347  O  OE1 . GLU   A 1 46  ? -37.125 11.809  6.051   1.00 56.45 ? 87  GLU   A OE1 1 
ATOM   348  O  OE2 . GLU   A 1 46  ? -36.765 12.524  8.096   1.00 59.75 ? 87  GLU   A OE2 1 
ATOM   349  N  N   . ASN   A 1 47  ? -35.090 10.956  2.950   1.00 51.37 ? 88  ASN   A N   1 
ATOM   350  C  CA  . ASN   A 1 47  ? -35.164 10.498  1.556   1.00 50.99 ? 88  ASN   A CA  1 
ATOM   351  C  C   . ASN   A 1 47  ? -33.802 10.206  0.942   1.00 52.73 ? 88  ASN   A C   1 
ATOM   352  O  O   . ASN   A 1 47  ? -33.644 10.263  -0.280  1.00 49.72 ? 88  ASN   A O   1 
ATOM   353  C  CB  . ASN   A 1 47  ? -35.916 11.490  0.666   1.00 55.26 ? 88  ASN   A CB  1 
ATOM   354  C  CG  . ASN   A 1 47  ? -36.970 10.811  -0.189  1.00 60.40 ? 88  ASN   A CG  1 
ATOM   355  O  OD1 . ASN   A 1 47  ? -37.577 9.822   0.225   1.00 64.10 ? 88  ASN   A OD1 1 
ATOM   356  N  ND2 . ASN   A 1 47  ? -37.157 11.308  -1.409  1.00 63.31 ? 88  ASN   A ND2 1 
ATOM   357  N  N   . VAL   A 1 48  ? -32.807 9.873   1.753   1.00 45.65 ? 89  VAL   A N   1 
ATOM   358  C  CA  . VAL   A 1 48  ? -31.472 9.595   1.245   1.00 47.02 ? 89  VAL   A CA  1 
ATOM   359  C  C   . VAL   A 1 48  ? -31.303 8.095   1.082   1.00 44.29 ? 89  VAL   A C   1 
ATOM   360  O  O   . VAL   A 1 48  ? -31.620 7.319   1.991   1.00 44.75 ? 89  VAL   A O   1 
ATOM   361  C  CB  . VAL   A 1 48  ? -30.384 10.177  2.160   1.00 45.40 ? 89  VAL   A CB  1 
ATOM   362  C  CG1 . VAL   A 1 48  ? -29.017 9.660   1.740   1.00 41.15 ? 89  VAL   A CG1 1 
ATOM   363  C  CG2 . VAL   A 1 48  ? -30.421 11.696  2.106   1.00 43.77 ? 89  VAL   A CG2 1 
ATOM   364  N  N   . THR   A 1 49  ? -30.825 7.692   -0.088  1.00 47.09 ? 90  THR   A N   1 
ATOM   365  C  CA  . THR   A 1 49  ? -30.367 6.337   -0.344  1.00 43.71 ? 90  THR   A CA  1 
ATOM   366  C  C   . THR   A 1 49  ? -28.865 6.400   -0.578  1.00 43.57 ? 90  THR   A C   1 
ATOM   367  O  O   . THR   A 1 49  ? -28.389 7.256   -1.332  1.00 44.43 ? 90  THR   A O   1 
ATOM   368  C  CB  . THR   A 1 49  ? -31.082 5.735   -1.557  1.00 43.43 ? 90  THR   A CB  1 
ATOM   369  O  OG1 . THR   A 1 49  ? -32.467 5.533   -1.246  1.00 47.47 ? 90  THR   A OG1 1 
ATOM   370  C  CG2 . THR   A 1 49  ? -30.459 4.395   -1.934  1.00 43.68 ? 90  THR   A CG2 1 
ATOM   371  N  N   . GLU   A 1 50  ? -28.118 5.518   0.080   1.00 41.20 ? 91  GLU   A N   1 
ATOM   372  C  CA  . GLU   A 1 50  ? -26.668 5.577   0.021   1.00 40.40 ? 91  GLU   A CA  1 
ATOM   373  C  C   . GLU   A 1 50  ? -26.118 4.169   -0.128  1.00 41.91 ? 91  GLU   A C   1 
ATOM   374  O  O   . GLU   A 1 50  ? -26.625 3.228   0.489   1.00 39.13 ? 91  GLU   A O   1 
ATOM   375  C  CB  . GLU   A 1 50  ? -26.094 6.261   1.273   1.00 41.46 ? 91  GLU   A CB  1 
ATOM   376  C  CG  . GLU   A 1 50  ? -24.579 6.419   1.282   1.00 41.43 ? 91  GLU   A CG  1 
ATOM   377  C  CD  . GLU   A 1 50  ? -24.108 7.641   0.505   1.00 42.89 ? 91  GLU   A CD  1 
ATOM   378  O  OE1 . GLU   A 1 50  ? -24.906 8.591   0.343   1.00 45.45 ? 91  GLU   A OE1 1 
ATOM   379  O  OE2 . GLU   A 1 50  ? -22.935 7.650   0.071   1.00 45.34 ? 91  GLU   A OE2 1 
ATOM   380  N  N   . ASN   A 1 51  ? -25.083 4.033   -0.954  1.00 42.13 ? 92  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? -24.441 2.747   -1.188  1.00 41.32 ? 92  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? -23.365 2.498   -0.144  1.00 39.08 ? 92  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? -22.566 3.388   0.157   1.00 39.78 ? 92  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? -23.832 2.683   -2.591  1.00 45.15 ? 92  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? -24.875 2.466   -3.674  1.00 48.56 ? 92  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? -26.017 2.909   -3.556  1.00 53.04 ? 92  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? -24.483 1.766   -4.735  1.00 50.84 ? 92  ASN   A ND2 1 
ATOM   388  N  N   . PHE   A 1 52  ? -23.345 1.282   0.397   1.00 36.44 ? 93  PHE   A N   1 
ATOM   389  C  CA  . PHE   A 1 52  ? -22.326 0.848   1.335   1.00 34.92 ? 93  PHE   A CA  1 
ATOM   390  C  C   . PHE   A 1 52  ? -21.607 -0.370  0.772   1.00 34.45 ? 93  PHE   A C   1 
ATOM   391  O  O   . PHE   A 1 52  ? -22.146 -1.106  -0.059  1.00 36.57 ? 93  PHE   A O   1 
ATOM   392  C  CB  . PHE   A 1 52  ? -22.930 0.497   2.702   1.00 31.14 ? 93  PHE   A CB  1 
ATOM   393  C  CG  . PHE   A 1 52  ? -23.406 1.688   3.487   1.00 32.86 ? 93  PHE   A CG  1 
ATOM   394  C  CD1 . PHE   A 1 52  ? -24.579 2.339   3.137   1.00 35.11 ? 93  PHE   A CD1 1 
ATOM   395  C  CD2 . PHE   A 1 52  ? -22.687 2.152   4.577   1.00 31.60 ? 93  PHE   A CD2 1 
ATOM   396  C  CE1 . PHE   A 1 52  ? -25.025 3.428   3.856   1.00 31.67 ? 93  PHE   A CE1 1 
ATOM   397  C  CE2 . PHE   A 1 52  ? -23.127 3.244   5.300   1.00 30.81 ? 93  PHE   A CE2 1 
ATOM   398  C  CZ  . PHE   A 1 52  ? -24.301 3.881   4.940   1.00 30.82 ? 93  PHE   A CZ  1 
ATOM   399  N  N   . ASN   A 1 53  ? -20.378 -0.581  1.243   1.00 33.53 ? 94  ASN   A N   1 
ATOM   400  C  CA  . ASN   A 1 53  ? -19.625 -1.785  0.901   1.00 34.29 ? 94  ASN   A CA  1 
ATOM   401  C  C   . ASN   A 1 53  ? -18.729 -2.109  2.094   1.00 31.23 ? 94  ASN   A C   1 
ATOM   402  O  O   . ASN   A 1 53  ? -17.629 -1.562  2.217   1.00 28.49 ? 94  ASN   A O   1 
ATOM   403  C  CB  . ASN   A 1 53  ? -18.820 -1.599  -0.378  1.00 34.88 ? 94  ASN   A CB  1 
ATOM   404  C  CG  . ASN   A 1 53  ? -18.116 -2.873  -0.813  1.00 36.51 ? 94  ASN   A CG  1 
ATOM   405  O  OD1 . ASN   A 1 53  ? -18.018 -3.839  -0.052  1.00 34.41 ? 94  ASN   A OD1 1 
ATOM   406  N  ND2 . ASN   A 1 53  ? -17.620 -2.880  -2.046  1.00 39.49 ? 94  ASN   A ND2 1 
ATOM   407  N  N   . MET   A 1 54  ? -19.206 -3.001  2.966   1.00 31.78 ? 95  MET   A N   1 
ATOM   408  C  CA  . MET   A 1 54  ? -18.450 -3.361  4.161   1.00 30.97 ? 95  MET   A CA  1 
ATOM   409  C  C   . MET   A 1 54  ? -17.119 -4.015  3.828   1.00 29.77 ? 95  MET   A C   1 
ATOM   410  O  O   . MET   A 1 54  ? -16.203 -3.996  4.655   1.00 27.83 ? 95  MET   A O   1 
ATOM   411  C  CB  . MET   A 1 54  ? -19.283 -4.302  5.031   1.00 28.17 ? 95  MET   A CB  1 
ATOM   412  C  CG  . MET   A 1 54  ? -19.471 -5.680  4.416   1.00 28.55 ? 95  MET   A CG  1 
ATOM   413  S  SD  . MET   A 1 54  ? -20.371 -6.821  5.497   1.00 28.35 ? 95  MET   A SD  1 
ATOM   414  C  CE  . MET   A 1 54  ? -19.034 -7.352  6.586   1.00 26.02 ? 95  MET   A CE  1 
ATOM   415  N  N   . TRP   A 1 55  ? -16.996 -4.608  2.645   1.00 28.46 ? 96  TRP   A N   1 
ATOM   416  C  CA  . TRP   A 1 55  ? -15.786 -5.328  2.279   1.00 32.12 ? 96  TRP   A CA  1 
ATOM   417  C  C   . TRP   A 1 55  ? -14.694 -4.416  1.742   1.00 35.41 ? 96  TRP   A C   1 
ATOM   418  O  O   . TRP   A 1 55  ? -13.541 -4.850  1.653   1.00 35.53 ? 96  TRP   A O   1 
ATOM   419  C  CB  . TRP   A 1 55  ? -16.149 -6.422  1.273   1.00 31.51 ? 96  TRP   A CB  1 
ATOM   420  C  CG  . TRP   A 1 55  ? -17.137 -7.358  1.874   1.00 30.57 ? 96  TRP   A CG  1 
ATOM   421  C  CD1 . TRP   A 1 55  ? -18.492 -7.357  1.698   1.00 29.04 ? 96  TRP   A CD1 1 
ATOM   422  C  CD2 . TRP   A 1 55  ? -16.855 -8.403  2.806   1.00 28.60 ? 96  TRP   A CD2 1 
ATOM   423  N  NE1 . TRP   A 1 55  ? -19.066 -8.352  2.449   1.00 30.69 ? 96  TRP   A NE1 1 
ATOM   424  C  CE2 . TRP   A 1 55  ? -18.081 -9.011  3.137   1.00 29.60 ? 96  TRP   A CE2 1 
ATOM   425  C  CE3 . TRP   A 1 55  ? -15.680 -8.893  3.380   1.00 30.64 ? 96  TRP   A CE3 1 
ATOM   426  C  CZ2 . TRP   A 1 55  ? -18.166 -10.080 4.024   1.00 30.33 ? 96  TRP   A CZ2 1 
ATOM   427  C  CZ3 . TRP   A 1 55  ? -15.766 -9.955  4.259   1.00 33.56 ? 96  TRP   A CZ3 1 
ATOM   428  C  CH2 . TRP   A 1 55  ? -16.998 -10.538 4.572   1.00 31.82 ? 96  TRP   A CH2 1 
ATOM   429  N  N   . LYS   A 1 56  ? -15.022 -3.162  1.416   1.00 32.46 ? 97  LYS   A N   1 
ATOM   430  C  CA  . LYS   A 1 56  ? -14.054 -2.159  0.969   1.00 36.05 ? 97  LYS   A CA  1 
ATOM   431  C  C   . LYS   A 1 56  ? -14.316 -0.902  1.797   1.00 33.21 ? 97  LYS   A C   1 
ATOM   432  O  O   . LYS   A 1 56  ? -14.936 0.051   1.324   1.00 34.59 ? 97  LYS   A O   1 
ATOM   433  C  CB  . LYS   A 1 56  ? -14.192 -1.902  -0.524  1.00 40.33 ? 97  LYS   A CB  1 
ATOM   434  C  CG  . LYS   A 1 56  ? -14.191 -3.156  -1.389  1.00 42.38 ? 97  LYS   A CG  1 
ATOM   435  C  CD  . LYS   A 1 56  ? -12.885 -3.339  -2.135  1.00 47.41 ? 97  LYS   A CD  1 
ATOM   436  C  CE  . LYS   A 1 56  ? -11.903 -4.180  -1.333  1.00 52.18 ? 97  LYS   A CE  1 
ATOM   437  N  NZ  . LYS   A 1 56  ? -10.809 -4.702  -2.196  1.00 55.08 ? 97  LYS   A NZ  1 
ATOM   438  N  N   . ASN   A 1 57  ? -13.848 -0.902  3.043   1.00 30.89 ? 98  ASN   A N   1 
ATOM   439  C  CA  . ASN   A 1 57  ? -14.198 0.155   3.989   1.00 33.84 ? 98  ASN   A CA  1 
ATOM   440  C  C   . ASN   A 1 57  ? -12.962 0.472   4.821   1.00 28.89 ? 98  ASN   A C   1 
ATOM   441  O  O   . ASN   A 1 57  ? -12.591 -0.303  5.707   1.00 28.06 ? 98  ASN   A O   1 
ATOM   442  C  CB  . ASN   A 1 57  ? -15.376 -0.272  4.871   1.00 30.61 ? 98  ASN   A CB  1 
ATOM   443  C  CG  . ASN   A 1 57  ? -15.707 0.742   5.951   1.00 32.01 ? 98  ASN   A CG  1 
ATOM   444  O  OD1 . ASN   A 1 57  ? -15.010 1.741   6.134   1.00 29.39 ? 98  ASN   A OD1 1 
ATOM   445  N  ND2 . ASN   A 1 57  ? -16.787 0.480   6.679   1.00 28.91 ? 98  ASN   A ND2 1 
ATOM   446  N  N   . ASN   A 1 58  ? -12.329 1.614   4.540   1.00 30.52 ? 99  ASN   A N   1 
ATOM   447  C  CA  . ASN   A 1 58  ? -11.082 1.969   5.203   1.00 29.52 ? 99  ASN   A CA  1 
ATOM   448  C  C   . ASN   A 1 58  ? -11.204 2.002   6.714   1.00 28.44 ? 99  ASN   A C   1 
ATOM   449  O  O   . ASN   A 1 58  ? -10.186 1.866   7.394   1.00 26.52 ? 99  ASN   A O   1 
ATOM   450  C  CB  . ASN   A 1 58  ? -10.580 3.323   4.696   1.00 30.08 ? 99  ASN   A CB  1 
ATOM   451  C  CG  . ASN   A 1 58  ? -9.185  3.645   5.189   1.00 33.05 ? 99  ASN   A CG  1 
ATOM   452  O  OD1 . ASN   A 1 58  ? -8.978  4.590   5.956   1.00 33.63 ? 99  ASN   A OD1 1 
ATOM   453  N  ND2 . ASN   A 1 58  ? -8.221  2.840   4.773   1.00 35.18 ? 99  ASN   A ND2 1 
ATOM   454  N  N   . MET   A 1 59  ? -12.412 2.195   7.257   1.00 24.70 ? 100 MET   A N   1 
ATOM   455  C  CA  . MET   A 1 59  ? -12.575 2.176   8.707   1.00 27.15 ? 100 MET   A CA  1 
ATOM   456  C  C   . MET   A 1 59  ? -12.048 0.878   9.293   1.00 27.03 ? 100 MET   A C   1 
ATOM   457  O  O   . MET   A 1 59  ? -11.473 0.868   10.386  1.00 23.16 ? 100 MET   A O   1 
ATOM   458  C  CB  . MET   A 1 59  ? -14.046 2.349   9.062   1.00 24.27 ? 100 MET   A CB  1 
ATOM   459  C  CG  . MET   A 1 59  ? -14.602 3.733   8.775   1.00 26.18 ? 100 MET   A CG  1 
ATOM   460  S  SD  . MET   A 1 59  ? -16.345 3.802   9.182   1.00 24.59 ? 100 MET   A SD  1 
ATOM   461  C  CE  . MET   A 1 59  ? -16.270 4.221   10.940  1.00 24.66 ? 100 MET   A CE  1 
ATOM   462  N  N   . VAL   A 1 60  ? -12.246 -0.231  8.579   1.00 24.58 ? 101 VAL   A N   1 
ATOM   463  C  CA  . VAL   A 1 60  ? -11.800 -1.534  9.060   1.00 22.85 ? 101 VAL   A CA  1 
ATOM   464  C  C   . VAL   A 1 60  ? -10.281 -1.566  9.152   1.00 27.33 ? 101 VAL   A C   1 
ATOM   465  O  O   . VAL   A 1 60  ? -9.708  -2.031  10.144  1.00 23.19 ? 101 VAL   A O   1 
ATOM   466  C  CB  . VAL   A 1 60  ? -12.328 -2.645  8.135   1.00 25.24 ? 101 VAL   A CB  1 
ATOM   467  C  CG1 . VAL   A 1 60  ? -11.652 -3.976  8.445   1.00 24.11 ? 101 VAL   A CG1 1 
ATOM   468  C  CG2 . VAL   A 1 60  ? -13.853 -2.760  8.250   1.00 22.44 ? 101 VAL   A CG2 1 
ATOM   469  N  N   A GLU   A 1 61  ? -9.601  -1.071  8.116   0.53 28.33 ? 102 GLU   A N   1 
ATOM   470  N  N   B GLU   A 1 61  ? -9.609  -1.072  8.110   0.47 28.08 ? 102 GLU   A N   1 
ATOM   471  C  CA  A GLU   A 1 61  ? -8.143  -1.033  8.148   0.53 30.33 ? 102 GLU   A CA  1 
ATOM   472  C  CA  B GLU   A 1 61  ? -8.151  -1.006  8.121   0.47 30.15 ? 102 GLU   A CA  1 
ATOM   473  C  C   A GLU   A 1 61  ? -7.646  -0.211  9.331   0.53 29.10 ? 102 GLU   A C   1 
ATOM   474  C  C   B GLU   A 1 61  ? -7.651  -0.207  9.317   0.47 29.11 ? 102 GLU   A C   1 
ATOM   475  O  O   A GLU   A 1 61  ? -6.666  -0.581  9.988   0.53 28.95 ? 102 GLU   A O   1 
ATOM   476  O  O   B GLU   A 1 61  ? -6.671  -0.589  9.966   0.47 29.05 ? 102 GLU   A O   1 
ATOM   477  C  CB  A GLU   A 1 61  ? -7.608  -0.454  6.837   0.53 32.25 ? 102 GLU   A CB  1 
ATOM   478  C  CB  B GLU   A 1 61  ? -7.659  -0.377  6.819   0.47 32.29 ? 102 GLU   A CB  1 
ATOM   479  C  CG  A GLU   A 1 61  ? -7.940  -1.273  5.594   0.53 34.59 ? 102 GLU   A CG  1 
ATOM   480  C  CG  B GLU   A 1 61  ? -7.083  -1.363  5.817   0.47 35.57 ? 102 GLU   A CG  1 
ATOM   481  C  CD  A GLU   A 1 61  ? -7.392  -2.691  5.649   0.53 37.06 ? 102 GLU   A CD  1 
ATOM   482  C  CD  B GLU   A 1 61  ? -8.109  -2.380  5.353   0.47 37.09 ? 102 GLU   A CD  1 
ATOM   483  O  OE1 A GLU   A 1 61  ? -6.470  -2.953  6.455   0.53 38.74 ? 102 GLU   A OE1 1 
ATOM   484  O  OE1 B GLU   A 1 61  ? -9.305  -2.024  5.257   0.47 39.21 ? 102 GLU   A OE1 1 
ATOM   485  O  OE2 A GLU   A 1 61  ? -7.885  -3.543  4.880   0.53 39.98 ? 102 GLU   A OE2 1 
ATOM   486  O  OE2 B GLU   A 1 61  ? -7.716  -3.532  5.075   0.47 39.55 ? 102 GLU   A OE2 1 
ATOM   487  N  N   . GLN   A 1 62  ? -8.320  0.905   9.628   1.00 30.00 ? 103 GLN   A N   1 
ATOM   488  C  CA  . GLN   A 1 62  ? -7.870  1.775   10.709  1.00 27.12 ? 103 GLN   A CA  1 
ATOM   489  C  C   . GLN   A 1 62  ? -8.071  1.127   12.071  1.00 28.09 ? 103 GLN   A C   1 
ATOM   490  O  O   . GLN   A 1 62  ? -7.220  1.261   12.958  1.00 25.44 ? 103 GLN   A O   1 
ATOM   491  C  CB  . GLN   A 1 62  ? -8.602  3.113   10.628  1.00 29.07 ? 103 GLN   A CB  1 
ATOM   492  C  CG  . GLN   A 1 62  ? -8.235  3.914   9.397   1.00 27.04 ? 103 GLN   A CG  1 
ATOM   493  C  CD  . GLN   A 1 62  ? -8.592  5.381   9.535   1.00 29.77 ? 103 GLN   A CD  1 
ATOM   494  O  OE1 . GLN   A 1 62  ? -8.288  6.015   10.545  1.00 25.36 ? 103 GLN   A OE1 1 
ATOM   495  N  NE2 . GLN   A 1 62  ? -9.230  5.930   8.512   1.00 31.61 ? 103 GLN   A NE2 1 
ATOM   496  N  N   . MET   A 1 63  ? -9.199  0.444   12.275  1.00 23.89 ? 104 MET   A N   1 
ATOM   497  C  CA  . MET   A 1 63  ? -9.375  -0.277  13.531  1.00 25.35 ? 104 MET   A CA  1 
ATOM   498  C  C   . MET   A 1 63  ? -8.316  -1.368  13.665  1.00 23.05 ? 104 MET   A C   1 
ATOM   499  O  O   . MET   A 1 63  ? -7.767  -1.595  14.749  1.00 22.82 ? 104 MET   A O   1 
ATOM   500  C  CB  . MET   A 1 63  ? -10.762 -0.917  13.601  1.00 21.82 ? 104 MET   A CB  1 
ATOM   501  C  CG  . MET   A 1 63  ? -11.005 -1.622  14.927  1.00 22.78 ? 104 MET   A CG  1 
ATOM   502  S  SD  . MET   A 1 63  ? -12.737 -1.891  15.318  1.00 22.83 ? 104 MET   A SD  1 
ATOM   503  C  CE  . MET   A 1 63  ? -12.607 -2.943  16.752  1.00 25.35 ? 104 MET   A CE  1 
ATOM   504  N  N   . HIS   A 1 64  ? -8.028  -2.067  12.568  1.00 23.42 ? 105 HIS   A N   1 
ATOM   505  C  CA  . HIS   A 1 64  ? -6.990  -3.091  12.588  1.00 27.56 ? 105 HIS   A CA  1 
ATOM   506  C  C   . HIS   A 1 64  ? -5.679  -2.508  13.098  1.00 25.58 ? 105 HIS   A C   1 
ATOM   507  O  O   . HIS   A 1 64  ? -5.065  -3.037  14.029  1.00 24.35 ? 105 HIS   A O   1 
ATOM   508  C  CB  . HIS   A 1 64  ? -6.821  -3.678  11.183  1.00 25.13 ? 105 HIS   A CB  1 
ATOM   509  C  CG  . HIS   A 1 64  ? -6.159  -5.020  11.156  1.00 27.70 ? 105 HIS   A CG  1 
ATOM   510  N  ND1 . HIS   A 1 64  ? -6.580  -6.074  11.939  1.00 27.37 ? 105 HIS   A ND1 1 
ATOM   511  C  CD2 . HIS   A 1 64  ? -5.114  -5.484  10.429  1.00 29.05 ? 105 HIS   A CD2 1 
ATOM   512  C  CE1 . HIS   A 1 64  ? -5.816  -7.126  11.703  1.00 33.74 ? 105 HIS   A CE1 1 
ATOM   513  N  NE2 . HIS   A 1 64  ? -4.918  -6.795  10.790  1.00 30.77 ? 105 HIS   A NE2 1 
ATOM   514  N  N   . GLU   A 1 65  ? -5.250  -1.392  12.509  1.00 26.89 ? 106 GLU   A N   1 
ATOM   515  C  CA  . GLU   A 1 65  ? -4.006  -0.761  12.937  1.00 26.95 ? 106 GLU   A CA  1 
ATOM   516  C  C   . GLU   A 1 65  ? -4.046  -0.402  14.421  1.00 27.65 ? 106 GLU   A C   1 
ATOM   517  O  O   . GLU   A 1 65  ? -3.051  -0.578  15.135  1.00 28.33 ? 106 GLU   A O   1 
ATOM   518  C  CB  . GLU   A 1 65  ? -3.724  0.460   12.054  1.00 30.06 ? 106 GLU   A CB  1 
ATOM   519  C  CG  . GLU   A 1 65  ? -3.620  0.095   10.561  1.00 36.14 ? 106 GLU   A CG  1 
ATOM   520  C  CD  . GLU   A 1 65  ? -3.799  1.271   9.601   1.00 44.64 ? 106 GLU   A CD  1 
ATOM   521  O  OE1 . GLU   A 1 65  ? -4.205  2.369   10.041  1.00 42.08 ? 106 GLU   A OE1 1 
ATOM   522  O  OE2 . GLU   A 1 65  ? -3.535  1.087   8.391   1.00 46.25 ? 106 GLU   A OE2 1 
ATOM   523  N  N   . ASP   A 1 66  ? -5.196  0.063   14.916  1.00 24.61 ? 107 ASP   A N   1 
ATOM   524  C  CA  . ASP   A 1 66  ? -5.314  0.386   16.337  1.00 25.75 ? 107 ASP   A CA  1 
ATOM   525  C  C   . ASP   A 1 66  ? -5.108  -0.840  17.217  1.00 28.36 ? 107 ASP   A C   1 
ATOM   526  O  O   . ASP   A 1 66  ? -4.352  -0.795  18.195  1.00 25.79 ? 107 ASP   A O   1 
ATOM   527  C  CB  . ASP   A 1 66  ? -6.673  1.029   16.629  1.00 27.58 ? 107 ASP   A CB  1 
ATOM   528  C  CG  . ASP   A 1 66  ? -6.704  2.517   16.322  1.00 30.04 ? 107 ASP   A CG  1 
ATOM   529  O  OD1 . ASP   A 1 66  ? -5.643  3.077   15.965  1.00 27.87 ? 107 ASP   A OD1 1 
ATOM   530  O  OD2 . ASP   A 1 66  ? -7.791  3.124   16.457  1.00 30.70 ? 107 ASP   A OD2 1 
ATOM   531  N  N   . ILE   A 1 67  ? -5.797  -1.942  16.910  1.00 26.15 ? 108 ILE   A N   1 
ATOM   532  C  CA  . ILE   A 1 67  ? -5.736  -3.097  17.801  1.00 25.24 ? 108 ILE   A CA  1 
ATOM   533  C  C   . ILE   A 1 67  ? -4.357  -3.740  17.761  1.00 26.33 ? 108 ILE   A C   1 
ATOM   534  O  O   . ILE   A 1 67  ? -3.861  -4.227  18.780  1.00 29.47 ? 108 ILE   A O   1 
ATOM   535  C  CB  . ILE   A 1 67  ? -6.854  -4.107  17.476  1.00 25.08 ? 108 ILE   A CB  1 
ATOM   536  C  CG1 . ILE   A 1 67  ? -8.192  -3.378  17.331  1.00 26.04 ? 108 ILE   A CG1 1 
ATOM   537  C  CG2 . ILE   A 1 67  ? -6.931  -5.175  18.563  1.00 23.62 ? 108 ILE   A CG2 1 
ATOM   538  C  CD1 . ILE   A 1 67  ? -8.463  -2.415  18.472  1.00 23.59 ? 108 ILE   A CD1 1 
ATOM   539  N  N   . ILE   A 1 68  ? -3.719  -3.772  16.593  1.00 26.65 ? 109 ILE   A N   1 
ATOM   540  C  CA  . ILE   A 1 68  ? -2.330  -4.226  16.544  1.00 32.45 ? 109 ILE   A CA  1 
ATOM   541  C  C   . ILE   A 1 68  ? -1.479  -3.395  17.493  1.00 33.36 ? 109 ILE   A C   1 
ATOM   542  O  O   . ILE   A 1 68  ? -0.706  -3.932  18.296  1.00 33.90 ? 109 ILE   A O   1 
ATOM   543  C  CB  . ILE   A 1 68  ? -1.785  -4.175  15.105  1.00 31.19 ? 109 ILE   A CB  1 
ATOM   544  C  CG1 . ILE   A 1 68  ? -2.468  -5.227  14.225  1.00 28.93 ? 109 ILE   A CG1 1 
ATOM   545  C  CG2 . ILE   A 1 68  ? -0.270  -4.380  15.108  1.00 32.83 ? 109 ILE   A CG2 1 
ATOM   546  C  CD1 . ILE   A 1 68  ? -2.128  -5.094  12.754  1.00 31.29 ? 109 ILE   A CD1 1 
ATOM   547  N  N   . SER   A 1 69  ? -1.624  -2.069  17.426  1.00 32.79 ? 110 SER   A N   1 
ATOM   548  C  CA  . SER   A 1 69  ? -0.912  -1.187  18.346  1.00 34.87 ? 110 SER   A CA  1 
ATOM   549  C  C   . SER   A 1 69  ? -1.256  -1.504  19.791  1.00 35.20 ? 110 SER   A C   1 
ATOM   550  O  O   . SER   A 1 69  ? -0.369  -1.547  20.651  1.00 37.76 ? 110 SER   A O   1 
ATOM   551  C  CB  . SER   A 1 69  ? -1.238  0.272   18.023  1.00 32.92 ? 110 SER   A CB  1 
ATOM   552  O  OG  . SER   A 1 69  ? -0.564  1.163   18.887  1.00 38.43 ? 110 SER   A OG  1 
ATOM   553  N  N   . LEU   A 1 70  ? -2.543  -1.726  20.078  1.00 31.11 ? 111 LEU   A N   1 
ATOM   554  C  CA  . LEU   A 1 70  ? -2.968  -2.032  21.439  1.00 31.46 ? 111 LEU   A CA  1 
ATOM   555  C  C   . LEU   A 1 70  ? -2.266  -3.277  21.965  1.00 35.16 ? 111 LEU   A C   1 
ATOM   556  O  O   . LEU   A 1 70  ? -1.737  -3.284  23.082  1.00 34.90 ? 111 LEU   A O   1 
ATOM   557  C  CB  . LEU   A 1 70  ? -4.487  -2.217  21.474  1.00 31.88 ? 111 LEU   A CB  1 
ATOM   558  C  CG  . LEU   A 1 70  ? -5.206  -2.130  22.817  1.00 32.67 ? 111 LEU   A CG  1 
ATOM   559  C  CD1 . LEU   A 1 70  ? -6.666  -1.736  22.600  1.00 28.40 ? 111 LEU   A CD1 1 
ATOM   560  C  CD2 . LEU   A 1 70  ? -5.118  -3.441  23.585  1.00 31.43 ? 111 LEU   A CD2 1 
ATOM   561  N  N   . TRP   A 1 71  ? -2.266  -4.353  21.176  1.00 32.97 ? 112 TRP   A N   1 
ATOM   562  C  CA  . TRP   A 1 71  ? -1.636  -5.590  21.623  1.00 35.92 ? 112 TRP   A CA  1 
ATOM   563  C  C   . TRP   A 1 71  ? -0.122  -5.426  21.745  1.00 37.28 ? 112 TRP   A C   1 
ATOM   564  O  O   . TRP   A 1 71  ? 0.483   -5.911  22.707  1.00 38.41 ? 112 TRP   A O   1 
ATOM   565  C  CB  . TRP   A 1 71  ? -1.996  -6.726  20.664  1.00 33.25 ? 112 TRP   A CB  1 
ATOM   566  C  CG  . TRP   A 1 71  ? -3.340  -7.339  20.964  1.00 30.40 ? 112 TRP   A CG  1 
ATOM   567  C  CD1 . TRP   A 1 71  ? -4.521  -6.673  21.150  1.00 29.79 ? 112 TRP   A CD1 1 
ATOM   568  C  CD2 . TRP   A 1 71  ? -3.643  -8.733  21.098  1.00 29.22 ? 112 TRP   A CD2 1 
ATOM   569  N  NE1 . TRP   A 1 71  ? -5.535  -7.565  21.406  1.00 29.30 ? 112 TRP   A NE1 1 
ATOM   570  C  CE2 . TRP   A 1 71  ? -5.023  -8.837  21.378  1.00 29.43 ? 112 TRP   A CE2 1 
ATOM   571  C  CE3 . TRP   A 1 71  ? -2.882  -9.904  21.014  1.00 33.58 ? 112 TRP   A CE3 1 
ATOM   572  C  CZ2 . TRP   A 1 71  ? -5.657  -10.064 21.573  1.00 27.32 ? 112 TRP   A CZ2 1 
ATOM   573  C  CZ3 . TRP   A 1 71  ? -3.513  -11.124 21.210  1.00 34.95 ? 112 TRP   A CZ3 1 
ATOM   574  C  CH2 . TRP   A 1 71  ? -4.887  -11.193 21.486  1.00 30.29 ? 112 TRP   A CH2 1 
ATOM   575  N  N   . ASP   A 1 72  ? 0.505   -4.732  20.789  1.00 37.89 ? 113 ASP   A N   1 
ATOM   576  C  CA  . ASP   A 1 72  ? 1.957   -4.556  20.818  1.00 43.28 ? 113 ASP   A CA  1 
ATOM   577  C  C   . ASP   A 1 72  ? 2.422   -3.788  22.048  1.00 43.38 ? 113 ASP   A C   1 
ATOM   578  O  O   . ASP   A 1 72  ? 3.561   -3.966  22.491  1.00 45.62 ? 113 ASP   A O   1 
ATOM   579  C  CB  . ASP   A 1 72  ? 2.429   -3.844  19.548  1.00 42.84 ? 113 ASP   A CB  1 
ATOM   580  C  CG  . ASP   A 1 72  ? 2.428   -4.757  18.336  1.00 52.34 ? 113 ASP   A CG  1 
ATOM   581  O  OD1 . ASP   A 1 72  ? 2.191   -5.973  18.512  1.00 52.09 ? 113 ASP   A OD1 1 
ATOM   582  O  OD2 . ASP   A 1 72  ? 2.659   -4.261  17.215  1.00 55.80 ? 113 ASP   A OD2 1 
ATOM   583  N  N   . GLN   A 1 73  ? 1.581   -2.917  22.601  1.00 40.95 ? 114 GLN   A N   1 
ATOM   584  C  CA  . GLN   A 1 73  ? 1.944   -2.158  23.791  1.00 42.46 ? 114 GLN   A CA  1 
ATOM   585  C  C   . GLN   A 1 73  ? 1.453   -2.804  25.076  1.00 42.83 ? 114 GLN   A C   1 
ATOM   586  O  O   . GLN   A 1 73  ? 1.695   -2.257  26.153  1.00 43.89 ? 114 GLN   A O   1 
ATOM   587  C  CB  . GLN   A 1 73  ? 1.380   -0.734  23.727  1.00 40.29 ? 114 GLN   A CB  1 
ATOM   588  C  CG  . GLN   A 1 73  ? 1.747   0.086   22.513  1.00 42.42 ? 114 GLN   A CG  1 
ATOM   589  C  CD  . GLN   A 1 73  ? 0.935   1.365   22.461  1.00 39.90 ? 114 GLN   A CD  1 
ATOM   590  O  OE1 . GLN   A 1 73  ? 0.347   1.774   23.465  1.00 42.37 ? 114 GLN   A OE1 1 
ATOM   591  N  NE2 . GLN   A 1 73  ? 0.889   1.999   21.295  1.00 42.74 ? 114 GLN   A NE2 1 
ATOM   592  N  N   . SER   A 1 74  ? 0.764   -3.922  24.998  1.00 39.86 ? 115 SER   A N   1 
ATOM   593  C  CA  . SER   A 1 74  ? 0.119   -4.461  26.188  1.00 37.61 ? 115 SER   A CA  1 
ATOM   594  C  C   . SER   A 1 74  ? 0.415   -5.933  26.415  1.00 43.75 ? 115 SER   A C   1 
ATOM   595  O  O   . SER   A 1 74  ? 0.661   -6.330  27.554  1.00 42.57 ? 115 SER   A O   1 
ATOM   596  C  CB  . SER   A 1 74  ? -1.399  -4.251  26.087  1.00 37.70 ? 115 SER   A CB  1 
ATOM   597  O  OG  . SER   A 1 74  ? -1.705  -3.101  25.308  1.00 41.60 ? 115 SER   A OG  1 
ATOM   598  N  N   . LEU   A 1 75  ? 0.380   -6.753  25.368  1.00 46.06 ? 116 LEU   A N   1 
ATOM   599  C  CA  . LEU   A 1 75  ? 0.528   -8.200  25.480  1.00 46.18 ? 116 LEU   A CA  1 
ATOM   600  C  C   . LEU   A 1 75  ? 1.888   -8.561  24.893  1.00 51.54 ? 116 LEU   A C   1 
ATOM   601  O  O   . LEU   A 1 75  ? 1.994   -9.062  23.771  1.00 48.58 ? 116 LEU   A O   1 
ATOM   602  C  CB  . LEU   A 1 75  ? -0.619  -8.914  24.753  1.00 45.78 ? 116 LEU   A CB  1 
ATOM   603  C  CG  . LEU   A 1 75  ? -1.037  -10.314 25.208  1.00 45.93 ? 116 LEU   A CG  1 
ATOM   604  C  CD1 . LEU   A 1 75  ? -0.814  -10.507 26.703  1.00 48.08 ? 116 LEU   A CD1 1 
ATOM   605  C  CD2 . LEU   A 1 75  ? -2.483  -10.586 24.829  1.00 40.41 ? 116 LEU   A CD2 1 
ATOM   606  N  N   . GLN   A 1 76  ? 2.945   -8.298  25.666  1.00 49.92 ? 117 GLN   A N   1 
ATOM   607  C  CA  . GLN   A 1 76  ? 4.232   -8.600  25.053  1.00 56.78 ? 117 GLN   A CA  1 
ATOM   608  C  C   . GLN   A 1 76  ? 4.679   -10.009 25.413  1.00 51.16 ? 117 GLN   A C   1 
ATOM   609  O  O   . GLN   A 1 76  ? 4.668   -10.377 26.592  1.00 50.73 ? 117 GLN   A O   1 
ATOM   610  C  CB  . GLN   A 1 76  ? 5.294   -7.589  25.460  1.00 57.37 ? 117 GLN   A CB  1 
ATOM   611  C  CG  . GLN   A 1 76  ? 4.757   -6.185  25.672  1.00 61.45 ? 117 GLN   A CG  1 
ATOM   612  C  CD  . GLN   A 1 76  ? 5.832   -5.127  25.504  1.00 68.59 ? 117 GLN   A CD  1 
ATOM   613  O  OE1 . GLN   A 1 76  ? 6.675   -4.937  26.378  1.00 72.57 ? 117 GLN   A OE1 1 
ATOM   614  N  NE2 . GLN   A 1 76  ? 5.817   -4.445  24.361  1.00 60.81 ? 117 GLN   A NE2 1 
ATOM   615  N  N   . PRO   A 1 77  ? 5.064   -10.807 24.425  1.00 47.06 ? 118 PRO   A N   1 
ATOM   616  C  CA  . PRO   A 1 77  ? 5.510   -12.175 24.693  1.00 47.60 ? 118 PRO   A CA  1 
ATOM   617  C  C   . PRO   A 1 77  ? 6.934   -12.214 25.228  1.00 54.69 ? 118 PRO   A C   1 
ATOM   618  O  O   . PRO   A 1 77  ? 7.736   -11.299 25.029  1.00 55.67 ? 118 PRO   A O   1 
ATOM   619  C  CB  . PRO   A 1 77  ? 5.430   -12.840 23.315  1.00 46.86 ? 118 PRO   A CB  1 
ATOM   620  C  CG  . PRO   A 1 77  ? 5.640   -11.712 22.351  1.00 51.52 ? 118 PRO   A CG  1 
ATOM   621  C  CD  . PRO   A 1 77  ? 5.006   -10.505 22.985  1.00 50.42 ? 118 PRO   A CD  1 
ATOM   622  N  N   . CYS   A 1 78  ? 7.232   -13.305 25.935  1.00 53.67 ? 119 CYS   A N   1 
ATOM   623  C  CA  . CYS   A 1 78  ? 8.594   -13.534 26.404  1.00 53.41 ? 119 CYS   A CA  1 
ATOM   624  C  C   . CYS   A 1 78  ? 9.577   -13.538 25.243  1.00 52.64 ? 119 CYS   A C   1 
ATOM   625  O  O   . CYS   A 1 78  ? 10.691  -13.011 25.356  1.00 58.04 ? 119 CYS   A O   1 
ATOM   626  C  CB  . CYS   A 1 78  ? 8.663   -14.853 27.169  1.00 52.93 ? 119 CYS   A CB  1 
ATOM   627  S  SG  . CYS   A 1 78  ? 7.361   -15.026 28.398  1.00 57.82 ? 119 CYS   A SG  1 
ATOM   628  N  N   . VAL   A 1 79  ? 9.178   -14.124 24.117  1.00 49.69 ? 120 VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 79  ? 10.016  -14.204 22.929  1.00 53.14 ? 120 VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 79  ? 9.131   -14.006 21.709  1.00 52.89 ? 120 VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 79  ? 8.081   -14.647 21.584  1.00 50.08 ? 120 VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 79  ? 10.765  -15.548 22.844  1.00 51.66 ? 120 VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 79  ? 11.512  -15.661 21.523  1.00 52.68 ? 120 VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 79  ? 11.710  -15.706 24.025  1.00 53.46 ? 120 VAL   A CG2 1 
ATOM   635  N  N   . LYS   A 1 80  ? 9.541   -13.103 20.825  1.00 52.68 ? 121 LYS   A N   1 
ATOM   636  C  CA  . LYS   A 1 80  ? 8.870   -12.859 19.559  1.00 54.84 ? 121 LYS   A CA  1 
ATOM   637  C  C   . LYS   A 1 80  ? 9.806   -13.291 18.439  1.00 55.30 ? 121 LYS   A C   1 
ATOM   638  O  O   . LYS   A 1 80  ? 10.995  -12.956 18.458  1.00 56.05 ? 121 LYS   A O   1 
ATOM   639  C  CB  . LYS   A 1 80  ? 8.501   -11.378 19.421  1.00 58.02 ? 121 LYS   A CB  1 
ATOM   640  C  CG  . LYS   A 1 80  ? 7.153   -11.099 18.765  1.00 59.27 ? 121 LYS   A CG  1 
ATOM   641  C  CD  . LYS   A 1 80  ? 6.455   -9.908  19.433  1.00 61.99 ? 121 LYS   A CD  1 
ATOM   642  C  CE  . LYS   A 1 80  ? 7.421   -8.740  19.632  1.00 70.53 ? 121 LYS   A CE  1 
ATOM   643  N  NZ  . LYS   A 1 80  ? 6.727   -7.416  19.654  1.00 64.27 ? 121 LYS   A NZ  1 
ATOM   644  N  N   . LEU   A 1 81  ? 9.282   -14.049 17.480  1.00 53.56 ? 122 LEU   A N   1 
ATOM   645  C  CA  . LEU   A 1 81  ? 10.082  -14.595 16.385  1.00 59.79 ? 122 LEU   A CA  1 
ATOM   646  C  C   . LEU   A 1 81  ? 9.508   -14.069 15.072  1.00 62.62 ? 122 LEU   A C   1 
ATOM   647  O  O   . LEU   A 1 81  ? 8.527   -14.616 14.557  1.00 62.78 ? 122 LEU   A O   1 
ATOM   648  C  CB  . LEU   A 1 81  ? 10.086  -16.125 16.424  1.00 57.98 ? 122 LEU   A CB  1 
ATOM   649  C  CG  . LEU   A 1 81  ? 11.091  -16.818 17.351  1.00 57.99 ? 122 LEU   A CG  1 
ATOM   650  C  CD1 . LEU   A 1 81  ? 10.417  -17.198 18.665  1.00 54.19 ? 122 LEU   A CD1 1 
ATOM   651  C  CD2 . LEU   A 1 81  ? 11.704  -18.044 16.691  1.00 58.78 ? 122 LEU   A CD2 1 
ATOM   652  N  N   . THR   A 1 82  ? 10.119  -13.016 14.525  1.00 66.45 ? 123 THR   A N   1 
ATOM   653  C  CA  . THR   A 1 82  ? 9.628   -12.372 13.312  1.00 69.86 ? 123 THR   A CA  1 
ATOM   654  C  C   . THR   A 1 82  ? 10.754  -12.238 12.297  1.00 74.48 ? 123 THR   A C   1 
ATOM   655  O  O   . THR   A 1 82  ? 11.782  -11.617 12.586  1.00 73.82 ? 123 THR   A O   1 
ATOM   656  C  CB  . THR   A 1 82  ? 9.025   -10.994 13.607  1.00 66.72 ? 123 THR   A CB  1 
ATOM   657  O  OG1 . THR   A 1 82  ? 8.376   -11.013 14.884  1.00 63.28 ? 123 THR   A OG1 1 
ATOM   658  C  CG2 . THR   A 1 82  ? 8.014   -10.622 12.531  1.00 65.37 ? 123 THR   A CG2 1 
ATOM   659  N  N   . GLY   A 1 83  ? 10.548  -12.808 11.108  1.00 76.39 ? 124 GLY   A N   1 
ATOM   660  C  CA  . GLY   A 1 83  ? 11.455  -12.611 9.987   1.00 76.75 ? 124 GLY   A CA  1 
ATOM   661  C  C   . GLY   A 1 83  ? 12.889  -13.020 10.241  1.00 75.36 ? 124 GLY   A C   1 
ATOM   662  O  O   . GLY   A 1 83  ? 13.804  -12.410 9.684   1.00 70.16 ? 124 GLY   A O   1 
ATOM   663  N  N   . GLY   A 1 84  ? 13.109  -14.050 11.058  1.00 75.15 ? 198 GLY   A N   1 
ATOM   664  C  CA  . GLY   A 1 84  ? 14.442  -14.456 11.444  1.00 71.92 ? 198 GLY   A CA  1 
ATOM   665  C  C   . GLY   A 1 84  ? 14.959  -13.810 12.712  1.00 75.57 ? 198 GLY   A C   1 
ATOM   666  O  O   . GLY   A 1 84  ? 15.852  -14.371 13.357  1.00 72.68 ? 198 GLY   A O   1 
ATOM   667  N  N   . SER   A 1 85  ? 14.426  -12.650 13.082  1.00 74.56 ? 199 SER   A N   1 
ATOM   668  C  CA  . SER   A 1 85  ? 14.814  -11.952 14.295  1.00 72.40 ? 199 SER   A CA  1 
ATOM   669  C  C   . SER   A 1 85  ? 14.150  -12.589 15.512  1.00 69.80 ? 199 SER   A C   1 
ATOM   670  O  O   . SER   A 1 85  ? 13.122  -13.267 15.407  1.00 71.15 ? 199 SER   A O   1 
ATOM   671  C  CB  . SER   A 1 85  ? 14.443  -10.473 14.187  1.00 72.72 ? 199 SER   A CB  1 
ATOM   672  O  OG  . SER   A 1 85  ? 14.845  -9.939  12.932  1.00 77.56 ? 199 SER   A OG  1 
ATOM   673  N  N   . VAL   A 1 86  ? 14.755  -12.366 16.681  1.00 65.05 ? 200 VAL   A N   1 
ATOM   674  C  CA  . VAL   A 1 86  ? 14.289  -12.994 17.911  1.00 63.81 ? 200 VAL   A CA  1 
ATOM   675  C  C   . VAL   A 1 86  ? 14.466  -12.025 19.076  1.00 62.25 ? 200 VAL   A C   1 
ATOM   676  O  O   . VAL   A 1 86  ? 15.589  -11.787 19.532  1.00 61.24 ? 200 VAL   A O   1 
ATOM   677  C  CB  . VAL   A 1 86  ? 15.040  -14.312 18.171  1.00 63.84 ? 200 VAL   A CB  1 
ATOM   678  C  CG1 . VAL   A 1 86  ? 15.058  -14.638 19.672  1.00 61.28 ? 200 VAL   A CG1 1 
ATOM   679  C  CG2 . VAL   A 1 86  ? 14.454  -15.457 17.364  1.00 60.79 ? 200 VAL   A CG2 1 
ATOM   680  N  N   . ILE   A 1 87  ? 13.362  -11.468 19.560  1.00 60.39 ? 201 ILE   A N   1 
ATOM   681  C  CA  . ILE   A 1 87  ? 13.364  -10.489 20.643  1.00 62.87 ? 201 ILE   A CA  1 
ATOM   682  C  C   . ILE   A 1 87  ? 12.996  -11.180 21.948  1.00 61.16 ? 201 ILE   A C   1 
ATOM   683  O  O   . ILE   A 1 87  ? 12.063  -11.991 21.990  1.00 60.79 ? 201 ILE   A O   1 
ATOM   684  C  CB  . ILE   A 1 87  ? 12.389  -9.332  20.348  1.00 66.82 ? 201 ILE   A CB  1 
