data_8QHF
# 
_entry.id   8QHF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8QHF         pdb_00008qhf 10.2210/pdb8qhf/pdb 
WWPDB D_1292130821 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QHF 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              nicolas.bayan@i2bc.paris-saclay.fr 
_pdbx_contact_author.name_first         Nicolas 
_pdbx_contact_author.name_last          Bayan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7760-0811 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li de la Sierra-Gallay, I.' 1 0000-0003-2770-7439 
'Lesur, E.'                  2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108243 
_citation.page_last                 108243 
_citation.title                     
'Synthetic mycolates derivatives to decipher protein mycoloylation, a unique post-translational modification in bacteria.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108243 
_citation.pdbx_database_id_PubMed   39880088 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lesur, E.'                  1  ? 
primary 'Zhang, Y.'                  2  ? 
primary 'Dautin, N.'                 3  ? 
primary 'Dietrich, C.'               4  ? 
primary 'Li de la Sierra-Gallay, I.' 5  ? 
primary 'Augusto, L.A.'              6  ? 
primary 'Rollando, P.'               7  ? 
primary 'Lazar, N.'                  8  ? 
primary 'Urban, D.'                  9  ? 
primary 'Doisneau, G.'               10 ? 
primary 'Constantinesco-Becker, F.'  11 ? 
primary 'Van Tilbeurgh, H.'          12 ? 
primary 
;Guianvarc'h, D.
;
13 ? 
primary 'Bourdreux, Y.'              14 ? 
primary 'Bayan, N.'                  15 ? 
# 
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 Cmt1                                                39537.074 1  ? ? ? ? 
2 branched    man 'alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose' 342.297   1  ? ? ? ? 
3 non-polymer syn '(2~{S},3~{R})-2-pentyloctane-1,3-diol'             216.360   1  ? ? ? ? 
4 non-polymer syn 'SULFATE ION'                                       96.063    1  ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                      35.453    4  ? ? ? ? 
6 water       nat water                                               18.015    31 ? ? ? ? 
# 
_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       
;MKLLRRIAAPAIALGIAMSTIVTPSTAGAAEVTPADVAGDTALSTISDSAPADEASAPRWRAHVNAADERVKEMWAYSPS
MDRNVPLVVITADESAGPRPVIYLLNGGDGGEGAANWVMQTDVLDFYLEKNVNVVIPMEGKFSYYTDWVEENASLGGKQM
WETFLVKELPGPLEEKLNTDGQRAIAGMSMSATTSLLFPQHFPGFYDAAASFSGCAATSSLLPWEYLKLTLDRGNATPEQ
MWGPRGGEYNIYNDALINSDKLRGTELYVSNASGLAGEWESVDSPRFEGLNQQVQSIAMAETVVTGGIIEAATNKCTHDL
KAKLDSAGIPADWNLRPTGTHSWGWWQDDLRGSWTTFARAFELEA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKLLRRIAAPAIALGIAMSTIVTPSTAGAAEVTPADVAGDTALSTISDSAPADEASAPRWRAHVNAADERVKEMWAYSPS
MDRNVPLVVITADESAGPRPVIYLLNGGDGGEGAANWVMQTDVLDFYLEKNVNVVIPMEGKFSYYTDWVEENASLGGKQM
WETFLVKELPGPLEEKLNTDGQRAIAGMSMSATTSLLFPQHFPGFYDAAASFSGCAATSSLLPWEYLKLTLDRGNATPEQ
MWGPRGGEYNIYNDALINSDKLRGTELYVSNASGLAGEWESVDSPRFEGLNQQVQSIAMAETVVTGGIIEAATNKCTHDL
KAKLDSAGIPADWNLRPTGTHSWGWWQDDLRGSWTTFARAFELEA
;
_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 
3 '(2~{S},3~{R})-2-pentyloctane-1,3-diol' VBL 
4 'SULFATE ION'                           SO4 
5 'CHLORIDE ION'                          CL  
6 water                                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LEU n 
1 4   LEU n 
1 5   ARG n 
1 6   ARG n 
1 7   ILE n 
1 8   ALA n 
1 9   ALA n 
1 10  PRO n 
1 11  ALA n 
1 12  ILE n 
1 13  ALA n 
1 14  LEU n 
1 15  GLY n 
1 16  ILE n 
1 17  ALA n 
1 18  MET n 
1 19  SER n 
1 20  THR n 
1 21  ILE n 
1 22  VAL n 
1 23  THR n 
1 24  PRO n 
1 25  SER n 
1 26  THR n 
1 27  ALA n 
1 28  GLY n 
1 29  ALA n 
1 30  ALA n 
1 31  GLU n 
1 32  VAL n 
1 33  THR n 
1 34  PRO n 
1 35  ALA n 
1 36  ASP n 
1 37  VAL n 
1 38  ALA n 
1 39  GLY n 
1 40  ASP n 
1 41  THR n 
1 42  ALA n 
1 43  LEU n 
1 44  SER n 
1 45  THR n 
1 46  ILE n 
1 47  SER n 
1 48  ASP n 
1 49  SER n 
1 50  ALA n 
1 51  PRO n 
1 52  ALA n 
1 53  ASP n 
1 54  GLU n 
1 55  ALA n 
1 56  SER n 
1 57  ALA n 
1 58  PRO n 
1 59  ARG n 
1 60  TRP n 
1 61  ARG n 
1 62  ALA n 
1 63  HIS n 
1 64  VAL n 
1 65  ASN n 
1 66  ALA n 
1 67  ALA n 
1 68  ASP n 
1 69  GLU n 
1 70  ARG n 
1 71  VAL n 
1 72  LYS n 
1 73  GLU n 
1 74  MET n 
1 75  TRP n 
1 76  ALA n 
1 77  TYR n 
1 78  SER n 
1 79  PRO n 
1 80  SER n 
1 81  MET n 
1 82  ASP n 
1 83  ARG n 
1 84  ASN n 
1 85  VAL n 
1 86  PRO n 
1 87  LEU n 
1 88  VAL n 
1 89  VAL n 
1 90  ILE n 
1 91  THR n 
1 92  ALA n 
1 93  ASP n 
1 94  GLU n 
1 95  SER n 
1 96  ALA n 
1 97  GLY n 
1 98  PRO n 
1 99  ARG n 
1 100 PRO n 
1 101 VAL n 
1 102 ILE n 
1 103 TYR n 
1 104 LEU n 
1 105 LEU n 
1 106 ASN n 
1 107 GLY n 
1 108 GLY n 
1 109 ASP n 
1 110 GLY n 
1 111 GLY n 
1 112 GLU n 
1 113 GLY n 
1 114 ALA n 
1 115 ALA n 
1 116 ASN n 
1 117 TRP n 
1 118 VAL n 
1 119 MET n 
1 120 GLN n 
1 121 THR n 
1 122 ASP n 
1 123 VAL n 
1 124 LEU n 
1 125 ASP n 
1 126 PHE n 
1 127 TYR n 
1 128 LEU n 
1 129 GLU n 
1 130 LYS n 
1 131 ASN n 
1 132 VAL n 
1 133 ASN n 
1 134 VAL n 
1 135 VAL n 
1 136 ILE n 
1 137 PRO n 
1 138 MET n 
1 139 GLU n 
1 140 GLY n 
1 141 LYS n 
1 142 PHE n 
1 143 SER n 
1 144 TYR n 
1 145 TYR n 
1 146 THR n 
1 147 ASP n 
1 148 TRP n 
1 149 VAL n 
1 150 GLU n 
1 151 GLU n 
1 152 ASN n 
1 153 ALA n 
1 154 SER n 
1 155 LEU n 
1 156 GLY n 
1 157 GLY n 
1 158 LYS n 
1 159 GLN n 
1 160 MET n 
1 161 TRP n 
1 162 GLU n 
1 163 THR n 
1 164 PHE n 
1 165 LEU n 
1 166 VAL n 
1 167 LYS n 
1 168 GLU n 
1 169 LEU n 
1 170 PRO n 
1 171 GLY n 
1 172 PRO n 
1 173 LEU n 
1 174 GLU n 
1 175 GLU n 
1 176 LYS n 
1 177 LEU n 
1 178 ASN n 
1 179 THR n 
1 180 ASP n 
1 181 GLY n 
1 182 GLN n 
1 183 ARG n 
1 184 ALA n 
1 185 ILE n 
1 186 ALA n 
1 187 GLY n 
1 188 MET n 
1 189 SER n 
1 190 MET n 
1 191 SER n 
1 192 ALA n 
1 193 THR n 
1 194 THR n 
1 195 SER n 
1 196 LEU n 
1 197 LEU n 
1 198 PHE n 
1 199 PRO n 
1 200 GLN n 
1 201 HIS n 
1 202 PHE n 
1 203 PRO n 
1 204 GLY n 
1 205 PHE n 
1 206 TYR n 
1 207 ASP n 
1 208 ALA n 
1 209 ALA n 
1 210 ALA n 
1 211 SER n 
1 212 PHE n 
1 213 SER n 
1 214 GLY n 
1 215 CYS n 
1 216 ALA n 
1 217 ALA n 
1 218 THR n 
1 219 SER n 
1 220 SER n 
1 221 LEU n 
1 222 LEU n 
1 223 PRO n 
1 224 TRP n 
1 225 GLU n 
1 226 TYR n 
1 227 LEU n 
1 228 LYS n 
1 229 LEU n 
1 230 THR n 
1 231 LEU n 
1 232 ASP n 
1 233 ARG n 
1 234 GLY n 
1 235 ASN n 
1 236 ALA n 
1 237 THR n 
1 238 PRO n 
1 239 GLU n 
1 240 GLN n 
1 241 MET n 
1 242 TRP n 
1 243 GLY n 
1 244 PRO n 
1 245 ARG n 
1 246 GLY n 
1 247 GLY n 
1 248 GLU n 
1 249 TYR n 
1 250 ASN n 
1 251 ILE n 
1 252 TYR n 
1 253 ASN n 
1 254 ASP n 
1 255 ALA n 
1 256 LEU n 
1 257 ILE n 
1 258 ASN n 
1 259 SER n 
1 260 ASP n 
1 261 LYS n 
1 262 LEU n 
1 263 ARG n 
1 264 GLY n 
1 265 THR n 
1 266 GLU n 
1 267 LEU n 
1 268 TYR n 
1 269 VAL n 
1 270 SER n 
1 271 ASN n 
1 272 ALA n 
1 273 SER n 
1 274 GLY n 
1 275 LEU n 
1 276 ALA n 
1 277 GLY n 
1 278 GLU n 
1 279 TRP n 
1 280 GLU n 
1 281 SER n 
1 282 VAL n 
1 283 ASP n 
1 284 SER n 
1 285 PRO n 
1 286 ARG n 
1 287 PHE n 
1 288 GLU n 
1 289 GLY n 
1 290 LEU n 
1 291 ASN n 
1 292 GLN n 
1 293 GLN n 
1 294 VAL n 
1 295 GLN n 
1 296 SER n 
1 297 ILE n 
1 298 ALA n 
1 299 MET n 
1 300 ALA n 
1 301 GLU n 
1 302 THR n 
1 303 VAL n 
1 304 VAL n 
1 305 THR n 
1 306 GLY n 
1 307 GLY n 
1 308 ILE n 
1 309 ILE n 
1 310 GLU n 
1 311 ALA n 
1 312 ALA n 
1 313 THR n 
1 314 ASN n 
1 315 LYS n 
1 316 CYS n 
1 317 THR n 
1 318 HIS n 
1 319 ASP n 
1 320 LEU n 
1 321 LYS n 
1 322 ALA n 
1 323 LYS n 
1 324 LEU n 
1 325 ASP n 
1 326 SER n 
1 327 ALA n 
1 328 GLY n 
1 329 ILE n 
1 330 PRO n 
1 331 ALA n 
1 332 ASP n 
1 333 TRP n 
1 334 ASN n 
1 335 LEU n 
1 336 ARG n 
1 337 PRO n 
1 338 THR n 
1 339 GLY n 
1 340 THR n 
1 341 HIS n 
1 342 SER n 
1 343 TRP n 
1 344 GLY n 
1 345 TRP n 
1 346 TRP n 
1 347 GLN n 
1 348 ASP n 
1 349 ASP n 
1 350 LEU n 
1 351 ARG n 
1 352 GLY n 
1 353 SER n 
1 354 TRP n 
1 355 THR n 
1 356 THR n 
1 357 PHE n 
1 358 ALA n 
1 359 ARG n 
1 360 ALA n 
1 361 PHE n 
1 362 GLU n 
1 363 LEU n 
1 364 GLU n 
1 365 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   365 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 cmt1 
_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      'Corynebacterium glutamicum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1718 
_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      'Corynebacterium glutamicum' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1718 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpa1-1DGlcpa                             'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a1-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(1+1)][a-D-Glcp]{}}'         LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   1 
_pdbx_entity_branch_link.comp_id_1                  GLC 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   2 
_pdbx_entity_branch_link.comp_id_2                  GLC 
_pdbx_entity_branch_link.atom_id_2                  O1 
_pdbx_entity_branch_link.leaving_atom_id_2          HO1 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE                                 ?                                     'C3 H7 N O2'     
89.093  
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 
CL  non-polymer                   . 'CHLORIDE ION'                          ?                                     'Cl -1'          
35.453  
CYS 'L-peptide linking'           y CYSTEINE                                ?                                     'C3 H7 N O2 S'   
121.158 
GLC 'D-saccharide, alpha linking' . alpha-D-glucopyranose                   'alpha-D-glucose; D-glucose; glucose' 'C6 H12 O6'      
180.156 
GLN 'L-peptide linking'           y GLUTAMINE                               ?                                     'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                         ?                                     'C5 H9 N O4'     
147.129 
GLY 'peptide linking'             y GLYCINE                                 ?                                     'C2 H5 N O2'     
75.067  
HIS 'L-peptide linking'           y HISTIDINE                               ?                                     'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer                   . WATER                                   ?                                     'H2 O'           
18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                              ?                                     'C6 H13 N O2'    
131.173 
LEU 'L-peptide linking'           y LEUCINE                                 ?                                     'C6 H13 N O2'    
131.173 
LYS 'L-peptide linking'           y LYSINE                                  ?                                     'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking'           y METHIONINE                              ?                                     'C5 H11 N O2 S'  
149.211 
PHE 'L-peptide linking'           y PHENYLALANINE                           ?                                     'C9 H11 N O2'    
165.189 
PRO 'L-peptide linking'           y PROLINE                                 ?                                     'C5 H9 N O2'     
115.130 
SER 'L-peptide linking'           y SERINE                                  ?                                     'C3 H7 N O3'     
105.093 
SO4 non-polymer                   . 'SULFATE ION'                           ?                                     'O4 S -2'        
96.063  
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 
VBL non-polymer                   . '(2~{S},3~{R})-2-pentyloctane-1,3-diol' ?                                     'C13 H28 O2'     
216.360 
# 
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 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   ?   ?   ?   A . n 
A 1 5   ARG 5   5   ?   ?   ?   A . n 
A 1 6   ARG 6   6   ?   ?   ?   A . n 
A 1 7   ILE 7   7   ?   ?   ?   A . n 
A 1 8   ALA 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  PRO 10  10  ?   ?   ?   A . n 
A 1 11  ALA 11  11  ?   ?   ?   A . n 
A 1 12  ILE 12  12  ?   ?   ?   A . n 
A 1 13  ALA 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  GLY 15  15  ?   ?   ?   A . n 
A 1 16  ILE 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  MET 18  18  ?   ?   ?   A . n 
A 1 19  SER 19  19  ?   ?   ?   A . n 
A 1 20  THR 20  20  ?   ?   ?   A . n 
A 1 21  ILE 21  21  ?   ?   ?   A . n 
A 1 22  VAL 22  22  ?   ?   ?   A . n 
A 1 23  THR 23  23  ?   ?   ?   A . n 
A 1 24  PRO 24  24  ?   ?   ?   A . n 
A 1 25  SER 25  25  ?   ?   ?   A . n 
A 1 26  THR 26  26  ?   ?   ?   A . n 
A 1 27  ALA 27  27  ?   ?   ?   A . n 
A 1 28  GLY 28  28  ?   ?   ?   A . n 
A 1 29  ALA 29  29  ?   ?   ?   A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  TRP 60  60  60  TRP TRP A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  TRP 75  75  75  TRP TRP A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  SER 78  78  78  SER SER A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  MET 81  81  81  MET MET A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 TRP 117 117 117 TRP TRP A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 MET 138 138 138 MET MET A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 TRP 148 148 148 TRP TRP A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 MET 160 160 160 MET MET A . n 
A 1 161 TRP 161 161 161 TRP TRP A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 MET 188 188 188 MET MET A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 PRO 203 203 203 PRO PRO A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 CYS 215 215 215 CYS CYS A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 TRP 224 224 224 TRP TRP A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 TYR 226 226 226 TYR TYR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 ARG 233 233 233 ARG ARG A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 GLN 240 240 240 GLN GLN A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 TRP 242 242 242 TRP TRP A . n 
A 1 243 GLY 243 243 243 GLY GLY A . n 
A 1 244 PRO 244 244 244 PRO PRO A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 TYR 249 249 249 TYR TYR A . n 
A 1 250 ASN 250 250 250 ASN ASN A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 TYR 252 252 252 TYR TYR A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ARG 263 263 263 ARG ARG A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 ASN 271 271 271 ASN ASN A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 TRP 279 279 279 TRP TRP A . n 
A 1 280 GLU 280 280 280 GLU GLU A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 ASP 283 283 ?   ?   ?   A . n 
A 1 284 SER 284 284 ?   ?   ?   A . n 
A 1 285 PRO 285 285 ?   ?   ?   A . n 
A 1 286 ARG 286 286 ?   ?   ?   A . n 
A 1 287 PHE 287 287 ?   ?   ?   A . n 
A 1 288 GLU 288 288 ?   ?   ?   A . n 
A 1 289 GLY 289 289 ?   ?   ?   A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 ASN 291 291 291 ASN ASN A . n 
A 1 292 GLN 292 292 292 GLN GLN A . n 
A 1 293 GLN 293 293 293 GLN GLN A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 GLN 295 295 295 GLN GLN A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 MET 299 299 299 MET MET A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 VAL 304 304 304 VAL VAL A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 ILE 308 308 308 ILE ILE A . n 
A 1 309 ILE 309 309 309 ILE ILE A . n 
A 1 310 GLU 310 310 310 GLU GLU A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 CYS 316 316 316 CYS CYS A . n 
A 1 317 THR 317 317 317 THR THR A . n 
A 1 318 HIS 318 318 318 HIS HIS A . n 
A 1 319 ASP 319 319 319 ASP ASP A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 LYS 321 321 321 LYS LYS A . n 
A 1 322 ALA 322 322 322 ALA ALA A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 SER 326 326 326 SER SER A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 PRO 330 330 330 PRO PRO A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 TRP 333 333 333 TRP TRP A . n 
A 1 334 ASN 334 334 334 ASN ASN A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 THR 338 338 338 THR THR A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 HIS 341 341 341 HIS HIS A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 TRP 343 343 343 TRP TRP A . n 
A 1 344 GLY 344 344 344 GLY GLY A . n 
A 1 345 TRP 345 345 345 TRP TRP A . n 
A 1 346 TRP 346 346 346 TRP TRP A . n 
A 1 347 GLN 347 347 347 GLN GLN A . n 
A 1 348 ASP 348 348 348 ASP ASP A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 ARG 351 351 351 ARG ARG A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 TRP 354 354 354 TRP TRP A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 THR 356 356 356 THR THR A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 ALA 358 358 358 ALA ALA A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 PHE 361 361 361 PHE PHE A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 GLU 364 364 ?   ?   ?   A . n 
A 1 365 ALA 365 365 ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 GLC 1 B GLC 1 B GLC 1 n 
B 2 GLC 2 B GLC 2 B GLC 2 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        VBL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   VBL 
_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 
C 3 VBL 1  401 401 VBL VBL A . 
D 4 SO4 1  402 1   SO4 SO4 A . 
E 5 CL  1  403 1   CL  CL  A . 
F 5 CL  1  404 2   CL  CL  A . 
G 5 CL  1  405 3   CL  CL  A . 
H 5 CL  1  406 4   CL  CL  A . 
I 6 HOH 1  501 30  HOH HOH A . 
I 6 HOH 2  502 29  HOH HOH A . 
I 6 HOH 3  503 6   HOH HOH A . 
I 6 HOH 4  504 1   HOH HOH A . 
I 6 HOH 5  505 22  HOH HOH A . 
I 6 HOH 6  506 8   HOH HOH A . 
I 6 HOH 7  507 17  HOH HOH A . 
I 6 HOH 8  508 16  HOH HOH A . 
I 6 HOH 9  509 5   HOH HOH A . 
I 6 HOH 10 510 3   HOH HOH A . 
I 6 HOH 11 511 14  HOH HOH A . 
I 6 HOH 12 512 9   HOH HOH A . 
I 6 HOH 13 513 21  HOH HOH A . 
I 6 HOH 14 514 11  HOH HOH A . 
I 6 HOH 15 515 19  HOH HOH A . 
I 6 HOH 16 516 26  HOH HOH A . 
I 6 HOH 17 517 31  HOH HOH A . 
I 6 HOH 18 518 28  HOH HOH A . 
I 6 HOH 19 519 15  HOH HOH A . 
I 6 HOH 20 520 23  HOH HOH A . 
I 6 HOH 21 521 4   HOH HOH A . 
I 6 HOH 22 522 2   HOH HOH A . 
I 6 HOH 23 523 13  HOH HOH A . 
I 6 HOH 24 524 25  HOH HOH A . 
I 6 HOH 25 525 24  HOH HOH A . 
I 6 HOH 26 526 27  HOH HOH A . 
I 6 HOH 27 527 10  HOH HOH A . 
I 6 HOH 28 528 20  HOH HOH A . 
I 6 HOH 29 529 12  HOH HOH A . 
I 6 HOH 30 530 18  HOH HOH A . 
I 6 HOH 31 531 7   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       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? '2.10.4 (10-JUL-2024)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                      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                     8QHF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     168.120 
_cell.length_a_esd                 ? 
_cell.length_b                     168.120 
_cell.length_b_esd                 ? 
_cell.length_c                     168.120 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         8QHF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                196 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'F 2 3' 
_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                   8QHF 
_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             2.50 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_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    'Ammonium sulfate, Sodium chloride, Hepes' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-13 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98013 
_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                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98013 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QHF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.688 
_reflns.d_resolution_low                               48.53 
_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                                     11045 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.21 
_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                                0.198 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.69 
_reflns_shell.d_res_low                                     2.85 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1723 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.449 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.349 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.00000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            0.00000 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               85.90 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.935 
_refine.correlation_coeff_Fo_to_Fc_free          0.914 
_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                                 8QHF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.69 
_refine.ls_d_res_low                             48.53 
_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                     11045 
_refine.ls_number_reflns_R_free                  553 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_percent_reflns_R_free                 5.010 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2545 
_refine.ls_R_factor_R_free                       0.2794 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2532 
_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                    ? 
_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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.363 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.354 
_refine.pdbx_overall_SU_R_Blow_DPI               1.148 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             1.321 
_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_analyze.entry_id                        8QHF 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.46 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.69 
_refine_hist.d_res_low                        48.53 
_refine_hist.number_atoms_solvent             31 
_refine_hist.number_atoms_total               2590 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2512 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         47 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 2620 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.89  ? 3571 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 866  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 443  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2620 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.00  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 14.36 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 341  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 1995 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.69 
_refine_ls_shell.d_res_low                        2.73 
_refine_ls_shell.number_reflns_all                410 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             389 
_refine_ls_shell.percent_reflns_obs               92.47 
_refine_ls_shell.percent_reflns_R_free            5.12 
_refine_ls_shell.R_factor_all                     0.4061 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.4002 
_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   28 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.5176 
# 
_struct.entry_id                     8QHF 
_struct.title                        'Corynebacterium glutamicum mycoloyltransferase C acyl-enzyme intermediate' 
_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        8QHF 
_struct_keywords.text            
'ALPHA / BETA HYDROLASE, MYCOLOYLTRANSFERASE, TREHALOSE O- 2 MYCOLYLTRANSFERASE, EXTERNAL MEMBRANE, TRANSFERASE, TMM analogs' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8NTG4_CORGL 
_struct_ref.pdbx_db_accession          Q8NTG4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKLLRRIAAPAIALGIAMSTIVTPSTAGAAEVTPADVAGDTALSTISDSAPADEASAPRWRAHVNAADERVKEMWAYSPS
MDRNVPLVVITADESAGPRPVIYLLNGGDGGEGAANWVMQTDVLDFYLEKNVNVVIPMEGKFSYYTDWVEENASLGGKQM
WETFLVKELPGPLEEKLNTDGQRAIAGMSMSATTSLLFPQHFPGFYDAAASFSGCAATSSLLPWEYLKLTLDRGNATPEQ
MWGPRGGEYNIYNDALINSDKLRGTELYVSNASGLAGEWESVDSPRFEGLNQQVQSIAMAETVVTGGIIEAATNKCTHDL
KAKLDSAGIPADWNLRPTGTHSWGWWQDDLRGSWTTFARAFELEA
;
_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              8QHF 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 365 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8NTG4 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  365 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       365 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 33  ? GLY A 39  ? THR A 33  GLY A 39  1 ? 7  
HELX_P HELX_P2  AA2 TRP A 60  ? ALA A 67  ? TRP A 60  ALA A 67  1 ? 8  
HELX_P HELX_P3  AA3 ASN A 116 ? THR A 121 ? ASN A 116 THR A 121 1 ? 6  
HELX_P HELX_P4  AA4 ASP A 122 ? ASN A 131 ? ASP A 122 ASN A 131 1 ? 10 
HELX_P HELX_P5  AA5 ASN A 152 ? GLY A 156 ? ASN A 152 GLY A 156 5 ? 5  
HELX_P HELX_P6  AA6 MET A 160 ? LYS A 167 ? MET A 160 LYS A 167 1 ? 8  
HELX_P HELX_P7  AA7 LEU A 169 ? ASN A 178 ? LEU A 169 ASN A 178 1 ? 10 
HELX_P HELX_P8  AA8 MET A 190 ? PHE A 202 ? MET A 190 PHE A 202 1 ? 13 
HELX_P HELX_P9  AA9 SER A 220 ? ARG A 233 ? SER A 220 ARG A 233 1 ? 14 
HELX_P HELX_P10 AB1 THR A 237 ? GLY A 243 ? THR A 237 GLY A 243 1 ? 7  
HELX_P HELX_P11 AB2 GLY A 247 ? ASN A 253 ? GLY A 247 ASN A 253 1 ? 7  
HELX_P HELX_P12 AB3 ASN A 258 ? ARG A 263 ? ASN A 258 ARG A 263 5 ? 6  
HELX_P HELX_P13 AB4 ASN A 291 ? ALA A 327 ? ASN A 291 ALA A 327 1 ? 37 
HELX_P HELX_P14 AB5 SER A 342 ? GLU A 362 ? SER A 342 GLU A 362 1 ? 21 
# 
_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 215 SG ? ? ? 1_555 A CYS 316 SG  ? ? A CYS 215 A CYS 316 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
covale1 covale none ? A SER 189 OG ? ? ? 1_555 C VBL .   C10 ? ? A SER 189 A VBL 401 1_555 ? ? ? ? ? ? ? 1.406 ? ? 
covale2 covale both ? B GLC .   C1 ? ? ? 1_555 B GLC .   O1  ? ? B GLC 1   B GLC 2   1_555 ? ? ? ? ? ? ? 1.506 ? ? 
# 
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 VBL C .   ? SER A 189 ? VBL A 401 ? 1_555 SER A 189 ? 1_555 C10 OG SER 1 VBL None Lipid/lipid-like   
2 CYS A 215 ? CYS A 316 ? CYS A 215 ? 1_555 CYS A 316 ? 1_555 SG  SG .   . .   None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? 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 THR A 45  ? SER A 47  ? THR A 45  SER A 47  
AA1 2 VAL A 71  ? SER A 78  ? VAL A 71  SER A 78  
AA1 3 ARG A 83  ? ILE A 90  ? ARG A 83  ILE A 90  
AA1 4 ASN A 133 ? PRO A 137 ? ASN A 133 PRO A 137 
AA1 5 VAL A 101 ? LEU A 105 ? VAL A 101 LEU A 105 
AA1 6 ARG A 183 ? MET A 188 ? ARG A 183 MET A 188 
AA1 7 ALA A 208 ? PHE A 212 ? ALA A 208 PHE A 212 
AA1 8 GLU A 266 ? SER A 270 ? GLU A 266 SER A 270 
AA1 9 ASP A 332 ? ASN A 334 ? ASP A 332 ASN A 334 
AA2 1 GLY A 274 ? ALA A 276 ? GLY A 274 ALA A 276 
AA2 2 GLY A 339 ? HIS A 341 ? GLY A 339 HIS A 341 
# 
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 SER A 47  ? N SER A 47  O TRP A 75  ? O TRP A 75  
AA1 2 3 N SER A 78  ? N SER A 78  O ARG A 83  ? O ARG A 83  
AA1 3 4 N ILE A 90  ? N ILE A 90  O VAL A 134 ? O VAL A 134 
AA1 4 5 O VAL A 135 ? O VAL A 135 N ILE A 102 ? N ILE A 102 
AA1 5 6 N LEU A 105 ? N LEU A 105 O ALA A 186 ? O ALA A 186 
AA1 6 7 N GLY A 187 ? N GLY A 187 O PHE A 212 ? O PHE A 212 
AA1 7 8 N SER A 211 ? N SER A 211 O TYR A 268 ? O TYR A 268 
AA1 8 9 N LEU A 267 ? N LEU A 267 O ASP A 332 ? O ASP A 332 
AA2 1 2 N ALA A 276 ? N ALA A 276 O THR A 340 ? O THR A 340 
# 
_pdbx_entry_details.entry_id                   8QHF 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    189 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O1 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   VBL 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.92 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 68  ? ? -49.68  153.27  
2 1 ASP A 122 ? ? -92.95  30.57   
3 1 SER A 189 ? ? 59.16   -112.04 
4 1 SER A 213 ? ? 59.84   76.45   
5 1 THR A 218 ? ? -140.06 -13.79  
# 
_pdbx_molecule_features.prd_id    PRD_900006 
_pdbx_molecule_features.name      trehalose 
_pdbx_molecule_features.type      Oligosaccharide 
_pdbx_molecule_features.class     Nutrient 
_pdbx_molecule_features.details   'oligosaccharide with reducing-end-to-reducing-end glycosidic bond' 
# 
_pdbx_molecule.instance_id   1 
_pdbx_molecule.prd_id        PRD_900006 
_pdbx_molecule.asym_id       B 
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A LYS 2   ? A LYS 2   
3  1 Y 1 A LEU 3   ? A LEU 3   
4  1 Y 1 A LEU 4   ? A LEU 4   
5  1 Y 1 A ARG 5   ? A ARG 5   
6  1 Y 1 A ARG 6   ? A ARG 6   
7  1 Y 1 A ILE 7   ? A ILE 7   
8  1 Y 1 A ALA 8   ? A ALA 8   
9  1 Y 1 A ALA 9   ? A ALA 9   
10 1 Y 1 A PRO 10  ? A PRO 10  
11 1 Y 1 A ALA 11  ? A ALA 11  
12 1 Y 1 A ILE 12  ? A ILE 12  
13 1 Y 1 A ALA 13  ? A ALA 13  
14 1 Y 1 A LEU 14  ? A LEU 14  
15 1 Y 1 A GLY 15  ? A GLY 15  
16 1 Y 1 A ILE 16  ? A ILE 16  
17 1 Y 1 A ALA 17  ? A ALA 17  
18 1 Y 1 A MET 18  ? A MET 18  
19 1 Y 1 A SER 19  ? A SER 19  
20 1 Y 1 A THR 20  ? A THR 20  
21 1 Y 1 A ILE 21  ? A ILE 21  
22 1 Y 1 A VAL 22  ? A VAL 22  
23 1 Y 1 A THR 23  ? A THR 23  
24 1 Y 1 A PRO 24  ? A PRO 24  
25 1 Y 1 A SER 25  ? A SER 25  
26 1 Y 1 A THR 26  ? A THR 26  
27 1 Y 1 A ALA 27  ? A ALA 27  
28 1 Y 1 A GLY 28  ? A GLY 28  
29 1 Y 1 A ALA 29  ? A ALA 29  
30 1 Y 1 A ASP 283 ? A ASP 283 
31 1 Y 1 A SER 284 ? A SER 284 
32 1 Y 1 A PRO 285 ? A PRO 285 
33 1 Y 1 A ARG 286 ? A ARG 286 
34 1 Y 1 A PHE 287 ? A PHE 287 
35 1 Y 1 A GLU 288 ? A GLU 288 
36 1 Y 1 A GLY 289 ? A GLY 289 
37 1 Y 1 A GLU 364 ? A GLU 364 
38 1 Y 1 A ALA 365 ? A ALA 365 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLC C1   C  N S 89  
GLC C2   C  N R 90  
GLC C3   C  N S 91  
GLC C4   C  N S 92  
GLC C5   C  N R 93  
GLC C6   C  N N 94  
GLC O1   O  N N 95  
GLC O2   O  N N 96  
GLC O3   O  N N 97  
GLC O4   O  N N 98  
GLC O5   O  N N 99  
GLC O6   O  N N 100 
GLC H1   H  N N 101 
GLC H2   H  N N 102 
GLC H3   H  N N 103 
GLC H4   H  N N 104 
GLC H5   H  N N 105 
GLC H61  H  N N 106 
GLC H62  H  N N 107 
GLC HO1  H  N N 108 
GLC HO2  H  N N 109 
GLC HO3  H  N N 110 
GLC HO4  H  N N 111 
GLC HO6  H  N N 112 
GLN N    N  N N 113 
GLN CA   C  N S 114 
GLN C    C  N N 115 
GLN O    O  N N 116 
GLN CB   C  N N 117 
GLN CG   C  N N 118 
GLN CD   C  N N 119 
GLN OE1  O  N N 120 
GLN NE2  N  N N 121 
GLN OXT  O  N N 122 
GLN H    H  N N 123 
GLN H2   H  N N 124 
GLN HA   H  N N 125 
GLN HB2  H  N N 126 
GLN HB3  H  N N 127 
GLN HG2  H  N N 128 
GLN HG3  H  N N 129 
GLN HE21 H  N N 130 
GLN HE22 H  N N 131 
GLN HXT  H  N N 132 
GLU N    N  N N 133 
GLU CA   C  N S 134 
GLU C    C  N N 135 
GLU O    O  N N 136 
GLU CB   C  N N 137 
GLU CG   C  N N 138 
GLU CD   C  N N 139 
GLU OE1  O  N N 140 
GLU OE2  O  N N 141 
GLU OXT  O  N N 142 
GLU H    H  N N 143 
GLU H2   H  N N 144 
GLU HA   H  N N 145 
GLU HB2  H  N N 146 
GLU HB3  H  N N 147 
GLU HG2  H  N N 148 
GLU HG3  H  N N 149 
GLU HE2  H  N N 150 
GLU HXT  H  N N 151 
GLY N    N  N N 152 
GLY CA   C  N N 153 
GLY C    C  N N 154 
GLY O    O  N N 155 
GLY OXT  O  N N 156 
GLY H    H  N N 157 
GLY H2   H  N N 158 
GLY HA2  H  N N 159 
GLY HA3  H  N N 160 
GLY HXT  H  N N 161 
HIS N    N  N N 162 
HIS CA   C  N S 163 
HIS C    C  N N 164 
HIS O    O  N N 165 
HIS CB   C  N N 166 
HIS CG   C  Y N 167 
HIS ND1  N  Y N 168 
HIS CD2  C  Y N 169 
HIS CE1  C  Y N 170 
HIS NE2  N  Y N 171 
HIS OXT  O  N N 172 
HIS H    H  N N 173 
HIS H2   H  N N 174 
HIS HA   H  N N 175 
HIS HB2  H  N N 176 
HIS HB3  H  N N 177 
HIS HD1  H  N N 178 
HIS HD2  H  N N 179 
HIS HE1  H  N N 180 
HIS HE2  H  N N 181 
HIS HXT  H  N N 182 
HOH O    O  N N 183 
HOH H1   H  N N 184 
HOH H2   H  N N 185 
ILE N    N  N N 186 
ILE CA   C  N S 187 
ILE C    C  N N 188 
ILE O    O  N N 189 
ILE CB   C  N S 190 
ILE CG1  C  N N 191 
ILE CG2  C  N N 192 
ILE CD1  C  N N 193 
ILE OXT  O  N N 194 
ILE H    H  N N 195 
ILE H2   H  N N 196 
ILE HA   H  N N 197 
ILE HB   H  N N 198 
ILE HG12 H  N N 199 
ILE HG13 H  N N 200 
ILE HG21 H  N N 201 
ILE HG22 H  N N 202 
ILE HG23 H  N N 203 
ILE HD11 H  N N 204 
ILE HD12 H  N N 205 
ILE HD13 H  N N 206 
ILE HXT  H  N N 207 
LEU N    N  N N 208 
LEU CA   C  N S 209 
LEU C    C  N N 210 
LEU O    O  N N 211 
LEU CB   C  N N 212 
LEU CG   C  N N 213 
LEU CD1  C  N N 214 
LEU CD2  C  N N 215 
LEU OXT  O  N N 216 
LEU H    H  N N 217 
LEU H2   H  N N 218 
LEU HA   H  N N 219 
LEU HB2  H  N N 220 
LEU HB3  H  N N 221 
LEU HG   H  N N 222 
LEU HD11 H  N N 223 
LEU HD12 H  N N 224 
LEU HD13 H  N N 225 
LEU HD21 H  N N 226 
LEU HD22 H  N N 227 
LEU HD23 H  N N 228 
LEU HXT  H  N N 229 
LYS N    N  N N 230 
LYS CA   C  N S 231 
LYS C    C  N N 232 
LYS O    O  N N 233 
LYS CB   C  N N 234 
LYS CG   C  N N 235 
LYS CD   C  N N 236 
LYS CE   C  N N 237 
LYS NZ   N  N N 238 
LYS OXT  O  N N 239 
LYS H    H  N N 240 
LYS H2   H  N N 241 
LYS HA   H  N N 242 
LYS HB2  H  N N 243 
LYS HB3  H  N N 244 
LYS HG2  H  N N 245 
LYS HG3  H  N N 246 
LYS HD2  H  N N 247 
LYS HD3  H  N N 248 
LYS HE2  H  N N 249 
LYS HE3  H  N N 250 
LYS HZ1  H  N N 251 
LYS HZ2  H  N N 252 
LYS HZ3  H  N N 253 
LYS HXT  H  N N 254 
MET N    N  N N 255 
MET CA   C  N S 256 
MET C    C  N N 257 
MET O    O  N N 258 
MET CB   C  N N 259 
MET CG   C  N N 260 
MET SD   S  N N 261 
MET CE   C  N N 262 
MET OXT  O  N N 263 
MET H    H  N N 264 
MET H2   H  N N 265 
MET HA   H  N N 266 
MET HB2  H  N N 267 
MET HB3  H  N N 268 
MET HG2  H  N N 269 
MET HG3  H  N N 270 
MET HE1  H  N N 271 
MET HE2  H  N N 272 
MET HE3  H  N N 273 
MET HXT  H  N N 274 
PHE N    N  N N 275 
PHE CA   C  N S 276 
PHE C    C  N N 277 
PHE O    O  N N 278 
PHE CB   C  N N 279 
PHE CG   C  Y N 280 
PHE CD1  C  Y N 281 
PHE CD2  C  Y N 282 
PHE CE1  C  Y N 283 
PHE CE2  C  Y N 284 
PHE CZ   C  Y N 285 
PHE OXT  O  N N 286 
PHE H    H  N N 287 
PHE H2   H  N N 288 
PHE HA   H  N N 289 
PHE HB2  H  N N 290 
