data_8QNA
# 
_entry.id   8QNA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8QNA         pdb_00008qna 10.2210/pdb8qna/pdb 
WWPDB D_1292133572 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QNA 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-26 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8QMX unspecified 
PDB . 8QN1 unspecified 
PDB . 8QN3 unspecified 
PDB . 8QN9 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              peter.macheroux@tugraz.at 
_pdbx_contact_author.name_first         Peter 
_pdbx_contact_author.name_last          Macheroux 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0242-454X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bijelic, A.'      1 ? 
'Macheroux, P.'    2 ? 
'Kerschbaumer, B.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structures of OPR3 wildtype and variants in complex with NAD(P)H' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kerschbaumer, B.' 1 ? 
primary 'Bijelic, A.'      2 ? 
primary 'Macheroux, P.'    3 ? 
# 
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 '12-oxophytodienoate reductase 3'                  44315.086 1   ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'                            456.344   1   ? ? ? ? 
3 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   1   ? ? ? ? 
4 non-polymer syn 'SULFATE ION'                                      96.063    1   ? ? ? ? 
5 water       nat water                                              18.015    424 ? ? ? ? 
# 
_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       
;HHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGF
PHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRA
IGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRV
GVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQG
TFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNAKTFYTQDPVVGYTDYPFLQGNGSNGPLS
RL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGF
PHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRA
IGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRV
GVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQG
TFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNAKTFYTQDPVVGYTDYPFLQGNGSNGPLS
RL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE'                            FMN 
3 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP 
4 'SULFATE ION'                                      SO4 
5 water                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   MET n 
1 8   ALA n 
1 9   SER n 
1 10  SER n 
1 11  ALA n 
1 12  GLN n 
1 13  ASP n 
1 14  GLY n 
1 15  ASN n 
1 16  ASN n 
1 17  PRO n 
1 18  LEU n 
1 19  PHE n 
1 20  SER n 
1 21  PRO n 
1 22  TYR n 
1 23  LYS n 
1 24  MET n 
1 25  GLY n 
1 26  LYS n 
1 27  PHE n 
1 28  ASN n 
1 29  LEU n 
1 30  SER n 
1 31  HIS n 
1 32  ARG n 
1 33  VAL n 
1 34  VAL n 
1 35  LEU n 
1 36  ALA n 
1 37  PRO n 
1 38  MET n 
1 39  THR n 
1 40  ARG n 
1 41  CYS n 
1 42  ARG n 
1 43  ALA n 
1 44  LEU n 
1 45  ASN n 
1 46  ASN n 
1 47  ILE n 
1 48  PRO n 
1 49  GLN n 
1 50  ALA n 
1 51  ALA n 
1 52  LEU n 
1 53  GLY n 
1 54  GLU n 
1 55  TYR n 
1 56  TYR n 
1 57  GLU n 
1 58  GLN n 
1 59  ARG n 
1 60  ALA n 
1 61  THR n 
1 62  ALA n 
1 63  GLY n 
1 64  GLY n 
1 65  PHE n 
1 66  LEU n 
1 67  ILE n 
1 68  THR n 
1 69  GLU n 
1 70  GLY n 
1 71  THR n 
1 72  MET n 
1 73  ILE n 
1 74  SER n 
1 75  PRO n 
1 76  THR n 
1 77  SER n 
1 78  ALA n 
1 79  GLY n 
1 80  PHE n 
1 81  PRO n 
1 82  HIS n 
1 83  VAL n 
1 84  PRO n 
1 85  GLY n 
1 86  ILE n 
1 87  PHE n 
1 88  THR n 
1 89  LYS n 
1 90  GLU n 
1 91  GLN n 
1 92  VAL n 
1 93  ARG n 
1 94  GLU n 
1 95  TRP n 
1 96  LYS n 
1 97  LYS n 
1 98  ILE n 
1 99  VAL n 
1 100 ASP n 
1 101 VAL n 
1 102 VAL n 
1 103 HIS n 
1 104 ALA n 
1 105 LYS n 
1 106 GLY n 
1 107 ALA n 
1 108 VAL n 
1 109 ILE n 
1 110 PHE n 
1 111 CYS n 
1 112 GLN n 
1 113 LEU n 
1 114 TRP n 
1 115 HIS n 
1 116 VAL n 
1 117 GLY n 
1 118 ARG n 
1 119 ALA n 
1 120 SER n 
1 121 HIS n 
1 122 GLU n 
1 123 VAL n 
1 124 TYR n 
1 125 GLN n 
1 126 PRO n 
1 127 ALA n 
1 128 GLY n 
1 129 ALA n 
1 130 ALA n 
1 131 PRO n 
1 132 ILE n 
1 133 SER n 
1 134 SER n 
1 135 THR n 
1 136 GLU n 
1 137 LYS n 
1 138 PRO n 
1 139 ILE n 
1 140 SER n 
1 141 ASN n 
1 142 ARG n 
1 143 TRP n 
1 144 ARG n 
1 145 ILE n 
1 146 LEU n 
1 147 MET n 
1 148 PRO n 
1 149 ASP n 
1 150 GLY n 
1 151 THR n 
1 152 HIS n 
1 153 GLY n 
1 154 ILE n 
1 155 TYR n 
1 156 PRO n 
1 157 LYS n 
1 158 PRO n 
1 159 ARG n 
1 160 ALA n 
1 161 ILE n 
1 162 GLY n 
1 163 THR n 
1 164 TYR n 
1 165 GLU n 
1 166 ILE n 
1 167 SER n 
1 168 GLN n 
1 169 VAL n 
1 170 VAL n 
1 171 GLU n 
1 172 ASP n 
1 173 TYR n 
1 174 ARG n 
1 175 ARG n 
1 176 SER n 
1 177 ALA n 
1 178 LEU n 
1 179 ASN n 
1 180 ALA n 
1 181 ILE n 
1 182 GLU n 
1 183 ALA n 
1 184 GLY n 
1 185 PHE n 
1 186 ASP n 
1 187 GLY n 
1 188 ILE n 
1 189 GLU n 
1 190 ILE n 
1 191 HIS n 
1 192 GLY n 
1 193 ALA n 
1 194 HIS n 
1 195 GLY n 
1 196 TYR n 
1 197 LEU n 
1 198 ILE n 
1 199 ASP n 
1 200 GLN n 
1 201 PHE n 
1 202 LEU n 
1 203 LYS n 
1 204 ASP n 
1 205 GLY n 
1 206 ILE n 
1 207 ASN n 
1 208 ASP n 
1 209 ARG n 
1 210 THR n 
1 211 ASP n 
1 212 GLU n 
1 213 TYR n 
1 214 GLY n 
1 215 GLY n 
1 216 SER n 
1 217 LEU n 
1 218 ALA n 
1 219 ASN n 
1 220 ARG n 
1 221 CYS n 
1 222 LYS n 
1 223 PHE n 
1 224 ILE n 
1 225 THR n 
1 226 GLN n 
1 227 VAL n 
1 228 VAL n 
1 229 GLN n 
1 230 ALA n 
1 231 VAL n 
1 232 VAL n 
1 233 SER n 
1 234 ALA n 
1 235 ILE n 
1 236 GLY n 
1 237 ALA n 
1 238 ASP n 
1 239 ARG n 
1 240 VAL n 
1 241 GLY n 
1 242 VAL n 
1 243 ARG n 
1 244 VAL n 
1 245 SER n 
1 246 PRO n 
1 247 ALA n 
1 248 ILE n 
1 249 ASP n 
1 250 HIS n 
1 251 LEU n 
1 252 ASP n 
1 253 ALA n 
1 254 MET n 
1 255 ASP n 
1 256 SER n 
1 257 ASN n 
1 258 PRO n 
1 259 LEU n 
1 260 SER n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 ALA n 
1 265 VAL n 
1 266 VAL n 
1 267 GLU n 
1 268 ARG n 
1 269 LEU n 
1 270 ASN n 
1 271 LYS n 
1 272 ILE n 
1 273 GLN n 
1 274 LEU n 
1 275 HIS n 
1 276 SER n 
1 277 GLY n 
1 278 SER n 
1 279 LYS n 
1 280 LEU n 
1 281 ALA n 
1 282 TYR n 
1 283 LEU n 
1 284 HIS n 
1 285 VAL n 
1 286 THR n 
1 287 GLN n 
1 288 PRO n 
1 289 ARG n 
1 290 TYR n 
1 291 VAL n 
1 292 ALA n 
1 293 TYR n 
1 294 GLY n 
1 295 GLN n 
1 296 THR n 
1 297 GLU n 
1 298 ALA n 
1 299 GLY n 
1 300 ARG n 
1 301 LEU n 
1 302 GLY n 
1 303 SER n 
1 304 GLU n 
1 305 GLU n 
1 306 GLU n 
1 307 GLU n 
1 308 ALA n 
1 309 ARG n 
1 310 LEU n 
1 311 MET n 
1 312 ARG n 
1 313 THR n 
1 314 LEU n 
1 315 ARG n 
1 316 ASN n 
1 317 ALA n 
1 318 TYR n 
1 319 GLN n 
1 320 GLY n 
1 321 THR n 
1 322 PHE n 
1 323 ILE n 
1 324 CYS n 
1 325 SER n 
1 326 GLY n 
1 327 GLY n 
1 328 TYR n 
1 329 THR n 
1 330 ARG n 
1 331 GLU n 
1 332 LEU n 
1 333 GLY n 
1 334 ILE n 
1 335 GLU n 
1 336 ALA n 
1 337 VAL n 
1 338 ALA n 
1 339 GLN n 
1 340 GLY n 
1 341 ASP n 
1 342 ALA n 
1 343 ASP n 
1 344 LEU n 
1 345 VAL n 
1 346 SER n 
1 347 TYR n 
1 348 GLY n 
1 349 ARG n 
1 350 LEU n 
1 351 PHE n 
1 352 ILE n 
1 353 SER n 
1 354 ASN n 
1 355 PRO n 
1 356 ASP n 
1 357 LEU n 
1 358 VAL n 
1 359 MET n 
1 360 ARG n 
1 361 ILE n 
1 362 LYS n 
1 363 LEU n 
1 364 ASN n 
1 365 ALA n 
1 366 PRO n 
1 367 LEU n 
1 368 ASN n 
1 369 LYS n 
1 370 TYR n 
1 371 ASN n 
1 372 ALA n 
1 373 LYS n 
1 374 THR n 
1 375 PHE n 
1 376 TYR n 
1 377 THR n 
1 378 GLN n 
1 379 ASP n 
1 380 PRO n 
1 381 VAL n 
1 382 VAL n 
1 383 GLY n 
1 384 TYR n 
1 385 THR n 
1 386 ASP n 
1 387 TYR n 
1 388 PRO n 
1 389 PHE n 
1 390 LEU n 
1 391 GLN n 
1 392 GLY n 
1 393 ASN n 
1 394 GLY n 
1 395 SER n 
1 396 ASN n 
1 397 GLY n 
1 398 PRO n 
1 399 LEU n 
1 400 SER n 
1 401 ARG n 
1 402 LEU 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                   402 
_entity_src_gen.gene_src_common_name               tomato 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 OPR3 
_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      'Solanum lycopersicum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4081 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
CYS 'L-peptide linking' y CYSTEINE                                           ?                                            