ATOM   685  C  CG1 . ILE   A 1 87  ? 12.989  -8.356  19.331  1.00 66.08 ? 201 ILE   A CG1 1 
ATOM   686  C  CG2 . ILE   A 1 87  ? 12.019  -8.612  21.642  1.00 67.81 ? 201 ILE   A CG2 1 
ATOM   687  C  CD1 . ILE   A 1 87  ? 12.017  -7.284  18.877  1.00 66.11 ? 201 ILE   A CD1 1 
ATOM   688  N  N   . LYS   A 1 88  ? 13.714  -10.847 23.021  1.00 62.68 ? 202 LYS   A N   1 
ATOM   689  C  CA  . LYS   A 1 88  ? 13.447  -11.381 24.358  1.00 63.62 ? 202 LYS   A CA  1 
ATOM   690  C  C   . LYS   A 1 88  ? 13.136  -10.209 25.283  1.00 66.57 ? 202 LYS   A C   1 
ATOM   691  O  O   . LYS   A 1 88  ? 14.052  -9.579  25.820  1.00 69.32 ? 202 LYS   A O   1 
ATOM   692  C  CB  . LYS   A 1 88  ? 14.634  -12.171 24.899  1.00 65.40 ? 202 LYS   A CB  1 
ATOM   693  C  CG  . LYS   A 1 88  ? 14.993  -13.429 24.144  1.00 64.13 ? 202 LYS   A CG  1 
ATOM   694  C  CD  . LYS   A 1 88  ? 16.320  -13.228 23.430  1.00 65.33 ? 202 LYS   A CD  1 
ATOM   695  C  CE  . LYS   A 1 88  ? 17.036  -14.546 23.205  1.00 63.96 ? 202 LYS   A CE  1 
ATOM   696  N  NZ  . LYS   A 1 88  ? 18.102  -14.406 22.174  1.00 69.80 ? 202 LYS   A NZ  1 
ATOM   697  N  N   . GLN   A 1 89  ? 11.857  -9.920  25.494  1.00 64.77 ? 203 GLN   A N   1 
ATOM   698  C  CA  . GLN   A 1 89  ? 11.470  -8.811  26.352  1.00 66.25 ? 203 GLN   A CA  1 
ATOM   699  C  C   . GLN   A 1 89  ? 10.594  -9.304  27.498  1.00 66.74 ? 203 GLN   A C   1 
ATOM   700  O  O   . GLN   A 1 89  ? 10.175  -10.464 27.544  1.00 65.88 ? 203 GLN   A O   1 
ATOM   701  C  CB  . GLN   A 1 89  ? 10.770  -7.709  25.542  1.00 68.84 ? 203 GLN   A CB  1 
ATOM   702  C  CG  . GLN   A 1 89  ? 9.336   -7.990  25.134  1.00 69.16 ? 203 GLN   A CG  1 
ATOM   703  C  CD  . GLN   A 1 89  ? 9.084   -7.648  23.676  1.00 72.28 ? 203 GLN   A CD  1 
ATOM   704  O  OE1 . GLN   A 1 89  ? 9.367   -8.445  22.781  1.00 74.49 ? 203 GLN   A OE1 1 
ATOM   705  N  NE2 . GLN   A 1 89  ? 8.582   -6.444  23.428  1.00 73.87 ? 203 GLN   A NE2 1 
ATOM   706  N  N   . ALA   A 1 90  ? 10.347  -8.400  28.444  1.00 67.51 ? 204 ALA   A N   1 
ATOM   707  C  CA  . ALA   A 1 90  ? 9.595   -8.747  29.642  1.00 65.76 ? 204 ALA   A CA  1 
ATOM   708  C  C   . ALA   A 1 90  ? 8.176   -9.170  29.285  1.00 62.82 ? 204 ALA   A C   1 
ATOM   709  O  O   . ALA   A 1 90  ? 7.501   -8.528  28.473  1.00 65.28 ? 204 ALA   A O   1 
ATOM   710  C  CB  . ALA   A 1 90  ? 9.567   -7.563  30.607  1.00 65.97 ? 204 ALA   A CB  1 
ATOM   711  N  N   . CYS   A 1 91  ? 7.722   -10.260 29.899  1.00 59.20 ? 205 CYS   A N   1 
ATOM   712  C  CA  . CYS   A 1 91  ? 6.400   -10.832 29.641  1.00 56.91 ? 205 CYS   A CA  1 
ATOM   713  C  C   . CYS   A 1 91  ? 5.700   -11.104 30.968  1.00 53.86 ? 205 CYS   A C   1 
ATOM   714  O  O   . CYS   A 1 91  ? 5.463   -12.263 31.334  1.00 53.60 ? 205 CYS   A O   1 
ATOM   715  C  CB  . CYS   A 1 91  ? 6.505   -12.117 28.815  1.00 55.53 ? 205 CYS   A CB  1 
ATOM   716  S  SG  . CYS   A 1 91  ? 7.589   -13.374 29.557  1.00 58.51 ? 205 CYS   A SG  1 
ATOM   717  N  N   . PRO   A 1 92  ? 5.347   -10.058 31.710  1.00 52.31 ? 206 PRO   A N   1 
ATOM   718  C  CA  . PRO   A 1 92  ? 4.604   -10.253 32.959  1.00 50.34 ? 206 PRO   A CA  1 
ATOM   719  C  C   . PRO   A 1 92  ? 3.147   -10.586 32.673  1.00 51.59 ? 206 PRO   A C   1 
ATOM   720  O  O   . PRO   A 1 92  ? 2.641   -10.406 31.564  1.00 53.13 ? 206 PRO   A O   1 
ATOM   721  C  CB  . PRO   A 1 92  ? 4.742   -8.911  33.683  1.00 53.44 ? 206 PRO   A CB  1 
ATOM   722  C  CG  . PRO   A 1 92  ? 5.047   -7.912  32.609  1.00 51.01 ? 206 PRO   A CG  1 
ATOM   723  C  CD  . PRO   A 1 92  ? 5.600   -8.636  31.413  1.00 56.05 ? 206 PRO   A CD  1 
ATOM   724  N  N   . LYS   A 1 93  ? 2.467   -11.083 33.704  1.00 47.26 ? 207 LYS   A N   1 
ATOM   725  C  CA  . LYS   A 1 93  ? 1.049   -11.393 33.587  1.00 51.35 ? 207 LYS   A CA  1 
ATOM   726  C  C   . LYS   A 1 93  ? 0.241   -10.112 33.769  1.00 48.47 ? 207 LYS   A C   1 
ATOM   727  O  O   . LYS   A 1 93  ? 0.511   -9.318  34.675  1.00 45.68 ? 207 LYS   A O   1 
ATOM   728  C  CB  . LYS   A 1 93  ? 0.631   -12.434 34.630  1.00 48.31 ? 207 LYS   A CB  1 
ATOM   729  C  CG  . LYS   A 1 93  ? 1.104   -13.862 34.346  1.00 51.40 ? 207 LYS   A CG  1 
ATOM   730  C  CD  . LYS   A 1 93  ? 1.256   -14.171 32.865  1.00 50.99 ? 207 LYS   A CD  1 
ATOM   731  C  CE  . LYS   A 1 93  ? 0.427   -15.374 32.435  1.00 47.37 ? 207 LYS   A CE  1 
ATOM   732  N  NZ  . LYS   A 1 93  ? 0.413   -15.501 30.946  1.00 46.29 ? 207 LYS   A NZ  1 
ATOM   733  N  N   . ILE   A 1 94  ? -0.759  -9.913  32.910  1.00 46.66 ? 208 ILE   A N   1 
ATOM   734  C  CA  . ILE   A 1 94  ? -1.447  -8.626  32.858  1.00 43.24 ? 208 ILE   A CA  1 
ATOM   735  C  C   . ILE   A 1 94  ? -2.928  -8.750  33.183  1.00 45.19 ? 208 ILE   A C   1 
ATOM   736  O  O   . ILE   A 1 94  ? -3.456  -9.852  33.376  1.00 40.58 ? 208 ILE   A O   1 
ATOM   737  C  CB  . ILE   A 1 94  ? -1.287  -7.969  31.476  1.00 42.35 ? 208 ILE   A CB  1 
ATOM   738  C  CG1 . ILE   A 1 94  ? -2.050  -8.782  30.423  1.00 41.84 ? 208 ILE   A CG1 1 
ATOM   739  C  CG2 . ILE   A 1 94  ? 0.185   -7.823  31.115  1.00 41.87 ? 208 ILE   A CG2 1 
ATOM   740  C  CD1 . ILE   A 1 94  ? -2.058  -8.160  29.049  1.00 42.12 ? 208 ILE   A CD1 1 
ATOM   741  N  N   . SER   A 1 95  ? -3.599  -7.601  33.246  1.00 39.25 ? 209 SER   A N   1 
ATOM   742  C  CA  . SER   A 1 95  ? -5.049  -7.514  33.333  1.00 41.88 ? 209 SER   A CA  1 
ATOM   743  C  C   . SER   A 1 95  ? -5.586  -7.237  31.934  1.00 38.91 ? 209 SER   A C   1 
ATOM   744  O  O   . SER   A 1 95  ? -5.171  -6.265  31.289  1.00 33.43 ? 209 SER   A O   1 
ATOM   745  C  CB  . SER   A 1 95  ? -5.465  -6.410  34.305  1.00 39.96 ? 209 SER   A CB  1 
ATOM   746  O  OG  . SER   A 1 95  ? -6.834  -6.502  34.650  1.00 38.33 ? 209 SER   A OG  1 
ATOM   747  N  N   . PHE   A 1 96  ? -6.503  -8.083  31.466  1.00 34.46 ? 210 PHE   A N   1 
ATOM   748  C  CA  . PHE   A 1 96  ? -6.915  -8.066  30.066  1.00 36.75 ? 210 PHE   A CA  1 
ATOM   749  C  C   . PHE   A 1 96  ? -8.408  -8.336  29.984  1.00 32.56 ? 210 PHE   A C   1 
ATOM   750  O  O   . PHE   A 1 96  ? -8.874  -9.391  30.422  1.00 28.81 ? 210 PHE   A O   1 
ATOM   751  C  CB  . PHE   A 1 96  ? -6.112  -9.098  29.260  1.00 34.03 ? 210 PHE   A CB  1 
ATOM   752  C  CG  . PHE   A 1 96  ? -6.377  -9.074  27.780  1.00 30.58 ? 210 PHE   A CG  1 
ATOM   753  C  CD1 . PHE   A 1 96  ? -7.524  -9.647  27.254  1.00 31.29 ? 210 PHE   A CD1 1 
ATOM   754  C  CD2 . PHE   A 1 96  ? -5.472  -8.482  26.915  1.00 32.35 ? 210 PHE   A CD2 1 
ATOM   755  C  CE1 . PHE   A 1 96  ? -7.761  -9.630  25.894  1.00 26.49 ? 210 PHE   A CE1 1 
ATOM   756  C  CE2 . PHE   A 1 96  ? -5.702  -8.458  25.553  1.00 30.52 ? 210 PHE   A CE2 1 
ATOM   757  C  CZ  . PHE   A 1 96  ? -6.856  -9.035  25.041  1.00 27.62 ? 210 PHE   A CZ  1 
ATOM   758  N  N   . ASP   A 1 97  ? -9.154  -7.375  29.437  1.00 31.35 ? 211 ASP   A N   1 
ATOM   759  C  CA  . ASP   A 1 97  ? -10.600 -7.457  29.266  1.00 32.16 ? 211 ASP   A CA  1 
ATOM   760  C  C   . ASP   A 1 97  ? -11.028 -6.344  28.316  1.00 30.73 ? 211 ASP   A C   1 
ATOM   761  O  O   . ASP   A 1 97  ? -11.052 -5.170  28.711  1.00 29.35 ? 211 ASP   A O   1 
ATOM   762  C  CB  . ASP   A 1 97  ? -11.318 -7.335  30.614  1.00 32.90 ? 211 ASP   A CB  1 
ATOM   763  C  CG  . ASP   A 1 97  ? -12.824 -7.552  30.505  1.00 37.58 ? 211 ASP   A CG  1 
ATOM   764  O  OD1 . ASP   A 1 97  ? -13.269 -8.223  29.547  1.00 33.72 ? 211 ASP   A OD1 1 
ATOM   765  O  OD2 . ASP   A 1 97  ? -13.559 -7.052  31.385  1.00 44.69 ? 211 ASP   A OD2 1 
ATOM   766  N  N   . PRO   A 1 98  ? -11.357 -6.661  27.063  1.00 28.81 ? 212 PRO   A N   1 
ATOM   767  C  CA  . PRO   A 1 98  ? -11.596 -5.599  26.076  1.00 28.08 ? 212 PRO   A CA  1 
ATOM   768  C  C   . PRO   A 1 98  ? -12.727 -4.666  26.494  1.00 27.41 ? 212 PRO   A C   1 
ATOM   769  O  O   . PRO   A 1 98  ? -13.693 -5.069  27.143  1.00 28.46 ? 212 PRO   A O   1 
ATOM   770  C  CB  . PRO   A 1 98  ? -11.955 -6.367  24.799  1.00 27.15 ? 212 PRO   A CB  1 
ATOM   771  C  CG  . PRO   A 1 98  ? -11.439 -7.768  25.012  1.00 29.54 ? 212 PRO   A CG  1 
ATOM   772  C  CD  . PRO   A 1 98  ? -11.499 -8.011  26.489  1.00 29.38 ? 212 PRO   A CD  1 
ATOM   773  N  N   . ILE   A 1 99  ? -12.599 -3.403  26.103  1.00 25.43 ? 213 ILE   A N   1 
ATOM   774  C  CA  . ILE   A 1 99  ? -13.602 -2.381  26.386  1.00 25.27 ? 213 ILE   A CA  1 
ATOM   775  C  C   . ILE   A 1 99  ? -14.054 -1.812  25.049  1.00 22.74 ? 213 ILE   A C   1 
ATOM   776  O  O   . ILE   A 1 99  ? -13.340 -1.915  24.029  1.00 20.63 ? 213 ILE   A O   1 
ATOM   777  C  CB  . ILE   A 1 99  ? -13.062 -1.286  27.336  1.00 26.89 ? 213 ILE   A CB  1 
ATOM   778  C  CG1 . ILE   A 1 99  ? -11.953 -0.487  26.654  1.00 26.46 ? 213 ILE   A CG1 1 
ATOM   779  C  CG2 . ILE   A 1 99  ? -12.573 -1.898  28.638  1.00 30.52 ? 213 ILE   A CG2 1 
ATOM   780  C  CD1 . ILE   A 1 99  ? -11.605 0.802   27.373  1.00 30.18 ? 213 ILE   A CD1 1 
ATOM   781  N  N   . PRO   A 1 100 ? -15.249 -1.225  25.006  1.00 25.70 ? 214 PRO   A N   1 
ATOM   782  C  CA  . PRO   A 1 100 ? -15.738 -0.661  23.742  1.00 23.98 ? 214 PRO   A CA  1 
ATOM   783  C  C   . PRO   A 1 100 ? -14.901 0.524   23.285  1.00 24.71 ? 214 PRO   A C   1 
ATOM   784  O  O   . PRO   A 1 100 ? -14.506 1.374   24.087  1.00 26.38 ? 214 PRO   A O   1 
ATOM   785  C  CB  . PRO   A 1 100 ? -17.171 -0.226  24.073  1.00 25.33 ? 214 PRO   A CB  1 
ATOM   786  C  CG  . PRO   A 1 100 ? -17.567 -1.055  25.237  1.00 28.05 ? 214 PRO   A CG  1 
ATOM   787  C  CD  . PRO   A 1 100 ? -16.298 -1.213  26.047  1.00 26.54 ? 214 PRO   A CD  1 
ATOM   788  N  N   . ILE   A 1 101 ? -14.635 0.574   21.979  1.00 21.13 ? 215 ILE   A N   1 
ATOM   789  C  CA  . ILE   A 1 101 ? -13.926 1.681   21.340  1.00 24.27 ? 215 ILE   A CA  1 
ATOM   790  C  C   . ILE   A 1 101 ? -14.852 2.306   20.304  1.00 24.19 ? 215 ILE   A C   1 
ATOM   791  O  O   . ILE   A 1 101 ? -15.463 1.588   19.503  1.00 23.19 ? 215 ILE   A O   1 
ATOM   792  C  CB  . ILE   A 1 101 ? -12.618 1.218   20.669  1.00 23.48 ? 215 ILE   A CB  1 
ATOM   793  C  CG1 . ILE   A 1 101 ? -11.671 0.559   21.680  1.00 25.83 ? 215 ILE   A CG1 1 
ATOM   794  C  CG2 . ILE   A 1 101 ? -11.927 2.394   19.975  1.00 24.48 ? 215 ILE   A CG2 1 
ATOM   795  C  CD1 . ILE   A 1 101 ? -11.583 1.259   23.013  1.00 29.79 ? 215 ILE   A CD1 1 
ATOM   796  N  N   . HIS   A 1 102 ? -14.952 3.636   20.318  1.00 23.09 ? 216 HIS   A N   1 
ATOM   797  C  CA  . HIS   A 1 102 ? -15.733 4.389   19.343  1.00 24.31 ? 216 HIS   A CA  1 
ATOM   798  C  C   . HIS   A 1 102 ? -14.814 5.006   18.295  1.00 21.83 ? 216 HIS   A C   1 
ATOM   799  O  O   . HIS   A 1 102 ? -13.749 5.533   18.624  1.00 27.53 ? 216 HIS   A O   1 
ATOM   800  C  CB  . HIS   A 1 102 ? -16.533 5.510   20.013  1.00 24.62 ? 216 HIS   A CB  1 
ATOM   801  C  CG  . HIS   A 1 102 ? -17.444 5.043   21.105  1.00 25.77 ? 216 HIS   A CG  1 
ATOM   802  N  ND1 . HIS   A 1 102 ? -18.814 4.994   20.966  1.00 29.63 ? 216 HIS   A ND1 1 
ATOM   803  C  CD2 . HIS   A 1 102 ? -17.181 4.636   22.370  1.00 26.28 ? 216 HIS   A CD2 1 
ATOM   804  C  CE1 . HIS   A 1 102 ? -19.355 4.559   22.091  1.00 28.57 ? 216 HIS   A CE1 1 
ATOM   805  N  NE2 . HIS   A 1 102 ? -18.385 4.338   22.960  1.00 27.59 ? 216 HIS   A NE2 1 
ATOM   806  N  N   . TYR   A 1 103 ? -15.237 4.971   17.039  1.00 21.61 ? 217 TYR   A N   1 
ATOM   807  C  CA  . TYR   A 1 103 ? -14.488 5.591   15.954  1.00 24.08 ? 217 TYR   A CA  1 
ATOM   808  C  C   . TYR   A 1 103 ? -15.226 6.823   15.455  1.00 25.62 ? 217 TYR   A C   1 
ATOM   809  O  O   . TYR   A 1 103 ? -16.424 6.764   15.154  1.00 23.93 ? 217 TYR   A O   1 
ATOM   810  C  CB  . TYR   A 1 103 ? -14.203 4.575   14.845  1.00 24.70 ? 217 TYR   A CB  1 
ATOM   811  C  CG  . TYR   A 1 103 ? -13.087 3.662   15.293  1.00 24.70 ? 217 TYR   A CG  1 
ATOM   812  C  CD1 . TYR   A 1 103 ? -11.766 4.063   15.168  1.00 25.20 ? 217 TYR   A CD1 1 
ATOM   813  C  CD2 . TYR   A 1 103 ? -13.350 2.460   15.934  1.00 24.78 ? 217 TYR   A CD2 1 
ATOM   814  C  CE1 . TYR   A 1 103 ? -10.727 3.267   15.611  1.00 25.91 ? 217 TYR   A CE1 1 
ATOM   815  C  CE2 . TYR   A 1 103 ? -12.319 1.646   16.384  1.00 21.72 ? 217 TYR   A CE2 1 
ATOM   816  C  CZ  . TYR   A 1 103 ? -11.009 2.060   16.217  1.00 24.05 ? 217 TYR   A CZ  1 
ATOM   817  O  OH  . TYR   A 1 103 ? -9.974  1.279   16.660  1.00 26.90 ? 217 TYR   A OH  1 
ATOM   818  N  N   . CYS   A 1 104 ? -14.498 7.937   15.378  1.00 25.54 ? 218 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? -15.069 9.260   15.191  1.00 26.81 ? 218 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? -14.319 10.004  14.097  1.00 28.48 ? 218 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? -13.106 9.845   13.933  1.00 28.06 ? 218 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? -15.000 10.072  16.491  1.00 26.76 ? 218 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? -15.580 9.201   17.954  1.00 30.51 ? 218 CYS   A SG  1 
ATOM   824  N  N   . THR   A 1 105 ? -15.055 10.850  13.366  1.00 26.45 ? 219 THR   A N   1 
ATOM   825  C  CA  . THR   A 1 105 ? -14.525 11.623  12.253  1.00 29.08 ? 219 THR   A CA  1 
ATOM   826  C  C   . THR   A 1 105 ? -14.068 13.004  12.714  1.00 29.56 ? 219 THR   A C   1 
ATOM   827  O  O   . THR   A 1 105 ? -14.653 13.588  13.634  1.00 30.22 ? 219 THR   A O   1 
ATOM   828  C  CB  . THR   A 1 105 ? -15.582 11.782  11.159  1.00 30.07 ? 219 THR   A CB  1 
ATOM   829  O  OG1 . THR   A 1 105 ? -16.882 11.874  11.757  1.00 28.21 ? 219 THR   A OG1 1 
ATOM   830  C  CG2 . THR   A 1 105 ? -15.552 10.592  10.211  1.00 27.14 ? 219 THR   A CG2 1 
ATOM   831  N  N   . PRO   A 1 106 ? -13.026 13.541  12.097  1.00 31.32 ? 220 PRO   A N   1 
ATOM   832  C  CA  . PRO   A 1 106 ? -12.610 14.914  12.380  1.00 28.56 ? 220 PRO   A CA  1 
ATOM   833  C  C   . PRO   A 1 106 ? -13.489 15.902  11.617  1.00 32.15 ? 220 PRO   A C   1 
ATOM   834  O  O   . PRO   A 1 106 ? -14.443 15.532  10.937  1.00 30.33 ? 220 PRO   A O   1 
ATOM   835  C  CB  . PRO   A 1 106 ? -11.164 14.938  11.890  1.00 32.47 ? 220 PRO   A CB  1 
ATOM   836  C  CG  . PRO   A 1 106 ? -11.167 13.992  10.738  1.00 31.00 ? 220 PRO   A CG  1 
ATOM   837  C  CD  . PRO   A 1 106 ? -12.132 12.885  11.123  1.00 31.31 ? 220 PRO   A CD  1 
ATOM   838  N  N   . ALA   A 1 107 ? -13.147 17.181  11.746  1.00 34.46 ? 221 ALA   A N   1 
ATOM   839  C  CA  . ALA   A 1 107 ? -13.935 18.231  11.113  1.00 33.60 ? 221 ALA   A CA  1 
ATOM   840  C  C   . ALA   A 1 107 ? -13.896 18.097  9.596   1.00 34.53 ? 221 ALA   A C   1 
ATOM   841  O  O   . ALA   A 1 107 ? -12.879 17.710  9.013   1.00 36.84 ? 221 ALA   A O   1 
ATOM   842  C  CB  . ALA   A 1 107 ? -13.425 19.610  11.540  1.00 38.15 ? 221 ALA   A CB  1 
ATOM   843  N  N   . GLY   A 1 108 ? -15.017 18.426  8.956   1.00 32.10 ? 222 GLY   A N   1 
ATOM   844  C  CA  . GLY   A 1 108 ? -15.152 18.291  7.522   1.00 36.21 ? 222 GLY   A CA  1 
ATOM   845  C  C   . GLY   A 1 108 ? -15.659 16.946  7.055   1.00 38.28 ? 222 GLY   A C   1 
ATOM   846  O  O   . GLY   A 1 108 ? -15.857 16.764  5.845   1.00 38.58 ? 222 GLY   A O   1 
ATOM   847  N  N   . TYR   A 1 109 ? -15.887 16.007  7.974   1.00 34.75 ? 223 TYR   A N   1 
ATOM   848  C  CA  . TYR   A 1 109 ? -16.323 14.660  7.647   1.00 33.43 ? 223 TYR   A CA  1 
ATOM   849  C  C   . TYR   A 1 109 ? -17.432 14.251  8.602   1.00 28.51 ? 223 TYR   A C   1 
ATOM   850  O  O   . TYR   A 1 109 ? -17.546 14.774  9.713   1.00 32.62 ? 223 TYR   A O   1 
ATOM   851  C  CB  . TYR   A 1 109 ? -15.167 13.653  7.747   1.00 31.50 ? 223 TYR   A CB  1 
ATOM   852  C  CG  . TYR   A 1 109 ? -14.013 13.924  6.809   1.00 34.16 ? 223 TYR   A CG  1 
ATOM   853  C  CD1 . TYR   A 1 109 ? -13.069 14.894  7.108   1.00 36.83 ? 223 TYR   A CD1 1 
ATOM   854  C  CD2 . TYR   A 1 109 ? -13.854 13.191  5.640   1.00 34.61 ? 223 TYR   A CD2 1 
ATOM   855  C  CE1 . TYR   A 1 109 ? -12.006 15.142  6.261   1.00 39.53 ? 223 TYR   A CE1 1 
ATOM   856  C  CE2 . TYR   A 1 109 ? -12.793 13.428  4.784   1.00 37.75 ? 223 TYR   A CE2 1 
ATOM   857  C  CZ  . TYR   A 1 109 ? -11.872 14.409  5.101   1.00 39.69 ? 223 TYR   A CZ  1 
ATOM   858  O  OH  . TYR   A 1 109 ? -10.811 14.658  4.257   1.00 43.27 ? 223 TYR   A OH  1 
ATOM   859  N  N   . VAL   A 1 110 ? -18.245 13.294  8.161   1.00 29.40 ? 224 VAL   A N   1 
ATOM   860  C  CA  . VAL   A 1 110 ? -19.206 12.621  9.024   1.00 30.85 ? 224 VAL   A CA  1 
ATOM   861  C  C   . VAL   A 1 110 ? -19.194 11.137  8.686   1.00 30.28 ? 224 VAL   A C   1 
ATOM   862  O  O   . VAL   A 1 110 ? -18.649 10.706  7.668   1.00 28.74 ? 224 VAL   A O   1 
ATOM   863  C  CB  . VAL   A 1 110 ? -20.638 13.184  8.886   1.00 31.74 ? 224 VAL   A CB  1 
ATOM   864  C  CG1 . VAL   A 1 110 ? -20.726 14.574  9.496   1.00 36.99 ? 224 VAL   A CG1 1 
ATOM   865  C  CG2 . VAL   A 1 110 ? -21.082 13.183  7.434   1.00 33.92 ? 224 VAL   A CG2 1 
ATOM   866  N  N   . ILE   A 1 111 ? -19.812 10.353  9.563   1.00 27.10 ? 225 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 111 ? -19.990 8.924   9.367   1.00 25.49 ? 225 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 111 ? -21.446 8.697   8.987   1.00 27.91 ? 225 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 111 ? -22.354 9.182   9.673   1.00 26.18 ? 225 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 111 ? -19.623 8.137   10.637  1.00 28.41 ? 225 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 111 ? -18.135 8.303   10.955  1.00 26.83 ? 225 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 111 ? -19.960 6.663   10.464  1.00 26.12 ? 225 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 111 ? -17.741 7.742   12.305  1.00 24.67 ? 225 ILE   A CD1 1 
ATOM   874  N  N   . LEU   A 1 112 ? -21.673 7.983   7.892   1.00 25.63 ? 226 LEU   A N   1 
ATOM   875  C  CA  . LEU   A 1 112 ? -23.024 7.598   7.515   1.00 27.24 ? 226 LEU   A CA  1 
ATOM   876  C  C   . LEU   A 1 112 ? -23.329 6.212   8.074   1.00 30.07 ? 226 LEU   A C   1 
ATOM   877  O  O   . LEU   A 1 112 ? -22.478 5.319   8.052   1.00 25.39 ? 226 LEU   A O   1 
ATOM   878  C  CB  . LEU   A 1 112 ? -23.199 7.613   5.996   1.00 29.10 ? 226 LEU   A CB  1 
ATOM   879  C  CG  . LEU   A 1 112 ? -23.116 8.988   5.314   1.00 31.73 ? 226 LEU   A CG  1 
ATOM   880  C  CD1 . LEU   A 1 112 ? -23.638 8.925   3.881   1.00 36.51 ? 226 LEU   A CD1 1 
ATOM   881  C  CD2 . LEU   A 1 112 ? -23.826 10.078  6.118   1.00 31.68 ? 226 LEU   A CD2 1 
ATOM   882  N  N   . LYS   A 1 113 ? -24.546 6.046   8.586   1.00 29.14 ? 227 LYS   A N   1 
ATOM   883  C  CA  . LYS   A 1 113 ? -24.969 4.843   9.288   1.00 26.71 ? 227 LYS   A CA  1 
ATOM   884  C  C   . LYS   A 1 113 ? -26.170 4.240   8.576   1.00 29.22 ? 227 LYS   A C   1 
ATOM   885  O  O   . LYS   A 1 113 ? -27.197 4.908   8.412   1.00 28.17 ? 227 LYS   A O   1 
ATOM   886  C  CB  . LYS   A 1 113 ? -25.313 5.166   10.741  1.00 28.06 ? 227 LYS   A CB  1 
ATOM   887  C  CG  . LYS   A 1 113 ? -25.503 3.958   11.633  1.00 29.46 ? 227 LYS   A CG  1 
ATOM   888  C  CD  . LYS   A 1 113 ? -25.907 4.442   13.019  1.00 29.48 ? 227 LYS   A CD  1 
ATOM   889  C  CE  . LYS   A 1 113 ? -26.469 3.328   13.874  1.00 37.34 ? 227 LYS   A CE  1 
ATOM   890  N  NZ  . LYS   A 1 113 ? -26.899 3.881   15.195  1.00 38.02 ? 227 LYS   A NZ  1 
ATOM   891  N  N   . CYS   A 1 114 ? -26.050 2.980   8.171   1.00 26.38 ? 228 CYS   A N   1 
ATOM   892  C  CA  . CYS   A 1 114 ? -27.146 2.271   7.524   1.00 27.29 ? 228 CYS   A CA  1 
ATOM   893  C  C   . CYS   A 1 114 ? -28.052 1.662   8.587   1.00 30.24 ? 228 CYS   A C   1 
ATOM   894  O  O   . CYS   A 1 114 ? -27.605 0.847   9.401   1.00 30.83 ? 228 CYS   A O   1 
ATOM   895  C  CB  . CYS   A 1 114 ? -26.627 1.184   6.586   1.00 31.96 ? 228 CYS   A CB  1 
ATOM   896  S  SG  . CYS   A 1 114 ? -27.975 0.312   5.741   1.00 36.54 ? 228 CYS   A SG  1 
ATOM   897  N  N   . ASN   A 1 115 ? -29.327 2.039   8.567   1.00 28.18 ? 229 ASN   A N   1 
ATOM   898  C  CA  . ASN   A 1 115 ? -30.279 1.583   9.568   1.00 32.76 ? 229 ASN   A CA  1 
ATOM   899  C  C   . ASN   A 1 115 ? -31.287 0.578   9.017   1.00 35.24 ? 229 ASN   A C   1 
ATOM   900  O  O   . ASN   A 1 115 ? -32.260 0.248   9.701   1.00 34.96 ? 229 ASN   A O   1 
ATOM   901  C  CB  . ASN   A 1 115 ? -30.988 2.789   10.185  1.00 36.09 ? 229 ASN   A CB  1 
ATOM   902  C  CG  . ASN   A 1 115 ? -30.016 3.775   10.795  1.00 34.40 ? 229 ASN   A CG  1 
ATOM   903  O  OD1 . ASN   A 1 115 ? -29.310 3.455   11.752  1.00 34.58 ? 229 ASN   A OD1 1 
ATOM   904  N  ND2 . ASN   A 1 115 ? -29.957 4.977   10.229  1.00 32.87 ? 229 ASN   A ND2 1 
ATOM   905  N  N   . ASP   A 1 116 ? -31.077 0.083   7.799   1.00 32.98 ? 230 ASP   A N   1 
ATOM   906  C  CA  . ASP   A 1 116 ? -31.897 -0.997  7.264   1.00 35.48 ? 230 ASP   A CA  1 
ATOM   907  C  C   . ASP   A 1 116 ? -31.618 -2.275  8.053   1.00 37.30 ? 230 ASP   A C   1 
ATOM   908  O  O   . ASP   A 1 116 ? -30.480 -2.757  8.072   1.00 33.32 ? 230 ASP   A O   1 
ATOM   909  C  CB  . ASP   A 1 116 ? -31.587 -1.196  5.780   1.00 35.16 ? 230 ASP   A CB  1 
ATOM   910  C  CG  . ASP   A 1 116 ? -32.118 -0.069  4.912   1.00 38.77 ? 230 ASP   A CG  1 
ATOM   911  O  OD1 . ASP   A 1 116 ? -32.698 0.890   5.464   1.00 37.96 ? 230 ASP   A OD1 1 
ATOM   912  O  OD2 . ASP   A 1 116 ? -31.936 -0.142  3.679   1.00 39.04 ? 230 ASP   A OD2 1 
ATOM   913  N  N   . LYS   A 1 117 ? -32.652 -2.844  8.683   1.00 31.66 ? 231 LYS   A N   1 
ATOM   914  C  CA  . LYS   A 1 117 ? -32.423 -3.985  9.563   1.00 36.41 ? 231 LYS   A CA  1 
ATOM   915  C  C   . LYS   A 1 117 ? -32.002 -5.239  8.810   1.00 38.96 ? 231 LYS   A C   1 
ATOM   916  O  O   . LYS   A 1 117 ? -31.422 -6.142  9.422   1.00 39.13 ? 231 LYS   A O   1 
ATOM   917  C  CB  . LYS   A 1 117 ? -33.667 -4.276  10.401  1.00 40.05 ? 231 LYS   A CB  1 
ATOM   918  C  CG  . LYS   A 1 117 ? -34.307 -3.045  11.012  1.00 44.07 ? 231 LYS   A CG  1 
ATOM   919  C  CD  . LYS   A 1 117 ? -35.089 -3.410  12.266  1.00 42.77 ? 231 LYS   A CD  1 
ATOM   920  C  CE  . LYS   A 1 117 ? -36.017 -2.285  12.682  1.00 49.32 ? 231 LYS   A CE  1 
ATOM   921  N  NZ  . LYS   A 1 117 ? -35.245 -1.117  13.186  1.00 49.99 ? 231 LYS   A NZ  1 
ATOM   922  N  N   . ASN   A 1 118 ? -32.272 -5.319  7.510   1.00 38.49 ? 232 ASN   A N   1 
ATOM   923  C  CA  . ASN   A 1 118 ? -31.898 -6.469  6.699   1.00 40.24 ? 232 ASN   A CA  1 
ATOM   924  C  C   . ASN   A 1 118 ? -30.625 -6.239  5.899   1.00 35.49 ? 232 ASN   A C   1 
ATOM   925  O  O   . ASN   A 1 118 ? -30.233 -7.115  5.124   1.00 37.38 ? 232 ASN   A O   1 
ATOM   926  C  CB  . ASN   A 1 118 ? -33.047 -6.833  5.756   1.00 42.99 ? 232 ASN   A CB  1 
ATOM   927  C  CG  . ASN   A 1 118 ? -33.410 -5.693  4.817   1.00 56.15 ? 232 ASN   A CG  1 
ATOM   928  O  OD1 . ASN   A 1 118 ? -32.774 -4.637  4.830   1.00 50.57 ? 232 ASN   A OD1 1 
ATOM   929  N  ND2 . ASN   A 1 118 ? -34.442 -5.899  4.003   1.00 49.83 ? 232 ASN   A ND2 1 
ATOM   930  N  N   . PHE   A 1 119 ? -29.979 -5.087  6.066   1.00 34.48 ? 233 PHE   A N   1 
ATOM   931  C  CA  . PHE   A 1 119 ? -28.794 -4.748  5.287   1.00 34.01 ? 233 PHE   A CA  1 
ATOM   932  C  C   . PHE   A 1 119 ? -27.735 -5.838  5.401   1.00 33.99 ? 233 PHE   A C   1 
ATOM   933  O  O   . PHE   A 1 119 ? -27.364 -6.248  6.505   1.00 32.47 ? 233 PHE   A O   1 
ATOM   934  C  CB  . PHE   A 1 119 ? -28.223 -3.418  5.775   1.00 34.90 ? 233 PHE   A CB  1 
ATOM   935  C  CG  . PHE   A 1 119 ? -27.092 -2.910  4.941   1.00 35.15 ? 233 PHE   A CG  1 
ATOM   936  C  CD1 . PHE   A 1 119 ? -27.218 -2.825  3.565   1.00 37.04 ? 233 PHE   A CD1 1 
ATOM   937  C  CD2 . PHE   A 1 119 ? -25.898 -2.536  5.525   1.00 34.94 ? 233 PHE   A CD2 1 
ATOM   938  C  CE1 . PHE   A 1 119 ? -26.177 -2.363  2.791   1.00 38.08 ? 233 PHE   A CE1 1 
ATOM   939  C  CE2 . PHE   A 1 119 ? -24.851 -2.068  4.752   1.00 35.33 ? 233 PHE   A CE2 1 
ATOM   940  C  CZ  . PHE   A 1 119 ? -24.994 -1.983  3.384   1.00 34.29 ? 233 PHE   A CZ  1 
ATOM   941  N  N   . ASN   A 1 120 ? -27.235 -6.297  4.255   1.00 30.81 ? 234 ASN   A N   1 
ATOM   942  C  CA  . ASN   A 1 120 ? -26.261 -7.379  4.240   1.00 32.27 ? 234 ASN   A CA  1 
ATOM   943  C  C   . ASN   A 1 120 ? -24.822 -6.893  4.147   1.00 31.50 ? 234 ASN   A C   1 
ATOM   944  O  O   . ASN   A 1 120 ? -23.903 -7.716  4.192   1.00 32.26 ? 234 ASN   A O   1 
ATOM   945  C  CB  . ASN   A 1 120 ? -26.568 -8.364  3.105   1.00 31.31 ? 234 ASN   A CB  1 
ATOM   946  C  CG  . ASN   A 1 120 ? -26.211 -7.828  1.727   1.00 36.02 ? 234 ASN   A CG  1 
ATOM   947  O  OD1 . ASN   A 1 120 ? -25.469 -6.855  1.572   1.00 36.12 ? 234 ASN   A OD1 1 
ATOM   948  N  ND2 . ASN   A 1 120 ? -26.739 -8.489  0.709   1.00 36.60 ? 234 ASN   A ND2 1 
ATOM   949  N  N   . GLY   A 1 121 ? -24.599 -5.585  4.023   1.00 32.34 ? 235 GLY   A N   1 
ATOM   950  C  CA  . GLY   A 1 121 ? -23.267 -5.016  4.027   1.00 33.31 ? 235 GLY   A CA  1 
ATOM   951  C  C   . GLY   A 1 121 ? -22.834 -4.413  2.709   1.00 33.46 ? 235 GLY   A C   1 
ATOM   952  O  O   . GLY   A 1 121 ? -21.928 -3.571  2.700   1.00 34.07 ? 235 GLY   A O   1 
ATOM   953  N  N   . THR   A 1 122 ? -23.448 -4.811  1.598   1.00 34.10 ? 236 THR   A N   1 
ATOM   954  C  CA  . THR   A 1 122 ? -23.147 -4.241  0.294   1.00 37.59 ? 236 THR   A CA  1 
ATOM   955  C  C   . THR   A 1 122 ? -24.441 -3.809  -0.372  1.00 39.19 ? 236 THR   A C   1 
ATOM   956  O  O   . THR   A 1 122 ? -25.476 -4.467  -0.226  1.00 40.11 ? 236 THR   A O   1 
ATOM   957  C  CB  . THR   A 1 122 ? -22.404 -5.236  -0.618  1.00 41.06 ? 236 THR   A CB  1 
ATOM   958  O  OG1 . THR   A 1 122 ? -23.351 -6.105  -1.251  1.00 44.83 ? 236 THR   A OG1 1 
ATOM   959  C  CG2 . THR   A 1 122 ? -21.419 -6.068  0.190   1.00 34.96 ? 236 THR   A CG2 1 
ATOM   960  N  N   . GLY   A 1 123 ? -24.376 -2.700  -1.101  1.00 37.52 ? 237 GLY   A N   1 
ATOM   961  C  CA  . GLY   A 1 123 ? -25.511 -2.224  -1.849  1.00 41.61 ? 237 GLY   A CA  1 
ATOM   962  C  C   . GLY   A 1 123 ? -26.195 -1.032  -1.215  1.00 39.13 ? 237 GLY   A C   1 
ATOM   963  O  O   . GLY   A 1 123 ? -25.717 -0.454  -0.235  1.00 38.61 ? 237 GLY   A O   1 
ATOM   964  N  N   . PRO   A 1 124 ? -27.347 -0.655  -1.761  1.00 41.48 ? 238 PRO   A N   1 
ATOM   965  C  CA  . PRO   A 1 124 ? -28.007 0.574   -1.315  1.00 39.39 ? 238 PRO   A CA  1 
ATOM   966  C  C   . PRO   A 1 124 ? -28.671 0.424   0.043   1.00 38.12 ? 238 PRO   A C   1 
ATOM   967  O  O   . PRO   A 1 124 ? -29.122 -0.657  0.432   1.00 40.20 ? 238 PRO   A O   1 
ATOM   968  C  CB  . PRO   A 1 124 ? -29.046 0.827   -2.412  1.00 43.49 ? 238 PRO   A CB  1 
ATOM   969  C  CG  . PRO   A 1 124 ? -29.365 -0.540  -2.922  1.00 42.82 ? 238 PRO   A CG  1 
ATOM   970  C  CD  . PRO   A 1 124 ? -28.061 -1.292  -2.881  1.00 40.06 ? 238 PRO   A CD  1 
ATOM   971  N  N   . CYS   A 1 125 ? -28.737 1.543   0.761   1.00 36.11 ? 239 CYS   A N   1 
ATOM   972  C  CA  . CYS   A 1 125 ? -29.395 1.626   2.058   1.00 39.69 ? 239 CYS   A CA  1 
ATOM   973  C  C   . CYS   A 1 125 ? -30.422 2.748   2.008   1.00 36.49 ? 239 CYS   A C   1 
ATOM   974  O  O   . CYS   A 1 125 ? -30.084 3.882   1.658   1.00 37.01 ? 239 CYS   A O   1 
ATOM   975  C  CB  . CYS   A 1 125 ? -28.375 1.879   3.175   1.00 37.79 ? 239 CYS   A CB  1 
ATOM   976  S  SG  . CYS   A 1 125 ? -29.036 1.817   4.847   1.00 35.77 ? 239 CYS   A SG  1 
ATOM   977  N  N   . LYS   A 1 126 ? -31.671 2.433   2.360   1.00 38.12 ? 240 LYS   A N   1 
ATOM   978  C  CA  . LYS   A 1 126 ? -32.776 3.385   2.275   1.00 37.80 ? 240 LYS   A CA  1 
ATOM   979  C  C   . LYS   A 1 126 ? -32.921 4.259   3.512   1.00 41.94 ? 240 LYS   A C   1 
ATOM   980  O  O   . LYS   A 1 126 ? -33.486 5.355   3.417   1.00 39.89 ? 240 LYS   A O   1 
ATOM   981  C  CB  . LYS   A 1 126 ? -34.103 2.642   2.066   1.00 42.15 ? 240 LYS   A CB  1 
ATOM   982  C  CG  . LYS   A 1 126 ? -34.268 1.942   0.726   1.00 46.90 ? 240 LYS   A CG  1 
ATOM   983  C  CD  . LYS   A 1 126 ? -33.669 2.732   -0.421  1.00 48.88 ? 240 LYS   A CD  1 
ATOM   984  C  CE  . LYS   A 1 126 ? -34.756 3.404   -1.245  1.00 53.32 ? 240 LYS   A CE  1 
ATOM   985  N  NZ  . LYS   A 1 126 ? -34.310 3.625   -2.648  1.00 57.17 ? 240 LYS   A NZ  1 
ATOM   986  N  N   . ASN   A 1 127 ? -32.442 3.795   4.663   1.00 36.27 ? 241 ASN   A N   1 
ATOM   987  C  CA  . ASN   A 1 127 ? -32.654 4.449   5.952   1.00 36.62 ? 241 ASN   A CA  1 
ATOM   988  C  C   . ASN   A 1 127 ? -31.276 4.834   6.481   1.00 36.08 ? 241 ASN   A C   1 
ATOM   989  O  O   . ASN   A 1 127 ? -30.645 4.071   7.217   1.00 32.57 ? 241 ASN   A O   1 
ATOM   990  C  CB  . ASN   A 1 127 ? -33.414 3.512   6.907   1.00 40.49 ? 241 ASN   A CB  1 
ATOM   991  C  CG  . ASN   A 1 127 ? -33.773 4.172   8.219   1.00 43.41 ? 241 ASN   A CG  1 
ATOM   992  O  OD1 . ASN   A 1 127 ? -33.467 5.341   8.442   1.00 43.15 ? 241 ASN   A OD1 1 
ATOM   993  N  ND2 . ASN   A 1 127 ? -34.435 3.423   9.101   1.00 48.19 ? 241 ASN   A ND2 1 
ATOM   994  N  N   . VAL   A 1 128 ? -30.809 6.019   6.093   1.00 35.36 ? 242 VAL   A N   1 
ATOM   995  C  CA  . VAL   A 1 128 ? -29.452 6.468   6.373   1.00 32.07 ? 242 VAL   A CA  1 
ATOM   996  C  C   . VAL   A 1 128 ? -29.498 7.602   7.385   1.00 36.03 ? 242 VAL   A C   1 
ATOM   997  O  O   . VAL   A 1 128 ? -30.325 8.515   7.277   1.00 36.77 ? 242 VAL   A O   1 
ATOM   998  C  CB  . VAL   A 1 128 ? -28.727 6.918   5.089   1.00 36.66 ? 242 VAL   A CB  1 
ATOM   999  C  CG1 . VAL   A 1 128 ? -27.288 7.299   5.399   1.00 33.05 ? 242 VAL   A CG1 1 
ATOM   1000 C  CG2 . VAL   A 1 128 ? -28.783 5.820   4.033   1.00 37.39 ? 242 VAL   A CG2 1 
ATOM   1001 N  N   . SER   A 1 129 ? -28.610 7.533   8.372   1.00 28.81 ? 243 SER   A N   1 
ATOM   1002 C  CA  . SER   A 1 129 ? -28.386 8.605   9.326   1.00 30.61 ? 243 SER   A CA  1 
ATOM   1003 C  C   . SER   A 1 129 ? -26.914 8.986   9.303   1.00 31.64 ? 243 SER   A C   1 
ATOM   1004 O  O   . SER   A 1 129 ? -26.078 8.256   8.767   1.00 29.58 ? 243 SER   A O   1 
ATOM   1005 C  CB  . SER   A 1 129 ? -28.813 8.190   10.742  1.00 34.46 ? 243 SER   A CB  1 
ATOM   1006 O  OG  . SER   A 1 129 ? -28.093 7.053   11.190  1.00 29.46 ? 243 SER   A OG  1 
ATOM   1007 N  N   . SER   A 1 130 ? -26.596 10.139  9.891   1.00 28.92 ? 244 SER   A N   1 
ATOM   1008 C  CA  . SER   A 1 130 ? -25.217 10.580  10.041  1.00 29.40 ? 244 SER   A CA  1 
ATOM   1009 C  C   . SER   A 1 130 ? -24.885 10.693  11.521  1.00 29.16 ? 244 SER   A C   1 
ATOM   1010 O  O   . SER   A 1 130 ? -25.702 11.166  12.317  1.00 30.55 ? 244 SER   A O   1 
ATOM   1011 C  CB  . SER   A 1 130 ? -24.959 11.919  9.338   1.00 33.28 ? 244 SER   A CB  1 
ATOM   1012 O  OG  . SER   A 1 130 ? -25.626 12.983  9.991   1.00 37.56 ? 244 SER   A OG  1 
ATOM   1013 N  N   . VAL   A 1 131 ? -23.680 10.252  11.884  1.00 26.74 ? 245 VAL   A N   1 
ATOM   1014 C  CA  . VAL   A 1 131 ? -23.221 10.263  13.264  1.00 27.82 ? 245 VAL   A CA  1 
ATOM   1015 C  C   . VAL   A 1 131 ? -21.800 10.801  13.297  1.00 25.94 ? 245 VAL   A C   1 
ATOM   1016 O  O   . VAL   A 1 131 ? -21.088 10.795  12.292  1.00 25.95 ? 245 VAL   A O   1 
ATOM   1017 C  CB  . VAL   A 1 131 ? -23.274 8.860   13.906  1.00 28.96 ? 245 VAL   A CB  1 
ATOM   1018 C  CG1 . VAL   A 1 131 ? -24.699 8.335   13.922  1.00 32.11 ? 245 VAL   A CG1 1 
ATOM   1019 C  CG2 . VAL   A 1 131 ? -22.347 7.899   13.160  1.00 26.82 ? 245 VAL   A CG2 1 
ATOM   1020 N  N   . GLN   A 1 132 ? -21.398 11.288  14.472  1.00 25.49 ? 246 GLN   A N   1 
ATOM   1021 C  CA  . GLN   A 1 132 ? -20.027 11.730  14.684  1.00 30.50 ? 246 GLN   A CA  1 