PHE HB3  H  N N 291 
PHE HD1  H  N N 292 
PHE HD2  H  N N 293 
PHE HE1  H  N N 294 
PHE HE2  H  N N 295 
PHE HZ   H  N N 296 
PHE HXT  H  N N 297 
PRO N    N  N N 298 
PRO CA   C  N S 299 
PRO C    C  N N 300 
PRO O    O  N N 301 
PRO CB   C  N N 302 
PRO CG   C  N N 303 
PRO CD   C  N N 304 
PRO OXT  O  N N 305 
PRO H    H  N N 306 
PRO HA   H  N N 307 
PRO HB2  H  N N 308 
PRO HB3  H  N N 309 
PRO HG2  H  N N 310 
PRO HG3  H  N N 311 
PRO HD2  H  N N 312 
PRO HD3  H  N N 313 
PRO HXT  H  N N 314 
SER N    N  N N 315 
SER CA   C  N S 316 
SER C    C  N N 317 
SER O    O  N N 318 
SER CB   C  N N 319 
SER OG   O  N N 320 
SER OXT  O  N N 321 
SER H    H  N N 322 
SER H2   H  N N 323 
SER HA   H  N N 324 
SER HB2  H  N N 325 
SER HB3  H  N N 326 
SER HG   H  N N 327 
SER HXT  H  N N 328 
SO4 S    S  N N 329 
SO4 O1   O  N N 330 
SO4 O2   O  N N 331 
SO4 O3   O  N N 332 
SO4 O4   O  N N 333 
THR N    N  N N 334 
THR CA   C  N S 335 
THR C    C  N N 336 
THR O    O  N N 337 
THR CB   C  N R 338 
THR OG1  O  N N 339 
THR CG2  C  N N 340 
THR OXT  O  N N 341 
THR H    H  N N 342 
THR H2   H  N N 343 
THR HA   H  N N 344 
THR HB   H  N N 345 
THR HG1  H  N N 346 
THR HG21 H  N N 347 
THR HG22 H  N N 348 
THR HG23 H  N N 349 
THR HXT  H  N N 350 
TRP N    N  N N 351 
TRP CA   C  N S 352 
TRP C    C  N N 353 
TRP O    O  N N 354 
TRP CB   C  N N 355 
TRP CG   C  Y N 356 
TRP CD1  C  Y N 357 
TRP CD2  C  Y N 358 
TRP NE1  N  Y N 359 
TRP CE2  C  Y N 360 
TRP CE3  C  Y N 361 
TRP CZ2  C  Y N 362 
TRP CZ3  C  Y N 363 
TRP CH2  C  Y N 364 
TRP OXT  O  N N 365 
TRP H    H  N N 366 
TRP H2   H  N N 367 
TRP HA   H  N N 368 
TRP HB2  H  N N 369 
TRP HB3  H  N N 370 
TRP HD1  H  N N 371 
TRP HE1  H  N N 372 
TRP HE3  H  N N 373 
TRP HZ2  H  N N 374 
TRP HZ3  H  N N 375 
TRP HH2  H  N N 376 
TRP HXT  H  N N 377 
TYR N    N  N N 378 
TYR CA   C  N S 379 
TYR C    C  N N 380 
TYR O    O  N N 381 
TYR CB   C  N N 382 
TYR CG   C  Y N 383 
TYR CD1  C  Y N 384 
TYR CD2  C  Y N 385 
TYR CE1  C  Y N 386 
TYR CE2  C  Y N 387 
TYR CZ   C  Y N 388 
TYR OH   O  N N 389 
TYR OXT  O  N N 390 
TYR H    H  N N 391 
TYR H2   H  N N 392 
TYR HA   H  N N 393 
TYR HB2  H  N N 394 
TYR HB3  H  N N 395 
TYR HD1  H  N N 396 
TYR HD2  H  N N 397 
TYR HE1  H  N N 398 
TYR HE2  H  N N 399 
TYR HH   H  N N 400 
TYR HXT  H  N N 401 
VAL N    N  N N 402 
VAL CA   C  N S 403 
VAL C    C  N N 404 
VAL O    O  N N 405 
VAL CB   C  N N 406 
VAL CG1  C  N N 407 
VAL CG2  C  N N 408 
VAL OXT  O  N N 409 
VAL H    H  N N 410 
VAL H2   H  N N 411 
VAL HA   H  N N 412 
VAL HB   H  N N 413 
VAL HG11 H  N N 414 
VAL HG12 H  N N 415 
VAL HG13 H  N N 416 
VAL HG21 H  N N 417 
VAL HG22 H  N N 418 
VAL HG23 H  N N 419 
VAL HXT  H  N N 420 
VBL C3   C  N S 421 
VBL C4   C  N R 422 
VBL C5   C  N N 423 
VBL C6   C  N N 424 
VBL C7   C  N N 425 
VBL C8   C  N N 426 
VBL C9   C  N N 427 
VBL C1   C  N N 428 
VBL C2   C  N N 429 
VBL C10  C  N N 430 
VBL C12  C  N N 431 
VBL C11  C  N N 432 
VBL C    C  N N 433 
VBL O    O  N N 434 
VBL O1   O  N N 435 
VBL H1   H  N N 436 
VBL H2   H  N N 437 
VBL H3   H  N N 438 
VBL H4   H  N N 439 
VBL H5   H  N N 440 
VBL H6   H  N N 441 
VBL H7   H  N N 442 
VBL H8   H  N N 443 
VBL H9   H  N N 444 
VBL H10  H  N N 445 
VBL H11  H  N N 446 
VBL H12  H  N N 447 
VBL H13  H  N N 448 
VBL H14  H  N N 449 
VBL H15  H  N N 450 
VBL H16  H  N N 451 
VBL H17  H  N N 452 
VBL H18  H  N N 453 
VBL H19  H  N N 454 
VBL H20  H  N N 455 
VBL H21  H  N N 456 
VBL H22  H  N N 457 
VBL H23  H  N N 458 
VBL H24  H  N N 459 
VBL H25  H  N N 460 
VBL H26  H  N N 461 
VBL H27  H  N N 462 
VBL H28  H  N N 463 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLC C1  C2   sing N N 83  
GLC C1  O1   sing N N 84  
GLC C1  O5   sing N N 85  
GLC C1  H1   sing N N 86  
GLC C2  C3   sing N N 87  
GLC C2  O2   sing N N 88  
GLC C2  H2   sing N N 89  
GLC C3  C4   sing N N 90  
GLC C3  O3   sing N N 91  
GLC C3  H3   sing N N 92  
GLC C4  C5   sing N N 93  
GLC C4  O4   sing N N 94  
GLC C4  H4   sing N N 95  
GLC C5  C6   sing N N 96  
GLC C5  O5   sing N N 97  
GLC C5  H5   sing N N 98  
GLC C6  O6   sing N N 99  
GLC C6  H61  sing N N 100 
GLC C6  H62  sing N N 101 
GLC O1  HO1  sing N N 102 
GLC O2  HO2  sing N N 103 
GLC O3  HO3  sing N N 104 
GLC O4  HO4  sing N N 105 
GLC O6  HO6  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
HOH O   H1   sing N N 174 
HOH O   H2   sing N N 175 
ILE N   CA   sing N N 176 
ILE N   H    sing N N 177 
ILE N   H2   sing N N 178 
ILE CA  C    sing N N 179 
ILE CA  CB   sing N N 180 
ILE CA  HA   sing N N 181 
ILE C   O    doub N N 182 
ILE C   OXT  sing N N 183 
ILE CB  CG1  sing N N 184 
ILE CB  CG2  sing N N 185 
ILE CB  HB   sing N N 186 
ILE CG1 CD1  sing N N 187 
ILE CG1 HG12 sing N N 188 
ILE CG1 HG13 sing N N 189 
ILE CG2 HG21 sing N N 190 
ILE CG2 HG22 sing N N 191 
ILE CG2 HG23 sing N N 192 
ILE CD1 HD11 sing N N 193 
ILE CD1 HD12 sing N N 194 
ILE CD1 HD13 sing N N 195 
ILE OXT HXT  sing N N 196 
LEU N   CA   sing N N 197 
LEU N   H    sing N N 198 
LEU N   H2   sing N N 199 
LEU CA  C    sing N N 200 
LEU CA  CB   sing N N 201 
LEU CA  HA   sing N N 202 
LEU C   O    doub N N 203 
LEU C   OXT  sing N N 204 
LEU CB  CG   sing N N 205 
LEU CB  HB2  sing N N 206 
LEU CB  HB3  sing N N 207 
LEU CG  CD1  sing N N 208 
LEU CG  CD2  sing N N 209 
LEU CG  HG   sing N N 210 
LEU CD1 HD11 sing N N 211 
LEU CD1 HD12 sing N N 212 
LEU CD1 HD13 sing N N 213 
LEU CD2 HD21 sing N N 214 
LEU CD2 HD22 sing N N 215 
LEU CD2 HD23 sing N N 216 
LEU OXT HXT  sing N N 217 
LYS N   CA   sing N N 218 
LYS N   H    sing N N 219 
LYS N   H2   sing N N 220 
LYS CA  C    sing N N 221 
LYS CA  CB   sing N N 222 
LYS CA  HA   sing N N 223 
LYS C   O    doub N N 224 
LYS C   OXT  sing N N 225 
LYS CB  CG   sing N N 226 
LYS CB  HB2  sing N N 227 
LYS CB  HB3  sing N N 228 
LYS CG  CD   sing N N 229 
LYS CG  HG2  sing N N 230 
LYS CG  HG3  sing N N 231 
LYS CD  CE   sing N N 232 
LYS CD  HD2  sing N N 233 
LYS CD  HD3  sing N N 234 
LYS CE  NZ   sing N N 235 
LYS CE  HE2  sing N N 236 
LYS CE  HE3  sing N N 237 
LYS NZ  HZ1  sing N N 238 
LYS NZ  HZ2  sing N N 239 
LYS NZ  HZ3  sing N N 240 
LYS OXT HXT  sing N N 241 
MET N   CA   sing N N 242 
MET N   H    sing N N 243 
MET N   H2   sing N N 244 
MET CA  C    sing N N 245 
MET CA  CB   sing N N 246 
MET CA  HA   sing N N 247 
MET C   O    doub N N 248 
MET C   OXT  sing N N 249 
MET CB  CG   sing N N 250 
MET CB  HB2  sing N N 251 
MET CB  HB3  sing N N 252 
MET CG  SD   sing N N 253 
MET CG  HG2  sing N N 254 
MET CG  HG3  sing N N 255 
MET SD  CE   sing N N 256 
MET CE  HE1  sing N N 257 
MET CE  HE2  sing N N 258 
MET CE  HE3  sing N N 259 
MET OXT HXT  sing N N 260 
PHE N   CA   sing N N 261 
PHE N   H    sing N N 262 
PHE N   H2   sing N N 263 
PHE CA  C    sing N N 264 
PHE CA  CB   sing N N 265 
PHE CA  HA   sing N N 266 
PHE C   O    doub N N 267 
PHE C   OXT  sing N N 268 
PHE CB  CG   sing N N 269 
PHE CB  HB2  sing N N 270 
PHE CB  HB3  sing N N 271 
PHE CG  CD1  doub Y N 272 
PHE CG  CD2  sing Y N 273 
PHE CD1 CE1  sing Y N 274 
PHE CD1 HD1  sing N N 275 
PHE CD2 CE2  doub Y N 276 
PHE CD2 HD2  sing N N 277 
PHE CE1 CZ   doub Y N 278 
PHE CE1 HE1  sing N N 279 
PHE CE2 CZ   sing Y N 280 
PHE CE2 HE2  sing N N 281 
PHE CZ  HZ   sing N N 282 
PHE OXT HXT  sing N N 283 
PRO N   CA   sing N N 284 
PRO N   CD   sing N N 285 
PRO N   H    sing N N 286 
PRO CA  C    sing N N 287 
PRO CA  CB   sing N N 288 
PRO CA  HA   sing N N 289 
PRO C   O    doub N N 290 
PRO C   OXT  sing N N 291 
PRO CB  CG   sing N N 292 
PRO CB  HB2  sing N N 293 
PRO CB  HB3  sing N N 294 
PRO CG  CD   sing N N 295 
PRO CG  HG2  sing N N 296 
PRO CG  HG3  sing N N 297 
PRO CD  HD2  sing N N 298 
PRO CD  HD3  sing N N 299 
PRO OXT HXT  sing N N 300 
SER N   CA   sing N N 301 
SER N   H    sing N N 302 
SER N   H2   sing N N 303 
SER CA  C    sing N N 304 
SER CA  CB   sing N N 305 
SER CA  HA   sing N N 306 
SER C   O    doub N N 307 
SER C   OXT  sing N N 308 
SER CB  OG   sing N N 309 
SER CB  HB2  sing N N 310 
SER CB  HB3  sing N N 311 
SER OG  HG   sing N N 312 
SER OXT HXT  sing N N 313 
SO4 S   O1   doub N N 314 
SO4 S   O2   doub N N 315 
SO4 S   O3   sing N N 316 
SO4 S   O4   sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
VBL C10 O1   sing N N 404 
VBL C10 C3   sing N N 405 
VBL C3  C4   sing N N 406 
VBL C3  C2   sing N N 407 
VBL O   C4   sing N N 408 
VBL C4  C5   sing N N 409 
VBL C2  C1   sing N N 410 
VBL C1  C    sing N N 411 
VBL C5  C6   sing N N 412 
VBL C6  C7   sing N N 413 
VBL C   C11  sing N N 414 
VBL C9  C8   sing N N 415 
VBL C7  C8   sing N N 416 
VBL C11 C12  sing N N 417 
VBL C3  H1   sing N N 418 
VBL C4  H2   sing N N 419 
VBL C5  H3   sing N N 420 
VBL C5  H4   sing N N 421 
VBL C6  H5   sing N N 422 
VBL C6  H6   sing N N 423 
VBL C7  H7   sing N N 424 
VBL C7  H8   sing N N 425 
VBL C8  H9   sing N N 426 
VBL C8  H10  sing N N 427 
VBL C9  H11  sing N N 428 
VBL C9  H12  sing N N 429 
VBL C9  H13  sing N N 430 
VBL C1  H14  sing N N 431 
VBL C1  H15  sing N N 432 
VBL C2  H16  sing N N 433 
VBL C2  H17  sing N N 434 
VBL C10 H18  sing N N 435 
VBL C10 H19  sing N N 436 
VBL C12 H20  sing N N 437 
VBL C12 H21  sing N N 438 
VBL C12 H22  sing N N 439 
VBL C11 H23  sing N N 440 
VBL C11 H24  sing N N 441 
VBL C   H25  sing N N 442 
VBL C   H26  sing N N 443 
VBL O   H27  sing N N 444 
VBL O1  H28  sing N N 445 
# 
_pdbx_audit_support.funding_organization   'French Infrastructure for Integrated Structural Biology (FRISBI)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-10-INBS-05 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 n 
# 
_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   4h18 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QHF 
_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]   0.005948 
_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]   0.005948 
_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]   0.005948 
_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 
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   . ALA A 1 30  ? 8.423  36.270 -8.566  1.00 93.29  ? 30  ALA A N   1 
ATOM   2    C  CA  . ALA A 1 30  ? 7.329  36.728 -7.729  1.00 93.42  ? 30  ALA A CA  1 
ATOM   3    C  C   . ALA A 1 30  ? 6.249  37.365 -8.573  1.00 93.52  ? 30  ALA A C   1 
ATOM   4    O  O   . ALA A 1 30  ? 6.521  37.927 -9.635  1.00 93.48  ? 30  ALA A O   1 
ATOM   5    C  CB  . ALA A 1 30  ? 7.836  37.720 -6.708  1.00 93.58  ? 30  ALA A CB  1 
ATOM   6    N  N   . GLU A 1 31  ? 5.017  37.289 -8.084  1.00 93.55  ? 31  GLU A N   1 
ATOM   7    C  CA  . GLU A 1 31  ? 3.849  37.849 -8.751  1.00 93.77  ? 31  GLU A CA  1 
ATOM   8    C  C   . GLU A 1 31  ? 3.698  39.351 -8.541  1.00 93.50  ? 31  GLU A C   1 
ATOM   9    O  O   . GLU A 1 31  ? 3.033  40.009 -9.340  1.00 94.01  ? 31  GLU A O   1 
ATOM   10   C  CB  . GLU A 1 31  ? 2.599  37.100 -8.297  1.00 96.59  ? 31  GLU A CB  1 
ATOM   11   C  CG  . GLU A 1 31  ? 2.662  35.632 -8.687  1.00 103.12 ? 31  GLU A CG  1 
ATOM   12   C  CD  . GLU A 1 31  ? 2.742  34.609 -7.568  1.00 111.58 ? 31  GLU A CD  1 
ATOM   13   O  OE1 . GLU A 1 31  ? 2.909  35.008 -6.389  1.00 113.76 ? 31  GLU A OE1 1 
ATOM   14   O  OE2 . GLU A 1 31  ? 2.638  33.399 -7.879  1.00 113.36 ? 31  GLU A OE2 1 
ATOM   15   N  N   . VAL A 1 32  ? 4.317  39.899 -7.480  1.00 92.53  ? 32  VAL A N   1 
ATOM   16   C  CA  . VAL A 1 32  ? 4.276  41.322 -7.171  1.00 92.03  ? 32  VAL A CA  1 
ATOM   17   C  C   . VAL A 1 32  ? 5.520  41.954 -7.743  1.00 92.13  ? 32  VAL A C   1 
ATOM   18   O  O   . VAL A 1 32  ? 6.619  41.485 -7.477  1.00 92.21  ? 32  VAL A O   1 
ATOM   19   C  CB  . VAL A 1 32  ? 4.176  41.554 -5.659  1.00 92.19  ? 32  VAL A CB  1 
ATOM   20   C  CG1 . VAL A 1 32  ? 4.190  43.036 -5.340  1.00 92.48  ? 32  VAL A CG1 1 
ATOM   21   C  CG2 . VAL A 1 32  ? 2.927  40.900 -5.093  1.00 92.42  ? 32  VAL A CG2 1 
ATOM   22   N  N   . THR A 1 33  ? 5.353  42.979 -8.568  1.00 92.06  ? 33  THR A N   1 
ATOM   23   C  CA  . THR A 1 33  ? 6.465  43.623 -9.258  1.00 92.62  ? 33  THR A CA  1 
ATOM   24   C  C   . THR A 1 33  ? 7.035  44.800 -8.476  1.00 92.49  ? 33  THR A C   1 
ATOM   25   O  O   . THR A 1 33  ? 6.379  45.329 -7.577  1.00 92.29  ? 33  THR A O   1 
ATOM   26   C  CB  . THR A 1 33  ? 6.020  44.069 -10.683 1.00 94.47  ? 33  THR A CB  1 
ATOM   27   O  OG1 . THR A 1 33  ? 5.237  45.264 -10.623 1.00 95.96  ? 33  THR A OG1 1 
ATOM   28   C  CG2 . THR A 1 33  ? 5.273  42.983 -11.438 1.00 94.88  ? 33  THR A CG2 1 
ATOM   29   N  N   . PRO A 1 34  ? 8.224  45.298 -8.872  1.00 92.51  ? 34  PRO A N   1 
ATOM   30   C  CA  . PRO A 1 34  ? 8.767  46.483 -8.205  1.00 92.79  ? 34  PRO A CA  1 
ATOM   31   C  C   . PRO A 1 34  ? 7.800  47.673 -8.244  1.00 93.69  ? 34  PRO A C   1 
ATOM   32   O  O   . PRO A 1 34  ? 7.612  48.324 -7.227  1.00 94.12  ? 34  PRO A O   1 
ATOM   33   C  CB  . PRO A 1 34  ? 10.037 46.768 -9.009  1.00 93.18  ? 34  PRO A CB  1 
ATOM   34   C  CG  . PRO A 1 34  ? 10.455 45.456 -9.552  1.00 93.39  ? 34  PRO A CG  1 
ATOM   35   C  CD  . PRO A 1 34  ? 9.160  44.786 -9.898  1.00 91.91  ? 34  PRO A CD  1 
ATOM   36   N  N   . ALA A 1 35  ? 7.149  47.919 -9.399  1.00 93.84  ? 35  ALA A N   1 
ATOM   37   C  CA  . ALA A 1 35  ? 6.194  49.015 -9.579  1.00 94.07  ? 35  ALA A CA  1 
ATOM   38   C  C   . ALA A 1 35  ? 4.940  48.846 -8.718  1.00 94.29  ? 35  ALA A C   1 
ATOM   39   O  O   . ALA A 1 35  ? 4.334  49.839 -8.322  1.00 94.45  ? 35  ALA A O   1 
ATOM   40   C  CB  . ALA A 1 35  ? 5.815  49.140 -11.043 1.00 94.14  ? 35  ALA A CB  1 
ATOM   41   N  N   . ASP A 1 36  ? 4.553  47.603 -8.419  1.00 94.28  ? 36  ASP A N   1 
ATOM   42   C  CA  . ASP A 1 36  ? 3.410  47.342 -7.556  1.00 94.86  ? 36  ASP A CA  1 
ATOM   43   C  C   . ASP A 1 36  ? 3.682  47.868 -6.148  1.00 95.04  ? 36  ASP A C   1 
ATOM   44   O  O   . ASP A 1 36  ? 2.818  48.522 -5.570  1.00 95.21  ? 36  ASP A O   1 
ATOM   45   C  CB  . ASP A 1 36  ? 3.100  45.836 -7.482  1.00 96.91  ? 36  ASP A CB  1 
ATOM   46   C  CG  . ASP A 1 36  ? 2.504  45.247 -8.735  1.00 102.28 ? 36  ASP A CG  1 
ATOM   47   O  OD1 . ASP A 1 36  ? 1.934  46.010 -9.532  1.00 103.94 ? 36  ASP A OD1 1 
ATOM   48   O  OD2 . ASP A 1 36  ? 2.627  44.021 -8.928  1.00 104.46 ? 36  ASP A OD2 1 
ATOM   49   N  N   . VAL A 1 37  ? 4.881  47.601 -5.595  1.00 94.90  ? 37  VAL A N   1 
ATOM   50   C  CA  . VAL A 1 37  ? 5.194  48.042 -4.234  1.00 95.04  ? 37  VAL A CA  1 
ATOM   51   C  C   . VAL A 1 37  ? 5.709  49.493 -4.159  1.00 95.08  ? 37  VAL A C   1 
ATOM   52   O  O   . VAL A 1 37  ? 5.542  50.127 -3.117  1.00 94.96  ? 37  VAL A O   1 
ATOM   53   C  CB  . VAL A 1 37  ? 6.142  47.069 -3.482  1.00 95.47  ? 37  VAL A CB  1 
ATOM   54   C  CG1 . VAL A 1 37  ? 5.542  45.674 -3.404  1.00 96.05  ? 37  VAL A CG1 1 
ATOM   55   C  CG2 . VAL A 1 37  ? 7.528  47.026 -4.111  1.00 95.78  ? 37  VAL A CG2 1 
ATOM   56   N  N   . ALA A 1 38  ? 6.325  50.016 -5.242  1.00 95.05  ? 38  ALA A N   1 
ATOM   57   C  CA  . ALA A 1 38  ? 6.886  51.370 -5.241  1.00 95.59  ? 38  ALA A CA  1 
ATOM   58   C  C   . ALA A 1 38  ? 5.837  52.471 -5.192  1.00 96.55  ? 38  ALA A C   1 
ATOM   59   O  O   . ALA A 1 38  ? 6.003  53.455 -4.466  1.00 96.46  ? 38  ALA A O   1 
ATOM   60   C  CB  . ALA A 1 38  ? 7.807  51.569 -6.435  1.00 95.43  ? 38  ALA A CB  1 
ATOM   61   N  N   . GLY A 1 39  ? 4.768  52.293 -5.964  1.00 97.18  ? 39  GLY A N   1 
ATOM   62   C  CA  . GLY A 1 39  ? 3.684  53.255 -6.065  1.00 98.13  ? 39  GLY A CA  1 
ATOM   63   C  C   . GLY A 1 39  ? 4.166  54.607 -6.541  1.00 99.11  ? 39  GLY A C   1 
ATOM   64   O  O   . GLY A 1 39  ? 4.769  54.723 -7.612  1.00 98.96  ? 39  GLY A O   1 
ATOM   65   N  N   . ASP A 1 40  ? 3.961  55.616 -5.687  1.00 99.95  ? 40  ASP A N   1 
ATOM   66   C  CA  . ASP A 1 40  ? 4.312  57.021 -5.892  1.00 101.14 ? 40  ASP A CA  1 
ATOM   67   C  C   . ASP A 1 40  ? 5.816  57.334 -5.780  1.00 101.83 ? 40  ASP A C   1 
ATOM   68   O  O   . ASP A 1 40  ? 6.265  58.318 -6.370  1.00 102.22 ? 40  ASP A O   1 
ATOM   69   C  CB  . ASP A 1 40  ? 3.526  57.900 -4.887  1.00 103.31 ? 40  ASP A CB  1 
ATOM   70   C  CG  . ASP A 1 40  ? 3.901  57.708 -3.413  1.00 108.07 ? 40  ASP A CG  1 
ATOM   71   O  OD1 . ASP A 1 40  ? 3.407  56.727 -2.789  1.00 108.64 ? 40  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A 1 40  ? 4.671  58.546 -2.880  1.00 109.98 ? 40  ASP A OD2 1 
ATOM   73   N  N   . THR A 1 41  ? 6.574  56.517 -5.007  1.00 101.65 ? 41  THR A N   1 
ATOM   74   C  CA  . THR A 1 41  ? 7.998  56.678 -4.673  1.00 101.69 ? 41  THR A CA  1 
ATOM   75   C  C   . THR A 1 41  ? 8.924  57.054 -5.823  1.00 101.96 ? 41  THR A C   1 
ATOM   76   O  O   . THR A 1 41  ? 8.906  56.405 -6.869  1.00 102.16 ? 41  THR A O   1 
ATOM   77   C  CB  . THR A 1 41  ? 8.552  55.415 -3.990  1.00 102.54 ? 41  THR A CB  1 
ATOM   78   O  OG1 . THR A 1 41  ? 7.632  54.932 -3.013  1.00 103.37 ? 41  THR A OG1 1 
ATOM   79   C  CG2 . THR A 1 41  ? 9.896  55.650 -3.348  1.00 102.83 ? 41  THR A CG2 1 
ATOM   80   N  N   . ALA A 1 42  ? 9.758  58.092 -5.612  1.00 101.76 ? 42  ALA A N   1 
ATOM   81   C  CA  . ALA A 1 42  ? 10.761 58.511 -6.583  1.00 102.09 ? 42  ALA A CA  1 
ATOM   82   C  C   . ALA A 1 42  ? 11.818 57.411 -6.607  1.00 102.83 ? 42  ALA A C   1 
ATOM   83   O  O   . ALA A 1 42  ? 12.300 56.999 -5.555  1.00 103.31 ? 42  ALA A O   1 
ATOM   84   C  CB  . ALA A 1 42  ? 11.384 59.826 -6.156  1.00 102.05 ? 42  ALA A CB  1 
ATOM   85   N  N   . LEU A 1 43  ? 12.130 56.890 -7.791  1.00 102.78 ? 43  LEU A N   1 
ATOM   86   C  CA  . LEU A 1 43  ? 13.044 55.763 -7.938  1.00 103.12 ? 43  LEU A CA  1 
ATOM   87   C  C   . LEU A 1 43  ? 14.539 56.120 -7.868  1.00 103.42 ? 43  LEU A C   1 
ATOM   88   O  O   . LEU A 1 43  ? 14.943 57.262 -8.098  1.00 103.62 ? 43  LEU A O   1 
ATOM   89   C  CB  . LEU A 1 43  ? 12.725 55.006 -9.242  1.00 103.30 ? 43  LEU A CB  1 
ATOM   90   C  CG  . LEU A 1 43  ? 11.906 53.710 -9.143  1.00 104.62 ? 43  LEU A CG  1 
ATOM   91   C  CD1 . LEU A 1 43  ? 10.614 53.894 -8.364  1.00 104.98 ? 43  LEU A CD1 1 
ATOM   92   C  CD2 . LEU A 1 43  ? 11.588 53.186 -10.516 1.00 105.33 ? 43  LEU A CD2 1 
ATOM   93   N  N   . SER A 1 44  ? 15.357 55.115 -7.541  1.00 103.29 ? 44  SER A N   1 
ATOM   94   C  CA  . SER A 1 44  ? 16.798 55.261 -7.442  1.00 103.46 ? 44  SER A CA  1 
ATOM   95   C  C   . SER A 1 44  ? 17.441 55.366 -8.829  1.00 103.76 ? 44  SER A C   1 
ATOM   96   O  O   . SER A 1 44  ? 16.892 54.890 -9.820  1.00 103.83 ? 44  SER A O   1 
ATOM   97   C  CB  . SER A 1 44  ? 17.401 54.086 -6.671  1.00 104.18 ? 44  SER A CB  1 
ATOM   98   O  OG  . SER A 1 44  ? 17.477 52.898 -7.441  1.00 106.30 ? 44  SER A OG  1 
ATOM   99   N  N   . THR A 1 45  ? 18.615 55.985 -8.887  1.00 103.54 ? 45  THR A N   1 
ATOM   100  C  CA  . THR A 1 45  ? 19.401 56.087 -10.100 1.00 103.67 ? 45  THR A CA  1 
ATOM   101  C  C   . THR A 1 45  ? 20.660 55.276 -9.847  1.00 103.62 ? 45  THR A C   1 
ATOM   102  O  O   . THR A 1 45  ? 21.385 55.559 -8.893  1.00 103.54 ? 45  THR A O   1 
ATOM   103  C  CB  . THR A 1 45  ? 19.763 57.542 -10.380 1.00 104.99 ? 45  THR A CB  1 
ATOM   104  O  OG1 . THR A 1 45  ? 18.565 58.308 -10.528 1.00 105.93 ? 45  THR A OG1 1 
ATOM   105  C  CG2 . THR A 1 45  ? 20.662 57.690 -11.603 1.00 105.38 ? 45  THR A CG2 1 
ATOM   106  N  N   . ILE A 1 46  ? 20.910 54.259 -10.673 1.00 103.53 ? 46  ILE A N   1 
ATOM   107  C  CA  . ILE A 1 46  ? 22.085 53.420 -10.506 1.00 104.10 ? 46  ILE A CA  1 
ATOM   108  C  C   . ILE A 1 46  ? 23.248 53.911 -11.363 1.00 104.67 ? 46  ILE A C   1 
ATOM   109  O  O   . ILE A 1 46  ? 23.078 54.200 -12.544 1.00 104.86 ? 46  ILE A O   1 
ATOM   110  C  CB  . ILE A 1 46  ? 21.778 51.913 -10.716 1.00 104.59 ? 46  ILE A CB  1 
ATOM   111  C  CG1 . ILE A 1 46  ? 20.821 51.400 -9.633  1.00 105.40 ? 46  ILE A CG1 1 
ATOM   112  C  CG2 . ILE A 1 46  ? 23.051 51.090 -10.643 1.00 105.01 ? 46  ILE A CG2 1 
ATOM   113  C  CD1 . ILE A 1 46  ? 19.466 51.432 -9.928  1.00 106.46 ? 46  ILE A CD1 1 
ATOM   114  N  N   . SER A 1 47  ? 24.427 54.031 -10.752 1.00 104.81 ? 47  SER A N   1 
ATOM   115  C  CA  . SER A 1 47  ? 25.657 54.455 -11.405 1.00 105.39 ? 47  SER A CA  1 
ATOM   116  C  C   . SER A 1 47  ? 26.684 53.318 -11.322 1.00 105.92 ? 47  SER A C   1 
ATOM   117  O  O   . SER A 1 47  ? 26.676 52.535 -10.368 1.00 105.92 ? 47  SER A O   1 
ATOM   118  C  CB  . SER A 1 47  ? 26.218 55.702 -10.725 1.00 106.72 ? 47  SER A CB  1 
ATOM   119  O  OG  . SER A 1 47  ? 25.216 56.659 -10.415 1.00 109.13 ? 47  SER A OG  1 
ATOM   120  N  N   . ASP A 1 48  ? 27.541 53.200 -12.333 1.00 106.29 ? 48  ASP A N   1 
ATOM   121  C  CA  . ASP A 1 48  ? 28.579 52.163 -12.326 1.00 107.30 ? 48  ASP A CA  1 
ATOM   122  C  C   . ASP A 1 48  ? 29.886 52.606 -11.676 1.00 107.74 ? 48  ASP A C   1 
ATOM   123  O  O   . ASP A 1 48  ? 30.829 51.823 -11.598 1.00 107.87 ? 48  ASP A O   1 
ATOM   124  C  CB  . ASP A 1 48  ? 28.832 51.626 -13.733 1.00 109.56 ? 48  ASP A CB  1 
ATOM   125  C  CG  . ASP A 1 48  ? 27.753 50.668 -14.172 1.00 114.78 ? 48  ASP A CG  1 
ATOM   126  O  OD1 . ASP A 1 48  ? 27.722 49.532 -13.650 1.00 115.34 ? 48  ASP A OD1 1 
ATOM   127  O  OD2 . ASP A 1 48  ? 26.921 51.060 -15.024 1.00 117.46 ? 48  ASP A OD2 1 
ATOM   128  N  N   . SER A 1 49  ? 29.944 53.849 -11.204 1.00 107.89 ? 49  SER A N   1 
ATOM   129  C  CA  . SER A 1 49  ? 31.131 54.391 -10.585 1.00 108.52 ? 49  SER A CA  1 
ATOM   130  C  C   . SER A 1 49  ? 30.774 55.142 -9.304  1.00 108.76 ? 49  SER A C   1 
ATOM   131  O  O   . SER A 1 49  ? 29.662 55.665 -9.161  1.00 108.77 ? 49  SER A O   1 
ATOM   132  C  CB  . SER A 1 49  ? 31.866 55.302 -11.567 1.00 110.00 ? 49  SER A CB  1 
ATOM   133  O  OG  . SER A 1 49  ? 30.995 56.243 -12.176 1.00 112.46 ? 49  SER A OG  1 
ATOM   134  N  N   . ALA A 1 50  ? 31.728 55.172 -8.365  1.00 108.67 ? 50  ALA A N   1 
ATOM   135  C  CA  . ALA A 1 50  ? 31.589 55.852 -7.082  1.00 109.03 ? 50  ALA A CA  1 
ATOM   136  C  C   . ALA A 1 50  ? 31.503 57.376 -7.270  1.00 109.40 ? 50  ALA A C   1 
ATOM   137  O  O   . ALA A 1 50  ? 31.959 57.890 -8.296  1.00 109.60 ? 50  ALA A O   1 
ATOM   138  C  CB  . ALA A 1 50  ? 32.777 55.499 -6.194  1.00 109.07 ? 50  ALA A CB  1 
ATOM   139  N  N   . PRO A 1 51  ? 30.930 58.125 -6.301  1.00 109.23 ? 51  PRO A N   1 
ATOM   140  C  CA  . PRO A 1 51  ? 30.879 59.591 -6.451  1.00 109.20 ? 51  PRO A CA  1 
ATOM   141  C  C   . PRO A 1 51  ? 32.280 60.188 -6.505  1.00 109.29 ? 51  PRO A C   1 
ATOM   142  O  O   . PRO A 1 51  ? 33.173 59.713 -5.805  1.00 109.48 ? 51  PRO A O   1 
ATOM   143  C  CB  . PRO A 1 51  ? 30.131 60.058 -5.196  1.00 109.90 ? 51  PRO A CB  1 
ATOM   144  C  CG  . PRO A 1 51  ? 29.452 58.836 -4.657  1.00 110.31 ? 51  PRO A CG  1 
ATOM   145  C  CD  . PRO A 1 51  ? 30.339 57.692 -5.022  1.00 108.74 ? 51  PRO A CD  1 
ATOM   146  N  N   . ALA A 1 52  ? 32.488 61.197 -7.358  1.00 108.98 ? 52  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 52  ? 33.806 61.827 -7.478  1.00 109.08 ? 52  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 52  ? 34.275 62.435 -6.153  1.00 108.80 ? 52  ALA A C   1 
ATOM   149  O  O   . ALA A 1 52  ? 35.481 62.509 -5.903  1.00 108.89 ? 52  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 52  ? 33.795 62.881 -8.573  1.00 109.26 ? 52  ALA A CB  1 
ATOM   151  N  N   . ASP A 1 53  ? 33.326 62.818 -5.281  1.00 108.23 ? 53  ASP A N   1 
ATOM   152  C  CA  . ASP A 1 53  ? 33.677 63.374 -3.984  1.00 108.24 ? 53  ASP A CA  1 
ATOM   153  C  C   . ASP A 1 53  ? 34.036 62.301 -2.931  1.00 107.70 ? 53  ASP A C   1 
ATOM   154  O  O   . ASP A 1 53  ? 34.090 62.615 -1.737  1.00 107.82 ? 53  ASP A O   1 
ATOM   155  C  CB  . ASP A 1 53  ? 32.586 64.334 -3.471  1.00 109.97 ? 53  ASP A CB  1 
ATOM   156  C  CG  . ASP A 1 53  ? 32.779 65.789 -3.891  1.00 114.26 ? 53  ASP A CG  1 
ATOM   157  O  OD1 . ASP A 1 53  ? 33.829 66.100 -4.510  1.00 114.68 ? 53  ASP A OD1 1 
ATOM   158  O  OD2 . ASP A 1 53  ? 31.885 66.617 -3.596  1.00 116.33 ? 53  ASP A OD2 1 
ATOM   159  N  N   . GLU A 1 54  ? 34.306 61.051 -3.362  1.00 106.70 ? 54  GLU A N   1 
ATOM   160  C  CA  . GLU A 1 54  ? 34.712 59.996 -2.439  1.00 106.02 ? 54  GLU A CA  1 
ATOM   161  C  C   . GLU A 1 54  ? 36.138 60.293 -1.975  1.00 105.60 ? 54  GLU A C   1 
ATOM   162  O  O   . GLU A 1 54  ? 37.054 60.328 -2.798  1.00 105.86 ? 54  GLU A O   1 
ATOM   163  C  CB  . GLU A 1 54  ? 34.652 58.619 -3.111  1.00 107.47 ? 54  GLU A CB  1 
ATOM   164  C  CG  . GLU A 1 54  ? 35.247 57.513 -2.258  1.00 111.46 ? 54  GLU A CG  1 
ATOM   165  C  CD  . GLU A 1 54  ? 35.357 56.179 -2.958  1.00 116.26 ? 54  GLU A CD  1 
ATOM   166  O  OE1 . GLU A 1 54  ? 34.473 55.320 -2.737  1.00 116.89 ? 54  GLU A OE1 1 
ATOM   167  O  OE2 . GLU A 1 54  ? 36.329 55.988 -3.724  1.00 117.91 ? 54  GLU A OE2 1 
ATOM   168  N  N   . ALA A 1 55  ? 36.328 60.510 -0.666  1.00 104.79 ? 55  ALA A N   1 
ATOM   169  C  CA  . ALA A 1 55  ? 37.649 60.825 -0.137  1.00 104.37 ? 55  ALA A CA  1 
ATOM   170  C  C   . ALA A 1 55  ? 38.603 59.611 -0.121  1.00 103.71 ? 55  ALA A C   1 
ATOM   171  O  O   . ALA A 1 55  ? 39.669 59.673 -0.728  1.00 103.99 ? 55  ALA A O   1 
ATOM   172  C  CB  . ALA A 1 55  ? 37.536 61.477 1.241   1.00 104.45 ? 55  ALA A CB  1 
ATOM   173  N  N   . SER A 1 56  ? 38.213 58.502 0.522   1.00 102.80 ? 56  SER A N   1 
ATOM   174  C  CA  . SER A 1 56  ? 39.053 57.311 0.586   1.00 102.17 ? 56  SER A CA  1 
ATOM   175  C  C   . SER A 1 56  ? 38.315 56.070 0.086   1.00 101.42 ? 56  SER A C   1 
ATOM   176  O  O   . SER A 1 56  ? 37.083 56.018 0.108   1.00 101.53 ? 56  SER A O   1 
ATOM   177  C  CB  . SER A 1 56  ? 39.561 57.095 2.006   1.00 103.16 ? 56  SER A CB  1 
ATOM   178  O  OG  . SER A 1 56  ? 40.286 58.229 2.451   1.00 105.25 ? 56  SER A OG  1 
ATOM   179  N  N   . ALA A 1 57  ? 39.072 55.073 -0.375  1.00 100.46 ? 57  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 57  ? 38.498 53.845 -0.902  1.00 99.76  ? 57  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 57  ? 37.976 52.955 0.207   1.00 99.12  ? 57  ALA A C   1 
ATOM   182  O  O   . ALA A 1 57  ? 38.675 52.715 1.194   1.00 99.29  ? 57  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 57  ? 39.535 53.095 -1.721  1.00 99.75  ? 57  ALA A CB  1 
ATOM   184  N  N   . PRO A 1 58  ? 36.740 52.441 0.053   1.00 98.27  ? 58  PRO A N   1 
ATOM   185  C  CA  . PRO A 1 58  ? 36.190 51.522 1.064   1.00 97.52  ? 58  PRO A CA  1 
ATOM   186  C  C   . PRO A 1 58  ? 37.048 50.270 1.210   1.00 97.05  ? 58  PRO A C   1 
ATOM   187  O  O   . PRO A 1 58  ? 37.695 49.856 0.246   1.00 97.63  ? 58  PRO A O   1 
ATOM   188  C  CB  . PRO A 1 58  ? 34.820 51.159 0.497   1.00 98.21  ? 58  PRO A CB  1 
ATOM   189  C  CG  . PRO A 1 58  ? 34.499 52.221 -0.506  1.00 98.79  ? 58  PRO A CG  1 
ATOM   190  C  CD  . PRO A 1 58  ? 35.806 52.632 -1.072  1.00 97.56  ? 58  PRO A CD  1 
ATOM   191  N  N   . ARG A 1 59  ? 37.057 49.660 2.397   1.00 96.05  ? 59  ARG A N   1 
ATOM   192  C  CA  . ARG A 1 59  ? 37.872 48.468 2.639   1.00 95.72  ? 59  ARG A CA  1 
ATOM   193  C  C   . ARG A 1 59  ? 37.530 47.301 1.725   1.00 94.79  ? 59  ARG A C   1 
ATOM   194  O  O   . ARG A 1 59  ? 38.399 46.502 1.389   1.00 94.63  ? 59  ARG A O   1 
ATOM   195  C  CB  . ARG A 1 59  ? 37.753 48.020 4.098   1.00 97.34  ? 59  ARG A CB  1 
ATOM   196  C  CG  . ARG A 1 59  ? 38.158 49.079 5.104   1.00 100.55 ? 59  ARG A CG  1 
ATOM   197  C  CD  . ARG A 1 59  ? 37.471 48.807 6.438   1.00 103.43 ? 59  ARG A CD  1 
ATOM   198  N  NE  . ARG A 1 59  ? 37.484 49.936 7.374   1.00 105.71 ? 59  ARG A NE  1 
ATOM   199  C  CZ  . ARG A 1 59  ? 36.739 51.031 7.247   1.00 107.16 ? 59  ARG A CZ  1 
ATOM   200  N  NH1 . ARG A 1 59  ? 35.965 51.197 6.180   1.00 105.93 ? 59  ARG A NH1 1 
ATOM   201  N  NH2 . ARG A 1 59  ? 36.786 51.982 8.169   1.00 107.24 ? 59  ARG A NH2 1 
ATOM   202  N  N   . TRP A 1 60  ? 36.271 47.204 1.324   1.00 94.10  ? 60  TRP A N   1 
ATOM   203  C  CA  . TRP A 1 60  ? 35.800 46.105 0.496   1.00 93.93  ? 60  TRP A CA  1 
ATOM   204  C  C   . TRP A 1 60  ? 36.156 46.220 -0.977  1.00 93.90  ? 60  TRP A C   1 
ATOM   205  O  O   . TRP A 1 60  ? 36.019 45.230 -1.688  1.00 93.98  ? 60  TRP A O   1 
ATOM   206  C  CB  . TRP A 1 60  ? 34.282 45.914 0.667   1.00 93.55  ? 60  TRP A CB  1 
ATOM   207  C  CG  . TRP A 1 60  ? 33.494 47.191 0.571   1.00 93.55  ? 60  TRP A CG  1 
ATOM   208  C  CD1 . TRP A 1 60  ? 33.093 47.991 1.603   1.00 94.15  ? 60  TRP A CD1 1 
ATOM   209  C  CD2 . TRP A 1 60  ? 33.037 47.826 -0.630  1.00 93.48  ? 60  TRP A CD2 1 
ATOM   210  N  NE1 . TRP A 1 60  ? 32.407 49.081 1.118   1.00 94.18  ? 60  TRP A NE1 1 
ATOM   211  C  CE2 . TRP A 1 60  ? 32.337 48.989 -0.249  1.00 94.01  ? 60  TRP A CE2 1 
ATOM   212  C  CE3 . TRP A 1 60  ? 33.128 47.509 -1.994  1.00 93.87  ? 60  TRP A CE3 1 
ATOM   213  C  CZ2 . TRP A 1 60  ? 31.777 49.857 -1.182  1.00 94.56  ? 60  TRP A CZ2 1 
ATOM   214  C  CZ3 . TRP A 1 60  ? 32.544 48.354 -2.911  1.00 94.50  ? 60  TRP A CZ3 1 
ATOM   215  C  CH2 . TRP A 1 60  ? 31.883 49.516 -2.505  1.00 94.57  ? 60  TRP A CH2 1 
ATOM   216  N  N   . ARG A 1 61  ? 36.590 47.405 -1.452  1.00 93.71  ? 61  ARG A N   1 
ATOM   217  C  CA  . ARG A 1 61  ? 36.895 47.586 -2.870  1.00 93.79  ? 61  ARG A CA  1 
ATOM   218  C  C   . ARG A 1 61  ? 37.962 46.620 -3.390  1.00 94.65  ? 61  ARG A C   1 
ATOM   219  O  O   . ARG A 1 61  ? 37.778 46.064 -4.470  1.00 95.01  ? 61  ARG A O   1 
ATOM   220  C  CB  . ARG A 1 61  ? 37.244 49.041 -3.200  1.00 94.17  ? 61  ARG A CB  1 
ATOM   221  C  CG  . ARG A 1 61  ? 37.528 49.264 -4.684  1.00 95.83  ? 61  ARG A CG  1 
ATOM   222  C  CD  . ARG A 1 61  ? 37.571 50.726 -5.041  1.00 97.70  ? 61  ARG A CD  1 
ATOM   223  N  NE  . ARG A 1 61  ? 36.257 51.345 -4.883  1.00 99.36  ? 61  ARG A NE  1 
ATOM   224  C  CZ  . ARG A 1 61  ? 36.059 52.614 -4.546  1.00 101.08 ? 61  ARG A CZ  1 
ATOM   225  N  NH1 . ARG A 1 61  ? 37.092 53.416 -4.318  1.00 101.05 ? 61  ARG A NH1 1 
ATOM   226  N  NH2 . ARG A 1 61  ? 34.826 53.090 -4.424  1.00 100.71 ? 61  ARG A NH2 1 
ATOM   227  N  N   . ALA A 1 62  ? 39.031 46.363 -2.617  1.00 94.86  ? 62  ALA A N   1 
ATOM   228  C  CA  . ALA A 1 62  ? 40.080 45.432 -3.037  1.00 95.61  ? 62  ALA A CA  1 
ATOM   229  C  C   . ALA A 1 62  ? 39.555 44.016 -3.234  1.00 96.58  ? 62  ALA A C   1 
ATOM   230  O  O   . ALA A 1 62  ? 40.048 43.301 -4.099  1.00 96.70  ? 62  ALA A O   1 
ATOM   231  C  CB  . ALA A 1 62  ? 41.211 45.424 -2.032  1.00 95.81  ? 62  ALA A CB  1 
ATOM   232  N  N   . HIS A 1 63  ? 38.554 43.613 -2.438  1.00 97.25  ? 63  HIS A N   1 
ATOM   233  C  CA  . HIS A 1 63  ? 37.926 42.295 -2.536  1.00 98.10  ? 63  HIS A CA  1 
ATOM   234  C  C   . HIS A 1 63  ? 37.103 42.188 -3.819  1.00 98.21  ? 63  HIS A C   1 
ATOM   235  O  O   . HIS A 1 63  ? 37.092 41.136 -4.452  1.00 98.07  ? 63  HIS A O   1 
ATOM   236  C  CB  . HIS A 1 63  ? 37.047 42.020 -1.307  1.00 99.45  ? 63  HIS A CB  1 
ATOM   237  C  CG  . HIS A 1 63  ? 37.811 41.957 -0.021  1.00 102.58 ? 63  HIS A CG  1 
ATOM   238  N  ND1 . HIS A 1 63  ? 38.304 40.757 0.471   1.00 104.76 ? 63  HIS A ND1 1 
ATOM   239  C  CD2 . HIS A 1 63  ? 38.151 42.951 0.833   1.00 103.90 ? 63  HIS A CD2 1 
ATOM   240  C  CE1 . HIS A 1 63  ? 38.923 41.058 1.602   1.00 105.35 ? 63  HIS A CE1 1 
ATOM   241  N  NE2 . HIS A 1 63  ? 38.856 42.366 1.864   1.00 105.17 ? 63  HIS A NE2 1 
ATOM   242  N  N   . VAL A 1 64  ? 36.421 43.273 -4.201  1.00 98.40  ? 64  VAL A N   1 
ATOM   243  C  CA  . VAL A 1 64  ? 35.647 43.325 -5.435  1.00 99.25  ? 64  VAL A CA  1 
ATOM   244  C  C   . VAL A 1 64  ? 36.604 43.242 -6.622  1.00 99.92  ? 64  VAL A C   1 
ATOM   245  O  O   . VAL A 1 64  ? 36.384 42.449 -7.535  1.00 100.04 ? 64  VAL A O   1 
ATOM   246  C  CB  . VAL A 1 64  ? 34.790 44.617 -5.494  1.00 99.98  ? 64  VAL A CB  1 
ATOM   247  C  CG1 . VAL A 1 64  ? 34.253 44.870 -6.898  1.00 100.46 ? 64  VAL A CG1 1 
ATOM   248  C  CG2 . VAL A 1 64  ? 33.652 44.566 -4.483  1.00 100.53 ? 64  VAL A CG2 1 
ATOM   249  N  N   . ASN A 1 65  ? 37.680 44.045 -6.591  1.00 100.23 ? 65  ASN A N   1 
ATOM   250  C  CA  . ASN A 1 65  ? 38.668 44.138 -7.665  1.00 100.92 ? 65  ASN A CA  1 
ATOM   251  C  C   . ASN A 1 65  ? 39.428 42.834 -7.926  1.00 101.59 ? 65  ASN A C   1 
ATOM   252  O  O   . ASN A 1 65  ? 39.877 42.603 -9.048  1.00 101.83 ? 65  ASN A O   1 
ATOM   253  C  CB  . ASN A 1 65  ? 39.633 45.304 -7.419  1.00 101.91 ? 65  ASN A CB  1 
ATOM   254  C  CG  . ASN A 1 65  ? 38.992 46.671 -7.541  1.00 104.89 ? 65  ASN A CG  1 
ATOM   255  O  OD1 . ASN A 1 65  ? 37.897 46.837 -8.097  1.00 105.64 ? 65  ASN A OD1 1 
ATOM   256  N  ND2 . ASN A 1 65  ? 39.663 47.684 -7.015  1.00 105.78 ? 65  ASN A ND2 1 
ATOM   257  N  N   . ALA A 1 66  ? 39.567 41.986 -6.904  1.00 101.75 ? 66  ALA A N   1 
ATOM   258  C  CA  . ALA A 1 66  ? 40.250 40.697 -7.034  1.00 102.46 ? 66  ALA A CA  1 
ATOM   259  C  C   . ALA A 1 66  ? 39.306 39.546 -7.445  1.00 103.31 ? 66  ALA A C   1 
ATOM   260  O  O   . ALA A 1 66  ? 39.775 38.459 -7.792  1.00 103.82 ? 66  ALA A O   1 
ATOM   261  C  CB  . ALA A 1 66  ? 40.951 40.351 -5.732  1.00 102.49 ? 66  ALA A CB  1 
ATOM   262  N  N   . ALA A 1 67  ? 37.986 39.772 -7.388  1.00 103.16 ? 67  ALA A N   1 
ATOM   263  C  CA  . ALA A 1 67  ? 36.990 38.773 -7.733  1.00 103.44 ? 67  ALA A CA  1 
ATOM   264  C  C   . ALA A 1 67  ? 36.713 38.762 -9.248  1.00 103.65 ? 67  ALA A C   1 
ATOM   265  O  O   . ALA A 1 67  ? 37.115 39.688 -9.951  1.00 103.95 ? 67  ALA A O   1 
ATOM   266  C  CB  . ALA A 1 67  ? 35.713 39.052 -6.948  1.00 103.62 ? 67  ALA A CB  1 
ATOM   267  N  N   . ASP A 1 68  ? 36.013 37.725 -9.761  1.00 103.32 ? 68  ASP A N   1 
ATOM   268  C  CA  . ASP A 1 68  ? 35.642 37.606 -11.167 1.00 103.49 ? 68  ASP A CA  1 
ATOM   269  C  C   . ASP A 1 68  ? 34.986 38.889 -11.696 1.00 103.35 ? 68  ASP A C   1 
ATOM   270  O  O   . ASP A 1 68  ? 34.412 39.659 -10.920 1.00 103.64 ? 68  ASP A O   1 
ATOM   271  C  CB  . ASP A 1 68  ? 34.683 36.425 -11.337 1.00 105.35 ? 68  ASP A CB  1 