'C3 H7 N O2 S'      121.158 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE'                            'RIBOFLAVIN MONOPHOSPHATE'                   
'C17 H21 N4 O9 P'   456.344 
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 
NAP non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
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 
# 
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   HIS 1   -5  ?   ?   ?   A . n 
A 1 2   HIS 2   -4  ?   ?   ?   A . n 
A 1 3   HIS 3   -3  ?   ?   ?   A . n 
A 1 4   HIS 4   -2  ?   ?   ?   A . n 
A 1 5   HIS 5   -1  ?   ?   ?   A . n 
A 1 6   HIS 6   0   ?   ?   ?   A . n 
A 1 7   MET 7   1   ?   ?   ?   A . n 
A 1 8   ALA 8   2   ?   ?   ?   A . n 
A 1 9   SER 9   3   ?   ?   ?   A . n 
A 1 10  SER 10  4   ?   ?   ?   A . n 
A 1 11  ALA 11  5   ?   ?   ?   A . n 
A 1 12  GLN 12  6   ?   ?   ?   A . n 
A 1 13  ASP 13  7   ?   ?   ?   A . n 
A 1 14  GLY 14  8   ?   ?   ?   A . n 
A 1 15  ASN 15  9   ?   ?   ?   A . n 
A 1 16  ASN 16  10  10  ASN ASN A . n 
A 1 17  PRO 17  11  11  PRO PRO A . n 
A 1 18  LEU 18  12  12  LEU LEU A . n 
A 1 19  PHE 19  13  13  PHE PHE A . n 
A 1 20  SER 20  14  14  SER SER A . n 
A 1 21  PRO 21  15  15  PRO PRO A . n 
A 1 22  TYR 22  16  16  TYR TYR A . n 
A 1 23  LYS 23  17  17  LYS LYS A . n 
A 1 24  MET 24  18  18  MET MET A . n 
A 1 25  GLY 25  19  19  GLY GLY A . n 
A 1 26  LYS 26  20  20  LYS LYS A . n 
A 1 27  PHE 27  21  21  PHE PHE A . n 
A 1 28  ASN 28  22  22  ASN ASN A . n 
A 1 29  LEU 29  23  23  LEU LEU A . n 
A 1 30  SER 30  24  24  SER SER A . n 
A 1 31  HIS 31  25  25  HIS HIS A . n 
A 1 32  ARG 32  26  26  ARG ARG A . n 
A 1 33  VAL 33  27  27  VAL VAL A . n 
A 1 34  VAL 34  28  28  VAL VAL A . n 
A 1 35  LEU 35  29  29  LEU LEU A . n 
A 1 36  ALA 36  30  30  ALA ALA A . n 
A 1 37  PRO 37  31  31  PRO PRO A . n 
A 1 38  MET 38  32  32  MET MET A . n 
A 1 39  THR 39  33  33  THR THR A . n 
A 1 40  ARG 40  34  34  ARG ARG A . n 
A 1 41  CYS 41  35  35  CYS CYS A . n 
A 1 42  ARG 42  36  36  ARG ARG A . n 
A 1 43  ALA 43  37  37  ALA ALA A . n 
A 1 44  LEU 44  38  38  LEU LEU A . n 
A 1 45  ASN 45  39  39  ASN ASN A . n 
A 1 46  ASN 46  40  40  ASN ASN A . n 
A 1 47  ILE 47  41  41  ILE ILE A . n 
A 1 48  PRO 48  42  42  PRO PRO A . n 
A 1 49  GLN 49  43  43  GLN GLN A . n 
A 1 50  ALA 50  44  44  ALA ALA A . n 
A 1 51  ALA 51  45  45  ALA ALA A . n 
A 1 52  LEU 52  46  46  LEU LEU A . n 
A 1 53  GLY 53  47  47  GLY GLY A . n 
A 1 54  GLU 54  48  48  GLU GLU A . n 
A 1 55  TYR 55  49  49  TYR TYR A . n 
A 1 56  TYR 56  50  50  TYR TYR A . n 
A 1 57  GLU 57  51  51  GLU GLU A . n 
A 1 58  GLN 58  52  52  GLN GLN A . n 
A 1 59  ARG 59  53  53  ARG ARG A . n 
A 1 60  ALA 60  54  54  ALA ALA A . n 
A 1 61  THR 61  55  55  THR THR A . n 
A 1 62  ALA 62  56  56  ALA ALA A . n 
A 1 63  GLY 63  57  57  GLY GLY A . n 
A 1 64  GLY 64  58  58  GLY GLY A . n 
A 1 65  PHE 65  59  59  PHE PHE A . n 
A 1 66  LEU 66  60  60  LEU LEU A . n 
A 1 67  ILE 67  61  61  ILE ILE A . n 
A 1 68  THR 68  62  62  THR THR A . n 
A 1 69  GLU 69  63  63  GLU GLU A . n 
A 1 70  GLY 70  64  64  GLY GLY A . n 
A 1 71  THR 71  65  65  THR THR A . n 
A 1 72  MET 72  66  66  MET MET A . n 
A 1 73  ILE 73  67  67  ILE ILE A . n 
A 1 74  SER 74  68  68  SER SER A . n 
A 1 75  PRO 75  69  69  PRO PRO A . n 
A 1 76  THR 76  70  70  THR THR A . n 
A 1 77  SER 77  71  71  SER SER A . n 
A 1 78  ALA 78  72  72  ALA ALA A . n 
A 1 79  GLY 79  73  73  GLY GLY A . n 
A 1 80  PHE 80  74  74  PHE PHE A . n 
A 1 81  PRO 81  75  75  PRO PRO A . n 
A 1 82  HIS 82  76  76  HIS HIS A . n 
A 1 83  VAL 83  77  77  VAL VAL A . n 
A 1 84  PRO 84  78  78  PRO PRO A . n 
A 1 85  GLY 85  79  79  GLY GLY A . n 
A 1 86  ILE 86  80  80  ILE ILE A . n 
A 1 87  PHE 87  81  81  PHE PHE A . n 
A 1 88  THR 88  82  82  THR THR A . n 
A 1 89  LYS 89  83  83  LYS LYS A . n 
A 1 90  GLU 90  84  84  GLU GLU A . n 
A 1 91  GLN 91  85  85  GLN GLN A . n 
A 1 92  VAL 92  86  86  VAL VAL A . n 
A 1 93  ARG 93  87  87  ARG ARG A . n 
A 1 94  GLU 94  88  88  GLU GLU A . n 
A 1 95  TRP 95  89  89  TRP TRP A . n 
A 1 96  LYS 96  90  90  LYS LYS A . n 
A 1 97  LYS 97  91  91  LYS LYS A . n 
A 1 98  ILE 98  92  92  ILE ILE A . n 
A 1 99  VAL 99  93  93  VAL VAL A . n 
A 1 100 ASP 100 94  94  ASP ASP A . n 
A 1 101 VAL 101 95  95  VAL VAL A . n 
A 1 102 VAL 102 96  96  VAL VAL A . n 
A 1 103 HIS 103 97  97  HIS HIS A . n 
A 1 104 ALA 104 98  98  ALA ALA A . n 
A 1 105 LYS 105 99  99  LYS LYS A . n 
A 1 106 GLY 106 100 100 GLY GLY A . n 
A 1 107 ALA 107 101 101 ALA ALA A . n 
A 1 108 VAL 108 102 102 VAL VAL A . n 
A 1 109 ILE 109 103 103 ILE ILE A . n 
A 1 110 PHE 110 104 104 PHE PHE A . n 
A 1 111 CYS 111 105 105 CYS CYS A . n 
A 1 112 GLN 112 106 106 GLN GLN A . n 
A 1 113 LEU 113 107 107 LEU LEU A . n 
A 1 114 TRP 114 108 108 TRP TRP A . n 
A 1 115 HIS 115 109 109 HIS HIS A . n 
A 1 116 VAL 116 110 110 VAL VAL A . n 
A 1 117 GLY 117 111 111 GLY GLY A . n 
A 1 118 ARG 118 112 112 ARG ARG A . n 
A 1 119 ALA 119 113 113 ALA ALA A . n 
A 1 120 SER 120 114 114 SER SER A . n 
A 1 121 HIS 121 115 115 HIS HIS A . n 
A 1 122 GLU 122 116 116 GLU GLU A . n 
A 1 123 VAL 123 117 117 VAL VAL A . n 
A 1 124 TYR 124 118 118 TYR TYR A . n 
A 1 125 GLN 125 119 119 GLN GLN A . n 
A 1 126 PRO 126 120 120 PRO PRO A . n 
A 1 127 ALA 127 121 121 ALA ALA A . n 
A 1 128 GLY 128 122 122 GLY GLY A . n 
A 1 129 ALA 129 123 123 ALA ALA A . n 
A 1 130 ALA 130 124 124 ALA ALA A . n 
A 1 131 PRO 131 125 125 PRO PRO A . n 
A 1 132 ILE 132 126 126 ILE ILE A . n 
A 1 133 SER 133 127 127 SER SER A . n 
A 1 134 SER 134 128 128 SER SER A . n 
A 1 135 THR 135 129 129 THR THR A . n 
A 1 136 GLU 136 130 130 GLU GLU A . n 
A 1 137 LYS 137 131 131 LYS LYS A . n 
A 1 138 PRO 138 132 132 PRO PRO A . n 
A 1 139 ILE 139 133 133 ILE ILE A . n 
A 1 140 SER 140 134 134 SER SER A . n 
A 1 141 ASN 141 135 135 ASN ASN A . n 
A 1 142 ARG 142 136 136 ARG ARG A . n 
A 1 143 TRP 143 137 137 TRP TRP A . n 
A 1 144 ARG 144 138 138 ARG ARG A . n 
A 1 145 ILE 145 139 139 ILE ILE A . n 
A 1 146 LEU 146 140 140 LEU LEU A . n 
A 1 147 MET 147 141 141 MET MET A . n 
A 1 148 PRO 148 142 142 PRO PRO A . n 
A 1 149 ASP 149 143 143 ASP ASP A . n 
A 1 150 GLY 150 144 144 GLY GLY A . n 
A 1 151 THR 151 145 145 THR THR A . n 
A 1 152 HIS 152 146 146 HIS HIS A . n 
A 1 153 GLY 153 147 147 GLY GLY A . n 
A 1 154 ILE 154 148 148 ILE ILE A . n 
A 1 155 TYR 155 149 149 TYR TYR A . n 
A 1 156 PRO 156 150 150 PRO PRO A . n 
A 1 157 LYS 157 151 151 LYS LYS A . n 
A 1 158 PRO 158 152 152 PRO PRO A . n 
A 1 159 ARG 159 153 153 ARG ARG A . n 
A 1 160 ALA 160 154 154 ALA ALA A . n 
A 1 161 ILE 161 155 155 ILE ILE A . n 
A 1 162 GLY 162 156 156 GLY GLY A . n 
A 1 163 THR 163 157 157 THR THR A . n 
A 1 164 TYR 164 158 158 TYR TYR A . n 
A 1 165 GLU 165 159 159 GLU GLU A . n 
A 1 166 ILE 166 160 160 ILE ILE A . n 
A 1 167 SER 167 161 161 SER SER A . n 
A 1 168 GLN 168 162 162 GLN GLN A . n 
A 1 169 VAL 169 163 163 VAL VAL A . n 
A 1 170 VAL 170 164 164 VAL VAL A . n 
A 1 171 GLU 171 165 165 GLU GLU A . n 
A 1 172 ASP 172 166 166 ASP ASP A . n 
A 1 173 TYR 173 167 167 TYR TYR A . n 
A 1 174 ARG 174 168 168 ARG ARG A . n 
A 1 175 ARG 175 169 169 ARG ARG A . n 
A 1 176 SER 176 170 170 SER SER A . n 
A 1 177 ALA 177 171 171 ALA ALA A . n 
A 1 178 LEU 178 172 172 LEU LEU A . n 
A 1 179 ASN 179 173 173 ASN ASN A . n 
A 1 180 ALA 180 174 174 ALA ALA A . n 
A 1 181 ILE 181 175 175 ILE ILE A . n 
A 1 182 GLU 182 176 176 GLU GLU A . n 
A 1 183 ALA 183 177 177 ALA ALA A . n 
A 1 184 GLY 184 178 178 GLY GLY A . n 
A 1 185 PHE 185 179 179 PHE PHE A . n 
A 1 186 ASP 186 180 180 ASP ASP A . n 
A 1 187 GLY 187 181 181 GLY GLY A . n 
A 1 188 ILE 188 182 182 ILE ILE A . n 
A 1 189 GLU 189 183 183 GLU GLU A . n 
A 1 190 ILE 190 184 184 ILE ILE A . n 
A 1 191 HIS 191 185 185 HIS HIS A . n 
A 1 192 GLY 192 186 186 GLY GLY A . n 
A 1 193 ALA 193 187 187 ALA ALA A . n 
A 1 194 HIS 194 188 188 HIS HIS A . n 
A 1 195 GLY 195 189 189 GLY GLY A . n 
A 1 196 TYR 196 190 190 TYR TYR A . n 