ATOM   1022 C  C   . GLN   A 1 132 ? -19.106 10.583  15.069  1.00 27.75 ? 246 GLN   A C   1 
ATOM   1023 O  O   . GLN   A 1 132 ? -17.901 10.643  14.794  1.00 27.44 ? 246 GLN   A O   1 
ATOM   1024 C  CB  . GLN   A 1 132 ? -19.980 12.798  15.779  1.00 33.53 ? 246 GLN   A CB  1 
ATOM   1025 C  CG  . GLN   A 1 132 ? -21.055 13.860  15.651  1.00 40.57 ? 246 GLN   A CG  1 
ATOM   1026 C  CD  . GLN   A 1 132 ? -20.923 14.666  14.379  1.00 43.77 ? 246 GLN   A CD  1 
ATOM   1027 O  OE1 . GLN   A 1 132 ? -19.851 15.187  14.065  1.00 47.67 ? 246 GLN   A OE1 1 
ATOM   1028 N  NE2 . GLN   A 1 132 ? -22.017 14.771  13.633  1.00 46.71 ? 246 GLN   A NE2 1 
ATOM   1029 N  N   . CYS   A 1 133 ? -19.654 9.549   15.703  1.00 26.55 ? 247 CYS   A N   1 
ATOM   1030 C  CA  . CYS   A 1 133 ? -18.892 8.409   16.178  1.00 27.40 ? 247 CYS   A CA  1 
ATOM   1031 C  C   . CYS   A 1 133 ? -19.716 7.152   15.948  1.00 25.37 ? 247 CYS   A C   1 
ATOM   1032 O  O   . CYS   A 1 133 ? -20.951 7.191   15.975  1.00 25.17 ? 247 CYS   A O   1 
ATOM   1033 C  CB  . CYS   A 1 133 ? -18.574 8.533   17.676  1.00 26.71 ? 247 CYS   A CB  1 
ATOM   1034 S  SG  . CYS   A 1 133 ? -17.495 9.904   18.152  1.00 34.18 ? 247 CYS   A SG  1 
ATOM   1035 N  N   . THR   A 1 134 ? -19.030 6.033   15.733  1.00 22.59 ? 248 THR   A N   1 
ATOM   1036 C  CA  . THR   A 1 134 ? -19.706 4.746   15.765  1.00 24.82 ? 248 THR   A CA  1 
ATOM   1037 C  C   . THR   A 1 134 ? -20.143 4.440   17.193  1.00 24.83 ? 248 THR   A C   1 
ATOM   1038 O  O   . THR   A 1 134 ? -19.818 5.160   18.144  1.00 23.49 ? 248 THR   A O   1 
ATOM   1039 C  CB  . THR   A 1 134 ? -18.789 3.626   15.277  1.00 25.52 ? 248 THR   A CB  1 
ATOM   1040 O  OG1 . THR   A 1 134 ? -17.698 3.482   16.198  1.00 21.35 ? 248 THR   A OG1 1 
ATOM   1041 C  CG2 . THR   A 1 134 ? -18.245 3.933   13.874  1.00 25.53 ? 248 THR   A CG2 1 
ATOM   1042 N  N   . HIS   A 1 135 ? -20.886 3.347   17.350  1.00 24.93 ? 249 HIS   A N   1 
ATOM   1043 C  CA  . HIS   A 1 135 ? -21.126 2.828   18.685  1.00 27.65 ? 249 HIS   A CA  1 
ATOM   1044 C  C   . HIS   A 1 135 ? -19.834 2.220   19.238  1.00 24.26 ? 249 HIS   A C   1 
ATOM   1045 O  O   . HIS   A 1 135 ? -18.825 2.093   18.536  1.00 24.88 ? 249 HIS   A O   1 
ATOM   1046 C  CB  . HIS   A 1 135 ? -22.250 1.788   18.672  1.00 26.60 ? 249 HIS   A CB  1 
ATOM   1047 C  CG  . HIS   A 1 135 ? -21.882 0.494   18.017  1.00 27.20 ? 249 HIS   A CG  1 
ATOM   1048 N  ND1 . HIS   A 1 135 ? -21.746 0.355   16.654  1.00 28.52 ? 249 HIS   A ND1 1 
ATOM   1049 C  CD2 . HIS   A 1 135 ? -21.644 -0.729  18.545  1.00 28.81 ? 249 HIS   A CD2 1 
ATOM   1050 C  CE1 . HIS   A 1 135 ? -21.418 -0.893  16.371  1.00 27.96 ? 249 HIS   A CE1 1 
ATOM   1051 N  NE2 . HIS   A 1 135 ? -21.357 -1.574  17.500  1.00 28.68 ? 249 HIS   A NE2 1 
ATOM   1052 N  N   . GLY   A 1 136 ? -19.878 1.833   20.512  1.00 24.82 ? 250 GLY   A N   1 
ATOM   1053 C  CA  . GLY   A 1 136 ? -18.716 1.253   21.162  1.00 24.39 ? 250 GLY   A CA  1 
ATOM   1054 C  C   . GLY   A 1 136 ? -18.518 -0.186  20.705  1.00 25.23 ? 250 GLY   A C   1 
ATOM   1055 O  O   . GLY   A 1 136 ? -19.387 -1.043  20.937  1.00 24.72 ? 250 GLY   A O   1 
ATOM   1056 N  N   . ILE   A 1 137 ? -17.375 -0.472  20.078  1.00 23.28 ? 251 ILE   A N   1 
ATOM   1057 C  CA  . ILE   A 1 137 ? -17.054 -1.801  19.566  1.00 24.03 ? 251 ILE   A CA  1 
ATOM   1058 C  C   . ILE   A 1 137 ? -15.943 -2.395  20.419  1.00 24.03 ? 251 ILE   A C   1 
ATOM   1059 O  O   . ILE   A 1 137 ? -14.863 -1.803  20.544  1.00 21.21 ? 251 ILE   A O   1 
ATOM   1060 C  CB  . ILE   A 1 137 ? -16.646 -1.755  18.085  1.00 21.16 ? 251 ILE   A CB  1 
ATOM   1061 C  CG1 . ILE   A 1 137 ? -17.732 -1.062  17.255  1.00 23.56 ? 251 ILE   A CG1 1 
ATOM   1062 C  CG2 . ILE   A 1 137 ? -16.349 -3.160  17.567  1.00 22.23 ? 251 ILE   A CG2 1 
ATOM   1063 C  CD1 . ILE   A 1 137 ? -17.295 -0.744  15.830  1.00 24.27 ? 251 ILE   A CD1 1 
ATOM   1064 N  N   . LYS   A 1 138 ? -16.200 -3.576  20.984  1.00 20.08 ? 252 LYS   A N   1 
ATOM   1065 C  CA  . LYS   A 1 138 ? -15.172 -4.315  21.715  1.00 24.89 ? 252 LYS   A CA  1 
ATOM   1066 C  C   . LYS   A 1 138 ? -14.242 -5.008  20.726  1.00 22.74 ? 252 LYS   A C   1 
ATOM   1067 O  O   . LYS   A 1 138 ? -14.716 -5.749  19.865  1.00 21.62 ? 252 LYS   A O   1 
ATOM   1068 C  CB  . LYS   A 1 138 ? -15.808 -5.353  22.630  1.00 23.79 ? 252 LYS   A CB  1 
ATOM   1069 C  CG  . LYS   A 1 138 ? -16.421 -4.805  23.908  1.00 24.59 ? 252 LYS   A CG  1 
ATOM   1070 C  CD  . LYS   A 1 138 ? -16.849 -5.962  24.819  1.00 28.19 ? 252 LYS   A CD  1 
ATOM   1071 C  CE  . LYS   A 1 138 ? -17.398 -5.460  26.150  1.00 27.94 ? 252 LYS   A CE  1 
ATOM   1072 N  NZ  . LYS   A 1 138 ? -17.668 -6.591  27.083  1.00 27.63 ? 252 LYS   A NZ  1 
ATOM   1073 N  N   . PRO   A 1 139 ? -12.922 -4.791  20.810  1.00 23.49 ? 253 PRO   A N   1 
ATOM   1074 C  CA  . PRO   A 1 139 ? -12.006 -5.423  19.834  1.00 23.03 ? 253 PRO   A CA  1 
ATOM   1075 C  C   . PRO   A 1 139 ? -11.648 -6.852  20.221  1.00 24.89 ? 253 PRO   A C   1 
ATOM   1076 O  O   . PRO   A 1 139 ? -10.515 -7.174  20.599  1.00 24.84 ? 253 PRO   A O   1 
ATOM   1077 C  CB  . PRO   A 1 139 ? -10.793 -4.487  19.868  1.00 23.38 ? 253 PRO   A CB  1 
ATOM   1078 C  CG  . PRO   A 1 139 ? -10.781 -3.934  21.269  1.00 22.68 ? 253 PRO   A CG  1 
ATOM   1079 C  CD  . PRO   A 1 139 ? -12.226 -3.866  21.723  1.00 25.54 ? 253 PRO   A CD  1 
ATOM   1080 N  N   . VAL   A 1 140 ? -12.623 -7.751  20.121  1.00 23.67 ? 254 VAL   A N   1 
ATOM   1081 C  CA  . VAL   A 1 140 ? -12.414 -9.130  20.548  1.00 23.14 ? 254 VAL   A CA  1 
ATOM   1082 C  C   . VAL   A 1 140 ? -11.701 -9.897  19.442  1.00 23.20 ? 254 VAL   A C   1 
ATOM   1083 O  O   . VAL   A 1 140 ? -12.204 -10.003 18.317  1.00 23.39 ? 254 VAL   A O   1 
ATOM   1084 C  CB  . VAL   A 1 140 ? -13.739 -9.801  20.925  1.00 29.07 ? 254 VAL   A CB  1 
ATOM   1085 C  CG1 . VAL   A 1 140 ? -13.478 -11.186 21.474  1.00 27.08 ? 254 VAL   A CG1 1 
ATOM   1086 C  CG2 . VAL   A 1 140 ? -14.490 -8.943  21.949  1.00 22.76 ? 254 VAL   A CG2 1 
ATOM   1087 N  N   . VAL   A 1 141 ? -10.536 -10.450 19.768  1.00 24.18 ? 255 VAL   A N   1 
ATOM   1088 C  CA  . VAL   A 1 141 ? -9.747  -11.242 18.830  1.00 25.57 ? 255 VAL   A CA  1 
ATOM   1089 C  C   . VAL   A 1 141 ? -10.160 -12.706 18.961  1.00 23.07 ? 255 VAL   A C   1 
ATOM   1090 O  O   . VAL   A 1 141 ? -10.114 -13.279 20.055  1.00 22.92 ? 255 VAL   A O   1 
ATOM   1091 C  CB  . VAL   A 1 141 ? -8.243  -11.065 19.090  1.00 25.60 ? 255 VAL   A CB  1 
ATOM   1092 C  CG1 . VAL   A 1 141 ? -7.439  -11.939 18.155  1.00 24.00 ? 255 VAL   A CG1 1 
ATOM   1093 C  CG2 . VAL   A 1 141 ? -7.845  -9.599  18.943  1.00 25.45 ? 255 VAL   A CG2 1 
ATOM   1094 N  N   . SER   A 1 142 ? -10.572 -13.316 17.854  1.00 21.18 ? 256 SER   A N   1 
ATOM   1095 C  CA  . SER   A 1 142 ? -11.011 -14.704 17.894  1.00 27.47 ? 256 SER   A CA  1 
ATOM   1096 C  C   . SER   A 1 142 ? -11.050 -15.270 16.483  1.00 22.95 ? 256 SER   A C   1 
ATOM   1097 O  O   . SER   A 1 142 ? -11.001 -14.535 15.491  1.00 22.99 ? 256 SER   A O   1 
ATOM   1098 C  CB  . SER   A 1 142 ? -12.389 -14.832 18.547  1.00 25.12 ? 256 SER   A CB  1 
ATOM   1099 O  OG  . SER   A 1 142 ? -13.386 -14.325 17.679  1.00 24.23 ? 256 SER   A OG  1 
ATOM   1100 N  N   . THR   A 1 143 ? -11.142 -16.596 16.414  1.00 22.31 ? 257 THR   A N   1 
ATOM   1101 C  CA  . THR   A 1 143 ? -11.401 -17.325 15.183  1.00 24.19 ? 257 THR   A CA  1 
ATOM   1102 C  C   . THR   A 1 143 ? -12.688 -18.129 15.324  1.00 23.24 ? 257 THR   A C   1 
ATOM   1103 O  O   . THR   A 1 143 ? -13.141 -18.419 16.436  1.00 22.39 ? 257 THR   A O   1 
ATOM   1104 C  CB  . THR   A 1 143 ? -10.238 -18.264 14.827  1.00 25.07 ? 257 THR   A CB  1 
ATOM   1105 O  OG1 . THR   A 1 143 ? -10.161 -19.323 15.789  1.00 25.17 ? 257 THR   A OG1 1 
ATOM   1106 C  CG2 . THR   A 1 143 ? -8.922  -17.495 14.813  1.00 24.06 ? 257 THR   A CG2 1 
ATOM   1107 N  N   . GLN   A 1 144 ? -13.265 -18.493 14.172  1.00 20.81 ? 258 GLN   A N   1 
ATOM   1108 C  CA  . GLN   A 1 144 ? -14.442 -19.359 14.078  1.00 23.36 ? 258 GLN   A CA  1 
ATOM   1109 C  C   . GLN   A 1 144 ? -15.717 -18.714 14.606  1.00 23.93 ? 258 GLN   A C   1 
ATOM   1110 O  O   . GLN   A 1 144 ? -16.729 -18.668 13.897  1.00 22.25 ? 258 GLN   A O   1 
ATOM   1111 C  CB  . GLN   A 1 144 ? -14.209 -20.683 14.816  1.00 23.16 ? 258 GLN   A CB  1 
ATOM   1112 C  CG  . GLN   A 1 144 ? -13.032 -21.483 14.287  1.00 24.58 ? 258 GLN   A CG  1 
ATOM   1113 C  CD  . GLN   A 1 144 ? -13.118 -22.941 14.664  1.00 26.02 ? 258 GLN   A CD  1 
ATOM   1114 O  OE1 . GLN   A 1 144 ? -14.096 -23.385 15.271  1.00 23.75 ? 258 GLN   A OE1 1 
ATOM   1115 N  NE2 . GLN   A 1 144 ? -12.092 -23.703 14.301  1.00 24.03 ? 258 GLN   A NE2 1 
ATOM   1116 N  N   . LEU   A 1 145 ? -15.693 -18.240 15.849  1.00 20.29 ? 259 LEU   A N   1 
ATOM   1117 C  CA  . LEU   A 1 145 ? -16.864 -17.665 16.496  1.00 22.36 ? 259 LEU   A CA  1 
ATOM   1118 C  C   . LEU   A 1 145 ? -16.596 -16.202 16.811  1.00 22.16 ? 259 LEU   A C   1 
ATOM   1119 O  O   . LEU   A 1 145 ? -15.532 -15.864 17.343  1.00 23.73 ? 259 LEU   A O   1 
ATOM   1120 C  CB  . LEU   A 1 145 ? -17.208 -18.425 17.784  1.00 21.52 ? 259 LEU   A CB  1 
ATOM   1121 C  CG  . LEU   A 1 145 ? -17.467 -19.928 17.646  1.00 25.58 ? 259 LEU   A CG  1 
ATOM   1122 C  CD1 . LEU   A 1 145 ? -17.718 -20.559 19.019  1.00 25.22 ? 259 LEU   A CD1 1 
ATOM   1123 C  CD2 . LEU   A 1 145 ? -18.627 -20.189 16.707  1.00 23.65 ? 259 LEU   A CD2 1 
ATOM   1124 N  N   . LEU   A 1 146 ? -17.553 -15.339 16.483  1.00 20.93 ? 260 LEU   A N   1 
ATOM   1125 C  CA  . LEU   A 1 146 ? -17.455 -13.927 16.819  1.00 21.17 ? 260 LEU   A CA  1 
ATOM   1126 C  C   . LEU   A 1 146 ? -18.092 -13.725 18.187  1.00 25.23 ? 260 LEU   A C   1 
ATOM   1127 O  O   . LEU   A 1 146 ? -19.232 -14.150 18.411  1.00 22.61 ? 260 LEU   A O   1 
ATOM   1128 C  CB  . LEU   A 1 146 ? -18.153 -13.068 15.761  1.00 21.03 ? 260 LEU   A CB  1 
ATOM   1129 C  CG  . LEU   A 1 146 ? -17.497 -13.119 14.368  1.00 20.42 ? 260 LEU   A CG  1 
ATOM   1130 C  CD1 . LEU   A 1 146 ? -18.326 -12.377 13.339  1.00 21.15 ? 260 LEU   A CD1 1 
ATOM   1131 C  CD2 . LEU   A 1 146 ? -16.069 -12.572 14.418  1.00 24.91 ? 260 LEU   A CD2 1 
ATOM   1132 N  N   . LEU   A 1 147 ? -17.361 -13.086 19.102  1.00 23.46 ? 261 LEU   A N   1 
ATOM   1133 C  CA  . LEU   A 1 147 ? -17.766 -13.035 20.500  1.00 23.22 ? 261 LEU   A CA  1 
ATOM   1134 C  C   . LEU   A 1 147 ? -18.033 -11.611 20.963  1.00 22.57 ? 261 LEU   A C   1 
ATOM   1135 O  O   . LEU   A 1 147 ? -17.347 -10.671 20.552  1.00 21.54 ? 261 LEU   A O   1 
ATOM   1136 C  CB  . LEU   A 1 147 ? -16.711 -13.674 21.407  1.00 22.85 ? 261 LEU   A CB  1 
ATOM   1137 C  CG  . LEU   A 1 147 ? -16.266 -15.095 21.056  1.00 25.83 ? 261 LEU   A CG  1 
ATOM   1138 C  CD1 . LEU   A 1 147 ? -15.106 -15.509 21.949  1.00 25.20 ? 261 LEU   A CD1 1 
ATOM   1139 C  CD2 . LEU   A 1 147 ? -17.427 -16.068 21.179  1.00 24.81 ? 261 LEU   A CD2 1 
ATOM   1140 N  N   . ASN   A 1 148 ? -19.033 -11.470 21.838  1.00 22.14 ? 262 ASN   A N   1 
ATOM   1141 C  CA  . ASN   A 1 148 ? -19.322 -10.210 22.519  1.00 24.30 ? 262 ASN   A CA  1 
ATOM   1142 C  C   . ASN   A 1 148 ? -19.619 -9.067  21.558  1.00 24.76 ? 262 ASN   A C   1 
ATOM   1143 O  O   . ASN   A 1 148 ? -19.374 -7.901  21.876  1.00 22.97 ? 262 ASN   A O   1 
ATOM   1144 C  CB  . ASN   A 1 148 ? -18.183 -9.820  23.458  1.00 25.12 ? 262 ASN   A CB  1 
ATOM   1145 C  CG  . ASN   A 1 148 ? -18.169 -10.639 24.723  1.00 25.88 ? 262 ASN   A CG  1 
ATOM   1146 O  OD1 . ASN   A 1 148 ? -19.071 -11.441 24.969  1.00 23.31 ? 262 ASN   A OD1 1 
ATOM   1147 N  ND2 . ASN   A 1 148 ? -17.158 -10.419 25.554  1.00 25.57 ? 262 ASN   A ND2 1 
ATOM   1148 N  N   . GLY   A 1 149 ? -20.151 -9.375  20.384  1.00 21.75 ? 263 GLY   A N   1 
ATOM   1149 C  CA  . GLY   A 1 149 ? -20.493 -8.367  19.407  1.00 23.41 ? 263 GLY   A CA  1 
ATOM   1150 C  C   . GLY   A 1 149 ? -21.932 -7.914  19.520  1.00 25.57 ? 263 GLY   A C   1 
ATOM   1151 O  O   . GLY   A 1 149 ? -22.612 -8.148  20.524  1.00 23.71 ? 263 GLY   A O   1 
ATOM   1152 N  N   . SER   A 1 150 ? -22.395 -7.243  18.473  1.00 22.36 ? 264 SER   A N   1 
ATOM   1153 C  CA  . SER   A 1 150 ? -23.790 -6.871  18.327  1.00 24.35 ? 264 SER   A CA  1 
ATOM   1154 C  C   . SER   A 1 150 ? -24.544 -7.970  17.584  1.00 27.51 ? 264 SER   A C   1 
ATOM   1155 O  O   . SER   A 1 150 ? -23.955 -8.855  16.957  1.00 25.34 ? 264 SER   A O   1 
ATOM   1156 C  CB  . SER   A 1 150 ? -23.917 -5.545  17.580  1.00 29.14 ? 264 SER   A CB  1 
ATOM   1157 O  OG  . SER   A 1 150 ? -23.659 -5.734  16.202  1.00 32.34 ? 264 SER   A OG  1 
ATOM   1158 N  N   . LEU   A 1 151 ? -25.869 -7.901  17.651  1.00 23.69 ? 265 LEU   A N   1 
ATOM   1159 C  CA  . LEU   A 1 151 ? -26.735 -8.879  17.010  1.00 27.13 ? 265 LEU   A CA  1 
ATOM   1160 C  C   . LEU   A 1 151 ? -27.481 -8.235  15.852  1.00 25.16 ? 265 LEU   A C   1 
ATOM   1161 O  O   . LEU   A 1 151 ? -27.754 -7.033  15.864  1.00 24.76 ? 265 LEU   A O   1 
ATOM   1162 C  CB  . LEU   A 1 151 ? -27.744 -9.457  18.009  1.00 25.44 ? 265 LEU   A CB  1 
ATOM   1163 C  CG  . LEU   A 1 151 ? -27.171 -10.344 19.118  1.00 27.97 ? 265 LEU   A CG  1 
ATOM   1164 C  CD1 . LEU   A 1 151 ? -28.259 -10.703 20.136  1.00 32.59 ? 265 LEU   A CD1 1 
ATOM   1165 C  CD2 . LEU   A 1 151 ? -26.531 -11.589 18.535  1.00 24.28 ? 265 LEU   A CD2 1 
ATOM   1166 N  N   . ALA   A 1 152 ? -27.801 -9.040  14.842  1.00 25.75 ? 266 ALA   A N   1 
ATOM   1167 C  CA  . ALA   A 1 152 ? -28.709 -8.581  13.804  1.00 27.68 ? 266 ALA   A CA  1 
ATOM   1168 C  C   . ALA   A 1 152 ? -30.082 -8.332  14.414  1.00 31.39 ? 266 ALA   A C   1 
ATOM   1169 O  O   . ALA   A 1 152 ? -30.514 -9.047  15.320  1.00 30.78 ? 266 ALA   A O   1 
ATOM   1170 C  CB  . ALA   A 1 152 ? -28.795 -9.604  12.674  1.00 24.68 ? 266 ALA   A CB  1 
ATOM   1171 N  N   . GLU   A 1 153 ? -30.768 -7.303  13.913  1.00 29.87 ? 267 GLU   A N   1 
ATOM   1172 C  CA  . GLU   A 1 153 ? -31.997 -6.844  14.547  1.00 35.05 ? 267 GLU   A CA  1 
ATOM   1173 C  C   . GLU   A 1 153 ? -33.211 -7.678  14.169  1.00 34.30 ? 267 GLU   A C   1 
ATOM   1174 O  O   . GLU   A 1 153 ? -34.126 -7.831  14.986  1.00 35.72 ? 267 GLU   A O   1 
ATOM   1175 C  CB  . GLU   A 1 153 ? -32.251 -5.384  14.191  1.00 35.34 ? 267 GLU   A CB  1 
ATOM   1176 C  CG  . GLU   A 1 153 ? -31.341 -4.411  14.890  1.00 40.63 ? 267 GLU   A CG  1 
ATOM   1177 C  CD  . GLU   A 1 153 ? -31.811 -2.987  14.720  1.00 43.56 ? 267 GLU   A CD  1 
ATOM   1178 O  OE1 . GLU   A 1 153 ? -31.435 -2.355  13.712  1.00 46.08 ? 267 GLU   A OE1 1 
ATOM   1179 O  OE2 . GLU   A 1 153 ? -32.578 -2.513  15.585  1.00 47.08 ? 267 GLU   A OE2 1 
ATOM   1180 N  N   . GLU   A 1 154 ? -33.254 -8.209  12.946  1.00 34.70 ? 268 GLU   A N   1 
ATOM   1181 C  CA  . GLU   A 1 154 ? -34.418 -8.944  12.488  1.00 35.02 ? 268 GLU   A CA  1 
ATOM   1182 C  C   . GLU   A 1 154 ? -33.983 -10.382 12.213  1.00 34.37 ? 268 GLU   A C   1 
ATOM   1183 O  O   . GLU   A 1 154 ? -33.909 -11.194 13.147  1.00 33.36 ? 268 GLU   A O   1 
ATOM   1184 C  CB  . GLU   A 1 154 ? -35.044 -8.261  11.267  1.00 40.82 ? 268 GLU   A CB  1 
ATOM   1185 C  CG  . GLU   A 1 154 ? -36.132 -7.261  11.616  1.00 47.35 ? 268 GLU   A CG  1 
ATOM   1186 C  CD  . GLU   A 1 154 ? -36.712 -6.574  10.394  1.00 57.36 ? 268 GLU   A CD  1 
ATOM   1187 O  OE1 . GLU   A 1 154 ? -36.291 -6.898  9.262   1.00 54.57 ? 268 GLU   A OE1 1 
ATOM   1188 O  OE2 . GLU   A 1 154 ? -37.583 -5.699  10.567  1.00 57.23 ? 268 GLU   A OE2 1 
ATOM   1189 N  N   . GLU   A 1 155 ? -33.689 -10.724 10.972  1.00 33.32 ? 269 GLU   A N   1 
ATOM   1190 C  CA  . GLU   A 1 155 ? -33.327 -12.082 10.617  1.00 33.59 ? 269 GLU   A CA  1 
ATOM   1191 C  C   . GLU   A 1 155 ? -31.824 -12.290 10.748  1.00 30.92 ? 269 GLU   A C   1 
ATOM   1192 O  O   . GLU   A 1 155 ? -31.041 -11.343 10.853  1.00 29.00 ? 269 GLU   A O   1 
ATOM   1193 C  CB  . GLU   A 1 155 ? -33.772 -12.385 9.189   1.00 35.66 ? 269 GLU   A CB  1 
ATOM   1194 C  CG  . GLU   A 1 155 ? -35.216 -11.995 8.914   1.00 42.62 ? 269 GLU   A CG  1 
ATOM   1195 C  CD  . GLU   A 1 155 ? -35.984 -13.076 8.190   1.00 42.00 ? 269 GLU   A CD  1 
ATOM   1196 O  OE1 . GLU   A 1 155 ? -35.343 -13.949 7.568   1.00 44.15 ? 269 GLU   A OE1 1 
ATOM   1197 O  OE2 . GLU   A 1 155 ? -37.231 -13.039 8.232   1.00 52.58 ? 269 GLU   A OE2 1 
ATOM   1198 N  N   . ILE   A 1 156 ? -31.428 -13.563 10.748  1.00 28.86 ? 270 ILE   A N   1 
ATOM   1199 C  CA  . ILE   A 1 156 ? -30.024 -13.908 10.590  1.00 30.68 ? 270 ILE   A CA  1 
ATOM   1200 C  C   . ILE   A 1 156 ? -29.552 -13.377 9.242   1.00 31.10 ? 270 ILE   A C   1 
ATOM   1201 O  O   . ILE   A 1 156 ? -30.256 -13.491 8.227   1.00 29.59 ? 270 ILE   A O   1 
ATOM   1202 C  CB  . ILE   A 1 156 ? -29.861 -15.433 10.683  1.00 26.92 ? 270 ILE   A CB  1 
ATOM   1203 C  CG1 . ILE   A 1 156 ? -30.228 -15.928 12.082  1.00 29.32 ? 270 ILE   A CG1 1 
ATOM   1204 C  CG2 . ILE   A 1 156 ? -28.433 -15.843 10.341  1.00 28.47 ? 270 ILE   A CG2 1 
ATOM   1205 C  CD1 . ILE   A 1 156 ? -30.044 -17.422 12.261  1.00 32.39 ? 270 ILE   A CD1 1 
ATOM   1206 N  N   . ILE   A 1 157 ? -28.353 -12.796 9.215   1.00 26.76 ? 271 ILE   A N   1 
ATOM   1207 C  CA  . ILE   A 1 157 ? -27.815 -12.178 8.006   1.00 30.01 ? 271 ILE   A CA  1 
ATOM   1208 C  C   . ILE   A 1 157 ? -26.567 -12.932 7.560   1.00 27.67 ? 271 ILE   A C   1 
ATOM   1209 O  O   . ILE   A 1 157 ? -25.663 -13.183 8.366   1.00 25.56 ? 271 ILE   A O   1 
ATOM   1210 C  CB  . ILE   A 1 157 ? -27.497 -10.685 8.210   1.00 29.97 ? 271 ILE   A CB  1 
ATOM   1211 C  CG1 . ILE   A 1 157 ? -28.681 -9.957  8.846   1.00 31.11 ? 271 ILE   A CG1 1 
ATOM   1212 C  CG2 . ILE   A 1 157 ? -27.111 -10.036 6.881   1.00 30.64 ? 271 ILE   A CG2 1 
ATOM   1213 C  CD1 . ILE   A 1 157 ? -29.780 -9.600  7.867   1.00 33.79 ? 271 ILE   A CD1 1 
ATOM   1214 N  N   . ILE   A 1 158 ? -26.519 -13.279 6.275   1.00 27.34 ? 272 ILE   A N   1 
ATOM   1215 C  CA  . ILE   A 1 158 ? -25.325 -13.817 5.634   1.00 25.49 ? 272 ILE   A CA  1 
ATOM   1216 C  C   . ILE   A 1 158 ? -24.588 -12.661 4.972   1.00 27.93 ? 272 ILE   A C   1 
ATOM   1217 O  O   . ILE   A 1 158 ? -25.180 -11.907 4.189   1.00 30.11 ? 272 ILE   A O   1 
ATOM   1218 C  CB  . ILE   A 1 158 ? -25.684 -14.895 4.595   1.00 31.83 ? 272 ILE   A CB  1 
ATOM   1219 C  CG1 . ILE   A 1 158 ? -26.478 -16.038 5.239   1.00 31.86 ? 272 ILE   A CG1 1 
ATOM   1220 C  CG2 . ILE   A 1 158 ? -24.419 -15.442 3.945   1.00 28.44 ? 272 ILE   A CG2 1 
ATOM   1221 C  CD1 . ILE   A 1 158 ? -25.922 -16.515 6.550   1.00 30.32 ? 272 ILE   A CD1 1 
ATOM   1222 N  N   . ARG   A 1 159 ? -23.299 -12.519 5.272   1.00 28.20 ? 273 ARG   A N   1 
ATOM   1223 C  CA  . ARG   A 1 159 ? -22.482 -11.447 4.721   1.00 25.24 ? 273 ARG   A CA  1 
ATOM   1224 C  C   . ARG   A 1 159 ? -21.289 -12.044 3.984   1.00 27.47 ? 273 ARG   A C   1 
ATOM   1225 O  O   . ARG   A 1 159 ? -20.583 -12.905 4.523   1.00 26.15 ? 273 ARG   A O   1 
ATOM   1226 C  CB  . ARG   A 1 159 ? -21.989 -10.505 5.819   1.00 27.00 ? 273 ARG   A CB  1 
ATOM   1227 C  CG  . ARG   A 1 159 ? -23.091 -9.874  6.663   1.00 25.95 ? 273 ARG   A CG  1 
ATOM   1228 C  CD  . ARG   A 1 159 ? -22.506 -8.902  7.691   1.00 26.04 ? 273 ARG   A CD  1 
ATOM   1229 N  NE  . ARG   A 1 159 ? -23.499 -8.487  8.678   1.00 25.28 ? 273 ARG   A NE  1 
ATOM   1230 C  CZ  . ARG   A 1 159 ? -24.549 -7.721  8.417   1.00 29.11 ? 273 ARG   A CZ  1 
ATOM   1231 N  NH1 . ARG   A 1 159 ? -24.774 -7.248  7.203   1.00 25.41 ? 273 ARG   A NH1 1 
ATOM   1232 N  NH2 . ARG   A 1 159 ? -25.396 -7.425  9.399   1.00 27.32 ? 273 ARG   A NH2 1 
ATOM   1233 N  N   . SER   A 1 160 ? -21.060 -11.584 2.757   1.00 28.25 ? 274 SER   A N   1 
ATOM   1234 C  CA  . SER   A 1 160 ? -19.903 -12.026 1.991   1.00 25.47 ? 274 SER   A CA  1 
ATOM   1235 C  C   . SER   A 1 160 ? -19.645 -11.051 0.852   1.00 28.36 ? 274 SER   A C   1 
ATOM   1236 O  O   . SER   A 1 160 ? -20.589 -10.530 0.254   1.00 29.76 ? 274 SER   A O   1 
ATOM   1237 C  CB  . SER   A 1 160 ? -20.102 -13.441 1.432   1.00 33.08 ? 274 SER   A CB  1 
ATOM   1238 O  OG  . SER   A 1 160 ? -19.185 -13.701 0.380   1.00 30.00 ? 274 SER   A OG  1 
ATOM   1239 N  N   . GLU   A 1 161 ? -18.362 -10.818 0.553   1.00 29.88 ? 275 GLU   A N   1 
ATOM   1240 C  CA  . GLU   A 1 161 ? -18.015 -9.972  -0.585  1.00 34.35 ? 275 GLU   A CA  1 
ATOM   1241 C  C   . GLU   A 1 161 ? -18.511 -10.570 -1.895  1.00 34.49 ? 275 GLU   A C   1 
ATOM   1242 O  O   . GLU   A 1 161 ? -18.741 -9.843  -2.867  1.00 37.57 ? 275 GLU   A O   1 
ATOM   1243 C  CB  . GLU   A 1 161 ? -16.503 -9.763  -0.650  1.00 33.69 ? 275 GLU   A CB  1 
ATOM   1244 C  CG  . GLU   A 1 161 ? -16.070 -8.831  -1.778  1.00 34.31 ? 275 GLU   A CG  1 
ATOM   1245 C  CD  . GLU   A 1 161 ? -14.626 -8.396  -1.663  1.00 38.66 ? 275 GLU   A CD  1 
ATOM   1246 O  OE1 . GLU   A 1 161 ? -13.832 -9.128  -1.034  1.00 41.18 ? 275 GLU   A OE1 1 
ATOM   1247 O  OE2 . GLU   A 1 161 ? -14.285 -7.316  -2.197  1.00 45.19 ? 275 GLU   A OE2 1 
ATOM   1248 N  N   . ASN   A 1 162 ? -18.663 -11.889 -1.944  1.00 31.90 ? 276 ASN   A N   1 
ATOM   1249 C  CA  . ASN   A 1 162 ? -19.117 -12.598 -3.135  1.00 37.76 ? 276 ASN   A CA  1 
ATOM   1250 C  C   . ASN   A 1 162 ? -19.438 -14.046 -2.785  1.00 35.97 ? 276 ASN   A C   1 
ATOM   1251 O  O   . ASN   A 1 162 ? -18.547 -14.900 -2.750  1.00 35.08 ? 276 ASN   A O   1 
ATOM   1252 C  CB  . ASN   A 1 162 ? -18.064 -12.520 -4.246  1.00 39.06 ? 276 ASN   A CB  1 
ATOM   1253 C  CG  . ASN   A 1 162 ? -18.519 -13.177 -5.534  1.00 39.27 ? 276 ASN   A CG  1 
ATOM   1254 O  OD1 . ASN   A 1 162 ? -19.661 -13.627 -5.650  1.00 39.40 ? 276 ASN   A OD1 1 
ATOM   1255 N  ND2 . ASN   A 1 162 ? -17.619 -13.243 -6.510  1.00 44.10 ? 276 ASN   A ND2 1 
ATOM   1256 N  N   . LEU   A 1 163 ? -20.717 -14.321 -2.516  1.00 32.89 ? 277 LEU   A N   1 
ATOM   1257 C  CA  . LEU   A 1 163 ? -21.134 -15.652 -2.088  1.00 35.13 ? 277 LEU   A CA  1 
ATOM   1258 C  C   . LEU   A 1 163 ? -20.725 -16.719 -3.097  1.00 42.14 ? 277 LEU   A C   1 
ATOM   1259 O  O   . LEU   A 1 163 ? -20.327 -17.826 -2.716  1.00 37.02 ? 277 LEU   A O   1 
ATOM   1260 C  CB  . LEU   A 1 163 ? -22.647 -15.668 -1.877  1.00 36.53 ? 277 LEU   A CB  1 
ATOM   1261 C  CG  . LEU   A 1 163 ? -23.234 -16.421 -0.684  1.00 41.35 ? 277 LEU   A CG  1 
ATOM   1262 C  CD1 . LEU   A 1 163 ? -22.296 -16.360 0.514   1.00 37.09 ? 277 LEU   A CD1 1 
ATOM   1263 C  CD2 . LEU   A 1 163 ? -24.598 -15.841 -0.324  1.00 39.26 ? 277 LEU   A CD2 1 
ATOM   1264 N  N   . THR   A 1 164 ? -20.811 -16.401 -4.392  1.00 38.41 ? 278 THR   A N   1 
ATOM   1265 C  CA  . THR   A 1 164 ? -20.498 -17.382 -5.425  1.00 40.98 ? 278 THR   A CA  1 
ATOM   1266 C  C   . THR   A 1 164 ? -19.038 -17.816 -5.372  1.00 40.06 ? 278 THR   A C   1 
ATOM   1267 O  O   . THR   A 1 164 ? -18.714 -18.941 -5.760  1.00 44.26 ? 278 THR   A O   1 
ATOM   1268 C  CB  . THR   A 1 164 ? -20.831 -16.808 -6.802  1.00 39.16 ? 278 THR   A CB  1 
ATOM   1269 O  OG1 . THR   A 1 164 ? -22.244 -16.589 -6.899  1.00 42.39 ? 278 THR   A OG1 1 
ATOM   1270 C  CG2 . THR   A 1 164 ? -20.386 -17.762 -7.897  1.00 49.30 ? 278 THR   A CG2 1 
ATOM   1271 N  N   . ASN   A 1 165 ? -18.148 -16.946 -4.900  1.00 39.21 ? 279 ASN   A N   1 
ATOM   1272 C  CA  . ASN   A 1 165 ? -16.724 -17.246 -4.807  1.00 38.97 ? 279 ASN   A CA  1 
ATOM   1273 C  C   . ASN   A 1 165 ? -16.475 -17.955 -3.479  1.00 41.08 ? 279 ASN   A C   1 
ATOM   1274 O  O   . ASN   A 1 165 ? -16.607 -17.352 -2.410  1.00 38.82 ? 279 ASN   A O   1 
ATOM   1275 C  CB  . ASN   A 1 165 ? -15.895 -15.966 -4.930  1.00 38.64 ? 279 ASN   A CB  1 
ATOM   1276 C  CG  . ASN   A 1 165 ? -14.408 -16.220 -4.830  1.00 40.79 ? 279 ASN   A CG  1 
ATOM   1277 O  OD1 . ASN   A 1 165 ? -13.967 -17.302 -4.432  1.00 42.27 ? 279 ASN   A OD1 1 
ATOM   1278 N  ND2 . ASN   A 1 165 ? -13.620 -15.212 -5.181  1.00 39.94 ? 279 ASN   A ND2 1 
ATOM   1279 N  N   . ASN   A 1 166 ? -16.085 -19.231 -3.546  1.00 37.63 ? 280 ASN   A N   1 
ATOM   1280 C  CA  . ASN   A 1 166 ? -15.924 -20.024 -2.332  1.00 37.33 ? 280 ASN   A CA  1 
ATOM   1281 C  C   . ASN   A 1 166 ? -14.716 -19.595 -1.509  1.00 37.92 ? 280 ASN   A C   1 
ATOM   1282 O  O   . ASN   A 1 166 ? -14.618 -19.973 -0.337  1.00 38.54 ? 280 ASN   A O   1 
ATOM   1283 C  CB  . ASN   A 1 166 ? -15.805 -21.510 -2.679  1.00 42.54 ? 280 ASN   A CB  1 
ATOM   1284 C  CG  . ASN   A 1 166 ? -14.606 -21.805 -3.556  1.00 45.73 ? 280 ASN   A CG  1 
ATOM   1285 O  OD1 . ASN   A 1 166 ? -13.474 -21.894 -3.074  1.00 49.62 ? 280 ASN   A OD1 1 
ATOM   1286 N  ND2 . ASN   A 1 166 ? -14.847 -21.971 -4.850  1.00 52.15 ? 280 ASN   A ND2 1 
ATOM   1287 N  N   . ALA   A 1 167 ? -13.788 -18.834 -2.089  1.00 36.84 ? 281 ALA   A N   1 
ATOM   1288 C  CA  . ALA   A 1 167 ? -12.632 -18.364 -1.339  1.00 36.82 ? 281 ALA   A CA  1 
ATOM   1289 C  C   . ALA   A 1 167 ? -12.953 -17.186 -0.428  1.00 34.08 ? 281 ALA   A C   1 
ATOM   1290 O  O   . ALA   A 1 167 ? -12.120 -16.830 0.409   1.00 38.76 ? 281 ALA   A O   1 
ATOM   1291 C  CB  . ALA   A 1 167 ? -11.503 -17.975 -2.295  1.00 38.38 ? 281 ALA   A CB  1 
ATOM   1292 N  N   . LYS   A 1 168 ? -14.131 -16.584 -0.558  1.00 33.02 ? 282 LYS   A N   1 
ATOM   1293 C  CA  . LYS   A 1 168 ? -14.482 -15.390 0.200   1.00 35.22 ? 282 LYS   A CA  1 
ATOM   1294 C  C   . LYS   A 1 168 ? -15.145 -15.787 1.511   1.00 33.41 ? 282 LYS   A C   1 
ATOM   1295 O  O   . LYS   A 1 168 ? -16.142 -16.515 1.515   1.00 32.44 ? 282 LYS   A O   1 
ATOM   1296 C  CB  . LYS   A 1 168 ? -15.390 -14.479 -0.625  1.00 35.38 ? 282 LYS   A CB  1 
ATOM   1297 C  CG  . LYS   A 1 168 ? -14.677 -13.832 -1.809  1.00 34.84 ? 282 LYS   A CG  1 
ATOM   1298 C  CD  . LYS   A 1 168 ? -13.547 -12.935 -1.341  1.00 39.76 ? 282 LYS   A CD  1 
ATOM   1299 C  CE  . LYS   A 1 168 ? -12.981 -12.093 -2.484  1.00 43.61 ? 282 LYS   A CE  1 
ATOM   1300 N  NZ  . LYS   A 1 168 ? -11.932 -11.139 -2.020  1.00 40.87 ? 282 LYS   A NZ  1 
ATOM   1301 N  N   . THR   A 1 169 ? -14.587 -15.300 2.615   1.00 35.39 ? 283 THR   A N   1 
ATOM   1302 C  CA  . THR   A 1 169 ? -15.111 -15.615 3.934   1.00 29.63 ? 283 THR   A CA  1 
ATOM   1303 C  C   . THR   A 1 169 ? -16.558 -15.160 4.078   1.00 30.27 ? 283 THR   A C   1 
ATOM   1304 O  O   . THR   A 1 169 ? -16.939 -14.072 3.640   1.00 30.58 ? 283 THR   A O   1 
ATOM   1305 C  CB  . THR   A 1 169 ? -14.246 -14.956 5.009   1.00 32.33 ? 283 THR   A CB  1 
ATOM   1306 O  OG1 . THR   A 1 169 ? -12.915 -15.483 4.947   1.00 34.81 ? 283 THR   A OG1 1 
ATOM   1307 C  CG2 . THR   A 1 169 ? -14.837 -15.204 6.401   1.00 30.84 ? 283 THR   A CG2 1 
ATOM   1308 N  N   . ILE   A 1 170 ? -17.359 -16.007 4.712   1.00 26.96 ? 284 ILE   A N   1 
ATOM   1309 C  CA  . ILE   A 1 170 ? -18.752 -15.719 5.023   1.00 27.71 ? 284 ILE   A CA  1 
ATOM   1310 C  C   . ILE   A 1 170 ? -18.821 -15.263 6.471   1.00 28.40 ? 284 ILE   A C   1 
ATOM   1311 O  O   . ILE   A 1 170 ? -18.222 -15.888 7.356   1.00 27.94 ? 284 ILE   A O   1 
ATOM   1312 C  CB  . ILE   A 1 170 ? -19.631 -16.962 4.810   1.00 29.97 ? 284 ILE   A CB  1 
ATOM   1313 C  CG1 . ILE   A 1 170 ? -19.802 -17.271 3.318   1.00 30.68 ? 284 ILE   A CG1 1 
ATOM   1314 C  CG2 . ILE   A 1 170 ? -21.000 -16.765 5.461   1.00 29.30 ? 284 ILE   A CG2 1 
ATOM   1315 C  CD1 . ILE   A 1 170 ? -20.265 -18.690 3.051   1.00 35.92 ? 284 ILE   A CD1 1 
ATOM   1316 N  N   . ILE   A 1 171 ? -19.538 -14.174 6.722   1.00 27.45 ? 285 ILE   A N   1 
ATOM   1317 C  CA  . ILE   A 1 171 ? -19.833 -13.735 8.079   1.00 25.40 ? 285 ILE   A CA  1 
ATOM   1318 C  C   . ILE   A 1 171 ? -21.311 -13.980 8.329   1.00 25.04 ? 285 ILE   A C   1 
ATOM   1319 O  O   . ILE   A 1 171 ? -22.168 -13.448 7.611   1.00 24.47 ? 285 ILE   A O   1 
ATOM   1320 C  CB  . ILE   A 1 171 ? -19.472 -12.261 8.308   1.00 27.73 ? 285 ILE   A CB  1 
ATOM   1321 C  CG1 . ILE   A 1 171 ? -17.966 -12.046 8.165   1.00 24.61 ? 285 ILE   A CG1 1 
ATOM   1322 C  CG2 . ILE   A 1 171 ? -19.920 -11.827 9.701   1.00 27.73 ? 285 ILE   A CG2 1 
ATOM   1323 C  CD1 . ILE   A 1 171 ? -17.557 -10.579 8.200   1.00 28.50 ? 285 ILE   A CD1 1 
ATOM   1324 N  N   . VAL   A 1 172 ? -21.608 -14.808 9.325   1.00 24.01 ? 286 VAL   A N   1 
ATOM   1325 C  CA  . VAL   A 1 172 ? -22.974 -15.046 9.772   1.00 22.42 ? 286 VAL   A CA  1 
ATOM   1326 C  C   . VAL   A 1 172 ? -23.239 -14.124 10.950  1.00 25.01 ? 286 VAL   A C   1 
ATOM   1327 O  O   . VAL   A 1 172 ? -22.476 -14.120 11.926  1.00 23.44 ? 286 VAL   A O   1 
ATOM   1328 C  CB  . VAL   A 1 172 ? -23.192 -16.515 10.169  1.00 25.92 ? 286 VAL   A CB  1 
ATOM   1329 C  CG1 . VAL   A 1 172 ? -24.612 -16.724 10.689  1.00 25.13 ? 286 VAL   A CG1 1 
ATOM   1330 C  CG2 . VAL   A 1 172 ? -22.885 -17.455 9.003   1.00 28.36 ? 286 VAL   A CG2 1 
ATOM   1331 N  N   . HIS   A 1 173 ? -24.295 -13.318 10.853  1.00 22.58 ? 287 HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 173 ? -24.658 -12.383 11.910  1.00 24.69 ? 287 HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 173 ? -25.909 -12.923 12.590  1.00 25.19 ? 287 HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 173 ? -27.004 -12.880 12.017  1.00 25.11 ? 287 HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 173 ? -24.883 -10.980 11.349  1.00 25.11 ? 287 HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 173 ? -24.805 -9.897  12.379  1.00 23.83 ? 287 HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 173 ? -25.037 -8.569  12.085  1.00 22.50 ? 287 HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 173 ? -24.512 -9.944  13.699  1.00 22.42 ? 287 HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 173 ? -24.893 -7.847  13.181  1.00 24.50 ? 287 HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 173 ? -24.574 -8.657  14.175  1.00 23.00 ? 287 HIS   A NE2 1 
ATOM   1341 N  N   . LEU   A 1 174 ? -25.744 -13.428 13.809  1.00 25.48 ? 288 LEU   A N   1 
ATOM   1342 C  CA  . LEU   A 1 174 ? -26.856 -14.009 14.546  1.00 24.87 ? 288 LEU   A CA  1 
ATOM   1343 C  C   . LEU   A 1 174 ? -27.809 -12.924 15.036  1.00 25.28 ? 288 LEU   A C   1 
ATOM   1344 O  O   . LEU   A 1 174 ? -27.426 -11.767 15.224  1.00 23.57 ? 288 LEU   A O   1 
ATOM   1345 C  CB  . LEU   A 1 174 ? -26.332 -14.820 15.733  1.00 24.47 ? 288 LEU   A CB  1 
ATOM   1346 C  CG  . LEU   A 1 174 ? -25.372 -15.970 15.397  1.00 24.47 ? 288 LEU   A CG  1 
ATOM   1347 C  CD1 . LEU   A 1 174 ? -24.950 -16.703 16.657  1.00 25.57 ? 288 LEU   A CD1 1 
ATOM   1348 C  CD2 . LEU   A 1 174 ? -26.004 -16.938 14.413  1.00 25.09 ? 288 LEU   A CD2 1 
ATOM   1349 N  N   . ASN   A 1 175 ? -29.071 -13.305 15.239  1.00 25.57 ? 289 ASN   A N   1 
ATOM   1350 C  CA  . ASN   A 1 175 ? -30.051 -12.422 15.857  1.00 26.96 ? 289 ASN   A CA  1 
ATOM   1351 C  C   . ASN   A 1 175 ? -30.405 -12.847 17.274  1.00 25.92 ? 289 ASN   A C   1 
ATOM   1352 O  O   . ASN   A 1 175 ? -31.239 -12.200 17.918  1.00 29.11 ? 289 ASN   A O   1 
ATOM   1353 C  CB  . ASN   A 1 175 ? -31.323 -12.349 15.009  1.00 29.32 ? 289 ASN   A CB  1 
ATOM   1354 C  CG  . ASN   A 1 175 ? -31.967 -13.701 14.797  1.00 31.69 ? 289 ASN   A CG  1 
ATOM   1355 O  OD1 . ASN   A 1 175 ? -31.479 -14.727 15.273  1.00 30.86 ? 289 ASN   A OD1 1 
ATOM   1356 N  ND2 . ASN   A 1 175 ? -33.086 -13.702 14.086  1.00 32.54 ? 289 ASN   A ND2 1 
ATOM   1357 N  N   . LYS   A 1 176 ? -29.791 -13.913 17.774  1.00 27.98 ? 290 LYS   A N   1 
ATOM   1358 C  CA  . LYS   A 1 176 ? -29.949 -14.331 19.160  1.00 30.84 ? 290 LYS   A CA  1 
ATOM   1359 C  C   . LYS   A 1 176 ? -28.623 -14.914 19.614  1.00 28.52 ? 290 LYS   A C   1 