ATOM   272  C  CG  . ASP A 1 68  ? 34.343 36.060 -12.768 1.00 110.52 ? 68  ASP A CG  1 
ATOM   273  O  OD1 . ASP A 1 68  ? 33.495 36.750 -13.372 1.00 111.39 ? 68  ASP A OD1 1 
ATOM   274  O  OD2 . ASP A 1 68  ? 34.909 35.073 -13.276 1.00 112.90 ? 68  ASP A OD2 1 
ATOM   275  N  N   . GLU A 1 69  ? 35.101 39.131 -13.011 1.00 102.65 ? 69  GLU A N   1 
ATOM   276  C  CA  . GLU A 1 69  ? 34.516 40.312 -13.644 1.00 102.24 ? 69  GLU A CA  1 
ATOM   277  C  C   . GLU A 1 69  ? 33.021 40.447 -13.390 1.00 101.16 ? 69  GLU A C   1 
ATOM   278  O  O   . GLU A 1 69  ? 32.501 41.558 -13.416 1.00 101.61 ? 69  GLU A O   1 
ATOM   279  C  CB  . GLU A 1 69  ? 34.840 40.368 -15.147 1.00 104.91 ? 69  GLU A CB  1 
ATOM   280  C  CG  . GLU A 1 69  ? 34.058 39.405 -16.028 1.00 110.07 ? 69  GLU A CG  1 
ATOM   281  C  CD  . GLU A 1 69  ? 34.589 39.256 -17.442 1.00 115.87 ? 69  GLU A CD  1 
ATOM   282  O  OE1 . GLU A 1 69  ? 34.925 40.286 -18.073 1.00 116.51 ? 69  GLU A OE1 1 
ATOM   283  O  OE2 . GLU A 1 69  ? 34.665 38.101 -17.922 1.00 117.66 ? 69  GLU A OE2 1 
ATOM   284  N  N   . ARG A 1 70  ? 32.335 39.330 -13.114 1.00 99.74  ? 70  ARG A N   1 
ATOM   285  C  CA  . ARG A 1 70  ? 30.915 39.342 -12.802 1.00 98.75  ? 70  ARG A CA  1 
ATOM   286  C  C   . ARG A 1 70  ? 30.598 40.021 -11.465 1.00 98.41  ? 70  ARG A C   1 
ATOM   287  O  O   . ARG A 1 70  ? 29.441 40.337 -11.215 1.00 98.65  ? 70  ARG A O   1 
ATOM   288  C  CB  . ARG A 1 70  ? 30.347 37.929 -12.841 1.00 98.87  ? 70  ARG A CB  1 
ATOM   289  C  CG  . ARG A 1 70  ? 30.206 37.393 -14.256 1.00 99.69  ? 70  ARG A CG  1 
ATOM   290  C  CD  . ARG A 1 70  ? 29.989 35.895 -14.274 1.00 100.70 ? 70  ARG A CD  1 
ATOM   291  N  NE  . ARG A 1 70  ? 28.883 35.492 -13.409 1.00 101.30 ? 70  ARG A NE  1 
ATOM   292  C  CZ  . ARG A 1 70  ? 28.734 34.274 -12.899 1.00 101.76 ? 70  ARG A CZ  1 
ATOM   293  N  NH1 . ARG A 1 70  ? 29.621 33.322 -13.163 1.00 100.04 ? 70  ARG A NH1 1 
ATOM   294  N  NH2 . ARG A 1 70  ? 27.707 34.004 -12.106 1.00 101.54 ? 70  ARG A NH2 1 
ATOM   295  N  N   . VAL A 1 71  ? 31.605 40.252 -10.605 1.00 97.76  ? 71  VAL A N   1 
ATOM   296  C  CA  . VAL A 1 71  ? 31.386 40.955 -9.347  1.00 97.43  ? 71  VAL A CA  1 
ATOM   297  C  C   . VAL A 1 71  ? 31.627 42.416 -9.621  1.00 97.15  ? 71  VAL A C   1 
ATOM   298  O  O   . VAL A 1 71  ? 32.695 42.785 -10.103 1.00 97.24  ? 71  VAL A O   1 
ATOM   299  C  CB  . VAL A 1 71  ? 32.266 40.441 -8.200  1.00 97.85  ? 71  VAL A CB  1 
ATOM   300  C  CG1 . VAL A 1 71  ? 31.964 41.201 -6.916  1.00 98.40  ? 71  VAL A CG1 1 
ATOM   301  C  CG2 . VAL A 1 71  ? 32.073 38.945 -7.996  1.00 98.08  ? 71  VAL A CG2 1 
ATOM   302  N  N   . LYS A 1 72  ? 30.617 43.246 -9.379  1.00 96.79  ? 72  LYS A N   1 
ATOM   303  C  CA  . LYS A 1 72  ? 30.683 44.659 -9.710  1.00 96.95  ? 72  LYS A CA  1 
ATOM   304  C  C   . LYS A 1 72  ? 30.356 45.575 -8.559  1.00 96.69  ? 72  LYS A C   1 
ATOM   305  O  O   . LYS A 1 72  ? 29.552 45.242 -7.697  1.00 96.86  ? 72  LYS A O   1 
ATOM   306  C  CB  . LYS A 1 72  ? 29.719 44.964 -10.874 1.00 98.93  ? 72  LYS A CB  1 
ATOM   307  C  CG  . LYS A 1 72  ? 29.908 44.027 -12.059 1.00 103.47 ? 72  LYS A CG  1 
ATOM   308  C  CD  . LYS A 1 72  ? 29.001 44.323 -13.224 1.00 108.25 ? 72  LYS A CD  1 
ATOM   309  C  CE  . LYS A 1 72  ? 29.302 43.363 -14.351 1.00 112.22 ? 72  LYS A CE  1 
ATOM   310  N  NZ  . LYS A 1 72  ? 28.687 43.803 -15.631 1.00 114.74 ? 72  LYS A NZ  1 
ATOM   311  N  N   . GLU A 1 73  ? 30.945 46.763 -8.581  1.00 95.99  ? 73  GLU A N   1 
ATOM   312  C  CA  . GLU A 1 73  ? 30.636 47.788 -7.607  1.00 95.69  ? 73  GLU A CA  1 
ATOM   313  C  C   . GLU A 1 73  ? 29.646 48.750 -8.284  1.00 95.26  ? 73  GLU A C   1 
ATOM   314  O  O   . GLU A 1 73  ? 29.943 49.304 -9.346  1.00 95.28  ? 73  GLU A O   1 
ATOM   315  C  CB  . GLU A 1 73  ? 31.915 48.526 -7.197  1.00 97.42  ? 73  GLU A CB  1 
ATOM   316  C  CG  . GLU A 1 73  ? 31.683 49.789 -6.391  1.00 100.76 ? 73  GLU A CG  1 
ATOM   317  C  CD  . GLU A 1 73  ? 32.959 50.509 -6.004  1.00 106.15 ? 73  GLU A CD  1 
ATOM   318  O  OE1 . GLU A 1 73  ? 34.033 49.864 -5.986  1.00 106.52 ? 73  GLU A OE1 1 
ATOM   319  O  OE2 . GLU A 1 73  ? 32.880 51.723 -5.710  1.00 108.56 ? 73  GLU A OE2 1 
ATOM   320  N  N   . MET A 1 74  ? 28.456 48.904 -7.708  1.00 94.47  ? 74  MET A N   1 
ATOM   321  C  CA  . MET A 1 74  ? 27.458 49.826 -8.235  1.00 94.47  ? 74  MET A CA  1 
ATOM   322  C  C   . MET A 1 74  ? 27.052 50.809 -7.153  1.00 94.13  ? 74  MET A C   1 
ATOM   323  O  O   . MET A 1 74  ? 27.281 50.549 -5.975  1.00 94.45  ? 74  MET A O   1 
ATOM   324  C  CB  . MET A 1 74  ? 26.237 49.077 -8.770  1.00 95.51  ? 74  MET A CB  1 
ATOM   325  C  CG  . MET A 1 74  ? 26.584 48.125 -9.876  1.00 98.63  ? 74  MET A CG  1 
ATOM   326  S  SD  . MET A 1 74  ? 25.145 47.260 -10.503 1.00 104.05 ? 74  MET A SD  1 
ATOM   327  C  CE  . MET A 1 74  ? 25.903 46.212 -11.702 1.00 100.69 ? 74  MET A CE  1 
ATOM   328  N  N   . TRP A 1 75  ? 26.476 51.946 -7.540  1.00 93.44  ? 75  TRP A N   1 
ATOM   329  C  CA  . TRP A 1 75  ? 26.064 52.948 -6.571  1.00 93.47  ? 75  TRP A CA  1 
ATOM   330  C  C   . TRP A 1 75  ? 24.651 53.378 -6.854  1.00 94.08  ? 75  TRP A C   1 
ATOM   331  O  O   . TRP A 1 75  ? 24.344 53.720 -7.983  1.00 94.53  ? 75  TRP A O   1 
ATOM   332  C  CB  . TRP A 1 75  ? 27.021 54.145 -6.593  1.00 92.82  ? 75  TRP A CB  1 
ATOM   333  C  CG  . TRP A 1 75  ? 28.338 53.856 -5.946  1.00 92.20  ? 75  TRP A CG  1 
ATOM   334  C  CD1 . TRP A 1 75  ? 29.368 53.127 -6.463  1.00 92.72  ? 75  TRP A CD1 1 
ATOM   335  C  CD2 . TRP A 1 75  ? 28.765 54.300 -4.656  1.00 91.87  ? 75  TRP A CD2 1 
ATOM   336  N  NE1 . TRP A 1 75  ? 30.412 53.086 -5.568  1.00 92.89  ? 75  TRP A NE1 1 
ATOM   337  C  CE2 . TRP A 1 75  ? 30.070 53.808 -4.454  1.00 92.60  ? 75  TRP A CE2 1 
ATOM   338  C  CE3 . TRP A 1 75  ? 28.174 55.079 -3.656  1.00 92.22  ? 75  TRP A CE3 1 
ATOM   339  C  CZ2 . TRP A 1 75  ? 30.785 54.060 -3.287  1.00 93.18  ? 75  TRP A CZ2 1 
ATOM   340  C  CZ3 . TRP A 1 75  ? 28.886 55.328 -2.501  1.00 93.02  ? 75  TRP A CZ3 1 
ATOM   341  C  CH2 . TRP A 1 75  ? 30.173 54.822 -2.325  1.00 93.18  ? 75  TRP A CH2 1 
ATOM   342  N  N   . ALA A 1 76  ? 23.784 53.353 -5.844  1.00 93.92  ? 76  ALA A N   1 
ATOM   343  C  CA  . ALA A 1 76  ? 22.387 53.712 -6.026  1.00 94.27  ? 76  ALA A CA  1 
ATOM   344  C  C   . ALA A 1 76  ? 22.047 54.955 -5.248  1.00 94.54  ? 76  ALA A C   1 
ATOM   345  O  O   . ALA A 1 76  ? 22.209 54.977 -4.028  1.00 94.89  ? 76  ALA A O   1 
ATOM   346  C  CB  . ALA A 1 76  ? 21.497 52.570 -5.573  1.00 94.48  ? 76  ALA A CB  1 
ATOM   347  N  N   . TYR A 1 77  ? 21.555 55.987 -5.939  1.00 94.14  ? 77  TYR A N   1 
ATOM   348  C  CA  . TYR A 1 77  ? 21.170 57.213 -5.266  1.00 94.12  ? 77  TYR A CA  1 
ATOM   349  C  C   . TYR A 1 77  ? 19.774 57.047 -4.680  1.00 94.81  ? 77  TYR A C   1 
ATOM   350  O  O   . TYR A 1 77  ? 18.842 56.667 -5.381  1.00 95.15  ? 77  TYR A O   1 
ATOM   351  C  CB  . TYR A 1 77  ? 21.247 58.417 -6.212  1.00 93.58  ? 77  TYR A CB  1 
ATOM   352  C  CG  . TYR A 1 77  ? 20.728 59.685 -5.574  1.00 93.67  ? 77  TYR A CG  1 
ATOM   353  C  CD1 . TYR A 1 77  ? 21.469 60.357 -4.614  1.00 94.28  ? 77  TYR A CD1 1 
ATOM   354  C  CD2 . TYR A 1 77  ? 19.472 60.179 -5.889  1.00 94.23  ? 77  TYR A CD2 1 
ATOM   355  C  CE1 . TYR A 1 77  ? 20.978 61.500 -3.994  1.00 94.93  ? 77  TYR A CE1 1 
ATOM   356  C  CE2 . TYR A 1 77  ? 18.966 61.312 -5.268  1.00 94.92  ? 77  TYR A CE2 1 
ATOM   357  C  CZ  . TYR A 1 77  ? 19.721 61.971 -4.320  1.00 95.64  ? 77  TYR A CZ  1 
ATOM   358  O  OH  . TYR A 1 77  ? 19.204 63.092 -3.722  1.00 97.12  ? 77  TYR A OH  1 
ATOM   359  N  N   . SER A 1 78  ? 19.627 57.342 -3.392  1.00 94.77  ? 78  SER A N   1 
ATOM   360  C  CA  . SER A 1 78  ? 18.351 57.257 -2.698  1.00 94.82  ? 78  SER A CA  1 
ATOM   361  C  C   . SER A 1 78  ? 17.755 58.639 -2.598  1.00 95.02  ? 78  SER A C   1 
ATOM   362  O  O   . SER A 1 78  ? 18.278 59.458 -1.852  1.00 95.20  ? 78  SER A O   1 
ATOM   363  C  CB  . SER A 1 78  ? 18.554 56.713 -1.286  1.00 95.55  ? 78  SER A CB  1 
ATOM   364  O  OG  . SER A 1 78  ? 17.357 56.754 -0.524  1.00 97.21  ? 78  SER A OG  1 
ATOM   365  N  N   . PRO A 1 79  ? 16.642 58.919 -3.291  1.00 94.97  ? 79  PRO A N   1 
ATOM   366  C  CA  . PRO A 1 79  ? 16.033 60.256 -3.180  1.00 94.78  ? 79  PRO A CA  1 
ATOM   367  C  C   . PRO A 1 79  ? 15.537 60.606 -1.770  1.00 94.71  ? 79  PRO A C   1 
ATOM   368  O  O   . PRO A 1 79  ? 15.699 61.748 -1.340  1.00 95.01  ? 79  PRO A O   1 
ATOM   369  C  CB  . PRO A 1 79  ? 14.872 60.192 -4.180  1.00 95.35  ? 79  PRO A CB  1 
ATOM   370  C  CG  . PRO A 1 79  ? 15.251 59.100 -5.140  1.00 95.87  ? 79  PRO A CG  1 
ATOM   371  C  CD  . PRO A 1 79  ? 15.924 58.081 -4.269  1.00 94.53  ? 79  PRO A CD  1 
ATOM   372  N  N   . SER A 1 80  ? 14.941 59.637 -1.045  1.00 94.11  ? 80  SER A N   1 
ATOM   373  C  CA  . SER A 1 80  ? 14.407 59.896 0.297   1.00 93.87  ? 80  SER A CA  1 
ATOM   374  C  C   . SER A 1 80  ? 15.476 60.218 1.325   1.00 93.50  ? 80  SER A C   1 
ATOM   375  O  O   . SER A 1 80  ? 15.248 61.028 2.224   1.00 93.88  ? 80  SER A O   1 
ATOM   376  C  CB  . SER A 1 80  ? 13.542 58.739 0.781   1.00 95.13  ? 80  SER A CB  1 
ATOM   377  O  OG  . SER A 1 80  ? 14.282 57.536 0.894   1.00 97.32  ? 80  SER A OG  1 
ATOM   378  N  N   . MET A 1 81  ? 16.634 59.590 1.203   1.00 92.69  ? 81  MET A N   1 
ATOM   379  C  CA  . MET A 1 81  ? 17.732 59.831 2.131   1.00 92.30  ? 81  MET A CA  1 
ATOM   380  C  C   . MET A 1 81  ? 18.713 60.889 1.622   1.00 92.54  ? 81  MET A C   1 
ATOM   381  O  O   . MET A 1 81  ? 19.499 61.402 2.419   1.00 92.96  ? 81  MET A O   1 
ATOM   382  C  CB  . MET A 1 81  ? 18.496 58.520 2.402   1.00 92.05  ? 81  MET A CB  1 
ATOM   383  C  CG  . MET A 1 81  ? 17.667 57.460 3.102   1.00 92.40  ? 81  MET A CG  1 
ATOM   384  S  SD  . MET A 1 81  ? 18.631 56.050 3.714   1.00 88.42  ? 81  MET A SD  1 
ATOM   385  C  CE  . MET A 1 81  ? 18.717 55.042 2.295   1.00 81.95  ? 81  MET A CE  1 
ATOM   386  N  N   . ASP A 1 82  ? 18.691 61.195 0.297   1.00 92.08  ? 82  ASP A N   1 
ATOM   387  C  CA  . ASP A 1 82  ? 19.644 62.062 -0.417  1.00 91.97  ? 82  ASP A CA  1 
ATOM   388  C  C   . ASP A 1 82  ? 21.044 61.462 -0.200  1.00 91.53  ? 82  ASP A C   1 
ATOM   389  O  O   . ASP A 1 82  ? 21.982 62.147 0.210   1.00 91.95  ? 82  ASP A O   1 
ATOM   390  C  CB  . ASP A 1 82  ? 19.549 63.530 0.045   1.00 93.78  ? 82  ASP A CB  1 
ATOM   391  C  CG  . ASP A 1 82  ? 20.423 64.486 -0.744  1.00 98.27  ? 82  ASP A CG  1 
ATOM   392  O  OD1 . ASP A 1 82  ? 20.665 64.218 -1.937  1.00 98.96  ? 82  ASP A OD1 1 
ATOM   393  O  OD2 . ASP A 1 82  ? 20.886 65.489 -0.158  1.00 100.24 ? 82  ASP A OD2 1 
ATOM   394  N  N   . ARG A 1 83  ? 21.155 60.141 -0.407  1.00 90.41  ? 83  ARG A N   1 
ATOM   395  C  CA  . ARG A 1 83  ? 22.370 59.407 -0.112  1.00 89.48  ? 83  ARG A CA  1 
ATOM   396  C  C   . ARG A 1 83  ? 22.761 58.531 -1.265  1.00 88.57  ? 83  ARG A C   1 
ATOM   397  O  O   . ARG A 1 83  ? 21.904 57.955 -1.913  1.00 88.59  ? 83  ARG A O   1 
ATOM   398  C  CB  . ARG A 1 83  ? 22.128 58.516 1.135   1.00 90.42  ? 83  ARG A CB  1 
ATOM   399  C  CG  . ARG A 1 83  ? 23.356 57.729 1.577   1.00 93.15  ? 83  ARG A CG  1 
ATOM   400  C  CD  . ARG A 1 83  ? 23.065 56.601 2.549   1.00 95.41  ? 83  ARG A CD  1 
ATOM   401  N  NE  . ARG A 1 83  ? 22.623 57.085 3.856   1.00 97.55  ? 83  ARG A NE  1 
ATOM   402  C  CZ  . ARG A 1 83  ? 23.156 56.720 5.019   1.00 98.01  ? 83  ARG A CZ  1 
ATOM   403  N  NH1 . ARG A 1 83  ? 24.187 55.881 5.053   1.00 96.98  ? 83  ARG A NH1 1 
ATOM   404  N  NH2 . ARG A 1 83  ? 22.671 57.201 6.156   1.00 97.02  ? 83  ARG A NH2 1 
ATOM   405  N  N   . ASN A 1 84  ? 24.059 58.409 -1.515  1.00 87.88  ? 84  ASN A N   1 
ATOM   406  C  CA  . ASN A 1 84  ? 24.572 57.494 -2.516  1.00 87.62  ? 84  ASN A CA  1 
ATOM   407  C  C   . ASN A 1 84  ? 24.940 56.247 -1.745  1.00 87.29  ? 84  ASN A C   1 
ATOM   408  O  O   . ASN A 1 84  ? 25.813 56.286 -0.878  1.00 87.45  ? 84  ASN A O   1 
ATOM   409  C  CB  . ASN A 1 84  ? 25.803 58.057 -3.192  1.00 88.75  ? 84  ASN A CB  1 
ATOM   410  C  CG  . ASN A 1 84  ? 25.479 59.191 -4.103  1.00 92.22  ? 84  ASN A CG  1 
ATOM   411  O  OD1 . ASN A 1 84  ? 24.661 59.062 -5.023  1.00 93.82  ? 84  ASN A OD1 1 
ATOM   412  N  ND2 . ASN A 1 84  ? 26.108 60.325 -3.858  1.00 92.78  ? 84  ASN A ND2 1 
ATOM   413  N  N   . VAL A 1 85  ? 24.255 55.150 -2.034  1.00 86.64  ? 85  VAL A N   1 
ATOM   414  C  CA  . VAL A 1 85  ? 24.454 53.892 -1.346  1.00 86.14  ? 85  VAL A CA  1 
ATOM   415  C  C   . VAL A 1 85  ? 25.304 52.936 -2.187  1.00 85.94  ? 85  VAL A C   1 
ATOM   416  O  O   . VAL A 1 85  ? 24.930 52.603 -3.305  1.00 86.16  ? 85  VAL A O   1 
ATOM   417  C  CB  . VAL A 1 85  ? 23.074 53.270 -1.015  1.00 86.28  ? 85  VAL A CB  1 
ATOM   418  C  CG1 . VAL A 1 85  ? 23.228 51.932 -0.299  1.00 86.55  ? 85  VAL A CG1 1 
ATOM   419  C  CG2 . VAL A 1 85  ? 22.203 54.236 -0.210  1.00 86.44  ? 85  VAL A CG2 1 
ATOM   420  N  N   . PRO A 1 86  ? 26.441 52.469 -1.657  1.00 85.45  ? 86  PRO A N   1 
ATOM   421  C  CA  . PRO A 1 86  ? 27.260 51.503 -2.402  1.00 85.57  ? 86  PRO A CA  1 
ATOM   422  C  C   . PRO A 1 86  ? 26.652 50.101 -2.364  1.00 86.20  ? 86  PRO A C   1 
ATOM   423  O  O   . PRO A 1 86  ? 26.052 49.711 -1.366  1.00 86.26  ? 86  PRO A O   1 
ATOM   424  C  CB  . PRO A 1 86  ? 28.597 51.530 -1.663  1.00 86.03  ? 86  PRO A CB  1 
ATOM   425  C  CG  . PRO A 1 86  ? 28.263 51.940 -0.292  1.00 86.38  ? 86  PRO A CG  1 
ATOM   426  C  CD  . PRO A 1 86  ? 27.043 52.812 -0.358  1.00 84.81  ? 86  PRO A CD  1 
ATOM   427  N  N   . LEU A 1 87  ? 26.792 49.350 -3.454  1.00 86.34  ? 87  LEU A N   1 
ATOM   428  C  CA  . LEU A 1 87  ? 26.240 48.005 -3.574  1.00 86.62  ? 87  LEU A CA  1 
ATOM   429  C  C   . LEU A 1 87  ? 27.336 47.087 -4.146  1.00 87.42  ? 87  LEU A C   1 
ATOM   430  O  O   . LEU A 1 87  ? 27.987 47.459 -5.122  1.00 87.95  ? 87  LEU A O   1 
ATOM   431  C  CB  . LEU A 1 87  ? 25.082 48.031 -4.598  1.00 86.37  ? 87  LEU A CB  1 
ATOM   432  C  CG  . LEU A 1 87  ? 23.631 48.330 -4.194  1.00 87.30  ? 87  LEU A CG  1 
ATOM   433  C  CD1 . LEU A 1 87  ? 23.466 49.615 -3.464  1.00 87.59  ? 87  LEU A CD1 1 
ATOM   434  C  CD2 . LEU A 1 87  ? 22.781 48.437 -5.415  1.00 88.04  ? 87  LEU A CD2 1 
ATOM   435  N  N   . VAL A 1 88  ? 27.541 45.903 -3.557  1.00 87.31  ? 88  VAL A N   1 
ATOM   436  C  CA  . VAL A 1 88  ? 28.463 44.921 -4.125  1.00 87.75  ? 88  VAL A CA  1 
ATOM   437  C  C   . VAL A 1 88  ? 27.538 43.931 -4.805  1.00 88.82  ? 88  VAL A C   1 
ATOM   438  O  O   . VAL A 1 88  ? 26.701 43.321 -4.146  1.00 89.11  ? 88  VAL A O   1 
ATOM   439  C  CB  . VAL A 1 88  ? 29.390 44.234 -3.102  1.00 87.86  ? 88  VAL A CB  1 
ATOM   440  C  CG1 . VAL A 1 88  ? 30.039 42.998 -3.709  1.00 87.98  ? 88  VAL A CG1 1 
ATOM   441  C  CG2 . VAL A 1 88  ? 30.452 45.202 -2.608  1.00 88.28  ? 88  VAL A CG2 1 
ATOM   442  N  N   . VAL A 1 89  ? 27.627 43.826 -6.132  1.00 89.07  ? 89  VAL A N   1 
ATOM   443  C  CA  . VAL A 1 89  ? 26.714 42.996 -6.898  1.00 89.43  ? 89  VAL A CA  1 
ATOM   444  C  C   . VAL A 1 89  ? 27.382 41.817 -7.587  1.00 90.78  ? 89  VAL A C   1 
ATOM   445  O  O   . VAL A 1 89  ? 28.276 42.007 -8.397  1.00 91.18  ? 89  VAL A O   1 
ATOM   446  C  CB  . VAL A 1 89  ? 25.957 43.868 -7.927  1.00 89.15  ? 89  VAL A CB  1 
ATOM   447  C  CG1 . VAL A 1 89  ? 24.950 43.041 -8.710  1.00 89.25  ? 89  VAL A CG1 1 
ATOM   448  C  CG2 . VAL A 1 89  ? 25.277 45.057 -7.259  1.00 89.36  ? 89  VAL A CG2 1 
ATOM   449  N  N   . ILE A 1 90  ? 26.929 40.600 -7.301  1.00 91.44  ? 90  ILE A N   1 
ATOM   450  C  CA  . ILE A 1 90  ? 27.403 39.412 -7.997  1.00 92.59  ? 90  ILE A CA  1 
ATOM   451  C  C   . ILE A 1 90  ? 26.405 39.235 -9.139  1.00 94.05  ? 90  ILE A C   1 
ATOM   452  O  O   . ILE A 1 90  ? 25.223 39.028 -8.874  1.00 94.35  ? 90  ILE A O   1 
ATOM   453  C  CB  . ILE A 1 90  ? 27.402 38.176 -7.070  1.00 92.77  ? 90  ILE A CB  1 
ATOM   454  C  CG1 . ILE A 1 90  ? 28.172 38.473 -5.774  1.00 93.29  ? 90  ILE A CG1 1 
ATOM   455  C  CG2 . ILE A 1 90  ? 27.960 36.944 -7.798  1.00 93.24  ? 90  ILE A CG2 1 
ATOM   456  C  CD1 . ILE A 1 90  ? 27.980 37.461 -4.704  1.00 94.38  ? 90  ILE A CD1 1 
ATOM   457  N  N   . THR A 1 91  ? 26.845 39.391 -10.392 1.00 94.55  ? 91  THR A N   1 
ATOM   458  C  CA  . THR A 1 91  ? 25.941 39.257 -11.529 1.00 95.35  ? 91  THR A CA  1 
ATOM   459  C  C   . THR A 1 91  ? 25.928 37.827 -12.063 1.00 96.82  ? 91  THR A C   1 
ATOM   460  O  O   . THR A 1 91  ? 26.935 37.116 -12.000 1.00 96.93  ? 91  THR A O   1 
ATOM   461  C  CB  . THR A 1 91  ? 26.289 40.274 -12.620 1.00 95.99  ? 91  THR A CB  1 
ATOM   462  O  OG1 . THR A 1 91  ? 27.537 39.927 -13.214 1.00 96.53  ? 91  THR A OG1 1 
ATOM   463  C  CG2 . THR A 1 91  ? 26.338 41.701 -12.099 1.00 96.05  ? 91  THR A CG2 1 
ATOM   464  N  N   . ALA A 1 92  ? 24.778 37.402 -12.576 1.00 97.76  ? 92  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 92  ? 24.636 36.083 -13.174 1.00 99.05  ? 92  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 92  ? 25.290 36.098 -14.561 1.00 100.59 ? 92  ALA A C   1 
ATOM   467  O  O   . ALA A 1 92  ? 25.491 37.167 -15.153 1.00 100.59 ? 92  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 92  ? 23.156 35.746 -13.310 1.00 99.05  ? 92  ALA A CB  1 
ATOM   469  N  N   . ASP A 1 93  ? 25.636 34.916 -15.079 1.00 101.73 ? 93  ASP A N   1 
ATOM   470  C  CA  . ASP A 1 93  ? 26.159 34.810 -16.438 1.00 103.15 ? 93  ASP A CA  1 
ATOM   471  C  C   . ASP A 1 93  ? 24.959 34.753 -17.425 1.00 103.83 ? 93  ASP A C   1 
ATOM   472  O  O   . ASP A 1 93  ? 23.796 34.683 -16.997 1.00 104.02 ? 93  ASP A O   1 
ATOM   473  C  CB  . ASP A 1 93  ? 27.119 33.610 -16.592 1.00 105.49 ? 93  ASP A CB  1 
ATOM   474  C  CG  . ASP A 1 93  ? 26.482 32.243 -16.428 1.00 111.14 ? 93  ASP A CG  1 
ATOM   475  O  OD1 . ASP A 1 93  ? 25.376 32.031 -16.976 1.00 112.46 ? 93  ASP A OD1 1 
ATOM   476  O  OD2 . ASP A 1 93  ? 27.096 31.379 -15.760 1.00 113.11 ? 93  ASP A OD2 1 
ATOM   477  N  N   . GLU A 1 94  ? 25.235 34.778 -18.733 1.00 103.98 ? 94  GLU A N   1 
ATOM   478  C  CA  . GLU A 1 94  ? 24.168 34.779 -19.726 1.00 104.52 ? 94  GLU A CA  1 
ATOM   479  C  C   . GLU A 1 94  ? 23.808 33.408 -20.282 1.00 104.83 ? 94  GLU A C   1 
ATOM   480  O  O   . GLU A 1 94  ? 22.934 33.335 -21.135 1.00 105.05 ? 94  GLU A O   1 
ATOM   481  C  CB  . GLU A 1 94  ? 24.509 35.750 -20.855 1.00 106.64 ? 94  GLU A CB  1 
ATOM   482  C  CG  . GLU A 1 94  ? 24.593 37.190 -20.377 1.00 111.49 ? 94  GLU A CG  1 
ATOM   483  C  CD  . GLU A 1 94  ? 25.941 37.863 -20.565 1.00 118.21 ? 94  GLU A CD  1 
ATOM   484  O  OE1 . GLU A 1 94  ? 26.979 37.168 -20.464 1.00 119.69 ? 94  GLU A OE1 1 
ATOM   485  O  OE2 . GLU A 1 94  ? 25.957 39.092 -20.805 1.00 120.28 ? 94  GLU A OE2 1 
ATOM   486  N  N   . SER A 1 95  ? 24.428 32.328 -19.781 1.00 104.80 ? 95  SER A N   1 
ATOM   487  C  CA  . SER A 1 95  ? 24.169 30.962 -20.248 1.00 105.17 ? 95  SER A CA  1 
ATOM   488  C  C   . SER A 1 95  ? 22.701 30.530 -20.124 1.00 105.46 ? 95  SER A C   1 
ATOM   489  O  O   . SER A 1 95  ? 22.253 29.653 -20.871 1.00 105.90 ? 95  SER A O   1 
ATOM   490  C  CB  . SER A 1 95  ? 25.076 29.957 -19.540 1.00 106.02 ? 95  SER A CB  1 
ATOM   491  O  OG  . SER A 1 95  ? 24.613 29.637 -18.237 1.00 107.51 ? 95  SER A OG  1 
ATOM   492  N  N   . ALA A 1 96  ? 21.959 31.134 -19.185 1.00 104.90 ? 96  ALA A N   1 
ATOM   493  C  CA  . ALA A 1 96  ? 20.553 30.790 -19.007 1.00 104.70 ? 96  ALA A CA  1 
ATOM   494  C  C   . ALA A 1 96  ? 19.608 31.998 -19.018 1.00 104.24 ? 96  ALA A C   1 
ATOM   495  O  O   . ALA A 1 96  ? 18.465 31.870 -18.582 1.00 104.50 ? 96  ALA A O   1 
ATOM   496  C  CB  . ALA A 1 96  ? 20.364 29.971 -17.743 1.00 104.85 ? 96  ALA A CB  1 
ATOM   497  N  N   . GLY A 1 97  ? 20.070 33.135 -19.541 1.00 103.32 ? 97  GLY A N   1 
ATOM   498  C  CA  . GLY A 1 97  ? 19.262 34.343 -19.646 1.00 102.95 ? 97  GLY A CA  1 
ATOM   499  C  C   . GLY A 1 97  ? 18.947 34.977 -18.310 1.00 102.45 ? 97  GLY A C   1 
ATOM   500  O  O   . GLY A 1 97  ? 19.781 34.921 -17.403 1.00 103.24 ? 97  GLY A O   1 
ATOM   501  N  N   . PRO A 1 98  ? 17.730 35.566 -18.153 1.00 100.90 ? 98  PRO A N   1 
ATOM   502  C  CA  . PRO A 1 98  ? 17.376 36.223 -16.881 1.00 99.77  ? 98  PRO A CA  1 
ATOM   503  C  C   . PRO A 1 98  ? 17.368 35.301 -15.673 1.00 98.51  ? 98  PRO A C   1 
ATOM   504  O  O   . PRO A 1 98  ? 16.793 34.214 -15.725 1.00 98.79  ? 98  PRO A O   1 
ATOM   505  C  CB  . PRO A 1 98  ? 15.983 36.795 -17.157 1.00 100.49 ? 98  PRO A CB  1 
ATOM   506  C  CG  . PRO A 1 98  ? 15.925 36.948 -18.636 1.00 101.05 ? 98  PRO A CG  1 
ATOM   507  C  CD  . PRO A 1 98  ? 16.652 35.735 -19.146 1.00 99.87  ? 98  PRO A CD  1 
ATOM   508  N  N   . ARG A 1 99  ? 18.029 35.737 -14.588 1.00 96.92  ? 99  ARG A N   1 
ATOM   509  C  CA  . ARG A 1 99  ? 18.144 34.957 -13.358 1.00 95.65  ? 99  ARG A CA  1 
ATOM   510  C  C   . ARG A 1 99  ? 17.607 35.723 -12.142 1.00 93.84  ? 99  ARG A C   1 
ATOM   511  O  O   . ARG A 1 99  ? 17.540 36.953 -12.169 1.00 93.83  ? 99  ARG A O   1 
ATOM   512  C  CB  . ARG A 1 99  ? 19.612 34.541 -13.144 1.00 97.07  ? 99  ARG A CB  1 
ATOM   513  C  CG  . ARG A 1 99  ? 20.157 33.661 -14.252 1.00 100.13 ? 99  ARG A CG  1 
ATOM   514  C  CD  . ARG A 1 99  ? 19.499 32.300 -14.241 1.00 103.77 ? 99  ARG A CD  1 
ATOM   515  N  NE  . ARG A 1 99  ? 20.130 31.426 -13.254 1.00 107.22 ? 99  ARG A NE  1 
ATOM   516  C  CZ  . ARG A 1 99  ? 19.890 30.124 -13.135 1.00 109.25 ? 99  ARG A CZ  1 
ATOM   517  N  NH1 . ARG A 1 99  ? 19.019 29.527 -13.938 1.00 108.55 ? 99  ARG A NH1 1 
ATOM   518  N  NH2 . ARG A 1 99  ? 20.523 29.409 -12.215 1.00 109.43 ? 99  ARG A NH2 1 
ATOM   519  N  N   . PRO A 1 100 ? 17.201 35.010 -11.069 1.00 92.20  ? 100 PRO A N   1 
ATOM   520  C  CA  . PRO A 1 100 ? 16.671 35.697 -9.876  1.00 90.97  ? 100 PRO A CA  1 
ATOM   521  C  C   . PRO A 1 100 ? 17.678 36.602 -9.186  1.00 89.61  ? 100 PRO A C   1 
ATOM   522  O  O   . PRO A 1 100 ? 18.857 36.590 -9.528  1.00 90.06  ? 100 PRO A O   1 
ATOM   523  C  CB  . PRO A 1 100 ? 16.285 34.541 -8.952  1.00 91.85  ? 100 PRO A CB  1 
ATOM   524  C  CG  . PRO A 1 100 ? 16.140 33.360 -9.839  1.00 92.54  ? 100 PRO A CG  1 
ATOM   525  C  CD  . PRO A 1 100 ? 17.168 33.546 -10.900 1.00 91.35  ? 100 PRO A CD  1 
ATOM   526  N  N   . VAL A 1 101 ? 17.212 37.412 -8.228  1.00 87.90  ? 101 VAL A N   1 
ATOM   527  C  CA  . VAL A 1 101 ? 18.098 38.278 -7.462  1.00 86.61  ? 101 VAL A CA  1 
ATOM   528  C  C   . VAL A 1 101 ? 17.895 38.029 -5.957  1.00 85.57  ? 101 VAL A C   1 
ATOM   529  O  O   . VAL A 1 101 ? 16.779 37.792 -5.503  1.00 85.68  ? 101 VAL A O   1 
ATOM   530  C  CB  . VAL A 1 101 ? 17.950 39.769 -7.849  1.00 86.46  ? 101 VAL A CB  1 
ATOM   531  C  CG1 . VAL A 1 101 ? 16.518 40.234 -7.678  1.00 87.11  ? 101 VAL A CG1 1 
ATOM   532  C  CG2 . VAL A 1 101 ? 18.904 40.655 -7.061  1.00 86.46  ? 101 VAL A CG2 1 
ATOM   533  N  N   . ILE A 1 102 ? 18.986 38.006 -5.203  1.00 84.11  ? 102 ILE A N   1 
ATOM   534  C  CA  . ILE A 1 102 ? 18.932 37.862 -3.766  1.00 83.25  ? 102 ILE A CA  1 
ATOM   535  C  C   . ILE A 1 102 ? 19.458 39.166 -3.188  1.00 82.51  ? 102 ILE A C   1 
ATOM   536  O  O   . ILE A 1 102 ? 20.553 39.588 -3.537  1.00 82.54  ? 102 ILE A O   1 
ATOM   537  C  CB  . ILE A 1 102 ? 19.791 36.678 -3.265  1.00 83.43  ? 102 ILE A CB  1 
ATOM   538  C  CG1 . ILE A 1 102 ? 19.343 35.345 -3.875  1.00 83.79  ? 102 ILE A CG1 1 
ATOM   539  C  CG2 . ILE A 1 102 ? 19.793 36.624 -1.740  1.00 83.98  ? 102 ILE A CG2 1 
ATOM   540  C  CD1 . ILE A 1 102 ? 20.398 34.282 -3.804  1.00 84.61  ? 102 ILE A CD1 1 
ATOM   541  N  N   . TYR A 1 103 ? 18.678 39.815 -2.324  1.00 81.58  ? 103 TYR A N   1 
ATOM   542  C  CA  . TYR A 1 103 ? 19.111 41.014 -1.630  1.00 80.81  ? 103 TYR A CA  1 
ATOM   543  C  C   . TYR A 1 103 ? 19.662 40.474 -0.314  1.00 79.35  ? 103 TYR A C   1 
ATOM   544  O  O   . TYR A 1 103 ? 18.904 39.923 0.472   1.00 79.50  ? 103 TYR A O   1 
ATOM   545  C  CB  . TYR A 1 103 ? 17.916 41.955 -1.397  1.00 81.36  ? 103 TYR A CB  1 
ATOM   546  C  CG  . TYR A 1 103 ? 17.371 42.552 -2.683  1.00 82.57  ? 103 TYR A CG  1 
ATOM   547  C  CD1 . TYR A 1 103 ? 16.384 41.903 -3.413  1.00 83.55  ? 103 TYR A CD1 1 
ATOM   548  C  CD2 . TYR A 1 103 ? 17.844 43.763 -3.164  1.00 83.74  ? 103 TYR A CD2 1 
ATOM   549  C  CE1 . TYR A 1 103 ? 15.901 42.433 -4.604  1.00 84.75  ? 103 TYR A CE1 1 
ATOM   550  C  CE2 . TYR A 1 103 ? 17.379 44.298 -4.359  1.00 84.86  ? 103 TYR A CE2 1 
ATOM   551  C  CZ  . TYR A 1 103 ? 16.408 43.629 -5.078  1.00 85.89  ? 103 TYR A CZ  1 
ATOM   552  O  OH  . TYR A 1 103 ? 15.948 44.155 -6.259  1.00 87.26  ? 103 TYR A OH  1 
ATOM   553  N  N   . LEU A 1 104 ? 20.986 40.524 -0.123  1.00 77.85  ? 104 LEU A N   1 
ATOM   554  C  CA  . LEU A 1 104 ? 21.656 39.976 1.060   1.00 76.69  ? 104 LEU A CA  1 
ATOM   555  C  C   . LEU A 1 104 ? 22.135 41.093 1.955   1.00 76.50  ? 104 LEU A C   1 
ATOM   556  O  O   . LEU A 1 104 ? 23.006 41.855 1.563   1.00 77.36  ? 104 LEU A O   1 
ATOM   557  C  CB  . LEU A 1 104 ? 22.852 39.125 0.615   1.00 76.07  ? 104 LEU A CB  1 
ATOM   558  C  CG  . LEU A 1 104 ? 23.696 38.479 1.706   1.00 76.52  ? 104 LEU A CG  1 
ATOM   559  C  CD1 . LEU A 1 104 ? 22.851 37.661 2.664   1.00 76.79  ? 104 LEU A CD1 1 
ATOM   560  C  CD2 . LEU A 1 104 ? 24.747 37.577 1.109   1.00 76.74  ? 104 LEU A CD2 1 
ATOM   561  N  N   . LEU A 1 105 ? 21.589 41.191 3.155   1.00 75.43  ? 105 LEU A N   1 
ATOM   562  C  CA  . LEU A 1 105 ? 21.920 42.272 4.066   1.00 75.00  ? 105 LEU A CA  1 
ATOM   563  C  C   . LEU A 1 105 ? 22.979 41.932 5.112   1.00 75.60  ? 105 LEU A C   1 
ATOM   564  O  O   . LEU A 1 105 ? 22.993 40.840 5.674   1.00 75.82  ? 105 LEU A O   1 
ATOM   565  C  CB  . LEU A 1 105 ? 20.647 42.775 4.760   1.00 74.32  ? 105 LEU A CB  1 
ATOM   566  C  CG  . LEU A 1 105 ? 19.486 43.172 3.871   1.00 74.11  ? 105 LEU A CG  1 
ATOM   567  C  CD1 . LEU A 1 105 ? 18.316 43.584 4.701   1.00 74.07  ? 105 LEU A CD1 1 
ATOM   568  C  CD2 . LEU A 1 105 ? 19.878 44.299 2.940   1.00 74.49  ? 105 LEU A CD2 1 
ATOM   569  N  N   . ASN A 1 106 ? 23.859 42.893 5.385   1.00 75.65  ? 106 ASN A N   1 
ATOM   570  C  CA  . ASN A 1 106 ? 24.863 42.752 6.427   1.00 76.07  ? 106 ASN A CA  1 
ATOM   571  C  C   . ASN A 1 106 ? 24.161 42.970 7.773   1.00 76.56  ? 106 ASN A C   1 
ATOM   572  O  O   . ASN A 1 106 ? 23.002 43.391 7.817   1.00 76.97  ? 106 ASN A O   1 
ATOM   573  C  CB  . ASN A 1 106 ? 25.972 43.801 6.247   1.00 76.80  ? 106 ASN A CB  1 
ATOM   574  C  CG  . ASN A 1 106 ? 26.780 43.658 4.982   1.00 79.50  ? 106 ASN A CG  1 
ATOM   575  O  OD1 . ASN A 1 106 ? 27.400 42.631 4.719   1.00 80.54  ? 106 ASN A OD1 1 
ATOM   576  N  ND2 . ASN A 1 106 ? 26.806 44.698 4.170   1.00 80.05  ? 106 ASN A ND2 1 
ATOM   577  N  N   . GLY A 1 107 ? 24.852 42.673 8.862   1.00 76.33  ? 107 GLY A N   1 
ATOM   578  C  CA  . GLY A 1 107 ? 24.325 42.917 10.192  1.00 76.70  ? 107 GLY A CA  1 
ATOM   579  C  C   . GLY A 1 107 ? 24.614 44.350 10.595  1.00 77.31  ? 107 GLY A C   1 
ATOM   580  O  O   . GLY A 1 107 ? 24.691 45.241 9.743   1.00 77.34  ? 107 GLY A O   1 
ATOM   581  N  N   . GLY A 1 108 ? 24.828 44.560 11.888  1.00 77.58  ? 108 GLY A N   1 
ATOM   582  C  CA  . GLY A 1 108 ? 25.089 45.874 12.466  1.00 78.20  ? 108 GLY A CA  1 
ATOM   583  C  C   . GLY A 1 108 ? 26.176 46.667 11.787  1.00 78.81  ? 108 GLY A C   1 
ATOM   584  O  O   . GLY A 1 108 ? 26.100 47.883 11.725  1.00 79.40  ? 108 GLY A O   1 
ATOM   585  N  N   . ASP A 1 109 ? 27.178 45.994 11.257  1.00 78.89  ? 109 ASP A N   1 
ATOM   586  C  CA  . ASP A 1 109 ? 28.278 46.642 10.543  1.00 79.66  ? 109 ASP A CA  1 
ATOM   587  C  C   . ASP A 1 109 ? 27.787 47.423 9.315   1.00 79.96  ? 109 ASP A C   1 
ATOM   588  O  O   . ASP A 1 109 ? 28.352 48.460 8.957   1.00 80.25  ? 109 ASP A O   1 
ATOM   589  C  CB  . ASP A 1 109 ? 29.264 45.566 10.093  1.00 81.48  ? 109 ASP A CB  1 
ATOM   590  C  CG  . ASP A 1 109 ? 30.465 46.126 9.397   1.00 85.93  ? 109 ASP A CG  1 
ATOM   591  O  OD1 . ASP A 1 109 ? 31.259 46.834 10.066  1.00 86.59  ? 109 ASP A OD1 1 
ATOM   592  O  OD2 . ASP A 1 109 ? 30.604 45.888 8.175   1.00 87.85  ? 109 ASP A OD2 1 
ATOM   593  N  N   . GLY A 1 110 ? 26.767 46.883 8.659   1.00 79.52  ? 110 GLY A N   1 
ATOM   594  C  CA  . GLY A 1 110 ? 26.160 47.474 7.482   1.00 79.32  ? 110 GLY A CA  1 
ATOM   595  C  C   . GLY A 1 110 ? 27.014 47.443 6.238   1.00 79.32  ? 110 GLY A C   1 
ATOM   596  O  O   . GLY A 1 110 ? 26.587 47.936 5.201   1.00 79.98  ? 110 GLY A O   1 
ATOM   597  N  N   . GLY A 1 111 ? 28.187 46.828 6.306   1.00 78.72  ? 111 GLY A N   1 
ATOM   598  C  CA  . GLY A 1 111 ? 29.145 46.838 5.200   1.00 78.34  ? 111 GLY A CA  1 
ATOM   599  C  C   . GLY A 1 111 ? 30.097 48.027 5.262   1.00 77.51  ? 111 GLY A C   1 
ATOM   600  O  O   . GLY A 1 111 ? 30.952 48.198 4.392   1.00 77.45  ? 111 GLY A O   1 
ATOM   601  N  N   . GLU A 1 112 ? 29.969 48.849 6.310   1.00 76.74  ? 112 GLU A N   1 
ATOM   602  C  CA  . GLU A 1 112 ? 30.758 50.044 6.549   1.00 76.40  ? 112 GLU A CA  1 
ATOM   603  C  C   . GLU A 1 112 ? 32.051 49.814 7.358   1.00 76.56  ? 112 GLU A C   1 
ATOM   604  O  O   . GLU A 1 112 ? 32.707 50.774 7.749   1.00 77.23  ? 112 GLU A O   1 
ATOM   605  C  CB  . GLU A 1 112 ? 29.878 51.071 7.272   1.00 77.30  ? 112 GLU A CB  1 
ATOM   606  C  CG  . GLU A 1 112 ? 28.567 51.328 6.565   1.00 78.76  ? 112 GLU A CG  1 
ATOM   607  C  CD  . GLU A 1 112 ? 27.912 52.611 7.006   1.00 81.90  ? 112 GLU A CD  1 
ATOM   608  O  OE1 . GLU A 1 112 ? 28.657 53.584 7.240   1.00 81.79  ? 112 GLU A OE1 1 
ATOM   609  O  OE2 . GLU A 1 112 ? 26.664 52.658 7.104   1.00 84.69  ? 112 GLU A OE2 1 
ATOM   610  N  N   . GLY A 1 113 ? 32.391 48.568 7.634   1.00 75.81  ? 113 GLY A N   1 
ATOM   611  C  CA  . GLY A 1 113 ? 33.581 48.231 8.395   1.00 75.14  ? 113 GLY A CA  1 
ATOM   612  C  C   . GLY A 1 113 ? 34.155 46.925 7.902   1.00 74.42  ? 113 GLY A C   1 
ATOM   613  O  O   . GLY A 1 113 ? 34.117 46.639 6.702   1.00 73.59  ? 113 GLY A O   1 
ATOM   614  N  N   . ALA A 1 114 ? 34.687 46.116 8.826   1.00 74.23  ? 114 ALA A N   1 
ATOM   615  C  CA  . ALA A 1 114 ? 35.281 44.834 8.462   1.00 74.06  ? 114 ALA A CA  1 
ATOM   616  C  C   . ALA A 1 114 ? 34.394 43.634 8.774   1.00 74.08  ? 114 ALA A C   1 
ATOM   617  O  O   . ALA A 1 114 ? 34.652 42.553 8.257   1.00 74.00  ? 114 ALA A O   1 
ATOM   618  C  CB  . ALA A 1 114 ? 36.616 44.672 9.162   1.00 74.16  ? 114 ALA A CB  1 
ATOM   619  N  N   . ALA A 1 115 ? 33.378 43.795 9.642   1.00 74.00  ? 115 ALA A N   1 
ATOM   620  C  CA  . ALA A 1 115 ? 32.508 42.698 10.066  1.00 74.11  ? 115 ALA A CA  1 
ATOM   621  C  C   . ALA A 1 115 ? 31.305 42.475 9.130   1.00 74.53  ? 115 ALA A C   1 
ATOM   622  O  O   . ALA A 1 115 ? 30.147 42.593 9.550   1.00 75.32  ? 115 ALA A O   1 
ATOM   623  C  CB  . ALA A 1 115 ? 32.050 42.948 11.491  1.00 74.03  ? 115 ALA A CB  1 
ATOM   624  N  N   . ASN A 1 116 ? 31.575 42.112 7.866   1.00 73.81  ? 116 ASN A N   1 
ATOM   625  C  CA  . ASN A 1 116 ? 30.518 41.955 6.872   1.00 73.57  ? 116 ASN A CA  1 
ATOM   626  C  C   . ASN A 1 116 ? 30.707 40.746 5.952   1.00 74.02  ? 116 ASN A C   1 
ATOM   627  O  O   . ASN A 1 116 ? 31.755 40.118 5.984   1.00 74.36  ? 116 ASN A O   1 
ATOM   628  C  CB  . ASN A 1 116 ? 30.389 43.249 6.077   1.00 73.36  ? 116 ASN A CB  1 
ATOM   629  C  CG  . ASN A 1 116 ? 31.646 43.651 5.373   1.00 74.33  ? 116 ASN A CG  1 
ATOM   630  O  OD1 . ASN A 1 116 ? 32.122 42.992 4.458   1.00 74.34  ? 116 ASN A OD1 1 
ATOM   631  N  ND2 . ASN A 1 116 ? 32.198 44.763 5.763   1.00 74.95  ? 116 ASN A ND2 1 
ATOM   632  N  N   . TRP A 1 117 ? 29.698 40.407 5.150   1.00 74.03  ? 117 TRP A N   1 
ATOM   633  C  CA  . TRP A 1 117 ? 29.754 39.254 4.249   1.00 74.45  ? 117 TRP A CA  1 
ATOM   634  C  C   . TRP A 1 117 ? 30.993 39.213 3.358   1.00 76.10  ? 117 TRP A C   1 
ATOM   635  O  O   . TRP A 1 117 ? 31.640 38.171 3.243   1.00 76.33  ? 117 TRP A O   1 
ATOM   636  C  CB  . TRP A 1 117 ? 28.488 39.198 3.361   1.00 73.32  ? 117 TRP A CB  1 
ATOM   637  C  CG  . TRP A 1 117 ? 27.216 38.917 4.101   1.00 71.99  ? 117 TRP A CG  1 
ATOM   638  C  CD1 . TRP A 1 117 ? 26.210 39.798 4.377   1.00 72.55  ? 117 TRP A CD1 1 
ATOM   639  C  CD2 . TRP A 1 117 ? 26.818 37.662 4.663   1.00 71.15  ? 117 TRP A CD2 1 
ATOM   640  N  NE1 . TRP A 1 117 ? 25.210 39.169 5.084   1.00 72.63  ? 117 TRP A NE1 1 
ATOM   641  C  CE2 . TRP A 1 117 ? 25.569 37.856 5.285   1.00 72.19  ? 117 TRP A CE2 1 
ATOM   642  C  CE3 . TRP A 1 117 ? 27.407 36.399 4.720   1.00 71.23  ? 117 TRP A CE3 1 
ATOM   643  C  CZ2 . TRP A 1 117 ? 24.897 36.821 5.941   1.00 72.47  ? 117 TRP A CZ2 1 
ATOM   644  C  CZ3 . TRP A 1 117 ? 26.742 35.382 5.375   1.00 72.03  ? 117 TRP A CZ3 1 
ATOM   645  C  CH2 . TRP A 1 117 ? 25.503 35.596 5.977   1.00 72.14  ? 117 TRP A CH2 1 
ATOM   646  N  N   . VAL A 1 118 ? 31.308 40.340 2.717   1.00 77.02  ? 118 VAL A N   1 
ATOM   647  C  CA  . VAL A 1 118 ? 32.396 40.467 1.754   1.00 78.09  ? 118 VAL A CA  1 
ATOM   648  C  C   . VAL A 1 118 ? 33.774 40.267 2.377   1.00 79.02  ? 118 VAL A C   1 
ATOM   649  O  O   . VAL A 1 118 ? 34.634 39.600 1.795   1.00 79.75  ? 118 VAL A O   1 
ATOM   650  C  CB  . VAL A 1 118 ? 32.256 41.825 1.021   1.00 78.81  ? 118 VAL A CB  1 
ATOM   651  C  CG1 . VAL A 1 118 ? 33.458 42.122 0.132   1.00 79.24  ? 118 VAL A CG1 1 
ATOM   652  C  CG2 . VAL A 1 118 ? 30.964 41.852 0.207   1.00 79.44  ? 118 VAL A CG2 1 
ATOM   653  N  N   . MET A 1 119 ? 33.960 40.779 3.581   1.00 78.76  ? 119 MET A N   1 
ATOM   654  C  CA  . MET A 1 119 ? 35.248 40.716 4.249   1.00 78.90  ? 119 MET A CA  1 
ATOM   655  C  C   . MET A 1 119 ? 35.433 39.543 5.179   1.00 79.83  ? 119 MET A C   1 
ATOM   656  O  O   . MET A 1 119 ? 36.554 39.339 5.645   1.00 80.43  ? 119 MET A O   1 
ATOM   657  C  CB  . MET A 1 119 ? 35.480 41.999 5.036   1.00 79.08  ? 119 MET A CB  1 