A 1 197 LEU 197 191 191 LEU LEU A . n 
A 1 198 ILE 198 192 192 ILE ILE A . n 
A 1 199 ASP 199 193 193 ASP ASP A . n 
A 1 200 GLN 200 194 194 GLN GLN A . n 
A 1 201 PHE 201 195 195 PHE PHE A . n 
A 1 202 LEU 202 196 196 LEU LEU A . n 
A 1 203 LYS 203 197 197 LYS LYS A . n 
A 1 204 ASP 204 198 198 ASP ASP A . n 
A 1 205 GLY 205 199 199 GLY GLY A . n 
A 1 206 ILE 206 200 200 ILE ILE A . n 
A 1 207 ASN 207 201 201 ASN ASN A . n 
A 1 208 ASP 208 202 202 ASP ASP A . n 
A 1 209 ARG 209 203 203 ARG ARG A . n 
A 1 210 THR 210 204 204 THR THR A . n 
A 1 211 ASP 211 205 205 ASP ASP A . n 
A 1 212 GLU 212 206 206 GLU GLU A . n 
A 1 213 TYR 213 207 207 TYR TYR A . n 
A 1 214 GLY 214 208 208 GLY GLY A . n 
A 1 215 GLY 215 209 209 GLY GLY A . n 
A 1 216 SER 216 210 210 SER SER A . n 
A 1 217 LEU 217 211 211 LEU LEU A . n 
A 1 218 ALA 218 212 212 ALA ALA A . n 
A 1 219 ASN 219 213 213 ASN ASN A . n 
A 1 220 ARG 220 214 214 ARG ARG A . n 
A 1 221 CYS 221 215 215 CYS CYS A . n 
A 1 222 LYS 222 216 216 LYS LYS A . n 
A 1 223 PHE 223 217 217 PHE PHE A . n 
A 1 224 ILE 224 218 218 ILE ILE A . n 
A 1 225 THR 225 219 219 THR THR A . n 
A 1 226 GLN 226 220 220 GLN GLN A . n 
A 1 227 VAL 227 221 221 VAL VAL A . n 
A 1 228 VAL 228 222 222 VAL VAL A . n 
A 1 229 GLN 229 223 223 GLN GLN A . n 
A 1 230 ALA 230 224 224 ALA ALA A . n 
A 1 231 VAL 231 225 225 VAL VAL A . n 
A 1 232 VAL 232 226 226 VAL VAL A . n 
A 1 233 SER 233 227 227 SER SER A . n 
A 1 234 ALA 234 228 228 ALA ALA A . n 
A 1 235 ILE 235 229 229 ILE ILE A . n 
A 1 236 GLY 236 230 230 GLY GLY A . n 
A 1 237 ALA 237 231 231 ALA ALA A . n 
A 1 238 ASP 238 232 232 ASP ASP A . n 
A 1 239 ARG 239 233 233 ARG ARG A . n 
A 1 240 VAL 240 234 234 VAL VAL A . n 
A 1 241 GLY 241 235 235 GLY GLY A . n 
A 1 242 VAL 242 236 236 VAL VAL A . n 
A 1 243 ARG 243 237 237 ARG ARG A . n 
A 1 244 VAL 244 238 238 VAL VAL A . n 
A 1 245 SER 245 239 239 SER SER A . n 
A 1 246 PRO 246 240 240 PRO PRO A . n 
A 1 247 ALA 247 241 241 ALA ALA A . n 
A 1 248 ILE 248 242 242 ILE ILE A . n 
A 1 249 ASP 249 243 243 ASP ASP A . n 
A 1 250 HIS 250 244 244 HIS HIS A . n 
A 1 251 LEU 251 245 245 LEU LEU A . n 
A 1 252 ASP 252 246 246 ASP ASP A . n 
A 1 253 ALA 253 247 247 ALA ALA A . n 
A 1 254 MET 254 248 248 MET MET A . n 
A 1 255 ASP 255 249 249 ASP ASP A . n 
A 1 256 SER 256 250 250 SER SER A . n 
A 1 257 ASN 257 251 251 ASN ASN A . n 
A 1 258 PRO 258 252 252 PRO PRO A . n 
A 1 259 LEU 259 253 253 LEU LEU A . n 
A 1 260 SER 260 254 254 SER SER A . n 
A 1 261 LEU 261 255 255 LEU LEU A . n 
A 1 262 GLY 262 256 256 GLY GLY A . n 
A 1 263 LEU 263 257 257 LEU LEU A . n 
A 1 264 ALA 264 258 258 ALA ALA A . n 
A 1 265 VAL 265 259 259 VAL VAL A . n 
A 1 266 VAL 266 260 260 VAL VAL A . n 
A 1 267 GLU 267 261 261 GLU GLU A . n 
A 1 268 ARG 268 262 262 ARG ARG A . n 
A 1 269 LEU 269 263 263 LEU LEU A . n 
A 1 270 ASN 270 264 264 ASN ASN A . n 
A 1 271 LYS 271 265 265 LYS LYS A . n 
A 1 272 ILE 272 266 266 ILE ILE A . n 
A 1 273 GLN 273 267 267 GLN GLN A . n 
A 1 274 LEU 274 268 268 LEU LEU A . n 
A 1 275 HIS 275 269 269 HIS HIS A . n 
A 1 276 SER 276 270 270 SER SER A . n 
A 1 277 GLY 277 271 271 GLY GLY A . n 
A 1 278 SER 278 272 272 SER SER A . n 
A 1 279 LYS 279 273 273 LYS LYS A . n 
A 1 280 LEU 280 274 274 LEU LEU A . n 
A 1 281 ALA 281 275 275 ALA ALA A . n 
A 1 282 TYR 282 276 276 TYR TYR A . n 
A 1 283 LEU 283 277 277 LEU LEU A . n 
A 1 284 HIS 284 278 278 HIS HIS A . n 
A 1 285 VAL 285 279 279 VAL VAL A . n 
A 1 286 THR 286 280 280 THR THR A . n 
A 1 287 GLN 287 281 281 GLN GLN A . n 
A 1 288 PRO 288 282 282 PRO PRO A . n 
A 1 289 ARG 289 283 283 ARG ARG A . n 
A 1 290 TYR 290 284 ?   ?   ?   A . n 
A 1 291 VAL 291 285 ?   ?   ?   A . n 
A 1 292 ALA 292 286 ?   ?   ?   A . n 
A 1 293 TYR 293 287 ?   ?   ?   A . n 
A 1 294 GLY 294 288 ?   ?   ?   A . n 
A 1 295 GLN 295 289 ?   ?   ?   A . n 
A 1 296 THR 296 290 ?   ?   ?   A . n 
A 1 297 GLU 297 291 ?   ?   ?   A . n 
A 1 298 ALA 298 292 ?   ?   ?   A . n 
A 1 299 GLY 299 293 ?   ?   ?   A . n 
A 1 300 ARG 300 294 ?   ?   ?   A . n 
A 1 301 LEU 301 295 ?   ?   ?   A . n 
A 1 302 GLY 302 296 ?   ?   ?   A . n 
A 1 303 SER 303 297 297 SER SER A . n 
A 1 304 GLU 304 298 298 GLU GLU A . n 
A 1 305 GLU 305 299 299 GLU GLU A . n 
A 1 306 GLU 306 300 300 GLU GLU A . n 
A 1 307 GLU 307 301 301 GLU GLU A . n 
A 1 308 ALA 308 302 302 ALA ALA A . n 
A 1 309 ARG 309 303 303 ARG ARG A . n 
A 1 310 LEU 310 304 304 LEU LEU A . n 
A 1 311 MET 311 305 305 MET MET A . n 
A 1 312 ARG 312 306 306 ARG ARG A . n 
A 1 313 THR 313 307 307 THR THR A . n 
A 1 314 LEU 314 308 308 LEU LEU A . n 
A 1 315 ARG 315 309 309 ARG ARG A . n 
A 1 316 ASN 316 310 310 ASN ASN A . n 
A 1 317 ALA 317 311 311 ALA ALA A . n 
A 1 318 TYR 318 312 312 TYR TYR A . n 
A 1 319 GLN 319 313 313 GLN GLN A . n 
A 1 320 GLY 320 314 314 GLY GLY A . n 
A 1 321 THR 321 315 315 THR THR A . n 
A 1 322 PHE 322 316 316 PHE PHE A . n 
A 1 323 ILE 323 317 317 ILE ILE A . n 
A 1 324 CYS 324 318 318 CYS CYS A . n 
A 1 325 SER 325 319 319 SER SER A . n 
A 1 326 GLY 326 320 320 GLY GLY A . n 
A 1 327 GLY 327 321 321 GLY GLY A . n 
A 1 328 TYR 328 322 322 TYR TYR A . n 
A 1 329 THR 329 323 323 THR THR A . n 
A 1 330 ARG 330 324 324 ARG ARG A . n 
A 1 331 GLU 331 325 325 GLU GLU A . n 
A 1 332 LEU 332 326 326 LEU LEU A . n 
A 1 333 GLY 333 327 327 GLY GLY A . n 
A 1 334 ILE 334 328 328 ILE ILE A . n 
A 1 335 GLU 335 329 329 GLU GLU A . n 
A 1 336 ALA 336 330 330 ALA ALA A . n 
A 1 337 VAL 337 331 331 VAL VAL A . n 
A 1 338 ALA 338 332 332 ALA ALA A . n 
A 1 339 GLN 339 333 333 GLN GLN A . n 
A 1 340 GLY 340 334 334 GLY GLY A . n 
A 1 341 ASP 341 335 335 ASP ASP A . n 
A 1 342 ALA 342 336 336 ALA ALA A . n 
A 1 343 ASP 343 337 337 ASP ASP A . n 
A 1 344 LEU 344 338 338 LEU LEU A . n 
A 1 345 VAL 345 339 339 VAL VAL A . n 
A 1 346 SER 346 340 340 SER SER A . n 
A 1 347 TYR 347 341 341 TYR TYR A . n 
A 1 348 GLY 348 342 342 GLY GLY A . n 
A 1 349 ARG 349 343 343 ARG ARG A . n 
A 1 350 LEU 350 344 344 LEU LEU A . n 
A 1 351 PHE 351 345 345 PHE PHE A . n 
A 1 352 ILE 352 346 346 ILE ILE A . n 
A 1 353 SER 353 347 347 SER SER A . n 
A 1 354 ASN 354 348 348 ASN ASN A . n 
A 1 355 PRO 355 349 349 PRO PRO A . n 
A 1 356 ASP 356 350 350 ASP ASP A . n 
A 1 357 LEU 357 351 351 LEU LEU A . n 
A 1 358 VAL 358 352 352 VAL VAL A . n 
A 1 359 MET 359 353 353 MET MET A . n 
A 1 360 ARG 360 354 354 ARG ARG A . n 
A 1 361 ILE 361 355 355 ILE ILE A . n 
A 1 362 LYS 362 356 356 LYS LYS A . n 
A 1 363 LEU 363 357 357 LEU LEU A . n 
A 1 364 ASN 364 358 358 ASN ASN A . n 
A 1 365 ALA 365 359 359 ALA ALA A . n 
A 1 366 PRO 366 360 360 PRO PRO A . n 
A 1 367 LEU 367 361 361 LEU LEU A . n 
A 1 368 ASN 368 362 362 ASN ASN A . n 
A 1 369 LYS 369 363 363 LYS LYS A . n 
A 1 370 TYR 370 364 364 TYR TYR A . n 
A 1 371 ASN 371 365 365 ASN ASN A . n 
A 1 372 ALA 372 366 366 ALA ALA A . n 
A 1 373 LYS 373 367 367 LYS LYS A . n 
A 1 374 THR 374 368 368 THR THR A . n 
A 1 375 PHE 375 369 369 PHE PHE A . n 
A 1 376 TYR 376 370 370 TYR TYR A . n 
A 1 377 THR 377 371 371 THR THR A . n 
A 1 378 GLN 378 372 372 GLN GLN A . n 
A 1 379 ASP 379 373 373 ASP ASP A . n 
A 1 380 PRO 380 374 374 PRO PRO A . n 
A 1 381 VAL 381 375 375 VAL VAL A . n 
A 1 382 VAL 382 376 376 VAL VAL A . n 
A 1 383 GLY 383 377 377 GLY GLY A . n 
A 1 384 TYR 384 378 378 TYR TYR A . n 
A 1 385 THR 385 379 379 THR THR A . n 
A 1 386 ASP 386 380 380 ASP ASP A . n 
A 1 387 TYR 387 381 381 TYR TYR A . n 
A 1 388 PRO 388 382 382 PRO PRO A . n 
A 1 389 PHE 389 383 383 PHE PHE A . n 
A 1 390 LEU 390 384 384 LEU LEU A . n 
A 1 391 GLN 391 385 385 GLN GLN A . n 
A 1 392 GLY 392 386 ?   ?   ?   A . n 
A 1 393 ASN 393 387 ?   ?   ?   A . n 
A 1 394 GLY 394 388 ?   ?   ?   A . n 
A 1 395 SER 395 389 ?   ?   ?   A . n 
A 1 396 ASN 396 390 ?   ?   ?   A . n 
A 1 397 GLY 397 391 ?   ?   ?   A . n 
A 1 398 PRO 398 392 ?   ?   ?   A . n 
A 1 399 LEU 399 393 ?   ?   ?   A . n 
A 1 400 SER 400 394 ?   ?   ?   A . n 
A 1 401 ARG 401 395 ?   ?   ?   A . n 
A 1 402 LEU 402 396 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FMN 1   401 401 FMN FMN A . 