ATOM   1360 O  O   . LYS   A 1 176 ? -28.119 -15.862 19.004  1.00 31.64 ? 290 LYS   A O   1 
ATOM   1361 C  CB  . LYS   A 1 176 ? -31.073 -15.357 19.314  1.00 31.88 ? 290 LYS   A CB  1 
ATOM   1362 C  CG  . LYS   A 1 176 ? -31.376 -15.693 20.762  1.00 34.12 ? 290 LYS   A CG  1 
ATOM   1363 C  CD  . LYS   A 1 176 ? -32.208 -16.957 20.880  1.00 43.34 ? 290 LYS   A CD  1 
ATOM   1364 C  CE  . LYS   A 1 176 ? -33.161 -16.857 22.056  1.00 54.08 ? 290 LYS   A CE  1 
ATOM   1365 N  NZ  . LYS   A 1 176 ? -32.498 -16.251 23.246  1.00 56.78 ? 290 LYS   A NZ  1 
ATOM   1366 N  N   . SER   A 1 177 ? -28.058 -14.350 20.676  1.00 27.88 ? 291 SER   A N   1 
ATOM   1367 C  CA  . SER   A 1 177 ? -26.748 -14.786 21.122  1.00 28.42 ? 291 SER   A CA  1 
ATOM   1368 C  C   . SER   A 1 177 ? -26.839 -16.109 21.879  1.00 29.49 ? 291 SER   A C   1 
ATOM   1369 O  O   . SER   A 1 177 ? -27.891 -16.488 22.410  1.00 29.39 ? 291 SER   A O   1 
ATOM   1370 C  CB  . SER   A 1 177 ? -26.093 -13.711 21.990  1.00 28.94 ? 291 SER   A CB  1 
ATOM   1371 O  OG  . SER   A 1 177 ? -26.842 -13.469 23.163  1.00 36.50 ? 291 SER   A OG  1 
ATOM   1372 N  N   . VAL   A 1 178 ? -25.713 -16.821 21.903  1.00 24.40 ? 292 VAL   A N   1 
ATOM   1373 C  CA  . VAL   A 1 178 ? -25.581 -18.093 22.603  1.00 27.08 ? 292 VAL   A CA  1 
ATOM   1374 C  C   . VAL   A 1 178 ? -24.358 -18.009 23.500  1.00 28.22 ? 292 VAL   A C   1 
ATOM   1375 O  O   . VAL   A 1 178 ? -23.243 -17.785 23.015  1.00 24.89 ? 292 VAL   A O   1 
ATOM   1376 C  CB  . VAL   A 1 178 ? -25.454 -19.279 21.633  1.00 27.79 ? 292 VAL   A CB  1 
ATOM   1377 C  CG1 . VAL   A 1 178 ? -25.286 -20.581 22.401  1.00 28.05 ? 292 VAL   A CG1 1 
ATOM   1378 C  CG2 . VAL   A 1 178 ? -26.670 -19.346 20.715  1.00 25.89 ? 292 VAL   A CG2 1 
ATOM   1379 N  N   . GLU   A 1 179 ? -24.563 -18.186 24.800  1.00 26.49 ? 293 GLU   A N   1 
ATOM   1380 C  CA  . GLU   A 1 179 ? -23.459 -18.113 25.745  1.00 30.59 ? 293 GLU   A CA  1 
ATOM   1381 C  C   . GLU   A 1 179 ? -22.470 -19.250 25.520  1.00 26.42 ? 293 GLU   A C   1 
ATOM   1382 O  O   . GLU   A 1 179 ? -22.858 -20.385 25.229  1.00 28.19 ? 293 GLU   A O   1 
ATOM   1383 C  CB  . GLU   A 1 179 ? -23.987 -18.165 27.178  1.00 33.47 ? 293 GLU   A CB  1 
ATOM   1384 C  CG  . GLU   A 1 179 ? -24.398 -16.825 27.739  1.00 41.43 ? 293 GLU   A CG  1 
ATOM   1385 C  CD  . GLU   A 1 179 ? -24.521 -16.851 29.251  1.00 48.39 ? 293 GLU   A CD  1 
ATOM   1386 O  OE1 . GLU   A 1 179 ? -24.444 -17.954 29.834  1.00 50.86 ? 293 GLU   A OE1 1 
ATOM   1387 O  OE2 . GLU   A 1 179 ? -24.699 -15.770 29.851  1.00 52.94 ? 293 GLU   A OE2 1 
ATOM   1388 N  N   . ILE   A 1 180 ? -21.184 -18.935 25.648  1.00 23.07 ? 294 ILE   A N   1 
ATOM   1389 C  CA  . ILE   A 1 180 ? -20.118 -19.931 25.657  1.00 22.75 ? 294 ILE   A CA  1 
ATOM   1390 C  C   . ILE   A 1 180 ? -19.267 -19.667 26.888  1.00 27.54 ? 294 ILE   A C   1 
ATOM   1391 O  O   . ILE   A 1 180 ? -18.676 -18.587 27.020  1.00 25.12 ? 294 ILE   A O   1 
ATOM   1392 C  CB  . ILE   A 1 180 ? -19.279 -19.899 24.367  1.00 24.48 ? 294 ILE   A CB  1 
ATOM   1393 C  CG1 . ILE   A 1 180 ? -18.161 -20.935 24.422  1.00 26.91 ? 294 ILE   A CG1 1 
ATOM   1394 C  CG2 . ILE   A 1 180 ? -18.716 -18.496 24.111  1.00 27.12 ? 294 ILE   A CG2 1 
ATOM   1395 C  CD1 . ILE   A 1 180 ? -17.620 -21.323 23.063  1.00 25.62 ? 294 ILE   A CD1 1 
ATOM   1396 N  N   . ASN   A 1 181 ? -19.238 -20.633 27.803  1.00 25.99 ? 295 ASN   A N   1 
ATOM   1397 C  CA  . ASN   A 1 181 ? -18.685 -20.468 29.144  1.00 28.44 ? 295 ASN   A CA  1 
ATOM   1398 C  C   . ASN   A 1 181 ? -17.430 -21.322 29.272  1.00 28.81 ? 295 ASN   A C   1 
ATOM   1399 O  O   . ASN   A 1 181 ? -17.519 -22.545 29.408  1.00 30.02 ? 295 ASN   A O   1 
ATOM   1400 C  CB  . ASN   A 1 181 ? -19.740 -20.841 30.185  1.00 34.06 ? 295 ASN   A CB  1 
ATOM   1401 C  CG  . ASN   A 1 181 ? -19.214 -20.800 31.604  1.00 34.07 ? 295 ASN   A CG  1 
ATOM   1402 O  OD1 . ASN   A 1 181 ? -18.156 -20.242 31.881  1.00 34.27 ? 295 ASN   A OD1 1 
ATOM   1403 N  ND2 . ASN   A 1 181 ? -19.965 -21.395 32.514  1.00 41.02 ? 295 ASN   A ND2 1 
ATOM   1404 N  N   . CYS   A 1 182 ? -16.267 -20.675 29.243  1.00 27.02 ? 296 CYS   A N   1 
ATOM   1405 C  CA  . CYS   A 1 182 ? -14.988 -21.365 29.181  1.00 29.74 ? 296 CYS   A CA  1 
ATOM   1406 C  C   . CYS   A 1 182 ? -14.231 -21.210 30.496  1.00 35.05 ? 296 CYS   A C   1 
ATOM   1407 O  O   . CYS   A 1 182 ? -14.181 -20.115 31.072  1.00 32.80 ? 296 CYS   A O   1 
ATOM   1408 C  CB  . CYS   A 1 182 ? -14.161 -20.819 28.022  1.00 30.36 ? 296 CYS   A CB  1 
ATOM   1409 S  SG  . CYS   A 1 182 ? -15.056 -20.875 26.438  1.00 32.57 ? 296 CYS   A SG  1 
ATOM   1410 N  N   . THR   A 1 183 ? -13.634 -22.308 30.962  1.00 31.56 ? 297 THR   A N   1 
ATOM   1411 C  CA  . THR   A 1 183 ? -12.996 -22.342 32.272  1.00 35.83 ? 297 THR   A CA  1 
ATOM   1412 C  C   . THR   A 1 183 ? -11.742 -23.200 32.249  1.00 35.87 ? 297 THR   A C   1 
ATOM   1413 O  O   . THR   A 1 183 ? -11.756 -24.308 31.704  1.00 35.22 ? 297 THR   A O   1 
ATOM   1414 C  CB  . THR   A 1 183 ? -13.963 -22.883 33.333  1.00 40.20 ? 297 THR   A CB  1 
ATOM   1415 O  OG1 . THR   A 1 183 ? -15.139 -22.064 33.380  1.00 39.82 ? 297 THR   A OG1 1 
ATOM   1416 C  CG2 . THR   A 1 183 ? -13.294 -22.914 34.707  1.00 40.02 ? 297 THR   A CG2 1 
ATOM   1417 N  N   . ARG   A 1 184 ? -10.660 -22.677 32.839  1.00 38.86 ? 298 ARG   A N   1 
ATOM   1418 C  CA  . ARG   A 1 184 ? -9.523  -23.494 33.232  1.00 36.95 ? 298 ARG   A CA  1 
ATOM   1419 C  C   . ARG   A 1 184 ? -9.646  -23.651 34.742  1.00 39.31 ? 298 ARG   A C   1 
ATOM   1420 O  O   . ARG   A 1 184 ? -9.312  -22.717 35.484  1.00 39.12 ? 298 ARG   A O   1 
ATOM   1421 C  CB  . ARG   A 1 184 ? -8.198  -22.818 32.862  1.00 36.63 ? 298 ARG   A CB  1 
ATOM   1422 C  CG  . ARG   A 1 184 ? -6.941  -23.712 33.020  1.00 37.96 ? 298 ARG   A CG  1 
ATOM   1423 C  CD  . ARG   A 1 184 ? -6.683  -24.210 34.447  1.00 39.27 ? 298 ARG   A CD  1 
ATOM   1424 N  NE  . ARG   A 1 184 ? -6.486  -23.160 35.440  1.00 40.37 ? 298 ARG   A NE  1 
ATOM   1425 C  CZ  . ARG   A 1 184 ? -5.345  -22.510 35.636  1.00 42.88 ? 298 ARG   A CZ  1 
ATOM   1426 N  NH1 . ARG   A 1 184 ? -4.274  -22.751 34.897  1.00 40.99 ? 298 ARG   A NH1 1 
ATOM   1427 N  NH2 . ARG   A 1 184 ? -5.278  -21.594 36.599  1.00 42.99 ? 298 ARG   A NH2 1 
ATOM   1428 N  N   . PRO   A 1 185 ? -10.133 -24.781 35.249  1.00 40.19 ? 299 PRO   A N   1 
ATOM   1429 C  CA  . PRO   A 1 185 ? -10.410 -24.880 36.686  1.00 44.40 ? 299 PRO   A CA  1 
ATOM   1430 C  C   . PRO   A 1 185 ? -9.143  -24.720 37.512  1.00 46.75 ? 299 PRO   A C   1 
ATOM   1431 O  O   . PRO   A 1 185 ? -8.044  -25.085 37.087  1.00 44.39 ? 299 PRO   A O   1 
ATOM   1432 C  CB  . PRO   A 1 185 ? -11.009 -26.282 36.834  1.00 43.93 ? 299 PRO   A CB  1 
ATOM   1433 C  CG  . PRO   A 1 185 ? -10.470 -27.035 35.656  1.00 40.73 ? 299 PRO   A CG  1 
ATOM   1434 C  CD  . PRO   A 1 185 ? -10.443 -26.035 34.544  1.00 38.44 ? 299 PRO   A CD  1 
ATOM   1435 N  N   . SER   A 1 186 ? -9.310  -24.168 38.708  1.00 51.90 ? 300 SER   A N   1 
ATOM   1436 C  CA  . SER   A 1 186 ? -8.176  -23.892 39.586  1.00 54.77 ? 300 SER   A CA  1 
ATOM   1437 C  C   . SER   A 1 186 ? -7.550  -25.187 40.098  1.00 53.61 ? 300 SER   A C   1 
ATOM   1438 O  O   . SER   A 1 186 ? -8.227  -26.209 40.210  1.00 54.83 ? 300 SER   A O   1 
ATOM   1439 C  CB  . SER   A 1 186 ? -8.603  -23.013 40.767  1.00 58.81 ? 300 SER   A CB  1 
ATOM   1440 O  OG  . SER   A 1 186 ? -8.877  -23.789 41.921  1.00 66.42 ? 300 SER   A OG  1 
ATOM   1441 N  N   . ASP   A 1 195 ? -3.140  -31.007 34.905  1.00 49.71 ? 325 ASP   A N   1 
ATOM   1442 C  CA  . ASP   A 1 195 ? -2.659  -30.265 33.743  1.00 44.04 ? 325 ASP   A CA  1 
ATOM   1443 C  C   . ASP   A 1 195 ? -3.175  -28.830 33.809  1.00 44.54 ? 325 ASP   A C   1 
ATOM   1444 O  O   . ASP   A 1 195 ? -4.380  -28.591 33.732  1.00 42.04 ? 325 ASP   A O   1 
ATOM   1445 C  CB  . ASP   A 1 195 ? -3.110  -30.942 32.446  1.00 42.55 ? 325 ASP   A CB  1 
ATOM   1446 C  CG  . ASP   A 1 195 ? -2.499  -30.305 31.209  1.00 40.97 ? 325 ASP   A CG  1 
ATOM   1447 O  OD1 . ASP   A 1 195 ? -1.924  -29.202 31.316  1.00 42.93 ? 325 ASP   A OD1 1 
ATOM   1448 O  OD2 . ASP   A 1 195 ? -2.596  -30.911 30.121  1.00 44.44 ? 325 ASP   A OD2 1 
ATOM   1449 N  N   . ILE   A 1 196 ? -2.256  -27.873 33.963  1.00 40.42 ? 326 ILE   A N   1 
ATOM   1450 C  CA  . ILE   A 1 196 ? -2.652  -26.477 34.133  1.00 41.02 ? 326 ILE   A CA  1 
ATOM   1451 C  C   . ILE   A 1 196 ? -3.069  -25.814 32.832  1.00 42.03 ? 326 ILE   A C   1 
ATOM   1452 O  O   . ILE   A 1 196 ? -3.554  -24.676 32.859  1.00 41.51 ? 326 ILE   A O   1 
ATOM   1453 C  CB  . ILE   A 1 196 ? -1.516  -25.679 34.801  1.00 42.88 ? 326 ILE   A CB  1 
ATOM   1454 C  CG1 . ILE   A 1 196 ? -0.386  -25.408 33.807  1.00 41.49 ? 326 ILE   A CG1 1 
ATOM   1455 C  CG2 . ILE   A 1 196 ? -0.995  -26.425 36.020  1.00 44.09 ? 326 ILE   A CG2 1 
ATOM   1456 C  CD1 . ILE   A 1 196 ? 0.825   -24.747 34.435  1.00 44.02 ? 326 ILE   A CD1 1 
ATOM   1457 N  N   . ARG   A 1 197 ? -2.914  -26.494 31.697  1.00 40.33 ? 327 ARG   A N   1 
ATOM   1458 C  CA  . ARG   A 1 197 ? -3.312  -25.961 30.401  1.00 39.83 ? 327 ARG   A CA  1 
ATOM   1459 C  C   . ARG   A 1 197 ? -4.614  -26.565 29.899  1.00 37.21 ? 327 ARG   A C   1 
ATOM   1460 O  O   . ARG   A 1 197 ? -5.115  -26.149 28.849  1.00 34.39 ? 327 ARG   A O   1 
ATOM   1461 C  CB  . ARG   A 1 197 ? -2.188  -26.194 29.388  1.00 36.98 ? 327 ARG   A CB  1 
ATOM   1462 C  CG  . ARG   A 1 197 ? -0.983  -25.321 29.672  1.00 36.20 ? 327 ARG   A CG  1 
ATOM   1463 C  CD  . ARG   A 1 197 ? 0.183   -25.597 28.745  1.00 41.50 ? 327 ARG   A CD  1 
ATOM   1464 N  NE  . ARG   A 1 197 ? 1.427   -25.199 29.392  1.00 43.97 ? 327 ARG   A NE  1 
ATOM   1465 C  CZ  . ARG   A 1 197 ? 1.949   -25.825 30.439  1.00 40.41 ? 327 ARG   A CZ  1 
ATOM   1466 N  NH1 . ARG   A 1 197 ? 1.370   -26.890 30.967  1.00 41.68 ? 327 ARG   A NH1 1 
ATOM   1467 N  NH2 . ARG   A 1 197 ? 3.069   -25.361 30.980  1.00 44.53 ? 327 ARG   A NH2 1 
ATOM   1468 N  N   . LYS   A 1 198 ? -5.173  -27.520 30.638  1.00 35.99 ? 328 LYS   A N   1 
ATOM   1469 C  CA  . LYS   A 1 198 ? -6.417  -28.181 30.270  1.00 38.64 ? 328 LYS   A CA  1 
ATOM   1470 C  C   . LYS   A 1 198 ? -7.610  -27.295 30.612  1.00 34.85 ? 328 LYS   A C   1 
ATOM   1471 O  O   . LYS   A 1 198 ? -7.760  -26.862 31.760  1.00 32.81 ? 328 LYS   A O   1 
ATOM   1472 C  CB  . LYS   A 1 198 ? -6.523  -29.511 31.012  1.00 38.89 ? 328 LYS   A CB  1 
ATOM   1473 C  CG  . LYS   A 1 198 ? -7.636  -30.430 30.556  1.00 41.09 ? 328 LYS   A CG  1 
ATOM   1474 C  CD  . LYS   A 1 198 ? -7.076  -31.546 29.682  1.00 49.28 ? 328 LYS   A CD  1 
ATOM   1475 C  CE  . LYS   A 1 198 ? -7.965  -32.780 29.732  1.00 53.61 ? 328 LYS   A CE  1 
ATOM   1476 N  NZ  . LYS   A 1 198 ? -7.520  -33.812 28.754  1.00 58.41 ? 328 LYS   A NZ  1 
ATOM   1477 N  N   . ALA   A 1 199 ? -8.458  -27.021 29.619  1.00 34.28 ? 329 ALA   A N   1 
ATOM   1478 C  CA  . ALA   A 1 199 ? -9.618  -26.155 29.800  1.00 32.58 ? 329 ALA   A CA  1 
ATOM   1479 C  C   . ALA   A 1 199 ? -10.802 -26.735 29.037  1.00 33.53 ? 329 ALA   A C   1 
ATOM   1480 O  O   . ALA   A 1 199 ? -10.691 -27.764 28.364  1.00 32.02 ? 329 ALA   A O   1 
ATOM   1481 C  CB  . ALA   A 1 199 ? -9.315  -24.721 29.350  1.00 34.53 ? 329 ALA   A CB  1 
ATOM   1482 N  N   . TYR   A 1 200 ? -11.951 -26.072 29.153  1.00 32.84 ? 330 TYR   A N   1 
ATOM   1483 C  CA  . TYR   A 1 200 ? -13.143 -26.511 28.440  1.00 33.24 ? 330 TYR   A CA  1 
ATOM   1484 C  C   . TYR   A 1 200 ? -14.121 -25.352 28.342  1.00 33.13 ? 330 TYR   A C   1 
ATOM   1485 O  O   . TYR   A 1 200 ? -14.051 -24.394 29.114  1.00 32.05 ? 330 TYR   A O   1 
ATOM   1486 C  CB  . TYR   A 1 200 ? -13.807 -27.709 29.132  1.00 37.58 ? 330 TYR   A CB  1 
ATOM   1487 C  CG  . TYR   A 1 200 ? -14.232 -27.451 30.560  1.00 40.53 ? 330 TYR   A CG  1 
ATOM   1488 C  CD1 . TYR   A 1 200 ? -13.347 -27.630 31.618  1.00 43.48 ? 330 TYR   A CD1 1 
ATOM   1489 C  CD2 . TYR   A 1 200 ? -15.526 -27.035 30.851  1.00 45.53 ? 330 TYR   A CD2 1 
ATOM   1490 C  CE1 . TYR   A 1 200 ? -13.739 -27.390 32.925  1.00 43.19 ? 330 TYR   A CE1 1 
ATOM   1491 C  CE2 . TYR   A 1 200 ? -15.928 -26.794 32.154  1.00 45.76 ? 330 TYR   A CE2 1 
ATOM   1492 C  CZ  . TYR   A 1 200 ? -15.032 -26.973 33.187  1.00 47.11 ? 330 TYR   A CZ  1 
ATOM   1493 O  OH  . TYR   A 1 200 ? -15.434 -26.732 34.482  1.00 48.68 ? 330 TYR   A OH  1 
ATOM   1494 N  N   . CYS   A 1 201 ? -15.039 -25.456 27.381  1.00 31.33 ? 331 CYS   A N   1 
ATOM   1495 C  CA  . CYS   A 1 201 ? -16.109 -24.487 27.187  1.00 31.81 ? 331 CYS   A CA  1 
ATOM   1496 C  C   . CYS   A 1 201 ? -17.443 -25.214 27.225  1.00 32.82 ? 331 CYS   A C   1 
ATOM   1497 O  O   . CYS   A 1 201 ? -17.597 -26.280 26.618  1.00 30.77 ? 331 CYS   A O   1 
ATOM   1498 C  CB  . CYS   A 1 201 ? -15.978 -23.747 25.848  1.00 32.01 ? 331 CYS   A CB  1 
ATOM   1499 S  SG  . CYS   A 1 201 ? -14.538 -22.694 25.674  1.00 36.55 ? 331 CYS   A SG  1 
ATOM   1500 N  N   . GLU   A 1 202 ? -18.409 -24.629 27.922  1.00 30.48 ? 332 GLU   A N   1 
ATOM   1501 C  CA  . GLU   A 1 202 ? -19.738 -25.204 28.047  1.00 29.16 ? 332 GLU   A CA  1 
ATOM   1502 C  C   . GLU   A 1 202 ? -20.728 -24.355 27.264  1.00 29.90 ? 332 GLU   A C   1 
ATOM   1503 O  O   . GLU   A 1 202 ? -20.706 -23.121 27.355  1.00 26.67 ? 332 GLU   A O   1 
ATOM   1504 C  CB  . GLU   A 1 202 ? -20.147 -25.308 29.518  1.00 33.80 ? 332 GLU   A CB  1 
ATOM   1505 C  CG  . GLU   A 1 202 ? -19.350 -26.361 30.277  1.00 35.50 ? 332 GLU   A CG  1 
ATOM   1506 C  CD  . GLU   A 1 202 ? -19.707 -26.432 31.750  1.00 44.08 ? 332 GLU   A CD  1 
ATOM   1507 O  OE1 . GLU   A 1 202 ? -20.129 -25.396 32.314  1.00 47.07 ? 332 GLU   A OE1 1 
ATOM   1508 O  OE2 . GLU   A 1 202 ? -19.552 -27.523 32.345  1.00 43.85 ? 332 GLU   A OE2 1 
ATOM   1509 N  N   . ILE   A 1 203 ? -21.573 -25.019 26.480  1.00 26.97 ? 333 ILE   A N   1 
ATOM   1510 C  CA  . ILE   A 1 203 ? -22.577 -24.363 25.652  1.00 28.91 ? 333 ILE   A CA  1 
ATOM   1511 C  C   . ILE   A 1 203 ? -23.897 -25.099 25.826  1.00 27.83 ? 333 ILE   A C   1 
ATOM   1512 O  O   . ILE   A 1 203 ? -23.928 -26.333 25.860  1.00 31.71 ? 333 ILE   A O   1 
ATOM   1513 C  CB  . ILE   A 1 203 ? -22.167 -24.344 24.163  1.00 29.78 ? 333 ILE   A CB  1 
ATOM   1514 C  CG1 . ILE   A 1 203 ? -20.857 -23.579 23.976  1.00 28.91 ? 333 ILE   A CG1 1 
ATOM   1515 C  CG2 . ILE   A 1 203 ? -23.263 -23.714 23.319  1.00 29.58 ? 333 ILE   A CG2 1 
ATOM   1516 C  CD1 . ILE   A 1 203 ? -19.753 -24.426 23.358  1.00 32.25 ? 333 ILE   A CD1 1 
ATOM   1517 N  N   . ASN   A 1 204 ? -24.987 -24.347 25.938  1.00 29.32 ? 334 ASN   A N   1 
ATOM   1518 C  CA  . ASN   A 1 204 ? -26.310 -24.958 26.037  1.00 30.57 ? 334 ASN   A CA  1 
ATOM   1519 C  C   . ASN   A 1 204 ? -26.660 -25.587 24.692  1.00 31.35 ? 334 ASN   A C   1 
ATOM   1520 O  O   . ASN   A 1 204 ? -26.934 -24.881 23.718  1.00 32.96 ? 334 ASN   A O   1 
ATOM   1521 C  CB  . ASN   A 1 204 ? -27.331 -23.906 26.462  1.00 27.09 ? 334 ASN   A CB  1 
ATOM   1522 C  CG  . ASN   A 1 204 ? -28.765 -24.431 26.484  1.00 33.73 ? 334 ASN   A CG  1 
ATOM   1523 O  OD1 . ASN   A 1 204 ? -29.111 -25.403 25.816  1.00 32.37 ? 334 ASN   A OD1 1 
ATOM   1524 N  ND2 . ASN   A 1 204 ? -29.607 -23.773 27.269  1.00 37.09 ? 334 ASN   A ND2 1 
ATOM   1525 N  N   . GLY   A 1 205 ? -26.631 -26.918 24.629  1.00 32.78 ? 335 GLY   A N   1 
ATOM   1526 C  CA  . GLY   A 1 205 ? -26.836 -27.598 23.362  1.00 35.49 ? 335 GLY   A CA  1 
ATOM   1527 C  C   . GLY   A 1 205 ? -28.199 -27.348 22.757  1.00 37.14 ? 335 GLY   A C   1 
ATOM   1528 O  O   . GLY   A 1 205 ? -28.334 -27.301 21.533  1.00 32.84 ? 335 GLY   A O   1 
ATOM   1529 N  N   . THR   A 1 206 ? -29.221 -27.173 23.599  1.00 35.74 ? 336 THR   A N   1 
ATOM   1530 C  CA  . THR   A 1 206 ? -30.544 -26.824 23.096  1.00 40.09 ? 336 THR   A CA  1 
ATOM   1531 C  C   . THR   A 1 206 ? -30.519 -25.455 22.425  1.00 38.00 ? 336 THR   A C   1 
ATOM   1532 O  O   . THR   A 1 206 ? -30.988 -25.292 21.293  1.00 37.50 ? 336 THR   A O   1 
ATOM   1533 C  CB  . THR   A 1 206 ? -31.554 -26.841 24.243  1.00 39.93 ? 336 THR   A CB  1 
ATOM   1534 O  OG1 . THR   A 1 206 ? -31.592 -28.147 24.834  1.00 38.77 ? 336 THR   A OG1 1 
ATOM   1535 C  CG2 . THR   A 1 206 ? -32.939 -26.480 23.734  1.00 40.12 ? 336 THR   A CG2 1 
ATOM   1536 N  N   . LYS   A 1 207 ? -29.987 -24.454 23.129  1.00 37.16 ? 337 LYS   A N   1 
ATOM   1537 C  CA  . LYS   A 1 207 ? -29.834 -23.115 22.572  1.00 35.23 ? 337 LYS   A CA  1 
ATOM   1538 C  C   . LYS   A 1 207 ? -29.085 -23.155 21.247  1.00 34.19 ? 337 LYS   A C   1 
ATOM   1539 O  O   . LYS   A 1 207 ? -29.555 -22.628 20.232  1.00 35.00 ? 337 LYS   A O   1 
ATOM   1540 C  CB  . LYS   A 1 207 ? -29.081 -22.232 23.572  1.00 38.10 ? 337 LYS   A CB  1 
ATOM   1541 C  CG  . LYS   A 1 207 ? -29.954 -21.469 24.571  1.00 42.71 ? 337 LYS   A CG  1 
ATOM   1542 C  CD  . LYS   A 1 207 ? -29.257 -20.187 25.056  1.00 40.26 ? 337 LYS   A CD  1 
ATOM   1543 C  CE  . LYS   A 1 207 ? -27.924 -20.473 25.752  1.00 41.51 ? 337 LYS   A CE  1 
ATOM   1544 N  NZ  . LYS   A 1 207 ? -27.197 -19.211 26.117  1.00 37.43 ? 337 LYS   A NZ  1 
ATOM   1545 N  N   . TRP   A 1 208 ? -27.904 -23.775 21.249  1.00 32.77 ? 338 TRP   A N   1 
ATOM   1546 C  CA  . TRP   A 1 208 ? -27.014 -23.719 20.097  1.00 33.53 ? 338 TRP   A CA  1 
ATOM   1547 C  C   . TRP   A 1 208 ? -27.605 -24.432 18.891  1.00 33.39 ? 338 TRP   A C   1 
ATOM   1548 O  O   . TRP   A 1 208 ? -27.652 -23.870 17.791  1.00 30.54 ? 338 TRP   A O   1 
ATOM   1549 C  CB  . TRP   A 1 208 ? -25.665 -24.331 20.461  1.00 27.56 ? 338 TRP   A CB  1 
ATOM   1550 C  CG  . TRP   A 1 208 ? -24.744 -24.479 19.295  1.00 30.77 ? 338 TRP   A CG  1 
ATOM   1551 C  CD1 . TRP   A 1 208 ? -24.330 -25.645 18.722  1.00 31.01 ? 338 TRP   A CD1 1 
ATOM   1552 C  CD2 . TRP   A 1 208 ? -24.106 -23.423 18.567  1.00 31.11 ? 338 TRP   A CD2 1 
ATOM   1553 N  NE1 . TRP   A 1 208 ? -23.483 -25.380 17.672  1.00 34.08 ? 338 TRP   A NE1 1 
ATOM   1554 C  CE2 . TRP   A 1 208 ? -23.326 -24.024 17.559  1.00 31.44 ? 338 TRP   A CE2 1 
ATOM   1555 C  CE3 . TRP   A 1 208 ? -24.121 -22.028 18.669  1.00 33.28 ? 338 TRP   A CE3 1 
ATOM   1556 C  CZ2 . TRP   A 1 208 ? -22.566 -23.280 16.660  1.00 33.85 ? 338 TRP   A CZ2 1 
ATOM   1557 C  CZ3 . TRP   A 1 208 ? -23.362 -21.287 17.773  1.00 34.68 ? 338 TRP   A CZ3 1 
ATOM   1558 C  CH2 . TRP   A 1 208 ? -22.598 -21.917 16.780  1.00 28.65 ? 338 TRP   A CH2 1 
ATOM   1559 N  N   . ASN   A 1 209 ? -28.028 -25.686 19.069  1.00 33.68 ? 339 ASN   A N   1 
ATOM   1560 C  CA  . ASN   A 1 209 ? -28.530 -26.456 17.937  1.00 34.67 ? 339 ASN   A CA  1 
ATOM   1561 C  C   . ASN   A 1 209 ? -29.720 -25.772 17.284  1.00 31.89 ? 339 ASN   A C   1 
ATOM   1562 O  O   . ASN   A 1 209 ? -29.877 -25.820 16.060  1.00 33.44 ? 339 ASN   A O   1 
ATOM   1563 C  CB  . ASN   A 1 209 ? -28.888 -27.874 18.379  1.00 36.79 ? 339 ASN   A CB  1 
ATOM   1564 C  CG  . ASN   A 1 209 ? -27.664 -28.703 18.703  1.00 38.54 ? 339 ASN   A CG  1 
ATOM   1565 O  OD1 . ASN   A 1 209 ? -26.649 -28.614 18.011  1.00 36.02 ? 339 ASN   A OD1 1 
ATOM   1566 N  ND2 . ASN   A 1 209 ? -27.749 -29.516 19.753  1.00 35.64 ? 339 ASN   A ND2 1 
ATOM   1567 N  N   . LYS   A 1 210 ? -30.574 -25.132 18.075  1.00 32.44 ? 340 LYS   A N   1 
ATOM   1568 C  CA  . LYS   A 1 210 ? -31.692 -24.421 17.476  1.00 36.75 ? 340 LYS   A CA  1 
ATOM   1569 C  C   . LYS   A 1 210 ? -31.202 -23.255 16.619  1.00 37.08 ? 340 LYS   A C   1 
ATOM   1570 O  O   . LYS   A 1 210 ? -31.606 -23.116 15.459  1.00 36.28 ? 340 LYS   A O   1 
ATOM   1571 C  CB  . LYS   A 1 210 ? -32.660 -23.988 18.575  1.00 40.10 ? 340 LYS   A CB  1 
ATOM   1572 C  CG  . LYS   A 1 210 ? -33.981 -23.453 18.089  1.00 45.89 ? 340 LYS   A CG  1 
ATOM   1573 C  CD  . LYS   A 1 210 ? -33.783 -22.015 17.720  1.00 49.16 ? 340 LYS   A CD  1 
ATOM   1574 C  CE  . LYS   A 1 210 ? -34.025 -21.209 18.962  1.00 54.59 ? 340 LYS   A CE  1 
ATOM   1575 N  NZ  . LYS   A 1 210 ? -33.261 -19.925 18.944  1.00 52.31 ? 340 LYS   A NZ  1 
ATOM   1576 N  N   . VAL   A 1 211 ? -30.284 -22.442 17.147  1.00 35.81 ? 341 VAL   A N   1 
ATOM   1577 C  CA  . VAL   A 1 211 ? -29.718 -21.342 16.364  1.00 34.55 ? 341 VAL   A CA  1 
ATOM   1578 C  C   . VAL   A 1 211 ? -29.053 -21.869 15.098  1.00 29.72 ? 341 VAL   A C   1 
ATOM   1579 O  O   . VAL   A 1 211 ? -29.239 -21.323 14.004  1.00 31.96 ? 341 VAL   A O   1 
ATOM   1580 C  CB  . VAL   A 1 211 ? -28.729 -20.528 17.218  1.00 34.16 ? 341 VAL   A CB  1 
ATOM   1581 C  CG1 . VAL   A 1 211 ? -27.842 -19.649 16.331  1.00 34.88 ? 341 VAL   A CG1 1 
ATOM   1582 C  CG2 . VAL   A 1 211 ? -29.481 -19.687 18.243  1.00 34.74 ? 341 VAL   A CG2 1 
ATOM   1583 N  N   . LEU   A 1 212 ? -28.262 -22.939 15.227  1.00 29.55 ? 342 LEU   A N   1 
ATOM   1584 C  CA  . LEU   A 1 212 ? -27.538 -23.467 14.076  1.00 29.49 ? 342 LEU   A CA  1 
ATOM   1585 C  C   . LEU   A 1 212 ? -28.497 -23.971 13.005  1.00 32.62 ? 342 LEU   A C   1 
ATOM   1586 O  O   . LEU   A 1 212 ? -28.245 -23.799 11.807  1.00 29.73 ? 342 LEU   A O   1 
ATOM   1587 C  CB  . LEU   A 1 212 ? -26.588 -24.578 14.520  1.00 32.21 ? 342 LEU   A CB  1 
ATOM   1588 C  CG  . LEU   A 1 212 ? -25.460 -24.954 13.560  1.00 32.03 ? 342 LEU   A CG  1 
ATOM   1589 C  CD1 . LEU   A 1 212 ? -24.739 -23.709 13.053  1.00 32.11 ? 342 LEU   A CD1 1 
ATOM   1590 C  CD2 . LEU   A 1 212 ? -24.487 -25.891 14.252  1.00 31.51 ? 342 LEU   A CD2 1 
ATOM   1591 N  N   . LYS   A 1 213 ? -29.603 -24.599 13.414  1.00 31.89 ? 343 LYS   A N   1 
ATOM   1592 C  CA  . LYS   A 1 213 ? -30.616 -24.998 12.442  1.00 32.83 ? 343 LYS   A CA  1 
ATOM   1593 C  C   . LYS   A 1 213 ? -31.147 -23.791 11.677  1.00 33.06 ? 343 LYS   A C   1 
ATOM   1594 O  O   . LYS   A 1 213 ? -31.297 -23.842 10.451  1.00 35.15 ? 343 LYS   A O   1 
ATOM   1595 C  CB  . LYS   A 1 213 ? -31.753 -25.744 13.143  1.00 33.76 ? 343 LYS   A CB  1 
ATOM   1596 C  CG  . LYS   A 1 213 ? -32.842 -26.272 12.207  1.00 39.61 ? 343 LYS   A CG  1 
ATOM   1597 C  CD  . LYS   A 1 213 ? -32.267 -27.050 11.026  1.00 42.45 ? 343 LYS   A CD  1 
ATOM   1598 C  CE  . LYS   A 1 213 ? -33.346 -27.887 10.339  1.00 48.25 ? 343 LYS   A CE  1 
ATOM   1599 N  NZ  . LYS   A 1 213 ? -32.766 -28.895 9.407   1.00 53.40 ? 343 LYS   A NZ  1 
ATOM   1600 N  N   . GLN   A 1 214 ? -31.435 -22.691 12.382  1.00 32.88 ? 344 GLN   A N   1 
ATOM   1601 C  CA  . GLN   A 1 214 ? -31.870 -21.479 11.693  1.00 32.40 ? 344 GLN   A CA  1 
ATOM   1602 C  C   . GLN   A 1 214 ? -30.797 -20.984 10.732  1.00 34.23 ? 344 GLN   A C   1 
ATOM   1603 O  O   . GLN   A 1 214 ? -31.105 -20.535 9.622   1.00 34.19 ? 344 GLN   A O   1 
ATOM   1604 C  CB  . GLN   A 1 214 ? -32.228 -20.389 12.705  1.00 32.01 ? 344 GLN   A CB  1 
ATOM   1605 C  CG  . GLN   A 1 214 ? -33.503 -20.670 13.498  1.00 37.39 ? 344 GLN   A CG  1 
ATOM   1606 C  CD  . GLN   A 1 214 ? -33.719 -19.681 14.630  1.00 43.98 ? 344 GLN   A CD  1 
ATOM   1607 O  OE1 . GLN   A 1 214 ? -32.817 -18.921 14.988  1.00 44.99 ? 344 GLN   A OE1 1 
ATOM   1608 N  NE2 . GLN   A 1 214 ? -34.920 -19.689 15.203  1.00 44.43 ? 344 GLN   A NE2 1 
ATOM   1609 N  N   . VAL   A 1 215 ? -29.530 -21.062 11.141  1.00 29.71 ? 345 VAL   A N   1 
ATOM   1610 C  CA  . VAL   A 1 215 ? -28.432 -20.656 10.266  1.00 29.81 ? 345 VAL   A CA  1 
ATOM   1611 C  C   . VAL   A 1 215 ? -28.452 -21.462 8.973   1.00 33.39 ? 345 VAL   A C   1 
ATOM   1612 O  O   . VAL   A 1 215 ? -28.341 -20.908 7.872   1.00 32.43 ? 345 VAL   A O   1 
ATOM   1613 C  CB  . VAL   A 1 215 ? -27.084 -20.800 10.995  1.00 30.52 ? 345 VAL   A CB  1 
ATOM   1614 C  CG1 . VAL   A 1 215 ? -25.934 -20.769 9.999   1.00 30.20 ? 345 VAL   A CG1 1 
ATOM   1615 C  CG2 . VAL   A 1 215 ? -26.925 -19.707 12.029  1.00 26.96 ? 345 VAL   A CG2 1 
ATOM   1616 N  N   . THR   A 1 216 ? -28.587 -22.786 9.084   1.00 30.26 ? 346 THR   A N   1 
ATOM   1617 C  CA  . THR   A 1 216 ? -28.614 -23.613 7.882   1.00 34.65 ? 346 THR   A CA  1 
ATOM   1618 C  C   . THR   A 1 216 ? -29.796 -23.252 6.993   1.00 36.19 ? 346 THR   A C   1 
ATOM   1619 O  O   . THR   A 1 216 ? -29.668 -23.220 5.763   1.00 39.85 ? 346 THR   A O   1 
ATOM   1620 C  CB  . THR   A 1 216 ? -28.640 -25.099 8.251   1.00 35.70 ? 346 THR   A CB  1 
ATOM   1621 O  OG1 . THR   A 1 216 ? -29.871 -25.412 8.912   1.00 35.04 ? 346 THR   A OG1 1 
ATOM   1622 C  CG2 . THR   A 1 216 ? -27.464 -25.447 9.161   1.00 36.90 ? 346 THR   A CG2 1 
ATOM   1623 N  N   . GLU   A 1 217 ? -30.959 -22.991 7.594   1.00 35.96 ? 347 GLU   A N   1 
ATOM   1624 C  CA  . GLU   A 1 217 ? -32.117 -22.590 6.804   1.00 39.87 ? 347 GLU   A CA  1 
ATOM   1625 C  C   . GLU   A 1 217 ? -31.860 -21.272 6.083   1.00 43.10 ? 347 GLU   A C   1 
ATOM   1626 O  O   . GLU   A 1 217 ? -32.259 -21.100 4.925   1.00 48.95 ? 347 GLU   A O   1 
ATOM   1627 C  CB  . GLU   A 1 217 ? -33.353 -22.484 7.695   1.00 36.94 ? 347 GLU   A CB  1 
ATOM   1628 C  CG  . GLU   A 1 217 ? -33.794 -23.812 8.286   1.00 42.86 ? 347 GLU   A CG  1 
ATOM   1629 C  CD  . GLU   A 1 217 ? -34.437 -24.714 7.250   1.00 49.16 ? 347 GLU   A CD  1 
ATOM   1630 O  OE1 . GLU   A 1 217 ? -35.567 -24.409 6.812   1.00 51.93 ? 347 GLU   A OE1 1 
ATOM   1631 O  OE2 . GLU   A 1 217 ? -33.806 -25.727 6.874   1.00 48.53 ? 347 GLU   A OE2 1 
ATOM   1632 N  N   . LYS   A 1 218 ? -31.204 -20.324 6.755   1.00 35.32 ? 348 LYS   A N   1 
ATOM   1633 C  CA  . LYS   A 1 218 ? -30.836 -19.076 6.095   1.00 39.72 ? 348 LYS   A CA  1 
ATOM   1634 C  C   . LYS   A 1 218 ? -29.886 -19.339 4.931   1.00 37.89 ? 348 LYS   A C   1 
ATOM   1635 O  O   . LYS   A 1 218 ? -30.010 -18.728 3.863   1.00 39.15 ? 348 LYS   A O   1 
ATOM   1636 C  CB  . LYS   A 1 218 ? -30.200 -18.121 7.107   1.00 36.08 ? 348 LYS   A CB  1 
ATOM   1637 C  CG  . LYS   A 1 218 ? -29.842 -16.756 6.545   1.00 36.66 ? 348 LYS   A CG  1 
ATOM   1638 C  CD  . LYS   A 1 218 ? -31.021 -16.138 5.794   1.00 35.87 ? 348 LYS   A CD  1 
ATOM   1639 C  CE  . LYS   A 1 218 ? -32.116 -15.726 6.759   1.00 37.49 ? 348 LYS   A CE  1 
ATOM   1640 N  NZ  . LYS   A 1 218 ? -33.171 -14.899 6.107   1.00 38.40 ? 348 LYS   A NZ  1 
ATOM   1641 N  N   . LEU   A 1 219 ? -28.927 -20.248 5.123   1.00 35.71 ? 349 LEU   A N   1 
ATOM   1642 C  CA  . LEU   A 1 219 ? -27.992 -20.592 4.059   1.00 36.13 ? 349 LEU   A CA  1 
ATOM   1643 C  C   . LEU   A 1 219 ? -28.694 -21.311 2.915   1.00 42.13 ? 349 LEU   A C   1 
ATOM   1644 O  O   . LEU   A 1 219 ? -28.266 -21.208 1.759   1.00 42.94 ? 349 LEU   A O   1 
ATOM   1645 C  CB  . LEU   A 1 219 ? -26.864 -21.457 4.624   1.00 34.32 ? 349 LEU   A CB  1 
ATOM   1646 C  CG  . LEU   A 1 219 ? -25.828 -20.735 5.496   1.00 36.63 ? 349 LEU   A CG  1 
ATOM   1647 C  CD1 . LEU   A 1 219 ? -24.857 -21.726 6.128   1.00 33.11 ? 349 LEU   A CD1 1 
ATOM   1648 C  CD2 . LEU   A 1 219 ? -25.079 -19.676 4.702   1.00 36.28 ? 349 LEU   A CD2 1 
ATOM   1649 N  N   . LYS   A 1 220 ? -29.761 -22.053 3.223   1.00 41.57 ? 350 LYS   A N   1 
ATOM   1650 C  CA  . LYS   A 1 220 ? -30.576 -22.668 2.182   1.00 43.65 ? 350 LYS   A CA  1 
ATOM   1651 C  C   . LYS   A 1 220 ? -31.127 -21.611 1.234   1.00 44.74 ? 350 LYS   A C   1 
ATOM   1652 O  O   . LYS   A 1 220 ? -31.138 -21.802 0.013   1.00 47.62 ? 350 LYS   A O   1 
ATOM   1653 C  CB  . LYS   A 1 220 ? -31.718 -23.450 2.832   1.00 42.50 ? 350 LYS   A CB  1 
ATOM   1654 C  CG  . LYS   A 1 220 ? -31.368 -24.870 3.248   1.00 43.19 ? 350 LYS   A CG  1 
ATOM   1655 C  CD  . LYS   A 1 220 ? -32.620 -25.650 3.629   1.00 47.49 ? 350 LYS   A CD  1 
ATOM   1656 C  CE  . LYS   A 1 220 ? -32.317 -27.121 3.878   1.00 47.87 ? 350 LYS   A CE  1 
ATOM   1657 N  NZ  . LYS   A 1 220 ? -33.085 -27.643 5.041   1.00 52.92 ? 350 LYS   A NZ  1 
ATOM   1658 N  N   . GLU   A 1 221 ? -31.582 -20.482 1.786   1.00 41.93 ? 351 GLU   A N   1 
ATOM   1659 C  CA  . GLU   A 1 221 ? -32.174 -19.421 0.981   1.00 42.69 ? 351 GLU   A CA  1 
ATOM   1660 C  C   . GLU   A 1 221 ? -31.187 -18.866 -0.035  1.00 43.44 ? 351 GLU   A C   1 
ATOM   1661 O  O   . GLU   A 1 221 ? -31.586 -18.491 -1.141  1.00 42.38 ? 351 GLU   A O   1 
ATOM   1662 C  CB  . GLU   A 1 221 ? -32.680 -18.313 1.906   1.00 45.69 ? 351 GLU   A CB  1 
ATOM   1663 C  CG  . GLU   A 1 221 ? -33.984 -18.657 2.627   1.00 44.90 ? 351 GLU   A CG  1 
ATOM   1664 C  CD  . GLU   A 1 221 ? -34.478 -17.552 3.551   1.00 50.13 ? 351 GLU   A CD  1 
ATOM   1665 O  OE1 . GLU   A 1 221 ? -33.643 -16.919 4.233   1.00 49.53 ? 351 GLU   A OE1 1 
ATOM   1666 O  OE2 . GLU   A 1 221 ? -35.706 -17.321 3.596   1.00 58.19 ? 351 GLU   A OE2 1 
ATOM   1667 N  N   . HIS   A 1 222 ? -29.901 -18.813 0.311   1.00 40.85 ? 352 HIS   A N   1 
ATOM   1668 C  CA  . HIS   A 1 222 ? -28.878 -18.297 -0.586  1.00 40.23 ? 352 HIS   A CA  1 
ATOM   1669 C  C   . HIS   A 1 222 ? -28.331 -19.354 -1.533  1.00 42.01 ? 352 HIS   A C   1 
ATOM   1670 O  O   . HIS   A 1 222 ? -27.654 -19.002 -2.503  1.00 43.22 ? 352 HIS   A O   1 
ATOM   1671 C  CB  . HIS   A 1 222 ? -27.723 -17.707 0.228   1.00 35.39 ? 352 HIS   A CB  1 
ATOM   1672 C  CG  . HIS   A 1 222 ? -28.070 -16.427 0.917   1.00 39.04 ? 352 HIS   A CG  1 
ATOM   1673 N  ND1 . HIS   A 1 222 ? -27.964 -15.199 0.303   1.00 40.29 ? 352 HIS   A ND1 1 
ATOM   1674 C  CD2 . HIS   A 1 222 ? -28.530 -16.185 2.167   1.00 35.27 ? 352 HIS   A CD2 1 
ATOM   1675 C  CE1 . HIS   A 1 222 ? -28.343 -14.255 1.145   1.00 38.44 ? 352 HIS   A CE1 1 
ATOM   1676 N  NE2 . HIS   A 1 222 ? -28.688 -14.826 2.284   1.00 35.74 ? 352 HIS   A NE2 1 
ATOM   1677 N  N   . PHE   A 1 223 ? -28.608 -20.629 -1.283  1.00 41.86 ? 353 PHE   A N   1 
ATOM   1678 C  CA  . PHE   A 1 223 ? -28.006 -21.719 -2.032  1.00 43.84 ? 353 PHE   A CA  1 
ATOM   1679 C  C   . PHE   A 1 223 ? -29.083 -22.646 -2.580  1.00 47.52 ? 353 PHE   A C   1 
ATOM   1680 O  O   . PHE   A 1 223 ? -28.916 -23.865 -2.641  1.00 47.46 ? 353 PHE   A O   1 
ATOM   1681 C  CB  . PHE   A 1 223 ? -26.990 -22.463 -1.170  1.00 43.99 ? 353 PHE   A CB  1 
ATOM   1682 C  CG  . PHE   A 1 223 ? -25.741 -21.668 -0.903  1.00 41.05 ? 353 PHE   A CG  1 
ATOM   1683 C  CD1 . PHE   A 1 223 ? -24.750 -21.575 -1.867  1.00 43.29 ? 353 PHE   A CD1 1 
ATOM   1684 C  CD2 . PHE   A 1 223 ? -25.573 -20.984 0.292   1.00 39.92 ? 353 PHE   A CD2 1 
ATOM   1685 C  CE1 . PHE   A 1 223 ? -23.601 -20.842 -1.638  1.00 43.58 ? 353 PHE   A CE1 1 
ATOM   1686 C  CE2 . PHE   A 1 223 ? -24.425 -20.242 0.529   1.00 38.10 ? 353 PHE   A CE2 1 
ATOM   1687 C  CZ  . PHE   A 1 223 ? -23.437 -20.171 -0.439  1.00 42.48 ? 353 PHE   A CZ  1 
ATOM   1688 N  N   . ASN   A 1 224 ? -30.210 -22.066 -2.992  1.00 44.98 ? 354 ASN   A N   1 
ATOM   1689 C  CA  . ASN   A 1 224 ? -31.239 -22.782 -3.755  1.00 51.18 ? 354 ASN   A CA  1 
ATOM   1690 C  C   . ASN   A 1 224 ? -31.784 -23.988 -2.988  1.00 51.69 ? 354 ASN   A C   1 
ATOM   1691 O  O   . ASN   A 1 224 ? -32.008 -25.057 -3.555  1.00 49.88 ? 354 ASN   A O   1 
ATOM   1692 C  CB  . ASN   A 1 224 ? -30.712 -23.210 -5.130  1.00 54.85 ? 354 ASN   A CB  1 
ATOM   1693 C  CG  . ASN   A 1 224 ? -30.570 -22.039 -6.095  1.00 55.76 ? 354 ASN   A CG  1 
ATOM   1694 O  OD1 . ASN   A 1 224 ? -31.410 -21.137 -6.131  1.00 58.34 ? 354 ASN   A OD1 1 
ATOM   1695 N  ND2 . ASN   A 1 224 ? -29.504 -22.055 -6.886  1.00 58.66 ? 354 ASN   A ND2 1 
ATOM   1696 N  N   . ASN   A 1 225 ? -32.013 -23.815 -1.689  1.00 46.56 ? 355 ASN   A N   1 
ATOM   1697 C  CA  . ASN   A 1 225 ? -32.602 -24.850 -0.841  1.00 50.53 ? 355 ASN   A CA  1 