ATOM   658  C  CG  . MET A 1 119 ? 35.116 43.254 4.279   1.00 80.66  ? 119 MET A CG  1 
ATOM   659  S  SD  . MET A 1 119 ? 36.561 44.070 3.649   1.00 82.53  ? 119 MET A SD  1 
ATOM   660  C  CE  . MET A 1 119 ? 37.391 44.481 5.223   1.00 81.87  ? 119 MET A CE  1 
ATOM   661  N  N   . GLN A 1 120 ? 34.355 38.801 5.513   1.00 79.74  ? 120 GLN A N   1 
ATOM   662  C  CA  . GLN A 1 120 ? 34.449 37.686 6.456   1.00 79.83  ? 120 GLN A CA  1 
ATOM   663  C  C   . GLN A 1 120 ? 34.066 36.334 5.906   1.00 81.31  ? 120 GLN A C   1 
ATOM   664  O  O   . GLN A 1 120 ? 34.201 35.345 6.625   1.00 81.32  ? 120 GLN A O   1 
ATOM   665  C  CB  . GLN A 1 120 ? 33.608 37.961 7.707   1.00 79.82  ? 120 GLN A CB  1 
ATOM   666  C  CG  . GLN A 1 120 ? 34.010 39.209 8.480   1.00 80.14  ? 120 GLN A CG  1 
ATOM   667  C  CD  . GLN A 1 120 ? 35.338 39.074 9.161   1.00 80.86  ? 120 GLN A CD  1 
ATOM   668  O  OE1 . GLN A 1 120 ? 35.836 37.975 9.391   1.00 81.90  ? 120 GLN A OE1 1 
ATOM   669  N  NE2 . GLN A 1 120 ? 35.943 40.191 9.500   1.00 80.72  ? 120 GLN A NE2 1 
ATOM   670  N  N   . THR A 1 121 ? 33.507 36.276 4.680   1.00 82.67  ? 121 THR A N   1 
ATOM   671  C  CA  . THR A 1 121 ? 33.064 35.017 4.065   1.00 84.26  ? 121 THR A CA  1 
ATOM   672  C  C   . THR A 1 121 ? 33.485 34.908 2.573   1.00 85.50  ? 121 THR A C   1 
ATOM   673  O  O   . THR A 1 121 ? 33.956 35.882 1.984   1.00 85.86  ? 121 THR A O   1 
ATOM   674  C  CB  . THR A 1 121 ? 31.519 34.853 4.202   1.00 85.67  ? 121 THR A CB  1 
ATOM   675  O  OG1 . THR A 1 121 ? 30.894 35.708 3.257   1.00 87.20  ? 121 THR A OG1 1 
ATOM   676  C  CG2 . THR A 1 121 ? 30.993 35.146 5.586   1.00 85.85  ? 121 THR A CG2 1 
ATOM   677  N  N   . ASP A 1 122 ? 33.267 33.732 1.955   1.00 86.08  ? 122 ASP A N   1 
ATOM   678  C  CA  . ASP A 1 122 ? 33.529 33.522 0.535   1.00 87.12  ? 122 ASP A CA  1 
ATOM   679  C  C   . ASP A 1 122 ? 32.271 33.781 -0.306  1.00 88.23  ? 122 ASP A C   1 
ATOM   680  O  O   . ASP A 1 122 ? 32.093 33.156 -1.348  1.00 88.64  ? 122 ASP A O   1 
ATOM   681  C  CB  . ASP A 1 122 ? 34.032 32.091 0.299   1.00 88.60  ? 122 ASP A CB  1 
ATOM   682  C  CG  . ASP A 1 122 ? 33.046 30.990 0.641   1.00 93.02  ? 122 ASP A CG  1 
ATOM   683  O  OD1 . ASP A 1 122 ? 31.981 31.299 1.217   1.00 93.97  ? 122 ASP A OD1 1 
ATOM   684  O  OD2 . ASP A 1 122 ? 33.334 29.820 0.322   1.00 95.04  ? 122 ASP A OD2 1 
ATOM   685  N  N   . VAL A 1 123 ? 31.397 34.692 0.148   1.00 88.62  ? 123 VAL A N   1 
ATOM   686  C  CA  . VAL A 1 123 ? 30.129 35.027 -0.493  1.00 89.38  ? 123 VAL A CA  1 
ATOM   687  C  C   . VAL A 1 123 ? 30.249 35.240 -2.010  1.00 90.35  ? 123 VAL A C   1 
ATOM   688  O  O   . VAL A 1 123 ? 29.389 34.777 -2.765  1.00 90.63  ? 123 VAL A O   1 
ATOM   689  C  CB  . VAL A 1 123 ? 29.467 36.238 0.217   1.00 89.79  ? 123 VAL A CB  1 
ATOM   690  C  CG1 . VAL A 1 123 ? 30.352 37.472 0.159   1.00 89.93  ? 123 VAL A CG1 1 
ATOM   691  C  CG2 . VAL A 1 123 ? 28.075 36.528 -0.334  1.00 90.32  ? 123 VAL A CG2 1 
ATOM   692  N  N   . LEU A 1 124 ? 31.326 35.901 -2.458  1.00 90.60  ? 124 LEU A N   1 
ATOM   693  C  CA  . LEU A 1 124 ? 31.518 36.170 -3.876  1.00 91.29  ? 124 LEU A CA  1 
ATOM   694  C  C   . LEU A 1 124 ? 31.744 34.894 -4.682  1.00 92.60  ? 124 LEU A C   1 
ATOM   695  O  O   . LEU A 1 124 ? 31.013 34.651 -5.643  1.00 93.33  ? 124 LEU A O   1 
ATOM   696  C  CB  . LEU A 1 124 ? 32.651 37.178 -4.092  1.00 91.07  ? 124 LEU A CB  1 
ATOM   697  C  CG  . LEU A 1 124 ? 32.536 38.486 -3.318  1.00 92.03  ? 124 LEU A CG  1 
ATOM   698  C  CD1 . LEU A 1 124 ? 33.709 39.378 -3.600  1.00 92.49  ? 124 LEU A CD1 1 
ATOM   699  C  CD2 . LEU A 1 124 ? 31.253 39.224 -3.653  1.00 92.55  ? 124 LEU A CD2 1 
ATOM   700  N  N   . ASP A 1 125 ? 32.710 34.056 -4.278  1.00 92.61  ? 125 ASP A N   1 
ATOM   701  C  CA  . ASP A 1 125 ? 32.980 32.811 -4.994  1.00 93.06  ? 125 ASP A CA  1 
ATOM   702  C  C   . ASP A 1 125 ? 31.812 31.830 -4.968  1.00 92.51  ? 125 ASP A C   1 
ATOM   703  O  O   . ASP A 1 125 ? 31.486 31.223 -5.991  1.00 92.76  ? 125 ASP A O   1 
ATOM   704  C  CB  . ASP A 1 125 ? 34.253 32.152 -4.458  1.00 95.82  ? 125 ASP A CB  1 
ATOM   705  C  CG  . ASP A 1 125 ? 35.544 32.727 -5.028  1.00 101.64 ? 125 ASP A CG  1 
ATOM   706  O  OD1 . ASP A 1 125 ? 35.466 33.598 -5.938  1.00 102.25 ? 125 ASP A OD1 1 
ATOM   707  O  OD2 . ASP A 1 125 ? 36.631 32.305 -4.575  1.00 104.27 ? 125 ASP A OD2 1 
ATOM   708  N  N   . PHE A 1 126 ? 31.174 31.690 -3.807  1.00 91.68  ? 126 PHE A N   1 
ATOM   709  C  CA  . PHE A 1 126 ? 30.040 30.796 -3.648  1.00 91.48  ? 126 PHE A CA  1 
ATOM   710  C  C   . PHE A 1 126 ? 28.899 31.079 -4.639  1.00 92.61  ? 126 PHE A C   1 
ATOM   711  O  O   . PHE A 1 126 ? 28.453 30.165 -5.328  1.00 93.01  ? 126 PHE A O   1 
ATOM   712  C  CB  . PHE A 1 126 ? 29.523 30.847 -2.200  1.00 90.44  ? 126 PHE A CB  1 
ATOM   713  C  CG  . PHE A 1 126 ? 28.327 29.964 -1.969  1.00 89.86  ? 126 PHE A CG  1 
ATOM   714  C  CD1 . PHE A 1 126 ? 28.461 28.589 -1.928  1.00 90.27  ? 126 PHE A CD1 1 
ATOM   715  C  CD2 . PHE A 1 126 ? 27.064 30.506 -1.830  1.00 90.05  ? 126 PHE A CD2 1 
ATOM   716  C  CE1 . PHE A 1 126 ? 27.355 27.774 -1.742  1.00 90.81  ? 126 PHE A CE1 1 
ATOM   717  C  CE2 . PHE A 1 126 ? 25.958 29.690 -1.650  1.00 90.60  ? 126 PHE A CE2 1 
ATOM   718  C  CZ  . PHE A 1 126 ? 26.109 28.330 -1.607  1.00 90.50  ? 126 PHE A CZ  1 
ATOM   719  N  N   . TYR A 1 127 ? 28.426 32.329 -4.697  1.00 93.17  ? 127 TYR A N   1 
ATOM   720  C  CA  . TYR A 1 127 ? 27.293 32.706 -5.537  1.00 94.19  ? 127 TYR A CA  1 
ATOM   721  C  C   . TYR A 1 127 ? 27.625 32.823 -7.009  1.00 95.87  ? 127 TYR A C   1 
ATOM   722  O  O   . TYR A 1 127 ? 26.740 32.627 -7.847  1.00 96.31  ? 127 TYR A O   1 
ATOM   723  C  CB  . TYR A 1 127 ? 26.633 33.985 -5.022  1.00 93.76  ? 127 TYR A CB  1 
ATOM   724  C  CG  . TYR A 1 127 ? 25.769 33.768 -3.797  1.00 93.93  ? 127 TYR A CG  1 
ATOM   725  C  CD1 . TYR A 1 127 ? 24.723 32.858 -3.813  1.00 94.55  ? 127 TYR A CD1 1 
ATOM   726  C  CD2 . TYR A 1 127 ? 25.954 34.526 -2.648  1.00 94.48  ? 127 TYR A CD2 1 
ATOM   727  C  CE1 . TYR A 1 127 ? 23.901 32.684 -2.705  1.00 95.28  ? 127 TYR A CE1 1 
ATOM   728  C  CE2 . TYR A 1 127 ? 25.127 34.374 -1.541  1.00 95.03  ? 127 TYR A CE2 1 
ATOM   729  C  CZ  . TYR A 1 127 ? 24.099 33.455 -1.574  1.00 95.87  ? 127 TYR A CZ  1 
ATOM   730  O  OH  . TYR A 1 127 ? 23.292 33.288 -0.476  1.00 97.12  ? 127 TYR A OH  1 
ATOM   731  N  N   . LEU A 1 128 ? 28.899 33.087 -7.341  1.00 96.59  ? 128 LEU A N   1 
ATOM   732  C  CA  . LEU A 1 128 ? 29.384 33.142 -8.724  1.00 97.61  ? 128 LEU A CA  1 
ATOM   733  C  C   . LEU A 1 128 ? 29.099 31.785 -9.401  1.00 98.93  ? 128 LEU A C   1 
ATOM   734  O  O   . LEU A 1 128 ? 28.558 31.736 -10.505 1.00 99.55  ? 128 LEU A O   1 
ATOM   735  C  CB  . LEU A 1 128 ? 30.897 33.373 -8.687  1.00 97.57  ? 128 LEU A CB  1 
ATOM   736  C  CG  . LEU A 1 128 ? 31.516 34.238 -9.735  1.00 98.96  ? 128 LEU A CG  1 
ATOM   737  C  CD1 . LEU A 1 128 ? 31.123 35.689 -9.543  1.00 99.49  ? 128 LEU A CD1 1 
ATOM   738  C  CD2 . LEU A 1 128 ? 33.008 34.085 -9.690  1.00 99.63  ? 128 LEU A CD2 1 
ATOM   739  N  N   . GLU A 1 129 ? 29.370 30.690 -8.682  1.00 99.41  ? 129 GLU A N   1 
ATOM   740  C  CA  . GLU A 1 129 ? 29.149 29.337 -9.178  1.00 100.23 ? 129 GLU A CA  1 
ATOM   741  C  C   . GLU A 1 129 ? 27.662 28.997 -9.326  1.00 99.59  ? 129 GLU A C   1 
ATOM   742  O  O   . GLU A 1 129 ? 27.302 28.206 -10.193 1.00 99.69  ? 129 GLU A O   1 
ATOM   743  C  CB  . GLU A 1 129 ? 29.844 28.320 -8.254  1.00 104.15 ? 129 GLU A CB  1 
ATOM   744  C  CG  . GLU A 1 129 ? 30.213 27.015 -8.945  1.00 111.34 ? 129 GLU A CG  1 
ATOM   745  C  CD  . GLU A 1 129 ? 31.614 26.948 -9.536  1.00 120.30 ? 129 GLU A CD  1 
ATOM   746  O  OE1 . GLU A 1 129 ? 32.382 27.924 -9.367  1.00 122.85 ? 129 GLU A OE1 1 
ATOM   747  O  OE2 . GLU A 1 129 ? 31.947 25.915 -10.163 1.00 122.22 ? 129 GLU A OE2 1 
ATOM   748  N  N   . LYS A 1 130 ? 26.800 29.591 -8.494  1.00 98.84  ? 130 LYS A N   1 
ATOM   749  C  CA  . LYS A 1 130 ? 25.358 29.327 -8.517  1.00 98.46  ? 130 LYS A CA  1 
ATOM   750  C  C   . LYS A 1 130 ? 24.604 29.977 -9.678  1.00 98.26  ? 130 LYS A C   1 
ATOM   751  O  O   . LYS A 1 130 ? 23.451 29.614 -9.927  1.00 98.59  ? 130 LYS A O   1 
ATOM   752  C  CB  . LYS A 1 130 ? 24.707 29.747 -7.187  1.00 99.29  ? 130 LYS A CB  1 
ATOM   753  C  CG  . LYS A 1 130 ? 25.202 28.970 -5.977  1.00 101.44 ? 130 LYS A CG  1 
ATOM   754  C  CD  . LYS A 1 130 ? 24.882 27.505 -6.087  1.00 104.55 ? 130 LYS A CD  1 
ATOM   755  C  CE  . LYS A 1 130 ? 25.282 26.776 -4.841  1.00 107.84 ? 130 LYS A CE  1 
ATOM   756  N  NZ  . LYS A 1 130 ? 26.755 26.610 -4.773  1.00 110.29 ? 130 LYS A NZ  1 
ATOM   757  N  N   . ASN A 1 131 ? 25.228 30.949 -10.362 1.00 97.43  ? 131 ASN A N   1 
ATOM   758  C  CA  . ASN A 1 131 ? 24.599 31.682 -11.460 1.00 96.90  ? 131 ASN A CA  1 
ATOM   759  C  C   . ASN A 1 131 ? 23.310 32.372 -11.003 1.00 95.78  ? 131 ASN A C   1 
ATOM   760  O  O   . ASN A 1 131 ? 22.214 32.047 -11.456 1.00 95.92  ? 131 ASN A O   1 
ATOM   761  C  CB  . ASN A 1 131 ? 24.360 30.797 -12.692 1.00 98.31  ? 131 ASN A CB  1 
ATOM   762  C  CG  . ASN A 1 131 ? 23.863 31.571 -13.887 1.00 101.68 ? 131 ASN A CG  1 
ATOM   763  O  OD1 . ASN A 1 131 ? 24.174 32.747 -14.048 1.00 103.13 ? 131 ASN A OD1 1 
ATOM   764  N  ND2 . ASN A 1 131 ? 23.066 30.943 -14.740 1.00 102.03 ? 131 ASN A ND2 1 
ATOM   765  N  N   . VAL A 1 132 ? 23.446 33.303 -10.076 1.00 94.51  ? 132 VAL A N   1 
ATOM   766  C  CA  . VAL A 1 132 ? 22.311 34.058 -9.556  1.00 93.52  ? 132 VAL A CA  1 
ATOM   767  C  C   . VAL A 1 132 ? 22.791 35.466 -9.252  1.00 92.35  ? 132 VAL A C   1 
ATOM   768  O  O   . VAL A 1 132 ? 23.978 35.663 -8.976  1.00 92.56  ? 132 VAL A O   1 
ATOM   769  C  CB  . VAL A 1 132 ? 21.712 33.364 -8.305  1.00 94.09  ? 132 VAL A CB  1 
ATOM   770  C  CG1 . VAL A 1 132 ? 22.734 33.279 -7.174  1.00 94.60  ? 132 VAL A CG1 1 
ATOM   771  C  CG2 . VAL A 1 132 ? 20.428 34.042 -7.840  1.00 94.52  ? 132 VAL A CG2 1 
ATOM   772  N  N   . ASN A 1 133 ? 21.901 36.458 -9.365  1.00 91.00  ? 133 ASN A N   1 
ATOM   773  C  CA  . ASN A 1 133 ? 22.261 37.830 -9.026  1.00 90.14  ? 133 ASN A CA  1 
ATOM   774  C  C   . ASN A 1 133 ? 22.161 37.997 -7.507  1.00 88.42  ? 133 ASN A C   1 
ATOM   775  O  O   . ASN A 1 133 ? 21.210 37.513 -6.899  1.00 88.31  ? 133 ASN A O   1 
ATOM   776  C  CB  . ASN A 1 133 ? 21.366 38.846 -9.741  1.00 91.35  ? 133 ASN A CB  1 
ATOM   777  C  CG  . ASN A 1 133 ? 21.447 38.759 -11.240 1.00 94.57  ? 133 ASN A CG  1 
ATOM   778  O  OD1 . ASN A 1 133 ? 22.434 39.153 -11.866 1.00 95.58  ? 133 ASN A OD1 1 
ATOM   779  N  ND2 . ASN A 1 133 ? 20.403 38.233 -11.848 1.00 95.70  ? 133 ASN A ND2 1 
ATOM   780  N  N   . VAL A 1 134 ? 23.177 38.621 -6.887  1.00 86.63  ? 134 VAL A N   1 
ATOM   781  C  CA  . VAL A 1 134 ? 23.200 38.865 -5.445  1.00 84.84  ? 134 VAL A CA  1 
ATOM   782  C  C   . VAL A 1 134 ? 23.574 40.311 -5.240  1.00 83.28  ? 134 VAL A C   1 
ATOM   783  O  O   . VAL A 1 134 ? 24.574 40.756 -5.782  1.00 83.15  ? 134 VAL A O   1 
ATOM   784  C  CB  . VAL A 1 134 ? 24.175 37.935 -4.693  1.00 85.00  ? 134 VAL A CB  1 
ATOM   785  C  CG1 . VAL A 1 134 ? 24.162 38.231 -3.199  1.00 85.66  ? 134 VAL A CG1 1 
ATOM   786  C  CG2 . VAL A 1 134 ? 23.849 36.469 -4.952  1.00 84.94  ? 134 VAL A CG2 1 
ATOM   787  N  N   . VAL A 1 135 ? 22.757 41.063 -4.500  1.00 82.10  ? 135 VAL A N   1 
ATOM   788  C  CA  . VAL A 1 135 ? 23.027 42.473 -4.256  1.00 81.28  ? 135 VAL A CA  1 
ATOM   789  C  C   . VAL A 1 135 ? 23.215 42.697 -2.763  1.00 80.51  ? 135 VAL A C   1 
ATOM   790  O  O   . VAL A 1 135 ? 22.364 42.335 -1.952  1.00 80.53  ? 135 VAL A O   1 
ATOM   791  C  CB  . VAL A 1 135 ? 22.020 43.437 -4.937  1.00 81.82  ? 135 VAL A CB  1 
ATOM   792  C  CG1 . VAL A 1 135 ? 20.606 42.920 -4.871  1.00 82.80  ? 135 VAL A CG1 1 
ATOM   793  C  CG2 . VAL A 1 135 ? 22.110 44.848 -4.386  1.00 82.05  ? 135 VAL A CG2 1 
ATOM   794  N  N   . ILE A 1 136 ? 24.400 43.198 -2.398  1.00 79.57  ? 136 ILE A N   1 
ATOM   795  C  CA  . ILE A 1 136 ? 24.767 43.420 -1.009  1.00 78.78  ? 136 ILE A CA  1 
ATOM   796  C  C   . ILE A 1 136 ? 25.002 44.894 -0.755  1.00 78.03  ? 136 ILE A C   1 
ATOM   797  O  O   . ILE A 1 136 ? 26.057 45.404 -1.096  1.00 77.65  ? 136 ILE A O   1 
ATOM   798  C  CB  . ILE A 1 136 ? 26.022 42.591 -0.603  1.00 78.79  ? 136 ILE A CB  1 
ATOM   799  C  CG1 . ILE A 1 136 ? 25.947 41.133 -1.101  1.00 79.48  ? 136 ILE A CG1 1 
ATOM   800  C  CG2 . ILE A 1 136 ? 26.199 42.629 0.897   1.00 79.03  ? 136 ILE A CG2 1 
ATOM   801  C  CD1 . ILE A 1 136 ? 27.212 40.352 -0.925  1.00 80.38  ? 136 ILE A CD1 1 
ATOM   802  N  N   . PRO A 1 137 ? 24.041 45.591 -0.132  1.00 77.81  ? 137 PRO A N   1 
ATOM   803  C  CA  . PRO A 1 137 ? 24.263 47.004 0.205   1.00 77.66  ? 137 PRO A CA  1 
ATOM   804  C  C   . PRO A 1 137 ? 25.411 47.132 1.209   1.00 77.83  ? 137 PRO A C   1 
ATOM   805  O  O   . PRO A 1 137 ? 25.460 46.362 2.170   1.00 78.56  ? 137 PRO A O   1 
ATOM   806  C  CB  . PRO A 1 137 ? 22.932 47.434 0.841   1.00 78.10  ? 137 PRO A CB  1 
ATOM   807  C  CG  . PRO A 1 137 ? 21.943 46.373 0.465   1.00 78.60  ? 137 PRO A CG  1 
ATOM   808  C  CD  . PRO A 1 137 ? 22.730 45.115 0.349   1.00 77.34  ? 137 PRO A CD  1 
ATOM   809  N  N   . MET A 1 138 ? 26.339 48.072 0.973   1.00 76.94  ? 138 MET A N   1 
ATOM   810  C  CA  . MET A 1 138 ? 27.505 48.257 1.824   1.00 76.60  ? 138 MET A CA  1 
ATOM   811  C  C   . MET A 1 138 ? 27.466 49.528 2.666   1.00 76.27  ? 138 MET A C   1 
ATOM   812  O  O   . MET A 1 138 ? 28.500 50.090 3.009   1.00 76.48  ? 138 MET A O   1 
ATOM   813  C  CB  . MET A 1 138 ? 28.783 48.167 1.002   1.00 77.04  ? 138 MET A CB  1 
ATOM   814  C  CG  . MET A 1 138 ? 28.950 46.814 0.360   1.00 78.87  ? 138 MET A CG  1 
ATOM   815  S  SD  . MET A 1 138 ? 29.738 45.667 1.517   1.00 83.97  ? 138 MET A SD  1 
ATOM   816  C  CE  . MET A 1 138 ? 28.775 44.381 1.383   1.00 80.03  ? 138 MET A CE  1 
ATOM   817  N  N   . GLU A 1 139 ? 26.269 49.938 3.040   1.00 75.82  ? 139 GLU A N   1 
ATOM   818  C  CA  . GLU A 1 139 ? 25.990 51.018 3.974   1.00 76.18  ? 139 GLU A CA  1 
ATOM   819  C  C   . GLU A 1 139 ? 24.721 50.653 4.728   1.00 76.65  ? 139 GLU A C   1 
ATOM   820  O  O   . GLU A 1 139 ? 23.953 49.796 4.277   1.00 76.86  ? 139 GLU A O   1 
ATOM   821  C  CB  . GLU A 1 139 ? 25.860 52.385 3.289   1.00 78.47  ? 139 GLU A CB  1 
ATOM   822  C  CG  . GLU A 1 139 ? 27.194 53.094 3.147   1.00 83.32  ? 139 GLU A CG  1 
ATOM   823  C  CD  . GLU A 1 139 ? 27.117 54.519 2.651   1.00 88.46  ? 139 GLU A CD  1 
ATOM   824  O  OE1 . GLU A 1 139 ? 26.051 55.146 2.824   1.00 89.36  ? 139 GLU A OE1 1 
ATOM   825  O  OE2 . GLU A 1 139 ? 28.120 55.010 2.085   1.00 91.04  ? 139 GLU A OE2 1 
ATOM   826  N  N   . GLY A 1 140 ? 24.529 51.255 5.891   1.00 76.67  ? 140 GLY A N   1 
ATOM   827  C  CA  . GLY A 1 140 ? 23.348 50.979 6.698   1.00 77.38  ? 140 GLY A CA  1 
ATOM   828  C  C   . GLY A 1 140 ? 23.659 50.428 8.068   1.00 77.53  ? 140 GLY A C   1 
ATOM   829  O  O   . GLY A 1 140 ? 22.849 49.687 8.639   1.00 77.94  ? 140 GLY A O   1 
ATOM   830  N  N   . LYS A 1 141 ? 24.834 50.806 8.607   1.00 76.73  ? 141 LYS A N   1 
ATOM   831  C  CA  . LYS A 1 141 ? 25.285 50.375 9.924   1.00 76.13  ? 141 LYS A CA  1 
ATOM   832  C  C   . LYS A 1 141 ? 24.293 50.762 11.011  1.00 76.40  ? 141 LYS A C   1 
ATOM   833  O  O   . LYS A 1 141 ? 23.722 51.846 10.960  1.00 76.88  ? 141 LYS A O   1 
ATOM   834  C  CB  . LYS A 1 141 ? 26.676 50.946 10.244  1.00 76.75  ? 141 LYS A CB  1 
ATOM   835  C  CG  . LYS A 1 141 ? 26.684 52.438 10.544  1.00 78.89  ? 141 LYS A CG  1 
ATOM   836  C  CD  . LYS A 1 141 ? 28.071 52.931 10.768  1.00 81.64  ? 141 LYS A CD  1 
ATOM   837  C  CE  . LYS A 1 141 ? 28.087 54.412 10.981  1.00 84.39  ? 141 LYS A CE  1 
ATOM   838  N  NZ  . LYS A 1 141 ? 29.454 54.872 11.306  1.00 86.07  ? 141 LYS A NZ  1 
ATOM   839  N  N   . PHE A 1 142 ? 24.047 49.845 11.955  1.00 76.23  ? 142 PHE A N   1 
ATOM   840  C  CA  . PHE A 1 142 ? 23.176 50.019 13.123  1.00 76.71  ? 142 PHE A CA  1 
ATOM   841  C  C   . PHE A 1 142 ? 21.796 50.612 12.769  1.00 76.80  ? 142 PHE A C   1 
ATOM   842  O  O   . PHE A 1 142 ? 21.221 51.335 13.570  1.00 77.11  ? 142 PHE A O   1 
ATOM   843  C  CB  . PHE A 1 142 ? 23.909 50.848 14.230  1.00 76.80  ? 142 PHE A CB  1 
ATOM   844  C  CG  . PHE A 1 142 ? 25.353 50.419 14.436  1.00 77.53  ? 142 PHE A CG  1 
ATOM   845  C  CD1 . PHE A 1 142 ? 25.661 49.130 14.831  1.00 78.26  ? 142 PHE A CD1 1 
ATOM   846  C  CD2 . PHE A 1 142 ? 26.399 51.260 14.099  1.00 78.01  ? 142 PHE A CD2 1 
ATOM   847  C  CE1 . PHE A 1 142 ? 26.983 48.714 14.941  1.00 78.55  ? 142 PHE A CE1 1 
ATOM   848  C  CE2 . PHE A 1 142 ? 27.720 50.831 14.204  1.00 78.26  ? 142 PHE A CE2 1 
ATOM   849  C  CZ  . PHE A 1 142 ? 28.001 49.563 14.619  1.00 77.85  ? 142 PHE A CZ  1 
ATOM   850  N  N   . SER A 1 143 ? 21.250 50.282 11.587  1.00 76.40  ? 143 SER A N   1 
ATOM   851  C  CA  . SER A 1 143 ? 19.985 50.856 11.110  1.00 76.09  ? 143 SER A CA  1 
ATOM   852  C  C   . SER A 1 143 ? 18.781 49.950 11.173  1.00 76.37  ? 143 SER A C   1 
ATOM   853  O  O   . SER A 1 143 ? 17.671 50.425 10.962  1.00 77.19  ? 143 SER A O   1 
ATOM   854  C  CB  . SER A 1 143 ? 20.138 51.293 9.656   1.00 76.19  ? 143 SER A CB  1 
ATOM   855  O  OG  . SER A 1 143 ? 20.294 50.184 8.787   1.00 76.93  ? 143 SER A OG  1 
ATOM   856  N  N   . TYR A 1 144 ? 18.993 48.645 11.344  1.00 75.80  ? 144 TYR A N   1 
ATOM   857  C  CA  . TYR A 1 144 ? 17.942 47.636 11.231  1.00 75.69  ? 144 TYR A CA  1 
ATOM   858  C  C   . TYR A 1 144 ? 17.307 47.619 9.838   1.00 77.01  ? 144 TYR A C   1 
ATOM   859  O  O   . TYR A 1 144 ? 16.325 46.909 9.650   1.00 78.27  ? 144 TYR A O   1 
ATOM   860  C  CB  . TYR A 1 144 ? 16.892 47.729 12.346  1.00 75.03  ? 144 TYR A CB  1 
ATOM   861  C  CG  . TYR A 1 144 ? 17.306 46.960 13.579  1.00 74.74  ? 144 TYR A CG  1 
ATOM   862  C  CD1 . TYR A 1 144 ? 18.107 47.543 14.549  1.00 75.20  ? 144 TYR A CD1 1 
ATOM   863  C  CD2 . TYR A 1 144 ? 16.959 45.630 13.738  1.00 75.20  ? 144 TYR A CD2 1 
ATOM   864  C  CE1 . TYR A 1 144 ? 18.532 46.827 15.656  1.00 75.94  ? 144 TYR A CE1 1 
ATOM   865  C  CE2 . TYR A 1 144 ? 17.389 44.900 14.833  1.00 76.03  ? 144 TYR A CE2 1 
ATOM   866  C  CZ  . TYR A 1 144 ? 18.181 45.498 15.789  1.00 76.93  ? 144 TYR A CZ  1 
ATOM   867  O  OH  . TYR A 1 144 ? 18.584 44.757 16.876  1.00 78.74  ? 144 TYR A OH  1 
ATOM   868  N  N   . TYR A 1 145 ? 17.896 48.358 8.857   1.00 76.77  ? 145 TYR A N   1 
ATOM   869  C  CA  . TYR A 1 145 ? 17.451 48.526 7.481   1.00 76.65  ? 145 TYR A CA  1 
ATOM   870  C  C   . TYR A 1 145 ? 15.982 48.850 7.409   1.00 77.33  ? 145 TYR A C   1 
ATOM   871  O  O   . TYR A 1 145 ? 15.267 48.320 6.572   1.00 77.33  ? 145 TYR A O   1 
ATOM   872  C  CB  . TYR A 1 145 ? 17.828 47.316 6.646   1.00 76.34  ? 145 TYR A CB  1 
ATOM   873  C  CG  . TYR A 1 145 ? 19.297 47.307 6.316   1.00 76.40  ? 145 TYR A CG  1 
ATOM   874  C  CD1 . TYR A 1 145 ? 19.830 48.210 5.411   1.00 76.86  ? 145 TYR A CD1 1 
ATOM   875  C  CD2 . TYR A 1 145 ? 20.158 46.396 6.912   1.00 77.00  ? 145 TYR A CD2 1 
ATOM   876  C  CE1 . TYR A 1 145 ? 21.183 48.211 5.104   1.00 77.61  ? 145 TYR A CE1 1 
ATOM   877  C  CE2 . TYR A 1 145 ? 21.514 46.382 6.606   1.00 77.71  ? 145 TYR A CE2 1 
ATOM   878  C  CZ  . TYR A 1 145 ? 22.024 47.296 5.705   1.00 78.34  ? 145 TYR A CZ  1 
ATOM   879  O  OH  . TYR A 1 145 ? 23.355 47.290 5.380   1.00 79.65  ? 145 TYR A OH  1 
ATOM   880  N  N   . THR A 1 146 ? 15.537 49.751 8.288   1.00 78.12  ? 146 THR A N   1 
ATOM   881  C  CA  . THR A 1 146 ? 14.149 50.182 8.396   1.00 79.01  ? 146 THR A CA  1 
ATOM   882  C  C   . THR A 1 146 ? 14.024 51.695 8.124   1.00 79.15  ? 146 THR A C   1 
ATOM   883  O  O   . THR A 1 146 ? 15.026 52.361 7.881   1.00 79.22  ? 146 THR A O   1 
ATOM   884  C  CB  . THR A 1 146 ? 13.614 49.776 9.795   1.00 81.12  ? 146 THR A CB  1 
ATOM   885  O  OG1 . THR A 1 146 ? 12.182 49.816 9.776   1.00 82.63  ? 146 THR A OG1 1 
ATOM   886  C  CG2 . THR A 1 146 ? 14.153 50.667 10.905  1.00 81.63  ? 146 THR A CG2 1 
ATOM   887  N  N   . ASP A 1 147 ? 12.784 52.217 8.110   1.00 79.23  ? 147 ASP A N   1 
ATOM   888  C  CA  . ASP A 1 147 ? 12.475 53.631 7.957   1.00 79.60  ? 147 ASP A CA  1 
ATOM   889  C  C   . ASP A 1 147 ? 12.375 54.181 9.372   1.00 79.93  ? 147 ASP A C   1 
ATOM   890  O  O   . ASP A 1 147 ? 11.502 53.771 10.141  1.00 80.41  ? 147 ASP A O   1 
ATOM   891  C  CB  . ASP A 1 147 ? 11.136 53.824 7.212   1.00 81.31  ? 147 ASP A CB  1 
ATOM   892  C  CG  . ASP A 1 147 ? 11.189 53.574 5.717   1.00 86.37  ? 147 ASP A CG  1 
ATOM   893  O  OD1 . ASP A 1 147 ? 12.262 53.206 5.216   1.00 88.45  ? 147 ASP A OD1 1 
ATOM   894  O  OD2 . ASP A 1 147 ? 10.152 53.740 5.050   1.00 87.58  ? 147 ASP A OD2 1 
ATOM   895  N  N   . TRP A 1 148 ? 13.278 55.083 9.730   1.00 79.53  ? 148 TRP A N   1 
ATOM   896  C  CA  . TRP A 1 148 ? 13.336 55.630 11.076  1.00 79.89  ? 148 TRP A CA  1 
ATOM   897  C  C   . TRP A 1 148 ? 12.358 56.761 11.289  1.00 80.77  ? 148 TRP A C   1 
ATOM   898  O  O   . TRP A 1 148 ? 12.168 57.584 10.399  1.00 80.96  ? 148 TRP A O   1 
ATOM   899  C  CB  . TRP A 1 148 ? 14.765 56.124 11.379  1.00 79.52  ? 148 TRP A CB  1 
ATOM   900  C  CG  . TRP A 1 148 ? 15.741 55.036 11.707  1.00 79.09  ? 148 TRP A CG  1 
ATOM   901  C  CD1 . TRP A 1 148 ? 15.938 53.873 11.023  1.00 79.63  ? 148 TRP A CD1 1 
ATOM   902  C  CD2 . TRP A 1 148 ? 16.676 55.029 12.794  1.00 78.93  ? 148 TRP A CD2 1 
ATOM   903  N  NE1 . TRP A 1 148 ? 16.924 53.132 11.625  1.00 79.93  ? 148 TRP A NE1 1 
ATOM   904  C  CE2 . TRP A 1 148 ? 17.397 53.820 12.718  1.00 79.47  ? 148 TRP A CE2 1 
ATOM   905  C  CE3 . TRP A 1 148 ? 16.965 55.920 13.839  1.00 79.18  ? 148 TRP A CE3 1 
ATOM   906  C  CZ2 . TRP A 1 148 ? 18.408 53.497 13.624  1.00 79.39  ? 148 TRP A CZ2 1 
ATOM   907  C  CZ3 . TRP A 1 148 ? 17.949 55.582 14.750  1.00 79.59  ? 148 TRP A CZ3 1 
ATOM   908  C  CH2 . TRP A 1 148 ? 18.654 54.383 14.638  1.00 79.41  ? 148 TRP A CH2 1 
ATOM   909  N  N   . VAL A 1 149 ? 11.763 56.832 12.485  1.00 81.10  ? 149 VAL A N   1 
ATOM   910  C  CA  . VAL A 1 149 ? 10.855 57.921 12.837  1.00 81.89  ? 149 VAL A CA  1 
ATOM   911  C  C   . VAL A 1 149 ? 11.632 59.254 12.914  1.00 83.46  ? 149 VAL A C   1 
ATOM   912  O  O   . VAL A 1 149 ? 11.139 60.283 12.435  1.00 83.95  ? 149 VAL A O   1 
ATOM   913  C  CB  . VAL A 1 149 ? 10.138 57.610 14.172  1.00 81.92  ? 149 VAL A CB  1 
ATOM   914  C  CG1 . VAL A 1 149 ? 9.393  58.817 14.712  1.00 82.41  ? 149 VAL A CG1 1 
ATOM   915  C  CG2 . VAL A 1 149 ? 9.197  56.439 14.014  1.00 82.12  ? 149 VAL A CG2 1 
ATOM   916  N  N   . GLU A 1 150 ? 12.857 59.228 13.494  1.00 83.83  ? 150 GLU A N   1 
ATOM   917  C  CA  . GLU A 1 150 ? 13.693 60.420 13.684  1.00 84.57  ? 150 GLU A CA  1 
ATOM   918  C  C   . GLU A 1 150 ? 15.019 60.337 12.951  1.00 84.90  ? 150 GLU A C   1 
ATOM   919  O  O   . GLU A 1 150 ? 15.491 59.250 12.637  1.00 85.20  ? 150 GLU A O   1 
ATOM   920  C  CB  . GLU A 1 150 ? 13.987 60.646 15.190  1.00 87.29  ? 150 GLU A CB  1 
ATOM   921  C  CG  . GLU A 1 150 ? 12.763 60.834 16.070  1.00 92.88  ? 150 GLU A CG  1 
ATOM   922  C  CD  . GLU A 1 150 ? 12.340 62.269 16.296  1.00 101.25 ? 150 GLU A CD  1 
ATOM   923  O  OE1 . GLU A 1 150 ? 13.147 63.183 16.007  1.00 103.29 ? 150 GLU A OE1 1 
ATOM   924  O  OE2 . GLU A 1 150 ? 11.200 62.479 16.772  1.00 104.19 ? 150 GLU A OE2 1 
ATOM   925  N  N   . GLU A 1 151 ? 15.646 61.490 12.714  1.00 84.89  ? 151 GLU A N   1 
ATOM   926  C  CA  . GLU A 1 151 ? 16.971 61.526 12.114  1.00 85.06  ? 151 GLU A CA  1 
ATOM   927  C  C   . GLU A 1 151 ? 18.030 61.261 13.207  1.00 84.74  ? 151 GLU A C   1 
ATOM   928  O  O   . GLU A 1 151 ? 17.765 61.411 14.410  1.00 84.30  ? 151 GLU A O   1 
ATOM   929  C  CB  . GLU A 1 151 ? 17.230 62.888 11.455  1.00 87.59  ? 151 GLU A CB  1 
ATOM   930  C  CG  . GLU A 1 151 ? 16.311 63.198 10.287  1.00 93.47  ? 151 GLU A CG  1 
ATOM   931  C  CD  . GLU A 1 151 ? 16.788 64.334 9.401   1.00 99.81  ? 151 GLU A CD  1 
ATOM   932  O  OE1 . GLU A 1 151 ? 17.997 64.667 9.447   1.00 100.49 ? 151 GLU A OE1 1 
ATOM   933  O  OE2 . GLU A 1 151 ? 15.947 64.891 8.658   1.00 101.84 ? 151 GLU A OE2 1 
ATOM   934  N  N   . ASN A 1 152 ? 19.230 60.856 12.778  1.00 84.45  ? 152 ASN A N   1 
ATOM   935  C  CA  . ASN A 1 152 ? 20.356 60.608 13.669  1.00 84.51  ? 152 ASN A CA  1 
ATOM   936  C  C   . ASN A 1 152 ? 21.606 60.905 12.864  1.00 84.66  ? 152 ASN A C   1 
ATOM   937  O  O   . ASN A 1 152 ? 21.930 60.166 11.939  1.00 84.81  ? 152 ASN A O   1 
ATOM   938  C  CB  . ASN A 1 152 ? 20.343 59.175 14.206  1.00 85.28  ? 152 ASN A CB  1 
ATOM   939  C  CG  . ASN A 1 152 ? 21.410 58.902 15.230  1.00 87.52  ? 152 ASN A CG  1 
ATOM   940  O  OD1 . ASN A 1 152 ? 22.592 58.881 14.915  1.00 88.77  ? 152 ASN A OD1 1 
ATOM   941  N  ND2 . ASN A 1 152 ? 21.016 58.662 16.475  1.00 87.43  ? 152 ASN A ND2 1 
ATOM   942  N  N   . ALA A 1 153 ? 22.269 62.034 13.167  1.00 84.51  ? 153 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 153 ? 23.447 62.506 12.450  1.00 84.48  ? 153 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 153 ? 24.583 61.502 12.445  1.00 85.13  ? 153 ALA A C   1 
ATOM   945  O  O   . ALA A 1 153 ? 25.277 61.376 11.434  1.00 85.25  ? 153 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 153 ? 23.917 63.816 13.042  1.00 84.35  ? 153 ALA A CB  1 
ATOM   947  N  N   . SER A 1 154 ? 24.760 60.763 13.560  1.00 85.34  ? 154 SER A N   1 
ATOM   948  C  CA  . SER A 1 154 ? 25.803 59.737 13.693  1.00 85.86  ? 154 SER A CA  1 
ATOM   949  C  C   . SER A 1 154 ? 25.663 58.603 12.665  1.00 86.51  ? 154 SER A C   1 
ATOM   950  O  O   . SER A 1 154 ? 26.647 57.933 12.345  1.00 86.76  ? 154 SER A O   1 
ATOM   951  C  CB  . SER A 1 154 ? 25.835 59.180 15.111  1.00 87.01  ? 154 SER A CB  1 
ATOM   952  O  OG  . SER A 1 154 ? 25.846 60.241 16.052  1.00 89.60  ? 154 SER A OG  1 
ATOM   953  N  N   . LEU A 1 155 ? 24.443 58.404 12.135  1.00 86.54  ? 155 LEU A N   1 
ATOM   954  C  CA  . LEU A 1 155 ? 24.150 57.389 11.134  1.00 86.61  ? 155 LEU A CA  1 
ATOM   955  C  C   . LEU A 1 155 ? 23.784 57.995 9.763   1.00 87.11  ? 155 LEU A C   1 
ATOM   956  O  O   . LEU A 1 155 ? 23.161 57.320 8.947   1.00 87.49  ? 155 LEU A O   1 
ATOM   957  C  CB  . LEU A 1 155 ? 23.034 56.467 11.642  1.00 86.39  ? 155 LEU A CB  1 
ATOM   958  C  CG  . LEU A 1 155 ? 23.317 55.769 12.968  1.00 87.15  ? 155 LEU A CG  1 
ATOM   959  C  CD1 . LEU A 1 155 ? 22.090 55.021 13.465  1.00 87.62  ? 155 LEU A CD1 1 
ATOM   960  C  CD2 . LEU A 1 155 ? 24.513 54.849 12.852  1.00 87.52  ? 155 LEU A CD2 1 
ATOM   961  N  N   . GLY A 1 156 ? 24.169 59.247 9.521   1.00 86.79  ? 156 GLY A N   1 
ATOM   962  C  CA  . GLY A 1 156 ? 23.954 59.899 8.237   1.00 86.87  ? 156 GLY A CA  1 
ATOM   963  C  C   . GLY A 1 156 ? 22.721 60.766 8.075   1.00 86.89  ? 156 GLY A C   1 
ATOM   964  O  O   . GLY A 1 156 ? 22.461 61.266 6.980   1.00 87.21  ? 156 GLY A O   1 
ATOM   965  N  N   . GLY A 1 157 ? 21.962 60.946 9.142   1.00 86.41  ? 157 GLY A N   1 
ATOM   966  C  CA  . GLY A 1 157 ? 20.771 61.778 9.104   1.00 86.65  ? 157 GLY A CA  1 
ATOM   967  C  C   . GLY A 1 157 ? 19.486 61.001 8.935   1.00 87.12  ? 157 GLY A C   1 
ATOM   968  O  O   . GLY A 1 157 ? 19.093 60.226 9.810   1.00 87.61  ? 157 GLY A O   1 
ATOM   969  N  N   . LYS A 1 158 ? 18.810 61.223 7.817   1.00 86.98  ? 158 LYS A N   1 
ATOM   970  C  CA  . LYS A 1 158 ? 17.538 60.577 7.528   1.00 86.94  ? 158 LYS A CA  1 
ATOM   971  C  C   . LYS A 1 158 ? 17.763 59.145 7.092   1.00 86.37  ? 158 LYS A C   1 
ATOM   972  O  O   . LYS A 1 158 ? 18.574 58.885 6.199   1.00 86.65  ? 158 LYS A O   1 
ATOM   973  C  CB  . LYS A 1 158 ? 16.788 61.366 6.445   1.00 89.11  ? 158 LYS A CB  1 
ATOM   974  C  CG  . LYS A 1 158 ? 15.359 60.920 6.234   1.00 94.14  ? 158 LYS A CG  1 
ATOM   975  C  CD  . LYS A 1 158 ? 14.552 62.012 5.543   1.00 99.42  ? 158 LYS A CD  1 
ATOM   976  C  CE  . LYS A 1 158 ? 13.143 61.569 5.213   1.00 103.64 ? 158 LYS A CE  1 
ATOM   977  N  NZ  . LYS A 1 158 ? 12.949 61.389 3.747   1.00 105.89 ? 158 LYS A NZ  1 
ATOM   978  N  N   . GLN A 1 159 ? 17.073 58.204 7.744   1.00 85.44  ? 159 GLN A N   1 
ATOM   979  C  CA  . GLN A 1 159 ? 17.216 56.795 7.392   1.00 84.68  ? 159 GLN A CA  1 
ATOM   980  C  C   . GLN A 1 159 ? 15.910 56.230 6.923   1.00 83.53  ? 159 GLN A C   1 
ATOM   981  O  O   . GLN A 1 159 ? 14.939 56.220 7.668   1.00 83.64  ? 159 GLN A O   1 
ATOM   982  C  CB  . GLN A 1 159 ? 17.779 56.002 8.556   1.00 86.33  ? 159 GLN A CB  1 
ATOM   983  C  CG  . GLN A 1 159 ? 19.159 56.495 8.917   1.00 89.21  ? 159 GLN A CG  1 
ATOM   984  C  CD  . GLN A 1 159 ? 19.813 55.560 9.857   1.00 92.25  ? 159 GLN A CD  1 
ATOM   985  O  OE1 . GLN A 1 159 ? 20.512 54.631 9.445   1.00 93.64  ? 159 GLN A OE1 1 
ATOM   986  N  NE2 . GLN A 1 159 ? 19.597 55.795 11.133  1.00 92.09  ? 159 GLN A NE2 1 
ATOM   987  N  N   . MET A 1 160 ? 15.865 55.832 5.651   1.00 82.32  ? 160 MET A N   1 
ATOM   988  C  CA  . MET A 1 160 ? 14.676 55.315 4.990   1.00 81.33  ? 160 MET A CA  1 
ATOM   989  C  C   . MET A 1 160 ? 15.107 54.091 4.194   1.00 79.73  ? 160 MET A C   1 
ATOM   990  O  O   . MET A 1 160 ? 14.985 54.055 2.968   1.00 80.26  ? 160 MET A O   1 
ATOM   991  C  CB  . MET A 1 160 ? 14.092 56.401 4.064   1.00 82.32  ? 160 MET A CB  1 
ATOM   992  C  CG  . MET A 1 160 ? 13.632 57.635 4.801   1.00 84.97  ? 160 MET A CG  1 
ATOM   993  S  SD  . MET A 1 160 ? 12.171 57.225 5.770   1.00 92.44  ? 160 MET A SD  1 
ATOM   994  C  CE  . MET A 1 160 ? 12.302 58.433 7.063   1.00 93.89  ? 160 MET A CE  1 
ATOM   995  N  N   . TRP A 1 161 ? 15.654 53.099 4.896   1.00 77.81  ? 161 TRP A N   1 
ATOM   996  C  CA  . TRP A 1 161 ? 16.205 51.898 4.283   1.00 76.38  ? 161 TRP A CA  1 
ATOM   997  C  C   . TRP A 1 161 ? 15.167 50.957 3.753   1.00 76.06  ? 161 TRP A C   1 
ATOM   998  O  O   . TRP A 1 161 ? 15.466 50.209 2.837   1.00 76.41  ? 161 TRP A O   1 
ATOM   999  C  CB  . TRP A 1 161 ? 17.121 51.172 5.262   1.00 75.74  ? 161 TRP A CB  1 
ATOM   1000 C  CG  . TRP A 1 161 ? 18.297 51.988 5.682   1.00 75.44  ? 161 TRP A CG  1 
ATOM   1001 C  CD1 . TRP A 1 161 ? 18.439 52.700 6.837   1.00 75.93  ? 161 TRP A CD1 1 
ATOM   1002 C  CD2 . TRP A 1 161 ? 19.480 52.225 4.912   1.00 75.20  ? 161 TRP A CD2 1 
ATOM   1003 N  NE1 . TRP A 1 161 ? 19.645 53.360 6.837   1.00 76.01  ? 161 TRP A NE1 1 
ATOM   1004 C  CE2 . TRP A 1 161 ? 20.300 53.090 5.662   1.00 75.72  ? 161 TRP A CE2 1 
ATOM   1005 C  CE3 . TRP A 1 161 ? 19.923 51.793 3.652   1.00 75.68  ? 161 TRP A CE3 1 
ATOM   1006 C  CZ2 . TRP A 1 161 ? 21.537 53.523 5.198   1.00 76.26  ? 161 TRP A CZ2 1 
ATOM   1007 C  CZ3 . TRP A 1 161 ? 21.156 52.216 3.201   1.00 76.34  ? 161 TRP A CZ3 1 
ATOM   1008 C  CH2 . TRP A 1 161 ? 21.956 53.053 3.979   1.00 76.43  ? 161 TRP A CH2 1 
ATOM   1009 N  N   . GLU A 1 162 ? 13.962 50.947 4.337   1.00 75.43  ? 162 GLU A N   1 
ATOM   1010 C  CA  . GLU A 1 162 ? 12.892 50.091 3.843   1.00 75.19  ? 162 GLU A CA  1 
ATOM   1011 C  C   . GLU A 1 162 ? 12.355 50.690 2.535   1.00 76.58  ? 162 GLU A C   1 
ATOM   1012 O  O   . GLU A 1 162 ? 12.140 49.969 1.574   1.00 77.25  ? 162 GLU A O   1 
ATOM   1013 C  CB  . GLU A 1 162 ? 11.781 49.956 4.877   1.00 75.29  ? 162 GLU A CB  1 
ATOM   1014 C  CG  . GLU A 1 162 ? 10.698 48.983 4.458   1.00 76.78  ? 162 GLU A CG  1 
ATOM   1015 C  CD  . GLU A 1 162 ? 9.769  48.571 5.580   1.00 79.37  ? 162 GLU A CD  1 
ATOM   1016 O  OE1 . GLU A 1 162 ? 9.693  49.299 6.597   1.00 79.89  ? 162 GLU A OE1 1 
ATOM   1017 O  OE2 . GLU A 1 162 ? 9.112  47.516 5.440   1.00 80.48  ? 162 GLU A OE2 1 
ATOM   1018 N  N   . THR A 1 163 ? 12.181 52.021 2.479   1.00 76.73  ? 163 THR A N   1 
ATOM   1019 C  CA  . THR A 1 163 ? 11.766 52.720 1.271   1.00 76.89  ? 163 THR A CA  1 
ATOM   1020 C  C   . THR A 1 163 ? 12.810 52.522 0.186   1.00 77.30  ? 163 THR A C   1 
ATOM   1021 O  O   . THR A 1 163 ? 12.455 52.241 -0.949  1.00 77.91  ? 163 THR A O   1 
ATOM   1022 C  CB  . THR A 1 163 ? 11.527 54.190 1.586   1.00 77.90  ? 163 THR A CB  1 
ATOM   1023 O  OG1 . THR A 1 163 ? 10.297 54.295 2.308   1.00 78.97  ? 163 THR A OG1 1 
ATOM   1024 C  CG2 . THR A 1 163 ? 11.475 55.063 0.337   1.00 78.09  ? 163 THR A CG2 1 
ATOM   1025 N  N   . PHE A 1 164 ? 14.088 52.621 0.539   1.00 77.06  ? 164 PHE A N   1 
ATOM   1026 C  CA  . PHE A 1 164 ? 15.153 52.411 -0.422  1.00 77.32  ? 164 PHE A CA  1 
ATOM   1027 C  C   . PHE A 1 164 ? 15.174 50.972 -0.942  1.00 78.43  ? 164 PHE A C   1 
ATOM   1028 O  O   . PHE A 1 164 ? 15.079 50.763 -2.143  1.00 78.81  ? 164 PHE A O   1 
ATOM   1029 C  CB  . PHE A 1 164 ? 16.516 52.834 0.157   1.00 76.61  ? 164 PHE A CB  1 
ATOM   1030 C  CG  . PHE A 1 164 ? 17.701 52.430 -0.696  1.00 76.72  ? 164 PHE A CG  1 
ATOM   1031 C  CD1 . PHE A 1 164 ? 17.975 53.082 -1.888  1.00 77.05  ? 164 PHE A CD1 1 
ATOM   1032 C  CD2 . PHE A 1 164 ? 18.534 51.392 -0.307  1.00 77.17  ? 164 PHE A CD2 1 
ATOM   1033 C  CE1 . PHE A 1 164 ? 19.056 52.702 -2.675  1.00 77.63  ? 164 PHE A CE1 1 
ATOM   1034 C  CE2 . PHE A 1 164 ? 19.608 51.006 -1.102  1.00 77.67  ? 164 PHE A CE2 1 
ATOM   1035 C  CZ  . PHE A 1 164 ? 19.871 51.671 -2.273  1.00 77.49  ? 164 PHE A CZ  1 
ATOM   1036 N  N   . LEU A 1 165 ? 15.303 49.987 -0.056  1.00 78.84  ? 165 LEU A N   1 
ATOM   1037 C  CA  . LEU A 1 165 ? 15.442 48.593 -0.457  1.00 79.71  ? 165 LEU A CA  1 
ATOM   1038 C  C   . LEU A 1 165 ? 14.222 47.983 -1.110  1.00 80.42  ? 165 LEU A C   1 
ATOM   1039 O  O   . LEU A 1 165 ? 14.368 47.083 -1.929  1.00 80.54  ? 165 LEU A O   1 
ATOM   1040 C  CB  . LEU A 1 165 ? 15.863 47.737 0.745   1.00 79.92  ? 165 LEU A CB  1 
ATOM   1041 C  CG  . LEU A 1 165 ? 17.240 48.008 1.288   1.00 80.77  ? 165 LEU A CG  1 
ATOM   1042 C  CD1 . LEU A 1 165 ? 17.434 47.298 2.605   1.00 81.09  ? 165 LEU A CD1 1 
ATOM   1043 C  CD2 . LEU A 1 165 ? 18.294 47.613 0.283   1.00 81.42  ? 165 LEU A CD2 1 