C 3 NAP 1   402 402 NAP NAP A . 
D 4 SO4 1   403 403 SO4 SO4 A . 
E 5 HOH 1   501 115 HOH HOH A . 
E 5 HOH 2   502 405 HOH HOH A . 
E 5 HOH 3   503 121 HOH HOH A . 
E 5 HOH 4   504 101 HOH HOH A . 
E 5 HOH 5   505 385 HOH HOH A . 
E 5 HOH 6   506 95  HOH HOH A . 
E 5 HOH 7   507 193 HOH HOH A . 
E 5 HOH 8   508 31  HOH HOH A . 
E 5 HOH 9   509 72  HOH HOH A . 
E 5 HOH 10  510 311 HOH HOH A . 
E 5 HOH 11  511 433 HOH HOH A . 
E 5 HOH 12  512 371 HOH HOH A . 
E 5 HOH 13  513 55  HOH HOH A . 
E 5 HOH 14  514 118 HOH HOH A . 
E 5 HOH 15  515 343 HOH HOH A . 
E 5 HOH 16  516 309 HOH HOH A . 
E 5 HOH 17  517 81  HOH HOH A . 
E 5 HOH 18  518 282 HOH HOH A . 
E 5 HOH 19  519 245 HOH HOH A . 
E 5 HOH 20  520 46  HOH HOH A . 
E 5 HOH 21  521 185 HOH HOH A . 
E 5 HOH 22  522 258 HOH HOH A . 
E 5 HOH 23  523 87  HOH HOH A . 
E 5 HOH 24  524 196 HOH HOH A . 
E 5 HOH 25  525 188 HOH HOH A . 
E 5 HOH 26  526 175 HOH HOH A . 
E 5 HOH 27  527 431 HOH HOH A . 
E 5 HOH 28  528 20  HOH HOH A . 
E 5 HOH 29  529 221 HOH HOH A . 
E 5 HOH 30  530 10  HOH HOH A . 
E 5 HOH 31  531 17  HOH HOH A . 
E 5 HOH 32  532 77  HOH HOH A . 
E 5 HOH 33  533 281 HOH HOH A . 
E 5 HOH 34  534 333 HOH HOH A . 
E 5 HOH 35  535 108 HOH HOH A . 
E 5 HOH 36  536 70  HOH HOH A . 
E 5 HOH 37  537 179 HOH HOH A . 
E 5 HOH 38  538 167 HOH HOH A . 
E 5 HOH 39  539 177 HOH HOH A . 
E 5 HOH 40  540 347 HOH HOH A . 
E 5 HOH 41  541 323 HOH HOH A . 
E 5 HOH 42  542 96  HOH HOH A . 
E 5 HOH 43  543 126 HOH HOH A . 
E 5 HOH 44  544 80  HOH HOH A . 
E 5 HOH 45  545 422 HOH HOH A . 
E 5 HOH 46  546 145 HOH HOH A . 
E 5 HOH 47  547 263 HOH HOH A . 
E 5 HOH 48  548 183 HOH HOH A . 
E 5 HOH 49  549 82  HOH HOH A . 
E 5 HOH 50  550 289 HOH HOH A . 
E 5 HOH 51  551 257 HOH HOH A . 
E 5 HOH 52  552 219 HOH HOH A . 
E 5 HOH 53  553 1   HOH HOH A . 
E 5 HOH 54  554 49  HOH HOH A . 
E 5 HOH 55  555 340 HOH HOH A . 
E 5 HOH 56  556 199 HOH HOH A . 
E 5 HOH 57  557 181 HOH HOH A . 
E 5 HOH 58  558 23  HOH HOH A . 
E 5 HOH 59  559 103 HOH HOH A . 
E 5 HOH 60  560 225 HOH HOH A . 
E 5 HOH 61  561 174 HOH HOH A . 
E 5 HOH 62  562 223 HOH HOH A . 
E 5 HOH 63  563 33  HOH HOH A . 
E 5 HOH 64  564 214 HOH HOH A . 
E 5 HOH 65  565 107 HOH HOH A . 
E 5 HOH 66  566 285 HOH HOH A . 
E 5 HOH 67  567 273 HOH HOH A . 
E 5 HOH 68  568 138 HOH HOH A . 
E 5 HOH 69  569 50  HOH HOH A . 
E 5 HOH 70  570 310 HOH HOH A . 
E 5 HOH 71  571 98  HOH HOH A . 
E 5 HOH 72  572 157 HOH HOH A . 
E 5 HOH 73  573 106 HOH HOH A . 
E 5 HOH 74  574 302 HOH HOH A . 
E 5 HOH 75  575 59  HOH HOH A . 
E 5 HOH 76  576 247 HOH HOH A . 
E 5 HOH 77  577 43  HOH HOH A . 
E 5 HOH 78  578 428 HOH HOH A . 
E 5 HOH 79  579 36  HOH HOH A . 
E 5 HOH 80  580 194 HOH HOH A . 
E 5 HOH 81  581 216 HOH HOH A . 
E 5 HOH 82  582 227 HOH HOH A . 
E 5 HOH 83  583 209 HOH HOH A . 
E 5 HOH 84  584 137 HOH HOH A . 
E 5 HOH 85  585 57  HOH HOH A . 
E 5 HOH 86  586 127 HOH HOH A . 
E 5 HOH 87  587 158 HOH HOH A . 
E 5 HOH 88  588 264 HOH HOH A . 
E 5 HOH 89  589 432 HOH HOH A . 
E 5 HOH 90  590 238 HOH HOH A . 
E 5 HOH 91  591 104 HOH HOH A . 
E 5 HOH 92  592 8   HOH HOH A . 
E 5 HOH 93  593 293 HOH HOH A . 
E 5 HOH 94  594 215 HOH HOH A . 
E 5 HOH 95  595 346 HOH HOH A . 
E 5 HOH 96  596 30  HOH HOH A . 
E 5 HOH 97  597 5   HOH HOH A . 
E 5 HOH 98  598 29  HOH HOH A . 
E 5 HOH 99  599 119 HOH HOH A . 
E 5 HOH 100 600 61  HOH HOH A . 
E 5 HOH 101 601 435 HOH HOH A . 
E 5 HOH 102 602 113 HOH HOH A . 
E 5 HOH 103 603 171 HOH HOH A . 
E 5 HOH 104 604 357 HOH HOH A . 
E 5 HOH 105 605 99  HOH HOH A . 
E 5 HOH 106 606 19  HOH HOH A . 
E 5 HOH 107 607 168 HOH HOH A . 
E 5 HOH 108 608 218 HOH HOH A . 
E 5 HOH 109 609 162 HOH HOH A . 
E 5 HOH 110 610 28  HOH HOH A . 
E 5 HOH 111 611 15  HOH HOH A . 
E 5 HOH 112 612 11  HOH HOH A . 
E 5 HOH 113 613 224 HOH HOH A . 
E 5 HOH 114 614 34  HOH HOH A . 
E 5 HOH 115 615 135 HOH HOH A . 
E 5 HOH 116 616 331 HOH HOH A . 
E 5 HOH 117 617 58  HOH HOH A . 
E 5 HOH 118 618 197 HOH HOH A . 
E 5 HOH 119 619 186 HOH HOH A . 
E 5 HOH 120 620 259 HOH HOH A . 
E 5 HOH 121 621 270 HOH HOH A . 
E 5 HOH 122 622 110 HOH HOH A . 
E 5 HOH 123 623 100 HOH HOH A . 
E 5 HOH 124 624 254 HOH HOH A . 
E 5 HOH 125 625 16  HOH HOH A . 
E 5 HOH 126 626 222 HOH HOH A . 
E 5 HOH 127 627 37  HOH HOH A . 
E 5 HOH 128 628 47  HOH HOH A . 
E 5 HOH 129 629 236 HOH HOH A . 
E 5 HOH 130 630 313 HOH HOH A . 
E 5 HOH 131 631 14  HOH HOH A . 
E 5 HOH 132 632 324 HOH HOH A . 
E 5 HOH 133 633 13  HOH HOH A . 
E 5 HOH 134 634 41  HOH HOH A . 
E 5 HOH 135 635 180 HOH HOH A . 
E 5 HOH 136 636 315 HOH HOH A . 
E 5 HOH 137 637 269 HOH HOH A . 
E 5 HOH 138 638 284 HOH HOH A . 
E 5 HOH 139 639 78  HOH HOH A . 
E 5 HOH 140 640 133 HOH HOH A . 
E 5 HOH 141 641 244 HOH HOH A . 
E 5 HOH 142 642 27  HOH HOH A . 
E 5 HOH 143 643 205 HOH HOH A . 
E 5 HOH 144 644 26  HOH HOH A . 
E 5 HOH 145 645 398 HOH HOH A . 
E 5 HOH 146 646 38  HOH HOH A . 
E 5 HOH 147 647 213 HOH HOH A . 
E 5 HOH 148 648 63  HOH HOH A . 
E 5 HOH 149 649 56  HOH HOH A . 
E 5 HOH 150 650 352 HOH HOH A . 
E 5 HOH 151 651 79  HOH HOH A . 
E 5 HOH 152 652 68  HOH HOH A . 
E 5 HOH 153 653 160 HOH HOH A . 
E 5 HOH 154 654 90  HOH HOH A . 
E 5 HOH 155 655 24  HOH HOH A . 
E 5 HOH 156 656 396 HOH HOH A . 
E 5 HOH 157 657 18  HOH HOH A . 
E 5 HOH 158 658 409 HOH HOH A . 
E 5 HOH 159 659 232 HOH HOH A . 
E 5 HOH 160 660 40  HOH HOH A . 
E 5 HOH 161 661 3   HOH HOH A . 
E 5 HOH 162 662 9   HOH HOH A . 
E 5 HOH 163 663 7   HOH HOH A . 
E 5 HOH 164 664 337 HOH HOH A . 
E 5 HOH 165 665 120 HOH HOH A . 
E 5 HOH 166 666 48  HOH HOH A . 
E 5 HOH 167 667 359 HOH HOH A . 
E 5 HOH 168 668 83  HOH HOH A . 
E 5 HOH 169 669 280 HOH HOH A . 
E 5 HOH 170 670 275 HOH HOH A . 
E 5 HOH 171 671 364 HOH HOH A . 
E 5 HOH 172 672 169 HOH HOH A . 
E 5 HOH 173 673 262 HOH HOH A . 
E 5 HOH 174 674 140 HOH HOH A . 
E 5 HOH 175 675 52  HOH HOH A . 
E 5 HOH 176 676 189 HOH HOH A . 