ATOM   1698 C  C   . ASN   A 1 225 ? -31.779 -26.141 -0.840  1.00 47.86 ? 355 ASN   A C   1 
ATOM   1699 O  O   . ASN   A 1 225 ? -32.317 -27.220 -0.566  1.00 50.63 ? 355 ASN   A O   1 
ATOM   1700 C  CB  . ASN   A 1 225 ? -34.054 -25.130 -1.265  1.00 47.81 ? 355 ASN   A CB  1 
ATOM   1701 C  CG  . ASN   A 1 225 ? -34.875 -25.788 -0.167  1.00 54.33 ? 355 ASN   A CG  1 
ATOM   1702 O  OD1 . ASN   A 1 225 ? -34.637 -25.565 1.022   1.00 54.36 ? 355 ASN   A OD1 1 
ATOM   1703 N  ND2 . ASN   A 1 225 ? -35.862 -26.588 -0.563  1.00 57.75 ? 355 ASN   A ND2 1 
ATOM   1704 N  N   . LYS   A 1 226 ? -30.484 -26.045 -1.146  1.00 48.97 ? 357 LYS   A N   1 
ATOM   1705 C  CA  . LYS   A 1 226 ? -29.588 -27.191 -1.159  1.00 50.49 ? 357 LYS   A CA  1 
ATOM   1706 C  C   . LYS   A 1 226 ? -29.376 -27.726 0.259   1.00 48.18 ? 357 LYS   A C   1 
ATOM   1707 O  O   . LYS   A 1 226 ? -29.773 -27.112 1.255   1.00 50.17 ? 357 LYS   A O   1 
ATOM   1708 C  CB  . LYS   A 1 226 ? -28.247 -26.802 -1.784  1.00 50.31 ? 357 LYS   A CB  1 
ATOM   1709 C  CG  . LYS   A 1 226 ? -28.095 -27.136 -3.270  1.00 49.42 ? 357 LYS   A CG  1 
ATOM   1710 C  CD  . LYS   A 1 226 ? -26.741 -26.670 -3.807  1.00 50.88 ? 357 LYS   A CD  1 
ATOM   1711 C  CE  . LYS   A 1 226 ? -25.852 -27.853 -4.203  1.00 55.33 ? 357 LYS   A CE  1 
ATOM   1712 N  NZ  . LYS   A 1 226 ? -24.501 -27.430 -4.685  1.00 57.83 ? 357 LYS   A NZ  1 
ATOM   1713 N  N   . THR   A 1 227 ? -28.726 -28.886 0.346   1.00 50.99 ? 358 THR   A N   1 
ATOM   1714 C  CA  . THR   A 1 227 ? -28.411 -29.482 1.640   1.00 50.84 ? 358 THR   A CA  1 
ATOM   1715 C  C   . THR   A 1 227 ? -27.197 -28.798 2.256   1.00 45.25 ? 358 THR   A C   1 
ATOM   1716 O  O   . THR   A 1 227 ? -26.140 -28.703 1.626   1.00 46.58 ? 358 THR   A O   1 
ATOM   1717 C  CB  . THR   A 1 227 ? -28.148 -30.985 1.512   1.00 49.97 ? 358 THR   A CB  1 
ATOM   1718 O  OG1 . THR   A 1 227 ? -29.084 -31.571 0.598   1.00 55.18 ? 358 THR   A OG1 1 
ATOM   1719 C  CG2 . THR   A 1 227 ? -28.287 -31.662 2.876   1.00 45.47 ? 358 THR   A CG2 1 
ATOM   1720 N  N   . ILE   A 1 228 ? -27.346 -28.347 3.499   1.00 43.97 ? 359 ILE   A N   1 
ATOM   1721 C  CA  . ILE   A 1 228 ? -26.319 -27.589 4.207   1.00 42.47 ? 359 ILE   A CA  1 
ATOM   1722 C  C   . ILE   A 1 228 ? -25.588 -28.534 5.153   1.00 40.47 ? 359 ILE   A C   1 
ATOM   1723 O  O   . ILE   A 1 228 ? -26.194 -29.081 6.082   1.00 39.95 ? 359 ILE   A O   1 
ATOM   1724 C  CB  . ILE   A 1 228 ? -26.933 -26.404 4.970   1.00 38.56 ? 359 ILE   A CB  1 
ATOM   1725 C  CG1 . ILE   A 1 228 ? -27.744 -25.516 4.017   1.00 40.88 ? 359 ILE   A CG1 1 
ATOM   1726 C  CG2 . ILE   A 1 228 ? -25.845 -25.590 5.660   1.00 37.85 ? 359 ILE   A CG2 1 
ATOM   1727 C  CD1 . ILE   A 1 228 ? -27.025 -25.186 2.727   1.00 40.52 ? 359 ILE   A CD1 1 
ATOM   1728 N  N   . ILE   A 1 229 ? -24.287 -28.716 4.931   1.00 42.19 ? 360 ILE   A N   1 
ATOM   1729 C  CA  . ILE   A 1 229 ? -23.463 -29.631 5.713   1.00 39.82 ? 360 ILE   A CA  1 
ATOM   1730 C  C   . ILE   A 1 229 ? -22.290 -28.865 6.309   1.00 40.34 ? 360 ILE   A C   1 
ATOM   1731 O  O   . ILE   A 1 229 ? -21.636 -28.073 5.620   1.00 36.14 ? 360 ILE   A O   1 
ATOM   1732 C  CB  . ILE   A 1 229 ? -22.949 -30.811 4.861   1.00 41.24 ? 360 ILE   A CB  1 
ATOM   1733 C  CG1 . ILE   A 1 229 ? -24.105 -31.696 4.391   1.00 41.59 ? 360 ILE   A CG1 1 
ATOM   1734 C  CG2 . ILE   A 1 229 ? -21.930 -31.624 5.648   1.00 41.31 ? 360 ILE   A CG2 1 
ATOM   1735 C  CD1 . ILE   A 1 229 ? -25.303 -31.680 5.310   1.00 47.12 ? 360 ILE   A CD1 1 
ATOM   1736 N  N   . PHE   A 1 230 ? -22.015 -29.119 7.586   1.00 38.62 ? 361 PHE   A N   1 
ATOM   1737 C  CA  . PHE   A 1 230 ? -20.868 -28.544 8.273   1.00 39.31 ? 361 PHE   A CA  1 
ATOM   1738 C  C   . PHE   A 1 230 ? -19.773 -29.589 8.418   1.00 37.46 ? 361 PHE   A C   1 
ATOM   1739 O  O   . PHE   A 1 230 ? -20.055 -30.768 8.665   1.00 38.44 ? 361 PHE   A O   1 
ATOM   1740 C  CB  . PHE   A 1 230 ? -21.257 -28.030 9.658   1.00 38.13 ? 361 PHE   A CB  1 
ATOM   1741 C  CG  . PHE   A 1 230 ? -22.074 -26.774 9.631   1.00 37.36 ? 361 PHE   A CG  1 
ATOM   1742 C  CD1 . PHE   A 1 230 ? -21.497 -25.551 9.322   1.00 32.10 ? 361 PHE   A CD1 1 
ATOM   1743 C  CD2 . PHE   A 1 230 ? -23.427 -26.820 9.921   1.00 34.42 ? 361 PHE   A CD2 1 
ATOM   1744 C  CE1 . PHE   A 1 230 ? -22.256 -24.403 9.300   1.00 32.62 ? 361 PHE   A CE1 1 
ATOM   1745 C  CE2 . PHE   A 1 230 ? -24.193 -25.673 9.899   1.00 39.55 ? 361 PHE   A CE2 1 
ATOM   1746 C  CZ  . PHE   A 1 230 ? -23.608 -24.461 9.589   1.00 29.16 ? 361 PHE   A CZ  1 
ATOM   1747 N  N   . GLN   A 1 231 ? -18.528 -29.149 8.277   1.00 37.52 ? 362 GLN   A N   1 
ATOM   1748 C  CA  . GLN   A 1 231 ? -17.377 -30.020 8.432   1.00 38.25 ? 362 GLN   A CA  1 
ATOM   1749 C  C   . GLN   A 1 231 ? -16.292 -29.271 9.188   1.00 41.08 ? 362 GLN   A C   1 
ATOM   1750 O  O   . GLN   A 1 231 ? -16.253 -28.033 9.162   1.00 34.83 ? 362 GLN   A O   1 
ATOM   1751 C  CB  . GLN   A 1 231 ? -16.835 -30.496 7.075   1.00 42.11 ? 362 GLN   A CB  1 
ATOM   1752 C  CG  . GLN   A 1 231 ? -17.654 -31.614 6.446   1.00 43.00 ? 362 GLN   A CG  1 
ATOM   1753 C  CD  . GLN   A 1 231 ? -17.487 -32.934 7.167   1.00 43.55 ? 362 GLN   A CD  1 
ATOM   1754 O  OE1 . GLN   A 1 231 ? -18.182 -33.215 8.145   1.00 42.24 ? 362 GLN   A OE1 1 
ATOM   1755 N  NE2 . GLN   A 1 231 ? -16.565 -33.757 6.684   1.00 51.16 ? 362 GLN   A NE2 1 
ATOM   1756 N  N   . PRO   A 1 232 ? -15.408 -29.991 9.883   1.00 38.59 ? 363 PRO   A N   1 
ATOM   1757 C  CA  . PRO   A 1 232 ? -14.326 -29.315 10.598  1.00 38.38 ? 363 PRO   A CA  1 
ATOM   1758 C  C   . PRO   A 1 232 ? -13.328 -28.723 9.632   1.00 38.99 ? 363 PRO   A C   1 
ATOM   1759 O  O   . PRO   A 1 232 ? -13.197 -29.184 8.480   1.00 42.72 ? 363 PRO   A O   1 
ATOM   1760 C  CB  . PRO   A 1 232 ? -13.703 -30.444 11.442  1.00 39.18 ? 363 PRO   A CB  1 
ATOM   1761 C  CG  . PRO   A 1 232 ? -14.026 -31.690 10.668  1.00 38.44 ? 363 PRO   A CG  1 
ATOM   1762 C  CD  . PRO   A 1 232 ? -15.393 -31.452 10.102  1.00 39.95 ? 363 PRO   A CD  1 
ATOM   1763 N  N   . PRO   A 1 233 ? -12.591 -27.690 10.040  1.00 36.69 ? 364 PRO   A N   1 
ATOM   1764 C  CA  . PRO   A 1 233 ? -11.612 -27.077 9.139   1.00 40.62 ? 364 PRO   A CA  1 
ATOM   1765 C  C   . PRO   A 1 233 ? -10.672 -28.121 8.550   1.00 44.61 ? 364 PRO   A C   1 
ATOM   1766 O  O   . PRO   A 1 233 ? -10.247 -29.058 9.231   1.00 43.61 ? 364 PRO   A O   1 
ATOM   1767 C  CB  . PRO   A 1 233 ? -10.872 -26.089 10.047  1.00 38.38 ? 364 PRO   A CB  1 
ATOM   1768 C  CG  . PRO   A 1 233 ? -11.891 -25.726 11.087  1.00 34.40 ? 364 PRO   A CG  1 
ATOM   1769 C  CD  . PRO   A 1 233 ? -12.602 -27.033 11.360  1.00 37.74 ? 364 PRO   A CD  1 
ATOM   1770 N  N   . SER   A 1 234 ? -10.352 -27.953 7.269   1.00 44.78 ? 365 SER   A N   1 
ATOM   1771 C  CA  . SER   A 1 234 ? -9.581  -28.947 6.520   1.00 49.23 ? 365 SER   A CA  1 
ATOM   1772 C  C   . SER   A 1 234 ? -8.086  -28.649 6.541   1.00 53.05 ? 365 SER   A C   1 
ATOM   1773 O  O   . SER   A 1 234 ? -7.419  -28.652 5.508   1.00 57.80 ? 365 SER   A O   1 
ATOM   1774 C  CB  . SER   A 1 234 ? -10.097 -29.034 5.088   1.00 48.97 ? 365 SER   A CB  1 
ATOM   1775 O  OG  . SER   A 1 234 ? -10.068 -27.771 4.456   1.00 48.49 ? 365 SER   A OG  1 
ATOM   1776 N  N   . GLY   A 1 235 ? -7.547  -28.387 7.722   1.00 50.50 ? 366 GLY   A N   1 
ATOM   1777 C  CA  . GLY   A 1 235 ? -6.130  -28.139 7.883   1.00 49.52 ? 366 GLY   A CA  1 
ATOM   1778 C  C   . GLY   A 1 235 ? -5.824  -26.668 8.101   1.00 51.80 ? 366 GLY   A C   1 
ATOM   1779 O  O   . GLY   A 1 235 ? -6.677  -25.788 7.973   1.00 51.02 ? 366 GLY   A O   1 
ATOM   1780 N  N   . GLY   A 1 236 ? -4.565  -26.420 8.431   1.00 47.27 ? 367 GLY   A N   1 
ATOM   1781 C  CA  . GLY   A 1 236 ? -4.083  -25.098 8.761   1.00 43.18 ? 367 GLY   A CA  1 
ATOM   1782 C  C   . GLY   A 1 236 ? -3.501  -25.069 10.155  1.00 43.25 ? 367 GLY   A C   1 
ATOM   1783 O  O   . GLY   A 1 236 ? -3.292  -26.101 10.799  1.00 46.86 ? 367 GLY   A O   1 
ATOM   1784 N  N   . ASP   A 1 237 ? -3.240  -23.859 10.629  1.00 40.78 ? 368 ASP   A N   1 
ATOM   1785 C  CA  . ASP   A 1 237 ? -2.657  -23.729 11.950  1.00 37.11 ? 368 ASP   A CA  1 
ATOM   1786 C  C   . ASP   A 1 237 ? -3.705  -23.946 13.032  1.00 34.96 ? 368 ASP   A C   1 
ATOM   1787 O  O   . ASP   A 1 237 ? -4.912  -23.839 12.800  1.00 35.28 ? 368 ASP   A O   1 
ATOM   1788 C  CB  . ASP   A 1 237 ? -1.983  -22.370 12.109  1.00 39.64 ? 368 ASP   A CB  1 
ATOM   1789 C  CG  . ASP   A 1 237 ? -0.719  -22.257 11.282  1.00 43.90 ? 368 ASP   A CG  1 
ATOM   1790 O  OD1 . ASP   A 1 237 ? 0.349   -22.670 11.785  1.00 43.77 ? 368 ASP   A OD1 1 
ATOM   1791 O  OD2 . ASP   A 1 237 ? -0.798  -21.773 10.135  1.00 46.81 ? 368 ASP   A OD2 1 
ATOM   1792 N  N   . LEU   A 1 238 ? -3.214  -24.265 14.234  1.00 31.47 ? 369 LEU   A N   1 
ATOM   1793 C  CA  . LEU   A 1 238 ? -4.092  -24.550 15.362  1.00 32.35 ? 369 LEU   A CA  1 
ATOM   1794 C  C   . LEU   A 1 238 ? -5.041  -23.390 15.636  1.00 29.52 ? 369 LEU   A C   1 
ATOM   1795 O  O   . LEU   A 1 238 ? -6.174  -23.604 16.077  1.00 28.19 ? 369 LEU   A O   1 
ATOM   1796 C  CB  . LEU   A 1 238 ? -3.239  -24.842 16.595  1.00 30.41 ? 369 LEU   A CB  1 
ATOM   1797 C  CG  . LEU   A 1 238 ? -2.655  -26.253 16.702  1.00 37.96 ? 369 LEU   A CG  1 
ATOM   1798 C  CD1 . LEU   A 1 238 ? -1.835  -26.385 17.975  1.00 38.61 ? 369 LEU   A CD1 1 
ATOM   1799 C  CD2 . LEU   A 1 238 ? -3.763  -27.291 16.656  1.00 38.78 ? 369 LEU   A CD2 1 
ATOM   1800 N  N   . GLU   A 1 239 ? -4.594  -22.159 15.379  1.00 29.41 ? 370 GLU   A N   1 
ATOM   1801 C  CA  . GLU   A 1 239 ? -5.401  -20.982 15.684  1.00 28.63 ? 370 GLU   A CA  1 
ATOM   1802 C  C   . GLU   A 1 239 ? -6.693  -20.952 14.881  1.00 29.55 ? 370 GLU   A C   1 
ATOM   1803 O  O   . GLU   A 1 239 ? -7.683  -20.361 15.324  1.00 30.87 ? 370 GLU   A O   1 
ATOM   1804 C  CB  . GLU   A 1 239 ? -4.580  -19.717 15.418  1.00 28.40 ? 370 GLU   A CB  1 
ATOM   1805 C  CG  . GLU   A 1 239 ? -3.496  -19.464 16.448  1.00 28.71 ? 370 GLU   A CG  1 
ATOM   1806 C  CD  . GLU   A 1 239 ? -2.250  -20.313 16.212  1.00 31.73 ? 370 GLU   A CD  1 
ATOM   1807 O  OE1 . GLU   A 1 239 ? -2.121  -20.892 15.114  1.00 30.79 ? 370 GLU   A OE1 1 
ATOM   1808 O  OE2 . GLU   A 1 239 ? -1.408  -20.399 17.131  1.00 33.00 ? 370 GLU   A OE2 1 
ATOM   1809 N  N   . ILE   A 1 240 ? -6.697  -21.557 13.695  1.00 29.67 ? 371 ILE   A N   1 
ATOM   1810 C  CA  . ILE   A 1 240 ? -7.859  -21.531 12.827  1.00 29.84 ? 371 ILE   A CA  1 
ATOM   1811 C  C   . ILE   A 1 240 ? -8.604  -22.858 12.786  1.00 27.71 ? 371 ILE   A C   1 
ATOM   1812 O  O   . ILE   A 1 240 ? -9.822  -22.848 12.600  1.00 29.67 ? 371 ILE   A O   1 
ATOM   1813 C  CB  . ILE   A 1 240 ? -7.446  -21.088 11.417  1.00 35.50 ? 371 ILE   A CB  1 
ATOM   1814 C  CG1 . ILE   A 1 240 ? -7.090  -19.592 11.421  1.00 34.25 ? 371 ILE   A CG1 1 
ATOM   1815 C  CG2 . ILE   A 1 240 ? -8.561  -21.370 10.402  1.00 37.52 ? 371 ILE   A CG2 1 
ATOM   1816 C  CD1 . ILE   A 1 240 ? -6.625  -19.053 10.087  1.00 39.85 ? 371 ILE   A CD1 1 
ATOM   1817 N  N   . THR   A 1 241 ? -7.927  -23.999 12.980  1.00 27.64 ? 372 THR   A N   1 
ATOM   1818 C  CA  . THR   A 1 241 ? -8.659  -25.254 13.100  1.00 28.93 ? 372 THR   A CA  1 
ATOM   1819 C  C   . THR   A 1 241 ? -9.413  -25.319 14.418  1.00 30.60 ? 372 THR   A C   1 
ATOM   1820 O  O   . THR   A 1 241 ? -10.458 -25.971 14.495  1.00 29.49 ? 372 THR   A O   1 
ATOM   1821 C  CB  . THR   A 1 241 ? -7.706  -26.445 12.960  1.00 30.84 ? 372 THR   A CB  1 
ATOM   1822 O  OG1 . THR   A 1 241 ? -6.675  -26.381 13.953  1.00 28.04 ? 372 THR   A OG1 1 
ATOM   1823 C  CG2 . THR   A 1 241 ? -7.073  -26.455 11.572  1.00 35.59 ? 372 THR   A CG2 1 
ATOM   1824 N  N   . MET   A 1 242 ? -8.901  -24.661 15.459  1.00 30.00 ? 373 MET   A N   1 
ATOM   1825 C  CA  . MET   A 1 242 ? -9.584  -24.515 16.736  1.00 26.07 ? 373 MET   A CA  1 
ATOM   1826 C  C   . MET   A 1 242 ? -10.248 -23.148 16.827  1.00 25.96 ? 373 MET   A C   1 
ATOM   1827 O  O   . MET   A 1 242 ? -9.890  -22.211 16.114  1.00 23.57 ? 373 MET   A O   1 
ATOM   1828 C  CB  . MET   A 1 242 ? -8.607  -24.666 17.905  1.00 25.62 ? 373 MET   A CB  1 
ATOM   1829 C  CG  . MET   A 1 242 ? -7.780  -25.956 17.919  1.00 29.34 ? 373 MET   A CG  1 
ATOM   1830 S  SD  . MET   A 1 242 ? -8.769  -27.363 18.420  1.00 39.47 ? 373 MET   A SD  1 
ATOM   1831 C  CE  . MET   A 1 242 ? -7.480  -28.530 18.858  1.00 45.68 ? 373 MET   A CE  1 
ATOM   1832 N  N   . HIS   A 1 243 ? -11.211 -23.040 17.736  1.00 23.12 ? 374 HIS   A N   1 
ATOM   1833 C  CA  . HIS   A 1 243 ? -11.757 -21.746 18.132  1.00 23.23 ? 374 HIS   A CA  1 
ATOM   1834 C  C   . HIS   A 1 243 ? -10.758 -21.086 19.074  1.00 25.01 ? 374 HIS   A C   1 
ATOM   1835 O  O   . HIS   A 1 243 ? -10.590 -21.524 20.218  1.00 22.24 ? 374 HIS   A O   1 
ATOM   1836 C  CB  . HIS   A 1 243 ? -13.131 -21.922 18.775  1.00 22.94 ? 374 HIS   A CB  1 
ATOM   1837 C  CG  . HIS   A 1 243 ? -13.610 -20.721 19.531  1.00 24.63 ? 374 HIS   A CG  1 
ATOM   1838 N  ND1 . HIS   A 1 243 ? -13.602 -19.451 18.998  1.00 23.00 ? 374 HIS   A ND1 1 
ATOM   1839 C  CD2 . HIS   A 1 243 ? -14.154 -20.608 20.766  1.00 26.43 ? 374 HIS   A CD2 1 
ATOM   1840 C  CE1 . HIS   A 1 243 ? -14.101 -18.603 19.881  1.00 25.38 ? 374 HIS   A CE1 1 
ATOM   1841 N  NE2 . HIS   A 1 243 ? -14.448 -19.280 20.961  1.00 24.43 ? 374 HIS   A NE2 1 
ATOM   1842 N  N   . SER   A 1 244 ? -10.076 -20.049 18.582  1.00 24.49 ? 375 SER   A N   1 
ATOM   1843 C  CA  . SER   A 1 244 ? -9.025  -19.358 19.319  1.00 26.93 ? 375 SER   A CA  1 
ATOM   1844 C  C   . SER   A 1 244 ? -9.545  -18.036 19.858  1.00 25.11 ? 375 SER   A C   1 
ATOM   1845 O  O   . SER   A 1 244 ? -10.281 -17.327 19.168  1.00 25.16 ? 375 SER   A O   1 
ATOM   1846 C  CB  . SER   A 1 244 ? -7.810  -19.093 18.422  1.00 24.44 ? 375 SER   A CB  1 
ATOM   1847 O  OG  . SER   A 1 244 ? -7.022  -20.257 18.283  1.00 35.16 ? 375 SER   A OG  1 
ATOM   1848 N  N   . PHE   A 1 245 ? -9.145  -17.700 21.083  1.00 22.99 ? 376 PHE   A N   1 
ATOM   1849 C  CA  . PHE   A 1 245 ? -9.526  -16.433 21.696  1.00 26.15 ? 376 PHE   A CA  1 
ATOM   1850 C  C   . PHE   A 1 245 ? -8.654  -16.226 22.925  1.00 29.57 ? 376 PHE   A C   1 
ATOM   1851 O  O   . PHE   A 1 245 ? -7.976  -17.145 23.395  1.00 25.55 ? 376 PHE   A O   1 
ATOM   1852 C  CB  . PHE   A 1 245 ? -11.013 -16.410 22.069  1.00 22.27 ? 376 PHE   A CB  1 
ATOM   1853 C  CG  . PHE   A 1 245 ? -11.412 -17.505 23.016  1.00 24.40 ? 376 PHE   A CG  1 
ATOM   1854 C  CD1 . PHE   A 1 245 ? -11.627 -18.795 22.555  1.00 24.28 ? 376 PHE   A CD1 1 
ATOM   1855 C  CD2 . PHE   A 1 245 ? -11.560 -17.249 24.369  1.00 26.70 ? 376 PHE   A CD2 1 
ATOM   1856 C  CE1 . PHE   A 1 245 ? -11.985 -19.806 23.424  1.00 26.26 ? 376 PHE   A CE1 1 
ATOM   1857 C  CE2 . PHE   A 1 245 ? -11.921 -18.256 25.245  1.00 27.63 ? 376 PHE   A CE2 1 
ATOM   1858 C  CZ  . PHE   A 1 245 ? -12.133 -19.536 24.773  1.00 26.47 ? 376 PHE   A CZ  1 
ATOM   1859 N  N   . ASN   A 1 246 ? -8.687  -15.006 23.447  1.00 27.48 ? 377 ASN   A N   1 
ATOM   1860 C  CA  . ASN   A 1 246 ? -7.917  -14.637 24.627  1.00 27.86 ? 377 ASN   A CA  1 
ATOM   1861 C  C   . ASN   A 1 246 ? -8.861  -14.422 25.801  1.00 28.89 ? 377 ASN   A C   1 
ATOM   1862 O  O   . ASN   A 1 246 ? -9.752  -13.571 25.740  1.00 27.54 ? 377 ASN   A O   1 
ATOM   1863 C  CB  . ASN   A 1 246 ? -7.076  -13.388 24.375  1.00 27.21 ? 377 ASN   A CB  1 
ATOM   1864 C  CG  . ASN   A 1 246 ? -6.069  -13.144 25.479  1.00 29.62 ? 377 ASN   A CG  1 
ATOM   1865 O  OD1 . ASN   A 1 246 ? -6.439  -12.962 26.638  1.00 28.69 ? 377 ASN   A OD1 1 
ATOM   1866 N  ND2 . ASN   A 1 246 ? -4.789  -13.157 25.131  1.00 33.29 ? 377 ASN   A ND2 1 
ATOM   1867 N  N   . CYS   A 1 247 ? -8.661  -15.192 26.865  1.00 28.33 ? 378 CYS   A N   1 
ATOM   1868 C  CA  . CYS   A 1 247 ? -9.447  -15.085 28.090  1.00 30.60 ? 378 CYS   A CA  1 
ATOM   1869 C  C   . CYS   A 1 247 ? -8.532  -14.632 29.223  1.00 35.03 ? 378 CYS   A C   1 
ATOM   1870 O  O   . CYS   A 1 247 ? -7.671  -15.397 29.668  1.00 30.88 ? 378 CYS   A O   1 
ATOM   1871 C  CB  . CYS   A 1 247 ? -10.118 -16.419 28.426  1.00 31.70 ? 378 CYS   A CB  1 
ATOM   1872 S  SG  . CYS   A 1 247 ? -10.977 -16.423 30.009  1.00 34.88 ? 378 CYS   A SG  1 
ATOM   1873 N  N   . ARG   A 1 248 ? -8.740  -13.401 29.701  1.00 36.15 ? 379 ARG   A N   1 
ATOM   1874 C  CA  . ARG   A 1 248 ? -7.961  -12.828 30.797  1.00 36.18 ? 379 ARG   A CA  1 
ATOM   1875 C  C   . ARG   A 1 248 ? -6.462  -12.838 30.498  1.00 33.04 ? 379 ARG   A C   1 
ATOM   1876 O  O   . ARG   A 1 248 ? -5.632  -12.945 31.408  1.00 37.61 ? 379 ARG   A O   1 
ATOM   1877 C  CB  . ARG   A 1 248 ? -8.225  -13.582 32.091  1.00 35.60 ? 379 ARG   A CB  1 
ATOM   1878 C  CG  . ARG   A 1 248 ? -9.667  -13.716 32.542  1.00 43.52 ? 379 ARG   A CG  1 
ATOM   1879 C  CD  . ARG   A 1 248 ? -9.824  -13.420 34.055  1.00 47.87 ? 379 ARG   A CD  1 
ATOM   1880 N  NE  . ARG   A 1 248 ? -10.791 -14.299 34.676  1.00 51.72 ? 379 ARG   A NE  1 
ATOM   1881 C  CZ  . ARG   A 1 248 ? -10.502 -15.113 35.676  1.00 55.97 ? 379 ARG   A CZ  1 
ATOM   1882 N  NH1 . ARG   A 1 248 ? -9.311  -15.090 36.282  1.00 54.07 ? 379 ARG   A NH1 1 
ATOM   1883 N  NH2 . ARG   A 1 248 ? -11.426 -15.974 36.067  1.00 48.40 ? 379 ARG   A NH2 1 
ATOM   1884 N  N   . GLY   A 1 249 ? -6.095  -12.683 29.227  1.00 29.04 ? 380 GLY   A N   1 
ATOM   1885 C  CA  . GLY   A 1 249 ? -4.712  -12.698 28.812  1.00 33.40 ? 380 GLY   A CA  1 
ATOM   1886 C  C   . GLY   A 1 249 ? -4.189  -14.050 28.377  1.00 34.87 ? 380 GLY   A C   1 
ATOM   1887 O  O   . GLY   A 1 249 ? -3.144  -14.108 27.719  1.00 33.90 ? 380 GLY   A O   1 
ATOM   1888 N  N   . GLU   A 1 250 ? -4.887  -15.132 28.721  1.00 34.82 ? 381 GLU   A N   1 
ATOM   1889 C  CA  . GLU   A 1 250 ? -4.493  -16.483 28.348  1.00 34.90 ? 381 GLU   A CA  1 
ATOM   1890 C  C   . GLU   A 1 250 ? -5.073  -16.819 26.979  1.00 34.78 ? 381 GLU   A C   1 
ATOM   1891 O  O   . GLU   A 1 250 ? -6.215  -16.462 26.672  1.00 31.44 ? 381 GLU   A O   1 
ATOM   1892 C  CB  . GLU   A 1 250 ? -5.005  -17.489 29.379  1.00 32.52 ? 381 GLU   A CB  1 
ATOM   1893 C  CG  . GLU   A 1 250 ? -4.616  -17.197 30.825  1.00 35.17 ? 381 GLU   A CG  1 
ATOM   1894 C  CD  . GLU   A 1 250 ? -3.120  -17.174 31.057  1.00 39.10 ? 381 GLU   A CD  1 
ATOM   1895 O  OE1 . GLU   A 1 250 ? -2.369  -17.680 30.194  1.00 42.73 ? 381 GLU   A OE1 1 
ATOM   1896 O  OE2 . GLU   A 1 250 ? -2.702  -16.652 32.112  1.00 37.81 ? 381 GLU   A OE2 1 
ATOM   1897 N  N   . PHE   A 1 251 ? -4.289  -17.515 26.160  1.00 31.02 ? 382 PHE   A N   1 
ATOM   1898 C  CA  . PHE   A 1 251 ? -4.726  -17.902 24.822  1.00 30.58 ? 382 PHE   A CA  1 
ATOM   1899 C  C   . PHE   A 1 251 ? -5.371  -19.283 24.875  1.00 31.04 ? 382 PHE   A C   1 
ATOM   1900 O  O   . PHE   A 1 251 ? -4.694  -20.287 25.127  1.00 29.42 ? 382 PHE   A O   1 
ATOM   1901 C  CB  . PHE   A 1 251 ? -3.557  -17.850 23.843  1.00 30.23 ? 382 PHE   A CB  1 
ATOM   1902 C  CG  . PHE   A 1 251 ? -3.081  -16.455 23.559  1.00 35.07 ? 382 PHE   A CG  1 
ATOM   1903 C  CD1 . PHE   A 1 251 ? -3.653  -15.714 22.536  1.00 38.30 ? 382 PHE   A CD1 1 
ATOM   1904 C  CD2 . PHE   A 1 251 ? -2.098  -15.868 24.338  1.00 34.96 ? 382 PHE   A CD2 1 
ATOM   1905 C  CE1 . PHE   A 1 251 ? -3.233  -14.427 22.277  1.00 35.22 ? 382 PHE   A CE1 1 
ATOM   1906 C  CE2 . PHE   A 1 251 ? -1.679  -14.580 24.088  1.00 39.51 ? 382 PHE   A CE2 1 
ATOM   1907 C  CZ  . PHE   A 1 251 ? -2.244  -13.858 23.054  1.00 36.40 ? 382 PHE   A CZ  1 
ATOM   1908 N  N   . PHE   A 1 252 ? -6.685  -19.323 24.638  1.00 26.75 ? 383 PHE   A N   1 
ATOM   1909 C  CA  . PHE   A 1 252 ? -7.461  -20.555 24.630  1.00 25.46 ? 383 PHE   A CA  1 
ATOM   1910 C  C   . PHE   A 1 252 ? -7.572  -21.095 23.208  1.00 27.68 ? 383 PHE   A C   1 
ATOM   1911 O  O   . PHE   A 1 252 ? -7.741  -20.327 22.256  1.00 26.93 ? 383 PHE   A O   1 
ATOM   1912 C  CB  . PHE   A 1 252 ? -8.867  -20.299 25.180  1.00 26.11 ? 383 PHE   A CB  1 
ATOM   1913 C  CG  . PHE   A 1 252 ? -8.977  -20.386 26.681  1.00 26.95 ? 383 PHE   A CG  1 
ATOM   1914 C  CD1 . PHE   A 1 252 ? -8.199  -19.580 27.499  1.00 29.46 ? 383 PHE   A CD1 1 
ATOM   1915 C  CD2 . PHE   A 1 252 ? -9.889  -21.245 27.269  1.00 29.36 ? 383 PHE   A CD2 1 
ATOM   1916 C  CE1 . PHE   A 1 252 ? -8.314  -19.650 28.881  1.00 30.40 ? 383 PHE   A CE1 1 
ATOM   1917 C  CE2 . PHE   A 1 252 ? -10.011 -21.320 28.646  1.00 32.27 ? 383 PHE   A CE2 1 
ATOM   1918 C  CZ  . PHE   A 1 252 ? -9.220  -20.523 29.452  1.00 35.46 ? 383 PHE   A CZ  1 
ATOM   1919 N  N   . TYR   A 1 253 ? -7.499  -22.419 23.074  1.00 23.46 ? 384 TYR   A N   1 
ATOM   1920 C  CA  . TYR   A 1 253 ? -7.699  -23.109 21.801  1.00 24.30 ? 384 TYR   A CA  1 
ATOM   1921 C  C   . TYR   A 1 253 ? -8.727  -24.203 22.055  1.00 24.06 ? 384 TYR   A C   1 
ATOM   1922 O  O   . TYR   A 1 253 ? -8.451  -25.149 22.798  1.00 28.82 ? 384 TYR   A O   1 
ATOM   1923 C  CB  . TYR   A 1 253 ? -6.395  -23.716 21.272  1.00 24.08 ? 384 TYR   A CB  1 
ATOM   1924 C  CG  . TYR   A 1 253 ? -5.351  -22.745 20.765  1.00 23.02 ? 384 TYR   A CG  1 
ATOM   1925 C  CD1 . TYR   A 1 253 ? -4.719  -21.859 21.630  1.00 27.92 ? 384 TYR   A CD1 1 
ATOM   1926 C  CD2 . TYR   A 1 253 ? -4.960  -22.748 19.433  1.00 27.74 ? 384 TYR   A CD2 1 
ATOM   1927 C  CE1 . TYR   A 1 253 ? -3.749  -20.990 21.183  1.00 29.81 ? 384 TYR   A CE1 1 
ATOM   1928 C  CE2 . TYR   A 1 253 ? -3.979  -21.871 18.972  1.00 28.47 ? 384 TYR   A CE2 1 
ATOM   1929 C  CZ  . TYR   A 1 253 ? -3.381  -20.999 19.856  1.00 29.99 ? 384 TYR   A CZ  1 
ATOM   1930 O  OH  . TYR   A 1 253 ? -2.413  -20.122 19.413  1.00 32.73 ? 384 TYR   A OH  1 
ATOM   1931 N  N   . CYS   A 1 254 ? -9.900  -24.098 21.440  1.00 24.29 ? 385 CYS   A N   1 
ATOM   1932 C  CA  . CYS   A 1 254 ? -11.009 -24.995 21.738  1.00 25.07 ? 385 CYS   A CA  1 
ATOM   1933 C  C   . CYS   A 1 254 ? -11.453 -25.749 20.493  1.00 25.60 ? 385 CYS   A C   1 
ATOM   1934 O  O   . CYS   A 1 254 ? -11.656 -25.149 19.434  1.00 25.24 ? 385 CYS   A O   1 
ATOM   1935 C  CB  . CYS   A 1 254 ? -12.183 -24.224 22.347  1.00 27.00 ? 385 CYS   A CB  1 
ATOM   1936 S  SG  . CYS   A 1 254 ? -11.776 -23.468 23.942  1.00 32.29 ? 385 CYS   A SG  1 
ATOM   1937 N  N   . ASN   A 1 255 ? -11.605 -27.064 20.637  1.00 26.13 ? 386 ASN   A N   1 
ATOM   1938 C  CA  . ASN   A 1 255 ? -12.090 -27.938 19.574  1.00 30.23 ? 386 ASN   A CA  1 
ATOM   1939 C  C   . ASN   A 1 255 ? -13.604 -27.794 19.426  1.00 27.66 ? 386 ASN   A C   1 
ATOM   1940 O  O   . ASN   A 1 255 ? -14.356 -28.084 20.363  1.00 28.13 ? 386 ASN   A O   1 
ATOM   1941 C  CB  . ASN   A 1 255 ? -11.707 -29.380 19.900  1.00 32.83 ? 386 ASN   A CB  1 
ATOM   1942 C  CG  . ASN   A 1 255 ? -11.992 -30.338 18.765  1.00 32.29 ? 386 ASN   A CG  1 
ATOM   1943 O  OD1 . ASN   A 1 255 ? -13.020 -30.239 18.093  1.00 33.44 ? 386 ASN   A OD1 1 
ATOM   1944 N  ND2 . ASN   A 1 255 ? -11.088 -31.283 18.551  1.00 37.12 ? 386 ASN   A ND2 1 
ATOM   1945 N  N   . THR   A 1 256 ? -14.053 -27.366 18.246  1.00 26.14 ? 387 THR   A N   1 
ATOM   1946 C  CA  . THR   A 1 256 ? -15.458 -27.069 17.989  1.00 27.06 ? 387 THR   A CA  1 
ATOM   1947 C  C   . THR   A 1 256 ? -16.170 -28.162 17.203  1.00 28.67 ? 387 THR   A C   1 
ATOM   1948 O  O   . THR   A 1 256 ? -17.272 -27.929 16.700  1.00 27.45 ? 387 THR   A O   1 
ATOM   1949 C  CB  . THR   A 1 256 ? -15.579 -25.743 17.238  1.00 27.84 ? 387 THR   A CB  1 
ATOM   1950 O  OG1 . THR   A 1 256 ? -14.861 -25.839 15.999  1.00 23.12 ? 387 THR   A OG1 1 
ATOM   1951 C  CG2 . THR   A 1 256 ? -15.006 -24.603 18.079  1.00 24.34 ? 387 THR   A CG2 1 
ATOM   1952 N  N   . THR   A 1 257 ? -15.563 -29.342 17.077  1.00 32.32 ? 388 THR   A N   1 
ATOM   1953 C  CA  . THR   A 1 257 ? -16.179 -30.428 16.320  1.00 33.55 ? 388 THR   A CA  1 
ATOM   1954 C  C   . THR   A 1 257 ? -17.614 -30.686 16.768  1.00 36.31 ? 388 THR   A C   1 
ATOM   1955 O  O   . THR   A 1 257 ? -18.505 -30.895 15.936  1.00 36.02 ? 388 THR   A O   1 
ATOM   1956 C  CB  . THR   A 1 257 ? -15.329 -31.691 16.464  1.00 35.07 ? 388 THR   A CB  1 
ATOM   1957 O  OG1 . THR   A 1 257 ? -14.057 -31.484 15.837  1.00 38.75 ? 388 THR   A OG1 1 
ATOM   1958 C  CG2 . THR   A 1 257 ? -16.016 -32.888 15.828  1.00 39.55 ? 388 THR   A CG2 1 
ATOM   1959 N  N   . GLN   A 1 258 ? -17.863 -30.650 18.080  1.00 34.65 ? 389 GLN   A N   1 
ATOM   1960 C  CA  . GLN   A 1 258 ? -19.192 -30.919 18.620  1.00 34.59 ? 389 GLN   A CA  1 
ATOM   1961 C  C   . GLN   A 1 258 ? -20.168 -29.781 18.374  1.00 35.84 ? 389 GLN   A C   1 
ATOM   1962 O  O   . GLN   A 1 258 ? -21.374 -29.966 18.580  1.00 30.68 ? 389 GLN   A O   1 
ATOM   1963 C  CB  . GLN   A 1 258 ? -19.098 -31.168 20.118  1.00 35.90 ? 389 GLN   A CB  1 
ATOM   1964 C  CG  . GLN   A 1 258 ? -18.333 -32.404 20.487  1.00 35.52 ? 389 GLN   A CG  1 
ATOM   1965 C  CD  . GLN   A 1 258 ? -18.141 -32.493 21.981  1.00 40.33 ? 389 GLN   A CD  1 
ATOM   1966 O  OE1 . GLN   A 1 258 ? -18.907 -33.155 22.680  1.00 45.01 ? 389 GLN   A OE1 1 
ATOM   1967 N  NE2 . GLN   A 1 258 ? -17.124 -31.804 22.486  1.00 37.17 ? 389 GLN   A NE2 1 
ATOM   1968 N  N   . LEU   A 1 259 ? -19.676 -28.605 17.981  1.00 32.61 ? 390 LEU   A N   1 
ATOM   1969 C  CA  . LEU   A 1 259 ? -20.554 -27.489 17.658  1.00 31.80 ? 390 LEU   A CA  1 
ATOM   1970 C  C   . LEU   A 1 259 ? -21.085 -27.590 16.239  1.00 33.96 ? 390 LEU   A C   1 
ATOM   1971 O  O   . LEU   A 1 259 ? -22.191 -27.123 15.955  1.00 39.47 ? 390 LEU   A O   1 
ATOM   1972 C  CB  . LEU   A 1 259 ? -19.798 -26.170 17.820  1.00 33.40 ? 390 LEU   A CB  1 
ATOM   1973 C  CG  . LEU   A 1 259 ? -19.733 -25.564 19.215  1.00 34.10 ? 390 LEU   A CG  1 
ATOM   1974 C  CD1 . LEU   A 1 259 ? -19.342 -24.095 19.113  1.00 27.35 ? 390 LEU   A CD1 1 
ATOM   1975 C  CD2 . LEU   A 1 259 ? -21.066 -25.721 19.928  1.00 33.19 ? 390 LEU   A CD2 1 
ATOM   1976 N  N   . PHE   A 1 260 ? -20.302 -28.175 15.340  1.00 36.49 ? 391 PHE   A N   1 
ATOM   1977 C  CA  . PHE   A 1 260 ? -20.634 -28.225 13.926  1.00 37.92 ? 391 PHE   A CA  1 
ATOM   1978 C  C   . PHE   A 1 260 ? -20.793 -29.668 13.483  1.00 45.50 ? 391 PHE   A C   1 
ATOM   1979 O  O   . PHE   A 1 260 ? -20.153 -30.102 12.519  1.00 51.27 ? 391 PHE   A O   1 
ATOM   1980 C  CB  . PHE   A 1 260 ? -19.549 -27.523 13.111  1.00 35.56 ? 391 PHE   A CB  1 
ATOM   1981 C  CG  . PHE   A 1 260 ? -19.379 -26.072 13.463  1.00 32.81 ? 391 PHE   A CG  1 
ATOM   1982 C  CD1 . PHE   A 1 260 ? -20.283 -25.123 13.007  1.00 34.85 ? 391 PHE   A CD1 1 
ATOM   1983 C  CD2 . PHE   A 1 260 ? -18.327 -25.659 14.267  1.00 31.90 ? 391 PHE   A CD2 1 
ATOM   1984 C  CE1 . PHE   A 1 260 ? -20.135 -23.791 13.330  1.00 31.11 ? 391 PHE   A CE1 1 
ATOM   1985 C  CE2 . PHE   A 1 260 ? -18.171 -24.318 14.598  1.00 31.63 ? 391 PHE   A CE2 1 
ATOM   1986 C  CZ  . PHE   A 1 260 ? -19.079 -23.386 14.131  1.00 30.84 ? 391 PHE   A CZ  1 
ATOM   1987 N  N   . ASN   A 1 261 ? -21.626 -30.418 14.170  1.00 48.09 ? 392 ASN   A N   1 
ATOM   1988 C  CA  . ASN   A 1 261 ? -21.924 -31.786 13.777  1.00 53.16 ? 392 ASN   A CA  1 
ATOM   1989 C  C   . ASN   A 1 261 ? -23.389 -31.870 13.372  1.00 49.79 ? 392 ASN   A C   1 
ATOM   1990 O  O   . ASN   A 1 261 ? -24.284 -31.523 14.149  1.00 49.41 ? 392 ASN   A O   1 
ATOM   1991 C  CB  . ASN   A 1 261 ? -21.564 -32.777 14.882  1.00 53.18 ? 392 ASN   A CB  1 
ATOM   1992 C  CG  . ASN   A 1 261 ? -22.797 -33.314 15.574  1.00 59.85 ? 392 ASN   A CG  1 
ATOM   1993 O  OD1 . ASN   A 1 261 ? -23.341 -34.342 15.164  1.00 53.52 ? 392 ASN   A OD1 1 
ATOM   1994 N  ND2 . ASN   A 1 261 ? -23.252 -32.624 16.614  1.00 56.37 ? 392 ASN   A ND2 1 
ATOM   1995 N  N   . ASN   A 1 262 ? -23.619 -32.356 12.160  1.00 48.25 ? 393 ASN   A N   1 
ATOM   1996 C  CA  . ASN   A 1 262 ? -24.889 -32.208 11.472  1.00 49.53 ? 393 ASN   A CA  1 
ATOM   1997 C  C   . ASN   A 1 262 ? -25.983 -33.087 12.050  1.00 48.39 ? 393 ASN   A C   1 
ATOM   1998 O  O   . ASN   A 1 262 ? -27.159 -32.826 11.786  1.00 48.26 ? 393 ASN   A O   1 
ATOM   1999 C  CB  . ASN   A 1 262 ? -24.668 -32.518 9.991   1.00 46.78 ? 393 ASN   A CB  1 
ATOM   2000 C  CG  . ASN   A 1 262 ? -23.540 -31.694 9.390   1.00 43.00 ? 393 ASN   A CG  1 
ATOM   2001 O  OD1 . ASN   A 1 262 ? -23.737 -30.554 8.983   1.00 46.95 ? 393 ASN   A OD1 1 
ATOM   2002 N  ND2 . ASN   A 1 262 ? -22.335 -32.259 9.380   1.00 41.69 ? 393 ASN   A ND2 1 
ATOM   2003 N  N   . THR   A 1 263 ? -25.633 -34.102 12.846  1.00 52.03 ? 394 THR   A N   1 
ATOM   2004 C  CA  . THR   A 1 263 ? -26.653 -35.018 13.341  1.00 52.94 ? 394 THR   A CA  1 
ATOM   2005 C  C   . THR   A 1 263 ? -27.702 -34.297 14.181  1.00 51.65 ? 394 THR   A C   1 
ATOM   2006 O  O   . THR   A 1 263 ? -28.889 -34.632 14.114  1.00 53.96 ? 394 THR   A O   1 
ATOM   2007 C  CB  . THR   A 1 263 ? -26.003 -36.156 14.129  1.00 56.55 ? 394 THR   A CB  1 
ATOM   2008 O  OG1 . THR   A 1 263 ? -24.862 -36.652 13.412  1.00 59.52 ? 394 THR   A OG1 1 
ATOM   2009 C  CG2 . THR   A 1 263 ? -27.002 -37.283 14.350  1.00 56.45 ? 394 THR   A CG2 1 
ATOM   2010 N  N   . CYS   A 1 264 ? -27.300 -33.314 14.981  1.00 50.00 ? 395 CYS   A N   1 
ATOM   2011 C  CA  . CYS   A 1 264 ? -28.277 -32.641 15.837  1.00 47.77 ? 395 CYS   A CA  1 
ATOM   2012 C  C   . CYS   A 1 264 ? -29.100 -31.606 15.063  1.00 50.95 ? 395 CYS   A C   1 
ATOM   2013 O  O   . CYS   A 1 264 ? -28.700 -31.135 13.996  1.00 54.27 ? 395 CYS   A O   1 
ATOM   2014 C  CB  . CYS   A 1 264 ? -27.589 -31.974 17.027  1.00 49.08 ? 395 CYS   A CB  1 
ATOM   2015 S  SG  . CYS   A 1 264 ? -26.729 -33.118 18.141  1.00 51.64 ? 395 CYS   A SG  1 
ATOM   2016 N  N   . GLY   A 1 272 ? -30.948 -37.762 20.935  1.00 56.07 ? 409 GLY   A N   1 
ATOM   2017 C  CA  . GLY   A 1 272 ? -30.001 -37.919 22.026  1.00 55.22 ? 409 GLY   A CA  1 
ATOM   2018 C  C   . GLY   A 1 272 ? -28.831 -36.956 21.960  1.00 64.50 ? 409 GLY   A C   1 
ATOM   2019 O  O   . GLY   A 1 272 ? -27.675 -37.375 21.959  1.00 66.27 ? 409 GLY   A O   1 
ATOM   2020 N  N   . CYS   A 1 273 ? -29.144 -35.658 21.901  1.00 68.87 ? 410 CYS   A N   1 
ATOM   2021 C  CA  . CYS   A 1 273 ? -28.163 -34.574 21.824  1.00 64.41 ? 410 CYS   A CA  1 
ATOM   2022 C  C   . CYS   A 1 273 ? -28.266 -33.601 22.993  1.00 64.12 ? 410 CYS   A C   1 
ATOM   2023 O  O   . CYS   A 1 273 ? -27.533 -33.671 23.985  1.00 62.71 ? 410 CYS   A O   1 
ATOM   2024 C  CB  . CYS   A 1 273 ? -28.365 -33.715 20.563  1.00 63.05 ? 410 CYS   A CB  1 
ATOM   2025 S  SG  . CYS   A 1 273 ? -28.141 -34.370 18.907  1.00 63.12 ? 410 CYS   A SG  1 
ATOM   2026 N  N   . ASN   A 1 274 ? -29.219 -32.685 22.816  1.00 61.60 ? 411 ASN   A N   1 
ATOM   2027 C  CA  . ASN   A 1 274 ? -29.567 -31.449 23.512  1.00 53.81 ? 411 ASN   A CA  1 
ATOM   2028 C  C   . ASN   A 1 274 ? -29.218 -31.185 24.979  1.00 50.77 ? 411 ASN   A C   1 
ATOM   2029 O  O   . ASN   A 1 274 ? -29.891 -30.366 25.613  1.00 53.07 ? 411 ASN   A O   1 
ATOM   2030 C  CB  . ASN   A 1 274 ? -31.079 -31.289 23.309  1.00 54.05 ? 411 ASN   A CB  1 
ATOM   2031 C  CG  . ASN   A 1 274 ? -31.895 -32.131 24.293  1.00 59.90 ? 411 ASN   A CG  1 
ATOM   2032 O  OD1 . ASN   A 1 274 ? -31.785 -31.992 25.509  1.00 61.65 ? 411 ASN   A OD1 1 
ATOM   2033 N  ND2 . ASN   A 1 274 ? -32.713 -33.031 23.750  1.00 64.39 ? 411 ASN   A ND2 1 
ATOM   2034 N  N   . GLY   A 1 275 ? -28.169 -31.791 25.521  1.00 49.41 ? 412 GLY   A N   1 
ATOM   2035 C  CA  . GLY   A 1 275 ? -27.650 -31.401 26.821  1.00 49.86 ? 412 GLY   A CA  1 
ATOM   2036 C  C   . GLY   A 1 275 ? -26.581 -30.330 26.705  1.00 41.31 ? 412 GLY   A C   1 