ATOM   1044 N  N   . VAL A 1 166 ? 13.031 48.413 -0.711  1.00 80.85  ? 166 VAL A N   1 
ATOM   1045 C  CA  . VAL A 1 166 ? 11.803 47.854 -1.252  1.00 82.04  ? 166 VAL A CA  1 
ATOM   1046 C  C   . VAL A 1 166 ? 11.233 48.667 -2.408  1.00 83.08  ? 166 VAL A C   1 
ATOM   1047 O  O   . VAL A 1 166 ? 10.758 48.092 -3.379  1.00 84.09  ? 166 VAL A O   1 
ATOM   1048 C  CB  . VAL A 1 166 ? 10.738 47.666 -0.148  1.00 83.12  ? 166 VAL A CB  1 
ATOM   1049 C  CG1 . VAL A 1 166 ? 9.437  47.132 -0.730  1.00 84.06  ? 166 VAL A CG1 1 
ATOM   1050 C  CG2 . VAL A 1 166 ? 11.239 46.750 0.954   1.00 83.52  ? 166 VAL A CG2 1 
ATOM   1051 N  N   . LYS A 1 167 ? 11.242 49.990 -2.300  1.00 82.92  ? 167 LYS A N   1 
ATOM   1052 C  CA  . LYS A 1 167 ? 10.592 50.842 -3.285  1.00 83.40  ? 167 LYS A CA  1 
ATOM   1053 C  C   . LYS A 1 167 ? 11.511 51.581 -4.277  1.00 84.77  ? 167 LYS A C   1 
ATOM   1054 O  O   . LYS A 1 167 ? 11.177 51.655 -5.466  1.00 85.53  ? 167 LYS A O   1 
ATOM   1055 C  CB  . LYS A 1 167 ? 9.687  51.843 -2.559  1.00 83.82  ? 167 LYS A CB  1 
ATOM   1056 C  CG  . LYS A 1 167 ? 8.677  51.156 -1.650  1.00 85.70  ? 167 LYS A CG  1 
ATOM   1057 C  CD  . LYS A 1 167 ? 7.764  52.152 -0.992  1.00 89.14  ? 167 LYS A CD  1 
ATOM   1058 C  CE  . LYS A 1 167 ? 6.835  51.510 -0.002  1.00 92.52  ? 167 LYS A CE  1 
ATOM   1059 N  NZ  . LYS A 1 167 ? 5.763  52.456 0.411   1.00 94.81  ? 167 LYS A NZ  1 
ATOM   1060 N  N   . GLU A 1 168 ? 12.627 52.151 -3.811  1.00 84.62  ? 168 GLU A N   1 
ATOM   1061 C  CA  . GLU A 1 168 ? 13.503 52.919 -4.692  1.00 84.83  ? 168 GLU A CA  1 
ATOM   1062 C  C   . GLU A 1 168 ? 14.416 52.061 -5.549  1.00 85.48  ? 168 GLU A C   1 
ATOM   1063 O  O   . GLU A 1 168 ? 14.626 52.364 -6.720  1.00 86.09  ? 168 GLU A O   1 
ATOM   1064 C  CB  . GLU A 1 168 ? 14.348 53.919 -3.882  1.00 86.01  ? 168 GLU A CB  1 
ATOM   1065 C  CG  . GLU A 1 168 ? 13.527 54.859 -3.018  1.00 89.44  ? 168 GLU A CG  1 
ATOM   1066 C  CD  . GLU A 1 168 ? 14.356 55.794 -2.166  1.00 95.07  ? 168 GLU A CD  1 
ATOM   1067 O  OE1 . GLU A 1 168 ? 15.527 55.460 -1.882  1.00 96.98  ? 168 GLU A OE1 1 
ATOM   1068 O  OE2 . GLU A 1 168 ? 13.843 56.871 -1.793  1.00 96.47  ? 168 GLU A OE2 1 
ATOM   1069 N  N   . LEU A 1 169 ? 14.989 51.015 -4.967  1.00 85.15  ? 169 LEU A N   1 
ATOM   1070 C  CA  . LEU A 1 169 ? 16.018 50.217 -5.618  1.00 85.07  ? 169 LEU A CA  1 
ATOM   1071 C  C   . LEU A 1 169 ? 15.570 49.082 -6.567  1.00 85.37  ? 169 LEU A C   1 
ATOM   1072 O  O   . LEU A 1 169 ? 16.215 48.926 -7.607  1.00 85.69  ? 169 LEU A O   1 
ATOM   1073 C  CB  . LEU A 1 169 ? 16.947 49.638 -4.536  1.00 84.75  ? 169 LEU A CB  1 
ATOM   1074 C  CG  . LEU A 1 169 ? 18.155 48.868 -5.023  1.00 85.65  ? 169 LEU A CG  1 
ATOM   1075 C  CD1 . LEU A 1 169 ? 19.127 49.786 -5.687  1.00 86.27  ? 169 LEU A CD1 1 
ATOM   1076 C  CD2 . LEU A 1 169 ? 18.807 48.110 -3.894  1.00 85.95  ? 169 LEU A CD2 1 
ATOM   1077 N  N   . PRO A 1 170 ? 14.570 48.229 -6.238  1.00 85.19  ? 170 PRO A N   1 
ATOM   1078 C  CA  . PRO A 1 170 ? 14.295 47.071 -7.100  1.00 85.60  ? 170 PRO A CA  1 
ATOM   1079 C  C   . PRO A 1 170 ? 13.986 47.356 -8.568  1.00 86.51  ? 170 PRO A C   1 
ATOM   1080 O  O   . PRO A 1 170 ? 14.536 46.665 -9.414  1.00 87.24  ? 170 PRO A O   1 
ATOM   1081 C  CB  . PRO A 1 170 ? 13.132 46.369 -6.399  1.00 85.98  ? 170 PRO A CB  1 
ATOM   1082 C  CG  . PRO A 1 170 ? 13.272 46.760 -4.986  1.00 86.08  ? 170 PRO A CG  1 
ATOM   1083 C  CD  . PRO A 1 170 ? 13.719 48.187 -5.033  1.00 84.49  ? 170 PRO A CD  1 
ATOM   1084 N  N   . GLY A 1 171 ? 13.140 48.343 -8.866  1.00 85.95  ? 171 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 171 ? 12.782 48.687 -10.238 1.00 85.69  ? 171 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 171 ? 13.966 48.931 -11.152 1.00 85.72  ? 171 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 171 ? 14.231 48.150 -12.069 1.00 85.91  ? 171 GLY A O   1 
ATOM   1088 N  N   . PRO A 1 172 ? 14.729 49.990 -10.877 1.00 85.48  ? 172 PRO A N   1 
ATOM   1089 C  CA  . PRO A 1 172 ? 15.891 50.296 -11.722 1.00 85.70  ? 172 PRO A CA  1 
ATOM   1090 C  C   . PRO A 1 172 ? 17.033 49.281 -11.665 1.00 86.14  ? 172 PRO A C   1 
ATOM   1091 O  O   . PRO A 1 172 ? 17.690 49.057 -12.685 1.00 86.12  ? 172 PRO A O   1 
ATOM   1092 C  CB  . PRO A 1 172 ? 16.343 51.671 -11.216 1.00 86.19  ? 172 PRO A CB  1 
ATOM   1093 C  CG  . PRO A 1 172 ? 15.222 52.191 -10.402 1.00 86.42  ? 172 PRO A CG  1 
ATOM   1094 C  CD  . PRO A 1 172 ? 14.521 51.018 -9.845  1.00 84.81  ? 172 PRO A CD  1 
ATOM   1095 N  N   . LEU A 1 173 ? 17.286 48.679 -10.490 1.00 86.29  ? 173 LEU A N   1 
ATOM   1096 C  CA  . LEU A 1 173 ? 18.379 47.723 -10.357 1.00 86.72  ? 173 LEU A CA  1 
ATOM   1097 C  C   . LEU A 1 173 ? 18.075 46.404 -11.047 1.00 87.50  ? 173 LEU A C   1 
ATOM   1098 O  O   . LEU A 1 173 ? 18.931 45.887 -11.765 1.00 87.39  ? 173 LEU A O   1 
ATOM   1099 C  CB  . LEU A 1 173 ? 18.753 47.506 -8.890  1.00 86.94  ? 173 LEU A CB  1 
ATOM   1100 C  CG  . LEU A 1 173 ? 19.895 46.512 -8.613  1.00 88.37  ? 173 LEU A CG  1 
ATOM   1101 C  CD1 . LEU A 1 173 ? 21.193 46.967 -9.274  1.00 88.74  ? 173 LEU A CD1 1 
ATOM   1102 C  CD2 . LEU A 1 173 ? 20.086 46.300 -7.114  1.00 88.72  ? 173 LEU A CD2 1 
ATOM   1103 N  N   . GLU A 1 174 ? 16.867 45.858 -10.853 1.00 88.27  ? 174 GLU A N   1 
ATOM   1104 C  CA  . GLU A 1 174 ? 16.496 44.598 -11.501 1.00 89.81  ? 174 GLU A CA  1 
ATOM   1105 C  C   . GLU A 1 174 ? 16.421 44.732 -13.025 1.00 91.63  ? 174 GLU A C   1 
ATOM   1106 O  O   . GLU A 1 174 ? 16.671 43.766 -13.745 1.00 91.91  ? 174 GLU A O   1 
ATOM   1107 C  CB  . GLU A 1 174 ? 15.199 44.028 -10.922 1.00 91.83  ? 174 GLU A CB  1 
ATOM   1108 C  CG  . GLU A 1 174 ? 15.348 43.522 -9.499  1.00 95.99  ? 174 GLU A CG  1 
ATOM   1109 C  CD  . GLU A 1 174 ? 14.097 42.904 -8.909  1.00 101.06 ? 174 GLU A CD  1 
ATOM   1110 O  OE1 . GLU A 1 174 ? 13.227 42.459 -9.689  1.00 102.38 ? 174 GLU A OE1 1 
ATOM   1111 O  OE2 . GLU A 1 174 ? 13.987 42.866 -7.664  1.00 103.01 ? 174 GLU A OE2 1 
ATOM   1112 N  N   . GLU A 1 175 ? 16.114 45.937 -13.515 1.00 92.71  ? 175 GLU A N   1 
ATOM   1113 C  CA  . GLU A 1 175 ? 16.093 46.233 -14.935 1.00 94.16  ? 175 GLU A CA  1 
ATOM   1114 C  C   . GLU A 1 175 ? 17.529 46.189 -15.470 1.00 94.90  ? 175 GLU A C   1 
ATOM   1115 O  O   . GLU A 1 175 ? 17.787 45.537 -16.478 1.00 95.02  ? 175 GLU A O   1 
ATOM   1116 C  CB  . GLU A 1 175 ? 15.463 47.612 -15.169 1.00 97.17  ? 175 GLU A CB  1 
ATOM   1117 C  CG  . GLU A 1 175 ? 15.436 48.010 -16.626 1.00 104.03 ? 175 GLU A CG  1 
ATOM   1118 C  CD  . GLU A 1 175 ? 14.404 49.068 -16.962 1.00 113.97 ? 175 GLU A CD  1 
ATOM   1119 O  OE1 . GLU A 1 175 ? 14.003 49.826 -16.047 1.00 116.08 ? 175 GLU A OE1 1 
ATOM   1120 O  OE2 . GLU A 1 175 ? 14.000 49.141 -18.146 1.00 117.27 ? 175 GLU A OE2 1 
ATOM   1121 N  N   . LYS A 1 176 ? 18.465 46.839 -14.764 1.00 95.31  ? 176 LYS A N   1 
ATOM   1122 C  CA  . LYS A 1 176 ? 19.884 46.872 -15.118 1.00 96.22  ? 176 LYS A CA  1 
ATOM   1123 C  C   . LYS A 1 176 ? 20.499 45.467 -15.091 1.00 97.15  ? 176 LYS A C   1 
ATOM   1124 O  O   . LYS A 1 176 ? 21.337 45.139 -15.930 1.00 97.34  ? 176 LYS A O   1 
ATOM   1125 C  CB  . LYS A 1 176 ? 20.634 47.795 -14.145 1.00 97.78  ? 176 LYS A CB  1 
ATOM   1126 C  CG  . LYS A 1 176 ? 22.123 47.907 -14.406 1.00 101.21 ? 176 LYS A CG  1 
ATOM   1127 C  CD  . LYS A 1 176 ? 22.780 48.771 -13.354 1.00 105.35 ? 176 LYS A CD  1 
ATOM   1128 C  CE  . LYS A 1 176 ? 24.240 49.031 -13.644 1.00 109.16 ? 176 LYS A CE  1 
ATOM   1129 N  NZ  . LYS A 1 176 ? 24.422 49.937 -14.809 1.00 111.37 ? 176 LYS A NZ  1 
ATOM   1130 N  N   . LEU A 1 177 ? 20.075 44.635 -14.134 1.00 97.51  ? 177 LEU A N   1 
ATOM   1131 C  CA  . LEU A 1 177 ? 20.591 43.271 -14.023 1.00 98.12  ? 177 LEU A CA  1 
ATOM   1132 C  C   . LEU A 1 177 ? 19.884 42.257 -14.915 1.00 98.93  ? 177 LEU A C   1 
ATOM   1133 O  O   . LEU A 1 177 ? 20.352 41.120 -15.018 1.00 99.33  ? 177 LEU A O   1 
ATOM   1134 C  CB  . LEU A 1 177 ? 20.556 42.791 -12.570 1.00 97.97  ? 177 LEU A CB  1 
ATOM   1135 C  CG  . LEU A 1 177 ? 21.391 43.594 -11.596 1.00 98.73  ? 177 LEU A CG  1 
ATOM   1136 C  CD1 . LEU A 1 177 ? 21.225 43.061 -10.201 1.00 99.21  ? 177 LEU A CD1 1 
ATOM   1137 C  CD2 . LEU A 1 177 ? 22.860 43.594 -11.989 1.00 99.03  ? 177 LEU A CD2 1 
ATOM   1138 N  N   . ASN A 1 178 ? 18.756 42.646 -15.530 1.00 98.98  ? 178 ASN A N   1 
ATOM   1139 C  CA  . ASN A 1 178 ? 17.972 41.784 -16.408 1.00 99.46  ? 178 ASN A CA  1 
ATOM   1140 C  C   . ASN A 1 178 ? 17.496 40.553 -15.644 1.00 99.04  ? 178 ASN A C   1 
ATOM   1141 O  O   . ASN A 1 178 ? 17.670 39.427 -16.107 1.00 99.25  ? 178 ASN A O   1 
ATOM   1142 C  CB  . ASN A 1 178 ? 18.776 41.400 -17.669 1.00 101.16 ? 178 ASN A CB  1 
ATOM   1143 C  CG  . ASN A 1 178 ? 17.946 40.752 -18.751 1.00 104.85 ? 178 ASN A CG  1 
ATOM   1144 O  OD1 . ASN A 1 178 ? 16.762 41.067 -18.928 1.00 106.27 ? 178 ASN A OD1 1 
ATOM   1145 N  ND2 . ASN A 1 178 ? 18.545 39.819 -19.485 1.00 105.28 ? 178 ASN A ND2 1 
ATOM   1146 N  N   . THR A 1 179 ? 16.935 40.763 -14.446 1.00 98.23  ? 179 THR A N   1 
ATOM   1147 C  CA  . THR A 1 179 ? 16.462 39.644 -13.629 1.00 97.65  ? 179 THR A CA  1 
ATOM   1148 C  C   . THR A 1 179 ? 15.232 38.979 -14.235 1.00 96.87  ? 179 THR A C   1 
ATOM   1149 O  O   . THR A 1 179 ? 14.527 39.585 -15.043 1.00 96.93  ? 179 THR A O   1 
ATOM   1150 C  CB  . THR A 1 179 ? 16.226 40.062 -12.167 1.00 98.76  ? 179 THR A CB  1 
ATOM   1151 O  OG1 . THR A 1 179 ? 14.987 40.767 -12.056 1.00 99.68  ? 179 THR A OG1 1 
ATOM   1152 C  CG2 . THR A 1 179 ? 17.372 40.883 -11.598 1.00 99.22  ? 179 THR A CG2 1 
ATOM   1153 N  N   . ASP A 1 180 ? 14.953 37.741 -13.820 1.00 95.92  ? 180 ASP A N   1 
ATOM   1154 C  CA  . ASP A 1 180 ? 13.788 37.019 -14.308 1.00 95.09  ? 180 ASP A CA  1 
ATOM   1155 C  C   . ASP A 1 180 ? 12.490 37.382 -13.559 1.00 93.84  ? 180 ASP A C   1 
ATOM   1156 O  O   . ASP A 1 180 ? 11.477 36.710 -13.740 1.00 94.14  ? 180 ASP A O   1 
ATOM   1157 C  CB  . ASP A 1 180 ? 14.042 35.506 -14.252 1.00 96.90  ? 180 ASP A CB  1 
ATOM   1158 C  CG  . ASP A 1 180 ? 13.972 34.915 -12.858 1.00 101.60 ? 180 ASP A CG  1 
ATOM   1159 O  OD1 . ASP A 1 180 ? 14.102 35.683 -11.880 1.00 102.75 ? 180 ASP A OD1 1 
ATOM   1160 O  OD2 . ASP A 1 180 ? 13.771 33.691 -12.745 1.00 103.27 ? 180 ASP A OD2 1 
ATOM   1161 N  N   . GLY A 1 181 ? 12.532 38.397 -12.703 1.00 92.48  ? 181 GLY A N   1 
ATOM   1162 C  CA  . GLY A 1 181 ? 11.365 38.805 -11.935 1.00 91.47  ? 181 GLY A CA  1 
ATOM   1163 C  C   . GLY A 1 181 ? 11.212 38.092 -10.605 1.00 89.95  ? 181 GLY A C   1 
ATOM   1164 O  O   . GLY A 1 181 ? 10.266 38.377 -9.864  1.00 90.09  ? 181 GLY A O   1 
ATOM   1165 N  N   . GLN A 1 182 ? 12.124 37.152 -10.287 1.00 88.19  ? 182 GLN A N   1 
ATOM   1166 C  CA  . GLN A 1 182 ? 12.096 36.468 -9.001  1.00 86.70  ? 182 GLN A CA  1 
ATOM   1167 C  C   . GLN A 1 182 ? 13.077 37.136 -8.049  1.00 85.63  ? 182 GLN A C   1 
ATOM   1168 O  O   . GLN A 1 182 ? 14.099 37.674 -8.491  1.00 85.97  ? 182 GLN A O   1 
ATOM   1169 C  CB  . GLN A 1 182 ? 12.418 34.981 -9.142  1.00 87.11  ? 182 GLN A CB  1 
ATOM   1170 C  CG  . GLN A 1 182 ? 11.384 34.225 -9.948  1.00 87.63  ? 182 GLN A CG  1 
ATOM   1171 C  CD  . GLN A 1 182 ? 11.648 32.755 -9.894  1.00 89.28  ? 182 GLN A CD  1 
ATOM   1172 O  OE1 . GLN A 1 182 ? 10.989 32.014 -9.160  1.00 90.92  ? 182 GLN A OE1 1 
ATOM   1173 N  NE2 . GLN A 1 182 ? 12.626 32.300 -10.662 1.00 88.31  ? 182 GLN A NE2 1 
ATOM   1174 N  N   . ARG A 1 183 ? 12.760 37.130 -6.745  1.00 84.09  ? 183 ARG A N   1 
ATOM   1175 C  CA  . ARG A 1 183 ? 13.623 37.774 -5.768  1.00 82.96  ? 183 ARG A CA  1 
ATOM   1176 C  C   . ARG A 1 183 ? 13.493 37.175 -4.387  1.00 81.83  ? 183 ARG A C   1 
ATOM   1177 O  O   . ARG A 1 183 ? 12.480 36.571 -4.070  1.00 81.56  ? 183 ARG A O   1 
ATOM   1178 C  CB  . ARG A 1 183 ? 13.383 39.292 -5.736  1.00 83.83  ? 183 ARG A CB  1 
ATOM   1179 C  CG  . ARG A 1 183 ? 12.070 39.681 -5.085  1.00 86.53  ? 183 ARG A CG  1 
ATOM   1180 C  CD  . ARG A 1 183 ? 11.752 41.147 -5.268  1.00 89.46  ? 183 ARG A CD  1 
ATOM   1181 N  NE  . ARG A 1 183 ? 11.614 41.502 -6.682  1.00 92.14  ? 183 ARG A NE  1 
ATOM   1182 C  CZ  . ARG A 1 183 ? 10.498 41.363 -7.388  1.00 93.02  ? 183 ARG A CZ  1 
ATOM   1183 N  NH1 . ARG A 1 183 ? 9.400  40.880 -6.821  1.00 92.12  ? 183 ARG A NH1 1 
ATOM   1184 N  NH2 . ARG A 1 183 ? 10.471 41.704 -8.668  1.00 92.46  ? 183 ARG A NH2 1 
ATOM   1185 N  N   . ALA A 1 184 ? 14.538 37.337 -3.569  1.00 81.05  ? 184 ALA A N   1 
ATOM   1186 C  CA  . ALA A 1 184 ? 14.582 36.876 -2.181  1.00 80.23  ? 184 ALA A CA  1 
ATOM   1187 C  C   . ALA A 1 184 ? 15.297 37.910 -1.320  1.00 79.10  ? 184 ALA A C   1 
ATOM   1188 O  O   . ALA A 1 184 ? 16.075 38.712 -1.825  1.00 79.08  ? 184 ALA A O   1 
ATOM   1189 C  CB  . ALA A 1 184 ? 15.304 35.544 -2.088  1.00 80.49  ? 184 ALA A CB  1 
ATOM   1190 N  N   . ILE A 1 185 ? 15.001 37.917 -0.023  1.00 78.24  ? 185 ILE A N   1 
ATOM   1191 C  CA  . ILE A 1 185 ? 15.633 38.807 0.951   1.00 77.63  ? 185 ILE A CA  1 
ATOM   1192 C  C   . ILE A 1 185 ? 16.320 37.924 2.011   1.00 77.72  ? 185 ILE A C   1 
ATOM   1193 O  O   . ILE A 1 185 ? 15.762 36.920 2.440   1.00 77.87  ? 185 ILE A O   1 
ATOM   1194 C  CB  . ILE A 1 185 ? 14.623 39.820 1.578   1.00 77.03  ? 185 ILE A CB  1 
ATOM   1195 C  CG1 . ILE A 1 185 ? 15.315 40.813 2.519   1.00 77.42  ? 185 ILE A CG1 1 
ATOM   1196 C  CG2 . ILE A 1 185 ? 13.474 39.122 2.283   1.00 77.12  ? 185 ILE A CG2 1 
ATOM   1197 C  CD1 . ILE A 1 185 ? 15.850 41.974 1.865   1.00 78.18  ? 185 ILE A CD1 1 
ATOM   1198 N  N   . ALA A 1 186 ? 17.547 38.257 2.385   1.00 77.28  ? 186 ALA A N   1 
ATOM   1199 C  CA  . ALA A 1 186 ? 18.279 37.517 3.408   1.00 77.08  ? 186 ALA A CA  1 
ATOM   1200 C  C   . ALA A 1 186 ? 18.983 38.509 4.308   1.00 76.83  ? 186 ALA A C   1 
ATOM   1201 O  O   . ALA A 1 186 ? 19.416 39.558 3.848   1.00 76.96  ? 186 ALA A O   1 
ATOM   1202 C  CB  . ALA A 1 186 ? 19.289 36.581 2.768   1.00 77.16  ? 186 ALA A CB  1 
ATOM   1203 N  N   . GLY A 1 187 ? 19.071 38.196 5.586   1.00 76.40  ? 187 GLY A N   1 
ATOM   1204 C  CA  . GLY A 1 187 ? 19.729 39.076 6.540   1.00 76.51  ? 187 GLY A CA  1 
ATOM   1205 C  C   . GLY A 1 187 ? 20.322 38.314 7.695   1.00 76.10  ? 187 GLY A C   1 
ATOM   1206 O  O   . GLY A 1 187 ? 19.876 37.208 7.991   1.00 76.13  ? 187 GLY A O   1 
ATOM   1207 N  N   . MET A 1 188 ? 21.315 38.906 8.375   1.00 75.31  ? 188 MET A N   1 
ATOM   1208 C  CA  . MET A 1 188 ? 21.929 38.264 9.529   1.00 74.80  ? 188 MET A CA  1 
ATOM   1209 C  C   . MET A 1 188 ? 21.950 39.181 10.726  1.00 75.09  ? 188 MET A C   1 
ATOM   1210 O  O   . MET A 1 188 ? 22.106 40.400 10.588  1.00 75.62  ? 188 MET A O   1 
ATOM   1211 C  CB  . MET A 1 188 ? 23.356 37.848 9.218   1.00 74.71  ? 188 MET A CB  1 
ATOM   1212 C  CG  . MET A 1 188 ? 24.201 38.991 8.778   1.00 74.69  ? 188 MET A CG  1 
ATOM   1213 S  SD  . MET A 1 188 ? 25.923 38.629 8.994   1.00 71.87  ? 188 MET A SD  1 
ATOM   1214 C  CE  . MET A 1 188 ? 26.613 40.090 8.274   1.00 68.67  ? 188 MET A CE  1 
ATOM   1215 N  N   . SER A 1 189 ? 21.786 38.603 11.909  1.00 74.57  ? 189 SER A N   1 
ATOM   1216 C  CA  . SER A 1 189 ? 21.846 39.361 13.144  1.00 74.63  ? 189 SER A CA  1 
ATOM   1217 C  C   . SER A 1 189 ? 20.789 40.481 13.190  1.00 74.75  ? 189 SER A C   1 
ATOM   1218 O  O   . SER A 1 189 ? 19.609 40.143 13.235  1.00 74.95  ? 189 SER A O   1 
ATOM   1219 C  CB  . SER A 1 189 ? 23.267 39.848 13.401  1.00 75.82  ? 189 SER A CB  1 
ATOM   1220 O  OG  . SER A 1 189 ? 23.744 39.244 14.588  1.00 78.47  ? 189 SER A OG  1 
ATOM   1221 N  N   . MET A 1 190 ? 21.164 41.779 13.154  1.00 74.35  ? 190 MET A N   1 
ATOM   1222 C  CA  . MET A 1 190 ? 20.161 42.839 13.164  1.00 74.14  ? 190 MET A CA  1 
ATOM   1223 C  C   . MET A 1 190 ? 19.234 42.763 11.931  1.00 74.46  ? 190 MET A C   1 
ATOM   1224 O  O   . MET A 1 190 ? 18.022 42.914 12.077  1.00 74.61  ? 190 MET A O   1 
ATOM   1225 C  CB  . MET A 1 190 ? 20.801 44.215 13.309  1.00 74.00  ? 190 MET A CB  1 
ATOM   1226 C  CG  . MET A 1 190 ? 21.393 44.743 12.050  1.00 74.33  ? 190 MET A CG  1 
ATOM   1227 S  SD  . MET A 1 190 ? 21.354 46.516 11.930  1.00 74.76  ? 190 MET A SD  1 
ATOM   1228 C  CE  . MET A 1 190 ? 21.728 46.668 10.285  1.00 70.94  ? 190 MET A CE  1 
ATOM   1229 N  N   . SER A 1 191 ? 19.787 42.464 10.739  1.00 74.33  ? 191 SER A N   1 
ATOM   1230 C  CA  . SER A 1 191 ? 18.974 42.362 9.536   1.00 74.62  ? 191 SER A CA  1 
ATOM   1231 C  C   . SER A 1 191 ? 18.259 41.011 9.380   1.00 75.10  ? 191 SER A C   1 
ATOM   1232 O  O   . SER A 1 191 ? 17.529 40.823 8.411   1.00 75.94  ? 191 SER A O   1 
ATOM   1233 C  CB  . SER A 1 191 ? 19.778 42.711 8.300   1.00 75.76  ? 191 SER A CB  1 
ATOM   1234 O  OG  . SER A 1 191 ? 20.836 41.784 8.174   1.00 78.55  ? 191 SER A OG  1 
ATOM   1235 N  N   . ALA A 1 192 ? 18.394 40.097 10.354  1.00 74.38  ? 192 ALA A N   1 
ATOM   1236 C  CA  . ALA A 1 192 ? 17.600 38.874 10.380  1.00 74.02  ? 192 ALA A CA  1 
ATOM   1237 C  C   . ALA A 1 192 ? 16.187 39.183 10.919  1.00 74.36  ? 192 ALA A C   1 
ATOM   1238 O  O   . ALA A 1 192 ? 15.320 38.321 10.857  1.00 75.02  ? 192 ALA A O   1 
ATOM   1239 C  CB  . ALA A 1 192 ? 18.271 37.800 11.208  1.00 73.95  ? 192 ALA A CB  1 
ATOM   1240 N  N   . THR A 1 193 ? 15.949 40.404 11.449  1.00 73.96  ? 193 THR A N   1 
ATOM   1241 C  CA  . THR A 1 193 ? 14.650 40.949 11.832  1.00 73.77  ? 193 THR A CA  1 
ATOM   1242 C  C   . THR A 1 193 ? 14.072 41.557 10.529  1.00 73.70  ? 193 THR A C   1 
ATOM   1243 O  O   . THR A 1 193 ? 12.931 41.297 10.184  1.00 74.32  ? 193 THR A O   1 
ATOM   1244 C  CB  . THR A 1 193 ? 14.805 42.040 12.926  1.00 75.00  ? 193 THR A CB  1 
ATOM   1245 O  OG1 . THR A 1 193 ? 15.352 41.456 14.122  1.00 75.97  ? 193 THR A OG1 1 
ATOM   1246 C  CG2 . THR A 1 193 ? 13.485 42.742 13.241  1.00 74.92  ? 193 THR A CG2 1 
ATOM   1247 N  N   . THR A 1 194 ? 14.877 42.334 9.795   1.00 72.85  ? 194 THR A N   1 
ATOM   1248 C  CA  . THR A 1 194 ? 14.532 42.961 8.530   1.00 72.54  ? 194 THR A CA  1 
ATOM   1249 C  C   . THR A 1 194 ? 14.043 41.955 7.495   1.00 73.18  ? 194 THR A C   1 
ATOM   1250 O  O   . THR A 1 194 ? 13.028 42.202 6.859   1.00 73.92  ? 194 THR A O   1 
ATOM   1251 C  CB  . THR A 1 194 ? 15.753 43.685 7.969   1.00 73.13  ? 194 THR A CB  1 
ATOM   1252 O  OG1 . THR A 1 194 ? 16.318 44.529 8.967   1.00 73.91  ? 194 THR A OG1 1 
ATOM   1253 C  CG2 . THR A 1 194 ? 15.437 44.464 6.737   1.00 73.44  ? 194 THR A CG2 1 
ATOM   1254 N  N   . SER A 1 195 ? 14.753 40.821 7.309   1.00 72.84  ? 195 SER A N   1 
ATOM   1255 C  CA  . SER A 1 195 ? 14.380 39.818 6.315   1.00 72.30  ? 195 SER A CA  1 
ATOM   1256 C  C   . SER A 1 195 ? 13.069 39.109 6.608   1.00 72.36  ? 195 SER A C   1 
ATOM   1257 O  O   . SER A 1 195 ? 12.530 38.465 5.714   1.00 72.87  ? 195 SER A O   1 
ATOM   1258 C  CB  . SER A 1 195 ? 15.497 38.812 6.120   1.00 73.10  ? 195 SER A CB  1 
ATOM   1259 O  OG  . SER A 1 195 ? 15.627 37.996 7.269   1.00 74.76  ? 195 SER A OG  1 
ATOM   1260 N  N   . LEU A 1 196 ? 12.548 39.219 7.845   1.00 71.73  ? 196 LEU A N   1 
ATOM   1261 C  CA  . LEU A 1 196 ? 11.237 38.695 8.192   1.00 71.34  ? 196 LEU A CA  1 
ATOM   1262 C  C   . LEU A 1 196 ? 10.196 39.819 8.052   1.00 71.63  ? 196 LEU A C   1 
ATOM   1263 O  O   . LEU A 1 196 ? 9.089  39.548 7.637   1.00 72.42  ? 196 LEU A O   1 
ATOM   1264 C  CB  . LEU A 1 196 ? 11.194 38.100 9.609   1.00 70.80  ? 196 LEU A CB  1 
ATOM   1265 C  CG  . LEU A 1 196 ? 12.017 36.842 9.838   1.00 71.71  ? 196 LEU A CG  1 
ATOM   1266 C  CD1 . LEU A 1 196 ? 11.866 36.372 11.246  1.00 71.63  ? 196 LEU A CD1 1 
ATOM   1267 C  CD2 . LEU A 1 196 ? 11.633 35.718 8.869   1.00 72.38  ? 196 LEU A CD2 1 
ATOM   1268 N  N   . LEU A 1 197 ? 10.542 41.069 8.390   1.00 71.03  ? 197 LEU A N   1 
ATOM   1269 C  CA  . LEU A 1 197 ? 9.621  42.202 8.320   1.00 70.39  ? 197 LEU A CA  1 
ATOM   1270 C  C   . LEU A 1 197 ? 9.263  42.598 6.905   1.00 72.34  ? 197 LEU A C   1 
ATOM   1271 O  O   . LEU A 1 197 ? 8.104  42.902 6.655   1.00 72.93  ? 197 LEU A O   1 
ATOM   1272 C  CB  . LEU A 1 197 ? 10.167 43.415 9.085   1.00 68.61  ? 197 LEU A CB  1 
ATOM   1273 C  CG  . LEU A 1 197 ? 10.142 43.340 10.593  1.00 67.52  ? 197 LEU A CG  1 
ATOM   1274 C  CD1 . LEU A 1 197 ? 10.782 44.572 11.207  1.00 67.04  ? 197 LEU A CD1 1 
ATOM   1275 C  CD2 . LEU A 1 197 ? 8.734  43.165 11.092  1.00 67.70  ? 197 LEU A CD2 1 
ATOM   1276 N  N   . PHE A 1 198 ? 10.239 42.633 5.987   1.00 73.43  ? 198 PHE A N   1 
ATOM   1277 C  CA  . PHE A 1 198 ? 9.986  43.001 4.593   1.00 74.73  ? 198 PHE A CA  1 
ATOM   1278 C  C   . PHE A 1 198 ? 8.905  42.135 3.932   1.00 76.63  ? 198 PHE A C   1 
ATOM   1279 O  O   . PHE A 1 198 ? 7.921  42.711 3.468   1.00 77.46  ? 198 PHE A O   1 
ATOM   1280 C  CB  . PHE A 1 198 ? 11.276 43.033 3.760   1.00 74.54  ? 198 PHE A CB  1 
ATOM   1281 C  CG  . PHE A 1 198 ? 12.160 44.250 3.920   1.00 75.00  ? 198 PHE A CG  1 
ATOM   1282 C  CD1 . PHE A 1 198 ? 11.970 45.137 4.964   1.00 75.65  ? 198 PHE A CD1 1 
ATOM   1283 C  CD2 . PHE A 1 198 ? 13.200 44.487 3.044   1.00 75.73  ? 198 PHE A CD2 1 
ATOM   1284 C  CE1 . PHE A 1 198 ? 12.807 46.226 5.129   1.00 75.95  ? 198 PHE A CE1 1 
ATOM   1285 C  CE2 . PHE A 1 198 ? 14.032 45.584 3.213   1.00 76.12  ? 198 PHE A CE2 1 
ATOM   1286 C  CZ  . PHE A 1 198 ? 13.833 46.439 4.256   1.00 75.66  ? 198 PHE A CZ  1 
ATOM   1287 N  N   . PRO A 1 199 ? 8.980  40.784 3.940   1.00 77.29  ? 199 PRO A N   1 
ATOM   1288 C  CA  . PRO A 1 199 ? 7.898  39.992 3.317   1.00 78.13  ? 199 PRO A CA  1 
ATOM   1289 C  C   . PRO A 1 199 ? 6.536  40.099 4.009   1.00 79.19  ? 199 PRO A C   1 
ATOM   1290 O  O   . PRO A 1 199 ? 5.509  39.819 3.390   1.00 79.67  ? 199 PRO A O   1 
ATOM   1291 C  CB  . PRO A 1 199 ? 8.427  38.554 3.361   1.00 78.60  ? 199 PRO A CB  1 
ATOM   1292 C  CG  . PRO A 1 199 ? 9.472  38.545 4.379   1.00 78.84  ? 199 PRO A CG  1 
ATOM   1293 C  CD  . PRO A 1 199 ? 10.078 39.914 4.402   1.00 77.07  ? 199 PRO A CD  1 
ATOM   1294 N  N   . GLN A 1 200 ? 6.526  40.463 5.294   1.00 79.12  ? 200 GLN A N   1 
ATOM   1295 C  CA  . GLN A 1 200 ? 5.284  40.657 6.034   1.00 79.53  ? 200 GLN A CA  1 
ATOM   1296 C  C   . GLN A 1 200 ? 4.650  41.998 5.615   1.00 80.85  ? 200 GLN A C   1 
ATOM   1297 O  O   . GLN A 1 200 ? 3.427  42.106 5.514   1.00 81.53  ? 200 GLN A O   1 
ATOM   1298 C  CB  . GLN A 1 200 ? 5.559  40.695 7.546   1.00 79.87  ? 200 GLN A CB  1 
ATOM   1299 C  CG  . GLN A 1 200 ? 5.959  39.370 8.175   1.00 80.24  ? 200 GLN A CG  1 
ATOM   1300 C  CD  . GLN A 1 200 ? 6.335  39.508 9.634   1.00 82.18  ? 200 GLN A CD  1 
ATOM   1301 O  OE1 . GLN A 1 200 ? 6.258  40.584 10.240  1.00 83.31  ? 200 GLN A OE1 1 
ATOM   1302 N  NE2 . GLN A 1 200 ? 6.751  38.412 10.239  1.00 82.17  ? 200 GLN A NE2 1 
ATOM   1303 N  N   . HIS A 1 201 ? 5.484  43.031 5.408   1.00 80.91  ? 201 HIS A N   1 
ATOM   1304 C  CA  . HIS A 1 201 ? 5.020  44.356 5.025   1.00 81.30  ? 201 HIS A CA  1 
ATOM   1305 C  C   . HIS A 1 201 ? 4.564  44.392 3.565   1.00 82.69  ? 201 HIS A C   1 
ATOM   1306 O  O   . HIS A 1 201 ? 3.685  45.173 3.217   1.00 83.07  ? 201 HIS A O   1 
ATOM   1307 C  CB  . HIS A 1 201 ? 6.130  45.396 5.263   1.00 81.27  ? 201 HIS A CB  1 
ATOM   1308 C  CG  . HIS A 1 201 ? 6.441  45.678 6.707   1.00 82.21  ? 201 HIS A CG  1 
ATOM   1309 N  ND1 . HIS A 1 201 ? 7.350  46.664 7.073   1.00 83.33  ? 201 HIS A ND1 1 
ATOM   1310 C  CD2 . HIS A 1 201 ? 5.950  45.108 7.833   1.00 83.07  ? 201 HIS A CD2 1 
ATOM   1311 C  CE1 . HIS A 1 201 ? 7.387  46.650 8.395   1.00 83.53  ? 201 HIS A CE1 1 
ATOM   1312 N  NE2 . HIS A 1 201 ? 6.561  45.734 8.899   1.00 83.66  ? 201 HIS A NE2 1 
ATOM   1313 N  N   . PHE A 1 202 ? 5.165  43.560 2.703   1.00 83.39  ? 202 PHE A N   1 
ATOM   1314 C  CA  . PHE A 1 202 ? 4.853  43.522 1.276   1.00 83.82  ? 202 PHE A CA  1 
ATOM   1315 C  C   . PHE A 1 202 ? 4.642  42.086 0.849   1.00 84.06  ? 202 PHE A C   1 
ATOM   1316 O  O   . PHE A 1 202 ? 5.496  41.490 0.186   1.00 84.56  ? 202 PHE A O   1 
ATOM   1317 C  CB  . PHE A 1 202 ? 5.994  44.155 0.469   1.00 84.22  ? 202 PHE A CB  1 
ATOM   1318 C  CG  . PHE A 1 202 ? 6.343  45.545 0.927   1.00 85.69  ? 202 PHE A CG  1 
ATOM   1319 C  CD1 . PHE A 1 202 ? 5.673  46.645 0.423   1.00 86.54  ? 202 PHE A CD1 1 
ATOM   1320 C  CD2 . PHE A 1 202 ? 7.326  45.751 1.878   1.00 86.99  ? 202 PHE A CD2 1 
ATOM   1321 C  CE1 . PHE A 1 202 ? 5.989  47.923 0.849   1.00 87.32  ? 202 PHE A CE1 1 
ATOM   1322 C  CE2 . PHE A 1 202 ? 7.622  47.030 2.320   1.00 87.79  ? 202 PHE A CE2 1 
ATOM   1323 C  CZ  . PHE A 1 202 ? 6.965  48.109 1.787   1.00 87.35  ? 202 PHE A CZ  1 
ATOM   1324 N  N   . PRO A 1 203 ? 3.508  41.491 1.257   1.00 83.86  ? 203 PRO A N   1 
ATOM   1325 C  CA  . PRO A 1 203 ? 3.266  40.080 0.927   1.00 83.46  ? 203 PRO A CA  1 
ATOM   1326 C  C   . PRO A 1 203 ? 3.314  39.793 -0.569  1.00 83.15  ? 203 PRO A C   1 
ATOM   1327 O  O   . PRO A 1 203 ? 2.811  40.588 -1.362  1.00 83.65  ? 203 PRO A O   1 
ATOM   1328 C  CB  . PRO A 1 203 ? 1.882  39.815 1.523   1.00 84.26  ? 203 PRO A CB  1 
ATOM   1329 C  CG  . PRO A 1 203 ? 1.724  40.846 2.617   1.00 84.84  ? 203 PRO A CG  1 
ATOM   1330 C  CD  . PRO A 1 203 ? 2.404  42.056 2.064   1.00 83.47  ? 203 PRO A CD  1 
ATOM   1331 N  N   . GLY A 1 204 ? 3.988  38.708 -0.945  1.00 82.01  ? 204 GLY A N   1 
ATOM   1332 C  CA  . GLY A 1 204 ? 4.119  38.324 -2.341  1.00 81.15  ? 204 GLY A CA  1 
ATOM   1333 C  C   . GLY A 1 204 ? 5.258  38.964 -3.106  1.00 80.40  ? 204 GLY A C   1 
ATOM   1334 O  O   . GLY A 1 204 ? 5.558  38.510 -4.210  1.00 80.49  ? 204 GLY A O   1 
ATOM   1335 N  N   . PHE A 1 205 ? 5.912  40.017 -2.553  1.00 79.66  ? 205 PHE A N   1 
ATOM   1336 C  CA  . PHE A 1 205 ? 7.025  40.684 -3.251  1.00 79.19  ? 205 PHE A CA  1 
ATOM   1337 C  C   . PHE A 1 205 ? 8.255  39.792 -3.315  1.00 78.90  ? 205 PHE A C   1 
ATOM   1338 O  O   . PHE A 1 205 ? 8.938  39.748 -4.332  1.00 79.25  ? 205 PHE A O   1 
ATOM   1339 C  CB  . PHE A 1 205 ? 7.376  42.026 -2.597  1.00 78.93  ? 205 PHE A CB  1 
ATOM   1340 C  CG  . PHE A 1 205 ? 8.371  42.856 -3.376  1.00 79.63  ? 205 PHE A CG  1 
ATOM   1341 C  CD1 . PHE A 1 205 ? 8.170  43.133 -4.715  1.00 80.37  ? 205 PHE A CD1 1 
ATOM   1342 C  CD2 . PHE A 1 205 ? 9.470  43.417 -2.751  1.00 80.31  ? 205 PHE A CD2 1 
ATOM   1343 C  CE1 . PHE A 1 205 ? 9.082  43.903 -5.425  1.00 81.05  ? 205 PHE A CE1 1 
ATOM   1344 C  CE2 . PHE A 1 205 ? 10.375 44.194 -3.464  1.00 80.91  ? 205 PHE A CE2 1 
ATOM   1345 C  CZ  . PHE A 1 205 ? 10.176 44.431 -4.796  1.00 80.77  ? 205 PHE A CZ  1 
ATOM   1346 N  N   . TYR A 1 206 ? 8.526  39.062 -2.232  1.00 78.18  ? 206 TYR A N   1 
ATOM   1347 C  CA  . TYR A 1 206 ? 9.676  38.164 -2.148  1.00 77.39  ? 206 TYR A CA  1 
ATOM   1348 C  C   . TYR A 1 206 ? 9.245  36.717 -2.259  1.00 77.91  ? 206 TYR A C   1 
ATOM   1349 O  O   . TYR A 1 206 ? 8.331  36.276 -1.564  1.00 78.28  ? 206 TYR A O   1 
ATOM   1350 C  CB  . TYR A 1 206 ? 10.457 38.381 -0.822  1.00 76.32  ? 206 TYR A CB  1 
ATOM   1351 C  CG  . TYR A 1 206 ? 11.064 39.764 -0.691  1.00 75.40  ? 206 TYR A CG  1 
ATOM   1352 C  CD1 . TYR A 1 206 ? 12.200 40.115 -1.403  1.00 75.36  ? 206 TYR A CD1 1 
ATOM   1353 C  CD2 . TYR A 1 206 ? 10.475 40.730 0.113   1.00 75.62  ? 206 TYR A CD2 1 
ATOM   1354 C  CE1 . TYR A 1 206 ? 12.737 41.391 -1.322  1.00 75.75  ? 206 TYR A CE1 1 
ATOM   1355 C  CE2 . TYR A 1 206 ? 11.000 42.013 0.200   1.00 75.92  ? 206 TYR A CE2 1 
ATOM   1356 C  CZ  . TYR A 1 206 ? 12.133 42.341 -0.522  1.00 76.59  ? 206 TYR A CZ  1 
ATOM   1357 O  OH  . TYR A 1 206 ? 12.679 43.601 -0.445  1.00 77.76  ? 206 TYR A OH  1 
ATOM   1358 N  N   . ASP A 1 207 ? 9.917  35.969 -3.116  1.00 78.03  ? 207 ASP A N   1 
ATOM   1359 C  CA  . ASP A 1 207 ? 9.672  34.537 -3.275  1.00 78.61  ? 207 ASP A CA  1 
ATOM   1360 C  C   . ASP A 1 207 ? 10.163 33.757 -2.058  1.00 78.45  ? 207 ASP A C   1 
ATOM   1361 O  O   . ASP A 1 207 ? 9.567  32.747 -1.677  1.00 78.53  ? 207 ASP A O   1 
ATOM   1362 C  CB  . ASP A 1 207 ? 10.390 34.020 -4.527  1.00 80.46  ? 207 ASP A CB  1 
ATOM   1363 C  CG  . ASP A 1 207 ? 9.790  34.563 -5.793  1.00 85.26  ? 207 ASP A CG  1 
ATOM   1364 O  OD1 . ASP A 1 207 ? 8.708  34.094 -6.180  1.00 86.34  ? 207 ASP A OD1 1 
ATOM   1365 O  OD2 . ASP A 1 207 ? 10.388 35.475 -6.389  1.00 87.63  ? 207 ASP A OD2 1 
ATOM   1366 N  N   . ALA A 1 208 ? 11.271 34.214 -1.473  1.00 78.19  ? 208 ALA A N   1 
ATOM   1367 C  CA  . ALA A 1 208 ? 11.895 33.581 -0.324  1.00 78.03  ? 208 ALA A CA  1 
ATOM   1368 C  C   . ALA A 1 208 ? 12.461 34.612 0.646   1.00 77.62  ? 208 ALA A C   1 
ATOM   1369 O  O   . ALA A 1 208 ? 12.761 35.737 0.264   1.00 77.90  ? 208 ALA A O   1 
ATOM   1370 C  CB  . ALA A 1 208 ? 13.002 32.648 -0.795  1.00 78.06  ? 208 ALA A CB  1 
ATOM   1371 N  N   . ALA A 1 209 ? 12.599 34.228 1.909   1.00 77.08  ? 209 ALA A N   1 
ATOM   1372 C  CA  . ALA A 1 209 ? 13.193 35.075 2.930   1.00 76.72  ? 209 ALA A CA  1 
ATOM   1373 C  C   . ALA A 1 209 ? 14.039 34.215 3.835   1.00 76.06  ? 209 ALA A C   1 
ATOM   1374 O  O   . ALA A 1 209 ? 13.583 33.160 4.266   1.00 76.22  ? 209 ALA A O   1 
ATOM   1375 C  CB  . ALA A 1 209 ? 12.115 35.771 3.737   1.00 76.99  ? 209 ALA A CB  1 
ATOM   1376 N  N   . ALA A 1 210 ? 15.276 34.643 4.107   1.00 75.45  ? 210 ALA A N   1 
ATOM   1377 C  CA  . ALA A 1 210 ? 16.205 33.931 4.994   1.00 74.92  ? 210 ALA A CA  1 
ATOM   1378 C  C   . ALA A 1 210 ? 16.569 34.824 6.171   1.00 74.54  ? 210 ALA A C   1 
ATOM   1379 O  O   . ALA A 1 210 ? 16.943 35.974 5.985   1.00 74.53  ? 210 ALA A O   1 
ATOM   1380 C  CB  . ALA A 1 210 ? 17.454 33.533 4.237   1.00 74.78  ? 210 ALA A CB  1 
ATOM   1381 N  N   . SER A 1 211 ? 16.406 34.318 7.387   1.00 74.31  ? 211 SER A N   1 
ATOM   1382 C  CA  . SER A 1 211 ? 16.692 35.048 8.624   1.00 74.02  ? 211 SER A CA  1 
ATOM   1383 C  C   . SER A 1 211 ? 17.806 34.301 9.336   1.00 73.27  ? 211 SER A C   1 
ATOM   1384 O  O   . SER A 1 211 ? 17.560 33.246 9.892   1.00 73.09  ? 211 SER A O   1 
ATOM   1385 C  CB  . SER A 1 211 ? 15.438 35.096 9.488   1.00 75.89  ? 211 SER A CB  1 
ATOM   1386 O  OG  . SER A 1 211 ? 15.663 35.664 10.766  1.00 79.58  ? 211 SER A OG  1 
ATOM   1387 N  N   . PHE A 1 212 ? 19.044 34.803 9.247   1.00 73.02  ? 212 PHE A N   1 
ATOM   1388 C  CA  . PHE A 1 212 ? 20.233 34.160 9.807   1.00 73.08  ? 212 PHE A CA  1 
ATOM   1389 C  C   . PHE A 1 212 ? 20.582 34.653 11.205  1.00 74.09  ? 212 PHE A C   1 
ATOM   1390 O  O   . PHE A 1 212 ? 21.313 35.633 11.342  1.00 75.20  ? 212 PHE A O   1 
ATOM   1391 C  CB  . PHE A 1 212 ? 21.451 34.402 8.903   1.00 72.32  ? 212 PHE A CB  1 
ATOM   1392 C  CG  . PHE A 1 212 ? 21.335 34.057 7.436   1.00 71.89  ? 212 PHE A CG  1 
ATOM   1393 C  CD1 . PHE A 1 212 ? 20.629 32.946 7.021   1.00 71.79  ? 212 PHE A CD1 1 
ATOM   1394 C  CD2 . PHE A 1 212 ? 21.991 34.808 6.481   1.00 72.29  ? 212 PHE A CD2 1 
ATOM   1395 C  CE1 . PHE A 1 212 ? 20.561 32.617 5.677   1.00 72.20  ? 212 PHE A CE1 1 
ATOM   1396 C  CE2 . PHE A 1 212 ? 21.921 34.470 5.138   1.00 72.56  ? 212 PHE A CE2 1 
ATOM   1397 C  CZ  . PHE A 1 212 ? 21.209 33.376 4.746   1.00 72.06  ? 212 PHE A CZ  1 
ATOM   1398 N  N   . SER A 1 213 ? 20.096 33.964 12.235  1.00 73.75  ? 213 SER A N   1 
ATOM   1399 C  CA  . SER A 1 213 ? 20.387 34.258 13.641  1.00 73.45  ? 213 SER A CA  1 
ATOM   1400 C  C   . SER A 1 213 ? 19.973 35.655 14.118  1.00 73.15  ? 213 SER A C   1 
ATOM   1401 O  O   . SER A 1 213 ? 20.818 36.510 14.330  1.00 73.34  ? 213 SER A O   1 
ATOM   1402 C  CB  . SER A 1 213 ? 21.862 34.014 13.936  1.00 73.93  ? 213 SER A CB  1 
ATOM   1403 O  OG  . SER A 1 213 ? 22.073 33.647 15.286  1.00 75.50  ? 213 SER A OG  1 
ATOM   1404 N  N   . GLY A 1 214 ? 18.693 35.852 14.349  1.00 72.88  ? 214 GLY A N   1 
ATOM   1405 C  CA  . GLY A 1 214 ? 18.194 37.129 14.837  1.00 73.42  ? 214 GLY A CA  1 
ATOM   1406 C  C   . GLY A 1 214 ? 17.057 36.980 15.817  1.00 74.05  ? 214 GLY A C   1 
ATOM   1407 O  O   . GLY A 1 214 ? 16.843 35.904 16.374  1.00 73.83  ? 214 GLY A O   1 
ATOM   1408 N  N   . CYS A 1 215 ? 16.339 38.067 16.056  1.00 74.75  ? 215 CYS A N   1 
ATOM   1409 C  CA  . CYS A 1 215 ? 15.184 38.045 16.943  1.00 76.04  ? 215 CYS A CA  1 
ATOM   1410 C  C   . CYS A 1 215 ? 14.020 38.691 16.198  1.00 76.78  ? 215 CYS A C   1 
ATOM   1411 O  O   . CYS A 1 215 ? 14.104 39.855 15.812  1.00 77.13  ? 215 CYS A O   1 
ATOM   1412 C  CB  . CYS A 1 215 ? 15.476 38.741 18.274  1.00 77.12  ? 215 CYS A CB  1 
ATOM   1413 S  SG  . CYS A 1 215 ? 14.215 38.479 19.553  1.00 80.83  ? 215 CYS A SG  1 
ATOM   1414 N  N   . ALA A 1 216 ? 12.983 37.891 15.894  1.00 76.62  ? 216 ALA A N   1 
ATOM   1415 C  CA  . ALA A 1 216 ? 11.819 38.358 15.176  1.00 76.48  ? 216 ALA A CA  1 
ATOM   1416 C  C   . ALA A 1 216 ? 11.045 39.340 16.055  1.00 77.01  ? 216 ALA A C   1 
ATOM   1417 O  O   . ALA A 1 216 ? 10.609 40.377 15.567  1.00 77.00  ? 216 ALA A O   1 
ATOM   1418 C  CB  . ALA A 1 216 ? 10.947 37.183 14.780  1.00 76.34  ? 216 ALA A CB  1 
ATOM   1419 N  N   . ALA A 1 217 ? 10.881 39.028 17.344  1.00 77.30  ? 217 ALA A N   1 
ATOM   1420 C  CA  . ALA A 1 217 ? 10.187 39.915 18.269  1.00 78.13  ? 217 ALA A CA  1 
ATOM   1421 C  C   . ALA A 1 217 ? 11.009 41.172 18.492  1.00 79.17  ? 217 ALA A C   1 
ATOM   1422 O  O   . ALA A 1 217 ? 12.234 41.116 18.512  1.00 79.73  ? 217 ALA A O   1 
ATOM   1423 C  CB  . ALA A 1 217 ? 9.955  39.213 19.591  1.00 78.20  ? 217 ALA A CB  1 
ATOM   1424 N  N   . THR A 1 218 ? 10.347 42.322 18.606  1.00 79.23  ? 218 THR A N   1 
ATOM   1425 C  CA  . THR A 1 218 ? 11.004 43.611 18.803  1.00 79.47  ? 218 THR A CA  1 
ATOM   1426 C  C   . THR A 1 218 ? 10.268 44.504 19.788  1.00 79.86  ? 218 THR A C   1 
ATOM   1427 O  O   . THR A 1 218 ? 10.819 45.529 20.175  1.00 80.10  ? 218 THR A O   1 
ATOM   1428 C  CB  . THR A 1 218 ? 11.149 44.396 17.478  1.00 80.66  ? 218 THR A CB  1 
ATOM   1429 O  OG1 . THR A 1 218 ? 9.879  44.841 17.012  1.00 82.07  ? 218 THR A OG1 1 