E 5 HOH 177 677 73  HOH HOH A . 
E 5 HOH 178 678 267 HOH HOH A . 
E 5 HOH 179 679 85  HOH HOH A . 
E 5 HOH 180 680 251 HOH HOH A . 
E 5 HOH 181 681 32  HOH HOH A . 
E 5 HOH 182 682 184 HOH HOH A . 
E 5 HOH 183 683 156 HOH HOH A . 
E 5 HOH 184 684 246 HOH HOH A . 
E 5 HOH 185 685 320 HOH HOH A . 
E 5 HOH 186 686 358 HOH HOH A . 
E 5 HOH 187 687 376 HOH HOH A . 
E 5 HOH 188 688 45  HOH HOH A . 
E 5 HOH 189 689 69  HOH HOH A . 
E 5 HOH 190 690 93  HOH HOH A . 
E 5 HOH 191 691 4   HOH HOH A . 
E 5 HOH 192 692 228 HOH HOH A . 
E 5 HOH 193 693 290 HOH HOH A . 
E 5 HOH 194 694 131 HOH HOH A . 
E 5 HOH 195 695 102 HOH HOH A . 
E 5 HOH 196 696 122 HOH HOH A . 
E 5 HOH 197 697 413 HOH HOH A . 
E 5 HOH 198 698 86  HOH HOH A . 
E 5 HOH 199 699 6   HOH HOH A . 
E 5 HOH 200 700 394 HOH HOH A . 
E 5 HOH 201 701 65  HOH HOH A . 
E 5 HOH 202 702 368 HOH HOH A . 
E 5 HOH 203 703 206 HOH HOH A . 
E 5 HOH 204 704 123 HOH HOH A . 
E 5 HOH 205 705 2   HOH HOH A . 
E 5 HOH 206 706 240 HOH HOH A . 
E 5 HOH 207 707 278 HOH HOH A . 
E 5 HOH 208 708 114 HOH HOH A . 
E 5 HOH 209 709 142 HOH HOH A . 
E 5 HOH 210 710 161 HOH HOH A . 
E 5 HOH 211 711 146 HOH HOH A . 
E 5 HOH 212 712 53  HOH HOH A . 
E 5 HOH 213 713 62  HOH HOH A . 
E 5 HOH 214 714 39  HOH HOH A . 
E 5 HOH 215 715 66  HOH HOH A . 
E 5 HOH 216 716 21  HOH HOH A . 
E 5 HOH 217 717 148 HOH HOH A . 
E 5 HOH 218 718 283 HOH HOH A . 
E 5 HOH 219 719 351 HOH HOH A . 
E 5 HOH 220 720 51  HOH HOH A . 
E 5 HOH 221 721 375 HOH HOH A . 
E 5 HOH 222 722 89  HOH HOH A . 
E 5 HOH 223 723 403 HOH HOH A . 
E 5 HOH 224 724 336 HOH HOH A . 
E 5 HOH 225 725 230 HOH HOH A . 
E 5 HOH 226 726 291 HOH HOH A . 
E 5 HOH 227 727 326 HOH HOH A . 
E 5 HOH 228 728 141 HOH HOH A . 
E 5 HOH 229 729 42  HOH HOH A . 
E 5 HOH 230 730 124 HOH HOH A . 
E 5 HOH 231 731 416 HOH HOH A . 
E 5 HOH 232 732 159 HOH HOH A . 
E 5 HOH 233 733 287 HOH HOH A . 
E 5 HOH 234 734 150 HOH HOH A . 
E 5 HOH 235 735 64  HOH HOH A . 
E 5 HOH 236 736 67  HOH HOH A . 
E 5 HOH 237 737 105 HOH HOH A . 
E 5 HOH 238 738 152 HOH HOH A . 
E 5 HOH 239 739 386 HOH HOH A . 
E 5 HOH 240 740 12  HOH HOH A . 
E 5 HOH 241 741 303 HOH HOH A . 
E 5 HOH 242 742 410 HOH HOH A . 
E 5 HOH 243 743 300 HOH HOH A . 
E 5 HOH 244 744 117 HOH HOH A . 
E 5 HOH 245 745 318 HOH HOH A . 
E 5 HOH 246 746 297 HOH HOH A . 
E 5 HOH 247 747 134 HOH HOH A . 
E 5 HOH 248 748 187 HOH HOH A . 
E 5 HOH 249 749 178 HOH HOH A . 
E 5 HOH 250 750 172 HOH HOH A . 
E 5 HOH 251 751 203 HOH HOH A . 
E 5 HOH 252 752 195 HOH HOH A . 
E 5 HOH 253 753 92  HOH HOH A . 
E 5 HOH 254 754 94  HOH HOH A . 
E 5 HOH 255 755 163 HOH HOH A . 
E 5 HOH 256 756 207 HOH HOH A . 
E 5 HOH 257 757 229 HOH HOH A . 
E 5 HOH 258 758 149 HOH HOH A . 
E 5 HOH 259 759 147 HOH HOH A . 
E 5 HOH 260 760 231 HOH HOH A . 
E 5 HOH 261 761 75  HOH HOH A . 
E 5 HOH 262 762 250 HOH HOH A . 
E 5 HOH 263 763 91  HOH HOH A . 
E 5 HOH 264 764 220 HOH HOH A . 
E 5 HOH 265 765 35  HOH HOH A . 
E 5 HOH 266 766 84  HOH HOH A . 
E 5 HOH 267 767 44  HOH HOH A . 
E 5 HOH 268 768 380 HOH HOH A . 
E 5 HOH 269 769 112 HOH HOH A . 
E 5 HOH 270 770 418 HOH HOH A . 
E 5 HOH 271 771 88  HOH HOH A . 
E 5 HOH 272 772 22  HOH HOH A . 
E 5 HOH 273 773 363 HOH HOH A . 
E 5 HOH 274 774 191 HOH HOH A . 
E 5 HOH 275 775 417 HOH HOH A . 
E 5 HOH 276 776 314 HOH HOH A . 
E 5 HOH 277 777 427 HOH HOH A . 
E 5 HOH 278 778 74  HOH HOH A . 
E 5 HOH 279 779 248 HOH HOH A . 
E 5 HOH 280 780 198 HOH HOH A . 
E 5 HOH 281 781 350 HOH HOH A . 
E 5 HOH 282 782 266 HOH HOH A . 
E 5 HOH 283 783 201 HOH HOH A . 
E 5 HOH 284 784 306 HOH HOH A . 
E 5 HOH 285 785 25  HOH HOH A . 
E 5 HOH 286 786 342 HOH HOH A . 
E 5 HOH 287 787 406 HOH HOH A . 
E 5 HOH 288 788 319 HOH HOH A . 
E 5 HOH 289 789 397 HOH HOH A . 
E 5 HOH 290 790 71  HOH HOH A . 
E 5 HOH 291 791 272 HOH HOH A . 
E 5 HOH 292 792 233 HOH HOH A . 
E 5 HOH 293 793 54  HOH HOH A . 
E 5 HOH 294 794 312 HOH HOH A . 
E 5 HOH 295 795 294 HOH HOH A . 
E 5 HOH 296 796 176 HOH HOH A . 
E 5 HOH 297 797 367 HOH HOH A . 
E 5 HOH 298 798 296 HOH HOH A . 
E 5 HOH 299 799 249 HOH HOH A . 
E 5 HOH 300 800 173 HOH HOH A . 
E 5 HOH 301 801 265 HOH HOH A . 
E 5 HOH 302 802 260 HOH HOH A . 
E 5 HOH 303 803 399 HOH HOH A . 
E 5 HOH 304 804 400 HOH HOH A . 
E 5 HOH 305 805 143 HOH HOH A . 
E 5 HOH 306 806 393 HOH HOH A . 
E 5 HOH 307 807 253 HOH HOH A . 
E 5 HOH 308 808 125 HOH HOH A . 
E 5 HOH 309 809 268 HOH HOH A . 
E 5 HOH 310 810 335 HOH HOH A . 
E 5 HOH 311 811 369 HOH HOH A . 
E 5 HOH 312 812 345 HOH HOH A . 
E 5 HOH 313 813 301 HOH HOH A . 
E 5 HOH 314 814 338 HOH HOH A . 
E 5 HOH 315 815 279 HOH HOH A . 
E 5 HOH 316 816 202 HOH HOH A . 
E 5 HOH 317 817 390 HOH HOH A . 
E 5 HOH 318 818 288 HOH HOH A . 
E 5 HOH 319 819 348 HOH HOH A . 
E 5 HOH 320 820 370 HOH HOH A . 
E 5 HOH 321 821 415 HOH HOH A . 
E 5 HOH 322 822 204 HOH HOH A . 
E 5 HOH 323 823 208 HOH HOH A . 
E 5 HOH 324 824 192 HOH HOH A . 
E 5 HOH 325 825 322 HOH HOH A . 
E 5 HOH 326 826 299 HOH HOH A . 
E 5 HOH 327 827 423 HOH HOH A . 
E 5 HOH 328 828 389 HOH HOH A . 
E 5 HOH 329 829 116 HOH HOH A . 
E 5 HOH 330 830 420 HOH HOH A . 
E 5 HOH 331 831 286 HOH HOH A . 
E 5 HOH 332 832 307 HOH HOH A . 
E 5 HOH 333 833 404 HOH HOH A . 
E 5 HOH 334 834 372 HOH HOH A . 
E 5 HOH 335 835 144 HOH HOH A . 
E 5 HOH 336 836 378 HOH HOH A . 
E 5 HOH 337 837 334 HOH HOH A . 
E 5 HOH 338 838 419 HOH HOH A . 
E 5 HOH 339 839 243 HOH HOH A . 
E 5 HOH 340 840 366 HOH HOH A . 
E 5 HOH 341 841 387 HOH HOH A . 
E 5 HOH 342 842 200 HOH HOH A . 
E 5 HOH 343 843 317 HOH HOH A . 
E 5 HOH 344 844 360 HOH HOH A . 
E 5 HOH 345 845 217 HOH HOH A . 
E 5 HOH 346 846 382 HOH HOH A . 
E 5 HOH 347 847 392 HOH HOH A . 
E 5 HOH 348 848 277 HOH HOH A . 
E 5 HOH 349 849 429 HOH HOH A . 
E 5 HOH 350 850 356 HOH HOH A . 
E 5 HOH 351 851 97  HOH HOH A . 
E 5 HOH 352 852 362 HOH HOH A . 
E 5 HOH 353 853 412 HOH HOH A . 
E 5 HOH 354 854 190 HOH HOH A . 
E 5 HOH 355 855 383 HOH HOH A . 
E 5 HOH 356 856 374 HOH HOH A . 
E 5 HOH 357 857 328 HOH HOH A . 
E 5 HOH 358 858 151 HOH HOH A . 
E 5 HOH 359 859 166 HOH HOH A . 
E 5 HOH 360 860 332 HOH HOH A . 
E 5 HOH 361 861 276 HOH HOH A . 
E 5 HOH 362 862 165 HOH HOH A . 
E 5 HOH 363 863 271 HOH HOH A . 
E 5 HOH 364 864 414 HOH HOH A . 
E 5 HOH 365 865 329 HOH HOH A . 
E 5 HOH 366 866 129 HOH HOH A . 
E 5 HOH 367 867 136 HOH HOH A . 
E 5 HOH 368 868 295 HOH HOH A . 
E 5 HOH 369 869 434 HOH HOH A . 
E 5 HOH 370 870 402 HOH HOH A . 
E 5 HOH 371 871 361 HOH HOH A . 
E 5 HOH 372 872 344 HOH HOH A . 
E 5 HOH 373 873 305 HOH HOH A . 
E 5 HOH 374 874 154 HOH HOH A . 
E 5 HOH 375 875 421 HOH HOH A . 
E 5 HOH 376 876 436 HOH HOH A . 
E 5 HOH 377 877 128 HOH HOH A . 
E 5 HOH 378 878 327 HOH HOH A . 
E 5 HOH 379 879 241 HOH HOH A . 
E 5 HOH 380 880 252 HOH HOH A . 
E 5 HOH 381 881 381 HOH HOH A . 