ATOM   2037 O  O   . GLY   A 1 275 ? -26.427 -29.672 25.670  1.00 39.22 ? 412 GLY   A O   1 
ATOM   2038 N  N   . THR   A 1 276 ? -25.826 -30.154 27.785  1.00 40.15 ? 413 THR   A N   1 
ATOM   2039 C  CA  . THR   A 1 276 ? -24.669 -29.266 27.746  1.00 37.88 ? 413 THR   A CA  1 
ATOM   2040 C  C   . THR   A 1 276 ? -23.606 -29.811 26.797  1.00 39.47 ? 413 THR   A C   1 
ATOM   2041 O  O   . THR   A 1 276 ? -23.225 -30.983 26.877  1.00 36.10 ? 413 THR   A O   1 
ATOM   2042 C  CB  . THR   A 1 276 ? -24.065 -29.083 29.142  1.00 39.14 ? 413 THR   A CB  1 
ATOM   2043 O  OG1 . THR   A 1 276 ? -25.017 -28.459 30.014  1.00 36.56 ? 413 THR   A OG1 1 
ATOM   2044 C  CG2 . THR   A 1 276 ? -22.797 -28.220 29.065  1.00 37.67 ? 413 THR   A CG2 1 
ATOM   2045 N  N   . ILE   A 1 277 ? -23.121 -28.953 25.901  1.00 36.03 ? 414 ILE   A N   1 
ATOM   2046 C  CA  . ILE   A 1 277 ? -22.015 -29.295 25.016  1.00 34.04 ? 414 ILE   A CA  1 
ATOM   2047 C  C   . ILE   A 1 277 ? -20.723 -28.854 25.690  1.00 33.00 ? 414 ILE   A C   1 
ATOM   2048 O  O   . ILE   A 1 277 ? -20.591 -27.692 26.091  1.00 32.22 ? 414 ILE   A O   1 
ATOM   2049 C  CB  . ILE   A 1 277 ? -22.176 -28.618 23.644  1.00 36.44 ? 414 ILE   A CB  1 
ATOM   2050 C  CG1 . ILE   A 1 277 ? -23.264 -29.310 22.818  1.00 37.33 ? 414 ILE   A CG1 1 
ATOM   2051 C  CG2 . ILE   A 1 277 ? -20.857 -28.643 22.879  1.00 35.50 ? 414 ILE   A CG2 1 
ATOM   2052 C  CD1 . ILE   A 1 277 ? -23.785 -28.449 21.682  1.00 36.71 ? 414 ILE   A CD1 1 
ATOM   2053 N  N   . THR   A 1 278 ? -19.770 -29.772 25.826  1.00 30.88 ? 415 THR   A N   1 
ATOM   2054 C  CA  . THR   A 1 278 ? -18.481 -29.470 26.444  1.00 30.41 ? 415 THR   A CA  1 
ATOM   2055 C  C   . THR   A 1 278 ? -17.381 -29.614 25.402  1.00 33.92 ? 415 THR   A C   1 
ATOM   2056 O  O   . THR   A 1 278 ? -17.076 -30.726 24.956  1.00 32.27 ? 415 THR   A O   1 
ATOM   2057 C  CB  . THR   A 1 278 ? -18.205 -30.370 27.645  1.00 35.82 ? 415 THR   A CB  1 
ATOM   2058 O  OG1 . THR   A 1 278 ? -19.223 -30.174 28.633  1.00 36.76 ? 415 THR   A OG1 1 
ATOM   2059 C  CG2 . THR   A 1 278 ? -16.845 -30.025 28.249  1.00 36.48 ? 415 THR   A CG2 1 
ATOM   2060 N  N   . LEU   A 1 279 ? -16.776 -28.501 25.042  1.00 27.18 ? 416 LEU   A N   1 
ATOM   2061 C  CA  . LEU   A 1 279 ? -15.659 -28.481 24.111  1.00 26.15 ? 416 LEU   A CA  1 
ATOM   2062 C  C   . LEU   A 1 279 ? -14.354 -28.656 24.874  1.00 27.54 ? 416 LEU   A C   1 
ATOM   2063 O  O   . LEU   A 1 279 ? -14.152 -27.991 25.897  1.00 28.27 ? 416 LEU   A O   1 
ATOM   2064 C  CB  . LEU   A 1 279 ? -15.630 -27.165 23.341  1.00 27.78 ? 416 LEU   A CB  1 
ATOM   2065 C  CG  . LEU   A 1 279 ? -16.940 -26.767 22.652  1.00 29.32 ? 416 LEU   A CG  1 
ATOM   2066 C  CD1 . LEU   A 1 279 ? -16.757 -25.450 21.902  1.00 29.48 ? 416 LEU   A CD1 1 
ATOM   2067 C  CD2 . LEU   A 1 279 ? -17.426 -27.858 21.720  1.00 28.56 ? 416 LEU   A CD2 1 
ATOM   2068 N  N   . PRO   A 1 280 ? -13.459 -29.535 24.429  1.00 26.40 ? 417 PRO   A N   1 
ATOM   2069 C  CA  . PRO   A 1 280 ? -12.131 -29.605 25.047  1.00 26.79 ? 417 PRO   A CA  1 
ATOM   2070 C  C   . PRO   A 1 280 ? -11.267 -28.452 24.570  1.00 26.39 ? 417 PRO   A C   1 
ATOM   2071 O  O   . PRO   A 1 280 ? -11.232 -28.134 23.378  1.00 24.93 ? 417 PRO   A O   1 
ATOM   2072 C  CB  . PRO   A 1 280 ? -11.583 -30.950 24.555  1.00 27.51 ? 417 PRO   A CB  1 
ATOM   2073 C  CG  . PRO   A 1 280 ? -12.256 -31.147 23.234  1.00 31.42 ? 417 PRO   A CG  1 
ATOM   2074 C  CD  . PRO   A 1 280 ? -13.635 -30.552 23.376  1.00 25.61 ? 417 PRO   A CD  1 
ATOM   2075 N  N   . CYS   A 1 281 ? -10.563 -27.824 25.511  1.00 27.76 ? 418 CYS   A N   1 
ATOM   2076 C  CA  . CYS   A 1 281 ? -9.723  -26.673 25.217  1.00 27.43 ? 418 CYS   A CA  1 
ATOM   2077 C  C   . CYS   A 1 281 ? -8.330  -26.871 25.793  1.00 29.02 ? 418 CYS   A C   1 
ATOM   2078 O  O   . CYS   A 1 281 ? -8.115  -27.679 26.699  1.00 30.01 ? 418 CYS   A O   1 
ATOM   2079 C  CB  . CYS   A 1 281 ? -10.315 -25.378 25.780  1.00 29.18 ? 418 CYS   A CB  1 
ATOM   2080 S  SG  . CYS   A 1 281 ? -11.982 -25.017 25.259  1.00 30.15 ? 418 CYS   A SG  1 
ATOM   2081 N  N   . LYS   A 1 282 ? -7.386  -26.102 25.257  1.00 27.38 ? 419 LYS   A N   1 
ATOM   2082 C  CA  . LYS   A 1 282 ? -6.035  -26.025 25.788  1.00 31.66 ? 419 LYS   A CA  1 
ATOM   2083 C  C   . LYS   A 1 282 ? -5.595  -24.569 25.799  1.00 30.84 ? 419 LYS   A C   1 
ATOM   2084 O  O   . LYS   A 1 282 ? -5.862  -23.824 24.851  1.00 30.83 ? 419 LYS   A O   1 
ATOM   2085 C  CB  . LYS   A 1 282 ? -5.055  -26.856 24.948  1.00 33.88 ? 419 LYS   A CB  1 
ATOM   2086 C  CG  . LYS   A 1 282 ? -5.129  -28.362 25.190  1.00 39.74 ? 419 LYS   A CG  1 
ATOM   2087 C  CD  . LYS   A 1 282 ? -5.228  -28.696 26.669  1.00 45.03 ? 419 LYS   A CD  1 
ATOM   2088 C  CE  . LYS   A 1 282 ? -4.552  -30.026 26.974  1.00 45.52 ? 419 LYS   A CE  1 
ATOM   2089 N  NZ  . LYS   A 1 282 ? -5.304  -31.169 26.380  1.00 46.11 ? 419 LYS   A NZ  1 
ATOM   2090 N  N   . ILE   A 1 283 ? -4.926  -24.165 26.873  1.00 30.23 ? 420 ILE   A N   1 
ATOM   2091 C  CA  . ILE   A 1 283 ? -4.229  -22.888 26.911  1.00 30.30 ? 420 ILE   A CA  1 
ATOM   2092 C  C   . ILE   A 1 283 ? -2.849  -23.115 26.311  1.00 33.23 ? 420 ILE   A C   1 
ATOM   2093 O  O   . ILE   A 1 283 ? -2.107  -23.999 26.756  1.00 34.53 ? 420 ILE   A O   1 
ATOM   2094 C  CB  . ILE   A 1 283 ? -4.122  -22.344 28.344  1.00 34.72 ? 420 ILE   A CB  1 
ATOM   2095 C  CG1 . ILE   A 1 283 ? -5.487  -21.883 28.851  1.00 32.22 ? 420 ILE   A CG1 1 
ATOM   2096 C  CG2 . ILE   A 1 283 ? -3.140  -21.175 28.384  1.00 33.43 ? 420 ILE   A CG2 1 
ATOM   2097 C  CD1 . ILE   A 1 283 ? -5.451  -21.386 30.280  1.00 35.79 ? 420 ILE   A CD1 1 
ATOM   2098 N  N   . LYS   A 1 284 ? -2.503  -22.336 25.293  1.00 31.49 ? 421 LYS   A N   1 
ATOM   2099 C  CA  . LYS   A 1 284 ? -1.216  -22.465 24.629  1.00 33.00 ? 421 LYS   A CA  1 
ATOM   2100 C  C   . LYS   A 1 284 ? -0.330  -21.282 24.996  1.00 35.14 ? 421 LYS   A C   1 
ATOM   2101 O  O   . LYS   A 1 284 ? -0.799  -20.143 25.081  1.00 34.21 ? 421 LYS   A O   1 
ATOM   2102 C  CB  . LYS   A 1 284 ? -1.385  -22.556 23.110  1.00 29.53 ? 421 LYS   A CB  1 
ATOM   2103 C  CG  . LYS   A 1 284 ? -1.726  -23.970 22.626  1.00 30.25 ? 421 LYS   A CG  1 
ATOM   2104 C  CD  . LYS   A 1 284 ? -1.879  -24.048 21.115  1.00 31.45 ? 421 LYS   A CD  1 
ATOM   2105 C  CE  . LYS   A 1 284 ? -0.563  -23.800 20.396  1.00 37.28 ? 421 LYS   A CE  1 
ATOM   2106 N  NZ  . LYS   A 1 284 ? 0.564   -24.540 21.020  1.00 39.18 ? 421 LYS   A NZ  1 
ATOM   2107 N  N   . GLN   A 1 285 ? 0.947   -21.563 25.243  1.00 34.45 ? 422 GLN   A N   1 
ATOM   2108 C  CA  . GLN   A 1 285 ? 1.910   -20.501 25.489  1.00 37.55 ? 422 GLN   A CA  1 
ATOM   2109 C  C   . GLN   A 1 285 ? 2.572   -20.016 24.208  1.00 37.13 ? 422 GLN   A C   1 
ATOM   2110 O  O   . GLN   A 1 285 ? 2.969   -18.847 24.126  1.00 37.61 ? 422 GLN   A O   1 
ATOM   2111 C  CB  . GLN   A 1 285 ? 2.986   -20.972 26.474  1.00 38.94 ? 422 GLN   A CB  1 
ATOM   2112 C  CG  . GLN   A 1 285 ? 2.449   -21.461 27.809  1.00 41.20 ? 422 GLN   A CG  1 
ATOM   2113 C  CD  . GLN   A 1 285 ? 3.551   -21.852 28.780  1.00 45.95 ? 422 GLN   A CD  1 
ATOM   2114 O  OE1 . GLN   A 1 285 ? 4.516   -21.109 28.975  1.00 49.36 ? 422 GLN   A OE1 1 
ATOM   2115 N  NE2 . GLN   A 1 285 ? 3.425   -23.035 29.377  1.00 47.14 ? 422 GLN   A NE2 1 
ATOM   2116 N  N   . ILE   A 1 286 ? 2.685   -20.882 23.206  1.00 35.46 ? 423 ILE   A N   1 
ATOM   2117 C  CA  . ILE   A 1 286 ? 3.329   -20.554 21.942  1.00 36.66 ? 423 ILE   A CA  1 
ATOM   2118 C  C   . ILE   A 1 286 ? 2.247   -20.327 20.899  1.00 38.63 ? 423 ILE   A C   1 
ATOM   2119 O  O   . ILE   A 1 286 ? 1.499   -21.250 20.553  1.00 38.30 ? 423 ILE   A O   1 
ATOM   2120 C  CB  . ILE   A 1 286 ? 4.315   -21.649 21.509  1.00 36.58 ? 423 ILE   A CB  1 
ATOM   2121 C  CG1 . ILE   A 1 286 ? 5.530   -21.643 22.440  1.00 35.65 ? 423 ILE   A CG1 1 
ATOM   2122 C  CG2 . ILE   A 1 286 ? 4.726   -21.459 20.056  1.00 37.05 ? 423 ILE   A CG2 1 
ATOM   2123 C  CD1 . ILE   A 1 286 ? 6.298   -22.950 22.457  1.00 36.10 ? 423 ILE   A CD1 1 
ATOM   2124 N  N   . ILE   A 1 287 ? 2.188   -19.102 20.382  1.00 34.54 ? 424 ILE   A N   1 
ATOM   2125 C  CA  . ILE   A 1 287 ? 1.069   -18.614 19.589  1.00 40.05 ? 424 ILE   A CA  1 
ATOM   2126 C  C   . ILE   A 1 287 ? 1.561   -18.231 18.203  1.00 36.40 ? 424 ILE   A C   1 
ATOM   2127 O  O   . ILE   A 1 287 ? 2.664   -17.694 18.050  1.00 40.76 ? 424 ILE   A O   1 
ATOM   2128 C  CB  . ILE   A 1 287 ? 0.403   -17.406 20.280  1.00 36.06 ? 424 ILE   A CB  1 
ATOM   2129 C  CG1 . ILE   A 1 287 ? -0.071  -17.789 21.687  1.00 37.90 ? 424 ILE   A CG1 1 
ATOM   2130 C  CG2 . ILE   A 1 287 ? -0.714  -16.836 19.420  1.00 41.70 ? 424 ILE   A CG2 1 
ATOM   2131 C  CD1 . ILE   A 1 287 ? -1.101  -18.883 21.706  1.00 34.72 ? 424 ILE   A CD1 1 
ATOM   2132 N  N   . ASN   A 1 288 ? 0.737   -18.500 17.195  1.00 36.92 ? 425 ASN   A N   1 
ATOM   2133 C  CA  . ASN   A 1 288 ? 0.939   -17.942 15.862  1.00 34.56 ? 425 ASN   A CA  1 
ATOM   2134 C  C   . ASN   A 1 288 ? 0.192   -16.615 15.801  1.00 37.66 ? 425 ASN   A C   1 
ATOM   2135 O  O   . ASN   A 1 288 ? -1.041  -16.588 15.729  1.00 34.50 ? 425 ASN   A O   1 
ATOM   2136 C  CB  . ASN   A 1 288 ? 0.463   -18.905 14.782  1.00 35.68 ? 425 ASN   A CB  1 
ATOM   2137 C  CG  . ASN   A 1 288 ? 1.327   -20.157 14.698  1.00 40.51 ? 425 ASN   A CG  1 
ATOM   2138 O  OD1 . ASN   A 1 288 ? 2.555   -20.084 14.785  1.00 44.89 ? 425 ASN   A OD1 1 
ATOM   2139 N  ND2 . ASN   A 1 288 ? 0.691   -21.306 14.521  1.00 33.76 ? 425 ASN   A ND2 1 
ATOM   2140 N  N   . MET   A 1 289 ? 0.946   -15.517 15.848  1.00 37.58 ? 426 MET   A N   1 
ATOM   2141 C  CA  . MET   A 1 289 ? 0.368   -14.190 16.017  1.00 35.59 ? 426 MET   A CA  1 
ATOM   2142 C  C   . MET   A 1 289 ? -0.586  -13.847 14.879  1.00 32.92 ? 426 MET   A C   1 
ATOM   2143 O  O   . MET   A 1 289 ? -0.358  -14.212 13.723  1.00 34.24 ? 426 MET   A O   1 
ATOM   2144 C  CB  . MET   A 1 289 ? 1.492   -13.156 16.089  1.00 37.68 ? 426 MET   A CB  1 
ATOM   2145 C  CG  . MET   A 1 289 ? 2.182   -13.084 17.438  1.00 37.81 ? 426 MET   A CG  1 
ATOM   2146 S  SD  . MET   A 1 289 ? 3.548   -11.900 17.418  1.00 46.13 ? 426 MET   A SD  1 
ATOM   2147 C  CE  . MET   A 1 289 ? 3.975   -11.932 15.680  1.00 47.54 ? 426 MET   A CE  1 
ATOM   2148 N  N   . TRP   A 1 290 ? -1.654  -13.116 15.209  1.00 32.96 ? 427 TRP   A N   1 
ATOM   2149 C  CA  . TRP   A 1 290 ? -2.577  -12.622 14.197  1.00 31.80 ? 427 TRP   A CA  1 
ATOM   2150 C  C   . TRP   A 1 290 ? -2.143  -11.272 13.643  1.00 35.06 ? 427 TRP   A C   1 
ATOM   2151 O  O   . TRP   A 1 290 ? -2.565  -10.906 12.545  1.00 34.45 ? 427 TRP   A O   1 
ATOM   2152 C  CB  . TRP   A 1 290 ? -3.992  -12.490 14.782  1.00 29.24 ? 427 TRP   A CB  1 
ATOM   2153 C  CG  . TRP   A 1 290 ? -4.048  -11.546 15.934  1.00 26.37 ? 427 TRP   A CG  1 
ATOM   2154 C  CD1 . TRP   A 1 290 ? -3.850  -11.827 17.252  1.00 28.80 ? 427 TRP   A CD1 1 
ATOM   2155 C  CD2 . TRP   A 1 290 ? -4.309  -10.143 15.856  1.00 28.88 ? 427 TRP   A CD2 1 
ATOM   2156 N  NE1 . TRP   A 1 290 ? -3.970  -10.681 18.004  1.00 29.64 ? 427 TRP   A NE1 1 
ATOM   2157 C  CE2 . TRP   A 1 290 ? -4.259  -9.633  17.169  1.00 29.65 ? 427 TRP   A CE2 1 
ATOM   2158 C  CE3 . TRP   A 1 290 ? -4.594  -9.269  14.803  1.00 30.75 ? 427 TRP   A CE3 1 
ATOM   2159 C  CZ2 . TRP   A 1 290 ? -4.481  -8.285  17.456  1.00 29.53 ? 427 TRP   A CZ2 1 
ATOM   2160 C  CZ3 . TRP   A 1 290 ? -4.806  -7.927  15.089  1.00 28.25 ? 427 TRP   A CZ3 1 
ATOM   2161 C  CH2 . TRP   A 1 290 ? -4.746  -7.450  16.401  1.00 28.30 ? 427 TRP   A CH2 1 
ATOM   2162 N  N   . GLN   A 1 291 ? -1.312  -10.531 14.384  1.00 34.83 ? 428 GLN   A N   1 
ATOM   2163 C  CA  . GLN   A 1 291 ? -0.915  -9.181  13.993  1.00 36.14 ? 428 GLN   A CA  1 
ATOM   2164 C  C   . GLN   A 1 291 ? -0.108  -9.188  12.709  1.00 39.34 ? 428 GLN   A C   1 
ATOM   2165 O  O   . GLN   A 1 291 ? -0.089  -8.198  11.971  1.00 40.75 ? 428 GLN   A O   1 
ATOM   2166 C  CB  . GLN   A 1 291 ? -0.067  -8.562  15.097  1.00 35.20 ? 428 GLN   A CB  1 
ATOM   2167 C  CG  . GLN   A 1 291 ? -0.802  -8.291  16.383  1.00 34.61 ? 428 GLN   A CG  1 
ATOM   2168 C  CD  . GLN   A 1 291 ? -0.565  -9.402  17.382  1.00 35.33 ? 428 GLN   A CD  1 
ATOM   2169 O  OE1 . GLN   A 1 291 ? -0.804  -10.575 17.086  1.00 35.23 ? 428 GLN   A OE1 1 
ATOM   2170 N  NE2 . GLN   A 1 291 ? -0.061  -9.049  18.557  1.00 35.49 ? 428 GLN   A NE2 1 
ATOM   2171 N  N   . GLY   A 1 292 ? 0.574   -10.287 12.448  1.00 43.07 ? 429 GLY   A N   1 
ATOM   2172 C  CA  . GLY   A 1 292 ? 1.476   -10.417 11.332  1.00 45.21 ? 429 GLY   A CA  1 
ATOM   2173 C  C   . GLY   A 1 292 ? 2.152   -11.759 11.458  1.00 45.35 ? 429 GLY   A C   1 
ATOM   2174 O  O   . GLY   A 1 292 ? 2.122   -12.360 12.530  1.00 45.36 ? 429 GLY   A O   1 
ATOM   2175 N  N   . THR   A 1 293 ? 2.749   -12.249 10.382  1.00 50.55 ? 430 THR   A N   1 
ATOM   2176 C  CA  . THR   A 1 293 ? 3.382   -13.553 10.443  1.00 50.73 ? 430 THR   A CA  1 
ATOM   2177 C  C   . THR   A 1 293 ? 4.480   -13.534 11.499  1.00 50.57 ? 430 THR   A C   1 
ATOM   2178 O  O   . THR   A 1 293 ? 5.366   -12.671 11.485  1.00 56.47 ? 430 THR   A O   1 
ATOM   2179 C  CB  . THR   A 1 293 ? 3.938   -13.923 9.073   1.00 53.57 ? 430 THR   A CB  1 
ATOM   2180 O  OG1 . THR   A 1 293 ? 2.883   -14.455 8.257   1.00 53.73 ? 430 THR   A OG1 1 
ATOM   2181 C  CG2 . THR   A 1 293 ? 5.022   -14.980 9.225   1.00 49.20 ? 430 THR   A CG2 1 
ATOM   2182 N  N   . GLY   A 1 294 ? 4.401   -14.482 12.424  1.00 48.77 ? 431 GLY   A N   1 
ATOM   2183 C  CA  . GLY   A 1 294 ? 5.327   -14.564 13.535  1.00 49.15 ? 431 GLY   A CA  1 
ATOM   2184 C  C   . GLY   A 1 294 ? 4.828   -15.471 14.642  1.00 47.89 ? 431 GLY   A C   1 
ATOM   2185 O  O   . GLY   A 1 294 ? 3.633   -15.775 14.705  1.00 48.97 ? 431 GLY   A O   1 
ATOM   2186 N  N   . GLN   A 1 295 ? 5.730   -15.918 15.515  1.00 49.24 ? 432 GLN   A N   1 
ATOM   2187 C  CA  . GLN   A 1 295 ? 5.382   -16.776 16.639  1.00 48.51 ? 432 GLN   A CA  1 
ATOM   2188 C  C   . GLN   A 1 295 ? 5.751   -16.075 17.936  1.00 46.78 ? 432 GLN   A C   1 
ATOM   2189 O  O   . GLN   A 1 295 ? 6.756   -15.360 17.998  1.00 50.08 ? 432 GLN   A O   1 
ATOM   2190 C  CB  . GLN   A 1 295 ? 6.088   -18.142 16.551  1.00 51.45 ? 432 GLN   A CB  1 
ATOM   2191 C  CG  . GLN   A 1 295 ? 6.518   -18.726 17.895  1.00 49.83 ? 432 GLN   A CG  1 
ATOM   2192 C  CD  . GLN   A 1 295 ? 7.455   -19.920 17.751  1.00 55.58 ? 432 GLN   A CD  1 
ATOM   2193 O  OE1 . GLN   A 1 295 ? 7.034   -21.073 17.842  1.00 56.44 ? 432 GLN   A OE1 1 
ATOM   2194 N  NE2 . GLN   A 1 295 ? 8.738   -19.642 17.537  1.00 50.58 ? 432 GLN   A NE2 1 
ATOM   2195 N  N   . ALA   A 1 296 ? 4.939   -16.278 18.973  1.00 45.64 ? 433 ALA   A N   1 
ATOM   2196 C  CA  . ALA   A 1 296 ? 5.161   -15.623 20.255  1.00 43.97 ? 433 ALA   A CA  1 
ATOM   2197 C  C   . ALA   A 1 296 ? 4.958   -16.615 21.388  1.00 41.91 ? 433 ALA   A C   1 
ATOM   2198 O  O   . ALA   A 1 296 ? 4.079   -17.477 21.314  1.00 39.98 ? 433 ALA   A O   1 
ATOM   2199 C  CB  . ALA   A 1 296 ? 4.227   -14.415 20.439  1.00 41.96 ? 433 ALA   A CB  1 
ATOM   2200 N  N   . MET   A 1 297 ? 5.760   -16.471 22.443  1.00 39.53 ? 434 MET   A N   1 
ATOM   2201 C  CA  . MET   A 1 297 ? 5.694   -17.341 23.605  1.00 40.33 ? 434 MET   A CA  1 
ATOM   2202 C  C   . MET   A 1 297 ? 5.400   -16.515 24.846  1.00 45.32 ? 434 MET   A C   1 
ATOM   2203 O  O   . MET   A 1 297 ? 6.067   -15.506 25.101  1.00 44.02 ? 434 MET   A O   1 
ATOM   2204 C  CB  . MET   A 1 297 ? 6.995   -18.125 23.800  1.00 36.80 ? 434 MET   A CB  1 
ATOM   2205 C  CG  . MET   A 1 297 ? 6.808   -19.357 24.658  1.00 42.25 ? 434 MET   A CG  1 
ATOM   2206 S  SD  . MET   A 1 297 ? 8.339   -20.243 24.984  1.00 43.14 ? 434 MET   A SD  1 
ATOM   2207 C  CE  . MET   A 1 297 ? 9.253   -19.001 25.896  1.00 37.92 ? 434 MET   A CE  1 
ATOM   2208 N  N   . TYR   A 1 298 ? 4.424   -16.968 25.625  1.00 42.18 ? 435 TYR   A N   1 
ATOM   2209 C  CA  . TYR   A 1 298 ? 4.000   -16.299 26.841  1.00 40.95 ? 435 TYR   A CA  1 
ATOM   2210 C  C   . TYR   A 1 298 ? 4.263   -17.214 28.029  1.00 41.59 ? 435 TYR   A C   1 
ATOM   2211 O  O   . TYR   A 1 298 ? 4.537   -18.407 27.878  1.00 44.97 ? 435 TYR   A O   1 
ATOM   2212 C  CB  . TYR   A 1 298 ? 2.514   -15.919 26.768  1.00 42.39 ? 435 TYR   A CB  1 
ATOM   2213 C  CG  . TYR   A 1 298 ? 2.229   -14.928 25.667  1.00 37.23 ? 435 TYR   A CG  1 
ATOM   2214 C  CD1 . TYR   A 1 298 ? 2.203   -15.339 24.341  1.00 40.22 ? 435 TYR   A CD1 1 
ATOM   2215 C  CD2 . TYR   A 1 298 ? 2.034   -13.583 25.942  1.00 46.63 ? 435 TYR   A CD2 1 
ATOM   2216 C  CE1 . TYR   A 1 298 ? 1.964   -14.446 23.317  1.00 41.45 ? 435 TYR   A CE1 1 
ATOM   2217 C  CE2 . TYR   A 1 298 ? 1.793   -12.675 24.926  1.00 45.47 ? 435 TYR   A CE2 1 
ATOM   2218 C  CZ  . TYR   A 1 298 ? 1.760   -13.113 23.614  1.00 45.41 ? 435 TYR   A CZ  1 
ATOM   2219 O  OH  . TYR   A 1 298 ? 1.520   -12.221 22.595  1.00 48.20 ? 435 TYR   A OH  1 
ATOM   2220 N  N   . ALA   A 1 299 ? 4.179   -16.640 29.223  1.00 43.72 ? 436 ALA   A N   1 
ATOM   2221 C  CA  . ALA   A 1 299 ? 4.381   -17.417 30.431  1.00 44.07 ? 436 ALA   A CA  1 
ATOM   2222 C  C   . ALA   A 1 299 ? 3.179   -18.321 30.695  1.00 46.51 ? 436 ALA   A C   1 
ATOM   2223 O  O   . ALA   A 1 299 ? 2.086   -18.096 30.170  1.00 45.86 ? 436 ALA   A O   1 
ATOM   2224 C  CB  . ALA   A 1 299 ? 4.621   -16.499 31.626  1.00 46.77 ? 436 ALA   A CB  1 
ATOM   2225 N  N   . PRO   A 1 300 ? 3.368   -19.365 31.495  1.00 48.69 ? 437 PRO   A N   1 
ATOM   2226 C  CA  . PRO   A 1 300 ? 2.269   -20.289 31.793  1.00 46.86 ? 437 PRO   A CA  1 
ATOM   2227 C  C   . PRO   A 1 300 ? 1.095   -19.578 32.440  1.00 48.46 ? 437 PRO   A C   1 
ATOM   2228 O  O   . PRO   A 1 300 ? 1.240   -18.470 32.980  1.00 44.97 ? 437 PRO   A O   1 
ATOM   2229 C  CB  . PRO   A 1 300 ? 2.913   -21.299 32.760  1.00 47.02 ? 437 PRO   A CB  1 
ATOM   2230 C  CG  . PRO   A 1 300 ? 4.230   -20.659 33.177  1.00 48.94 ? 437 PRO   A CG  1 
ATOM   2231 C  CD  . PRO   A 1 300 ? 4.652   -19.909 31.961  1.00 46.30 ? 437 PRO   A CD  1 
ATOM   2232 N  N   . PRO   A 1 301 ? -0.086  -20.191 32.407  1.00 46.32 ? 438 PRO   A N   1 
ATOM   2233 C  CA  . PRO   A 1 301 ? -1.285  -19.537 32.943  1.00 45.92 ? 438 PRO   A CA  1 
ATOM   2234 C  C   . PRO   A 1 301 ? -1.163  -19.176 34.416  1.00 50.70 ? 438 PRO   A C   1 
ATOM   2235 O  O   . PRO   A 1 301 ? -0.448  -19.819 35.189  1.00 51.95 ? 438 PRO   A O   1 
ATOM   2236 C  CB  . PRO   A 1 301 ? -2.388  -20.579 32.715  1.00 42.22 ? 438 PRO   A CB  1 
ATOM   2237 C  CG  . PRO   A 1 301 ? -1.671  -21.869 32.388  1.00 42.85 ? 438 PRO   A CG  1 
ATOM   2238 C  CD  . PRO   A 1 301 ? -0.398  -21.465 31.741  1.00 45.90 ? 438 PRO   A CD  1 
ATOM   2239 N  N   . ILE   A 1 302 ? -1.882  -18.113 34.787  1.00 47.22 ? 439 ILE   A N   1 
ATOM   2240 C  CA  . ILE   A 1 302 ? -2.018  -17.728 36.181  1.00 51.56 ? 439 ILE   A CA  1 
ATOM   2241 C  C   . ILE   A 1 302 ? -2.712  -18.842 36.962  1.00 51.45 ? 439 ILE   A C   1 
ATOM   2242 O  O   . ILE   A 1 302 ? -3.381  -19.718 36.400  1.00 52.06 ? 439 ILE   A O   1 
ATOM   2243 C  CB  . ILE   A 1 302 ? -2.803  -16.411 36.278  1.00 49.36 ? 439 ILE   A CB  1 
ATOM   2244 C  CG1 . ILE   A 1 302 ? -4.217  -16.609 35.730  1.00 47.77 ? 439 ILE   A CG1 1 
ATOM   2245 C  CG2 . ILE   A 1 302 ? -2.107  -15.327 35.476  1.00 47.52 ? 439 ILE   A CG2 1 
ATOM   2246 C  CD1 . ILE   A 1 302 ? -5.278  -15.783 36.430  1.00 51.34 ? 439 ILE   A CD1 1 
ATOM   2247 N  N   . ASP   A 1 303 ? -2.553  -18.804 38.280  1.00 53.47 ? 440 ASP   A N   1 
ATOM   2248 C  CA  . ASP   A 1 303 ? -3.135  -19.852 39.098  1.00 54.80 ? 440 ASP   A CA  1 
ATOM   2249 C  C   . ASP   A 1 303 ? -4.613  -19.568 39.363  1.00 52.87 ? 440 ASP   A C   1 
ATOM   2250 O  O   . ASP   A 1 303 ? -5.112  -18.457 39.158  1.00 53.36 ? 440 ASP   A O   1 
ATOM   2251 C  CB  . ASP   A 1 303 ? -2.349  -20.003 40.403  1.00 59.34 ? 440 ASP   A CB  1 
ATOM   2252 C  CG  . ASP   A 1 303 ? -0.857  -20.174 40.161  1.00 60.99 ? 440 ASP   A CG  1 
ATOM   2253 O  OD1 . ASP   A 1 303 ? -0.459  -20.250 38.980  1.00 61.19 ? 440 ASP   A OD1 1 
ATOM   2254 O  OD2 . ASP   A 1 303 ? -0.088  -20.244 41.144  1.00 64.33 ? 440 ASP   A OD2 1 
ATOM   2255 N  N   . GLY   A 1 304 ? -5.319  -20.604 39.803  1.00 49.78 ? 441 GLY   A N   1 
ATOM   2256 C  CA  . GLY   A 1 304 ? -6.728  -20.482 40.111  1.00 52.68 ? 441 GLY   A CA  1 
ATOM   2257 C  C   . GLY   A 1 304 ? -7.635  -20.587 38.898  1.00 51.29 ? 441 GLY   A C   1 
ATOM   2258 O  O   . GLY   A 1 304 ? -7.213  -20.795 37.760  1.00 46.87 ? 441 GLY   A O   1 
ATOM   2259 N  N   . LYS   A 1 305 ? -8.931  -20.433 39.175  1.00 51.30 ? 442 LYS   A N   1 
ATOM   2260 C  CA  . LYS   A 1 305 ? -9.997  -20.485 38.181  1.00 46.44 ? 442 LYS   A CA  1 
ATOM   2261 C  C   . LYS   A 1 305 ? -9.888  -19.367 37.148  1.00 45.99 ? 442 LYS   A C   1 
ATOM   2262 O  O   . LYS   A 1 305 ? -10.077 -18.191 37.478  1.00 48.94 ? 442 LYS   A O   1 
ATOM   2263 C  CB  . LYS   A 1 305 ? -11.352 -20.411 38.891  1.00 47.73 ? 442 LYS   A CB  1 
ATOM   2264 C  CG  . LYS   A 1 305 ? -12.555 -20.807 38.060  1.00 44.51 ? 442 LYS   A CG  1 
ATOM   2265 C  CD  . LYS   A 1 305 ? -13.831 -20.639 38.872  1.00 47.10 ? 442 LYS   A CD  1 
ATOM   2266 C  CE  . LYS   A 1 305 ? -15.021 -21.314 38.210  1.00 53.62 ? 442 LYS   A CE  1 
ATOM   2267 N  NZ  . LYS   A 1 305 ? -16.277 -20.536 38.407  1.00 55.17 ? 442 LYS   A NZ  1 
ATOM   2268 N  N   . ILE   A 1 306 ? -9.595  -19.719 35.898  1.00 42.60 ? 443 ILE   A N   1 
ATOM   2269 C  CA  . ILE   A 1 306 ? -9.596  -18.780 34.780  1.00 42.18 ? 443 ILE   A CA  1 
ATOM   2270 C  C   . ILE   A 1 306 ? -10.901 -18.994 34.023  1.00 42.06 ? 443 ILE   A C   1 
ATOM   2271 O  O   . ILE   A 1 306 ? -11.104 -20.055 33.420  1.00 37.80 ? 443 ILE   A O   1 
ATOM   2272 C  CB  . ILE   A 1 306 ? -8.395  -18.997 33.851  1.00 43.75 ? 443 ILE   A CB  1 
ATOM   2273 C  CG1 . ILE   A 1 306 ? -7.082  -19.059 34.633  1.00 43.79 ? 443 ILE   A CG1 1 
ATOM   2274 C  CG2 . ILE   A 1 306 ? -8.325  -17.878 32.818  1.00 37.66 ? 443 ILE   A CG2 1 
ATOM   2275 C  CD1 . ILE   A 1 306 ? -5.864  -19.182 33.732  1.00 40.43 ? 443 ILE   A CD1 1 
ATOM   2276 N  N   . ASN   A 1 307 ? -11.787 -17.995 34.019  1.00 41.43 ? 444 ASN   A N   1 
ATOM   2277 C  CA  . ASN   A 1 307 ? -13.108 -18.194 33.439  1.00 39.47 ? 444 ASN   A CA  1 
ATOM   2278 C  C   . ASN   A 1 307 ? -13.513 -16.983 32.606  1.00 38.40 ? 444 ASN   A C   1 
ATOM   2279 O  O   . ASN   A 1 307 ? -13.163 -15.843 32.925  1.00 40.83 ? 444 ASN   A O   1 
ATOM   2280 C  CB  . ASN   A 1 307 ? -14.148 -18.485 34.537  1.00 38.99 ? 444 ASN   A CB  1 
ATOM   2281 C  CG  . ASN   A 1 307 ? -15.575 -18.421 34.032  1.00 40.02 ? 444 ASN   A CG  1 
ATOM   2282 O  OD1 . ASN   A 1 307 ? -16.206 -17.368 34.052  1.00 37.51 ? 444 ASN   A OD1 1 
ATOM   2283 N  ND2 . ASN   A 1 307 ? -16.094 -19.561 33.578  1.00 38.07 ? 444 ASN   A ND2 1 
ATOM   2284 N  N   . CYS   A 1 308 ? -14.247 -17.251 31.522  1.00 31.78 ? 445 CYS   A N   1 
ATOM   2285 C  CA  . CYS   A 1 308 ? -14.780 -16.220 30.637  1.00 34.33 ? 445 CYS   A CA  1 
ATOM   2286 C  C   . CYS   A 1 308 ? -16.131 -16.679 30.119  1.00 32.49 ? 445 CYS   A C   1 
ATOM   2287 O  O   . CYS   A 1 308 ? -16.241 -17.779 29.568  1.00 30.26 ? 445 CYS   A O   1 
ATOM   2288 C  CB  . CYS   A 1 308 ? -13.856 -15.947 29.448  1.00 31.85 ? 445 CYS   A CB  1 
ATOM   2289 S  SG  . CYS   A 1 308 ? -12.391 -14.976 29.814  1.00 38.84 ? 445 CYS   A SG  1 
ATOM   2290 N  N   . VAL   A 1 309 ? -17.148 -15.839 30.286  1.00 29.21 ? 446 VAL   A N   1 
ATOM   2291 C  CA  . VAL   A 1 309 ? -18.478 -16.099 29.750  1.00 31.35 ? 446 VAL   A CA  1 
ATOM   2292 C  C   . VAL   A 1 309 ? -18.720 -15.093 28.638  1.00 28.28 ? 446 VAL   A C   1 
ATOM   2293 O  O   . VAL   A 1 309 ? -18.775 -13.883 28.889  1.00 27.75 ? 446 VAL   A O   1 
ATOM   2294 C  CB  . VAL   A 1 309 ? -19.562 -15.996 30.831  1.00 33.15 ? 446 VAL   A CB  1 
ATOM   2295 C  CG1 . VAL   A 1 309 ? -20.928 -16.340 30.248  1.00 30.27 ? 446 VAL   A CG1 1 
ATOM   2296 C  CG2 . VAL   A 1 309 ? -19.226 -16.882 32.021  1.00 38.36 ? 446 VAL   A CG2 1 
ATOM   2297 N  N   . SER   A 1 310 ? -18.845 -15.582 27.409  1.00 24.31 ? 447 SER   A N   1 
ATOM   2298 C  CA  . SER   A 1 310 ? -18.997 -14.717 26.253  1.00 25.60 ? 447 SER   A CA  1 
ATOM   2299 C  C   . SER   A 1 310 ? -20.284 -15.039 25.505  1.00 25.65 ? 447 SER   A C   1 
ATOM   2300 O  O   . SER   A 1 310 ? -20.841 -16.132 25.626  1.00 25.19 ? 447 SER   A O   1 
ATOM   2301 C  CB  . SER   A 1 310 ? -17.793 -14.836 25.306  1.00 24.46 ? 447 SER   A CB  1 
ATOM   2302 O  OG  . SER   A 1 310 ? -16.560 -14.818 26.014  1.00 26.38 ? 447 SER   A OG  1 
ATOM   2303 N  N   . ASN   A 1 311 ? -20.757 -14.059 24.737  1.00 24.67 ? 448 ASN   A N   1 
ATOM   2304 C  CA  . ASN   A 1 311 ? -21.873 -14.248 23.822  1.00 24.35 ? 448 ASN   A CA  1 
ATOM   2305 C  C   . ASN   A 1 311 ? -21.338 -14.573 22.436  1.00 24.66 ? 448 ASN   A C   1 
ATOM   2306 O  O   . ASN   A 1 311 ? -20.544 -13.804 21.884  1.00 26.28 ? 448 ASN   A O   1 
ATOM   2307 C  CB  . ASN   A 1 311 ? -22.723 -12.985 23.719  1.00 25.56 ? 448 ASN   A CB  1 
ATOM   2308 C  CG  . ASN   A 1 311 ? -23.677 -12.811 24.869  1.00 37.83 ? 448 ASN   A CG  1 
ATOM   2309 O  OD1 . ASN   A 1 311 ? -24.025 -13.755 25.581  1.00 34.82 ? 448 ASN   A OD1 1 
ATOM   2310 N  ND2 . ASN   A 1 311 ? -24.120 -11.577 25.044  1.00 39.83 ? 448 ASN   A ND2 1 
ATOM   2311 N  N   . ILE   A 1 312 ? -21.786 -15.686 21.865  1.00 23.31 ? 449 ILE   A N   1 
ATOM   2312 C  CA  . ILE   A 1 312 ? -21.580 -15.922 20.442  1.00 21.87 ? 449 ILE   A CA  1 
ATOM   2313 C  C   . ILE   A 1 312 ? -22.595 -15.074 19.687  1.00 24.45 ? 449 ILE   A C   1 
ATOM   2314 O  O   . ILE   A 1 312 ? -23.809 -15.265 19.827  1.00 24.08 ? 449 ILE   A O   1 
ATOM   2315 C  CB  . ILE   A 1 312 ? -21.733 -17.403 20.084  1.00 25.71 ? 449 ILE   A CB  1 
ATOM   2316 C  CG1 . ILE   A 1 312 ? -20.707 -18.255 20.827  1.00 25.95 ? 449 ILE   A CG1 1 
ATOM   2317 C  CG2 . ILE   A 1 312 ? -21.548 -17.585 18.575  1.00 22.80 ? 449 ILE   A CG2 1 
ATOM   2318 C  CD1 . ILE   A 1 312 ? -21.016 -19.745 20.756  1.00 26.50 ? 449 ILE   A CD1 1 
ATOM   2319 N  N   . THR   A 1 313 ? -22.104 -14.124 18.896  1.00 20.81 ? 450 THR   A N   1 
ATOM   2320 C  CA  . THR   A 1 313 ? -22.977 -13.275 18.108  1.00 21.43 ? 450 THR   A CA  1 
ATOM   2321 C  C   . THR   A 1 313 ? -22.769 -13.413 16.609  1.00 22.86 ? 450 THR   A C   1 
ATOM   2322 O  O   . THR   A 1 313 ? -23.551 -12.837 15.841  1.00 24.37 ? 450 THR   A O   1 
ATOM   2323 C  CB  . THR   A 1 313 ? -22.814 -11.800 18.520  1.00 25.43 ? 450 THR   A CB  1 
ATOM   2324 O  OG1 . THR   A 1 313 ? -21.468 -11.369 18.288  1.00 24.39 ? 450 THR   A OG1 1 
ATOM   2325 C  CG2 . THR   A 1 313 ? -23.154 -11.626 20.004  1.00 24.37 ? 450 THR   A CG2 1 
ATOM   2326 N  N   . GLY   A 1 314 ? -21.749 -14.149 16.171  1.00 21.49 ? 451 GLY   A N   1 
ATOM   2327 C  CA  . GLY   A 1 314 ? -21.512 -14.363 14.756  1.00 23.47 ? 451 GLY   A CA  1 
ATOM   2328 C  C   . GLY   A 1 314 ? -20.679 -15.606 14.544  1.00 23.76 ? 451 GLY   A C   1 
ATOM   2329 O  O   . GLY   A 1 314 ? -20.126 -16.185 15.484  1.00 20.30 ? 451 GLY   A O   1 
ATOM   2330 N  N   . ILE   A 1 315 ? -20.607 -16.015 13.281  1.00 23.46 ? 452 ILE   A N   1 
ATOM   2331 C  CA  . ILE   A 1 315 ? -19.830 -17.180 12.874  1.00 23.52 ? 452 ILE   A CA  1 
ATOM   2332 C  C   . ILE   A 1 315 ? -19.063 -16.834 11.607  1.00 23.96 ? 452 ILE   A C   1 
ATOM   2333 O  O   . ILE   A 1 315 ? -19.595 -16.174 10.708  1.00 24.80 ? 452 ILE   A O   1 
ATOM   2334 C  CB  . ILE   A 1 315 ? -20.718 -18.417 12.631  1.00 26.22 ? 452 ILE   A CB  1 
ATOM   2335 C  CG1 . ILE   A 1 315 ? -21.706 -18.611 13.780  1.00 25.67 ? 452 ILE   A CG1 1 
ATOM   2336 C  CG2 . ILE   A 1 315 ? -19.846 -19.667 12.444  1.00 22.00 ? 452 ILE   A CG2 1 
ATOM   2337 C  CD1 . ILE   A 1 315 ? -22.750 -19.680 13.490  1.00 26.50 ? 452 ILE   A CD1 1 
ATOM   2338 N  N   . LEU   A 1 316 ? -17.813 -17.281 11.536  1.00 22.77 ? 453 LEU   A N   1 
ATOM   2339 C  CA  . LEU   A 1 316 ? -16.983 -17.119 10.351  1.00 26.42 ? 453 LEU   A CA  1 
ATOM   2340 C  C   . LEU   A 1 316 ? -16.936 -18.460 9.626   1.00 27.04 ? 453 LEU   A C   1 
ATOM   2341 O  O   . LEU   A 1 316 ? -16.574 -19.478 10.227  1.00 26.92 ? 453 LEU   A O   1 
ATOM   2342 C  CB  . LEU   A 1 316 ? -15.575 -16.658 10.731  1.00 25.88 ? 453 LEU   A CB  1 
ATOM   2343 C  CG  . LEU   A 1 316 ? -15.456 -15.275 11.383  1.00 26.50 ? 453 LEU   A CG  1 
ATOM   2344 C  CD1 . LEU   A 1 316 ? -14.067 -15.089 11.981  1.00 28.36 ? 453 LEU   A CD1 1 
ATOM   2345 C  CD2 . LEU   A 1 316 ? -15.778 -14.150 10.411  1.00 27.55 ? 453 LEU   A CD2 1 
ATOM   2346 N  N   . LEU   A 1 317 ? -17.301 -18.465 8.345   1.00 26.80 ? 454 LEU   A N   1 
ATOM   2347 C  CA  . LEU   A 1 317 ? -17.403 -19.707 7.594   1.00 27.50 ? 454 LEU   A CA  1 
ATOM   2348 C  C   . LEU   A 1 317 ? -16.672 -19.604 6.265   1.00 30.08 ? 454 LEU   A C   1 
ATOM   2349 O  O   . LEU   A 1 317 ? -16.549 -18.525 5.681   1.00 27.82 ? 454 LEU   A O   1 
ATOM   2350 C  CB  . LEU   A 1 317 ? -18.869 -20.101 7.335   1.00 27.63 ? 454 LEU   A CB  1 
ATOM   2351 C  CG  . LEU   A 1 317 ? -19.721 -20.462 8.554   1.00 30.67 ? 454 LEU   A CG  1 
ATOM   2352 C  CD1 . LEU   A 1 317 ? -21.181 -20.650 8.140   1.00 29.20 ? 454 LEU   A CD1 1 
ATOM   2353 C  CD2 . LEU   A 1 317 ? -19.186 -21.701 9.252   1.00 27.80 ? 454 LEU   A CD2 1 
ATOM   2354 N  N   . THR   A 1 318 ? -16.193 -20.756 5.799   1.00 29.94 ? 455 THR   A N   1 
ATOM   2355 C  CA  . THR   A 1 318 ? -15.616 -20.912 4.474   1.00 31.96 ? 455 THR   A CA  1 
ATOM   2356 C  C   . THR   A 1 318 ? -16.348 -22.052 3.786   1.00 33.95 ? 455 THR   A C   1 
ATOM   2357 O  O   . THR   A 1 318 ? -16.520 -23.123 4.377   1.00 33.91 ? 455 THR   A O   1 
ATOM   2358 C  CB  . THR   A 1 318 ? -14.115 -21.210 4.545   1.00 36.30 ? 455 THR   A CB  1 
ATOM   2359 O  OG1 . THR   A 1 318 ? -13.430 -20.090 5.119   1.00 34.55 ? 455 THR   A OG1 1 
ATOM   2360 C  CG2 . THR   A 1 318 ? -13.566 -21.473 3.150   1.00 42.31 ? 455 THR   A CG2 1 
ATOM   2361 N  N   . ARG   A 1 319 ? -16.778 -21.828 2.550   1.00 34.97 ? 456 ARG   A N   1 
ATOM   2362 C  CA  . ARG   A 1 319 ? -17.532 -22.831 1.813   1.00 37.12 ? 456 ARG   A CA  1 
ATOM   2363 C  C   . ARG   A 1 319 ? -16.596 -23.668 0.953   1.00 41.33 ? 456 ARG   A C   1 
ATOM   2364 O  O   . ARG   A 1 319 ? -15.600 -23.165 0.427   1.00 38.45 ? 456 ARG   A O   1 
ATOM   2365 C  CB  . ARG   A 1 319 ? -18.609 -22.160 0.959   1.00 38.74 ? 456 ARG   A CB  1 
ATOM   2366 C  CG  . ARG   A 1 319 ? -19.436 -23.108 0.106   1.00 41.44 ? 456 ARG   A CG  1 
ATOM   2367 C  CD  . ARG   A 1 319 ? -20.612 -22.363 -0.499  1.00 41.82 ? 456 ARG   A CD  1 
ATOM   2368 N  NE  . ARG   A 1 319 ? -20.165 -21.358 -1.457  1.00 42.01 ? 456 ARG   A NE  1 
ATOM   2369 C  CZ  . ARG   A 1 319 ? -19.987 -21.580 -2.752  1.00 45.40 ? 456 ARG   A CZ  1 
ATOM   2370 N  NH1 . ARG   A 1 319 ? -20.238 -22.760 -3.292  1.00 46.14 ? 456 ARG   A NH1 1 
ATOM   2371 N  NH2 . ARG   A 1 319 ? -19.549 -20.589 -3.525  1.00 42.05 ? 456 ARG   A NH2 1 
ATOM   2372 N  N   . ASP   A 1 320 ? -16.918 -24.956 0.832   1.00 43.09 ? 457 ASP   A N   1 
ATOM   2373 C  CA  . ASP   A 1 320 ? -16.105 -25.870 0.042   1.00 48.79 ? 457 ASP   A CA  1 
ATOM   2374 C  C   . ASP   A 1 320 ? -16.296 -25.597 -1.445  1.00 47.05 ? 457 ASP   A C   1 