ATOM   1430 C  CG2 . THR A 1 218 ? 11.836 43.621 16.386  1.00 80.80  ? 218 THR A CG2 1 
ATOM   1431 N  N   . SER A 1 219 ? 9.013  44.180 20.141  1.00 79.84  ? 219 SER A N   1 
ATOM   1432 C  CA  . SER A 1 219 ? 8.205  45.024 21.026  1.00 80.25  ? 219 SER A CA  1 
ATOM   1433 C  C   . SER A 1 219 ? 8.072  44.524 22.447  1.00 80.35  ? 219 SER A C   1 
ATOM   1434 O  O   . SER A 1 219 ? 7.655  45.281 23.327  1.00 80.60  ? 219 SER A O   1 
ATOM   1435 C  CB  . SER A 1 219 ? 6.818  45.237 20.437  1.00 81.65  ? 219 SER A CB  1 
ATOM   1436 O  OG  . SER A 1 219 ? 6.086  44.028 20.408  1.00 83.68  ? 219 SER A OG  1 
ATOM   1437 N  N   . SER A 1 220 ? 8.400  43.252 22.674  1.00 80.05  ? 220 SER A N   1 
ATOM   1438 C  CA  . SER A 1 220 ? 8.371  42.643 23.993  1.00 80.24  ? 220 SER A CA  1 
ATOM   1439 C  C   . SER A 1 220 ? 9.540  43.212 24.836  1.00 80.40  ? 220 SER A C   1 
ATOM   1440 O  O   . SER A 1 220 ? 10.452 43.850 24.301  1.00 80.93  ? 220 SER A O   1 
ATOM   1441 C  CB  . SER A 1 220 ? 8.445  41.121 23.885  1.00 81.38  ? 220 SER A CB  1 
ATOM   1442 O  OG  . SER A 1 220 ? 7.712  40.600 22.787  1.00 83.88  ? 220 SER A OG  1 
ATOM   1443 N  N   . LEU A 1 221 ? 9.491  43.009 26.154  1.00 79.81  ? 221 LEU A N   1 
ATOM   1444 C  CA  . LEU A 1 221 ? 10.455 43.547 27.097  1.00 79.53  ? 221 LEU A CA  1 
ATOM   1445 C  C   . LEU A 1 221 ? 11.908 43.231 26.755  1.00 78.56  ? 221 LEU A C   1 
ATOM   1446 O  O   . LEU A 1 221 ? 12.690 44.153 26.540  1.00 79.47  ? 221 LEU A O   1 
ATOM   1447 C  CB  . LEU A 1 221 ? 10.089 43.070 28.502  1.00 80.43  ? 221 LEU A CB  1 
ATOM   1448 C  CG  . LEU A 1 221 ? 10.709 43.861 29.626  1.00 82.80  ? 221 LEU A CG  1 
ATOM   1449 C  CD1 . LEU A 1 221 ? 9.812  45.017 30.018  1.00 83.24  ? 221 LEU A CD1 1 
ATOM   1450 C  CD2 . LEU A 1 221 ? 11.015 42.951 30.823  1.00 83.70  ? 221 LEU A CD2 1 
ATOM   1451 N  N   . LEU A 1 222 ? 12.267 41.948 26.689  1.00 76.74  ? 222 LEU A N   1 
ATOM   1452 C  CA  . LEU A 1 222 ? 13.617 41.552 26.355  1.00 75.56  ? 222 LEU A CA  1 
ATOM   1453 C  C   . LEU A 1 222 ? 13.970 41.901 24.923  1.00 75.31  ? 222 LEU A C   1 
ATOM   1454 O  O   . LEU A 1 222 ? 14.961 42.601 24.746  1.00 75.86  ? 222 LEU A O   1 
ATOM   1455 C  CB  . LEU A 1 222 ? 13.868 40.078 26.677  1.00 75.36  ? 222 LEU A CB  1 
ATOM   1456 C  CG  . LEU A 1 222 ? 14.163 39.748 28.139  1.00 76.12  ? 222 LEU A CG  1 
ATOM   1457 C  CD1 . LEU A 1 222 ? 14.360 38.271 28.313  1.00 76.29  ? 222 LEU A CD1 1 
ATOM   1458 C  CD2 . LEU A 1 222 ? 15.384 40.512 28.647  1.00 76.43  ? 222 LEU A CD2 1 
ATOM   1459 N  N   . PRO A 1 223 ? 13.163 41.537 23.891  1.00 74.51  ? 223 PRO A N   1 
ATOM   1460 C  CA  . PRO A 1 223 ? 13.508 41.920 22.512  1.00 74.36  ? 223 PRO A CA  1 
ATOM   1461 C  C   . PRO A 1 223 ? 13.737 43.408 22.249  1.00 74.53  ? 223 PRO A C   1 
ATOM   1462 O  O   . PRO A 1 223 ? 14.560 43.744 21.401  1.00 74.85  ? 223 PRO A O   1 
ATOM   1463 C  CB  . PRO A 1 223 ? 12.333 41.385 21.712  1.00 75.05  ? 223 PRO A CB  1 
ATOM   1464 C  CG  . PRO A 1 223 ? 11.883 40.204 22.484  1.00 75.14  ? 223 PRO A CG  1 
ATOM   1465 C  CD  . PRO A 1 223 ? 11.979 40.655 23.896  1.00 73.73  ? 223 PRO A CD  1 
ATOM   1466 N  N   . TRP A 1 224 ? 13.049 44.291 22.975  1.00 74.36  ? 224 TRP A N   1 
ATOM   1467 C  CA  . TRP A 1 224 ? 13.274 45.733 22.842  1.00 74.80  ? 224 TRP A CA  1 
ATOM   1468 C  C   . TRP A 1 224 ? 14.674 46.103 23.355  1.00 74.83  ? 224 TRP A C   1 
ATOM   1469 O  O   . TRP A 1 224 ? 15.349 46.963 22.790  1.00 74.83  ? 224 TRP A O   1 
ATOM   1470 C  CB  . TRP A 1 224 ? 12.206 46.509 23.626  1.00 74.89  ? 224 TRP A CB  1 
ATOM   1471 C  CG  . TRP A 1 224 ? 12.358 48.002 23.587  1.00 75.58  ? 224 TRP A CG  1 
ATOM   1472 C  CD1 . TRP A 1 224 ? 12.926 48.793 24.542  1.00 76.58  ? 224 TRP A CD1 1 
ATOM   1473 C  CD2 . TRP A 1 224 ? 11.854 48.892 22.580  1.00 75.65  ? 224 TRP A CD2 1 
ATOM   1474 N  NE1 . TRP A 1 224 ? 12.851 50.116 24.170  1.00 76.75  ? 224 TRP A NE1 1 
ATOM   1475 C  CE2 . TRP A 1 224 ? 12.196 50.203 22.968  1.00 76.36  ? 224 TRP A CE2 1 
ATOM   1476 C  CE3 . TRP A 1 224 ? 11.188 48.707 21.362  1.00 76.06  ? 224 TRP A CE3 1 
ATOM   1477 C  CZ2 . TRP A 1 224 ? 11.850 51.317 22.210  1.00 76.77  ? 224 TRP A CZ2 1 
ATOM   1478 C  CZ3 . TRP A 1 224 ? 10.860 49.817 20.605  1.00 76.60  ? 224 TRP A CZ3 1 
ATOM   1479 C  CH2 . TRP A 1 224 ? 11.208 51.099 21.022  1.00 76.65  ? 224 TRP A CH2 1 
ATOM   1480 N  N   . GLU A 1 225 ? 15.107 45.448 24.430  1.00 74.59  ? 225 GLU A N   1 
ATOM   1481 C  CA  . GLU A 1 225 ? 16.419 45.667 25.000  1.00 74.51  ? 225 GLU A CA  1 
ATOM   1482 C  C   . GLU A 1 225 ? 17.533 45.174 24.074  1.00 74.27  ? 225 GLU A C   1 
ATOM   1483 O  O   . GLU A 1 225 ? 18.618 45.748 24.073  1.00 74.27  ? 225 GLU A O   1 
ATOM   1484 C  CB  . GLU A 1 225 ? 16.476 45.020 26.377  1.00 76.98  ? 225 GLU A CB  1 
ATOM   1485 C  CG  . GLU A 1 225 ? 15.417 45.559 27.327  1.00 81.82  ? 225 GLU A CG  1 
ATOM   1486 C  CD  . GLU A 1 225 ? 15.537 47.032 27.670  1.00 88.92  ? 225 GLU A CD  1 
ATOM   1487 O  OE1 . GLU A 1 225 ? 16.675 47.549 27.669  1.00 89.62  ? 225 GLU A OE1 1 
ATOM   1488 O  OE2 . GLU A 1 225 ? 14.496 47.670 27.954  1.00 91.91  ? 225 GLU A OE2 1 
ATOM   1489 N  N   . TYR A 1 226 ? 17.262 44.139 23.256  1.00 73.87  ? 226 TYR A N   1 
ATOM   1490 C  CA  . TYR A 1 226 ? 18.228 43.646 22.272  1.00 73.35  ? 226 TYR A CA  1 
ATOM   1491 C  C   . TYR A 1 226 ? 18.436 44.671 21.150  1.00 73.77  ? 226 TYR A C   1 
ATOM   1492 O  O   . TYR A 1 226 ? 19.501 44.697 20.526  1.00 74.24  ? 226 TYR A O   1 
ATOM   1493 C  CB  . TYR A 1 226 ? 17.769 42.343 21.635  1.00 72.76  ? 226 TYR A CB  1 
ATOM   1494 C  CG  . TYR A 1 226 ? 17.331 41.238 22.571  1.00 72.67  ? 226 TYR A CG  1 
ATOM   1495 C  CD1 . TYR A 1 226 ? 17.843 41.136 23.859  1.00 73.69  ? 226 TYR A CD1 1 
ATOM   1496 C  CD2 . TYR A 1 226 ? 16.517 40.213 22.124  1.00 72.83  ? 226 TYR A CD2 1 
ATOM   1497 C  CE1 . TYR A 1 226 ? 17.463 40.096 24.709  1.00 74.22  ? 226 TYR A CE1 1 
ATOM   1498 C  CE2 . TYR A 1 226 ? 16.122 39.181 22.961  1.00 73.36  ? 226 TYR A CE2 1 
ATOM   1499 C  CZ  . TYR A 1 226 ? 16.604 39.115 24.249  1.00 74.25  ? 226 TYR A CZ  1 
ATOM   1500 O  OH  . TYR A 1 226 ? 16.220 38.061 25.039  1.00 75.07  ? 226 TYR A OH  1 
ATOM   1501 N  N   . LEU A 1 227 ? 17.419 45.497 20.852  1.00 73.84  ? 227 LEU A N   1 
ATOM   1502 C  CA  . LEU A 1 227 ? 17.555 46.573 19.859  1.00 74.58  ? 227 LEU A CA  1 
ATOM   1503 C  C   . LEU A 1 227 ? 18.632 47.562 20.352  1.00 75.19  ? 227 LEU A C   1 
ATOM   1504 O  O   . LEU A 1 227 ? 19.460 48.000 19.572  1.00 75.49  ? 227 LEU A O   1 
ATOM   1505 C  CB  . LEU A 1 227 ? 16.203 47.305 19.635  1.00 74.73  ? 227 LEU A CB  1 
ATOM   1506 C  CG  . LEU A 1 227 ? 15.016 46.469 19.116  1.00 75.91  ? 227 LEU A CG  1 
ATOM   1507 C  CD1 . LEU A 1 227 ? 13.825 47.347 18.834  1.00 76.59  ? 227 LEU A CD1 1 
ATOM   1508 C  CD2 . LEU A 1 227 ? 15.364 45.699 17.863  1.00 76.32  ? 227 LEU A CD2 1 
ATOM   1509 N  N   . LYS A 1 228 ? 18.655 47.838 21.669  1.00 75.33  ? 228 LYS A N   1 
ATOM   1510 C  CA  . LYS A 1 228 ? 19.644 48.686 22.324  1.00 75.36  ? 228 LYS A CA  1 
ATOM   1511 C  C   . LYS A 1 228 ? 21.090 48.171 22.163  1.00 76.67  ? 228 LYS A C   1 
ATOM   1512 O  O   . LYS A 1 228 ? 21.974 48.991 22.002  1.00 77.14  ? 228 LYS A O   1 
ATOM   1513 C  CB  . LYS A 1 228 ? 19.292 48.928 23.794  1.00 74.80  ? 228 LYS A CB  1 
ATOM   1514 C  CG  . LYS A 1 228 ? 17.985 49.671 23.955  1.00 75.45  ? 228 LYS A CG  1 
ATOM   1515 C  CD  . LYS A 1 228 ? 17.642 49.841 25.400  1.00 76.57  ? 228 LYS A CD  1 
ATOM   1516 C  CE  . LYS A 1 228 ? 16.247 50.369 25.565  1.00 78.61  ? 228 LYS A CE  1 
ATOM   1517 N  NZ  . LYS A 1 228 ? 15.637 49.935 26.848  1.00 80.10  ? 228 LYS A NZ  1 
ATOM   1518 N  N   . LEU A 1 229 ? 21.348 46.853 22.140  1.00 77.22  ? 229 LEU A N   1 
ATOM   1519 C  CA  . LEU A 1 229 ? 22.722 46.342 21.931  1.00 78.45  ? 229 LEU A CA  1 
ATOM   1520 C  C   . LEU A 1 229 ? 23.296 46.861 20.583  1.00 79.31  ? 229 LEU A C   1 
ATOM   1521 O  O   . LEU A 1 229 ? 24.442 47.308 20.500  1.00 79.23  ? 229 LEU A O   1 
ATOM   1522 C  CB  . LEU A 1 229 ? 22.764 44.792 21.911  1.00 78.81  ? 229 LEU A CB  1 
ATOM   1523 C  CG  . LEU A 1 229 ? 23.138 44.034 23.179  1.00 80.05  ? 229 LEU A CG  1 
ATOM   1524 C  CD1 . LEU A 1 229 ? 24.403 44.578 23.823  1.00 80.19  ? 229 LEU A CD1 1 
ATOM   1525 C  CD2 . LEU A 1 229 ? 21.978 43.977 24.132  1.00 81.07  ? 229 LEU A CD2 1 
ATOM   1526 N  N   . THR A 1 230 ? 22.474 46.800 19.534  1.00 79.68  ? 230 THR A N   1 
ATOM   1527 C  CA  . THR A 1 230 ? 22.877 47.231 18.206  1.00 79.52  ? 230 THR A CA  1 
ATOM   1528 C  C   . THR A 1 230 ? 22.891 48.746 18.082  1.00 78.42  ? 230 THR A C   1 
ATOM   1529 O  O   . THR A 1 230 ? 23.882 49.314 17.640  1.00 78.13  ? 230 THR A O   1 
ATOM   1530 C  CB  . THR A 1 230 ? 21.974 46.572 17.160  1.00 81.12  ? 230 THR A CB  1 
ATOM   1531 O  OG1 . THR A 1 230 ? 22.061 45.146 17.294  1.00 82.37  ? 230 THR A OG1 1 
ATOM   1532 C  CG2 . THR A 1 230 ? 22.342 46.971 15.752  1.00 81.60  ? 230 THR A CG2 1 
ATOM   1533 N  N   . LEU A 1 231 ? 21.808 49.401 18.508  1.00 77.79  ? 231 LEU A N   1 
ATOM   1534 C  CA  . LEU A 1 231 ? 21.653 50.843 18.356  1.00 77.57  ? 231 LEU A CA  1 
ATOM   1535 C  C   . LEU A 1 231 ? 22.579 51.681 19.208  1.00 79.04  ? 231 LEU A C   1 
ATOM   1536 O  O   . LEU A 1 231 ? 22.969 52.763 18.763  1.00 79.97  ? 231 LEU A O   1 
ATOM   1537 C  CB  . LEU A 1 231 ? 20.195 51.279 18.565  1.00 76.39  ? 231 LEU A CB  1 
ATOM   1538 C  CG  . LEU A 1 231 ? 19.155 50.711 17.587  1.00 75.67  ? 231 LEU A CG  1 
ATOM   1539 C  CD1 . LEU A 1 231 ? 17.876 51.416 17.725  1.00 75.80  ? 231 LEU A CD1 1 
ATOM   1540 C  CD2 . LEU A 1 231 ? 19.584 50.862 16.150  1.00 75.41  ? 231 LEU A CD2 1 
ATOM   1541 N  N   . ASP A 1 232 ? 22.966 51.201 20.399  1.00 79.09  ? 232 ASP A N   1 
ATOM   1542 C  CA  . ASP A 1 232 ? 23.891 51.933 21.266  1.00 79.55  ? 232 ASP A CA  1 
ATOM   1543 C  C   . ASP A 1 232 ? 25.228 52.184 20.573  1.00 81.02  ? 232 ASP A C   1 
ATOM   1544 O  O   . ASP A 1 232 ? 25.821 53.248 20.764  1.00 81.36  ? 232 ASP A O   1 
ATOM   1545 C  CB  . ASP A 1 232 ? 24.105 51.207 22.600  1.00 80.12  ? 232 ASP A CB  1 
ATOM   1546 C  CG  . ASP A 1 232 ? 22.993 51.392 23.618  1.00 83.03  ? 232 ASP A CG  1 
ATOM   1547 O  OD1 . ASP A 1 232 ? 21.982 52.058 23.285  1.00 84.68  ? 232 ASP A OD1 1 
ATOM   1548 O  OD2 . ASP A 1 232 ? 23.122 50.854 24.739  1.00 83.37  ? 232 ASP A OD2 1 
ATOM   1549 N  N   . ARG A 1 233 ? 25.673 51.232 19.727  1.00 81.76  ? 233 ARG A N   1 
ATOM   1550 C  CA  . ARG A 1 233 ? 26.912 51.345 18.955  1.00 82.92  ? 233 ARG A CA  1 
ATOM   1551 C  C   . ARG A 1 233 ? 26.868 52.467 17.896  1.00 83.43  ? 233 ARG A C   1 
ATOM   1552 O  O   . ARG A 1 233 ? 27.908 52.934 17.456  1.00 83.71  ? 233 ARG A O   1 
ATOM   1553 C  CB  . ARG A 1 233 ? 27.256 50.009 18.290  1.00 85.10  ? 233 ARG A CB  1 
ATOM   1554 C  CG  . ARG A 1 233 ? 27.552 48.869 19.256  1.00 90.26  ? 233 ARG A CG  1 
ATOM   1555 C  CD  . ARG A 1 233 ? 29.040 48.711 19.578  1.00 96.40  ? 233 ARG A CD  1 
ATOM   1556 N  NE  . ARG A 1 233 ? 29.910 48.765 18.394  1.00 101.89 ? 233 ARG A NE  1 
ATOM   1557 C  CZ  . ARG A 1 233 ? 30.887 47.897 18.135  1.00 105.05 ? 233 ARG A CZ  1 
ATOM   1558 N  NH1 . ARG A 1 233 ? 31.121 46.883 18.962  1.00 105.14 ? 233 ARG A NH1 1 
ATOM   1559 N  NH2 . ARG A 1 233 ? 31.622 48.021 17.036  1.00 104.83 ? 233 ARG A NH2 1 
ATOM   1560 N  N   . GLY A 1 234 ? 25.679 52.854 17.470  1.00 83.58  ? 234 GLY A N   1 
ATOM   1561 C  CA  . GLY A 1 234 ? 25.509 53.923 16.501  1.00 84.11  ? 234 GLY A CA  1 
ATOM   1562 C  C   . GLY A 1 234 ? 24.976 55.197 17.127  1.00 84.53  ? 234 GLY A C   1 
ATOM   1563 O  O   . GLY A 1 234 ? 24.407 56.038 16.422  1.00 84.66  ? 234 GLY A O   1 
ATOM   1564 N  N   . ASN A 1 235 ? 25.149 55.343 18.465  1.00 84.41  ? 235 ASN A N   1 
ATOM   1565 C  CA  . ASN A 1 235 ? 24.728 56.490 19.269  1.00 84.58  ? 235 ASN A CA  1 
ATOM   1566 C  C   . ASN A 1 235 ? 23.256 56.783 19.076  1.00 83.68  ? 235 ASN A C   1 
ATOM   1567 O  O   . ASN A 1 235 ? 22.859 57.935 18.927  1.00 83.91  ? 235 ASN A O   1 
ATOM   1568 C  CB  . ASN A 1 235 ? 25.600 57.711 18.962  1.00 86.58  ? 235 ASN A CB  1 
ATOM   1569 C  CG  . ASN A 1 235 ? 27.080 57.459 19.190  1.00 90.67  ? 235 ASN A CG  1 
ATOM   1570 O  OD1 . ASN A 1 235 ? 27.932 57.876 18.388  1.00 92.62  ? 235 ASN A OD1 1 
ATOM   1571 N  ND2 . ASN A 1 235 ? 27.421 56.760 20.281  1.00 90.61  ? 235 ASN A ND2 1 
ATOM   1572 N  N   . ALA A 1 236 ? 22.447 55.725 19.073  1.00 82.60  ? 236 ALA A N   1 
ATOM   1573 C  CA  . ALA A 1 236 ? 21.021 55.815 18.800  1.00 81.70  ? 236 ALA A CA  1 
ATOM   1574 C  C   . ALA A 1 236 ? 20.180 55.062 19.845  1.00 80.38  ? 236 ALA A C   1 
ATOM   1575 O  O   . ALA A 1 236 ? 20.702 54.264 20.630  1.00 80.68  ? 236 ALA A O   1 
ATOM   1576 C  CB  . ALA A 1 236 ? 20.744 55.270 17.386  1.00 81.73  ? 236 ALA A CB  1 
ATOM   1577 N  N   . THR A 1 237 ? 18.880 55.354 19.886  1.00 78.67  ? 237 THR A N   1 
ATOM   1578 C  CA  . THR A 1 237 ? 17.951 54.663 20.754  1.00 77.61  ? 237 THR A CA  1 
ATOM   1579 C  C   . THR A 1 237 ? 16.847 54.044 19.881  1.00 76.74  ? 237 THR A C   1 
ATOM   1580 O  O   . THR A 1 237 ? 16.542 54.560 18.799  1.00 76.63  ? 237 THR A O   1 
ATOM   1581 C  CB  . THR A 1 237 ? 17.372 55.610 21.797  1.00 78.34  ? 237 THR A CB  1 
ATOM   1582 O  OG1 . THR A 1 237 ? 16.500 56.536 21.158  1.00 79.81  ? 237 THR A OG1 1 
ATOM   1583 C  CG2 . THR A 1 237 ? 18.440 56.332 22.571  1.00 78.31  ? 237 THR A CG2 1 
ATOM   1584 N  N   . PRO A 1 238 ? 16.213 52.946 20.349  1.00 75.61  ? 238 PRO A N   1 
ATOM   1585 C  CA  . PRO A 1 238 ? 15.133 52.344 19.552  1.00 74.86  ? 238 PRO A CA  1 
ATOM   1586 C  C   . PRO A 1 238 ? 13.904 53.246 19.375  1.00 74.45  ? 238 PRO A C   1 
ATOM   1587 O  O   . PRO A 1 238 ? 13.182 53.085 18.405  1.00 74.08  ? 238 PRO A O   1 
ATOM   1588 C  CB  . PRO A 1 238 ? 14.841 51.033 20.275  1.00 75.23  ? 238 PRO A CB  1 
ATOM   1589 C  CG  . PRO A 1 238 ? 15.343 51.234 21.650  1.00 75.69  ? 238 PRO A CG  1 
ATOM   1590 C  CD  . PRO A 1 238 ? 16.457 52.202 21.600  1.00 74.42  ? 238 PRO A CD  1 
ATOM   1591 N  N   . GLU A 1 239 ? 13.703 54.224 20.271  1.00 74.46  ? 239 GLU A N   1 
ATOM   1592 C  CA  . GLU A 1 239 ? 12.614 55.194 20.175  1.00 74.72  ? 239 GLU A CA  1 
ATOM   1593 C  C   . GLU A 1 239 ? 12.822 56.117 18.957  1.00 75.12  ? 239 GLU A C   1 
ATOM   1594 O  O   . GLU A 1 239 ? 11.850 56.507 18.311  1.00 75.44  ? 239 GLU A O   1 
ATOM   1595 C  CB  . GLU A 1 239 ? 12.506 56.005 21.468  1.00 75.88  ? 239 GLU A CB  1 
ATOM   1596 C  CG  . GLU A 1 239 ? 11.932 55.221 22.628  1.00 79.15  ? 239 GLU A CG  1 
ATOM   1597 C  CD  . GLU A 1 239 ? 12.937 54.459 23.470  1.00 86.62  ? 239 GLU A CD  1 
ATOM   1598 O  OE1 . GLU A 1 239 ? 14.153 54.534 23.181  1.00 87.21  ? 239 GLU A OE1 1 
ATOM   1599 O  OE2 . GLU A 1 239 ? 12.506 53.799 24.443  1.00 90.91  ? 239 GLU A OE2 1 
ATOM   1600 N  N   . GLN A 1 240 ? 14.080 56.440 18.623  1.00 74.84  ? 240 GLN A N   1 
ATOM   1601 C  CA  . GLN A 1 240 ? 14.387 57.233 17.420  1.00 75.03  ? 240 GLN A CA  1 
ATOM   1602 C  C   . GLN A 1 240 ? 14.030 56.466 16.147  1.00 74.85  ? 240 GLN A C   1 
ATOM   1603 O  O   . GLN A 1 240 ? 13.649 57.058 15.151  1.00 75.20  ? 240 GLN A O   1 
ATOM   1604 C  CB  . GLN A 1 240 ? 15.879 57.553 17.358  1.00 76.52  ? 240 GLN A CB  1 
ATOM   1605 C  CG  . GLN A 1 240 ? 16.335 58.497 18.453  1.00 80.53  ? 240 GLN A CG  1 
ATOM   1606 C  CD  . GLN A 1 240 ? 17.830 58.648 18.507  1.00 86.37  ? 240 GLN A CD  1 
ATOM   1607 O  OE1 . GLN A 1 240 ? 18.588 57.901 17.887  1.00 88.90  ? 240 GLN A OE1 1 
ATOM   1608 N  NE2 . GLN A 1 240 ? 18.297 59.615 19.268  1.00 87.69  ? 240 GLN A NE2 1 
ATOM   1609 N  N   . MET A 1 241 ? 14.191 55.151 16.180  1.00 74.08  ? 241 MET A N   1 
ATOM   1610 C  CA  . MET A 1 241 ? 13.943 54.252 15.082  1.00 73.48  ? 241 MET A CA  1 
ATOM   1611 C  C   . MET A 1 241 ? 12.458 53.924 14.882  1.00 73.49  ? 241 MET A C   1 
ATOM   1612 O  O   . MET A 1 241 ? 11.941 54.176 13.803  1.00 74.17  ? 241 MET A O   1 
ATOM   1613 C  CB  . MET A 1 241 ? 14.777 52.977 15.306  1.00 73.30  ? 241 MET A CB  1 
ATOM   1614 C  CG  . MET A 1 241 ? 14.670 51.978 14.208  1.00 74.28  ? 241 MET A CG  1 
ATOM   1615 S  SD  . MET A 1 241 ? 15.915 50.686 14.400  1.00 72.08  ? 241 MET A SD  1 
ATOM   1616 C  CE  . MET A 1 241 ? 15.214 49.762 15.712  1.00 64.53  ? 241 MET A CE  1 
ATOM   1617 N  N   . TRP A 1 242 ? 11.774 53.364 15.900  1.00 73.02  ? 242 TRP A N   1 
ATOM   1618 C  CA  . TRP A 1 242 ? 10.386 52.896 15.786  1.00 73.08  ? 242 TRP A CA  1 
ATOM   1619 C  C   . TRP A 1 242 ? 9.373  53.492 16.761  1.00 74.26  ? 242 TRP A C   1 
ATOM   1620 O  O   . TRP A 1 242 ? 8.264  52.961 16.891  1.00 74.52  ? 242 TRP A O   1 
ATOM   1621 C  CB  . TRP A 1 242 ? 10.319 51.358 15.904  1.00 72.06  ? 242 TRP A CB  1 
ATOM   1622 C  CG  . TRP A 1 242 ? 10.893 50.615 14.736  1.00 71.41  ? 242 TRP A CG  1 
ATOM   1623 C  CD1 . TRP A 1 242 ? 10.959 51.038 13.440  1.00 72.17  ? 242 TRP A CD1 1 
ATOM   1624 C  CD2 . TRP A 1 242 ? 11.488 49.316 14.766  1.00 71.06  ? 242 TRP A CD2 1 
ATOM   1625 N  NE1 . TRP A 1 242 ? 11.567 50.083 12.662  1.00 72.48  ? 242 TRP A NE1 1 
ATOM   1626 C  CE2 . TRP A 1 242 ? 11.913 49.018 13.457  1.00 72.00  ? 242 TRP A CE2 1 
ATOM   1627 C  CE3 . TRP A 1 242 ? 11.747 48.394 15.782  1.00 71.34  ? 242 TRP A CE3 1 
ATOM   1628 C  CZ2 . TRP A 1 242 ? 12.541 47.821 13.134  1.00 72.47  ? 242 TRP A CZ2 1 
ATOM   1629 C  CZ3 . TRP A 1 242 ? 12.377 47.214 15.457  1.00 72.18  ? 242 TRP A CZ3 1 
ATOM   1630 C  CH2 . TRP A 1 242 ? 12.768 46.938 14.149  1.00 72.37  ? 242 TRP A CH2 1 
ATOM   1631 N  N   . GLY A 1 243 ? 9.740  54.563 17.431  1.00 74.96  ? 243 GLY A N   1 
ATOM   1632 C  CA  . GLY A 1 243 ? 8.836  55.212 18.367  1.00 76.55  ? 243 GLY A CA  1 
ATOM   1633 C  C   . GLY A 1 243 ? 8.760  54.526 19.711  1.00 78.19  ? 243 GLY A C   1 
ATOM   1634 O  O   . GLY A 1 243 ? 9.627  53.731 20.067  1.00 78.74  ? 243 GLY A O   1 
ATOM   1635 N  N   . PRO A 1 244 ? 7.722  54.838 20.490  1.00 78.97  ? 244 PRO A N   1 
ATOM   1636 C  CA  . PRO A 1 244 ? 7.596  54.239 21.827  1.00 79.52  ? 244 PRO A CA  1 
ATOM   1637 C  C   . PRO A 1 244 ? 7.404  52.728 21.799  1.00 79.75  ? 244 PRO A C   1 
ATOM   1638 O  O   . PRO A 1 244 ? 6.694  52.222 20.932  1.00 80.05  ? 244 PRO A O   1 
ATOM   1639 C  CB  . PRO A 1 244 ? 6.351  54.933 22.404  1.00 80.28  ? 244 PRO A CB  1 
ATOM   1640 C  CG  . PRO A 1 244 ? 5.553  55.356 21.194  1.00 80.62  ? 244 PRO A CG  1 
ATOM   1641 C  CD  . PRO A 1 244 ? 6.614  55.768 20.202  1.00 78.83  ? 244 PRO A CD  1 
ATOM   1642 N  N   . ARG A 1 245 ? 8.003  52.007 22.763  1.00 79.50  ? 245 ARG A N   1 
ATOM   1643 C  CA  . ARG A 1 245 ? 7.847  50.559 22.832  1.00 79.97  ? 245 ARG A CA  1 
ATOM   1644 C  C   . ARG A 1 245 ? 6.371  50.175 22.976  1.00 80.82  ? 245 ARG A C   1 
ATOM   1645 O  O   . ARG A 1 245 ? 5.650  50.795 23.758  1.00 81.30  ? 245 ARG A O   1 
ATOM   1646 C  CB  . ARG A 1 245 ? 8.665  49.964 23.979  1.00 80.78  ? 245 ARG A CB  1 
ATOM   1647 C  CG  . ARG A 1 245 ? 8.598  48.443 23.986  1.00 83.40  ? 245 ARG A CG  1 
ATOM   1648 C  CD  . ARG A 1 245 ? 9.265  47.829 25.192  1.00 86.03  ? 245 ARG A CD  1 
ATOM   1649 N  NE  . ARG A 1 245 ? 8.442  47.913 26.400  1.00 87.75  ? 245 ARG A NE  1 
ATOM   1650 C  CZ  . ARG A 1 245 ? 7.602  46.963 26.803  1.00 89.28  ? 245 ARG A CZ  1 
ATOM   1651 N  NH1 . ARG A 1 245 ? 7.455  45.850 26.094  1.00 88.56  ? 245 ARG A NH1 1 
ATOM   1652 N  NH2 . ARG A 1 245 ? 6.899  47.120 27.917  1.00 89.41  ? 245 ARG A NH2 1 
ATOM   1653 N  N   . GLY A 1 246 ? 5.919  49.224 22.170  1.00 80.84  ? 246 GLY A N   1 
ATOM   1654 C  CA  . GLY A 1 246 ? 4.520  48.823 22.183  1.00 81.38  ? 246 GLY A CA  1 
ATOM   1655 C  C   . GLY A 1 246 ? 3.619  49.689 21.314  1.00 82.05  ? 246 GLY A C   1 
ATOM   1656 O  O   . GLY A 1 246 ? 2.473  49.325 21.065  1.00 82.51  ? 246 GLY A O   1 
ATOM   1657 N  N   . GLY A 1 247 ? 4.124  50.829 20.845  1.00 81.97  ? 247 GLY A N   1 
ATOM   1658 C  CA  . GLY A 1 247 ? 3.380  51.727 19.980  1.00 82.27  ? 247 GLY A CA  1 
ATOM   1659 C  C   . GLY A 1 247 ? 3.079  51.111 18.631  1.00 82.71  ? 247 GLY A C   1 
ATOM   1660 O  O   . GLY A 1 247 ? 3.654  50.086 18.257  1.00 83.18  ? 247 GLY A O   1 
ATOM   1661 N  N   . GLU A 1 248 ? 2.168  51.738 17.894  1.00 82.42  ? 248 GLU A N   1 
ATOM   1662 C  CA  . GLU A 1 248 ? 1.704  51.295 16.585  1.00 82.24  ? 248 GLU A CA  1 
ATOM   1663 C  C   . GLU A 1 248 ? 2.824  50.894 15.609  1.00 80.96  ? 248 GLU A C   1 
ATOM   1664 O  O   . GLU A 1 248 ? 2.774  49.826 15.003  1.00 81.05  ? 248 GLU A O   1 
ATOM   1665 C  CB  . GLU A 1 248 ? 0.805  52.399 15.990  1.00 85.47  ? 248 GLU A CB  1 
ATOM   1666 C  CG  . GLU A 1 248 ? 0.344  52.140 14.572  1.00 92.60  ? 248 GLU A CG  1 
ATOM   1667 C  CD  . GLU A 1 248 ? -1.137 52.363 14.365  1.00 101.59 ? 248 GLU A CD  1 
ATOM   1668 O  OE1 . GLU A 1 248 ? -1.903 52.197 15.343  1.00 103.12 ? 248 GLU A OE1 1 
ATOM   1669 O  OE2 . GLU A 1 248 ? -1.532 52.695 13.222  1.00 104.72 ? 248 GLU A OE2 1 
ATOM   1670 N  N   . TYR A 1 249 ? 3.815  51.756 15.450  1.00 79.88  ? 249 TYR A N   1 
ATOM   1671 C  CA  . TYR A 1 249 ? 4.904  51.525 14.512  1.00 79.33  ? 249 TYR A CA  1 
ATOM   1672 C  C   . TYR A 1 249 ? 5.840  50.418 14.993  1.00 79.29  ? 249 TYR A C   1 
ATOM   1673 O  O   . TYR A 1 249 ? 6.355  49.662 14.175  1.00 79.52  ? 249 TYR A O   1 
ATOM   1674 C  CB  . TYR A 1 249 ? 5.637  52.850 14.232  1.00 78.93  ? 249 TYR A CB  1 
ATOM   1675 C  CG  . TYR A 1 249 ? 6.565  52.812 13.042  1.00 79.15  ? 249 TYR A CG  1 
ATOM   1676 C  CD1 . TYR A 1 249 ? 6.173  52.229 11.845  1.00 79.85  ? 249 TYR A CD1 1 
ATOM   1677 C  CD2 . TYR A 1 249 ? 7.832  53.373 13.107  1.00 79.57  ? 249 TYR A CD2 1 
ATOM   1678 C  CE1 . TYR A 1 249 ? 7.030  52.183 10.753  1.00 80.46  ? 249 TYR A CE1 1 
ATOM   1679 C  CE2 . TYR A 1 249 ? 8.696  53.334 12.022  1.00 80.18  ? 249 TYR A CE2 1 
ATOM   1680 C  CZ  . TYR A 1 249 ? 8.293  52.738 10.847  1.00 81.08  ? 249 TYR A CZ  1 
ATOM   1681 O  OH  . TYR A 1 249 ? 9.157  52.694 9.785   1.00 82.60  ? 249 TYR A OH  1 
ATOM   1682 N  N   . ASN A 1 250 ? 6.030  50.289 16.314  1.00 78.82  ? 250 ASN A N   1 
ATOM   1683 C  CA  . ASN A 1 250 ? 6.865  49.232 16.866  1.00 78.46  ? 250 ASN A CA  1 
ATOM   1684 C  C   . ASN A 1 250 ? 6.208  47.880 16.623  1.00 78.64  ? 250 ASN A C   1 
ATOM   1685 O  O   . ASN A 1 250 ? 6.896  46.953 16.209  1.00 79.49  ? 250 ASN A O   1 
ATOM   1686 C  CB  . ASN A 1 250 ? 7.108  49.455 18.358  1.00 78.93  ? 250 ASN A CB  1 
ATOM   1687 C  CG  . ASN A 1 250 ? 7.949  48.398 19.048  1.00 80.83  ? 250 ASN A CG  1 
ATOM   1688 O  OD1 . ASN A 1 250 ? 7.889  48.243 20.273  1.00 81.19  ? 250 ASN A OD1 1 
ATOM   1689 N  ND2 . ASN A 1 250 ? 8.759  47.651 18.299  1.00 81.06  ? 250 ASN A ND2 1 
ATOM   1690 N  N   . ILE A 1 251 ? 4.886  47.758 16.850  1.00 77.80  ? 251 ILE A N   1 
ATOM   1691 C  CA  . ILE A 1 251 ? 4.168  46.499 16.609  1.00 77.38  ? 251 ILE A CA  1 
ATOM   1692 C  C   . ILE A 1 251 ? 4.207  46.121 15.138  1.00 76.41  ? 251 ILE A C   1 
ATOM   1693 O  O   . ILE A 1 251 ? 4.448  44.967 14.810  1.00 76.61  ? 251 ILE A O   1 
ATOM   1694 C  CB  . ILE A 1 251 ? 2.719  46.554 17.117  1.00 78.24  ? 251 ILE A CB  1 
ATOM   1695 C  CG1 . ILE A 1 251 ? 2.671  46.897 18.606  1.00 79.61  ? 251 ILE A CG1 1 
ATOM   1696 C  CG2 . ILE A 1 251 ? 2.005  45.242 16.843  1.00 78.86  ? 251 ILE A CG2 1 
ATOM   1697 C  CD1 . ILE A 1 251 ? 3.352  45.908 19.507  1.00 81.10  ? 251 ILE A CD1 1 
ATOM   1698 N  N   . TYR A 1 252 ? 4.024  47.101 14.244  1.00 75.35  ? 252 TYR A N   1 
ATOM   1699 C  CA  . TYR A 1 252 ? 4.128  46.914 12.790  1.00 74.69  ? 252 TYR A CA  1 
ATOM   1700 C  C   . TYR A 1 252 ? 5.495  46.283 12.420  1.00 74.61  ? 252 TYR A C   1 
ATOM   1701 O  O   . TYR A 1 252 ? 5.599  45.468 11.495  1.00 74.65  ? 252 TYR A O   1 
ATOM   1702 C  CB  . TYR A 1 252 ? 3.970  48.281 12.106  1.00 74.26  ? 252 TYR A CB  1 
ATOM   1703 C  CG  . TYR A 1 252 ? 4.065  48.248 10.602  1.00 74.97  ? 252 TYR A CG  1 
ATOM   1704 C  CD1 . TYR A 1 252 ? 3.199  47.475 9.849   1.00 76.00  ? 252 TYR A CD1 1 
ATOM   1705 C  CD2 . TYR A 1 252 ? 4.981  49.041 9.927   1.00 76.34  ? 252 TYR A CD2 1 
ATOM   1706 C  CE1 . TYR A 1 252 ? 3.277  47.447 8.460   1.00 77.35  ? 252 TYR A CE1 1 
ATOM   1707 C  CE2 . TYR A 1 252 ? 5.055  49.040 8.541   1.00 77.56  ? 252 TYR A CE2 1 
ATOM   1708 C  CZ  . TYR A 1 252 ? 4.213  48.229 7.809   1.00 78.76  ? 252 TYR A CZ  1 
ATOM   1709 O  OH  . TYR A 1 252 ? 4.308  48.215 6.435   1.00 81.02  ? 252 TYR A OH  1 
ATOM   1710 N  N   . ASN A 1 253 ? 6.538  46.657 13.182  1.00 74.24  ? 253 ASN A N   1 
ATOM   1711 C  CA  . ASN A 1 253 ? 7.897  46.178 13.031  1.00 73.63  ? 253 ASN A CA  1 
ATOM   1712 C  C   . ASN A 1 253 ? 8.274  45.104 14.053  1.00 73.80  ? 253 ASN A C   1 
ATOM   1713 O  O   . ASN A 1 253 ? 9.417  45.034 14.485  1.00 74.39  ? 253 ASN A O   1 
ATOM   1714 C  CB  . ASN A 1 253 ? 8.866  47.331 13.052  1.00 73.30  ? 253 ASN A CB  1 
ATOM   1715 C  CG  . ASN A 1 253 ? 8.816  48.146 11.797  1.00 73.99  ? 253 ASN A CG  1 
ATOM   1716 O  OD1 . ASN A 1 253 ? 9.206  47.699 10.719  1.00 74.16  ? 253 ASN A OD1 1 
ATOM   1717 N  ND2 . ASN A 1 253 ? 8.352  49.368 11.917  1.00 74.29  ? 253 ASN A ND2 1 
ATOM   1718 N  N   . ASP A 1 254 ? 7.309  44.277 14.453  1.00 73.16  ? 254 ASP A N   1 
ATOM   1719 C  CA  . ASP A 1 254 ? 7.550  43.141 15.341  1.00 72.64  ? 254 ASP A CA  1 
ATOM   1720 C  C   . ASP A 1 254 ? 7.228  41.926 14.486  1.00 72.30  ? 254 ASP A C   1 
ATOM   1721 O  O   . ASP A 1 254 ? 6.069  41.697 14.158  1.00 72.03  ? 254 ASP A O   1 
ATOM   1722 C  CB  . ASP A 1 254 ? 6.684  43.197 16.607  1.00 73.52  ? 254 ASP A CB  1 
ATOM   1723 C  CG  . ASP A 1 254 ? 6.987  42.075 17.576  1.00 77.49  ? 254 ASP A CG  1 
ATOM   1724 O  OD1 . ASP A 1 254 ? 7.007  40.913 17.150  1.00 78.42  ? 254 ASP A OD1 1 
ATOM   1725 O  OD2 . ASP A 1 254 ? 7.225  42.361 18.753  1.00 79.91  ? 254 ASP A OD2 1 
ATOM   1726 N  N   . ALA A 1 255 ? 8.256  41.195 14.060  1.00 72.35  ? 255 ALA A N   1 
ATOM   1727 C  CA  . ALA A 1 255 ? 8.074  40.062 13.163  1.00 73.15  ? 255 ALA A CA  1 
ATOM   1728 C  C   . ALA A 1 255 ? 7.534  38.800 13.829  1.00 73.54  ? 255 ALA A C   1 
ATOM   1729 O  O   . ALA A 1 255 ? 7.160  37.866 13.121  1.00 73.97  ? 255 ALA A O   1 
ATOM   1730 C  CB  . ALA A 1 255 ? 9.362  39.761 12.417  1.00 73.58  ? 255 ALA A CB  1 
ATOM   1731 N  N   . LEU A 1 256 ? 7.488  38.756 15.168  1.00 73.23  ? 256 LEU A N   1 
ATOM   1732 C  CA  . LEU A 1 256 ? 6.902  37.610 15.862  1.00 73.68  ? 256 LEU A CA  1 
ATOM   1733 C  C   . LEU A 1 256 ? 5.390  37.813 15.899  1.00 75.65  ? 256 LEU A C   1 
ATOM   1734 O  O   . LEU A 1 256 ? 4.645  36.933 15.472  1.00 76.58  ? 256 LEU A O   1 
ATOM   1735 C  CB  . LEU A 1 256 ? 7.456  37.418 17.287  1.00 72.47  ? 256 LEU A CB  1 
ATOM   1736 C  CG  . LEU A 1 256 ? 6.864  36.235 18.044  1.00 71.87  ? 256 LEU A CG  1 
ATOM   1737 C  CD1 . LEU A 1 256 ? 7.204  34.945 17.385  1.00 71.70  ? 256 LEU A CD1 1 
ATOM   1738 C  CD2 . LEU A 1 256 ? 7.300  36.219 19.497  1.00 71.72  ? 256 LEU A CD2 1 
ATOM   1739 N  N   . ILE A 1 257 ? 4.925  38.992 16.351  1.00 75.88  ? 257 ILE A N   1 
ATOM   1740 C  CA  . ILE A 1 257 ? 3.495  39.306 16.386  1.00 76.50  ? 257 ILE A CA  1 
ATOM   1741 C  C   . ILE A 1 257 ? 2.829  39.119 15.008  1.00 77.28  ? 257 ILE A C   1 
ATOM   1742 O  O   . ILE A 1 257 ? 1.773  38.488 14.899  1.00 77.78  ? 257 ILE A O   1 
ATOM   1743 C  CB  . ILE A 1 257 ? 3.281  40.738 16.945  1.00 76.83  ? 257 ILE A CB  1 
ATOM   1744 C  CG1 . ILE A 1 257 ? 3.679  40.812 18.417  1.00 77.10  ? 257 ILE A CG1 1 
ATOM   1745 C  CG2 . ILE A 1 257 ? 1.842  41.227 16.718  1.00 77.70  ? 257 ILE A CG2 1 
ATOM   1746 C  CD1 . ILE A 1 257 ? 3.589  42.164 19.000  1.00 78.26  ? 257 ILE A CD1 1 
ATOM   1747 N  N   . ASN A 1 258 ? 3.488  39.605 13.958  1.00 77.43  ? 258 ASN A N   1 
ATOM   1748 C  CA  . ASN A 1 258 ? 2.962  39.519 12.599  1.00 78.13  ? 258 ASN A CA  1 
ATOM   1749 C  C   . ASN A 1 258 ? 3.459  38.321 11.782  1.00 78.78  ? 258 ASN A C   1 
ATOM   1750 O  O   . ASN A 1 258 ? 3.387  38.349 10.564  1.00 78.61  ? 258 ASN A O   1 
ATOM   1751 C  CB  . ASN A 1 258 ? 3.276  40.806 11.870  1.00 79.44  ? 258 ASN A CB  1 
ATOM   1752 C  CG  . ASN A 1 258 ? 2.648  42.004 12.519  1.00 83.19  ? 258 ASN A CG  1 
ATOM   1753 O  OD1 . ASN A 1 258 ? 1.436  42.239 12.405  1.00 85.04  ? 258 ASN A OD1 1 
ATOM   1754 N  ND2 . ASN A 1 258 ? 3.451  42.780 13.221  1.00 83.34  ? 258 ASN A ND2 1 
ATOM   1755 N  N   . SER A 1 259 ? 3.923  37.266 12.442  1.00 79.60  ? 259 SER A N   1 
ATOM   1756 C  CA  . SER A 1 259 ? 4.476  36.082 11.789  1.00 80.70  ? 259 SER A CA  1 
ATOM   1757 C  C   . SER A 1 259 ? 3.557  35.433 10.777  1.00 81.99  ? 259 SER A C   1 
ATOM   1758 O  O   . SER A 1 259 ? 4.034  34.898 9.773   1.00 82.10  ? 259 SER A O   1 
ATOM   1759 C  CB  . SER A 1 259 ? 4.916  35.050 12.824  1.00 81.52  ? 259 SER A CB  1 
ATOM   1760 O  OG  . SER A 1 259 ? 3.827  34.569 13.597  1.00 82.96  ? 259 SER A OG  1 
ATOM   1761 N  N   . ASP A 1 260 ? 2.246  35.466 11.029  1.00 82.63  ? 260 ASP A N   1 
ATOM   1762 C  CA  . ASP A 1 260 ? 1.280  34.841 10.128  1.00 83.35  ? 260 ASP A CA  1 
ATOM   1763 C  C   . ASP A 1 260 ? 1.317  35.428 8.726   1.00 82.90  ? 260 ASP A C   1 
ATOM   1764 O  O   . ASP A 1 260 ? 1.023  34.711 7.769   1.00 83.48  ? 260 ASP A O   1 
ATOM   1765 C  CB  . ASP A 1 260 ? -0.130 34.909 10.716  1.00 86.21  ? 260 ASP A CB  1 
ATOM   1766 C  CG  . ASP A 1 260 ? -0.374 34.004 11.909  1.00 92.96  ? 260 ASP A CG  1 
ATOM   1767 O  OD1 . ASP A 1 260 ? 0.538  33.211 12.259  1.00 94.20  ? 260 ASP A OD1 1 
ATOM   1768 O  OD2 . ASP A 1 260 ? -1.473 34.086 12.498  1.00 95.94  ? 260 ASP A OD2 1 
ATOM   1769 N  N   . LYS A 1 261 ? 1.714  36.720 8.595   1.00 81.44  ? 261 LYS A N   1 
ATOM   1770 C  CA  . LYS A 1 261 ? 1.829  37.415 7.304   1.00 80.08  ? 261 LYS A CA  1 
ATOM   1771 C  C   . LYS A 1 261 ? 2.940  36.863 6.391   1.00 79.25  ? 261 LYS A C   1 
ATOM   1772 O  O   . LYS A 1 261 ? 3.031  37.245 5.230   1.00 79.26  ? 261 LYS A O   1 
ATOM   1773 C  CB  . LYS A 1 261 ? 2.002  38.927 7.508   1.00 80.81  ? 261 LYS A CB  1 
ATOM   1774 C  CG  . LYS A 1 261 ? 0.874  39.593 8.288   1.00 83.03  ? 261 LYS A CG  1 
ATOM   1775 C  CD  . LYS A 1 261 ? 1.027  41.108 8.276   1.00 86.06  ? 261 LYS A CD  1 
ATOM   1776 C  CE  . LYS A 1 261 ? -0.142 41.830 8.904   1.00 88.92  ? 261 LYS A CE  1 
ATOM   1777 N  NZ  . LYS A 1 261 ? -0.349 41.454 10.324  1.00 90.36  ? 261 LYS A NZ  1 
ATOM   1778 N  N   . LEU A 1 262 ? 3.786  35.978 6.912   1.00 78.89  ? 262 LEU A N   1 
ATOM   1779 C  CA  . LEU A 1 262 ? 4.835  35.323 6.136   1.00 78.96  ? 262 LEU A CA  1 
ATOM   1780 C  C   . LEU A 1 262 ? 4.259  34.247 5.214   1.00 79.11  ? 262 LEU A C   1 
ATOM   1781 O  O   . LEU A 1 262 ? 4.881  33.940 4.204   1.00 79.22  ? 262 LEU A O   1 
ATOM   1782 C  CB  . LEU A 1 262 ? 5.881  34.694 7.068   1.00 78.93  ? 262 LEU A CB  1 
ATOM   1783 C  CG  . LEU A 1 262 ? 6.711  35.684 7.852   1.00 79.38  ? 262 LEU A CG  1 
ATOM   1784 C  CD1 . LEU A 1 262 ? 7.465  34.999 8.966   1.00 79.53  ? 262 LEU A CD1 1 
ATOM   1785 C  CD2 . LEU A 1 262 ? 7.638  36.437 6.925   1.00 79.66  ? 262 LEU A CD2 1 
ATOM   1786 N  N   . ARG A 1 263 ? 3.061  33.689 5.532   1.00 79.02  ? 263 ARG A N   1 
ATOM   1787 C  CA  . ARG A 1 263 ? 2.380  32.663 4.725   1.00 79.32  ? 263 ARG A CA  1 
ATOM   1788 C  C   . ARG A 1 263 ? 2.463  32.939 3.217   1.00 79.51  ? 263 ARG A C   1 
ATOM   1789 O  O   . ARG A 1 263 ? 2.129  34.035 2.773   1.00 79.68  ? 263 ARG A O   1 
ATOM   1790 C  CB  . ARG A 1 263 ? 0.910  32.507 5.146   1.00 79.95  ? 263 ARG A CB  1 
ATOM   1791 C  CG  . ARG A 1 263 ? 0.279  31.251 4.550   1.00 81.80  ? 263 ARG A CG  1 
ATOM   1792 C  CD  . ARG A 1 263 ? -1.186 31.067 4.898   1.00 83.70  ? 263 ARG A CD  1 
ATOM   1793 N  NE  . ARG A 1 263 ? -1.435 31.158 6.338   1.00 84.79  ? 263 ARG A NE  1 
ATOM   1794 C  CZ  . ARG A 1 263 ? -1.340 30.140 7.187   1.00 85.14  ? 263 ARG A CZ  1 
ATOM   1795 N  NH1 . ARG A 1 263 ? -0.999 28.931 6.752   1.00 83.35  ? 263 ARG A NH1 1 
ATOM   1796 N  NH2 . ARG A 1 263 ? -1.583 30.322 8.479   1.00 84.75  ? 263 ARG A NH2 1 
ATOM   1797 N  N   . GLY A 1 264 ? 2.993  31.982 2.478   1.00 79.31  ? 264 GLY A N   1 
ATOM   1798 C  CA  . GLY A 1 264 ? 3.191  32.133 1.045   1.00 79.94  ? 264 GLY A CA  1 
ATOM   1799 C  C   . GLY A 1 264 ? 4.642  32.332 0.648   1.00 80.81  ? 264 GLY A C   1 
ATOM   1800 O  O   . GLY A 1 264 ? 4.999  32.159 -0.519  1.00 81.52  ? 264 GLY A O   1 
ATOM   1801 N  N   . THR A 1 265 ? 5.494  32.712 1.603   1.00 80.72  ? 265 THR A N   1 
ATOM   1802 C  CA  . THR A 1 265 ? 6.912  32.931 1.340   1.00 80.45  ? 265 THR A CA  1 
ATOM   1803 C  C   . THR A 1 265 ? 7.686  31.668 1.717   1.00 80.27  ? 265 THR A C   1 
ATOM   1804 O  O   . THR A 1 265 ? 7.379  31.040 2.737   1.00 80.47  ? 265 THR A O   1 
ATOM   1805 C  CB  . THR A 1 265 ? 7.413  34.120 2.185   1.00 81.12  ? 265 THR A CB  1 
ATOM   1806 O  OG1 . THR A 1 265 ? 6.538  35.246 2.034   1.00 81.67  ? 265 THR A OG1 1 
ATOM   1807 C  CG2 . THR A 1 265 ? 8.845  34.508 1.861   1.00 81.52  ? 265 THR A CG2 1 
ATOM   1808 N  N   . GLU A 1 266 ? 8.676  31.279 0.899   1.00 79.55  ? 266 GLU A N   1 
ATOM   1809 C  CA  . GLU A 1 266 ? 9.541  30.159 1.260   1.00 79.09  ? 266 GLU A CA  1 
ATOM   1810 C  C   . GLU A 1 266 ? 10.481 30.707 2.327   1.00 77.75  ? 266 GLU A C   1 
ATOM   1811 O  O   . GLU A 1 266 ? 11.026 31.792 2.141   1.00 78.15  ? 266 GLU A O   1 
ATOM   1812 C  CB  . GLU A 1 266 ? 10.350 29.682 0.054   1.00 81.95  ? 266 GLU A CB  1 
ATOM   1813 C  CG  . GLU A 1 266 ? 9.471  29.234 -1.089  1.00 87.57  ? 266 GLU A CG  1 
ATOM   1814 C  CD  . GLU A 1 266 ? 8.903  27.836 -0.973  1.00 95.02  ? 266 GLU A CD  1 
ATOM   1815 O  OE1 . GLU A 1 266 ? 9.174  27.156 0.041   1.00 97.21  ? 266 GLU A OE1 1 
ATOM   1816 O  OE2 . GLU A 1 266 ? 8.188  27.417 -1.911  1.00 97.22  ? 266 GLU A OE2 1 