E 5 HOH 382 882 212 HOH HOH A . 
E 5 HOH 383 883 430 HOH HOH A . 
E 5 HOH 384 884 211 HOH HOH A . 
E 5 HOH 385 885 237 HOH HOH A . 
E 5 HOH 386 886 239 HOH HOH A . 
E 5 HOH 387 887 292 HOH HOH A . 
E 5 HOH 388 888 353 HOH HOH A . 
E 5 HOH 389 889 210 HOH HOH A . 
E 5 HOH 390 890 395 HOH HOH A . 
E 5 HOH 391 891 111 HOH HOH A . 
E 5 HOH 392 892 407 HOH HOH A . 
E 5 HOH 393 893 132 HOH HOH A . 
E 5 HOH 394 894 256 HOH HOH A . 
E 5 HOH 395 895 234 HOH HOH A . 
E 5 HOH 396 896 130 HOH HOH A . 
E 5 HOH 397 897 182 HOH HOH A . 
E 5 HOH 398 898 377 HOH HOH A . 
E 5 HOH 399 899 365 HOH HOH A . 
E 5 HOH 400 900 316 HOH HOH A . 
E 5 HOH 401 901 373 HOH HOH A . 
E 5 HOH 402 902 60  HOH HOH A . 
E 5 HOH 403 903 255 HOH HOH A . 
E 5 HOH 404 904 235 HOH HOH A . 
E 5 HOH 405 905 411 HOH HOH A . 
E 5 HOH 406 906 226 HOH HOH A . 
E 5 HOH 407 907 76  HOH HOH A . 
E 5 HOH 408 908 330 HOH HOH A . 
E 5 HOH 409 909 170 HOH HOH A . 
E 5 HOH 410 910 304 HOH HOH A . 
E 5 HOH 411 911 408 HOH HOH A . 
E 5 HOH 412 912 401 HOH HOH A . 
E 5 HOH 413 913 139 HOH HOH A . 
E 5 HOH 414 914 321 HOH HOH A . 
E 5 HOH 415 915 155 HOH HOH A . 
E 5 HOH 416 916 349 HOH HOH A . 
E 5 HOH 417 917 388 HOH HOH A . 
E 5 HOH 418 918 354 HOH HOH A . 
E 5 HOH 419 919 274 HOH HOH A . 
E 5 HOH 420 920 379 HOH HOH A . 
E 5 HOH 421 921 164 HOH HOH A . 
E 5 HOH 422 922 355 HOH HOH A . 
E 5 HOH 423 923 391 HOH HOH A . 
E 5 HOH 424 924 384 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 20  ? CG  ? A LYS 26  CG  
2  1 Y 1 A LYS 20  ? CD  ? A LYS 26  CD  
3  1 Y 1 A LYS 20  ? CE  ? A LYS 26  CE  
4  1 Y 1 A LYS 20  ? NZ  ? A LYS 26  NZ  
5  1 Y 1 A LYS 83  ? CG  ? A LYS 89  CG  
6  1 Y 1 A LYS 83  ? CD  ? A LYS 89  CD  
7  1 Y 1 A LYS 83  ? CE  ? A LYS 89  CE  
8  1 Y 1 A LYS 83  ? NZ  ? A LYS 89  NZ  
9  1 Y 1 A GLU 116 ? CG  ? A GLU 122 CG  
10 1 Y 1 A GLU 116 ? CD  ? A GLU 122 CD  
11 1 Y 1 A GLU 116 ? OE1 ? A GLU 122 OE1 
12 1 Y 1 A GLU 116 ? OE2 ? A GLU 122 OE2 
13 1 Y 1 A ARG 136 ? CG  ? A ARG 142 CG  
14 1 Y 1 A ARG 136 ? CD  ? A ARG 142 CD  
15 1 Y 1 A ARG 136 ? NE  ? A ARG 142 NE  
16 1 Y 1 A ARG 136 ? CZ  ? A ARG 142 CZ  
17 1 Y 1 A ARG 136 ? NH1 ? A ARG 142 NH1 
18 1 Y 1 A ARG 136 ? NH2 ? A ARG 142 NH2 
19 1 Y 1 A ARG 169 ? CG  ? A ARG 175 CG  
20 1 Y 1 A ARG 169 ? CD  ? A ARG 175 CD  
21 1 Y 1 A ARG 169 ? NE  ? A ARG 175 NE  
22 1 Y 1 A ARG 169 ? CZ  ? A ARG 175 CZ  
23 1 Y 1 A ARG 169 ? NH1 ? A ARG 175 NH1 
24 1 Y 1 A ARG 169 ? NH2 ? A ARG 175 NH2 
25 1 Y 1 A ASP 243 ? CG  ? A ASP 249 CG  
26 1 Y 1 A ASP 243 ? OD1 ? A ASP 249 OD1 
27 1 Y 1 A ASP 243 ? OD2 ? A ASP 249 OD2 
28 1 Y 1 A MET 248 ? CG  ? A MET 254 CG  
29 1 Y 1 A MET 248 ? SD  ? A MET 254 SD  
30 1 Y 1 A MET 248 ? CE  ? A MET 254 CE  
31 1 Y 1 A SER 297 ? OG  ? A SER 303 OG  
32 1 Y 1 A GLU 298 ? CG  ? A GLU 304 CG  
33 1 Y 1 A GLU 298 ? CD  ? A GLU 304 CD  
34 1 Y 1 A GLU 298 ? OE1 ? A GLU 304 OE1 
35 1 Y 1 A GLU 298 ? OE2 ? A GLU 304 OE2 
36 1 Y 1 A GLU 299 ? CG  ? A GLU 305 CG  
37 1 Y 1 A GLU 299 ? CD  ? A GLU 305 CD  
38 1 Y 1 A GLU 299 ? OE1 ? A GLU 305 OE1 
39 1 Y 1 A GLU 299 ? OE2 ? A GLU 305 OE2 
40 1 Y 1 A GLU 300 ? CG  ? A GLU 306 CG  
41 1 Y 1 A GLU 300 ? CD  ? A GLU 306 CD  
42 1 Y 1 A GLU 300 ? OE1 ? A GLU 306 OE1 
43 1 Y 1 A GLU 300 ? OE2 ? A GLU 306 OE2 
44 1 Y 1 A GLU 301 ? CG  ? A GLU 307 CG  
45 1 Y 1 A GLU 301 ? CD  ? A GLU 307 CD  
46 1 Y 1 A GLU 301 ? OE1 ? A GLU 307 OE1 
47 1 Y 1 A GLU 301 ? OE2 ? A GLU 307 OE2 
48 1 Y 1 A GLU 325 ? CG  ? A GLU 331 CG  
49 1 Y 1 A GLU 325 ? CD  ? A GLU 331 CD  
50 1 Y 1 A GLU 325 ? OE1 ? A GLU 331 OE1 
51 1 Y 1 A GLU 325 ? OE2 ? A GLU 331 OE2 
52 1 Y 1 A GLU 329 ? CG  ? A GLU 335 CG  
53 1 Y 1 A GLU 329 ? CD  ? A GLU 335 CD  
54 1 Y 1 A GLU 329 ? OE1 ? A GLU 335 OE1 
55 1 Y 1 A GLU 329 ? OE2 ? A GLU 335 OE2 
56 1 Y 1 A GLN 385 ? CG  ? A GLN 391 CG  
57 1 Y 1 A GLN 385 ? CD  ? A GLN 391 CD  
58 1 Y 1 A GLN 385 ? OE1 ? A GLN 391 OE1 
59 1 Y 1 A GLN 385 ? NE2 ? A GLN 391 NE2 
60 1 N 1 A NAP 402 ? C5D ? C NAP 1   C5D 
61 1 N 1 A NAP 402 ? C4D ? C NAP 1   C4D 
62 1 N 1 A NAP 402 ? O4D ? C NAP 1   O4D 
63 1 N 1 A NAP 402 ? C3D ? C NAP 1   C3D 
64 1 N 1 A NAP 402 ? O3D ? C NAP 1   O3D 
65 1 N 1 A NAP 402 ? C2D ? C NAP 1   C2D 
66 1 N 1 A NAP 402 ? O2D ? C NAP 1   O2D 
67 1 N 1 A NAP 402 ? C1D ? C NAP 1   C1D 
68 1 N 1 A NAP 402 ? N1N ? C NAP 1   N1N 
69 1 N 1 A NAP 402 ? C2N ? C NAP 1   C2N 
70 1 N 1 A NAP 402 ? C3N ? C NAP 1   C3N 
71 1 N 1 A NAP 402 ? C7N ? C NAP 1   C7N 
72 1 N 1 A NAP 402 ? O7N ? C NAP 1   O7N 
73 1 N 1 A NAP 402 ? N7N ? C NAP 1   N7N 
74 1 N 1 A NAP 402 ? C4N ? C NAP 1   C4N 
75 1 N 1 A NAP 402 ? C5N ? C NAP 1   C5N 
76 1 N 1 A NAP 402 ? C6N ? C NAP 1   C6N 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? dev_4761 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? dev_4761 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QNA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     88.250 
_cell.length_a_esd                 ? 
_cell.length_b                     90.330 
_cell.length_b_esd                 ? 
_cell.length_c                     49.170 
_cell.length_c_esd                 ? 
_cell.volume                       391964.678 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8QNA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8QNA 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.38 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Tris-HCl, 50 mM sodium tartrate, 18% PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-03-19 
_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   1.0332 
_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                        'PETRA III, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          18.74 
_reflns.entry_id                                       8QNA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               49.17 
_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                                     62151 
_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                           97.54 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.41 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_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                                    1.5 
_reflns_shell.d_res_low                                     1.52 
_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                             62149 
_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                               ? 