ATOM   2375 O  O   . ASP   A 1 320 ? -17.410 -25.342 -1.911  1.00 46.40 ? 457 ASP   A O   1 
ATOM   2376 C  CB  . ASP   A 1 320 ? -16.476 -27.318 0.372   1.00 47.52 ? 457 ASP   A CB  1 
ATOM   2377 C  CG  . ASP   A 1 320 ? -15.648 -27.896 1.514   1.00 47.97 ? 457 ASP   A CG  1 
ATOM   2378 O  OD1 . ASP   A 1 320 ? -14.944 -27.126 2.204   1.00 48.36 ? 457 ASP   A OD1 1 
ATOM   2379 O  OD2 . ASP   A 1 320 ? -15.714 -29.128 1.723   1.00 47.67 ? 457 ASP   A OD2 1 
ATOM   2380 N  N   . GLY   A 1 321 ? -15.202 -25.687 -2.197  1.00 50.47 ? 458 GLY   A N   1 
ATOM   2381 C  CA  . GLY   A 1 321 ? -15.193 -25.277 -3.588  1.00 55.29 ? 458 GLY   A CA  1 
ATOM   2382 C  C   . GLY   A 1 321 ? -15.949 -26.150 -4.574  1.00 62.98 ? 458 GLY   A C   1 
ATOM   2383 O  O   . GLY   A 1 321 ? -17.152 -25.962 -4.794  1.00 64.15 ? 458 GLY   A O   1 
ATOM   2384 N  N   . GLY   A 1 322 ? -15.242 -27.105 -5.180  1.00 61.54 ? 459 GLY   A N   1 
ATOM   2385 C  CA  . GLY   A 1 322 ? -15.749 -27.862 -6.313  1.00 64.22 ? 459 GLY   A CA  1 
ATOM   2386 C  C   . GLY   A 1 322 ? -16.978 -28.712 -6.053  1.00 70.83 ? 459 GLY   A C   1 
ATOM   2387 O  O   . GLY   A 1 322 ? -16.964 -29.925 -6.287  1.00 74.10 ? 459 GLY   A O   1 
ATOM   2388 N  N   . ALA   A 1 323 ? -18.051 -28.087 -5.567  1.00 72.19 ? 460 ALA   A N   1 
ATOM   2389 C  CA  . ALA   A 1 323 ? -19.357 -28.722 -5.454  1.00 75.30 ? 460 ALA   A CA  1 
ATOM   2390 C  C   . ALA   A 1 323 ? -20.343 -28.152 -6.462  1.00 76.75 ? 460 ALA   A C   1 
ATOM   2391 O  O   . ALA   A 1 323 ? -21.563 -28.318 -6.306  1.00 75.57 ? 460 ALA   A O   1 
ATOM   2392 C  CB  . ALA   A 1 323 ? -19.903 -28.578 -4.035  1.00 69.67 ? 460 ALA   A CB  1 
ATOM   2393 N  N   . ASN   A 1 324 ? -19.825 -27.503 -7.505  1.00 77.82 ? 461 ASN   A N   1 
ATOM   2394 C  CA  . ASN   A 1 324 ? -20.651 -26.803 -8.476  1.00 79.51 ? 461 ASN   A CA  1 
ATOM   2395 C  C   . ASN   A 1 324 ? -21.775 -27.690 -9.002  1.00 81.12 ? 461 ASN   A C   1 
ATOM   2396 O  O   . ASN   A 1 324 ? -22.895 -27.221 -9.226  1.00 81.68 ? 461 ASN   A O   1 
ATOM   2397 C  CB  . ASN   A 1 324 ? -19.757 -26.344 -9.614  1.00 78.02 ? 461 ASN   A CB  1 
ATOM   2398 C  CG  . ASN   A 1 324 ? -19.348 -24.901 -9.479  1.00 77.60 ? 461 ASN   A CG  1 
ATOM   2399 O  OD1 . ASN   A 1 324 ? -20.034 -24.099 -8.850  1.00 75.83 ? 461 ASN   A OD1 1 
ATOM   2400 N  ND2 . ASN   A 1 324 ? -18.158 -24.588 -9.981  1.00 76.14 ? 461 ASN   A ND2 1 
ATOM   2401 N  N   . ASN   A 1 325 ? -21.499 -28.986 -9.165  1.00 81.28 ? 462 ASN   A N   1 
ATOM   2402 C  CA  . ASN   A 1 325 ? -22.438 -29.930 -9.751  1.00 83.89 ? 462 ASN   A CA  1 
ATOM   2403 C  C   . ASN   A 1 325 ? -22.782 -31.058 -8.788  1.00 83.08 ? 462 ASN   A C   1 
ATOM   2404 O  O   . ASN   A 1 325 ? -23.113 -32.162 -9.220  1.00 83.17 ? 462 ASN   A O   1 
ATOM   2405 C  CB  . ASN   A 1 325 ? -21.878 -30.518 -11.045 1.00 88.59 ? 462 ASN   A CB  1 
ATOM   2406 C  CG  . ASN   A 1 325 ? -20.372 -30.687 -11.003 1.00 86.90 ? 462 ASN   A CG  1 
ATOM   2407 O  OD1 . ASN   A 1 325 ? -19.773 -30.787 -9.929  1.00 85.23 ? 462 ASN   A OD1 1 
ATOM   2408 N  ND2 . ASN   A 1 325 ? -19.757 -30.766 -12.176 1.00 84.18 ? 462 ASN   A ND2 1 
ATOM   2409 N  N   . THR   A 1 326 ? -22.698 -30.814 -7.488  1.00 79.18 ? 463 THR   A N   1 
ATOM   2410 C  CA  . THR   A 1 326 ? -23.155 -31.792 -6.512  1.00 74.34 ? 463 THR   A CA  1 
ATOM   2411 C  C   . THR   A 1 326 ? -24.421 -31.279 -5.838  1.00 69.94 ? 463 THR   A C   1 
ATOM   2412 O  O   . THR   A 1 326 ? -24.960 -30.229 -6.194  1.00 70.93 ? 463 THR   A O   1 
ATOM   2413 C  CB  . THR   A 1 326 ? -22.048 -32.117 -5.504  1.00 73.92 ? 463 THR   A CB  1 
ATOM   2414 O  OG1 . THR   A 1 326 ? -22.543 -31.981 -4.166  1.00 69.29 ? 463 THR   A OG1 1 
ATOM   2415 C  CG2 . THR   A 1 326 ? -20.857 -31.214 -5.708  1.00 73.51 ? 463 THR   A CG2 1 
ATOM   2416 N  N   . SER   A 1 327 ? -24.913 -32.043 -4.868  1.00 65.51 ? 464 SER   A N   1 
ATOM   2417 C  CA  . SER   A 1 327 ? -26.144 -31.699 -4.174  1.00 63.50 ? 464 SER   A CA  1 
ATOM   2418 C  C   . SER   A 1 327 ? -25.898 -31.070 -2.814  1.00 60.51 ? 464 SER   A C   1 
ATOM   2419 O  O   . SER   A 1 327 ? -26.862 -30.764 -2.102  1.00 55.72 ? 464 SER   A O   1 
ATOM   2420 C  CB  . SER   A 1 327 ? -27.016 -32.944 -3.997  1.00 66.11 ? 464 SER   A CB  1 
ATOM   2421 O  OG  . SER   A 1 327 ? -26.273 -34.026 -3.453  1.00 68.51 ? 464 SER   A OG  1 
ATOM   2422 N  N   . ASN   A 1 328 ? -24.641 -30.851 -2.443  1.00 62.80 ? 465 ASN   A N   1 
ATOM   2423 C  CA  . ASN   A 1 328 ? -24.314 -30.461 -1.087  1.00 59.01 ? 465 ASN   A CA  1 
ATOM   2424 C  C   . ASN   A 1 328 ? -23.470 -29.203 -1.104  1.00 54.61 ? 465 ASN   A C   1 
ATOM   2425 O  O   . ASN   A 1 328 ? -22.630 -29.014 -1.988  1.00 57.23 ? 465 ASN   A O   1 
ATOM   2426 C  CB  . ASN   A 1 328 ? -23.566 -31.578 -0.362  1.00 58.29 ? 465 ASN   A CB  1 
ATOM   2427 C  CG  . ASN   A 1 328 ? -24.414 -32.823 -0.202  1.00 60.44 ? 465 ASN   A CG  1 
ATOM   2428 O  OD1 . ASN   A 1 328 ? -24.479 -33.663 -1.102  1.00 65.04 ? 465 ASN   A OD1 1 
ATOM   2429 N  ND2 . ASN   A 1 328 ? -25.112 -32.923 0.919   1.00 57.41 ? 465 ASN   A ND2 1 
ATOM   2430 N  N   . GLU   A 1 329 ? -23.704 -28.350 -0.114  1.00 49.55 ? 466 GLU   A N   1 
ATOM   2431 C  CA  . GLU   A 1 329 ? -22.848 -27.211 0.157   1.00 48.50 ? 466 GLU   A CA  1 
ATOM   2432 C  C   . GLU   A 1 329 ? -22.325 -27.439 1.568   1.00 41.90 ? 466 GLU   A C   1 
ATOM   2433 O  O   . GLU   A 1 329 ? -23.119 -27.542 2.510   1.00 42.86 ? 466 GLU   A O   1 
ATOM   2434 C  CB  . GLU   A 1 329 ? -23.635 -25.900 0.061   1.00 44.63 ? 466 GLU   A CB  1 
ATOM   2435 C  CG  . GLU   A 1 329 ? -23.952 -25.411 -1.366  1.00 46.02 ? 466 GLU   A CG  1 
ATOM   2436 C  CD  . GLU   A 1 329 ? -22.742 -25.180 -2.257  1.00 47.56 ? 466 GLU   A CD  1 
ATOM   2437 O  OE1 . GLU   A 1 329 ? -21.595 -25.315 -1.787  1.00 51.74 ? 466 GLU   A OE1 1 
ATOM   2438 O  OE2 . GLU   A 1 329 ? -22.953 -24.869 -3.450  1.00 55.38 ? 466 GLU   A OE2 1 
ATOM   2439 N  N   . THR   A 1 330 ? -21.014 -27.582 1.714   1.00 43.22 ? 467 THR   A N   1 
ATOM   2440 C  CA  . THR   A 1 330 ? -20.420 -27.808 3.022   1.00 42.96 ? 467 THR   A CA  1 
ATOM   2441 C  C   . THR   A 1 330 ? -19.657 -26.569 3.457   1.00 40.25 ? 467 THR   A C   1 
ATOM   2442 O  O   . THR   A 1 330 ? -18.962 -25.935 2.654   1.00 39.14 ? 467 THR   A O   1 
ATOM   2443 C  CB  . THR   A 1 330 ? -19.487 -29.025 3.036   1.00 42.76 ? 467 THR   A CB  1 
ATOM   2444 O  OG1 . THR   A 1 330 ? -18.184 -28.640 2.588   1.00 49.15 ? 467 THR   A OG1 1 
ATOM   2445 C  CG2 . THR   A 1 330 ? -20.030 -30.124 2.143   1.00 38.79 ? 467 THR   A CG2 1 
ATOM   2446 N  N   . PHE   A 1 331 ? -19.780 -26.242 4.737   1.00 33.62 ? 468 PHE   A N   1 
ATOM   2447 C  CA  . PHE   A 1 331 ? -19.185 -25.044 5.299   1.00 36.48 ? 468 PHE   A CA  1 
ATOM   2448 C  C   . PHE   A 1 331 ? -18.270 -25.438 6.445   1.00 32.48 ? 468 PHE   A C   1 
ATOM   2449 O  O   . PHE   A 1 331 ? -18.579 -26.356 7.210   1.00 32.79 ? 468 PHE   A O   1 
ATOM   2450 C  CB  . PHE   A 1 331 ? -20.272 -24.081 5.777   1.00 32.44 ? 468 PHE   A CB  1 
ATOM   2451 C  CG  . PHE   A 1 331 ? -21.199 -23.642 4.683   1.00 38.13 ? 468 PHE   A CG  1 
ATOM   2452 C  CD1 . PHE   A 1 331 ? -22.238 -24.467 4.273   1.00 36.41 ? 468 PHE   A CD1 1 
ATOM   2453 C  CD2 . PHE   A 1 331 ? -21.021 -22.427 4.044   1.00 33.62 ? 468 PHE   A CD2 1 
ATOM   2454 C  CE1 . PHE   A 1 331 ? -23.088 -24.085 3.259   1.00 38.51 ? 468 PHE   A CE1 1 
ATOM   2455 C  CE2 . PHE   A 1 331 ? -21.871 -22.034 3.027   1.00 35.39 ? 468 PHE   A CE2 1 
ATOM   2456 C  CZ  . PHE   A 1 331 ? -22.907 -22.864 2.634   1.00 37.99 ? 468 PHE   A CZ  1 
ATOM   2457 N  N   . ARG   A 1 332 ? -17.139 -24.751 6.551   1.00 32.09 ? 469 ARG   A N   1 
ATOM   2458 C  CA  . ARG   A 1 332 ? -16.191 -25.017 7.612   1.00 29.40 ? 469 ARG   A CA  1 
ATOM   2459 C  C   . ARG   A 1 332 ? -15.914 -23.746 8.400   1.00 29.74 ? 469 ARG   A C   1 
ATOM   2460 O  O   . ARG   A 1 332 ? -15.855 -22.659 7.815   1.00 30.93 ? 469 ARG   A O   1 
ATOM   2461 C  CB  . ARG   A 1 332 ? -14.877 -25.574 7.047   1.00 33.29 ? 469 ARG   A CB  1 
ATOM   2462 C  CG  . ARG   A 1 332 ? -15.072 -26.894 6.325   1.00 39.34 ? 469 ARG   A CG  1 
ATOM   2463 C  CD  . ARG   A 1 332 ? -13.846 -27.347 5.557   1.00 44.57 ? 469 ARG   A CD  1 
ATOM   2464 N  NE  . ARG   A 1 332 ? -14.234 -28.286 4.513   1.00 43.60 ? 469 ARG   A NE  1 
ATOM   2465 C  CZ  . ARG   A 1 332 ? -14.108 -29.603 4.606   1.00 45.58 ? 469 ARG   A CZ  1 
ATOM   2466 N  NH1 . ARG   A 1 332 ? -13.585 -30.174 5.677   1.00 42.67 ? 469 ARG   A NH1 1 
ATOM   2467 N  NH2 . ARG   A 1 332 ? -14.533 -30.366 3.603   1.00 48.02 ? 469 ARG   A NH2 1 
ATOM   2468 N  N   . PRO   A 1 333 ? -15.755 -23.845 9.717   1.00 31.09 ? 470 PRO   A N   1 
ATOM   2469 C  CA  . PRO   A 1 333 ? -15.410 -22.657 10.502  1.00 29.40 ? 470 PRO   A CA  1 
ATOM   2470 C  C   . PRO   A 1 333 ? -14.077 -22.094 10.048  1.00 31.70 ? 470 PRO   A C   1 
ATOM   2471 O  O   . PRO   A 1 333 ? -13.112 -22.831 9.813   1.00 31.50 ? 470 PRO   A O   1 
ATOM   2472 C  CB  . PRO   A 1 333 ? -15.345 -23.172 11.945  1.00 28.77 ? 470 PRO   A CB  1 
ATOM   2473 C  CG  . PRO   A 1 333 ? -16.019 -24.510 11.938  1.00 30.65 ? 470 PRO   A CG  1 
ATOM   2474 C  CD  . PRO   A 1 333 ? -15.965 -25.046 10.542  1.00 31.50 ? 470 PRO   A CD  1 
ATOM   2475 N  N   . GLY   A 1 334 ? -14.036 -20.772 9.918   1.00 32.74 ? 471 GLY   A N   1 
ATOM   2476 C  CA  . GLY   A 1 334 ? -12.831 -20.116 9.458   1.00 33.13 ? 471 GLY   A CA  1 
ATOM   2477 C  C   . GLY   A 1 334 ? -12.368 -18.999 10.365  1.00 31.18 ? 471 GLY   A C   1 
ATOM   2478 O  O   . GLY   A 1 334 ? -12.692 -18.989 11.551  1.00 28.79 ? 471 GLY   A O   1 
ATOM   2479 N  N   . GLY   A 1 335 ? -11.617 -18.059 9.814   1.00 30.98 ? 472 GLY   A N   1 
ATOM   2480 C  CA  . GLY   A 1 335 ? -11.081 -16.930 10.535  1.00 31.83 ? 472 GLY   A CA  1 
ATOM   2481 C  C   . GLY   A 1 335 ? -9.594  -16.805 10.311  1.00 34.04 ? 472 GLY   A C   1 
ATOM   2482 O  O   . GLY   A 1 335 ? -8.996  -17.505 9.484   1.00 32.80 ? 472 GLY   A O   1 
ATOM   2483 N  N   . GLY   A 1 336 ? -8.981  -15.895 11.065  1.00 30.96 ? 473 GLY   A N   1 
ATOM   2484 C  CA  . GLY   A 1 336 ? -7.562  -15.639 10.932  1.00 35.37 ? 473 GLY   A CA  1 
ATOM   2485 C  C   . GLY   A 1 336 ? -7.258  -14.197 10.600  1.00 30.18 ? 473 GLY   A C   1 
ATOM   2486 O  O   . GLY   A 1 336 ? -6.302  -13.620 11.127  1.00 32.79 ? 473 GLY   A O   1 
ATOM   2487 N  N   . ASP   A 1 337 ? -8.080  -13.603 9.735   1.00 31.11 ? 474 ASP   A N   1 
ATOM   2488 C  CA  . ASP   A 1 337 ? -7.966  -12.191 9.379   1.00 30.67 ? 474 ASP   A CA  1 
ATOM   2489 C  C   . ASP   A 1 337 ? -8.905  -11.402 10.286  1.00 26.67 ? 474 ASP   A C   1 
ATOM   2490 O  O   . ASP   A 1 337 ? -10.106 -11.314 10.028  1.00 27.00 ? 474 ASP   A O   1 
ATOM   2491 C  CB  . ASP   A 1 337 ? -8.299  -11.975 7.906   1.00 30.71 ? 474 ASP   A CB  1 
ATOM   2492 C  CG  . ASP   A 1 337 ? -7.969  -10.568 7.428   1.00 33.14 ? 474 ASP   A CG  1 
ATOM   2493 O  OD1 . ASP   A 1 337 ? -7.665  -9.705  8.279   1.00 29.16 ? 474 ASP   A OD1 1 
ATOM   2494 O  OD2 . ASP   A 1 337 ? -8.019  -10.335 6.202   1.00 36.25 ? 474 ASP   A OD2 1 
ATOM   2495 N  N   . MET   A 1 338 ? -8.360  -10.832 11.363  1.00 26.61 ? 475 MET   A N   1 
ATOM   2496 C  CA  . MET   A 1 338 ? -9.179  -10.090 12.322  1.00 25.61 ? 475 MET   A CA  1 
ATOM   2497 C  C   . MET   A 1 338 ? -9.914  -8.923  11.693  1.00 27.67 ? 475 MET   A C   1 
ATOM   2498 O  O   . MET   A 1 338 ? -10.842 -8.386  12.310  1.00 23.78 ? 475 MET   A O   1 
ATOM   2499 C  CB  . MET   A 1 338 ? -8.306  -9.608  13.485  1.00 24.36 ? 475 MET   A CB  1 
ATOM   2500 C  CG  . MET   A 1 338 ? -7.664  -10.746 14.260  1.00 26.07 ? 475 MET   A CG  1 
ATOM   2501 S  SD  . MET   A 1 338 ? -8.893  -12.054 14.599  1.00 25.46 ? 475 MET   A SD  1 
ATOM   2502 C  CE  . MET   A 1 338 ? -7.747  -13.421 14.956  1.00 25.65 ? 475 MET   A CE  1 
ATOM   2503 N  N   . ARG   A 1 339 ? -9.514  -8.495  10.495  1.00 23.49 ? 476 ARG   A N   1 
ATOM   2504 C  CA  . ARG   A 1 339 ? -10.283 -7.463  9.803   1.00 26.37 ? 476 ARG   A CA  1 
ATOM   2505 C  C   . ARG   A 1 339 ? -11.739 -7.885  9.632   1.00 26.05 ? 476 ARG   A C   1 
ATOM   2506 O  O   . ARG   A 1 339 ? -12.654 -7.058  9.745   1.00 24.69 ? 476 ARG   A O   1 
ATOM   2507 C  CB  . ARG   A 1 339 ? -9.621  -7.147  8.460   1.00 29.47 ? 476 ARG   A CB  1 
ATOM   2508 C  CG  . ARG   A 1 339 ? -8.316  -6.386  8.658   1.00 32.10 ? 476 ARG   A CG  1 
ATOM   2509 C  CD  . ARG   A 1 339 ? -7.726  -5.842  7.366   1.00 39.29 ? 476 ARG   A CD  1 
ATOM   2510 N  NE  . ARG   A 1 339 ? -7.827  -6.794  6.266   1.00 42.63 ? 476 ARG   A NE  1 
ATOM   2511 C  CZ  . ARG   A 1 339 ? -6.840  -7.595  5.890   1.00 47.63 ? 476 ARG   A CZ  1 
ATOM   2512 N  NH1 . ARG   A 1 339 ? -5.686  -7.616  6.533   1.00 50.01 ? 476 ARG   A NH1 1 
ATOM   2513 N  NH2 . ARG   A 1 339 ? -7.021  -8.402  4.847   1.00 47.03 ? 476 ARG   A NH2 1 
ATOM   2514 N  N   . ASP   A 1 340 ? -11.977 -9.173  9.374   1.00 22.41 ? 477 ASP   A N   1 
ATOM   2515 C  CA  . ASP   A 1 340 ? -13.345 -9.667  9.300   1.00 23.01 ? 477 ASP   A CA  1 
ATOM   2516 C  C   . ASP   A 1 340 ? -14.071 -9.485  10.627  1.00 23.63 ? 477 ASP   A C   1 
ATOM   2517 O  O   . ASP   A 1 340 ? -15.260 -9.155  10.644  1.00 23.48 ? 477 ASP   A O   1 
ATOM   2518 C  CB  . ASP   A 1 340 ? -13.353 -11.132 8.860   1.00 24.72 ? 477 ASP   A CB  1 
ATOM   2519 C  CG  . ASP   A 1 340 ? -12.932 -11.307 7.407   1.00 28.99 ? 477 ASP   A CG  1 
ATOM   2520 O  OD1 . ASP   A 1 340 ? -13.075 -10.339 6.636   1.00 30.28 ? 477 ASP   A OD1 1 
ATOM   2521 O  OD2 . ASP   A 1 340 ? -12.458 -12.405 7.042   1.00 29.78 ? 477 ASP   A OD2 1 
ATOM   2522 N  N   . ASN   A 1 341 ? -13.382 -9.695  11.753  1.00 22.75 ? 478 ASN   A N   1 
ATOM   2523 C  CA  . ASN   A 1 341 ? -13.997 -9.396  13.047  1.00 21.93 ? 478 ASN   A CA  1 
ATOM   2524 C  C   . ASN   A 1 341 ? -14.443 -7.938  13.125  1.00 24.23 ? 478 ASN   A C   1 
ATOM   2525 O  O   . ASN   A 1 341 ? -15.591 -7.645  13.486  1.00 22.72 ? 478 ASN   A O   1 
ATOM   2526 C  CB  . ASN   A 1 341 ? -13.031 -9.714  14.190  1.00 21.70 ? 478 ASN   A CB  1 
ATOM   2527 C  CG  . ASN   A 1 341 ? -12.691 -11.189 14.281  1.00 23.66 ? 478 ASN   A CG  1 
ATOM   2528 O  OD1 . ASN   A 1 341 ? -12.526 -11.860 13.267  1.00 24.70 ? 478 ASN   A OD1 1 
ATOM   2529 N  ND2 . ASN   A 1 341 ? -12.590 -11.703 15.508  1.00 19.84 ? 478 ASN   A ND2 1 
ATOM   2530 N  N   . TRP   A 1 342 ? -13.542 -7.002  12.805  1.00 21.29 ? 479 TRP   A N   1 
ATOM   2531 C  CA  . TRP   A 1 342 ? -13.907 -5.589  12.858  1.00 21.97 ? 479 TRP   A CA  1 
ATOM   2532 C  C   . TRP   A 1 342 ? -15.005 -5.289  11.853  1.00 22.50 ? 479 TRP   A C   1 
ATOM   2533 O  O   . TRP   A 1 342 ? -15.930 -4.521  12.136  1.00 21.11 ? 479 TRP   A O   1 
ATOM   2534 C  CB  . TRP   A 1 342 ? -12.699 -4.700  12.564  1.00 22.32 ? 479 TRP   A CB  1 
ATOM   2535 C  CG  . TRP   A 1 342 ? -11.412 -5.186  13.149  1.00 21.85 ? 479 TRP   A CG  1 
ATOM   2536 C  CD1 . TRP   A 1 342 ? -10.174 -5.106  12.573  1.00 22.15 ? 479 TRP   A CD1 1 
ATOM   2537 C  CD2 . TRP   A 1 342 ? -11.230 -5.848  14.406  1.00 21.81 ? 479 TRP   A CD2 1 
ATOM   2538 N  NE1 . TRP   A 1 342 ? -9.231  -5.650  13.406  1.00 22.53 ? 479 TRP   A NE1 1 
ATOM   2539 C  CE2 . TRP   A 1 342 ? -9.851  -6.123  14.534  1.00 23.33 ? 479 TRP   A CE2 1 
ATOM   2540 C  CE3 . TRP   A 1 342 ? -12.095 -6.233  15.439  1.00 22.07 ? 479 TRP   A CE3 1 
ATOM   2541 C  CZ2 . TRP   A 1 342 ? -9.317  -6.770  15.653  1.00 22.04 ? 479 TRP   A CZ2 1 
ATOM   2542 C  CZ3 . TRP   A 1 342 ? -11.566 -6.867  16.548  1.00 21.55 ? 479 TRP   A CZ3 1 
ATOM   2543 C  CH2 . TRP   A 1 342 ? -10.189 -7.131  16.646  1.00 22.99 ? 479 TRP   A CH2 1 
ATOM   2544 N  N   . ARG   A 1 343 ? -14.909 -5.893  10.668  1.00 21.64 ? 480 ARG   A N   1 
ATOM   2545 C  CA  . ARG   A 1 343 ? -15.906 -5.724  9.621   1.00 22.94 ? 480 ARG   A CA  1 
ATOM   2546 C  C   . ARG   A 1 343 ? -17.295 -6.117  10.110  1.00 23.89 ? 480 ARG   A C   1 
ATOM   2547 O  O   . ARG   A 1 343 ? -18.293 -5.517  9.699   1.00 23.23 ? 480 ARG   A O   1 
ATOM   2548 C  CB  . ARG   A 1 343 ? -15.498 -6.587  8.428   1.00 25.79 ? 480 ARG   A CB  1 
ATOM   2549 C  CG  . ARG   A 1 343 ? -16.015 -6.172  7.089   1.00 31.97 ? 480 ARG   A CG  1 
ATOM   2550 C  CD  . ARG   A 1 343 ? -15.531 -7.162  6.032   1.00 29.29 ? 480 ARG   A CD  1 
ATOM   2551 N  NE  . ARG   A 1 343 ? -14.079 -7.318  6.001   1.00 29.49 ? 480 ARG   A NE  1 
ATOM   2552 C  CZ  . ARG   A 1 343 ? -13.225 -6.380  5.614   1.00 31.54 ? 480 ARG   A CZ  1 
ATOM   2553 N  NH1 . ARG   A 1 343 ? -13.641 -5.186  5.228   1.00 30.50 ? 480 ARG   A NH1 1 
ATOM   2554 N  NH2 . ARG   A 1 343 ? -11.921 -6.655  5.599   1.00 27.53 ? 480 ARG   A NH2 1 
ATOM   2555 N  N   . SER   A 1 344 ? -17.376 -7.122  10.986  1.00 19.97 ? 481 SER   A N   1 
ATOM   2556 C  CA  . SER   A 1 344 ? -18.663 -7.615  11.462  1.00 23.65 ? 481 SER   A CA  1 
ATOM   2557 C  C   . SER   A 1 344 ? -19.410 -6.585  12.296  1.00 22.19 ? 481 SER   A C   1 
ATOM   2558 O  O   . SER   A 1 344 ? -20.622 -6.727  12.490  1.00 22.16 ? 481 SER   A O   1 
ATOM   2559 C  CB  . SER   A 1 344 ? -18.456 -8.905  12.261  1.00 22.64 ? 481 SER   A CB  1 
ATOM   2560 O  OG  . SER   A 1 344 ? -17.975 -8.628  13.573  1.00 21.50 ? 481 SER   A OG  1 
ATOM   2561 N  N   . GLU   A 1 345 ? -18.724 -5.558  12.795  1.00 21.20 ? 482 GLU   A N   1 
ATOM   2562 C  CA  . GLU   A 1 345 ? -19.369 -4.490  13.545  1.00 23.09 ? 482 GLU   A CA  1 
ATOM   2563 C  C   . GLU   A 1 345 ? -19.375 -3.162  12.807  1.00 23.23 ? 482 GLU   A C   1 
ATOM   2564 O  O   . GLU   A 1 345 ? -20.274 -2.347  13.030  1.00 25.62 ? 482 GLU   A O   1 
ATOM   2565 C  CB  . GLU   A 1 345 ? -18.686 -4.315  14.911  1.00 24.32 ? 482 GLU   A CB  1 
ATOM   2566 C  CG  . GLU   A 1 345 ? -18.750 -5.564  15.794  1.00 20.07 ? 482 GLU   A CG  1 
ATOM   2567 C  CD  . GLU   A 1 345 ? -20.172 -5.889  16.246  1.00 27.03 ? 482 GLU   A CD  1 
ATOM   2568 O  OE1 . GLU   A 1 345 ? -20.996 -4.951  16.336  1.00 27.92 ? 482 GLU   A OE1 1 
ATOM   2569 O  OE2 . GLU   A 1 345 ? -20.461 -7.076  16.504  1.00 26.67 ? 482 GLU   A OE2 1 
ATOM   2570 N  N   . LEU   A 1 346 ? -18.403 -2.932  11.923  1.00 20.97 ? 483 LEU   A N   1 
ATOM   2571 C  CA  . LEU   A 1 346 ? -18.284 -1.692  11.168  1.00 23.57 ? 483 LEU   A CA  1 
ATOM   2572 C  C   . LEU   A 1 346 ? -19.090 -1.699  9.874   1.00 22.85 ? 483 LEU   A C   1 
ATOM   2573 O  O   . LEU   A 1 346 ? -19.120 -0.679  9.178   1.00 24.32 ? 483 LEU   A O   1 
ATOM   2574 C  CB  . LEU   A 1 346 ? -16.808 -1.423  10.848  1.00 20.77 ? 483 LEU   A CB  1 
ATOM   2575 C  CG  . LEU   A 1 346 ? -15.958 -1.005  12.046  1.00 19.67 ? 483 LEU   A CG  1 
ATOM   2576 C  CD1 . LEU   A 1 346 ? -14.478 -1.016  11.659  1.00 23.65 ? 483 LEU   A CD1 1 
ATOM   2577 C  CD2 . LEU   A 1 346 ? -16.371 0.370   12.519  1.00 22.88 ? 483 LEU   A CD2 1 
ATOM   2578 N  N   . TYR   A 1 347 ? -19.752 -2.815  9.548   1.00 22.06 ? 484 TYR   A N   1 
ATOM   2579 C  CA  . TYR   A 1 347 ? -20.401 -2.975  8.248   1.00 25.23 ? 484 TYR   A CA  1 
ATOM   2580 C  C   . TYR   A 1 347 ? -21.427 -1.889  7.946   1.00 25.66 ? 484 TYR   A C   1 
ATOM   2581 O  O   . TYR   A 1 347 ? -21.696 -1.606  6.773   1.00 24.89 ? 484 TYR   A O   1 
ATOM   2582 C  CB  . TYR   A 1 347 ? -21.060 -4.355  8.170   1.00 24.84 ? 484 TYR   A CB  1 
ATOM   2583 C  CG  . TYR   A 1 347 ? -22.289 -4.467  9.051   1.00 23.20 ? 484 TYR   A CG  1 
ATOM   2584 C  CD1 . TYR   A 1 347 ? -22.161 -4.834  10.388  1.00 23.20 ? 484 TYR   A CD1 1 
ATOM   2585 C  CD2 . TYR   A 1 347 ? -23.553 -4.158  8.574   1.00 25.24 ? 484 TYR   A CD2 1 
ATOM   2586 C  CE1 . TYR   A 1 347 ? -23.251 -4.924  11.211  1.00 24.85 ? 484 TYR   A CE1 1 
ATOM   2587 C  CE2 . TYR   A 1 347 ? -24.665 -4.236  9.397   1.00 26.40 ? 484 TYR   A CE2 1 
ATOM   2588 C  CZ  . TYR   A 1 347 ? -24.504 -4.624  10.718  1.00 29.28 ? 484 TYR   A CZ  1 
ATOM   2589 O  OH  . TYR   A 1 347 ? -25.593 -4.711  11.551  1.00 30.76 ? 484 TYR   A OH  1 
ATOM   2590 N  N   . LYS   A 1 348 ? -22.037 -1.289  8.965   1.00 25.26 ? 485 LYS   A N   1 
ATOM   2591 C  CA  . LYS   A 1 348 ? -23.112 -0.332  8.728   1.00 25.13 ? 485 LYS   A CA  1 
ATOM   2592 C  C   . LYS   A 1 348 ? -22.636 1.118   8.706   1.00 26.14 ? 485 LYS   A C   1 
ATOM   2593 O  O   . LYS   A 1 348 ? -23.468 2.031   8.652   1.00 26.88 ? 485 LYS   A O   1 
ATOM   2594 C  CB  . LYS   A 1 348 ? -24.217 -0.522  9.769   1.00 27.34 ? 485 LYS   A CB  1 
ATOM   2595 C  CG  . LYS   A 1 348 ? -23.889 -0.065  11.176  1.00 26.66 ? 485 LYS   A CG  1 
ATOM   2596 C  CD  . LYS   A 1 348 ? -24.761 -0.818  12.178  1.00 35.46 ? 485 LYS   A CD  1 
ATOM   2597 C  CE  . LYS   A 1 348 ? -25.444 0.117   13.157  1.00 37.94 ? 485 LYS   A CE  1 
ATOM   2598 N  NZ  . LYS   A 1 348 ? -26.586 -0.570  13.833  1.00 46.84 ? 485 LYS   A NZ  1 
ATOM   2599 N  N   . TYR   A 1 349 ? -21.323 1.350   8.705   1.00 24.39 ? 486 TYR   A N   1 
ATOM   2600 C  CA  . TYR   A 1 349 ? -20.753 2.687   8.749   1.00 24.77 ? 486 TYR   A CA  1 
ATOM   2601 C  C   . TYR   A 1 349 ? -19.883 2.937   7.526   1.00 25.66 ? 486 TYR   A C   1 
ATOM   2602 O  O   . TYR   A 1 349 ? -19.286 2.014   6.962   1.00 24.24 ? 486 TYR   A O   1 
ATOM   2603 C  CB  . TYR   A 1 349 ? -19.883 2.888   9.989   1.00 25.31 ? 486 TYR   A CB  1 
ATOM   2604 C  CG  . TYR   A 1 349 ? -20.595 2.725   11.310  1.00 24.21 ? 486 TYR   A CG  1 
ATOM   2605 C  CD1 . TYR   A 1 349 ? -21.486 3.687   11.775  1.00 24.17 ? 486 TYR   A CD1 1 
ATOM   2606 C  CD2 . TYR   A 1 349 ? -20.351 1.616   12.103  1.00 21.99 ? 486 TYR   A CD2 1 
ATOM   2607 C  CE1 . TYR   A 1 349 ? -22.120 3.536   12.991  1.00 25.92 ? 486 TYR   A CE1 1 
ATOM   2608 C  CE2 . TYR   A 1 349 ? -20.982 1.453   13.322  1.00 23.87 ? 486 TYR   A CE2 1 
ATOM   2609 C  CZ  . TYR   A 1 349 ? -21.864 2.411   13.760  1.00 25.25 ? 486 TYR   A CZ  1 
ATOM   2610 O  OH  . TYR   A 1 349 ? -22.485 2.254   14.977  1.00 22.44 ? 486 TYR   A OH  1 
ATOM   2611 N  N   . LYS   A 1 350 ? -19.788 4.204   7.144   1.00 25.50 ? 487 LYS   A N   1 
ATOM   2612 C  CA  . LYS   A 1 350 ? -18.859 4.611   6.105   1.00 27.03 ? 487 LYS   A CA  1 
ATOM   2613 C  C   . LYS   A 1 350 ? -18.598 6.101   6.248   1.00 29.51 ? 487 LYS   A C   1 
ATOM   2614 O  O   . LYS   A 1 350 ? -19.478 6.864   6.658   1.00 27.40 ? 487 LYS   A O   1 
ATOM   2615 C  CB  . LYS   A 1 350 ? -19.390 4.241   4.716   1.00 31.99 ? 487 LYS   A CB  1 
ATOM   2616 C  CG  . LYS   A 1 350 ? -20.351 5.220   4.083   1.00 34.63 ? 487 LYS   A CG  1 
ATOM   2617 C  CD  . LYS   A 1 350 ? -20.229 5.139   2.558   1.00 37.95 ? 487 LYS   A CD  1 
ATOM   2618 C  CE  . LYS   A 1 350 ? -21.316 5.946   1.869   1.00 40.98 ? 487 LYS   A CE  1 
ATOM   2619 N  NZ  . LYS   A 1 350 ? -21.179 5.872   0.385   1.00 44.99 ? 487 LYS   A NZ  1 
ATOM   2620 N  N   . VAL   A 1 351 ? -17.367 6.497   5.943   1.00 26.10 ? 488 VAL   A N   1 
ATOM   2621 C  CA  . VAL   A 1 351 ? -16.929 7.878   6.101   1.00 26.78 ? 488 VAL   A CA  1 
ATOM   2622 C  C   . VAL   A 1 351 ? -17.198 8.633   4.811   1.00 31.91 ? 488 VAL   A C   1 
ATOM   2623 O  O   . VAL   A 1 351 ? -16.966 8.116   3.714   1.00 33.60 ? 488 VAL   A O   1 
ATOM   2624 C  CB  . VAL   A 1 351 ? -15.437 7.945   6.476   1.00 27.65 ? 488 VAL   A CB  1 
ATOM   2625 C  CG1 . VAL   A 1 351 ? -14.939 9.387   6.447   1.00 26.56 ? 488 VAL   A CG1 1 
ATOM   2626 C  CG2 . VAL   A 1 351 ? -15.190 7.298   7.838   1.00 25.82 ? 488 VAL   A CG2 1 
ATOM   2627 N  N   . VAL   A 1 352 ? -17.701 9.856   4.938   1.00 32.21 ? 489 VAL   A N   1 
ATOM   2628 C  CA  . VAL   A 1 352 ? -17.902 10.738  3.798   1.00 35.09 ? 489 VAL   A CA  1 
ATOM   2629 C  C   . VAL   A 1 352 ? -17.337 12.104  4.147   1.00 37.14 ? 489 VAL   A C   1 
ATOM   2630 O  O   . VAL   A 1 352 ? -17.271 12.489  5.319   1.00 36.29 ? 489 VAL   A O   1 
ATOM   2631 C  CB  . VAL   A 1 352 ? -19.392 10.850  3.403   1.00 36.41 ? 489 VAL   A CB  1 
ATOM   2632 C  CG1 . VAL   A 1 352 ? -19.921 9.496   2.936   1.00 34.74 ? 489 VAL   A CG1 1 
ATOM   2633 C  CG2 . VAL   A 1 352 ? -20.217 11.389  4.559   1.00 37.14 ? 489 VAL   A CG2 1 
ATOM   2634 N  N   . GLN   A 1 353 ? -16.915 12.834  3.120   1.00 35.07 ? 490 GLN   A N   1 
ATOM   2635 C  CA  . GLN   A 1 353 ? -16.435 14.195  3.289   1.00 42.60 ? 490 GLN   A CA  1 
ATOM   2636 C  C   . GLN   A 1 353 ? -17.572 15.156  2.979   1.00 41.28 ? 490 GLN   A C   1 
ATOM   2637 O  O   . GLN   A 1 353 ? -18.226 15.039  1.937   1.00 42.88 ? 490 GLN   A O   1 
ATOM   2638 C  CB  . GLN   A 1 353 ? -15.234 14.480  2.388   1.00 42.19 ? 490 GLN   A CB  1 
ATOM   2639 C  CG  . GLN   A 1 353 ? -14.566 15.810  2.688   1.00 45.13 ? 490 GLN   A CG  1 
ATOM   2640 C  CD  . GLN   A 1 353 ? -13.332 16.052  1.845   1.00 48.38 ? 490 GLN   A CD  1 
ATOM   2641 O  OE1 . GLN   A 1 353 ? -13.260 15.623  0.695   1.00 50.86 ? 490 GLN   A OE1 1 
ATOM   2642 N  NE2 . GLN   A 1 353 ? -12.345 16.730  2.421   1.00 53.60 ? 490 GLN   A NE2 1 
ATOM   2643 N  N   . ILE   A 1 354 ? -17.816 16.089  3.893   1.00 46.48 ? 491 ILE   A N   1 
ATOM   2644 C  CA  . ILE   A 1 354 ? -18.884 17.064  3.710   1.00 46.57 ? 491 ILE   A CA  1 
ATOM   2645 C  C   . ILE   A 1 354 ? -18.430 18.028  2.618   1.00 51.10 ? 491 ILE   A C   1 
ATOM   2646 O  O   . ILE   A 1 354 ? -17.492 18.803  2.821   1.00 49.29 ? 491 ILE   A O   1 
ATOM   2647 C  CB  . ILE   A 1 354 ? -19.192 17.813  5.010   1.00 49.11 ? 491 ILE   A CB  1 
ATOM   2648 C  CG1 . ILE   A 1 354 ? -20.005 16.927  5.960   1.00 45.56 ? 491 ILE   A CG1 1 
ATOM   2649 C  CG2 . ILE   A 1 354 ? -19.952 19.095  4.710   1.00 52.73 ? 491 ILE   A CG2 1 
ATOM   2650 C  CD1 . ILE   A 1 354 ? -21.037 16.075  5.272   1.00 40.65 ? 491 ILE   A CD1 1 
ATOM   2651 N  N   . GLU   A 1 355 ? -19.075 17.986  1.460   1.00 54.74 ? 492 GLU   A N   1 
ATOM   2652 C  CA  . GLU   A 1 355 ? -18.584 18.800  0.359   1.00 59.98 ? 492 GLU   A CA  1 
ATOM   2653 C  C   . GLU   A 1 355 ? -19.021 20.259  0.438   1.00 66.28 ? 492 GLU   A C   1 
ATOM   2654 O  O   . GLU   A 1 355 ? -18.517 21.080  -0.327  1.00 69.42 ? 492 GLU   A O   1 
ATOM   2655 C  CB  . GLU   A 1 355 ? -18.995 18.213  -0.989  1.00 59.72 ? 492 GLU   A CB  1 
ATOM   2656 C  CG  . GLU   A 1 355 ? -17.936 17.281  -1.540  1.00 60.28 ? 492 GLU   A CG  1 
ATOM   2657 C  CD  . GLU   A 1 355 ? -17.728 17.459  -3.026  1.00 64.79 ? 492 GLU   A CD  1 
ATOM   2658 O  OE1 . GLU   A 1 355 ? -18.525 16.920  -3.819  1.00 63.34 ? 492 GLU   A OE1 1 
ATOM   2659 O  OE2 . GLU   A 1 355 ? -16.762 18.166  -3.394  1.00 71.59 ? 492 GLU   A OE2 1 
ATOM   2660 O  OXT . GLU   A 1 355 ? -19.862 20.654  1.243   1.00 71.35 ? 492 GLU   A OXT 1 
HETATM 2661 C  C1  . NAG   B 2 .   ? -26.507 -8.143  -0.663  1.00 39.24 ? 501 NAG   A C1  1 
HETATM 2662 C  C2  . NAG   B 2 .   ? -26.436 -9.407  -1.492  1.00 39.81 ? 501 NAG   A C2  1 
HETATM 2663 C  C3  . NAG   B 2 .   ? -26.147 -9.059  -2.944  1.00 43.02 ? 501 NAG   A C3  1 
HETATM 2664 C  C4  . NAG   B 2 .   ? -27.166 -8.051  -3.463  1.00 44.03 ? 501 NAG   A C4  1 
HETATM 2665 C  C5  . NAG   B 2 .   ? -27.345 -6.867  -2.508  1.00 43.77 ? 501 NAG   A C5  1 
HETATM 2666 C  C6  . NAG   B 2 .   ? -28.563 -6.038  -2.845  1.00 43.17 ? 501 NAG   A C6  1 
HETATM 2667 C  C7  . NAG   B 2 .   ? -25.726 -11.290 -0.095  1.00 39.19 ? 501 NAG   A C7  1 
HETATM 2668 C  C8  . NAG   B 2 .   ? -24.579 -12.145 0.347   1.00 35.83 ? 501 NAG   A C8  1 
HETATM 2669 N  N2  . NAG   B 2 .   ? -25.435 -10.323 -0.971  1.00 39.27 ? 501 NAG   A N2  1 
HETATM 2670 O  O3  . NAG   B 2 .   ? -26.214 -10.246 -3.726  1.00 48.03 ? 501 NAG   A O3  1 
HETATM 2671 O  O4  . NAG   B 2 .   ? -26.734 -7.558  -4.726  1.00 45.89 ? 501 NAG   A O4  1 
HETATM 2672 O  O5  . NAG   B 2 .   ? -27.534 -7.315  -1.156  1.00 39.10 ? 501 NAG   A O5  1 
HETATM 2673 O  O6  . NAG   B 2 .   ? -28.231 -4.913  -3.645  1.00 50.79 ? 501 NAG   A O6  1 
HETATM 2674 O  O7  . NAG   B 2 .   ? -26.867 -11.466 0.322   1.00 43.37 ? 501 NAG   A O7  1 
HETATM 2675 C  C1  . NAG   C 2 .   ? -34.803 4.000   10.374  1.00 52.36 ? 502 NAG   A C1  1 
HETATM 2676 C  C2  . NAG   C 2 .   ? -36.212 3.596   10.881  1.00 57.88 ? 502 NAG   A C2  1 
HETATM 2677 C  C3  . NAG   C 2 .   ? -36.205 3.112   12.353  1.00 58.85 ? 502 NAG   A C3  1 
HETATM 2678 C  C4  . NAG   C 2 .   ? -35.269 3.901   13.269  1.00 57.11 ? 502 NAG   A C4  1 
HETATM 2679 C  C5  . NAG   C 2 .   ? -34.140 4.557   12.495  1.00 54.01 ? 502 NAG   A C5  1 
HETATM 2680 C  C6  . NAG   C 2 .   ? -32.853 4.674   13.278  1.00 52.20 ? 502 NAG   A C6  1 
HETATM 2681 C  C7  . NAG   C 2 .   ? -37.663 5.010   9.501   1.00 65.07 ? 502 NAG   A C7  1 
HETATM 2682 C  C8  . NAG   C 2 .   ? -38.623 6.161   9.485   1.00 67.51 ? 502 NAG   A C8  1 
HETATM 2683 N  N2  . NAG   C 2 .   ? -37.161 4.682   10.697  1.00 61.63 ? 502 NAG   A N2  1 
HETATM 2684 O  O3  . NAG   C 2 .   ? -35.902 1.723   12.407  1.00 64.90 ? 502 NAG   A O3  1 
HETATM 2685 O  O4  . NAG   C 2 .   ? -35.994 4.888   13.993  1.00 58.42 ? 502 NAG   A O4  1 
HETATM 2686 O  O5  . NAG   C 2 .   ? -33.863 3.752   11.351  1.00 52.50 ? 502 NAG   A O5  1 
HETATM 2687 O  O6  . NAG   C 2 .   ? -32.288 5.971   13.143  1.00 53.26 ? 502 NAG   A O6  1 
HETATM 2688 O  O7  . NAG   C 2 .   ? -37.357 4.402   8.479   1.00 64.75 ? 502 NAG   A O7  1 
HETATM 2689 C  C1  . NAG   D 2 .   ? -17.089 -11.088 26.821  1.00 24.08 ? 503 NAG   A C1  1 
HETATM 2690 C  C2  . NAG   D 2 .   ? -15.685 -11.480 27.274  1.00 27.15 ? 503 NAG   A C2  1 
HETATM 2691 C  C3  . NAG   D 2 .   ? -15.725 -11.984 28.717  1.00 27.65 ? 503 NAG   A C3  1 
HETATM 2692 C  C4  . NAG   D 2 .   ? -16.344 -10.923 29.619  1.00 32.75 ? 503 NAG   A C4  1 
HETATM 2693 C  C5  . NAG   D 2 .   ? -17.738 -10.582 29.106  1.00 32.39 ? 503 NAG   A C5  1 
HETATM 2694 C  C6  . NAG   D 2 .   ? -18.415 -9.481  29.891  1.00 32.85 ? 503 NAG   A C6  1 
HETATM 2695 C  C7  . NAG   D 2 .   ? -13.948 -12.303 25.749  1.00 26.26 ? 503 NAG   A C7  1 
HETATM 2696 C  C8  . NAG   D 2 .   ? -13.491 -13.448 24.895  1.00 24.98 ? 503 NAG   A C8  1 
HETATM 2697 N  N2  . NAG   D 2 .   ? -15.103 -12.483 26.397  1.00 23.92 ? 503 NAG   A N2  1 
HETATM 2698 O  O3  . NAG   D 2 .   ? -14.418 -12.326 29.163  1.00 33.14 ? 503 NAG   A O3  1 
HETATM 2699 O  O4  . NAG   D 2 .   ? -16.425 -11.385 30.963  1.00 34.46 ? 503 NAG   A O4  1 
HETATM 2700 O  O5  . NAG   D 2 .   ? -17.648 -10.126 27.749  1.00 26.71 ? 503 NAG   A O5  1 
HETATM 2701 O  O6  . NAG   D 2 .   ? -17.583 -8.337  30.020  1.00 36.32 ? 503 NAG   A O6  1 
HETATM 2702 O  O7  . NAG   D 2 .   ? -13.301 -11.260 25.846  1.00 24.46 ? 503 NAG   A O7  1 
HETATM 2703 C  C1  . NAG   E 2 .   ? -17.913 -13.874 -7.773  1.00 46.81 ? 504 NAG   A C1  1 
HETATM 2704 C  C2  . NAG   E 2 .   ? -17.609 -12.992 -8.993  1.00 49.34 ? 504 NAG   A C2  1 
HETATM 2705 C  C3  . NAG   E 2 .   ? -17.788 -13.783 -10.292 1.00 50.09 ? 504 NAG   A C3  1 
HETATM 2706 C  C4  . NAG   E 2 .   ? -17.034 -15.106 -10.238 1.00 55.18 ? 504 NAG   A C4  1 
HETATM 2707 C  C5  . NAG   E 2 .   ? -17.423 -15.872 -8.982  1.00 52.17 ? 504 NAG   A C5  1 
HETATM 2708 C  C6  . NAG   E 2 .   ? -16.655 -17.162 -8.808  1.00 50.77 ? 504 NAG   A C6  1 
HETATM 2709 C  C7  . NAG   E 2 .   ? -18.018 -10.578 -8.770  1.00 51.57 ? 504 NAG   A C7  1 
HETATM 2710 C  C8  . NAG   E 2 .   ? -19.048 -9.489  -8.818  1.00 48.40 ? 504 NAG   A C8  1 
HETATM 2711 N  N2  . NAG   E 2 .   ? -18.465 -11.817 -8.999  1.00 47.63 ? 504 NAG   A N2  1 
HETATM 2712 O  O3  . NAG   E 2 .   ? -17.311 -13.006 -11.385 1.00 51.90 ? 504 NAG   A O3  1 
HETATM 2713 O  O4  . NAG   E 2 .   ? -17.351 -15.892 -11.381 1.00 56.66 ? 504 NAG   A O4  1 