ATOM   1817 N  N   . LEU A 1 267 ? 10.641 30.004 3.459   1.00 75.98  ? 267 LEU A N   1 
ATOM   1818 C  CA  . LEU A 1 267 ? 11.459 30.532 4.557   1.00 74.36  ? 267 LEU A CA  1 
ATOM   1819 C  C   . LEU A 1 267 ? 12.632 29.672 4.946   1.00 73.45  ? 267 LEU A C   1 
ATOM   1820 O  O   . LEU A 1 267 ? 12.559 28.451 4.880   1.00 73.25  ? 267 LEU A O   1 
ATOM   1821 C  CB  . LEU A 1 267 ? 10.595 30.755 5.803   1.00 73.66  ? 267 LEU A CB  1 
ATOM   1822 C  CG  . LEU A 1 267 ? 9.403  31.660 5.658   1.00 74.30  ? 267 LEU A CG  1 
ATOM   1823 C  CD1 . LEU A 1 267 ? 8.418  31.436 6.780   1.00 74.58  ? 267 LEU A CD1 1 
ATOM   1824 C  CD2 . LEU A 1 267 ? 9.831  33.090 5.584   1.00 75.09  ? 267 LEU A CD2 1 
ATOM   1825 N  N   . TYR A 1 268 ? 13.708 30.324 5.394   1.00 72.68  ? 268 TYR A N   1 
ATOM   1826 C  CA  . TYR A 1 268 ? 14.878 29.671 5.962   1.00 72.36  ? 268 TYR A CA  1 
ATOM   1827 C  C   . TYR A 1 268 ? 15.200 30.449 7.227   1.00 71.20  ? 268 TYR A C   1 
ATOM   1828 O  O   . TYR A 1 268 ? 15.452 31.644 7.154   1.00 71.11  ? 268 TYR A O   1 
ATOM   1829 C  CB  . TYR A 1 268 ? 16.085 29.689 5.010   1.00 72.82  ? 268 TYR A CB  1 
ATOM   1830 C  CG  . TYR A 1 268 ? 17.363 29.162 5.632   1.00 73.83  ? 268 TYR A CG  1 
ATOM   1831 C  CD1 . TYR A 1 268 ? 17.614 27.801 5.709   1.00 74.84  ? 268 TYR A CD1 1 
ATOM   1832 C  CD2 . TYR A 1 268 ? 18.330 30.027 6.123   1.00 75.13  ? 268 TYR A CD2 1 
ATOM   1833 C  CE1 . TYR A 1 268 ? 18.782 27.312 6.288   1.00 76.11  ? 268 TYR A CE1 1 
ATOM   1834 C  CE2 . TYR A 1 268 ? 19.506 29.551 6.692   1.00 76.23  ? 268 TYR A CE2 1 
ATOM   1835 C  CZ  . TYR A 1 268 ? 19.741 28.193 6.751   1.00 77.22  ? 268 TYR A CZ  1 
ATOM   1836 O  OH  . TYR A 1 268 ? 20.918 27.731 7.285   1.00 78.78  ? 268 TYR A OH  1 
ATOM   1837 N  N   . VAL A 1 269 ? 15.129 29.799 8.387   1.00 69.96  ? 269 VAL A N   1 
ATOM   1838 C  CA  . VAL A 1 269 ? 15.457 30.443 9.643   1.00 69.13  ? 269 VAL A CA  1 
ATOM   1839 C  C   . VAL A 1 269 ? 16.547 29.621 10.320  1.00 68.84  ? 269 VAL A C   1 
ATOM   1840 O  O   . VAL A 1 269 ? 16.439 28.394 10.388  1.00 68.46  ? 269 VAL A O   1 
ATOM   1841 C  CB  . VAL A 1 269 ? 14.211 30.657 10.522  1.00 69.30  ? 269 VAL A CB  1 
ATOM   1842 C  CG1 . VAL A 1 269 ? 14.574 31.365 11.817  1.00 69.32  ? 269 VAL A CG1 1 
ATOM   1843 C  CG2 . VAL A 1 269 ? 13.137 31.441 9.773   1.00 69.47  ? 269 VAL A CG2 1 
ATOM   1844 N  N   . SER A 1 270 ? 17.646 30.283 10.747  1.00 68.92  ? 270 SER A N   1 
ATOM   1845 C  CA  . SER A 1 270 ? 18.777 29.575 11.332  1.00 68.55  ? 270 SER A CA  1 
ATOM   1846 C  C   . SER A 1 270 ? 19.312 30.207 12.648  1.00 68.35  ? 270 SER A C   1 
ATOM   1847 O  O   . SER A 1 270 ? 18.764 31.198 13.147  1.00 67.44  ? 270 SER A O   1 
ATOM   1848 C  CB  . SER A 1 270 ? 19.876 29.404 10.283  1.00 68.88  ? 270 SER A CB  1 
ATOM   1849 O  OG  . SER A 1 270 ? 20.814 30.458 10.326  1.00 71.03  ? 270 SER A OG  1 
ATOM   1850 N  N   . ASN A 1 271 ? 20.404 29.593 13.179  1.00 68.93  ? 271 ASN A N   1 
ATOM   1851 C  CA  . ASN A 1 271 ? 21.136 29.893 14.404  1.00 69.62  ? 271 ASN A CA  1 
ATOM   1852 C  C   . ASN A 1 271 ? 22.630 29.972 14.133  1.00 70.78  ? 271 ASN A C   1 
ATOM   1853 O  O   . ASN A 1 271 ? 23.197 29.004 13.626  1.00 71.29  ? 271 ASN A O   1 
ATOM   1854 C  CB  . ASN A 1 271 ? 20.955 28.724 15.359  1.00 70.26  ? 271 ASN A CB  1 
ATOM   1855 C  CG  . ASN A 1 271 ? 20.043 28.999 16.499  1.00 73.58  ? 271 ASN A CG  1 
ATOM   1856 O  OD1 . ASN A 1 271 ? 19.399 30.049 16.580  1.00 75.18  ? 271 ASN A OD1 1 
ATOM   1857 N  ND2 . ASN A 1 271 ? 19.970 28.056 17.411  1.00 74.16  ? 271 ASN A ND2 1 
ATOM   1858 N  N   . ALA A 1 272 ? 23.284 31.065 14.522  1.00 70.82  ? 272 ALA A N   1 
ATOM   1859 C  CA  . ALA A 1 272 ? 24.729 31.189 14.364  1.00 71.35  ? 272 ALA A CA  1 
ATOM   1860 C  C   . ALA A 1 272 ? 25.349 31.263 15.756  1.00 71.78  ? 272 ALA A C   1 
ATOM   1861 O  O   . ALA A 1 272 ? 26.194 32.123 16.021  1.00 72.22  ? 272 ALA A O   1 
ATOM   1862 C  CB  . ALA A 1 272 ? 25.079 32.423 13.547  1.00 71.64  ? 272 ALA A CB  1 
ATOM   1863 N  N   . SER A 1 273 ? 24.924 30.335 16.656  1.00 71.28  ? 273 SER A N   1 
ATOM   1864 C  CA  . SER A 1 273 ? 25.383 30.233 18.045  1.00 70.72  ? 273 SER A CA  1 
ATOM   1865 C  C   . SER A 1 273 ? 26.883 30.093 18.071  1.00 70.45  ? 273 SER A C   1 
ATOM   1866 O  O   . SER A 1 273 ? 27.405 29.150 17.509  1.00 71.25  ? 273 SER A O   1 
ATOM   1867 C  CB  . SER A 1 273 ? 24.770 29.005 18.715  1.00 71.56  ? 273 SER A CB  1 
ATOM   1868 O  OG  . SER A 1 273 ? 23.373 28.888 18.509  1.00 73.38  ? 273 SER A OG  1 
ATOM   1869 N  N   . GLY A 1 274 ? 27.571 31.034 18.682  1.00 69.51  ? 274 GLY A N   1 
ATOM   1870 C  CA  . GLY A 1 274 ? 29.023 30.998 18.757  1.00 68.97  ? 274 GLY A CA  1 
ATOM   1871 C  C   . GLY A 1 274 ? 29.535 31.771 19.936  1.00 68.82  ? 274 GLY A C   1 
ATOM   1872 O  O   . GLY A 1 274 ? 28.784 32.538 20.531  1.00 69.72  ? 274 GLY A O   1 
ATOM   1873 N  N   . LEU A 1 275 ? 30.803 31.573 20.301  1.00 68.20  ? 275 LEU A N   1 
ATOM   1874 C  CA  . LEU A 1 275 ? 31.413 32.285 21.421  1.00 68.12  ? 275 LEU A CA  1 
ATOM   1875 C  C   . LEU A 1 275 ? 31.924 33.629 20.904  1.00 69.60  ? 275 LEU A C   1 
ATOM   1876 O  O   . LEU A 1 275 ? 31.591 34.667 21.474  1.00 70.16  ? 275 LEU A O   1 
ATOM   1877 C  CB  . LEU A 1 275 ? 32.560 31.473 22.051  1.00 67.56  ? 275 LEU A CB  1 
ATOM   1878 C  CG  . LEU A 1 275 ? 32.258 30.018 22.392  1.00 67.72  ? 275 LEU A CG  1 
ATOM   1879 C  CD1 . LEU A 1 275 ? 33.531 29.253 22.616  1.00 67.41  ? 275 LEU A CD1 1 
ATOM   1880 C  CD2 . LEU A 1 275 ? 31.286 29.901 23.561  1.00 67.76  ? 275 LEU A CD2 1 
ATOM   1881 N  N   . ALA A 1 276 ? 32.722 33.620 19.810  1.00 69.89  ? 276 ALA A N   1 
ATOM   1882 C  CA  . ALA A 1 276 ? 33.211 34.841 19.178  1.00 70.07  ? 276 ALA A CA  1 
ATOM   1883 C  C   . ALA A 1 276 ? 32.162 35.198 18.157  1.00 71.17  ? 276 ALA A C   1 
ATOM   1884 O  O   . ALA A 1 276 ? 31.876 34.409 17.272  1.00 71.42  ? 276 ALA A O   1 
ATOM   1885 C  CB  . ALA A 1 276 ? 34.540 34.583 18.497  1.00 69.95  ? 276 ALA A CB  1 
ATOM   1886 N  N   . GLY A 1 277 ? 31.548 36.350 18.317  1.00 72.12  ? 277 GLY A N   1 
ATOM   1887 C  CA  . GLY A 1 277 ? 30.437 36.762 17.473  1.00 73.12  ? 277 GLY A CA  1 
ATOM   1888 C  C   . GLY A 1 277 ? 30.725 37.541 16.219  1.00 74.26  ? 277 GLY A C   1 
ATOM   1889 O  O   . GLY A 1 277 ? 31.715 37.303 15.533  1.00 74.66  ? 277 GLY A O   1 
ATOM   1890 N  N   . GLU A 1 278 ? 29.801 38.437 15.891  1.00 75.25  ? 278 GLU A N   1 
ATOM   1891 C  CA  . GLU A 1 278 ? 29.765 39.292 14.710  1.00 76.75  ? 278 GLU A CA  1 
ATOM   1892 C  C   . GLU A 1 278 ? 30.986 40.190 14.590  1.00 79.48  ? 278 GLU A C   1 
ATOM   1893 O  O   . GLU A 1 278 ? 31.428 40.481 13.485  1.00 79.55  ? 278 GLU A O   1 
ATOM   1894 C  CB  . GLU A 1 278 ? 28.489 40.142 14.769  1.00 77.71  ? 278 GLU A CB  1 
ATOM   1895 C  CG  . GLU A 1 278 ? 28.057 40.721 13.441  1.00 80.92  ? 278 GLU A CG  1 
ATOM   1896 C  CD  . GLU A 1 278 ? 26.750 41.487 13.472  1.00 84.95  ? 278 GLU A CD  1 
ATOM   1897 O  OE1 . GLU A 1 278 ? 26.233 41.764 14.578  1.00 84.96  ? 278 GLU A OE1 1 
ATOM   1898 O  OE2 . GLU A 1 278 ? 26.240 41.811 12.378  1.00 86.54  ? 278 GLU A OE2 1 
ATOM   1899 N  N   . TRP A 1 279 ? 31.538 40.622 15.729  1.00 81.76  ? 279 TRP A N   1 
ATOM   1900 C  CA  . TRP A 1 279 ? 32.713 41.489 15.825  1.00 84.24  ? 279 TRP A CA  1 
ATOM   1901 C  C   . TRP A 1 279 ? 34.022 40.777 15.493  1.00 86.08  ? 279 TRP A C   1 
ATOM   1902 O  O   . TRP A 1 279 ? 34.987 41.441 15.118  1.00 86.83  ? 279 TRP A O   1 
ATOM   1903 C  CB  . TRP A 1 279 ? 32.803 42.074 17.250  1.00 85.07  ? 279 TRP A CB  1 
ATOM   1904 C  CG  . TRP A 1 279 ? 32.816 41.032 18.345  1.00 86.83  ? 279 TRP A CG  1 
ATOM   1905 C  CD1 . TRP A 1 279 ? 33.905 40.360 18.830  1.00 88.15  ? 279 TRP A CD1 1 
ATOM   1906 C  CD2 . TRP A 1 279 ? 31.679 40.528 19.074  1.00 87.15  ? 279 TRP A CD2 1 
ATOM   1907 N  NE1 . TRP A 1 279 ? 33.512 39.430 19.768  1.00 88.54  ? 279 TRP A NE1 1 
ATOM   1908 C  CE2 . TRP A 1 279 ? 32.156 39.534 19.960  1.00 88.26  ? 279 TRP A CE2 1 
ATOM   1909 C  CE3 . TRP A 1 279 ? 30.303 40.795 19.036  1.00 87.47  ? 279 TRP A CE3 1 
ATOM   1910 C  CZ2 . TRP A 1 279 ? 31.307 38.838 20.829  1.00 88.99  ? 279 TRP A CZ2 1 
ATOM   1911 C  CZ3 . TRP A 1 279 ? 29.465 40.093 19.881  1.00 88.58  ? 279 TRP A CZ3 1 
ATOM   1912 C  CH2 . TRP A 1 279 ? 29.967 39.138 20.776  1.00 88.97  ? 279 TRP A CH2 1 
ATOM   1913 N  N   . GLU A 1 280 ? 34.067 39.437 15.636  1.00 86.94  ? 280 GLU A N   1 
ATOM   1914 C  CA  . GLU A 1 280 ? 35.274 38.635 15.472  1.00 88.38  ? 280 GLU A CA  1 
ATOM   1915 C  C   . GLU A 1 280 ? 35.384 37.781 14.197  1.00 89.45  ? 280 GLU A C   1 
ATOM   1916 O  O   . GLU A 1 280 ? 34.520 36.964 13.898  1.00 89.90  ? 280 GLU A O   1 
ATOM   1917 C  CB  . GLU A 1 280 ? 35.437 37.727 16.691  1.00 91.45  ? 280 GLU A CB  1 
ATOM   1918 C  CG  . GLU A 1 280 ? 36.877 37.375 17.010  1.00 97.62  ? 280 GLU A CG  1 
ATOM   1919 C  CD  . GLU A 1 280 ? 37.599 38.441 17.812  1.00 104.64 ? 280 GLU A CD  1 
ATOM   1920 O  OE1 . GLU A 1 280 ? 37.217 38.658 18.985  1.00 106.17 ? 280 GLU A OE1 1 
ATOM   1921 O  OE2 . GLU A 1 280 ? 38.546 39.056 17.268  1.00 106.29 ? 280 GLU A OE2 1 
ATOM   1922 N  N   . SER A 1 281 ? 36.531 37.895 13.529  1.00 90.00  ? 281 SER A N   1 
ATOM   1923 C  CA  . SER A 1 281 ? 36.879 37.161 12.322  1.00 91.23  ? 281 SER A CA  1 
ATOM   1924 C  C   . SER A 1 281 ? 37.358 35.746 12.615  1.00 92.31  ? 281 SER A C   1 
ATOM   1925 O  O   . SER A 1 281 ? 38.050 35.517 13.605  1.00 92.78  ? 281 SER A O   1 
ATOM   1926 C  CB  . SER A 1 281 ? 37.958 37.908 11.536  1.00 92.92  ? 281 SER A CB  1 
ATOM   1927 O  OG  . SER A 1 281 ? 39.030 38.365 12.346  1.00 95.47  ? 281 SER A OG  1 
ATOM   1928 N  N   . VAL A 1 282 ? 37.035 34.804 11.725  1.00 92.45  ? 282 VAL A N   1 
ATOM   1929 C  CA  . VAL A 1 282 ? 37.440 33.416 11.891  1.00 92.87  ? 282 VAL A CA  1 
ATOM   1930 C  C   . VAL A 1 282 ? 38.916 33.233 11.549  1.00 93.52  ? 282 VAL A C   1 
ATOM   1931 O  O   . VAL A 1 282 ? 39.772 33.340 12.429  1.00 93.96  ? 282 VAL A O   1 
ATOM   1932 C  CB  . VAL A 1 282 ? 36.543 32.461 11.069  1.00 93.37  ? 282 VAL A CB  1 
ATOM   1933 C  CG1 . VAL A 1 282 ? 36.865 31.004 11.386  1.00 93.76  ? 282 VAL A CG1 1 
ATOM   1934 C  CG2 . VAL A 1 282 ? 35.067 32.751 11.309  1.00 93.73  ? 282 VAL A CG2 1 
ATOM   1935 N  N   . LEU A 1 290 ? 49.559 39.632 23.867  1.00 108.62 ? 290 LEU A N   1 
ATOM   1936 C  CA  . LEU A 1 290 ? 49.738 40.203 25.205  1.00 109.07 ? 290 LEU A CA  1 
ATOM   1937 C  C   . LEU A 1 290 ? 49.718 39.124 26.328  1.00 109.29 ? 290 LEU A C   1 
ATOM   1938 O  O   . LEU A 1 290 ? 49.570 37.940 26.025  1.00 109.63 ? 290 LEU A O   1 
ATOM   1939 C  CB  . LEU A 1 290 ? 48.758 41.371 25.502  1.00 109.39 ? 290 LEU A CB  1 
ATOM   1940 C  CG  . LEU A 1 290 ? 47.546 41.615 24.604  1.00 110.96 ? 290 LEU A CG  1 
ATOM   1941 C  CD1 . LEU A 1 290 ? 46.551 40.477 24.688  1.00 111.76 ? 290 LEU A CD1 1 
ATOM   1942 C  CD2 . LEU A 1 290 ? 46.858 42.897 24.990  1.00 111.48 ? 290 LEU A CD2 1 
ATOM   1943 N  N   . ASN A 1 291 ? 49.934 39.535 27.608  1.00 108.98 ? 291 ASN A N   1 
ATOM   1944 C  CA  . ASN A 1 291 ? 49.981 38.691 28.811  1.00 109.18 ? 291 ASN A CA  1 
ATOM   1945 C  C   . ASN A 1 291 ? 48.896 37.632 28.833  1.00 109.18 ? 291 ASN A C   1 
ATOM   1946 O  O   . ASN A 1 291 ? 47.764 37.903 28.437  1.00 109.37 ? 291 ASN A O   1 
ATOM   1947 C  CB  . ASN A 1 291 ? 49.869 39.566 30.067  1.00 110.38 ? 291 ASN A CB  1 
ATOM   1948 C  CG  . ASN A 1 291 ? 50.093 38.893 31.404  1.00 113.64 ? 291 ASN A CG  1 
ATOM   1949 O  OD1 . ASN A 1 291 ? 50.597 37.767 31.510  1.00 114.82 ? 291 ASN A OD1 1 
ATOM   1950 N  ND2 . ASN A 1 291 ? 49.720 39.585 32.470  1.00 114.27 ? 291 ASN A ND2 1 
ATOM   1951 N  N   . GLN A 1 292 ? 49.237 36.428 29.324  1.00 108.81 ? 292 GLN A N   1 
ATOM   1952 C  CA  . GLN A 1 292 ? 48.306 35.298 29.432  1.00 108.76 ? 292 GLN A CA  1 
ATOM   1953 C  C   . GLN A 1 292 ? 47.145 35.555 30.412  1.00 107.75 ? 292 GLN A C   1 
ATOM   1954 O  O   . GLN A 1 292 ? 46.148 34.845 30.360  1.00 107.73 ? 292 GLN A O   1 
ATOM   1955 C  CB  . GLN A 1 292 ? 49.053 34.001 29.792  1.00 110.98 ? 292 GLN A CB  1 
ATOM   1956 C  CG  . GLN A 1 292 ? 50.314 33.748 28.956  1.00 115.43 ? 292 GLN A CG  1 
ATOM   1957 C  CD  . GLN A 1 292 ? 50.023 33.500 27.492  1.00 120.93 ? 292 GLN A CD  1 
ATOM   1958 O  OE1 . GLN A 1 292 ? 50.111 34.404 26.651  1.00 122.86 ? 292 GLN A OE1 1 
ATOM   1959 N  NE2 . GLN A 1 292 ? 49.683 32.263 27.151  1.00 121.75 ? 292 GLN A NE2 1 
ATOM   1960 N  N   . GLN A 1 293 ? 47.276 36.567 31.292  1.00 106.86 ? 293 GLN A N   1 
ATOM   1961 C  CA  . GLN A 1 293 ? 46.254 36.989 32.254  1.00 106.36 ? 293 GLN A CA  1 
ATOM   1962 C  C   . GLN A 1 293 ? 45.183 37.791 31.519  1.00 105.10 ? 293 GLN A C   1 
ATOM   1963 O  O   . GLN A 1 293 ? 43.997 37.587 31.764  1.00 105.35 ? 293 GLN A O   1 
ATOM   1964 C  CB  . GLN A 1 293 ? 46.879 37.848 33.374  1.00 108.22 ? 293 GLN A CB  1 
ATOM   1965 C  CG  . GLN A 1 293 ? 45.874 38.426 34.375  1.00 111.71 ? 293 GLN A CG  1 
ATOM   1966 C  CD  . GLN A 1 293 ? 45.968 39.934 34.517  1.00 116.53 ? 293 GLN A CD  1 
ATOM   1967 O  OE1 . GLN A 1 293 ? 46.899 40.587 34.018  1.00 118.53 ? 293 GLN A OE1 1 
ATOM   1968 N  NE2 . GLN A 1 293 ? 44.998 40.525 35.208  1.00 116.51 ? 293 GLN A NE2 1 
ATOM   1969 N  N   . VAL A 1 294 ? 45.592 38.690 30.601  1.00 103.40 ? 294 VAL A N   1 
ATOM   1970 C  CA  . VAL A 1 294 ? 44.624 39.484 29.833  1.00 101.95 ? 294 VAL A CA  1 
ATOM   1971 C  C   . VAL A 1 294 ? 44.076 38.687 28.638  1.00 100.09 ? 294 VAL A C   1 
ATOM   1972 O  O   . VAL A 1 294 ? 42.939 38.913 28.238  1.00 100.19 ? 294 VAL A O   1 
ATOM   1973 C  CB  . VAL A 1 294 ? 45.130 40.891 29.435  1.00 102.62 ? 294 VAL A CB  1 
ATOM   1974 C  CG1 . VAL A 1 294 ? 45.894 41.537 30.580  1.00 103.19 ? 294 VAL A CG1 1 
ATOM   1975 C  CG2 . VAL A 1 294 ? 45.993 40.840 28.189  1.00 103.09 ? 294 VAL A CG2 1 
ATOM   1976 N  N   . GLN A 1 295 ? 44.849 37.719 28.112  1.00 98.33  ? 295 GLN A N   1 
ATOM   1977 C  CA  . GLN A 1 295 ? 44.392 36.846 27.033  1.00 97.19  ? 295 GLN A CA  1 
ATOM   1978 C  C   . GLN A 1 295 ? 43.301 35.887 27.527  1.00 95.68  ? 295 GLN A C   1 
ATOM   1979 O  O   . GLN A 1 295 ? 42.429 35.511 26.752  1.00 95.75  ? 295 GLN A O   1 
ATOM   1980 C  CB  . GLN A 1 295 ? 45.560 36.046 26.456  1.00 98.75  ? 295 GLN A CB  1 
ATOM   1981 C  CG  . GLN A 1 295 ? 46.150 36.665 25.204  1.00 102.53 ? 295 GLN A CG  1 
ATOM   1982 C  CD  . GLN A 1 295 ? 47.202 35.799 24.552  1.00 108.60 ? 295 GLN A CD  1 
ATOM   1983 O  OE1 . GLN A 1 295 ? 47.599 34.733 25.057  1.00 110.41 ? 295 GLN A OE1 1 
ATOM   1984 N  NE2 . GLN A 1 295 ? 47.687 36.250 23.402  1.00 109.98 ? 295 GLN A NE2 1 
ATOM   1985 N  N   . SER A 1 296 ? 43.358 35.488 28.808  1.00 94.17  ? 296 SER A N   1 
ATOM   1986 C  CA  . SER A 1 296 ? 42.365 34.620 29.415  1.00 93.18  ? 296 SER A CA  1 
ATOM   1987 C  C   . SER A 1 296 ? 41.172 35.433 29.909  1.00 91.76  ? 296 SER A C   1 
ATOM   1988 O  O   . SER A 1 296 ? 40.057 34.928 29.852  1.00 91.89  ? 296 SER A O   1 
ATOM   1989 C  CB  . SER A 1 296 ? 42.973 33.795 30.546  1.00 94.94  ? 296 SER A CB  1 
ATOM   1990 O  OG  . SER A 1 296 ? 43.318 34.578 31.677  1.00 97.48  ? 296 SER A OG  1 
ATOM   1991 N  N   . ILE A 1 297 ? 41.386 36.684 30.377  1.00 90.47  ? 297 ILE A N   1 
ATOM   1992 C  CA  . ILE A 1 297 ? 40.284 37.557 30.812  1.00 89.78  ? 297 ILE A CA  1 
ATOM   1993 C  C   . ILE A 1 297 ? 39.397 37.925 29.612  1.00 88.78  ? 297 ILE A C   1 
ATOM   1994 O  O   . ILE A 1 297 ? 38.179 37.819 29.706  1.00 88.73  ? 297 ILE A O   1 
ATOM   1995 C  CB  . ILE A 1 297 ? 40.753 38.833 31.578  1.00 90.28  ? 297 ILE A CB  1 
ATOM   1996 C  CG1 . ILE A 1 297 ? 41.388 38.491 32.933  1.00 91.10  ? 297 ILE A CG1 1 
ATOM   1997 C  CG2 . ILE A 1 297 ? 39.583 39.784 31.800  1.00 90.62  ? 297 ILE A CG2 1 
ATOM   1998 C  CD1 . ILE A 1 297 ? 41.953 39.712 33.685  1.00 92.24  ? 297 ILE A CD1 1 
ATOM   1999 N  N   . ALA A 1 298 ? 40.002 38.345 28.487  1.00 87.84  ? 298 ALA A N   1 
ATOM   2000 C  CA  . ALA A 1 298 ? 39.241 38.705 27.290  1.00 87.16  ? 298 ALA A CA  1 
ATOM   2001 C  C   . ALA A 1 298 ? 38.499 37.506 26.701  1.00 86.13  ? 298 ALA A C   1 
ATOM   2002 O  O   . ALA A 1 298 ? 37.388 37.657 26.208  1.00 86.33  ? 298 ALA A O   1 
ATOM   2003 C  CB  . ALA A 1 298 ? 40.158 39.321 26.246  1.00 87.34  ? 298 ALA A CB  1 
ATOM   2004 N  N   . MET A 1 299 ? 39.105 36.319 26.773  1.00 84.99  ? 299 MET A N   1 
ATOM   2005 C  CA  . MET A 1 299 ? 38.531 35.061 26.284  1.00 84.37  ? 299 MET A CA  1 
ATOM   2006 C  C   . MET A 1 299 ? 37.361 34.617 27.135  1.00 82.58  ? 299 MET A C   1 
ATOM   2007 O  O   . MET A 1 299 ? 36.458 33.982 26.631  1.00 82.74  ? 299 MET A O   1 
ATOM   2008 C  CB  . MET A 1 299 ? 39.601 33.978 26.313  1.00 86.29  ? 299 MET A CB  1 
ATOM   2009 C  CG  . MET A 1 299 ? 39.283 32.772 25.483  1.00 90.31  ? 299 MET A CG  1 
ATOM   2010 S  SD  . MET A 1 299 ? 40.700 31.649 25.482  1.00 98.86  ? 299 MET A SD  1 
ATOM   2011 C  CE  . MET A 1 299 ? 41.925 32.671 24.650  1.00 99.17  ? 299 MET A CE  1 
ATOM   2012 N  N   . ALA A 1 300 ? 37.396 34.901 28.435  1.00 81.31  ? 300 ALA A N   1 
ATOM   2013 C  CA  . ALA A 1 300 ? 36.308 34.603 29.367  1.00 80.47  ? 300 ALA A CA  1 
ATOM   2014 C  C   . ALA A 1 300 ? 35.087 35.455 29.050  1.00 79.79  ? 300 ALA A C   1 
ATOM   2015 O  O   . ALA A 1 300 ? 33.967 35.010 29.273  1.00 80.39  ? 300 ALA A O   1 
ATOM   2016 C  CB  . ALA A 1 300 ? 36.752 34.878 30.797  1.00 80.33  ? 300 ALA A CB  1 
ATOM   2017 N  N   . GLU A 1 301 ? 35.299 36.686 28.566  1.00 78.49  ? 301 GLU A N   1 
ATOM   2018 C  CA  . GLU A 1 301 ? 34.250 37.607 28.201  1.00 77.93  ? 301 GLU A CA  1 
ATOM   2019 C  C   . GLU A 1 301 ? 33.557 37.156 26.961  1.00 76.88  ? 301 GLU A C   1 
ATOM   2020 O  O   . GLU A 1 301 ? 32.349 37.297 26.908  1.00 77.43  ? 301 GLU A O   1 
ATOM   2021 C  CB  . GLU A 1 301 ? 34.825 38.992 27.938  1.00 81.30  ? 301 GLU A CB  1 
ATOM   2022 C  CG  . GLU A 1 301 ? 35.489 39.604 29.148  1.00 88.25  ? 301 GLU A CG  1 
ATOM   2023 C  CD  . GLU A 1 301 ? 34.984 40.996 29.454  1.00 97.34  ? 301 GLU A CD  1 
ATOM   2024 O  OE1 . GLU A 1 301 ? 34.567 41.694 28.499  1.00 98.98  ? 301 GLU A OE1 1 
ATOM   2025 O  OE2 . GLU A 1 301 ? 34.995 41.383 30.647  1.00 100.18 ? 301 GLU A OE2 1 
ATOM   2026 N  N   . THR A 1 302 ? 34.285 36.650 25.941  1.00 75.50  ? 302 THR A N   1 
ATOM   2027 C  CA  . THR A 1 302 ? 33.611 36.242 24.710  1.00 74.56  ? 302 THR A CA  1 
ATOM   2028 C  C   . THR A 1 302 ? 32.741 35.017 24.982  1.00 73.10  ? 302 THR A C   1 
ATOM   2029 O  O   . THR A 1 302 ? 31.637 34.960 24.473  1.00 73.71  ? 302 THR A O   1 
ATOM   2030 C  CB  . THR A 1 302 ? 34.535 36.122 23.489  1.00 76.24  ? 302 THR A CB  1 
ATOM   2031 O  OG1 . THR A 1 302 ? 35.079 34.814 23.386  1.00 78.10  ? 302 THR A OG1 1 
ATOM   2032 C  CG2 . THR A 1 302 ? 35.620 37.176 23.450  1.00 76.55  ? 302 THR A CG2 1 
ATOM   2033 N  N   . VAL A 1 303 ? 33.182 34.086 25.828  1.00 71.47  ? 303 VAL A N   1 
ATOM   2034 C  CA  . VAL A 1 303 ? 32.385 32.910 26.176  1.00 70.30  ? 303 VAL A CA  1 
ATOM   2035 C  C   . VAL A 1 303 ? 31.078 33.335 26.857  1.00 70.22  ? 303 VAL A C   1 
ATOM   2036 O  O   . VAL A 1 303 ? 30.015 32.827 26.506  1.00 70.85  ? 303 VAL A O   1 
ATOM   2037 C  CB  . VAL A 1 303 ? 33.196 31.884 27.017  1.00 69.73  ? 303 VAL A CB  1 
ATOM   2038 C  CG1 . VAL A 1 303 ? 32.325 30.720 27.463  1.00 69.68  ? 303 VAL A CG1 1 
ATOM   2039 C  CG2 . VAL A 1 303 ? 34.405 31.377 26.241  1.00 69.51  ? 303 VAL A CG2 1 
ATOM   2040 N  N   . VAL A 1 304 ? 31.145 34.343 27.749  1.00 69.45  ? 304 VAL A N   1 
ATOM   2041 C  CA  . VAL A 1 304 ? 29.994 34.905 28.464  1.00 68.77  ? 304 VAL A CA  1 
ATOM   2042 C  C   . VAL A 1 304 ? 29.050 35.698 27.536  1.00 69.18  ? 304 VAL A C   1 
ATOM   2043 O  O   . VAL A 1 304 ? 27.871 35.362 27.486  1.00 69.69  ? 304 VAL A O   1 
ATOM   2044 C  CB  . VAL A 1 304 ? 30.447 35.720 29.700  1.00 68.65  ? 304 VAL A CB  1 
ATOM   2045 C  CG1 . VAL A 1 304 ? 29.313 36.573 30.263  1.00 69.11  ? 304 VAL A CG1 1 
ATOM   2046 C  CG2 . VAL A 1 304 ? 31.007 34.791 30.779  1.00 68.51  ? 304 VAL A CG2 1 
ATOM   2047 N  N   . THR A 1 305 ? 29.552 36.709 26.779  1.00 69.03  ? 305 THR A N   1 
ATOM   2048 C  CA  . THR A 1 305 ? 28.751 37.527 25.848  1.00 69.33  ? 305 THR A CA  1 
ATOM   2049 C  C   . THR A 1 305 ? 28.141 36.733 24.693  1.00 69.17  ? 305 THR A C   1 
ATOM   2050 O  O   . THR A 1 305 ? 26.987 36.947 24.326  1.00 69.25  ? 305 THR A O   1 
ATOM   2051 C  CB  . THR A 1 305 ? 29.575 38.676 25.292  1.00 71.50  ? 305 THR A CB  1 
ATOM   2052 O  OG1 . THR A 1 305 ? 30.523 38.156 24.365  1.00 73.65  ? 305 THR A OG1 1 
ATOM   2053 C  CG2 . THR A 1 305 ? 30.262 39.485 26.372  1.00 71.89  ? 305 THR A CG2 1 
ATOM   2054 N  N   . GLY A 1 306 ? 28.936 35.845 24.105  1.00 68.72  ? 306 GLY A N   1 
ATOM   2055 C  CA  . GLY A 1 306 ? 28.476 34.972 23.036  1.00 69.05  ? 306 GLY A CA  1 
ATOM   2056 C  C   . GLY A 1 306 ? 27.396 34.045 23.537  1.00 70.01  ? 306 GLY A C   1 
ATOM   2057 O  O   . GLY A 1 306 ? 26.461 33.740 22.813  1.00 71.33  ? 306 GLY A O   1 
ATOM   2058 N  N   . GLY A 1 307 ? 27.530 33.622 24.786  1.00 69.75  ? 307 GLY A N   1 
ATOM   2059 C  CA  . GLY A 1 307 ? 26.588 32.788 25.510  1.00 69.55  ? 307 GLY A CA  1 
ATOM   2060 C  C   . GLY A 1 307 ? 25.295 33.517 25.776  1.00 69.47  ? 307 GLY A C   1 
ATOM   2061 O  O   . GLY A 1 307 ? 24.242 32.926 25.588  1.00 70.32  ? 307 GLY A O   1 
ATOM   2062 N  N   . ILE A 1 308 ? 25.340 34.793 26.204  1.00 68.74  ? 308 ILE A N   1 
ATOM   2063 C  CA  . ILE A 1 308 ? 24.129 35.598 26.401  1.00 68.79  ? 308 ILE A CA  1 
ATOM   2064 C  C   . ILE A 1 308 ? 23.456 35.873 25.040  1.00 69.46  ? 308 ILE A C   1 
ATOM   2065 O  O   . ILE A 1 308 ? 22.236 35.835 24.937  1.00 69.94  ? 308 ILE A O   1 
ATOM   2066 C  CB  . ILE A 1 308 ? 24.450 36.930 27.147  1.00 68.99  ? 308 ILE A CB  1 
ATOM   2067 C  CG1 . ILE A 1 308 ? 24.928 36.685 28.594  1.00 69.32  ? 308 ILE A CG1 1 
ATOM   2068 C  CG2 . ILE A 1 308 ? 23.268 37.902 27.105  1.00 69.30  ? 308 ILE A CG2 1 
ATOM   2069 C  CD1 . ILE A 1 308 ? 25.494 37.856 29.229  1.00 70.00  ? 308 ILE A CD1 1 
ATOM   2070 N  N   . ILE A 1 309 ? 24.242 36.154 24.005  1.00 69.62  ? 309 ILE A N   1 
ATOM   2071 C  CA  . ILE A 1 309 ? 23.703 36.422 22.671  1.00 70.13  ? 309 ILE A CA  1 
ATOM   2072 C  C   . ILE A 1 309 ? 23.031 35.179 22.124  1.00 70.49  ? 309 ILE A C   1 
ATOM   2073 O  O   . ILE A 1 309 ? 21.925 35.258 21.588  1.00 71.17  ? 309 ILE A O   1 
ATOM   2074 C  CB  . ILE A 1 309 ? 24.790 36.970 21.717  1.00 70.58  ? 309 ILE A CB  1 
ATOM   2075 C  CG1 . ILE A 1 309 ? 25.206 38.390 22.131  1.00 71.72  ? 309 ILE A CG1 1 
ATOM   2076 C  CG2 . ILE A 1 309 ? 24.315 36.959 20.278  1.00 70.70  ? 309 ILE A CG2 1 
ATOM   2077 C  CD1 . ILE A 1 309 ? 26.440 38.859 21.451  1.00 73.06  ? 309 ILE A CD1 1 
ATOM   2078 N  N   . GLU A 1 310 ? 23.691 34.023 22.267  1.00 69.98  ? 310 GLU A N   1 
ATOM   2079 C  CA  . GLU A 1 310 ? 23.156 32.742 21.813  1.00 69.59  ? 310 GLU A CA  1 
ATOM   2080 C  C   . GLU A 1 310 ? 21.849 32.433 22.517  1.00 69.26  ? 310 GLU A C   1 
ATOM   2081 O  O   . GLU A 1 310 ? 20.887 32.127 21.842  1.00 70.09  ? 310 GLU A O   1 
ATOM   2082 C  CB  . GLU A 1 310 ? 24.166 31.613 22.043  1.00 71.34  ? 310 GLU A CB  1 
ATOM   2083 C  CG  . GLU A 1 310 ? 23.614 30.241 21.728  1.00 76.24  ? 310 GLU A CG  1 
ATOM   2084 C  CD  . GLU A 1 310 ? 24.408 29.090 22.294  1.00 84.61  ? 310 GLU A CD  1 
ATOM   2085 O  OE1 . GLU A 1 310 ? 25.648 29.222 22.411  1.00 86.16  ? 310 GLU A OE1 1 
ATOM   2086 O  OE2 . GLU A 1 310 ? 23.789 28.052 22.622  1.00 88.43  ? 310 GLU A OE2 1 
ATOM   2087 N  N   . ALA A 1 311 ? 21.801 32.543 23.851  1.00 68.07  ? 311 ALA A N   1 
ATOM   2088 C  CA  . ALA A 1 311 ? 20.605 32.291 24.639  1.00 67.44  ? 311 ALA A CA  1 
ATOM   2089 C  C   . ALA A 1 311 ? 19.423 33.171 24.218  1.00 67.52  ? 311 ALA A C   1 
ATOM   2090 O  O   . ALA A 1 311 ? 18.310 32.679 24.090  1.00 67.46  ? 311 ALA A O   1 
ATOM   2091 C  CB  . ALA A 1 311 ? 20.917 32.499 26.110  1.00 67.48  ? 311 ALA A CB  1 
ATOM   2092 N  N   . ALA A 1 312 ? 19.669 34.469 23.979  1.00 67.84  ? 312 ALA A N   1 
ATOM   2093 C  CA  . ALA A 1 312 ? 18.669 35.446 23.551  1.00 68.00  ? 312 ALA A CA  1 
ATOM   2094 C  C   . ALA A 1 312 ? 18.066 35.089 22.184  1.00 68.91  ? 312 ALA A C   1 
ATOM   2095 O  O   . ALA A 1 312 ? 16.854 35.112 22.038  1.00 69.47  ? 312 ALA A O   1 
ATOM   2096 C  CB  . ALA A 1 312 ? 19.298 36.831 23.509  1.00 67.73  ? 312 ALA A CB  1 
ATOM   2097 N  N   . THR A 1 313 ? 18.908 34.742 21.194  1.00 69.00  ? 313 THR A N   1 
ATOM   2098 C  CA  . THR A 1 313 ? 18.522 34.366 19.838  1.00 69.15  ? 313 THR A CA  1 
ATOM   2099 C  C   . THR A 1 313 ? 17.807 33.007 19.845  1.00 70.01  ? 313 THR A C   1 
ATOM   2100 O  O   . THR A 1 313 ? 16.854 32.799 19.092  1.00 71.18  ? 313 THR A O   1 
ATOM   2101 C  CB  . THR A 1 313 ? 19.792 34.304 18.992  1.00 70.13  ? 313 THR A CB  1 
ATOM   2102 O  OG1 . THR A 1 313 ? 20.457 35.575 19.006  1.00 70.89  ? 313 THR A OG1 1 
ATOM   2103 C  CG2 . THR A 1 313 ? 19.552 33.788 17.590  1.00 70.59  ? 313 THR A CG2 1 
ATOM   2104 N  N   . ASN A 1 314 ? 18.263 32.077 20.686  1.00 69.28  ? 314 ASN A N   1 
ATOM   2105 C  CA  . ASN A 1 314 ? 17.665 30.754 20.786  1.00 69.06  ? 314 ASN A CA  1 
ATOM   2106 C  C   . ASN A 1 314 ? 16.217 30.819 21.204  1.00 69.73  ? 314 ASN A C   1 
ATOM   2107 O  O   . ASN A 1 314 ? 15.425 30.018 20.718  1.00 70.50  ? 314 ASN A O   1 
ATOM   2108 C  CB  . ASN A 1 314 ? 18.429 29.863 21.774  1.00 69.07  ? 314 ASN A CB  1 
ATOM   2109 C  CG  . ASN A 1 314 ? 19.685 29.255 21.224  1.00 69.53  ? 314 ASN A CG  1 
ATOM   2110 O  OD1 . ASN A 1 314 ? 20.023 29.427 20.058  1.00 70.25  ? 314 ASN A OD1 1 
ATOM   2111 N  ND2 . ASN A 1 314 ? 20.409 28.537 22.055  1.00 69.31  ? 314 ASN A ND2 1 
ATOM   2112 N  N   . LYS A 1 315 ? 15.869 31.710 22.131  1.00 69.78  ? 315 LYS A N   1 
ATOM   2113 C  CA  . LYS A 1 315 ? 14.484 31.815 22.579  1.00 70.39  ? 315 LYS A CA  1 
ATOM   2114 C  C   . LYS A 1 315 ? 13.658 32.514 21.533  1.00 72.13  ? 315 LYS A C   1 
ATOM   2115 O  O   . LYS A 1 315 ? 12.567 32.067 21.234  1.00 73.10  ? 315 LYS A O   1 
ATOM   2116 C  CB  . LYS A 1 315 ? 14.395 32.536 23.913  1.00 71.48  ? 315 LYS A CB  1 
ATOM   2117 C  CG  . LYS A 1 315 ? 12.987 32.572 24.456  1.00 75.02  ? 315 LYS A CG  1 
ATOM   2118 C  CD  . LYS A 1 315 ? 12.859 31.891 25.805  1.00 78.21  ? 315 LYS A CD  1 
ATOM   2119 C  CE  . LYS A 1 315 ? 11.405 31.629 26.085  1.00 81.11  ? 315 LYS A CE  1 
ATOM   2120 N  NZ  . LYS A 1 315 ? 10.824 30.686 25.098  1.00 82.89  ? 315 LYS A NZ  1 
ATOM   2121 N  N   . CYS A 1 316 ? 14.196 33.566 20.904  1.00 72.67  ? 316 CYS A N   1 
ATOM   2122 C  CA  . CYS A 1 316 ? 13.515 34.301 19.844  1.00 73.54  ? 316 CYS A CA  1 
ATOM   2123 C  C   . CYS A 1 316 ? 13.129 33.386 18.700  1.00 73.97  ? 316 CYS A C   1 
ATOM   2124 O  O   . CYS A 1 316 ? 12.039 33.506 18.152  1.00 74.58  ? 316 CYS A O   1 
ATOM   2125 C  CB  . CYS A 1 316 ? 14.400 35.436 19.347  1.00 75.16  ? 316 CYS A CB  1 
ATOM   2126 S  SG  . CYS A 1 316 ? 14.670 36.766 20.547  1.00 80.79  ? 316 CYS A SG  1 
ATOM   2127 N  N   . THR A 1 317 ? 14.050 32.504 18.318  1.00 73.88  ? 317 THR A N   1 
ATOM   2128 C  CA  . THR A 1 317 ? 13.862 31.540 17.245  1.00 74.40  ? 317 THR A CA  1 
ATOM   2129 C  C   . THR A 1 317 ? 12.883 30.463 17.658  1.00 76.14  ? 317 THR A C   1 
ATOM   2130 O  O   . THR A 1 317 ? 12.075 30.036 16.845  1.00 76.54  ? 317 THR A O   1 
ATOM   2131 C  CB  . THR A 1 317 ? 15.199 30.952 16.815  1.00 74.57  ? 317 THR A CB  1 
ATOM   2132 O  OG1 . THR A 1 317 ? 16.156 32.002 16.630  1.00 75.50  ? 317 THR A OG1 1 
ATOM   2133 C  CG2 . THR A 1 317 ? 15.081 30.167 15.546  1.00 74.22  ? 317 THR A CG2 1 
ATOM   2134 N  N   . HIS A 1 318 ? 12.928 30.025 18.921  1.00 77.21  ? 318 HIS A N   1 
ATOM   2135 C  CA  . HIS A 1 318 ? 11.987 29.034 19.427  1.00 78.40  ? 318 HIS A CA  1 
ATOM   2136 C  C   . HIS A 1 318 ? 10.580 29.602 19.414  1.00 78.66  ? 318 HIS A C   1 
ATOM   2137 O  O   . HIS A 1 318 ? 9.656  28.898 19.029  1.00 79.12  ? 318 HIS A O   1 
ATOM   2138 C  CB  . HIS A 1 318 ? 12.347 28.585 20.848  1.00 80.42  ? 318 HIS A CB  1 
ATOM   2139 C  CG  . HIS A 1 318 ? 11.462 27.481 21.358  1.00 84.53  ? 318 HIS A CG  1 
ATOM   2140 N  ND1 . HIS A 1 318 ? 10.295 27.750 22.077  1.00 86.81  ? 318 HIS A ND1 1 
ATOM   2141 C  CD2 . HIS A 1 318 ? 11.585 26.139 21.215  1.00 85.85  ? 318 HIS A CD2 1 
ATOM   2142 C  CE1 . HIS A 1 318 ? 9.765  26.567 22.353  1.00 87.30  ? 318 HIS A CE1 1 
ATOM   2143 N  NE2 . HIS A 1 318 ? 10.506 25.568 21.861  1.00 87.04  ? 318 HIS A NE2 1 
ATOM   2144 N  N   . ASP A 1 319 ? 10.402 30.865 19.821  1.00 78.33  ? 319 ASP A N   1 
ATOM   2145 C  CA  . ASP A 1 319 ? 9.080  31.492 19.818  1.00 78.46  ? 319 ASP A CA  1 
ATOM   2146 C  C   . ASP A 1 319 ? 8.522  31.627 18.411  1.00 79.26  ? 319 ASP A C   1 
ATOM   2147 O  O   . ASP A 1 319 ? 7.324  31.457 18.212  1.00 79.80  ? 319 ASP A O   1 
ATOM   2148 C  CB  . ASP A 1 319 ? 9.126  32.866 20.487  1.00 78.96  ? 319 ASP A CB  1 
ATOM   2149 C  CG  . ASP A 1 319 ? 9.454  32.844 21.959  1.00 82.04  ? 319 ASP A CG  1 
ATOM   2150 O  OD1 . ASP A 1 319 ? 9.492  31.739 22.547  1.00 82.42  ? 319 ASP A OD1 1 
ATOM   2151 O  OD2 . ASP A 1 319 ? 9.683  33.927 22.524  1.00 84.29  ? 319 ASP A OD2 1 
ATOM   2152 N  N   . LEU A 1 320 ? 9.378  31.944 17.439  1.00 79.30  ? 320 LEU A N   1 
ATOM   2153 C  CA  . LEU A 1 320 ? 8.947  32.096 16.059  1.00 79.80  ? 320 LEU A CA  1 
ATOM   2154 C  C   . LEU A 1 320 ? 8.540  30.749 15.489  1.00 80.39  ? 320 LEU A C   1 
ATOM   2155 O  O   . LEU A 1 320 ? 7.515  30.653 14.826  1.00 80.68  ? 320 LEU A O   1 
ATOM   2156 C  CB  . LEU A 1 320 ? 10.069 32.723 15.231  1.00 80.05  ? 320 LEU A CB  1 
ATOM   2157 C  CG  . LEU A 1 320 ? 9.802  32.875 13.752  1.00 81.62  ? 320 LEU A CG  1 
ATOM   2158 C  CD1 . LEU A 1 320 ? 8.687  33.850 13.506  1.00 82.16  ? 320 LEU A CD1 1 
ATOM   2159 C  CD2 . LEU A 1 320 ? 11.044 33.299 13.027  1.00 82.17  ? 320 LEU A CD2 1 
ATOM   2160 N  N   . LYS A 1 321 ? 9.322  29.701 15.763  1.00 80.39  ? 321 LYS A N   1 
ATOM   2161 C  CA  . LYS A 1 321 ? 9.019  28.362 15.273  1.00 80.67  ? 321 LYS A CA  1 
ATOM   2162 C  C   . LYS A 1 321 ? 7.728  27.854 15.841  1.00 81.42  ? 321 LYS A C   1 
ATOM   2163 O  O   . LYS A 1 321 ? 6.924  27.330 15.102  1.00 81.86  ? 321 LYS A O   1 
ATOM   2164 C  CB  . LYS A 1 321 ? 10.159 27.381 15.578  1.00 81.81  ? 321 LYS A CB  1 
ATOM   2165 C  CG  . LYS A 1 321 ? 9.897  25.970 15.065  1.00 84.37  ? 321 LYS A CG  1 
ATOM   2166 C  CD  . LYS A 1 321 ? 11.167 25.165 14.946  1.00 86.39  ? 321 LYS A CD  1 
ATOM   2167 C  CE  . LYS A 1 321 ? 10.917 23.690 15.056  1.00 88.85  ? 321 LYS A CE  1 
ATOM   2168 N  NZ  . LYS A 1 321 ? 9.866  23.232 14.120  1.00 91.24  ? 321 LYS A NZ  1 
ATOM   2169 N  N   . ALA A 1 322 ? 7.495  28.039 17.137  1.00 81.66  ? 322 ALA A N   1 
ATOM   2170 C  CA  . ALA A 1 322 ? 6.255  27.607 17.770  1.00 82.29  ? 322 ALA A CA  1 
ATOM   2171 C  C   . ALA A 1 322 ? 5.058  28.310 17.151  1.00 82.90  ? 322 ALA A C   1 
ATOM   2172 O  O   . ALA A 1 322 ? 4.067  27.656 16.860  1.00 83.38  ? 322 ALA A O   1 
ATOM   2173 C  CB  . ALA A 1 322 ? 6.307  27.875 19.267  1.00 82.47  ? 322 ALA A CB  1 
ATOM   2174 N  N   . LYS A 1 323 ? 5.185  29.621 16.879  1.00 83.02  ? 323 LYS A N   1 
ATOM   2175 C  CA  . LYS A 1 323 ? 4.134  30.449 16.277  1.00 83.50  ? 323 LYS A CA  1 
ATOM   2176 C  C   . LYS A 1 323 ? 3.863  30.104 14.812  1.00 84.36  ? 323 LYS A C   1 
ATOM   2177 O  O   . LYS A 1 323 ? 2.706  30.098 14.396  1.00 84.88  ? 323 LYS A O   1 
ATOM   2178 C  CB  . LYS A 1 323 ? 4.463  31.938 16.440  1.00 84.69  ? 323 LYS A CB  1 
ATOM   2179 C  CG  . LYS A 1 323 ? 3.229  32.819 16.574  1.00 87.98  ? 323 LYS A CG  1 
ATOM   2180 C  CD  . LYS A 1 323 ? 3.542  34.186 17.157  1.00 90.82  ? 323 LYS A CD  1 
ATOM   2181 C  CE  . LYS A 1 323 ? 2.362  35.119 17.076  1.00 93.91  ? 323 LYS A CE  1 
ATOM   2182 N  NZ  . LYS A 1 323 ? 1.926  35.333 15.672  1.00 96.10  ? 323 LYS A NZ  1 
ATOM   2183 N  N   . LEU A 1 324 ? 4.914  29.818 14.028  1.00 84.40  ? 324 LEU A N   1 
ATOM   2184 C  CA  . LEU A 1 324 ? 4.752  29.425 12.630  1.00 84.72  ? 324 LEU A CA  1 
ATOM   2185 C  C   . LEU A 1 324 ? 4.220  27.994 12.549  1.00 85.97  ? 324 LEU A C   1 
ATOM   2186 O  O   . LEU A 1 324 ? 3.418  27.699 11.670  1.00 86.40  ? 324 LEU A O   1 
ATOM   2187 C  CB  . LEU A 1 324 ? 6.074  29.508 11.848  1.00 84.13  ? 324 LEU A CB  1 
ATOM   2188 C  CG  . LEU A 1 324 ? 6.660  30.877 11.581  1.00 84.39  ? 324 LEU A CG  1 
ATOM   2189 C  CD1 . LEU A 1 324 ? 7.936  30.749 10.800  1.00 84.91  ? 324 LEU A CD1 1 
ATOM   2190 C  CD2 . LEU A 1 324 ? 5.712  31.734 10.797  1.00 84.42  ? 324 LEU A CD2 1 
ATOM   2191 N  N   . ASP A 1 325 ? 4.674  27.100 13.439  1.00 86.46  ? 325 ASP A N   1 
ATOM   2192 C  CA  . ASP A 1 325 ? 4.229  25.707 13.454  1.00 87.19  ? 325 ASP A CA  1 
ATOM   2193 C  C   . ASP A 1 325 ? 2.751  25.645 13.810  1.00 87.33  ? 325 ASP A C   1 
ATOM   2194 O  O   . ASP A 1 325 ? 1.996  24.935 13.151  1.00 87.43  ? 325 ASP A O   1 
ATOM   2195 C  CB  . ASP A 1 325 ? 5.056  24.866 14.441  1.00 89.70  ? 325 ASP A CB  1 
ATOM   2196 C  CG  . ASP A 1 325 ? 6.444  24.470 13.946  1.00 95.43  ? 325 ASP A CG  1 
ATOM   2197 O  OD1 . ASP A 1 325 ? 6.769  24.767 12.765  1.00 96.44  ? 325 ASP A OD1 1 
ATOM   2198 O  OD2 . ASP A 1 325 ? 7.207  23.867 14.737  1.00 97.55  ? 325 ASP A OD2 1 
ATOM   2199 N  N   . SER A 1 326 ? 2.322  26.425 14.815  1.00 87.34  ? 326 SER A N   1 
ATOM   2200 C  CA  . SER A 1 326 ? 0.914  26.484 15.220  1.00 87.72  ? 326 SER A CA  1 
ATOM   2201 C  C   . SER A 1 326 ? 0.013  27.013 14.106  1.00 87.88  ? 326 SER A C   1 
ATOM   2202 O  O   . SER A 1 326 ? -1.143 26.613 14.024  1.00 88.35  ? 326 SER A O   1 