_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                                  0.281 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               21.56 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8QNA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.50 
_refine.ls_d_res_low                             49.17 
_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                     62151 
_refine.ls_number_reflns_R_free                  3108 
_refine.ls_number_reflns_R_work                  59043 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.55 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1559 
_refine.ls_R_factor_R_free                       0.1938 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1539 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 18.9783 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2031 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        49.17 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               3265 
_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        2772 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_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' ? 0.0078  ? 2922 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0398  ? 3990 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0579  ? 440  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0104  ? 509  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.6959 ? 1038 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.50 1.52  . . 119 2269 83.55 . . . . 0.3120 . . . . . . . . . . . 0.3391 
'X-RAY DIFFRACTION' 1.52 1.55  . . 134 2541 93.86 . . . . 0.2890 . . . . . . . . . . . 0.3268 
'X-RAY DIFFRACTION' 1.55 1.58  . . 139 2648 97.28 . . . . 0.2589 . . . . . . . . . . . 0.3189 
'X-RAY DIFFRACTION' 1.58 1.60  . . 140 2643 97.58 . . . . 0.2378 . . . . . . . . . . . 0.2842 
'X-RAY DIFFRACTION' 1.60 1.63  . . 140 2670 97.67 . . . . 0.2129 . . . . . . . . . . . 0.2840 
'X-RAY DIFFRACTION' 1.63 1.67  . . 139 2635 97.88 . . . . 0.2052 . . . . . . . . . . . 0.2808 
'X-RAY DIFFRACTION' 1.67 1.70  . . 142 2692 97.99 . . . . 0.1913 . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 1.70 1.74  . . 140 2670 98.42 . . . . 0.1780 . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 1.74 1.79  . . 139 2650 98.41 . . . . 0.1779 . . . . . . . . . . . 0.2272 
'X-RAY DIFFRACTION' 1.79 1.84  . . 143 2717 98.38 . . . . 0.1687 . . . . . . . . . . . 0.2260 
'X-RAY DIFFRACTION' 1.84 1.89  . . 139 2635 96.59 . . . . 0.1740 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 1.89 1.95  . . 141 2672 98.36 . . . . 0.1541 . . . . . . . . . . . 0.2157 
'X-RAY DIFFRACTION' 1.95 2.02  . . 143 2711 98.79 . . . . 0.1396 . . . . . . . . . . . 0.2252 
'X-RAY DIFFRACTION' 2.02 2.10  . . 142 2707 98.65 . . . . 0.1309 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 2.10 2.20  . . 143 2713 99.20 . . . . 0.1305 . . . . . . . . . . . 0.1891 
'X-RAY DIFFRACTION' 2.20 2.31  . . 143 2729 99.17 . . . . 0.1232 . . . . . . . . . . . 0.1765 
'X-RAY DIFFRACTION' 2.31 2.46  . . 146 2766 99.52 . . . . 0.1303 . . . . . . . . . . . 0.1761 
'X-RAY DIFFRACTION' 2.46 2.65  . . 142 2694 98.40 . . . . 0.1423 . . . . . . . . . . . 0.1759 
'X-RAY DIFFRACTION' 2.65 2.91  . . 145 2755 98.24 . . . . 0.1471 . . . . . . . . . . . 0.1869 
'X-RAY DIFFRACTION' 2.91 3.34  . . 146 2781 99.69 . . . . 0.1446 . . . . . . . . . . . 0.1575 
'X-RAY DIFFRACTION' 3.34 4.20  . . 149 2819 99.73 . . . . 0.1364 . . . . . . . . . . . 0.1631 
'X-RAY DIFFRACTION' 4.20 49.17 . . 154 2926 98.43 . . . . 0.1561 . . . . . . . . . . . 0.1728 
# 
_struct.entry_id                     8QNA 
_struct.title                        'OPR3 variant - R366A' 
_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        8QNA 
_struct_keywords.text            'Old Yellow Enzyme, ene-reductase, flavoenzyme, oxidoreductase, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    OPR3_SOLLC 
_struct_ref.pdbx_db_accession          Q9FEW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGFPHVPGI
FTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEI
SQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRVGVRVSP
AIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_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              8QNA 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 7 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 402 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9FEW9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  396 
_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       396 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8QNA HIS A 1   ? UNP Q9FEW9 ?   ?   'expression tag'      -5  1 
1 8QNA HIS A 2   ? UNP Q9FEW9 ?   ?   'expression tag'      -4  2 
1 8QNA HIS A 3   ? UNP Q9FEW9 ?   ?   'expression tag'      -3  3 
1 8QNA HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'      -2  4 
1 8QNA HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'      -1  5 
1 8QNA HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'      0   6 
1 8QNA ALA A 372 ? UNP Q9FEW9 ARG 366 'engineered mutation' 366 7 
# 
_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 
# 
_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 ASN A 16  ? SER A 20  ? ASN A 10  SER A 14  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 43  ? ILE A 47  ? ALA A 37  ILE A 41  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 49  ? ALA A 60  ? GLN A 43  ALA A 54  1 ? 12 
HELX_P HELX_P4  AA4 THR A 88  ? LYS A 105 ? THR A 82  LYS A 99  1 ? 18 
HELX_P HELX_P5  AA5 HIS A 121 ? ALA A 129 ? HIS A 115 ALA A 123 5 ? 9  
HELX_P HELX_P6  AA6 GLY A 162 ? ALA A 183 ? GLY A 156 ALA A 177 1 ? 22 
HELX_P HELX_P7  AA7 TYR A 196 ? LYS A 203 ? TYR A 190 LYS A 197 1 ? 8  
HELX_P HELX_P8  AA8 SER A 216 ? CYS A 221 ? SER A 210 CYS A 215 1 ? 6  
HELX_P HELX_P9  AA9 CYS A 221 ? GLY A 236 ? CYS A 215 GLY A 230 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 257 ? GLY A 277 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P11 AB2 GLU A 304 ? TYR A 318 ? GLU A 298 TYR A 312 1 ? 15 
HELX_P HELX_P12 AB3 THR A 329 ? GLN A 339 ? THR A 323 GLN A 333 1 ? 11 
HELX_P HELX_P13 AB4 GLY A 348 ? ASN A 354 ? GLY A 342 ASN A 348 1 ? 7  
HELX_P HELX_P14 AB5 ASP A 356 ? ASN A 364 ? ASP A 350 ASN A 358 1 ? 9  
HELX_P HELX_P15 AB6 ASN A 371 ? PHE A 375 ? ASN A 365 PHE A 369 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 22  ? MET A 24  ? TYR A 16  MET A 18  
AA1 2 PHE A 27  ? LEU A 29  ? PHE A 21  LEU A 23  
AA2 1 VAL A 33  ? LEU A 35  ? VAL A 27  LEU A 29  
AA2 2 PHE A 65  ? MET A 72  ? PHE A 59  MET A 66  
AA2 3 VAL A 108 ? TRP A 114 ? VAL A 102 TRP A 108 
AA2 4 GLY A 187 ? GLY A 192 ? GLY A 181 GLY A 186 
AA2 5 VAL A 240 ? VAL A 244 ? VAL A 234 VAL A 238 
AA2 6 TYR A 282 ? THR A 286 ? TYR A 276 THR A 280 
AA2 7 PHE A 322 ? SER A 325 ? PHE A 316 SER A 319 
AA2 8 LEU A 344 ? TYR A 347 ? LEU A 338 TYR A 341 
AA2 9 VAL A 33  ? LEU A 35  ? VAL A 27  LEU A 29  
AA3 1 ILE A 132 ? SER A 133 ? ILE A 126 SER A 127 
AA3 2 ARG A 159 ? ALA A 160 ? ARG A 153 ALA A 154 
AA4 1 ILE A 145 ? LEU A 146 ? ILE A 139 LEU A 140 
AA4 2 HIS A 152 ? GLY A 153 ? HIS A 146 GLY A 147 
# 
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 TYR A 22  ? N TYR A 16  O LEU A 29  ? O LEU A 23  
AA2 1 2 N LEU A 35  ? N LEU A 29  O PHE A 65  ? O PHE A 59  
AA2 2 3 N THR A 71  ? N THR A 65  O TRP A 114 ? O TRP A 108 
AA2 3 4 N LEU A 113 ? N LEU A 107 O GLU A 189 ? O GLU A 183 
AA2 4 5 N ILE A 190 ? N ILE A 184 O GLY A 241 ? O GLY A 235 
AA2 5 6 N VAL A 242 ? N VAL A 236 O HIS A 284 ? O HIS A 278 
AA2 6 7 N LEU A 283 ? N LEU A 277 O ILE A 323 ? O ILE A 317 
AA2 7 8 N CYS A 324 ? N CYS A 318 O SER A 346 ? O SER A 340 
AA2 8 9 O VAL A 345 ? O VAL A 339 N VAL A 34  ? N VAL A 28  
AA3 1 2 N SER A 133 ? N SER A 127 O ARG A 159 ? O ARG A 153 
AA4 1 2 N ILE A 145 ? N ILE A 139 O GLY A 153 ? O GLY A 147 
# 
_pdbx_entry_details.entry_id                   8QNA 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 686 ? ? O A HOH 789 ? ? 2.11 
2 1 O A HOH 502 ? ? O A HOH 658 ? ? 2.13 
3 1 O A HOH 789 ? ? O A HOH 806 ? ? 2.19 
4 1 O A HOH 748 ? ? O A HOH 792 ? ? 2.19 
# 
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 GLU A 63  ? ? -46.91  151.46 
2 1 ILE A 80  ? ? -141.15 32.69  
3 1 ALA A 121 ? ? 56.35   19.95  
4 1 SER A 239 ? ? -151.72 71.66  
5 1 ALA A 247 ? ? -105.46 63.44  
6 1 ASP A 350 ? ? -96.77  41.99  
7 1 VAL A 375 ? ? -121.66 -54.22 
8 1 TYR A 378 ? ? -131.03 -61.17 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
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 HIS -5  ? A HIS 1   
2  1 Y 1 A HIS -4  ? A HIS 2   
3  1 Y 1 A HIS -3  ? A HIS 3   
4  1 Y 1 A HIS -2  ? A HIS 4   
5  1 Y 1 A HIS -1  ? A HIS 5   
6  1 Y 1 A HIS 0   ? A HIS 6   
7  1 Y 1 A MET 1   ? A MET 7   
8  1 Y 1 A ALA 2   ? A ALA 8   
9  1 Y 1 A SER 3   ? A SER 9   
10 1 Y 1 A SER 4   ? A SER 10  
11 1 Y 1 A ALA 5   ? A ALA 11  
12 1 Y 1 A GLN 6   ? A GLN 12  
13 1 Y 1 A ASP 7   ? A ASP 13  
14 1 Y 1 A GLY 8   ? A GLY 14  
15 1 Y 1 A ASN 9   ? A ASN 15  
16 1 Y 1 A TYR 284 ? A TYR 290 
17 1 Y 1 A VAL 285 ? A VAL 291 
18 1 Y 1 A ALA 286 ? A ALA 292 
19 1 Y 1 A TYR 287 ? A TYR 293 
20 1 Y 1 A GLY 288 ? A GLY 294 
21 1 Y 1 A GLN 289 ? A GLN 295 
22 1 Y 1 A THR 290 ? A THR 296 
23 1 Y 1 A GLU 291 ? A GLU 297 
24 1 Y 1 A ALA 292 ? A ALA 298 
25 1 Y 1 A GLY 293 ? A GLY 299 
26 1 Y 1 A ARG 294 ? A ARG 300 
27 1 Y 1 A LEU 295 ? A LEU 301 
28 1 Y 1 A GLY 296 ? A GLY 302 
29 1 Y 1 A GLY 386 ? A GLY 392 
30 1 Y 1 A ASN 387 ? A ASN 393 
31 1 Y 1 A GLY 388 ? A GLY 394 
32 1 Y 1 A SER 389 ? A SER 395 
33 1 Y 1 A ASN 390 ? A ASN 396 
34 1 Y 1 A GLY 391 ? A GLY 397 