HETATM 2714 O  O5  . NAG   E 2 .   ? -17.139 -15.064 -7.835  1.00 48.32 ? 504 NAG   A O5  1 
HETATM 2715 O  O6  . NAG   E 2 .   ? -15.317 -16.923 -8.392  1.00 47.41 ? 504 NAG   A O6  1 
HETATM 2716 O  O7  . NAG   E 2 .   ? -16.836 -10.347 -8.537  1.00 51.21 ? 504 NAG   A O7  1 
HETATM 2717 C  C1  . NAG   F 2 .   ? -33.821 -14.896 13.774  1.00 35.47 ? 505 NAG   A C1  1 
HETATM 2718 C  C2  . NAG   F 2 .   ? -35.220 -14.879 14.403  1.00 39.01 ? 505 NAG   A C2  1 
HETATM 2719 C  C3  . NAG   F 2 .   ? -36.033 -16.076 13.923  1.00 40.55 ? 505 NAG   A C3  1 
HETATM 2720 C  C4  . NAG   F 2 .   ? -36.050 -16.137 12.402  1.00 39.17 ? 505 NAG   A C4  1 
HETATM 2721 C  C5  . NAG   F 2 .   ? -34.624 -16.125 11.864  1.00 36.42 ? 505 NAG   A C5  1 
HETATM 2722 C  C6  . NAG   F 2 .   ? -34.563 -16.061 10.356  1.00 39.01 ? 505 NAG   A C6  1 
HETATM 2723 C  C7  . NAG   F 2 .   ? -35.269 -13.766 16.594  1.00 38.55 ? 505 NAG   A C7  1 
HETATM 2724 C  C8  . NAG   F 2 .   ? -35.153 -13.950 18.078  1.00 38.00 ? 505 NAG   A C8  1 
HETATM 2725 N  N2  . NAG   F 2 .   ? -35.137 -14.873 15.855  1.00 39.55 ? 505 NAG   A N2  1 
HETATM 2726 O  O3  . NAG   F 2 .   ? -37.363 -15.973 14.419  1.00 45.58 ? 505 NAG   A O3  1 
HETATM 2727 O  O4  . NAG   F 2 .   ? -36.702 -17.327 11.972  1.00 43.53 ? 505 NAG   A O4  1 
HETATM 2728 O  O5  . NAG   F 2 .   ? -33.932 -14.967 12.350  1.00 34.98 ? 505 NAG   A O5  1 
HETATM 2729 O  O6  . NAG   F 2 .   ? -33.220 -16.047 9.892   1.00 36.97 ? 505 NAG   A O6  1 
HETATM 2730 O  O7  . NAG   F 2 .   ? -35.476 -12.668 16.088  1.00 37.11 ? 505 NAG   A O7  1 
HETATM 2731 C  C1  . NAG   G 2 .   ? -19.558 -21.448 33.889  1.00 46.65 ? 506 NAG   A C1  1 
HETATM 2732 C  C2  . NAG   G 2 .   ? -20.699 -21.159 34.865  1.00 49.69 ? 506 NAG   A C2  1 
HETATM 2733 C  C3  . NAG   G 2 .   ? -20.229 -21.350 36.309  1.00 53.76 ? 506 NAG   A C3  1 
HETATM 2734 C  C4  . NAG   G 2 .   ? -19.533 -22.694 36.491  1.00 57.03 ? 506 NAG   A C4  1 
HETATM 2735 C  C5  . NAG   G 2 .   ? -18.461 -22.896 35.426  1.00 51.55 ? 506 NAG   A C5  1 
HETATM 2736 C  C6  . NAG   G 2 .   ? -17.841 -24.274 35.464  1.00 50.59 ? 506 NAG   A C6  1 
HETATM 2737 C  C7  . NAG   G 2 .   ? -22.360 -19.535 34.056  1.00 46.48 ? 506 NAG   A C7  1 
HETATM 2738 C  C8  . NAG   G 2 .   ? -22.719 -18.083 33.951  1.00 44.44 ? 506 NAG   A C8  1 
HETATM 2739 N  N2  . NAG   G 2 .   ? -21.206 -19.809 34.675  1.00 49.34 ? 506 NAG   A N2  1 
HETATM 2740 O  O3  . NAG   G 2 .   ? -21.356 -21.270 37.175  1.00 56.28 ? 506 NAG   A O3  1 
HETATM 2741 O  O4  . NAG   G 2 .   ? -18.910 -22.744 37.770  1.00 58.06 ? 506 NAG   A O4  1 
HETATM 2742 O  O5  . NAG   G 2 .   ? -19.044 -22.746 34.127  1.00 48.58 ? 506 NAG   A O5  1 
HETATM 2743 O  O6  . NAG   G 2 .   ? -18.743 -25.261 34.983  1.00 53.75 ? 506 NAG   A O6  1 
HETATM 2744 O  O7  . NAG   G 2 .   ? -23.079 -20.419 33.599  1.00 48.79 ? 506 NAG   A O7  1 
HETATM 2745 C  C1  . NAG   H 2 .   ? -30.993 -24.141 27.353  1.00 40.18 ? 507 NAG   A C1  1 
HETATM 2746 C  C2  . NAG   H 2 .   ? -31.584 -23.883 28.752  1.00 45.80 ? 507 NAG   A C2  1 
HETATM 2747 C  C3  . NAG   H 2 .   ? -33.111 -23.994 28.728  1.00 43.73 ? 507 NAG   A C3  1 
HETATM 2748 C  C4  . NAG   H 2 .   ? -33.699 -23.123 27.628  1.00 45.38 ? 507 NAG   A C4  1 
HETATM 2749 C  C5  . NAG   H 2 .   ? -33.072 -23.513 26.300  1.00 45.99 ? 507 NAG   A C5  1 
HETATM 2750 C  C6  . NAG   H 2 .   ? -33.565 -22.682 25.140  1.00 44.37 ? 507 NAG   A C6  1 
HETATM 2751 C  C7  . NAG   H 2 .   ? -30.532 -24.432 30.904  1.00 47.01 ? 507 NAG   A C7  1 
HETATM 2752 C  C8  . NAG   H 2 .   ? -30.005 -25.529 31.780  1.00 50.81 ? 507 NAG   A C8  1 
HETATM 2753 N  N2  . NAG   H 2 .   ? -31.027 -24.812 29.722  1.00 46.90 ? 507 NAG   A N2  1 
HETATM 2754 O  O3  . NAG   H 2 .   ? -33.639 -23.596 29.988  1.00 50.36 ? 507 NAG   A O3  1 
HETATM 2755 O  O4  . NAG   H 2 .   ? -35.110 -23.290 27.554  1.00 49.56 ? 507 NAG   A O4  1 
HETATM 2756 O  O5  . NAG   H 2 .   ? -31.656 -23.314 26.383  1.00 42.26 ? 507 NAG   A O5  1 
HETATM 2757 O  O6  . NAG   H 2 .   ? -33.206 -21.315 25.291  1.00 49.09 ? 507 NAG   A O6  1 
HETATM 2758 O  O7  . NAG   H 2 .   ? -30.510 -23.257 31.249  1.00 48.09 ? 507 NAG   A O7  1 
HETATM 2759 C  C1  . NAG   I 2 .   ? -11.285 -32.261 17.514  1.00 40.95 ? 508 NAG   A C1  1 
HETATM 2760 C  C2  . NAG   I 2 .   ? -9.958  -32.652 16.835  1.00 42.37 ? 508 NAG   A C2  1 
HETATM 2761 C  C3  . NAG   I 2 .   ? -10.151 -33.854 15.908  1.00 46.57 ? 508 NAG   A C3  1 
HETATM 2762 C  C4  . NAG   I 2 .   ? -10.856 -34.991 16.632  1.00 44.36 ? 508 NAG   A C4  1 
HETATM 2763 C  C5  . NAG   I 2 .   ? -12.169 -34.476 17.198  1.00 44.09 ? 508 NAG   A C5  1 
HETATM 2764 C  C6  . NAG   I 2 .   ? -12.956 -35.527 17.945  1.00 44.88 ? 508 NAG   A C6  1 
HETATM 2765 C  C7  . NAG   I 2 .   ? -8.176  -31.062 16.253  1.00 44.03 ? 508 NAG   A C7  1 
HETATM 2766 C  C8  . NAG   I 2 .   ? -7.795  -29.892 15.395  1.00 46.74 ? 508 NAG   A C8  1 
HETATM 2767 N  N2  . NAG   I 2 .   ? -9.418  -31.526 16.089  1.00 44.80 ? 508 NAG   A N2  1 
HETATM 2768 O  O3  . NAG   I 2 .   ? -8.883  -34.292 15.436  1.00 50.49 ? 508 NAG   A O3  1 
HETATM 2769 O  O4  . NAG   I 2 .   ? -11.116 -36.064 15.734  1.00 53.06 ? 508 NAG   A O4  1 
HETATM 2770 O  O5  . NAG   I 2 .   ? -11.883 -33.421 18.124  1.00 42.03 ? 508 NAG   A O5  1 
HETATM 2771 O  O6  . NAG   I 2 .   ? -12.722 -35.456 19.344  1.00 48.58 ? 508 NAG   A O6  1 
HETATM 2772 O  O7  . NAG   I 2 .   ? -7.395  -31.561 17.057  1.00 48.91 ? 508 NAG   A O7  1 
HETATM 2773 C  C1  . NAG   J 2 .   ? -25.040 -11.129 26.042  1.00 50.76 ? 509 NAG   A C1  1 
HETATM 2774 C  C2  . NAG   J 2 .   ? -24.627 -9.698  26.413  1.00 53.34 ? 509 NAG   A C2  1 
HETATM 2775 C  C3  . NAG   J 2 .   ? -25.692 -9.032  27.284  1.00 55.19 ? 509 NAG   A C3  1 
HETATM 2776 C  C4  . NAG   J 2 .   ? -27.062 -9.135  26.630  1.00 57.52 ? 509 NAG   A C4  1 
HETATM 2777 C  C5  . NAG   J 2 .   ? -27.372 -10.596 26.332  1.00 56.39 ? 509 NAG   A C5  1 
HETATM 2778 C  C6  . NAG   J 2 .   ? -28.696 -10.795 25.630  1.00 56.71 ? 509 NAG   A C6  1 
HETATM 2779 C  C7  . NAG   J 2 .   ? -22.206 -9.277  26.518  1.00 46.86 ? 509 NAG   A C7  1 
HETATM 2780 C  C8  . NAG   J 2 .   ? -20.974 -9.358  27.367  1.00 40.07 ? 509 NAG   A C8  1 
HETATM 2781 N  N2  . NAG   J 2 .   ? -23.339 -9.697  27.090  1.00 49.16 ? 509 NAG   A N2  1 
HETATM 2782 O  O3  . NAG   J 2 .   ? -25.351 -7.664  27.474  1.00 57.63 ? 509 NAG   A O3  1 
HETATM 2783 O  O4  . NAG   J 2 .   ? -28.062 -8.600  27.489  1.00 59.85 ? 509 NAG   A O4  1 
HETATM 2784 O  O5  . NAG   J 2 .   ? -26.357 -11.123 25.469  1.00 51.64 ? 509 NAG   A O5  1 
HETATM 2785 O  O6  . NAG   J 2 .   ? -28.529 -11.002 24.234  1.00 53.08 ? 509 NAG   A O6  1 
HETATM 2786 O  O7  . NAG   J 2 .   ? -22.177 -8.848  25.368  1.00 45.31 ? 509 NAG   A O7  1 
HETATM 2787 N  N1  . EPE   K 3 .   ? -4.611  7.065   17.139  1.00 34.95 ? 510 EPE   A N1  1 
HETATM 2788 C  C2  . EPE   K 3 .   ? -4.211  6.570   15.811  1.00 32.80 ? 510 EPE   A C2  1 
HETATM 2789 C  C3  . EPE   K 3 .   ? -5.440  6.420   14.918  1.00 35.01 ? 510 EPE   A C3  1 
HETATM 2790 N  N4  . EPE   K 3 .   ? -6.598  5.843   15.585  1.00 34.10 ? 510 EPE   A N4  1 
HETATM 2791 C  C5  . EPE   K 3 .   ? -6.784  6.059   17.006  1.00 31.38 ? 510 EPE   A C5  1 
HETATM 2792 C  C6  . EPE   K 3 .   ? -5.477  6.070   17.771  1.00 31.90 ? 510 EPE   A C6  1 
HETATM 2793 C  C7  . EPE   K 3 .   ? -7.813  5.646   14.810  1.00 28.88 ? 510 EPE   A C7  1 
HETATM 2794 C  C8  . EPE   K 3 .   ? -7.634  4.705   13.625  1.00 33.15 ? 510 EPE   A C8  1 
HETATM 2795 O  O8  . EPE   K 3 .   ? -7.056  5.400   12.538  1.00 33.48 ? 510 EPE   A O8  1 
HETATM 2796 C  C9  . EPE   K 3 .   ? -3.419  7.230   17.977  1.00 34.00 ? 510 EPE   A C9  1 
HETATM 2797 C  C10 . EPE   K 3 .   ? -3.547  8.504   18.802  1.00 34.84 ? 510 EPE   A C10 1 
HETATM 2798 S  S   . EPE   K 3 .   ? -1.930  8.980   19.450  1.00 35.40 ? 510 EPE   A S   1 
HETATM 2799 O  O1S . EPE   K 3 .   ? -1.282  7.800   20.023  1.00 36.66 ? 510 EPE   A O1S 1 
HETATM 2800 O  O2S . EPE   K 3 .   ? -1.136  9.473   18.335  1.00 36.58 ? 510 EPE   A O2S 1 
HETATM 2801 O  O3S . EPE   K 3 .   ? -2.089  10.013  20.462  1.00 34.59 ? 510 EPE   A O3S 1 
HETATM 2802 C  C10 . A1ATA L 4 .   ? -4.464  -16.211 13.619  1.00 32.14 ? 511 A1ATA A C10 1 
HETATM 2803 C  CG  . A1ATA L 4 .   ? -3.304  -10.673 6.380   1.00 51.68 ? 511 A1ATA A CG  1 
HETATM 2804 N  ND1 . A1ATA L 4 .   ? -3.005  -9.123  5.811   1.00 55.29 ? 511 A1ATA A ND1 1 
HETATM 2805 C  CD2 . A1ATA L 4 .   ? -3.449  -11.510 5.377   1.00 54.99 ? 511 A1ATA A CD2 1 
HETATM 2806 C  CE1 . A1ATA L 4 .   ? -3.708  -10.584 4.137   1.00 56.78 ? 511 A1ATA A CE1 1 
HETATM 2807 C  CE2 . A1ATA L 4 .   ? -2.984  -9.205  4.512   1.00 56.43 ? 511 A1ATA A CE2 1 
HETATM 2808 C  CZ  . A1ATA L 4 .   ? -2.812  -7.894  6.627   1.00 55.14 ? 511 A1ATA A CZ  1 
HETATM 2809 N  NH1 . A1ATA L 4 .   ? -2.858  -7.918  7.889   1.00 51.16 ? 511 A1ATA A NH1 1 
HETATM 2810 N  NH2 . A1ATA L 4 .   ? -2.612  -6.818  6.037   1.00 58.27 ? 511 A1ATA A NH2 1 
HETATM 2811 C  C01 . A1ATA L 4 .   ? -2.058  -11.115 7.065   1.00 54.84 ? 511 A1ATA A C01 1 
HETATM 2812 C  C03 . A1ATA L 4 .   ? -0.692  -12.379 8.657   1.00 50.64 ? 511 A1ATA A C03 1 
HETATM 2813 C  C04 . A1ATA L 4 .   ? -0.696  -12.773 10.120  1.00 45.70 ? 511 A1ATA A C04 1 
HETATM 2814 C  C06 . A1ATA L 4 .   ? -1.358  -15.213 10.420  1.00 44.46 ? 511 A1ATA A C06 1 
HETATM 2815 C  C08 . A1ATA L 4 .   ? -3.855  -16.389 10.866  1.00 42.23 ? 511 A1ATA A C08 1 
HETATM 2816 C  C09 . A1ATA L 4 .   ? -3.568  -16.395 12.386  1.00 36.20 ? 511 A1ATA A C09 1 
HETATM 2817 C  C13 . A1ATA L 4 .   ? -4.437  -15.856 16.257  1.00 26.60 ? 511 A1ATA A C13 1 
HETATM 2818 C  C14 . A1ATA L 4 .   ? -5.823  -15.822 16.317  1.00 29.33 ? 511 A1ATA A C14 1 
HETATM 2819 C  C15 . A1ATA L 4 .   ? -6.455  -15.651 17.533  1.00 26.54 ? 511 A1ATA A C15 1 
HETATM 2820 C  C17 . A1ATA L 4 .   ? -5.714  -15.508 18.684  1.00 31.35 ? 511 A1ATA A C17 1 
HETATM 2821 C  C19 . A1ATA L 4 .   ? -4.320  -15.543 18.629  1.00 29.73 ? 511 A1ATA A C19 1 
HETATM 2822 C  C20 . A1ATA L 4 .   ? -3.691  -15.719 17.416  1.00 30.24 ? 511 A1ATA A C20 1 
HETATM 2823 C  C21 . A1ATA L 4 .   ? -2.931  -17.737 12.850  1.00 38.78 ? 511 A1ATA A C21 1 
HETATM 2824 C  C22 . A1ATA L 4 .   ? -1.656  -18.176 12.193  1.00 37.03 ? 511 A1ATA A C22 1 
HETATM 2825 C  C23 . A1ATA L 4 .   ? -1.755  -17.756 10.723  1.00 43.64 ? 511 A1ATA A C23 1 
HETATM 2826 C  C25 . A1ATA L 4 .   ? -3.000  -13.118 10.380  1.00 47.35 ? 511 A1ATA A C25 1 
HETATM 2827 C  C26 . A1ATA L 4 .   ? -3.184  -12.713 8.857   1.00 46.34 ? 511 A1ATA A C26 1 
HETATM 2828 F  F16 . A1ATA L 4 .   ? -7.801  -15.617 17.585  1.00 29.12 ? 511 A1ATA A F16 1 
HETATM 2829 N  N02 . A1ATA L 4 .   ? -2.036  -12.076 8.174   1.00 50.51 ? 511 A1ATA A N02 1 
HETATM 2830 N  N05 . A1ATA L 4 .   ? -1.717  -13.773 10.350  1.00 45.10 ? 511 A1ATA A N05 1 
HETATM 2831 N  N07 . A1ATA L 4 .   ? -2.324  -16.357 10.607  1.00 45.53 ? 511 A1ATA A N07 1 
HETATM 2832 N  N12 . A1ATA L 4 .   ? -3.754  -16.041 14.971  1.00 30.72 ? 511 A1ATA A N12 1 
HETATM 2833 O  O11 . A1ATA L 4 .   ? -5.603  -16.213 13.491  1.00 34.53 ? 511 A1ATA A O11 1 
HETATM 2834 O  O24 . A1ATA L 4 .   ? -0.187  -15.484 10.305  1.00 47.96 ? 511 A1ATA A O24 1 
HETATM 2835 O  O27 . A1ATA L 4 .   ? -1.029  -10.706 6.655   1.00 55.52 ? 511 A1ATA A O27 1 
HETATM 2836 CL CL1 . A1ATA L 4 .   ? -6.545  -15.280 20.260  1.00 51.93 ? 511 A1ATA A CL1 1 
HETATM 2837 O  O   . HOH   M 5 .   ? -21.058 5.736   -2.625  1.00 52.02 ? 601 HOH   A O   1 
HETATM 2838 O  O   . HOH   M 5 .   ? -12.837 -10.789 28.796  1.00 38.04 ? 602 HOH   A O   1 
HETATM 2839 O  O   . HOH   M 5 .   ? -15.807 18.968  4.286   1.00 48.72 ? 603 HOH   A O   1 
HETATM 2840 O  O   . HOH   M 5 .   ? -5.201  -31.162 17.368  1.00 52.27 ? 604 HOH   A O   1 
HETATM 2841 O  O   . HOH   M 5 .   ? -32.161 8.216   12.623  1.00 46.80 ? 605 HOH   A O   1 
HETATM 2842 O  O   . HOH   M 5 .   ? -21.521 -31.868 28.190  1.00 41.12 ? 606 HOH   A O   1 
HETATM 2843 O  O   . HOH   M 5 .   ? -4.582  4.093   11.598  1.00 40.95 ? 607 HOH   A O   1 
HETATM 2844 O  O   . HOH   M 5 .   ? -2.259  -11.844 32.897  1.00 50.98 ? 608 HOH   A O   1 
HETATM 2845 O  O   . HOH   M 5 .   ? -31.831 -17.120 16.238  1.00 31.60 ? 609 HOH   A O   1 
HETATM 2846 O  O   . HOH   M 5 .   ? -18.822 -29.584 31.323  1.00 45.88 ? 610 HOH   A O   1 
HETATM 2847 O  O   . HOH   M 5 .   ? -1.167  -12.591 18.379  1.00 35.27 ? 611 HOH   A O   1 
HETATM 2848 O  O   . HOH   M 5 .   ? -11.333 -13.124 5.015   1.00 39.47 ? 612 HOH   A O   1 
HETATM 2849 O  O   . HOH   M 5 .   ? -18.603 22.064  2.769   1.00 53.81 ? 613 HOH   A O   1 
HETATM 2850 O  O   . HOH   M 5 .   ? -19.723 -26.583 -0.842  1.00 48.26 ? 614 HOH   A O   1 
HETATM 2851 O  O   . HOH   M 5 .   ? -3.113  -21.403 9.363   1.00 47.20 ? 615 HOH   A O   1 
HETATM 2852 O  O   . HOH   M 5 .   ? -10.742 -13.157 22.440  1.00 28.79 ? 616 HOH   A O   1 
HETATM 2853 O  O   . HOH   M 5 .   ? -15.870 -23.616 -9.981  1.00 63.14 ? 617 HOH   A O   1 
HETATM 2854 O  O   . HOH   M 5 .   ? -13.224 5.349   4.813   1.00 36.65 ? 618 HOH   A O   1 
HETATM 2855 O  O   . HOH   M 5 .   ? -25.940 -29.373 8.889   1.00 47.39 ? 619 HOH   A O   1 
HETATM 2856 O  O   . HOH   M 5 .   ? -22.606 -9.447  22.962  1.00 31.74 ? 620 HOH   A O   1 
HETATM 2857 O  O   . HOH   M 5 .   ? -16.929 -13.620 32.016  1.00 31.66 ? 621 HOH   A O   1 
HETATM 2858 O  O   . HOH   M 5 .   ? -27.791 -5.746  8.945   1.00 32.17 ? 622 HOH   A O   1 
HETATM 2859 O  O   . HOH   M 5 .   ? -24.738 -4.010  14.664  1.00 39.18 ? 623 HOH   A O   1 
HETATM 2860 O  O   . HOH   M 5 .   ? -9.704  -29.489 11.690  1.00 40.65 ? 624 HOH   A O   1 
HETATM 2861 O  O   . HOH   M 5 .   ? -27.083 -4.621  15.281  1.00 40.04 ? 625 HOH   A O   1 
HETATM 2862 O  O   . HOH   M 5 .   ? -28.398 0.440   12.312  1.00 43.94 ? 626 HOH   A O   1 
HETATM 2863 O  O   . HOH   M 5 .   ? -0.567  1.597   25.867  1.00 39.45 ? 627 HOH   A O   1 
HETATM 2864 O  O   . HOH   M 5 .   ? -24.051 14.352  12.107  1.00 41.17 ? 628 HOH   A O   1 
HETATM 2865 O  O   . HOH   M 5 .   ? -31.898 -9.555  17.434  1.00 36.36 ? 629 HOH   A O   1 
HETATM 2866 O  O   . HOH   M 5 .   ? -34.287 -34.978 24.368  1.00 52.66 ? 630 HOH   A O   1 
HETATM 2867 O  O   . HOH   M 5 .   ? -12.795 -25.541 -1.277  1.00 49.65 ? 631 HOH   A O   1 
HETATM 2868 O  O   . HOH   M 5 .   ? 2.553   -9.852  27.999  1.00 52.56 ? 632 HOH   A O   1 
HETATM 2869 O  O   . HOH   M 5 .   ? -19.460 -0.243  5.676   1.00 27.56 ? 633 HOH   A O   1 
HETATM 2870 O  O   . HOH   M 5 .   ? -33.296 -18.602 9.393   1.00 39.47 ? 634 HOH   A O   1 
HETATM 2871 O  O   . HOH   M 5 .   ? -19.029 -9.184  15.958  1.00 25.20 ? 635 HOH   A O   1 
HETATM 2872 O  O   . HOH   M 5 .   ? -35.015 7.129   4.564   1.00 42.11 ? 636 HOH   A O   1 
HETATM 2873 O  O   . HOH   M 5 .   ? -28.342 -1.863  9.272   1.00 32.58 ? 637 HOH   A O   1 
HETATM 2874 O  O   . HOH   M 5 .   ? -0.620  -0.575  14.165  1.00 32.35 ? 638 HOH   A O   1 
HETATM 2875 O  O   . HOH   M 5 .   ? -10.726 7.152   26.066  1.00 32.63 ? 639 HOH   A O   1 
HETATM 2876 O  O   . HOH   M 5 .   ? -12.920 -29.525 14.514  1.00 34.48 ? 640 HOH   A O   1 
HETATM 2877 O  O   . HOH   M 5 .   ? -10.263 17.650  9.287   1.00 40.53 ? 641 HOH   A O   1 
HETATM 2878 O  O   . HOH   M 5 .   ? -10.637 -11.604 29.377  1.00 36.46 ? 642 HOH   A O   1 
HETATM 2879 O  O   . HOH   M 5 .   ? -0.438  -19.238 29.308  1.00 37.45 ? 643 HOH   A O   1 
HETATM 2880 O  O   . HOH   M 5 .   ? 2.127   -22.854 18.557  1.00 39.83 ? 644 HOH   A O   1 
HETATM 2881 O  O   . HOH   M 5 .   ? -31.326 -12.601 5.981   1.00 34.93 ? 645 HOH   A O   1 
HETATM 2882 O  O   . HOH   M 5 .   ? -10.793 -14.502 12.857  1.00 30.13 ? 646 HOH   A O   1 
HETATM 2883 O  O   . HOH   M 5 .   ? -29.661 -3.408  -5.280  1.00 43.39 ? 647 HOH   A O   1 
HETATM 2884 O  O   . HOH   M 5 .   ? -16.361 8.709   29.288  1.00 37.78 ? 648 HOH   A O   1 
HETATM 2885 O  O   . HOH   M 5 .   ? -13.610 7.484   32.358  1.00 43.76 ? 649 HOH   A O   1 
HETATM 2886 O  O   . HOH   M 5 .   ? -5.384  -11.160 11.494  1.00 28.57 ? 650 HOH   A O   1 
HETATM 2887 O  O   . HOH   M 5 .   ? -6.930  -27.938 34.071  1.00 39.93 ? 651 HOH   A O   1 
HETATM 2888 O  O   . HOH   M 5 .   ? -22.269 -10.116 -1.759  1.00 39.49 ? 652 HOH   A O   1 
HETATM 2889 O  O   . HOH   M 5 .   ? -6.874  10.912  14.470  1.00 40.99 ? 653 HOH   A O   1 
HETATM 2890 O  O   . HOH   M 5 .   ? -33.141 -21.037 30.521  1.00 46.46 ? 654 HOH   A O   1 
HETATM 2891 O  O   . HOH   M 5 .   ? -11.975 -6.964  2.056   1.00 41.84 ? 655 HOH   A O   1 
HETATM 2892 O  O   . HOH   M 5 .   ? -25.081 -21.565 26.104  1.00 28.38 ? 656 HOH   A O   1 
HETATM 2893 O  O   . HOH   M 5 .   ? 7.359   -14.058 31.872  1.00 50.22 ? 657 HOH   A O   1 
HETATM 2894 O  O   . HOH   M 5 .   ? -4.773  -2.132  8.354   1.00 37.64 ? 658 HOH   A O   1 
HETATM 2895 O  O   . HOH   M 5 .   ? -32.714 -35.952 20.055  1.00 49.73 ? 659 HOH   A O   1 
HETATM 2896 O  O   . HOH   M 5 .   ? -18.267 -16.282 -0.104  1.00 32.68 ? 660 HOH   A O   1 
HETATM 2897 O  O   . HOH   M 5 .   ? -14.641 -9.368  17.390  1.00 30.57 ? 661 HOH   A O   1 
HETATM 2898 O  O   . HOH   M 5 .   ? -20.290 -32.311 25.123  1.00 39.22 ? 662 HOH   A O   1 
HETATM 2899 O  O   . HOH   M 5 .   ? -10.913 -11.188 24.612  1.00 28.91 ? 663 HOH   A O   1 
HETATM 2900 O  O   . HOH   M 5 .   ? -5.098  -9.942  9.052   1.00 38.17 ? 664 HOH   A O   1 
HETATM 2901 O  O   . HOH   M 5 .   ? -11.693 -27.559 16.297  1.00 34.19 ? 665 HOH   A O   1 
HETATM 2902 O  O   . HOH   M 5 .   ? -31.456 -8.608  10.967  1.00 29.75 ? 666 HOH   A O   1 
HETATM 2903 O  O   . HOH   M 5 .   ? -34.811 -3.640  16.615  1.00 41.26 ? 667 HOH   A O   1 
HETATM 2904 O  O   . HOH   M 5 .   ? -23.192 6.399   17.267  1.00 36.64 ? 668 HOH   A O   1 
HETATM 2905 O  O   . HOH   M 5 .   ? -17.942 9.214   21.501  1.00 33.94 ? 669 HOH   A O   1 
HETATM 2906 O  O   . HOH   M 5 .   ? -14.960 -7.427  27.545  1.00 28.94 ? 670 HOH   A O   1 
HETATM 2907 O  O   . HOH   M 5 .   ? -1.129  -1.819  32.625  1.00 43.34 ? 671 HOH   A O   1 
HETATM 2908 O  O   . HOH   M 5 .   ? 1.586   -15.783 12.663  1.00 40.46 ? 672 HOH   A O   1 
HETATM 2909 O  O   . HOH   M 5 .   ? -15.247 -9.487  32.506  1.00 43.00 ? 673 HOH   A O   1 
HETATM 2910 O  O   . HOH   M 5 .   ? -32.500 7.621   4.543   1.00 38.76 ? 674 HOH   A O   1 
HETATM 2911 O  O   . HOH   M 5 .   ? -14.836 -12.139 18.406  1.00 24.26 ? 675 HOH   A O   1 
HETATM 2912 O  O   . HOH   M 5 .   ? -17.474 14.591  12.430  1.00 40.24 ? 676 HOH   A O   1 
HETATM 2913 O  O   . HOH   M 5 .   ? -16.231 -12.038 1.967   1.00 28.10 ? 677 HOH   A O   1 
HETATM 2914 O  O   . HOH   M 5 .   ? -16.694 13.316  15.424  1.00 34.93 ? 678 HOH   A O   1 
HETATM 2915 O  O   . HOH   M 5 .   ? -3.203  -13.816 32.304  1.00 35.92 ? 679 HOH   A O   1 
HETATM 2916 O  O   . HOH   M 5 .   ? -29.766 -5.782  11.572  1.00 37.76 ? 680 HOH   A O   1 
HETATM 2917 O  O   . HOH   M 5 .   ? -8.051  -30.362 26.149  1.00 42.20 ? 681 HOH   A O   1 
HETATM 2918 O  O   . HOH   M 5 .   ? -17.086 -9.205  18.246  1.00 22.34 ? 682 HOH   A O   1 
HETATM 2919 O  O   . HOH   M 5 .   ? -20.890 -3.805  19.033  1.00 33.75 ? 683 HOH   A O   1 
HETATM 2920 O  O   . HOH   M 5 .   ? -23.852 -11.234 29.314  1.00 53.87 ? 684 HOH   A O   1 
HETATM 2921 O  O   . HOH   M 5 .   ? -16.532 6.347   1.651   1.00 40.70 ? 685 HOH   A O   1 
HETATM 2922 O  O   . HOH   M 5 .   ? -8.248  10.021  27.418  1.00 37.91 ? 686 HOH   A O   1 
HETATM 2923 O  O   . HOH   M 5 .   ? -13.046 3.238   2.342   1.00 30.91 ? 687 HOH   A O   1 
HETATM 2924 O  O   . HOH   M 5 .   ? -21.364 -10.442 15.690  1.00 25.53 ? 688 HOH   A O   1 
HETATM 2925 O  O   . HOH   M 5 .   ? -16.892 -19.168 1.352   1.00 37.78 ? 689 HOH   A O   1 
HETATM 2926 O  O   . HOH   M 5 .   ? -16.993 -23.841 31.793  1.00 36.85 ? 690 HOH   A O   1 
HETATM 2927 O  O   . HOH   M 5 .   ? -32.376 -11.832 20.416  1.00 43.79 ? 691 HOH   A O   1 
HETATM 2928 O  O   . HOH   M 5 .   ? -21.927 -8.887  10.934  1.00 22.09 ? 692 HOH   A O   1 
HETATM 2929 O  O   . HOH   M 5 .   ? -1.353  -18.155 26.943  1.00 33.39 ? 693 HOH   A O   1 
HETATM 2930 O  O   . HOH   M 5 .   ? -21.903 -8.620  2.486   1.00 30.79 ? 694 HOH   A O   1 
HETATM 2931 O  O   . HOH   M 5 .   ? -27.557 -14.355 -2.316  1.00 43.95 ? 695 HOH   A O   1 
HETATM 2932 O  O   . HOH   M 5 .   ? -10.040 12.785  2.350   1.00 43.65 ? 696 HOH   A O   1 
HETATM 2933 O  O   . HOH   M 5 .   ? -14.871 -8.854  25.252  1.00 24.31 ? 697 HOH   A O   1 
HETATM 2934 O  O   . HOH   M 5 .   ? -19.362 1.158   3.173   1.00 33.51 ? 698 HOH   A O   1 
HETATM 2935 O  O   . HOH   M 5 .   ? -8.287  -7.111  22.279  1.00 28.54 ? 699 HOH   A O   1 
HETATM 2936 O  O   . HOH   M 5 .   ? -19.223 -17.936 35.272  1.00 47.77 ? 700 HOH   A O   1 
HETATM 2937 O  O   . HOH   M 5 .   ? -2.176  -4.905  33.229  1.00 34.22 ? 701 HOH   A O   1 
HETATM 2938 O  O   . HOH   M 5 .   ? -17.173 -6.522  18.773  1.00 26.64 ? 702 HOH   A O   1 
HETATM 2939 O  O   . HOH   M 5 .   ? -27.702 -11.272 3.157   1.00 35.18 ? 703 HOH   A O   1 
HETATM 2940 O  O   . HOH   M 5 .   ? -0.180  -22.913 17.055  1.00 35.36 ? 704 HOH   A O   1 
HETATM 2941 O  O   . HOH   M 5 .   ? -21.992 -23.254 31.982  1.00 44.43 ? 705 HOH   A O   1 
HETATM 2942 O  O   . HOH   M 5 .   ? -14.735 -27.676 13.887  1.00 33.21 ? 706 HOH   A O   1 
HETATM 2943 O  O   . HOH   M 5 .   ? -33.958 -6.443  17.415  1.00 42.57 ? 707 HOH   A O   1 
HETATM 2944 O  O   . HOH   M 5 .   ? -28.990 -13.262 4.591   1.00 35.94 ? 708 HOH   A O   1 
HETATM 2945 O  O   . HOH   M 5 .   ? -0.639  -15.299 27.250  1.00 40.85 ? 709 HOH   A O   1 
HETATM 2946 O  O   . HOH   M 5 .   ? -7.805  8.892   18.885  1.00 27.03 ? 710 HOH   A O   1 
HETATM 2947 O  O   . HOH   M 5 .   ? -20.593 -1.284  23.469  1.00 37.73 ? 711 HOH   A O   1 
HETATM 2948 O  O   . HOH   M 5 .   ? -15.716 -17.491 26.286  1.00 26.52 ? 712 HOH   A O   1 
HETATM 2949 O  O   . HOH   M 5 .   ? -36.762 9.265   4.893   1.00 51.31 ? 713 HOH   A O   1 
HETATM 2950 O  O   . HOH   M 5 .   ? -10.438 -1.408  2.749   1.00 44.23 ? 714 HOH   A O   1 
HETATM 2951 O  O   . HOH   M 5 .   ? -15.543 4.466   5.231   1.00 29.86 ? 715 HOH   A O   1 
HETATM 2952 O  O   . HOH   M 5 .   ? -18.860 -19.124 -0.332  1.00 40.07 ? 716 HOH   A O   1 
HETATM 2953 O  O   . HOH   M 5 .   ? -22.570 -3.019  14.529  1.00 32.26 ? 717 HOH   A O   1 
HETATM 2954 O  O   . HOH   M 5 .   ? -10.963 -14.209 8.622   1.00 37.83 ? 718 HOH   A O   1 
HETATM 2955 O  O   . HOH   M 5 .   ? -15.600 2.461   26.475  1.00 33.11 ? 719 HOH   A O   1 
HETATM 2956 O  O   . HOH   M 5 .   ? -9.047  -3.844  -0.149  1.00 52.07 ? 720 HOH   A O   1 
HETATM 2957 O  O   . HOH   M 5 .   ? -19.828 -35.585 21.546  1.00 49.16 ? 721 HOH   A O   1 
HETATM 2958 O  O   . HOH   M 5 .   ? -23.942 6.523   -2.328  1.00 50.06 ? 722 HOH   A O   1 
HETATM 2959 O  O   . HOH   M 5 .   ? -15.809 -30.531 20.036  1.00 33.07 ? 723 HOH   A O   1 
HETATM 2960 O  O   . HOH   M 5 .   ? -30.652 -9.548  3.722   1.00 43.04 ? 724 HOH   A O   1 
HETATM 2961 O  O   . HOH   M 5 .   ? -12.100 -3.108  4.053   1.00 34.53 ? 725 HOH   A O   1 
HETATM 2962 O  O   . HOH   M 5 .   ? -1.046  -26.377 25.608  1.00 36.86 ? 726 HOH   A O   1 
HETATM 2963 O  O   . HOH   M 5 .   ? -22.924 10.659  17.106  1.00 33.58 ? 727 HOH   A O   1 
HETATM 2964 O  O   . HOH   M 5 .   ? -35.609 1.451   15.233  1.00 51.44 ? 728 HOH   A O   1 
HETATM 2965 O  O   . HOH   M 5 .   ? -18.368 3.200   25.581  1.00 37.97 ? 729 HOH   A O   1 
HETATM 2966 O  O   . HOH   M 5 .   ? -14.345 -24.367 2.995   1.00 41.41 ? 730 HOH   A O   1 
HETATM 2967 O  O   . HOH   M 5 .   ? -22.041 2.217   22.348  1.00 33.16 ? 731 HOH   A O   1 
HETATM 2968 O  O   . HOH   M 5 .   ? -5.917  3.212   32.443  1.00 36.28 ? 732 HOH   A O   1 
HETATM 2969 O  O   . HOH   M 5 .   ? -21.969 -11.965 -6.020  1.00 47.34 ? 733 HOH   A O   1 
HETATM 2970 O  O   . HOH   M 5 .   ? -10.790 -14.808 -4.927  1.00 48.17 ? 734 HOH   A O   1 
HETATM 2971 O  O   . HOH   M 5 .   ? -0.360  -24.545 14.499  1.00 39.50 ? 735 HOH   A O   1 
HETATM 2972 O  O   . HOH   M 5 .   ? -17.263 1.583   2.060   1.00 38.97 ? 736 HOH   A O   1 
HETATM 2973 O  O   . HOH   M 5 .   ? -35.254 -1.720  8.144   1.00 42.38 ? 737 HOH   A O   1 
HETATM 2974 O  O   . HOH   M 5 .   ? -17.281 -2.351  6.966   1.00 36.45 ? 738 HOH   A O   1 
HETATM 2975 O  O   . HOH   M 5 .   ? -6.232  -10.647 33.256  1.00 41.75 ? 739 HOH   A O   1 
HETATM 2976 O  O   . HOH   M 5 .   ? -11.787 6.915   6.443   1.00 37.15 ? 740 HOH   A O   1 
HETATM 2977 O  O   . HOH   M 5 .   ? -18.648 -5.021  20.451  1.00 26.94 ? 741 HOH   A O   1 
HETATM 2978 O  O   . HOH   M 5 .   ? -34.275 -24.056 14.806  1.00 39.00 ? 742 HOH   A O   1 
HETATM 2979 O  O   . HOH   M 5 .   ? -22.715 -12.260 -2.987  1.00 41.38 ? 743 HOH   A O   1 
HETATM 2980 O  O   . HOH   M 5 .   ? -25.062 13.840  14.045  1.00 39.83 ? 744 HOH   A O   1 
HETATM 2981 O  O   . HOH   M 5 .   ? -7.511  12.884  4.712   1.00 44.58 ? 745 HOH   A O   1 
HETATM 2982 O  O   . HOH   M 5 .   ? -1.881  -0.990  27.317  1.00 37.61 ? 746 HOH   A O   1 
HETATM 2983 O  O   . HOH   M 5 .   ? -25.463 -13.064 -3.574  1.00 47.74 ? 747 HOH   A O   1 
HETATM 2984 O  O   . HOH   M 5 .   ? -15.822 -14.508 34.521  1.00 46.12 ? 748 HOH   A O   1 
HETATM 2985 O  O   . HOH   M 5 .   ? -30.317 -2.380  2.693   1.00 40.91 ? 749 HOH   A O   1 
HETATM 2986 O  O   . HOH   M 5 .   ? -24.070 4.403   16.192  1.00 38.62 ? 750 HOH   A O   1 
HETATM 2987 O  O   . HOH   M 5 .   ? -30.497 9.633   -2.270  1.00 46.20 ? 751 HOH   A O   1 
HETATM 2988 O  O   . HOH   M 5 .   ? -17.569 10.893  28.659  1.00 42.64 ? 752 HOH   A O   1 
HETATM 2989 O  O   . HOH   M 5 .   ? -23.663 -13.324 28.589  1.00 49.30 ? 753 HOH   A O   1 
HETATM 2990 O  O   . HOH   M 5 .   ? -29.179 -16.510 16.336  1.00 32.19 ? 754 HOH   A O   1 
HETATM 2991 O  O   . HOH   M 5 .   ? -16.893 -23.337 -6.473  1.00 60.10 ? 755 HOH   A O   1 
HETATM 2992 O  O   . HOH   M 5 .   ? -35.086 -21.794 4.436   1.00 45.89 ? 756 HOH   A O   1 
HETATM 2993 O  O   . HOH   M 5 .   ? -27.098 -6.460  19.923  1.00 30.17 ? 757 HOH   A O   1 
HETATM 2994 O  O   . HOH   M 5 .   ? -33.512 -8.893  8.649   1.00 36.29 ? 758 HOH   A O   1 
HETATM 2995 O  O   . HOH   M 5 .   ? -32.212 7.269   10.313  1.00 44.28 ? 759 HOH   A O   1 
HETATM 2996 O  O   . HOH   M 5 .   ? -8.647  0.773   2.680   1.00 43.58 ? 760 HOH   A O   1 
HETATM 2997 O  O   . HOH   M 5 .   ? -10.790 -25.212 6.183   1.00 47.45 ? 761 HOH   A O   1 
HETATM 2998 O  O   . HOH   M 5 .   ? -28.969 -5.640  1.921   1.00 36.20 ? 762 HOH   A O   1 
HETATM 2999 O  O   . HOH   M 5 .   ? -22.084 6.112   19.834  1.00 35.33 ? 763 HOH   A O   1 
HETATM 3000 O  O   . HOH   M 5 .   ? -28.631 -8.595  -6.784  1.00 49.85 ? 764 HOH   A O   1 
HETATM 3001 O  O   . HOH   M 5 .   ? -27.416 -16.330 -3.815  1.00 47.83 ? 765 HOH   A O   1 
HETATM 3002 O  O   . HOH   M 5 .   ? -9.415  -9.886  22.480  1.00 23.72 ? 766 HOH   A O   1 
HETATM 3003 O  O   . HOH   M 5 .   ? -22.775 -35.769 17.729  1.00 53.79 ? 767 HOH   A O   1 
HETATM 3004 O  O   . HOH   M 5 .   ? -15.144 14.190  24.417  1.00 42.67 ? 768 HOH   A O   1 
HETATM 3005 O  O   . HOH   M 5 .   ? -12.447 -13.199 2.628   1.00 35.40 ? 769 HOH   A O   1 
HETATM 3006 O  O   . HOH   M 5 .   ? -16.532 -5.471  -3.124  1.00 40.41 ? 770 HOH   A O   1 
HETATM 3007 O  O   . HOH   M 5 .   ? -30.239 -12.657 22.356  1.00 33.11 ? 771 HOH   A O   1 
HETATM 3008 O  O   . HOH   M 5 .   ? -2.819  5.793   30.046  1.00 36.29 ? 772 HOH   A O   1 
HETATM 3009 O  O   . HOH   M 5 .   ? -12.882 -6.655  34.318  1.00 53.55 ? 773 HOH   A O   1 
HETATM 3010 O  O   . HOH   M 5 .   ? -15.196 -18.669 23.847  1.00 27.91 ? 774 HOH   A O   1 
HETATM 3011 O  O   . HOH   M 5 .   ? -35.058 -33.326 25.674  1.00 58.23 ? 775 HOH   A O   1 
HETATM 3012 O  O   . HOH   M 5 .   ? -22.617 -32.463 19.808  1.00 42.62 ? 776 HOH   A O   1 
HETATM 3013 O  O   . HOH   M 5 .   ? -14.740 -12.302 -6.039  1.00 35.96 ? 777 HOH   A O   1 
HETATM 3014 O  O   . HOH   M 5 .   ? -8.834  -31.617 20.607  1.00 42.47 ? 778 HOH   A O   1 
HETATM 3015 O  O   . HOH   M 5 .   ? -4.062  5.186   32.652  1.00 40.16 ? 779 HOH   A O   1 
HETATM 3016 O  O   . HOH   M 5 .   ? 0.599   -29.034 34.241  1.00 48.37 ? 780 HOH   A O   1 
HETATM 3017 O  O   . HOH   M 5 .   ? -1.586  -22.743 36.471  1.00 44.27 ? 781 HOH   A O   1 
HETATM 3018 O  O   . HOH   M 5 .   ? -29.720 -5.808  17.954  1.00 36.53 ? 782 HOH   A O   1 
HETATM 3019 O  O   . HOH   M 5 .   ? -8.465  -29.379 22.558  1.00 40.44 ? 783 HOH   A O   1 
HETATM 3020 O  O   . HOH   M 5 .   ? -5.864  9.962   17.008  1.00 35.32 ? 784 HOH   A O   1 
HETATM 3021 O  O   . HOH   M 5 .   ? -35.935 -18.234 17.824  1.00 49.06 ? 785 HOH   A O   1 
HETATM 3022 O  O   . HOH   M 5 .   ? -20.920 10.798  19.059  1.00 34.03 ? 786 HOH   A O   1 
HETATM 3023 O  O   . HOH   M 5 .   ? -21.565 -11.600 -9.643  1.00 50.15 ? 787 HOH   A O   1 
HETATM 3024 O  O   . HOH   M 5 .   ? -11.562 8.065   28.802  1.00 38.17 ? 788 HOH   A O   1 
HETATM 3025 O  O   . HOH   M 5 .   ? -6.347  -17.225 7.644   1.00 48.99 ? 789 HOH   A O   1 
HETATM 3026 O  O   . HOH   M 5 .   ? -32.432 -27.858 19.930  1.00 41.46 ? 790 HOH   A O   1 
HETATM 3027 O  O   . HOH   M 5 .   ? -5.612  -8.444  1.902   1.00 50.20 ? 791 HOH   A O   1 
HETATM 3028 O  O   . HOH   M 5 .   ? -16.820 -13.436 -14.599 1.00 45.01 ? 792 HOH   A O   1 
HETATM 3029 O  O   . HOH   M 5 .   ? -21.459 -11.163 12.973  1.00 25.57 ? 793 HOH   A O   1 
HETATM 3030 O  O   . HOH   M 5 .   ? -14.134 -32.491 20.450  1.00 38.55 ? 794 HOH   A O   1 
HETATM 3031 O  O   . HOH   M 5 .   ? -34.759 -18.776 6.985   1.00 41.14 ? 795 HOH   A O   1 
HETATM 3032 O  O   . HOH   M 5 .   ? -11.697 1.305   0.742   1.00 43.15 ? 796 HOH   A O   1 
HETATM 3033 O  O   . HOH   M 5 .   ? -6.126  -15.078 7.148   1.00 45.27 ? 797 HOH   A O   1 
HETATM 3034 O  O   . HOH   M 5 .   ? -11.798 -24.836 3.285   1.00 48.54 ? 798 HOH   A O   1 
HETATM 3035 O  O   . HOH   M 5 .   ? -24.531 8.723   17.659  1.00 38.78 ? 799 HOH   A O   1 
HETATM 3036 O  O   . HOH   M 5 .   ? -35.418 -11.561 4.749   1.00 47.76 ? 800 HOH   A O   1 
HETATM 3037 O  O   . HOH   M 5 .   ? -33.268 0.069   -3.137  1.00 52.24 ? 801 HOH   A O   1 
HETATM 3038 O  O   . HOH   M 5 .   ? -13.794 9.025   30.411  1.00 37.34 ? 802 HOH   A O   1 
HETATM 3039 O  O   . HOH   M 5 .   ? -20.645 8.388   20.993  1.00 36.65 ? 803 HOH   A O   1 
HETATM 3040 O  O   . HOH   M 5 .   ? -15.233 0.907   29.074  1.00 35.52 ? 804 HOH   A O   1 
HETATM 3041 O  O   . HOH   M 5 .   ? -15.536 3.979   2.448   1.00 37.60 ? 805 HOH   A O   1 
HETATM 3042 O  O   . HOH   M 5 .   ? -33.483 -27.620 17.061  1.00 46.77 ? 806 HOH   A O   1 
HETATM 3043 O  O   . HOH   M 5 .   ? -23.381 -0.922  22.012  1.00 44.40 ? 807 HOH   A O   1 
HETATM 3044 O  O   . HOH   M 5 .   ? -20.695 0.895   24.718  1.00 42.15 ? 808 HOH   A O   1 
HETATM 3045 O  O   . HOH   M 5 .   ? -24.331 -36.906 19.157  1.00 55.23 ? 809 HOH   A O   1 
HETATM 3046 O  O   . HOH   M 5 .   ? -15.951 14.533  21.465  1.00 46.21 ? 810 HOH   A O   1 
HETATM 3047 O  O   . HOH   M 5 .   ? 7.487   -18.484 33.392  1.00 47.34 ? 811 HOH   A O   1 
HETATM 3048 O  O   . HOH   M 5 .   ? 5.270   -17.048 35.085  1.00 47.62 ? 812 HOH   A O   1 
HETATM 3049 O  O   . HOH   M 5 .   ? -16.914 15.031  17.752  1.00 47.82 ? 813 HOH   A O   1 
HETATM 3050 O  O   . HOH   M 5 .   ? -21.703 -37.540 18.610  1.00 49.73 ? 814 HOH   A O   1 
HETATM 3051 O  O   . HOH   M 5 .   ? -35.602 -26.233 14.956  1.00 48.46 ? 815 HOH   A O   1 
# 