ATOM   2203 C  CB  . SER A 1 326 ? 0.738  27.337 16.471  1.00 89.17  ? 326 SER A CB  1 
ATOM   2204 O  OG  . SER A 1 326 ? 1.320  26.698 17.595  1.00 91.95  ? 326 SER A OG  1 
ATOM   2205 N  N   . ALA A 1 327 ? 0.540  27.891 13.246  1.00 87.33  ? 327 ALA A N   1 
ATOM   2206 C  CA  . ALA A 1 327 ? -0.187 28.446 12.110  1.00 87.23  ? 327 ALA A CA  1 
ATOM   2207 C  C   . ALA A 1 327 ? -0.083 27.612 10.825  1.00 86.78  ? 327 ALA A C   1 
ATOM   2208 O  O   . ALA A 1 327 ? -0.694 27.975 9.832   1.00 87.20  ? 327 ALA A O   1 
ATOM   2209 C  CB  . ALA A 1 327 ? 0.296  29.855 11.837  1.00 87.60  ? 327 ALA A CB  1 
ATOM   2210 N  N   . GLY A 1 328 ? 0.702  26.544 10.831  1.00 86.11  ? 328 GLY A N   1 
ATOM   2211 C  CA  . GLY A 1 328 ? 0.882  25.698 9.660   1.00 86.13  ? 328 GLY A CA  1 
ATOM   2212 C  C   . GLY A 1 328 ? 1.696  26.344 8.556   1.00 86.11  ? 328 GLY A C   1 
ATOM   2213 O  O   . GLY A 1 328 ? 1.453  26.088 7.374   1.00 86.26  ? 328 GLY A O   1 
ATOM   2214 N  N   . ILE A 1 329 ? 2.657  27.209 8.929   1.00 85.75  ? 329 ILE A N   1 
ATOM   2215 C  CA  . ILE A 1 329 ? 3.523  27.904 7.974   1.00 85.68  ? 329 ILE A CA  1 
ATOM   2216 C  C   . ILE A 1 329 ? 4.884  27.234 7.986   1.00 86.16  ? 329 ILE A C   1 
ATOM   2217 O  O   . ILE A 1 329 ? 5.586  27.273 8.998   1.00 86.54  ? 329 ILE A O   1 
ATOM   2218 C  CB  . ILE A 1 329 ? 3.629  29.418 8.295   1.00 85.53  ? 329 ILE A CB  1 
ATOM   2219 C  CG1 . ILE A 1 329 ? 2.255  30.092 8.231   1.00 85.81  ? 329 ILE A CG1 1 
ATOM   2220 C  CG2 . ILE A 1 329 ? 4.631  30.108 7.361   1.00 85.89  ? 329 ILE A CG2 1 
ATOM   2221 C  CD1 . ILE A 1 329 ? 2.240  31.516 8.652   1.00 86.64  ? 329 ILE A CD1 1 
ATOM   2222 N  N   . PRO A 1 330 ? 5.268  26.578 6.878   1.00 85.92  ? 330 PRO A N   1 
ATOM   2223 C  CA  . PRO A 1 330 ? 6.546  25.862 6.867   1.00 85.81  ? 330 PRO A CA  1 
ATOM   2224 C  C   . PRO A 1 330 ? 7.781  26.712 6.571   1.00 85.83  ? 330 PRO A C   1 
ATOM   2225 O  O   . PRO A 1 330 ? 7.742  27.650 5.768   1.00 86.20  ? 330 PRO A O   1 
ATOM   2226 C  CB  . PRO A 1 330 ? 6.332  24.801 5.790   1.00 86.16  ? 330 PRO A CB  1 
ATOM   2227 C  CG  . PRO A 1 330 ? 5.418  25.451 4.832   1.00 86.50  ? 330 PRO A CG  1 
ATOM   2228 C  CD  . PRO A 1 330 ? 4.533  26.391 5.613   1.00 85.26  ? 330 PRO A CD  1 
ATOM   2229 N  N   . ALA A 1 331 ? 8.891  26.332 7.202   1.00 85.00  ? 331 ALA A N   1 
ATOM   2230 C  CA  . ALA A 1 331 ? 10.186 26.956 7.021   1.00 84.68  ? 331 ALA A CA  1 
ATOM   2231 C  C   . ALA A 1 331 ? 11.267 25.887 7.082   1.00 84.35  ? 331 ALA A C   1 
ATOM   2232 O  O   . ALA A 1 331 ? 11.063 24.819 7.662   1.00 84.61  ? 331 ALA A O   1 
ATOM   2233 C  CB  . ALA A 1 331 ? 10.427 27.986 8.117   1.00 84.76  ? 331 ALA A CB  1 
ATOM   2234 N  N   . ASP A 1 332 ? 12.417 26.170 6.480   1.00 83.57  ? 332 ASP A N   1 
ATOM   2235 C  CA  . ASP A 1 332 ? 13.575 25.306 6.582   1.00 83.37  ? 332 ASP A CA  1 
ATOM   2236 C  C   . ASP A 1 332 ? 14.306 25.800 7.834   1.00 82.06  ? 332 ASP A C   1 
ATOM   2237 O  O   . ASP A 1 332 ? 14.625 26.980 7.938   1.00 81.90  ? 332 ASP A O   1 
ATOM   2238 C  CB  . ASP A 1 332 ? 14.470 25.433 5.340   1.00 86.12  ? 332 ASP A CB  1 
ATOM   2239 C  CG  . ASP A 1 332 ? 13.845 24.850 4.088   1.00 92.58  ? 332 ASP A CG  1 
ATOM   2240 O  OD1 . ASP A 1 332 ? 13.148 23.818 4.197   1.00 93.73  ? 332 ASP A OD1 1 
ATOM   2241 O  OD2 . ASP A 1 332 ? 14.056 25.424 3.001   1.00 95.36  ? 332 ASP A OD2 1 
ATOM   2242 N  N   . TRP A 1 333 ? 14.522 24.911 8.804   1.00 81.02  ? 333 TRP A N   1 
ATOM   2243 C  CA  . TRP A 1 333 ? 15.153 25.258 10.074  1.00 80.32  ? 333 TRP A CA  1 
ATOM   2244 C  C   . TRP A 1 333 ? 16.569 24.755 10.202  1.00 79.37  ? 333 TRP A C   1 
ATOM   2245 O  O   . TRP A 1 333 ? 16.803 23.548 10.075  1.00 80.02  ? 333 TRP A O   1 
ATOM   2246 C  CB  . TRP A 1 333 ? 14.322 24.698 11.225  1.00 80.07  ? 333 TRP A CB  1 
ATOM   2247 C  CG  . TRP A 1 333 ? 12.946 25.270 11.238  1.00 80.33  ? 333 TRP A CG  1 
ATOM   2248 C  CD1 . TRP A 1 333 ? 11.818 24.732 10.690  1.00 81.26  ? 333 TRP A CD1 1 
ATOM   2249 C  CD2 . TRP A 1 333 ? 12.574 26.541 11.760  1.00 80.06  ? 333 TRP A CD2 1 
ATOM   2250 N  NE1 . TRP A 1 333 ? 10.756 25.589 10.862  1.00 81.45  ? 333 TRP A NE1 1 
ATOM   2251 C  CE2 . TRP A 1 333 ? 11.194 26.706 11.522  1.00 80.92  ? 333 TRP A CE2 1 
ATOM   2252 C  CE3 . TRP A 1 333 ? 13.269 27.547 12.439  1.00 80.07  ? 333 TRP A CE3 1 
ATOM   2253 C  CZ2 . TRP A 1 333 ? 10.504 27.836 11.933  1.00 81.31  ? 333 TRP A CZ2 1 
ATOM   2254 C  CZ3 . TRP A 1 333 ? 12.570 28.644 12.880  1.00 80.67  ? 333 TRP A CZ3 1 
ATOM   2255 C  CH2 . TRP A 1 333 ? 11.222 28.811 12.572  1.00 81.06  ? 333 TRP A CH2 1 
ATOM   2256 N  N   . ASN A 1 334 ? 17.515 25.665 10.483  1.00 77.46  ? 334 ASN A N   1 
ATOM   2257 C  CA  . ASN A 1 334 ? 18.894 25.252 10.660  1.00 76.02  ? 334 ASN A CA  1 
ATOM   2258 C  C   . ASN A 1 334 ? 19.329 25.685 12.018  1.00 74.96  ? 334 ASN A C   1 
ATOM   2259 O  O   . ASN A 1 334 ? 20.088 26.630 12.171  1.00 74.62  ? 334 ASN A O   1 
ATOM   2260 C  CB  . ASN A 1 334 ? 19.795 25.785 9.566   1.00 76.42  ? 334 ASN A CB  1 
ATOM   2261 C  CG  . ASN A 1 334 ? 20.999 24.916 9.288   1.00 78.94  ? 334 ASN A CG  1 
ATOM   2262 O  OD1 . ASN A 1 334 ? 21.251 23.914 9.965   1.00 79.60  ? 334 ASN A OD1 1 
ATOM   2263 N  ND2 . ASN A 1 334 ? 21.781 25.286 8.277   1.00 79.59  ? 334 ASN A ND2 1 
ATOM   2264 N  N   . LEU A 1 335 ? 18.780 25.027 13.018  1.00 74.23  ? 335 LEU A N   1 
ATOM   2265 C  CA  . LEU A 1 335 ? 19.087 25.297 14.409  1.00 73.54  ? 335 LEU A CA  1 
ATOM   2266 C  C   . LEU A 1 335 ? 20.374 24.536 14.677  1.00 73.06  ? 335 LEU A C   1 
ATOM   2267 O  O   . LEU A 1 335 ? 20.439 23.331 14.467  1.00 72.89  ? 335 LEU A O   1 
ATOM   2268 C  CB  . LEU A 1 335 ? 17.928 24.800 15.283  1.00 73.00  ? 335 LEU A CB  1 
ATOM   2269 C  CG  . LEU A 1 335 ? 16.553 25.359 14.926  1.00 73.52  ? 335 LEU A CG  1 
ATOM   2270 C  CD1 . LEU A 1 335 ? 15.480 24.749 15.785  1.00 73.73  ? 335 LEU A CD1 1 
ATOM   2271 C  CD2 . LEU A 1 335 ? 16.519 26.862 15.066  1.00 73.82  ? 335 LEU A CD2 1 
ATOM   2272 N  N   . ARG A 1 336 ? 21.423 25.259 15.048  1.00 72.65  ? 336 ARG A N   1 
ATOM   2273 C  CA  . ARG A 1 336 ? 22.762 24.708 15.194  1.00 72.00  ? 336 ARG A CA  1 
ATOM   2274 C  C   . ARG A 1 336 ? 23.332 24.825 16.593  1.00 71.72  ? 336 ARG A C   1 
ATOM   2275 O  O   . ARG A 1 336 ? 22.897 25.678 17.363  1.00 72.26  ? 336 ARG A O   1 
ATOM   2276 C  CB  . ARG A 1 336 ? 23.678 25.372 14.150  1.00 72.15  ? 336 ARG A CB  1 
ATOM   2277 C  CG  . ARG A 1 336 ? 23.554 24.668 12.806  1.00 73.53  ? 336 ARG A CG  1 
ATOM   2278 C  CD  . ARG A 1 336 ? 24.109 25.436 11.628  1.00 74.94  ? 336 ARG A CD  1 
ATOM   2279 N  NE  . ARG A 1 336 ? 23.870 26.873 11.735  1.00 75.60  ? 336 ARG A NE  1 
ATOM   2280 C  CZ  . ARG A 1 336 ? 24.000 27.734 10.736  1.00 76.99  ? 336 ARG A CZ  1 
ATOM   2281 N  NH1 . ARG A 1 336 ? 24.303 27.308 9.518   1.00 76.16  ? 336 ARG A NH1 1 
ATOM   2282 N  NH2 . ARG A 1 336 ? 23.810 29.024 10.942  1.00 77.88  ? 336 ARG A NH2 1 
ATOM   2283 N  N   . PRO A 1 337 ? 24.301 23.962 16.956  1.00 70.93  ? 337 PRO A N   1 
ATOM   2284 C  CA  . PRO A 1 337 ? 24.872 24.043 18.302  1.00 70.66  ? 337 PRO A CA  1 
ATOM   2285 C  C   . PRO A 1 337 ? 25.859 25.207 18.451  1.00 71.27  ? 337 PRO A C   1 
ATOM   2286 O  O   . PRO A 1 337 ? 26.126 25.929 17.479  1.00 71.57  ? 337 PRO A O   1 
ATOM   2287 C  CB  . PRO A 1 337 ? 25.547 22.673 18.457  1.00 70.80  ? 337 PRO A CB  1 
ATOM   2288 C  CG  . PRO A 1 337 ? 25.979 22.334 17.094  1.00 71.07  ? 337 PRO A CG  1 
ATOM   2289 C  CD  . PRO A 1 337 ? 24.931 22.876 16.170  1.00 70.05  ? 337 PRO A CD  1 
ATOM   2290 N  N   . THR A 1 338 ? 26.426 25.390 19.666  1.00 71.10  ? 338 THR A N   1 
ATOM   2291 C  CA  . THR A 1 338 ? 27.418 26.440 19.871  1.00 71.16  ? 338 THR A CA  1 
ATOM   2292 C  C   . THR A 1 338 ? 28.671 26.096 19.083  1.00 71.57  ? 338 THR A C   1 
ATOM   2293 O  O   . THR A 1 338 ? 29.250 25.022 19.258  1.00 72.02  ? 338 THR A O   1 
ATOM   2294 C  CB  . THR A 1 338 ? 27.772 26.588 21.349  1.00 71.99  ? 338 THR A CB  1 
ATOM   2295 O  OG1 . THR A 1 338 ? 26.576 26.708 22.116  1.00 73.19  ? 338 THR A OG1 1 
ATOM   2296 C  CG2 . THR A 1 338 ? 28.696 27.770 21.617  1.00 71.92  ? 338 THR A CG2 1 
ATOM   2297 N  N   . GLY A 1 339 ? 29.011 26.971 18.157  1.00 71.05  ? 339 GLY A N   1 
ATOM   2298 C  CA  . GLY A 1 339 ? 30.220 26.881 17.356  1.00 70.61  ? 339 GLY A CA  1 
ATOM   2299 C  C   . GLY A 1 339 ? 31.288 27.786 17.936  1.00 70.10  ? 339 GLY A C   1 
ATOM   2300 O  O   . GLY A 1 339 ? 31.043 28.566 18.868  1.00 69.98  ? 339 GLY A O   1 
ATOM   2301 N  N   . THR A 1 340 ? 32.494 27.673 17.407  1.00 69.57  ? 340 THR A N   1 
ATOM   2302 C  CA  . THR A 1 340 ? 33.618 28.461 17.888  1.00 69.36  ? 340 THR A CA  1 
ATOM   2303 C  C   . THR A 1 340 ? 33.454 29.936 17.493  1.00 69.30  ? 340 THR A C   1 
ATOM   2304 O  O   . THR A 1 340 ? 33.697 30.832 18.310  1.00 69.56  ? 340 THR A O   1 
ATOM   2305 C  CB  . THR A 1 340 ? 34.937 27.801 17.453  1.00 70.31  ? 340 THR A CB  1 
ATOM   2306 O  OG1 . THR A 1 340 ? 36.008 28.649 17.828  1.00 72.20  ? 340 THR A OG1 1 
ATOM   2307 C  CG2 . THR A 1 340 ? 34.992 27.463 15.961  1.00 69.75  ? 340 THR A CG2 1 
ATOM   2308 N  N   . HIS A 1 341 ? 32.973 30.178 16.263  1.00 68.86  ? 341 HIS A N   1 
ATOM   2309 C  CA  . HIS A 1 341 ? 32.751 31.516 15.733  1.00 68.95  ? 341 HIS A CA  1 
ATOM   2310 C  C   . HIS A 1 341 ? 31.406 31.608 15.067  1.00 68.88  ? 341 HIS A C   1 
ATOM   2311 O  O   . HIS A 1 341 ? 31.009 30.688 14.362  1.00 69.29  ? 341 HIS A O   1 
ATOM   2312 C  CB  . HIS A 1 341 ? 33.825 31.864 14.681  1.00 69.77  ? 341 HIS A CB  1 
ATOM   2313 C  CG  . HIS A 1 341 ? 35.181 32.100 15.257  1.00 71.33  ? 341 HIS A CG  1 
ATOM   2314 N  ND1 . HIS A 1 341 ? 35.998 31.050 15.622  1.00 73.39  ? 341 HIS A ND1 1 
ATOM   2315 C  CD2 . HIS A 1 341 ? 35.806 33.264 15.544  1.00 72.09  ? 341 HIS A CD2 1 
ATOM   2316 C  CE1 . HIS A 1 341 ? 37.091 31.605 16.121  1.00 73.86  ? 341 HIS A CE1 1 
ATOM   2317 N  NE2 . HIS A 1 341 ? 37.026 32.937 16.079  1.00 73.38  ? 341 HIS A NE2 1 
ATOM   2318 N  N   . SER A 1 342 ? 30.743 32.751 15.212  1.00 68.59  ? 342 SER A N   1 
ATOM   2319 C  CA  . SER A 1 342 ? 29.478 33.012 14.557  1.00 68.70  ? 342 SER A CA  1 
ATOM   2320 C  C   . SER A 1 342 ? 29.638 33.154 13.048  1.00 69.25  ? 342 SER A C   1 
ATOM   2321 O  O   . SER A 1 342 ? 28.789 32.664 12.327  1.00 69.35  ? 342 SER A O   1 
ATOM   2322 C  CB  . SER A 1 342 ? 28.822 34.252 15.142  1.00 69.35  ? 342 SER A CB  1 
ATOM   2323 O  OG  . SER A 1 342 ? 28.249 33.976 16.408  1.00 70.80  ? 342 SER A OG  1 
ATOM   2324 N  N   . TRP A 1 343 ? 30.738 33.745 12.561  1.00 69.61  ? 343 TRP A N   1 
ATOM   2325 C  CA  . TRP A 1 343 ? 30.967 33.894 11.113  1.00 69.46  ? 343 TRP A CA  1 
ATOM   2326 C  C   . TRP A 1 343 ? 31.143 32.586 10.367  1.00 70.14  ? 343 TRP A C   1 
ATOM   2327 O  O   . TRP A 1 343 ? 30.878 32.533 9.163   1.00 71.07  ? 343 TRP A O   1 
ATOM   2328 C  CB  . TRP A 1 343 ? 32.134 34.835 10.813  1.00 68.70  ? 343 TRP A CB  1 
ATOM   2329 C  CG  . TRP A 1 343 ? 31.729 36.262 10.874  1.00 68.31  ? 343 TRP A CG  1 
ATOM   2330 C  CD1 . TRP A 1 343 ? 32.007 37.153 11.865  1.00 68.99  ? 343 TRP A CD1 1 
ATOM   2331 C  CD2 . TRP A 1 343 ? 30.902 36.953 9.931   1.00 67.82  ? 343 TRP A CD2 1 
ATOM   2332 N  NE1 . TRP A 1 343 ? 31.434 38.371 11.576  1.00 68.85  ? 343 TRP A NE1 1 
ATOM   2333 C  CE2 . TRP A 1 343 ? 30.712 38.258 10.421  1.00 68.27  ? 343 TRP A CE2 1 
ATOM   2334 C  CE3 . TRP A 1 343 ? 30.293 36.586 8.721   1.00 67.96  ? 343 TRP A CE3 1 
ATOM   2335 C  CZ2 . TRP A 1 343 ? 29.937 39.189 9.753   1.00 68.96  ? 343 TRP A CZ2 1 
ATOM   2336 C  CZ3 . TRP A 1 343 ? 29.511 37.506 8.071   1.00 68.38  ? 343 TRP A CZ3 1 
ATOM   2337 C  CH2 . TRP A 1 343 ? 29.380 38.804 8.559   1.00 68.89  ? 343 TRP A CH2 1 
ATOM   2338 N  N   . GLY A 1 344 ? 31.569 31.543 11.067  1.00 69.70  ? 344 GLY A N   1 
ATOM   2339 C  CA  . GLY A 1 344 ? 31.688 30.217 10.477  1.00 69.92  ? 344 GLY A CA  1 
ATOM   2340 C  C   . GLY A 1 344 ? 30.312 29.668 10.153  1.00 70.39  ? 344 GLY A C   1 
ATOM   2341 O  O   . GLY A 1 344 ? 30.093 29.076 9.092   1.00 70.91  ? 344 GLY A O   1 
ATOM   2342 N  N   . TRP A 1 345 ? 29.358 29.917 11.054  1.00 70.24  ? 345 TRP A N   1 
ATOM   2343 C  CA  . TRP A 1 345 ? 27.978 29.525 10.873  1.00 70.14  ? 345 TRP A CA  1 
ATOM   2344 C  C   . TRP A 1 345 ? 27.327 30.370 9.805   1.00 71.03  ? 345 TRP A C   1 
ATOM   2345 O  O   . TRP A 1 345 ? 26.562 29.838 9.032   1.00 72.06  ? 345 TRP A O   1 
ATOM   2346 C  CB  . TRP A 1 345 ? 27.178 29.652 12.176  1.00 69.36  ? 345 TRP A CB  1 
ATOM   2347 C  CG  . TRP A 1 345 ? 27.428 28.627 13.257  1.00 68.84  ? 345 TRP A CG  1 
ATOM   2348 C  CD1 . TRP A 1 345 ? 27.422 28.865 14.592  1.00 69.34  ? 345 TRP A CD1 1 
ATOM   2349 C  CD2 . TRP A 1 345 ? 27.559 27.196 13.109  1.00 68.78  ? 345 TRP A CD2 1 
ATOM   2350 N  NE1 . TRP A 1 345 ? 27.574 27.692 15.289  1.00 69.63  ? 345 TRP A NE1 1 
ATOM   2351 C  CE2 . TRP A 1 345 ? 27.673 26.653 14.405  1.00 69.33  ? 345 TRP A CE2 1 
ATOM   2352 C  CE3 . TRP A 1 345 ? 27.634 26.326 12.008  1.00 69.18  ? 345 TRP A CE3 1 
ATOM   2353 C  CZ2 . TRP A 1 345 ? 27.875 25.288 14.633  1.00 69.58  ? 345 TRP A CZ2 1 
ATOM   2354 C  CZ3 . TRP A 1 345 ? 27.831 24.976 12.240  1.00 69.85  ? 345 TRP A CZ3 1 
ATOM   2355 C  CH2 . TRP A 1 345 ? 27.931 24.470 13.541  1.00 69.75  ? 345 TRP A CH2 1 
ATOM   2356 N  N   . TRP A 1 346 ? 27.597 31.669 9.758   1.00 70.87  ? 346 TRP A N   1 
ATOM   2357 C  CA  . TRP A 1 346 ? 27.005 32.552 8.758   1.00 71.39  ? 346 TRP A CA  1 
ATOM   2358 C  C   . TRP A 1 346 ? 27.450 32.208 7.362   1.00 73.81  ? 346 TRP A C   1 
ATOM   2359 O  O   . TRP A 1 346 ? 26.627 32.270 6.450   1.00 74.68  ? 346 TRP A O   1 
ATOM   2360 C  CB  . TRP A 1 346 ? 27.219 34.040 9.091   1.00 70.11  ? 346 TRP A CB  1 
ATOM   2361 C  CG  . TRP A 1 346 ? 26.303 34.503 10.185  1.00 69.26  ? 346 TRP A CG  1 
ATOM   2362 C  CD1 . TRP A 1 346 ? 24.981 34.190 10.332  1.00 69.75  ? 346 TRP A CD1 1 
ATOM   2363 C  CD2 . TRP A 1 346 ? 26.639 35.349 11.291  1.00 68.96  ? 346 TRP A CD2 1 
ATOM   2364 N  NE1 . TRP A 1 346 ? 24.478 34.779 11.469  1.00 69.91  ? 346 TRP A NE1 1 
ATOM   2365 C  CE2 . TRP A 1 346 ? 25.476 35.494 12.079  1.00 69.52  ? 346 TRP A CE2 1 
ATOM   2366 C  CE3 . TRP A 1 346 ? 27.821 35.966 11.721  1.00 69.12  ? 346 TRP A CE3 1 
ATOM   2367 C  CZ2 . TRP A 1 346 ? 25.463 36.250 13.254  1.00 69.47  ? 346 TRP A CZ2 1 
ATOM   2368 C  CZ3 . TRP A 1 346 ? 27.787 36.755 12.854  1.00 69.32  ? 346 TRP A CZ3 1 
ATOM   2369 C  CH2 . TRP A 1 346 ? 26.626 36.874 13.615  1.00 69.26  ? 346 TRP A CH2 1 
ATOM   2370 N  N   . GLN A 1 347 ? 28.705 31.774 7.181   1.00 74.76  ? 347 GLN A N   1 
ATOM   2371 C  CA  . GLN A 1 347 ? 29.154 31.337 5.851   1.00 75.92  ? 347 GLN A CA  1 
ATOM   2372 C  C   . GLN A 1 347 ? 28.408 30.058 5.430   1.00 76.98  ? 347 GLN A C   1 
ATOM   2373 O  O   . GLN A 1 347 ? 28.024 29.907 4.276   1.00 77.37  ? 347 GLN A O   1 
ATOM   2374 C  CB  . GLN A 1 347 ? 30.659 31.090 5.838   1.00 77.36  ? 347 GLN A CB  1 
ATOM   2375 C  CG  . GLN A 1 347 ? 31.136 30.757 4.445   1.00 80.38  ? 347 GLN A CG  1 
ATOM   2376 C  CD  . GLN A 1 347 ? 32.616 30.711 4.311   1.00 83.17  ? 347 GLN A CD  1 
ATOM   2377 O  OE1 . GLN A 1 347 ? 33.258 31.741 4.180   1.00 85.24  ? 347 GLN A OE1 1 
ATOM   2378 N  NE2 . GLN A 1 347 ? 33.176 29.513 4.289   1.00 82.63  ? 347 GLN A NE2 1 
ATOM   2379 N  N   . ASP A 1 348 ? 28.197 29.152 6.391   1.00 77.56  ? 348 ASP A N   1 
ATOM   2380 C  CA  . ASP A 1 348 ? 27.462 27.898 6.252   1.00 78.16  ? 348 ASP A CA  1 
ATOM   2381 C  C   . ASP A 1 348 ? 25.972 28.180 5.944   1.00 77.67  ? 348 ASP A C   1 
ATOM   2382 O  O   . ASP A 1 348 ? 25.345 27.386 5.257   1.00 77.59  ? 348 ASP A O   1 
ATOM   2383 C  CB  . ASP A 1 348 ? 27.652 27.071 7.544   1.00 81.07  ? 348 ASP A CB  1 
ATOM   2384 C  CG  . ASP A 1 348 ? 27.055 25.677 7.565   1.00 89.11  ? 348 ASP A CG  1 
ATOM   2385 O  OD1 . ASP A 1 348 ? 27.265 24.927 6.587   1.00 91.24  ? 348 ASP A OD1 1 
ATOM   2386 O  OD2 . ASP A 1 348 ? 26.394 25.324 8.579   1.00 91.76  ? 348 ASP A OD2 1 
ATOM   2387 N  N   . ASP A 1 349 ? 25.423 29.324 6.418   1.00 77.58  ? 349 ASP A N   1 
ATOM   2388 C  CA  . ASP A 1 349 ? 24.046 29.795 6.171   1.00 77.89  ? 349 ASP A CA  1 
ATOM   2389 C  C   . ASP A 1 349 ? 23.827 30.125 4.707   1.00 78.72  ? 349 ASP A C   1 
ATOM   2390 O  O   . ASP A 1 349 ? 22.704 30.014 4.226   1.00 79.25  ? 349 ASP A O   1 
ATOM   2391 C  CB  . ASP A 1 349 ? 23.709 31.037 7.018   1.00 78.72  ? 349 ASP A CB  1 
ATOM   2392 C  CG  . ASP A 1 349 ? 23.085 30.721 8.353   1.00 81.89  ? 349 ASP A CG  1 
ATOM   2393 O  OD1 . ASP A 1 349 ? 22.580 29.588 8.520   1.00 83.11  ? 349 ASP A OD1 1 
ATOM   2394 O  OD2 . ASP A 1 349 ? 23.073 31.615 9.231   1.00 82.47  ? 349 ASP A OD2 1 
ATOM   2395 N  N   . LEU A 1 350 ? 24.877 30.548 3.993   1.00 78.60  ? 350 LEU A N   1 
ATOM   2396 C  CA  . LEU A 1 350 ? 24.767 30.777 2.561   1.00 78.87  ? 350 LEU A CA  1 
ATOM   2397 C  C   . LEU A 1 350 ? 24.504 29.436 1.854   1.00 80.33  ? 350 LEU A C   1 
ATOM   2398 O  O   . LEU A 1 350 ? 23.712 29.382 0.917   1.00 81.06  ? 350 LEU A O   1 
ATOM   2399 C  CB  . LEU A 1 350 ? 26.030 31.440 2.013   1.00 78.23  ? 350 LEU A CB  1 
ATOM   2400 C  CG  . LEU A 1 350 ? 26.379 32.797 2.592   1.00 78.88  ? 350 LEU A CG  1 
ATOM   2401 C  CD1 . LEU A 1 350 ? 27.607 33.338 1.940   1.00 79.26  ? 350 LEU A CD1 1 
ATOM   2402 C  CD2 . LEU A 1 350 ? 25.242 33.791 2.422   1.00 79.38  ? 350 LEU A CD2 1 
ATOM   2403 N  N   . ARG A 1 351 ? 25.123 28.352 2.334   1.00 80.58  ? 351 ARG A N   1 
ATOM   2404 C  CA  . ARG A 1 351 ? 24.908 27.014 1.801   1.00 80.95  ? 351 ARG A CA  1 
ATOM   2405 C  C   . ARG A 1 351 ? 23.518 26.514 2.190   1.00 81.99  ? 351 ARG A C   1 
ATOM   2406 O  O   . ARG A 1 351 ? 22.772 26.075 1.314   1.00 82.44  ? 351 ARG A O   1 
ATOM   2407 C  CB  . ARG A 1 351 ? 25.976 26.030 2.316   1.00 80.97  ? 351 ARG A CB  1 
ATOM   2408 C  CG  . ARG A 1 351 ? 27.252 26.046 1.521   1.00 82.28  ? 351 ARG A CG  1 
ATOM   2409 C  CD  . ARG A 1 351 ? 28.084 27.270 1.832   1.00 84.18  ? 351 ARG A CD  1 
ATOM   2410 N  NE  . ARG A 1 351 ? 29.396 27.176 1.204   1.00 85.57  ? 351 ARG A NE  1 
ATOM   2411 C  CZ  . ARG A 1 351 ? 30.253 28.180 1.096   1.00 86.94  ? 351 ARG A CZ  1 
ATOM   2412 N  NH1 . ARG A 1 351 ? 29.941 29.382 1.566   1.00 85.65  ? 351 ARG A NH1 1 
ATOM   2413 N  NH2 . ARG A 1 351 ? 31.422 27.998 0.500   1.00 87.16  ? 351 ARG A NH2 1 
ATOM   2414 N  N   . GLY A 1 352 ? 23.191 26.577 3.487   1.00 82.00  ? 352 GLY A N   1 
ATOM   2415 C  CA  . GLY A 1 352 ? 21.913 26.120 4.018   1.00 82.61  ? 352 GLY A CA  1 
ATOM   2416 C  C   . GLY A 1 352 ? 20.718 26.779 3.359   1.00 83.19  ? 352 GLY A C   1 
ATOM   2417 O  O   . GLY A 1 352 ? 19.765 26.101 2.975   1.00 83.27  ? 352 GLY A O   1 
ATOM   2418 N  N   . SER A 1 353 ? 20.767 28.106 3.203   1.00 83.52  ? 353 SER A N   1 
ATOM   2419 C  CA  . SER A 1 353 ? 19.687 28.848 2.563   1.00 84.41  ? 353 SER A CA  1 
ATOM   2420 C  C   . SER A 1 353 ? 19.582 28.592 1.074   1.00 85.54  ? 353 SER A C   1 
ATOM   2421 O  O   . SER A 1 353 ? 18.558 28.940 0.500   1.00 85.90  ? 353 SER A O   1 
ATOM   2422 C  CB  . SER A 1 353 ? 19.818 30.346 2.816   1.00 85.28  ? 353 SER A CB  1 
ATOM   2423 O  OG  . SER A 1 353 ? 20.948 30.877 2.145   1.00 86.95  ? 353 SER A OG  1 
ATOM   2424 N  N   . TRP A 1 354 ? 20.601 27.983 0.439   1.00 86.17  ? 354 TRP A N   1 
ATOM   2425 C  CA  . TRP A 1 354 ? 20.515 27.692 -0.980  1.00 87.16  ? 354 TRP A CA  1 
ATOM   2426 C  C   . TRP A 1 354 ? 19.442 26.685 -1.303  1.00 87.65  ? 354 TRP A C   1 
ATOM   2427 O  O   . TRP A 1 354 ? 18.831 26.793 -2.354  1.00 88.09  ? 354 TRP A O   1 
ATOM   2428 C  CB  . TRP A 1 354 ? 21.848 27.286 -1.608  1.00 87.58  ? 354 TRP A CB  1 
ATOM   2429 C  CG  . TRP A 1 354 ? 21.744 27.218 -3.100  1.00 88.70  ? 354 TRP A CG  1 
ATOM   2430 C  CD1 . TRP A 1 354 ? 21.678 26.094 -3.869  1.00 89.87  ? 354 TRP A CD1 1 
ATOM   2431 C  CD2 . TRP A 1 354 ? 21.507 28.323 -3.983  1.00 88.90  ? 354 TRP A CD2 1 
ATOM   2432 N  NE1 . TRP A 1 354 ? 21.491 26.438 -5.189  1.00 90.30  ? 354 TRP A NE1 1 
ATOM   2433 C  CE2 . TRP A 1 354 ? 21.361 27.800 -5.282  1.00 89.85  ? 354 TRP A CE2 1 
ATOM   2434 C  CE3 . TRP A 1 354 ? 21.402 29.705 -3.797  1.00 89.43  ? 354 TRP A CE3 1 
ATOM   2435 C  CZ2 . TRP A 1 354 ? 21.144 28.613 -6.390  1.00 90.53  ? 354 TRP A CZ2 1 
ATOM   2436 C  CZ3 . TRP A 1 354 ? 21.190 30.508 -4.895  1.00 90.42  ? 354 TRP A CZ3 1 
ATOM   2437 C  CH2 . TRP A 1 354 ? 21.066 29.964 -6.174  1.00 90.62  ? 354 TRP A CH2 1 
ATOM   2438 N  N   . THR A 1 355 ? 19.168 25.737 -0.405  1.00 87.51  ? 355 THR A N   1 
ATOM   2439 C  CA  . THR A 1 355 ? 18.103 24.767 -0.642  1.00 87.70  ? 355 THR A CA  1 
ATOM   2440 C  C   . THR A 1 355 ? 16.739 25.495 -0.682  1.00 87.73  ? 355 THR A C   1 
ATOM   2441 O  O   . THR A 1 355 ? 15.922 25.203 -1.551  1.00 88.04  ? 355 THR A O   1 
ATOM   2442 C  CB  . THR A 1 355 ? 18.199 23.590 0.326   1.00 89.10  ? 355 THR A CB  1 
ATOM   2443 O  OG1 . THR A 1 355 ? 17.771 23.992 1.628   1.00 90.70  ? 355 THR A OG1 1 
ATOM   2444 C  CG2 . THR A 1 355 ? 19.608 23.001 0.385   1.00 89.18  ? 355 THR A CG2 1 
ATOM   2445 N  N   . THR A 1 356 ? 16.544 26.505 0.176   1.00 87.24  ? 356 THR A N   1 
ATOM   2446 C  CA  . THR A 1 356 ? 15.313 27.290 0.179   1.00 87.42  ? 356 THR A CA  1 
ATOM   2447 C  C   . THR A 1 356 ? 15.215 28.114 -1.103  1.00 88.01  ? 356 THR A C   1 
ATOM   2448 O  O   . THR A 1 356 ? 14.167 28.124 -1.741  1.00 88.22  ? 356 THR A O   1 
ATOM   2449 C  CB  . THR A 1 356 ? 15.265 28.204 1.411   1.00 87.98  ? 356 THR A CB  1 
ATOM   2450 O  OG1 . THR A 1 356 ? 15.611 27.448 2.568   1.00 88.21  ? 356 THR A OG1 1 
ATOM   2451 C  CG2 . THR A 1 356 ? 13.907 28.864 1.594   1.00 88.49  ? 356 THR A CG2 1 
ATOM   2452 N  N   . PHE A 1 357 ? 16.313 28.786 -1.490  1.00 88.15  ? 357 PHE A N   1 
ATOM   2453 C  CA  . PHE A 1 357 ? 16.353 29.630 -2.679  1.00 88.75  ? 357 PHE A CA  1 
ATOM   2454 C  C   . PHE A 1 357 ? 16.207 28.851 -3.973  1.00 90.30  ? 357 PHE A C   1 
ATOM   2455 O  O   . PHE A 1 357 ? 15.418 29.253 -4.816  1.00 90.54  ? 357 PHE A O   1 
ATOM   2456 C  CB  . PHE A 1 357 ? 17.602 30.516 -2.696  1.00 88.07  ? 357 PHE A CB  1 
ATOM   2457 C  CG  . PHE A 1 357 ? 17.692 31.529 -1.575  1.00 88.18  ? 357 PHE A CG  1 
ATOM   2458 C  CD1 . PHE A 1 357 ? 16.562 31.922 -0.875  1.00 88.76  ? 357 PHE A CD1 1 
ATOM   2459 C  CD2 . PHE A 1 357 ? 18.899 32.115 -1.245  1.00 88.64  ? 357 PHE A CD2 1 
ATOM   2460 C  CE1 . PHE A 1 357 ? 16.644 32.859 0.147   1.00 89.12  ? 357 PHE A CE1 1 
ATOM   2461 C  CE2 . PHE A 1 357 ? 18.974 33.060 -0.230  1.00 89.19  ? 357 PHE A CE2 1 
ATOM   2462 C  CZ  . PHE A 1 357 ? 17.845 33.427 0.458   1.00 88.82  ? 357 PHE A CZ  1 
ATOM   2463 N  N   . ALA A 1 358 ? 16.907 27.721 -4.126  1.00 91.02  ? 358 ALA A N   1 
ATOM   2464 C  CA  . ALA A 1 358 ? 16.772 26.892 -5.324  1.00 92.47  ? 358 ALA A CA  1 
ATOM   2465 C  C   . ALA A 1 358 ? 15.314 26.397 -5.485  1.00 93.91  ? 358 ALA A C   1 
ATOM   2466 O  O   . ALA A 1 358 ? 14.791 26.381 -6.596  1.00 94.42  ? 358 ALA A O   1 
ATOM   2467 C  CB  . ALA A 1 358 ? 17.729 25.708 -5.262  1.00 92.74  ? 358 ALA A CB  1 
ATOM   2468 N  N   . ARG A 1 359 ? 14.644 26.060 -4.375  1.00 94.44  ? 359 ARG A N   1 
ATOM   2469 C  CA  . ARG A 1 359 ? 13.247 25.623 -4.408  1.00 95.47  ? 359 ARG A CA  1 
ATOM   2470 C  C   . ARG A 1 359 ? 12.294 26.773 -4.746  1.00 97.31  ? 359 ARG A C   1 
ATOM   2471 O  O   . ARG A 1 359 ? 11.413 26.606 -5.589  1.00 97.70  ? 359 ARG A O   1 
ATOM   2472 C  CB  . ARG A 1 359 ? 12.848 24.976 -3.075  1.00 95.80  ? 359 ARG A CB  1 
ATOM   2473 C  CG  . ARG A 1 359 ? 11.430 24.447 -3.052  1.00 96.98  ? 359 ARG A CG  1 
ATOM   2474 C  CD  . ARG A 1 359 ? 11.080 23.865 -1.702  1.00 99.03  ? 359 ARG A CD  1 
ATOM   2475 N  NE  . ARG A 1 359 ? 11.013 24.899 -0.669  1.00 100.88 ? 359 ARG A NE  1 
ATOM   2476 C  CZ  . ARG A 1 359 ? 11.851 24.987 0.361   1.00 102.03 ? 359 ARG A CZ  1 
ATOM   2477 N  NH1 . ARG A 1 359 ? 12.819 24.089 0.520   1.00 100.91 ? 359 ARG A NH1 1 
ATOM   2478 N  NH2 . ARG A 1 359 ? 11.715 25.960 1.254   1.00 101.48 ? 359 ARG A NH2 1 
ATOM   2479 N  N   . ALA A 1 360 ? 12.467 27.940 -4.108  1.00 98.34  ? 360 ALA A N   1 
ATOM   2480 C  CA  . ALA A 1 360 ? 11.604 29.094 -4.365  1.00 99.73  ? 360 ALA A CA  1 
ATOM   2481 C  C   . ALA A 1 360 ? 11.751 29.625 -5.785  1.00 101.51 ? 360 ALA A C   1 
ATOM   2482 O  O   . ALA A 1 360 ? 10.789 30.128 -6.359  1.00 101.60 ? 360 ALA A O   1 
ATOM   2483 C  CB  . ALA A 1 360 ? 11.918 30.205 -3.382  1.00 99.80  ? 360 ALA A CB  1 
ATOM   2484 N  N   . PHE A 1 361 ? 12.965 29.542 -6.336  1.00 102.72 ? 361 PHE A N   1 
ATOM   2485 C  CA  . PHE A 1 361 ? 13.275 30.043 -7.672  1.00 104.15 ? 361 PHE A CA  1 
ATOM   2486 C  C   . PHE A 1 361 ? 13.129 29.012 -8.779  1.00 106.29 ? 361 PHE A C   1 
ATOM   2487 O  O   . PHE A 1 361 ? 13.290 29.371 -9.946  1.00 106.74 ? 361 PHE A O   1 
ATOM   2488 C  CB  . PHE A 1 361 ? 14.702 30.606 -7.709  1.00 103.68 ? 361 PHE A CB  1 
ATOM   2489 C  CG  . PHE A 1 361 ? 14.934 31.837 -6.863  1.00 103.76 ? 361 PHE A CG  1 
ATOM   2490 C  CD1 . PHE A 1 361 ? 13.904 32.718 -6.597  1.00 104.16 ? 361 PHE A CD1 1 
ATOM   2491 C  CD2 . PHE A 1 361 ? 16.191 32.127 -6.365  1.00 104.22 ? 361 PHE A CD2 1 
ATOM   2492 C  CE1 . PHE A 1 361 ? 14.123 33.852 -5.842  1.00 104.73 ? 361 PHE A CE1 1 
ATOM   2493 C  CE2 . PHE A 1 361 ? 16.405 33.259 -5.604  1.00 104.75 ? 361 PHE A CE2 1 
ATOM   2494 C  CZ  . PHE A 1 361 ? 15.373 34.120 -5.356  1.00 104.54 ? 361 PHE A CZ  1 
ATOM   2495 N  N   . GLU A 1 362 ? 12.861 27.742 -8.432  1.00 107.51 ? 362 GLU A N   1 
ATOM   2496 C  CA  . GLU A 1 362 ? 12.728 26.651 -9.391  1.00 109.16 ? 362 GLU A CA  1 
ATOM   2497 C  C   . GLU A 1 362 ? 13.999 26.505 -10.236 1.00 110.28 ? 362 GLU A C   1 
ATOM   2498 O  O   . GLU A 1 362 ? 13.919 26.413 -11.463 1.00 110.63 ? 362 GLU A O   1 
ATOM   2499 C  CB  . GLU A 1 362 ? 11.474 26.831 -10.272 1.00 111.90 ? 362 GLU A CB  1 
ATOM   2500 C  CG  . GLU A 1 362 ? 10.185 26.992 -9.479  1.00 117.24 ? 362 GLU A CG  1 
ATOM   2501 C  CD  . GLU A 1 362 ? 8.954  27.306 -10.309 1.00 124.05 ? 362 GLU A CD  1 
ATOM   2502 O  OE1 . GLU A 1 362 ? 9.036  28.181 -11.202 1.00 125.30 ? 362 GLU A OE1 1 
ATOM   2503 O  OE2 . GLU A 1 362 ? 7.898  26.684 -10.053 1.00 126.32 ? 362 GLU A OE2 1 
ATOM   2504 N  N   . LEU A 1 363 ? 15.174 26.515 -9.585  1.00 110.66 ? 363 LEU A N   1 
ATOM   2505 C  CA  . LEU A 1 363 ? 16.439 26.375 -10.307 1.00 111.49 ? 363 LEU A CA  1 
ATOM   2506 C  C   . LEU A 1 363 ? 16.922 24.908 -10.307 1.00 112.28 ? 363 LEU A C   1 
ATOM   2507 O  O   . LEU A 1 363 ? 16.756 24.214 -9.275  1.00 112.27 ? 363 LEU A O   1 
ATOM   2508 C  CB  . LEU A 1 363 ? 17.522 27.298 -9.721  1.00 111.57 ? 363 LEU A CB  1 
ATOM   2509 C  CG  . LEU A 1 363 ? 17.194 28.785 -9.639  1.00 112.76 ? 363 LEU A CG  1 
ATOM   2510 C  CD1 . LEU A 1 363 ? 18.287 29.536 -8.898  1.00 113.41 ? 363 LEU A CD1 1 
ATOM   2511 C  CD2 . LEU A 1 363 ? 16.987 29.377 -11.014 1.00 113.14 ? 363 LEU A CD2 1 
HETATM 2512 C  C1  . GLC B 2 .   ? 22.409 46.339 26.797  1.00 101.13 ? 1   GLC B C1  1 
HETATM 2513 C  C2  . GLC B 2 .   ? 21.755 47.707 26.818  1.00 100.40 ? 1   GLC B C2  1 
HETATM 2514 C  C3  . GLC B 2 .   ? 20.779 47.801 27.982  1.00 100.37 ? 1   GLC B C3  1 
HETATM 2515 C  C4  . GLC B 2 .   ? 19.794 46.629 27.980  1.00 100.34 ? 1   GLC B C4  1 
HETATM 2516 C  C5  . GLC B 2 .   ? 20.517 45.273 27.926  1.00 100.23 ? 1   GLC B C5  1 
HETATM 2517 C  C6  . GLC B 2 .   ? 19.582 44.090 27.747  1.00 99.45  ? 1   GLC B C6  1 
HETATM 2518 O  O2  . GLC B 2 .   ? 22.747 48.730 26.816  1.00 99.89  ? 1   GLC B O2  1 
HETATM 2519 O  O3  . GLC B 2 .   ? 20.080 49.045 27.900  1.00 100.29 ? 1   GLC B O3  1 
HETATM 2520 O  O4  . GLC B 2 .   ? 19.003 46.668 29.165  1.00 100.36 ? 1   GLC B O4  1 
HETATM 2521 O  O5  . GLC B 2 .   ? 21.422 45.280 26.791  1.00 100.80 ? 1   GLC B O5  1 
HETATM 2522 O  O6  . GLC B 2 .   ? 20.255 42.836 27.593  1.00 98.75  ? 1   GLC B O6  1 
HETATM 2523 C  C1  . GLC B 2 .   ? 24.154 45.235 28.298  1.00 102.70 ? 2   GLC B C1  1 
HETATM 2524 C  C2  . GLC B 2 .   ? 24.485 45.173 29.786  1.00 102.87 ? 2   GLC B C2  1 
HETATM 2525 C  C3  . GLC B 2 .   ? 25.516 46.227 30.147  1.00 103.20 ? 2   GLC B C3  1 
HETATM 2526 C  C4  . GLC B 2 .   ? 26.739 46.145 29.230  1.00 103.30 ? 2   GLC B C4  1 
HETATM 2527 C  C5  . GLC B 2 .   ? 26.326 46.211 27.742  1.00 103.30 ? 2   GLC B C5  1 
HETATM 2528 C  C6  . GLC B 2 .   ? 27.465 45.980 26.765  1.00 103.25 ? 2   GLC B C6  1 
HETATM 2529 O  O1  . GLC B 2 .   ? 23.346 46.334 27.976  1.00 101.99 ? 2   GLC B O1  1 
HETATM 2530 O  O2  . GLC B 2 .   ? 23.304 45.283 30.576  1.00 102.70 ? 2   GLC B O2  1 
HETATM 2531 O  O3  . GLC B 2 .   ? 25.892 46.059 31.516  1.00 103.34 ? 2   GLC B O3  1 
HETATM 2532 O  O4  . GLC B 2 .   ? 27.605 47.242 29.518  1.00 103.27 ? 2   GLC B O4  1 
HETATM 2533 O  O5  . GLC B 2 .   ? 25.338 45.181 27.477  1.00 103.16 ? 2   GLC B O5  1 
HETATM 2534 O  O6  . GLC B 2 .   ? 27.974 44.638 26.797  1.00 103.10 ? 2   GLC B O6  1 
HETATM 2535 C  C3  . VBL C 3 .   ? 23.312 40.153 17.330  1.00 78.20  ? 401 VBL A C3  1 
HETATM 2536 C  C4  . VBL C 3 .   ? 24.565 41.070 17.636  1.00 78.44  ? 401 VBL A C4  1 
HETATM 2537 C  C5  . VBL C 3 .   ? 24.758 41.268 19.152  1.00 78.40  ? 401 VBL A C5  1 
HETATM 2538 C  C6  . VBL C 3 .   ? 25.130 42.698 19.584  1.00 78.62  ? 401 VBL A C6  1 
HETATM 2539 C  C7  . VBL C 3 .   ? 26.583 43.099 19.249  1.00 78.85  ? 401 VBL A C7  1 
HETATM 2540 C  C8  . VBL C 3 .   ? 26.725 44.593 18.902  1.00 78.83  ? 401 VBL A C8  1 
HETATM 2541 C  C9  . VBL C 3 .   ? 26.324 44.906 17.459  1.00 78.82  ? 401 VBL A C9  1 
HETATM 2542 C  C1  . VBL C 3 .   ? 20.819 39.579 17.642  1.00 77.44  ? 401 VBL A C1  1 
HETATM 2543 C  C2  . VBL C 3 .   ? 21.891 40.704 17.695  1.00 77.84  ? 401 VBL A C2  1 
HETATM 2544 C  C10 . VBL C 3 .   ? 23.291 39.577 15.877  1.00 78.41  ? 401 VBL A C10 1 
HETATM 2545 C  C12 . VBL C 3 .   ? 20.242 39.162 20.787  1.00 77.30  ? 401 VBL A C12 1 
HETATM 2546 C  C11 . VBL C 3 .   ? 19.400 38.762 19.578  1.00 77.14  ? 401 VBL A C11 1 
HETATM 2547 C  C   . VBL C 3 .   ? 19.556 39.820 18.477  1.00 77.23  ? 401 VBL A C   1 
HETATM 2548 O  O   . VBL C 3 .   ? 25.719 40.371 17.214  1.00 78.66  ? 401 VBL A O   1 
HETATM 2549 O  O1  . VBL C 3 .   ? 23.142 38.169 16.055  1.00 78.81  ? 401 VBL A O1  1 
HETATM 2550 S  S   . SO4 D 4 .   ? 5.784  42.810 27.629  1.00 145.02 ? 402 SO4 A S   1 
HETATM 2551 O  O1  . SO4 D 4 .   ? 6.863  41.826 27.795  1.00 144.96 ? 402 SO4 A O1  1 
HETATM 2552 O  O2  . SO4 D 4 .   ? 5.831  43.394 26.282  1.00 144.96 ? 402 SO4 A O2  1 
HETATM 2553 O  O3  . SO4 D 4 .   ? 4.506  42.081 27.756  1.00 145.20 ? 402 SO4 A O3  1 
HETATM 2554 O  O4  . SO4 D 4 .   ? 5.831  43.889 28.639  1.00 144.96 ? 402 SO4 A O4  1 
HETATM 2555 CL CL  . CL  E 5 .   ? 30.596 24.859 -0.913  1.00 97.93  ? 403 CL  A CL  1 
HETATM 2556 CL CL  . CL  F 5 .   ? 28.362 56.080 -14.225 1.00 88.22  ? 404 CL  A CL  1 
HETATM 2557 CL CL  . CL  G 5 .   ? 21.361 63.918 15.549  1.00 99.81  ? 405 CL  A CL  1 
HETATM 2558 CL CL  . CL  H 5 .   ? 26.868 60.730 -0.425  1.00 107.08 ? 406 CL  A CL  1 
HETATM 2559 O  O   . HOH I 6 .   ? 17.948 40.377 14.890  1.00 55.42  ? 501 HOH A O   1 
HETATM 2560 O  O   . HOH I 6 .   ? 6.294  52.590 18.171  1.00 80.13  ? 502 HOH A O   1 
HETATM 2561 O  O   . HOH I 6 .   ? 39.796 48.479 -0.787  1.00 74.65  ? 503 HOH A O   1 
HETATM 2562 O  O   . HOH I 6 .   ? 5.188  43.102 10.054  1.00 59.06  ? 504 HOH A O   1 
HETATM 2563 O  O   . HOH I 6 .   ? 20.446 62.910 4.554   1.00 70.39  ? 505 HOH A O   1 
HETATM 2564 O  O   . HOH I 6 .   ? 4.041  54.127 -1.138  1.00 95.74  ? 506 HOH A O   1 
HETATM 2565 O  O   . HOH I 6 .   ? -1.163 39.057 11.860  1.00 66.69  ? 507 HOH A O   1 
HETATM 2566 O  O   . HOH I 6 .   ? 36.066 42.254 12.474  1.00 73.40  ? 508 HOH A O   1 
HETATM 2567 O  O   . HOH I 6 .   ? 23.361 53.821 8.751   1.00 64.06  ? 509 HOH A O   1 
HETATM 2568 O  O   . HOH I 6 .   ? 6.864  38.178 0.216   1.00 66.79  ? 510 HOH A O   1 
HETATM 2569 O  O   . HOH I 6 .   ? 37.146 36.364 2.255   1.00 70.55  ? 511 HOH A O   1 
HETATM 2570 O  O   . HOH I 6 .   ? 34.819 47.220 17.255  1.00 73.75  ? 512 HOH A O   1 
HETATM 2571 O  O   . HOH I 6 .   ? 36.657 32.164 22.141  1.00 70.15  ? 513 HOH A O   1 
HETATM 2572 O  O   . HOH I 6 .   ? 41.478 43.265 3.815   1.00 79.60  ? 514 HOH A O   1 
HETATM 2573 O  O   . HOH I 6 .   ? 19.353 26.250 -13.062 1.00 85.66  ? 515 HOH A O   1 
HETATM 2574 O  O   . HOH I 6 .   ? 0.875  23.448 18.537  1.00 70.72  ? 516 HOH A O   1 
HETATM 2575 O  O   . HOH I 6 .   ? 28.501 44.429 14.686  1.00 58.70  ? 517 HOH A O   1 
HETATM 2576 O  O   . HOH I 6 .   ? 28.786 55.945 14.612  1.00 66.30  ? 518 HOH A O   1 
HETATM 2577 O  O   . HOH I 6 .   ? 42.291 56.456 -1.176  1.00 67.06  ? 519 HOH A O   1 
HETATM 2578 O  O   . HOH I 6 .   ? 22.957 55.658 23.102  1.00 65.24  ? 520 HOH A O   1 
HETATM 2579 O  O   . HOH I 6 .   ? 30.941 45.193 14.531  1.00 70.68  ? 521 HOH A O   1 
HETATM 2580 O  O   . HOH I 6 .   ? 8.540  56.462 9.275   1.00 63.54  ? 522 HOH A O   1 
HETATM 2581 O  O   . HOH I 6 .   ? 31.726 39.274 31.293  1.00 86.14  ? 523 HOH A O   1 
HETATM 2582 O  O   . HOH I 6 .   ? 11.433 50.733 -13.119 1.00 72.28  ? 524 HOH A O   1 
HETATM 2583 O  O   . HOH I 6 .   ? 19.129 20.979 8.047   1.00 71.29  ? 525 HOH A O   1 
HETATM 2584 O  O   . HOH I 6 .   ? 8.238  22.463 9.651   1.00 70.94  ? 526 HOH A O   1 
HETATM 2585 O  O   . HOH I 6 .   ? 30.628 40.965 29.815  1.00 65.59  ? 527 HOH A O   1 
HETATM 2586 O  O   . HOH I 6 .   ? 39.517 36.364 22.470  1.00 66.12  ? 528 HOH A O   1 
HETATM 2587 O  O   . HOH I 6 .   ? -0.632 50.619 -7.445  1.00 77.43  ? 529 HOH A O   1 
HETATM 2588 O  O   . HOH I 6 .   ? 3.135  52.318 8.082   1.00 68.50  ? 530 HOH A O   1 
HETATM 2589 O  O   . HOH I 6 .   ? 39.941 29.284 20.190  1.00 80.13  ? 531 HOH A O   1 
# 