35 1 Y 1 A PRO 392 ? A PRO 398 
36 1 Y 1 A LEU 393 ? A LEU 399 
37 1 Y 1 A SER 394 ? A SER 400 
38 1 Y 1 A ARG 395 ? A ARG 401 
39 1 Y 1 A LEU 396 ? A LEU 402 
# 
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  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FMN N1     N N N 88  
FMN C2     C N N 89  
FMN O2     O N N 90  
FMN N3     N N N 91  
FMN C4     C N N 92  
FMN O4     O N N 93  
FMN C4A    C N N 94  
FMN N5     N N N 95  
FMN C5A    C Y N 96  
FMN C6     C Y N 97  
FMN C7     C Y N 98  
FMN C7M    C N N 99  
FMN C8     C Y N 100 
FMN C8M    C N N 101 
FMN C9     C Y N 102 
FMN C9A    C Y N 103 
FMN N10    N N N 104 
FMN C10    C N N 105 
FMN "C1'"  C N N 106 
FMN "C2'"  C N S 107 
FMN "O2'"  O N N 108 
FMN "C3'"  C N S 109 
FMN "O3'"  O N N 110 
FMN "C4'"  C N R 111 
FMN "O4'"  O N N 112 
FMN "C5'"  C N N 113 
FMN "O5'"  O N N 114 
FMN P      P N N 115 
FMN O1P    O N N 116 
FMN O2P    O N N 117 
FMN O3P    O N N 118 
FMN HN3    H N N 119 
FMN H6     H N N 120 
FMN HM71   H N N 121 
FMN HM72   H N N 122 
FMN HM73   H N N 123 
FMN HM81   H N N 124 
FMN HM82   H N N 125 
FMN HM83   H N N 126 
FMN H9     H N N 127 
FMN "H1'1" H N N 128 
FMN "H1'2" H N N 129 
FMN "H2'"  H N N 130 
FMN "HO2'" H N N 131 
FMN "H3'"  H N N 132 
FMN "HO3'" H N N 133 
FMN "H4'"  H N N 134 
FMN "HO4'" H N N 135 
FMN "H5'1" H N N 136 
FMN "H5'2" H N N 137 
FMN HOP2   H N N 138 
FMN HOP3   H N N 139 
GLN N      N N N 140 
GLN CA     C N S 141 
GLN C      C N N 142 
GLN O      O N N 143 
GLN CB     C N N 144 
GLN CG     C N N 145 
GLN CD     C N N 146 
GLN OE1    O N N 147 
GLN NE2    N N N 148 
GLN OXT    O N N 149 
GLN H      H N N 150 
GLN H2     H N N 151 
GLN HA     H N N 152 
GLN HB2    H N N 153 
GLN HB3    H N N 154 
GLN HG2    H N N 155 
GLN HG3    H N N 156 
GLN HE21   H N N 157 
GLN HE22   H N N 158 
GLN HXT    H N N 159 
GLU N      N N N 160 
GLU CA     C N S 161 
GLU C      C N N 162 
GLU O      O N N 163 
GLU CB     C N N 164 
GLU CG     C N N 165 
GLU CD     C N N 166 
GLU OE1    O N N 167 
GLU OE2    O N N 168 
GLU OXT    O N N 169 
GLU H      H N N 170 
GLU H2     H N N 171 
GLU HA     H N N 172 
GLU HB2    H N N 173 
GLU HB3    H N N 174 
GLU HG2    H N N 175 
GLU HG3    H N N 176 
GLU HE2    H N N 177 
GLU HXT    H N N 178 
GLY N      N N N 179 
GLY CA     C N N 180 
GLY C      C N N 181 
GLY O      O N N 182 
GLY OXT    O N N 183 
GLY H      H N N 184 
GLY H2     H N N 185 
GLY HA2    H N N 186 
GLY HA3    H N N 187 
GLY HXT    H N N 188 
HIS N      N N N 189 
HIS CA     C N S 190 
HIS C      C N N 191 
HIS O      O N N 192 
HIS CB     C N N 193 
HIS CG     C Y N 194 
HIS ND1    N Y N 195 
HIS CD2    C Y N 196 
HIS CE1    C Y N 197 
HIS NE2    N Y N 198 
HIS OXT    O N N 199 
HIS H      H N N 200 
HIS H2     H N N 201 
HIS HA     H N N 202 
HIS HB2    H N N 203 
HIS HB3    H N N 204 
HIS HD1    H N N 205 
HIS HD2    H N N 206 
HIS HE1    H N N 207 
HIS HE2    H N N 208 
HIS HXT    H N N 209 
HOH O      O N N 210 
HOH H1     H N N 211 
HOH H2     H N N 212 
ILE N      N N N 213 
ILE CA     C N S 214 
ILE C      C N N 215 
ILE O      O N N 216 
ILE CB     C N S 217 
ILE CG1    C N N 218 
ILE CG2    C N N 219 
ILE CD1    C N N 220 
ILE OXT    O N N 221 
ILE H      H N N 222 
ILE H2     H N N 223 
ILE HA     H N N 224 
ILE HB     H N N 225 
ILE HG12   H N N 226 
ILE HG13   H N N 227 
ILE HG21   H N N 228 
ILE HG22   H N N 229 
ILE HG23   H N N 230 
ILE HD11   H N N 231 
ILE HD12   H N N 232 
ILE HD13   H N N 233 
ILE HXT    H N N 234 
LEU N      N N N 235 
LEU CA     C N S 236 
LEU C      C N N 237 
LEU O      O N N 238 
LEU CB     C N N 239 
LEU CG     C N N 240 
LEU CD1    C N N 241 
LEU CD2    C N N 242 
LEU OXT    O N N 243 
LEU H      H N N 244 
LEU H2     H N N 245 
LEU HA     H N N 246 
LEU HB2    H N N 247 
LEU HB3    H N N 248 
LEU HG     H N N 249 
LEU HD11   H N N 250 
LEU HD12   H N N 251 
LEU HD13   H N N 252 
LEU HD21   H N N 253 
LEU HD22   H N N 254 
LEU HD23   H N N 255 
LEU HXT    H N N 256 
LYS N      N N N 257 
LYS CA     C N S 258 
LYS C      C N N 259 
LYS O      O N N 260 
LYS CB     C N N 261 
LYS CG     C N N 262 
LYS CD     C N N 263 
LYS CE     C N N 264 
LYS NZ     N N N 265 
LYS OXT    O N N 266 
LYS H      H N N 267 
LYS H2     H N N 268 
LYS HA     H N N 269 
LYS HB2    H N N 270 
LYS HB3    H N N 271 
LYS HG2    H N N 272 
LYS HG3    H N N 273 
LYS HD2    H N N 274 
LYS HD3    H N N 275 
LYS HE2    H N N 276 
LYS HE3    H N N 277 
LYS HZ1    H N N 278 
LYS HZ2    H N N 279 
LYS HZ3    H N N 280 
LYS HXT    H N N 281 
MET N      N N N 282 
MET CA     C N S 283 
MET C      C N N 284 
MET O      O N N 285 
MET CB     C N N 286 
MET CG     C N N 287 
MET SD     S N N 288 
MET CE     C N N 289 
MET OXT    O N N 290 
MET H      H N N 291 
MET H2     H N N 292 
MET HA     H N N 293 
MET HB2    H N N 294 
MET HB3    H N N 295 
MET HG2    H N N 296 
MET HG3    H N N 297 
MET HE1    H N N 298 
MET HE2    H N N 299 
MET HE3    H N N 300 
MET HXT    H N N 301 
NAP PA     P N R 302 
NAP O1A    O N N 303 
NAP O2A    O N N 304 
NAP O5B    O N N 305 
NAP C5B    C N N 306 
NAP C4B    C N R 307 
NAP O4B    O N N 308 
NAP C3B    C N R 309 
NAP O3B    O N N 310 
NAP C2B    C N R 311 
NAP O2B    O N N 312 
NAP C1B    C N R 313 
NAP N9A    N Y N 314 
NAP C8A    C Y N 315 
NAP N7A    N Y N 316 
NAP C5A    C Y N 317 
NAP C6A    C Y N 318 
NAP N6A    N N N 319 
NAP N1A    N Y N 320 
NAP C2A    C Y N 321 
NAP N3A    N Y N 322 
NAP C4A    C Y N 323 
NAP O3     O N N 324 
NAP PN     P N N 325 
NAP O1N    O N N 326 
NAP O2N    O N N 327 
NAP O5D    O N N 328 
NAP C5D    C N N 329 
NAP C4D    C N R 330 
NAP O4D    O N N 331 
NAP C3D    C N S 332 
NAP O3D    O N N 333 
NAP C2D    C N R 334 
NAP O2D    O N N 335 
NAP C1D    C N R 336 
NAP N1N    N Y N 337 
NAP C2N    C Y N 338 
NAP C3N    C Y N 339 
NAP C7N    C N N 340 
NAP O7N    O N N 341 
NAP N7N    N N N 342 
NAP C4N    C Y N 343 
NAP C5N    C Y N 344 
NAP C6N    C Y N 345 
NAP P2B    P N N 346 
NAP O1X    O N N 347 
NAP O2X    O N N 348 
NAP O3X    O N N 349 
NAP HOA2   H N N 350 
NAP H51A   H N N 351 
NAP H52A   H N N 352 
NAP H4B    H N N 353 
NAP H3B    H N N 354 
NAP HO3A   H N N 355 
NAP H2B    H N N 356 
NAP H1B    H N N 357 
NAP H8A    H N N 358 
NAP H61A   H N N 359 
NAP H62A   H N N 360 
NAP H2A    H N N 361 
NAP H51N   H N N 362 
NAP H52N   H N N 363 
NAP H4D    H N N 364 
NAP H3D    H N N 365 
NAP HO3N   H N N 366 
NAP H2D    H N N 367 
NAP HO2N   H N N 368 
NAP H1D    H N N 369 
NAP H2N    H N N 370 
NAP H71N   H N N 371 
NAP H72N   H N N 372 
NAP H4N    H N N 373 
NAP H5N    H N N 374 
NAP H6N    H N N 375 
NAP HOP2   H N N 376 
NAP HOP3   H N N 377 
PHE N      N N N 378 
PHE CA     C N S 379 
PHE C      C N N 380 
PHE O      O N N 381 
PHE CB     C N N 382 
PHE CG     C Y N 383 
PHE CD1    C Y N 384 
PHE CD2    C Y N 385 
PHE CE1    C Y N 386 
PHE CE2    C Y N 387 
PHE CZ     C Y N 388 
PHE OXT    O N N 389 
PHE H      H N N 390 
PHE H2     H N N 391 
PHE HA     H N N 392 
PHE HB2    H N N 393 
PHE HB3    H N N 394 
PHE HD1    H N N 395 
PHE HD2    H N N 396 
PHE HE1    H N N 397 
PHE HE2    H N N 398 
PHE HZ     H N N 399 
PHE HXT    H N N 400 
PRO N      N N N 401 
PRO CA     C N S 402 
PRO C      C N N 403 
PRO O      O N N 404 
PRO CB     C N N 405 
PRO CG     C N N 406 
PRO CD     C N N 407 
PRO OXT    O N N 408 
PRO H      H N N 409 
PRO HA     H N N 410 
PRO HB2    H N N 411 
PRO HB3    H N N 412 
PRO HG2    H N N 413 
PRO HG3    H N N 414 
PRO HD2    H N N 415 
PRO HD3    H N N 416 
PRO HXT    H N N 417 
SER N      N N N 418 
SER CA     C N S 419 
SER C      C N N 420 
SER O      O N N 421 
SER CB     C N N 422 
SER OG     O N N 423 
SER OXT    O N N 424 
SER H      H N N 425 
SER H2     H N N 426 
SER HA     H N N 427 
SER HB2    H N N 428 
SER HB3    H N N 429 
SER HG     H N N 430 
SER HXT    H N N 431 
SO4 S      S N N 432 
SO4 O1     O N N 433 
SO4 O2     O N N 434 
SO4 O3     O N N 435 
SO4 O4     O N N 436 
THR N      N N N 437 
THR CA     C N S 438 
THR C      C N N 439 
THR O      O N N 440 
THR CB     C N R 441 
THR OG1    O N N 442 
THR CG2    C N N 443 
THR OXT    O N N 444 
THR H      H N N 445 
THR H2     H N N 446 
THR HA     H N N 447 
THR HB     H N N 448 
THR HG1    H N N 449 
THR HG21   H N N 450 
THR HG22   H N N 451 
THR HG23   H N N 452 
THR HXT    H N N 453 
TRP N      N N N 454 
TRP CA     C N S 455 
TRP C      C N N 456 
TRP O      O N N 457 
TRP CB     C N N 458 
TRP CG     C Y N 459 
TRP CD1    C Y N 460 
TRP CD2    C Y N 461 
TRP NE1    N Y N 462 
TRP CE2    C Y N 463 
TRP CE3    C Y N 464 
TRP CZ2    C Y N 465 
TRP CZ3    C Y N 466 
TRP CH2    C Y N 467 
TRP OXT    O N N 468 
TRP H      H N N 469 
TRP H2     H N N 470 
TRP HA     H N N 471 
TRP HB2    H N N 472 
TRP HB3    H N N 473 
TRP HD1    H N N 474 
TRP HE1    H N N 475 
TRP HE3    H N N 476 
TRP HZ2    H N N 477 
TRP HZ3    H N N 478 
TRP HH2    H N N 479 
TRP HXT    H N N 480 
TYR N      N N N 481 
TYR CA     C N S 482 
TYR C      C N N 483 
TYR O      O N N 484 
TYR CB     C N N 485 
TYR CG     C Y N 486 
TYR CD1    C Y N 487 
TYR CD2    C Y N 488 
TYR CE1    C Y N 489 
TYR CE2    C Y N 490 
TYR CZ     C Y N 491 
TYR OH     O N N 492 
TYR OXT    O N N 493 
TYR H      H N N 494 
TYR H2     H N N 495 
TYR HA     H N N 496 
TYR HB2    H N N 497 
TYR HB3    H N N 498 
TYR HD1    H N N 499 
TYR HD2    H N N 500 
TYR HE1    H N N 501 
TYR HE2    H N N 502 
TYR HH     H N N 503 
TYR HXT    H N N 504 
VAL N      N N N 505 
VAL CA     C N S 506 
VAL C      C N N 507 
VAL O      O N N 508 
VAL CB     C N N 509 
VAL CG1    C N N 510 
VAL CG2    C N N 511 
VAL OXT    O N N 512 
VAL H      H N N 513 
VAL H2     H N N 514 
VAL HA     H N N 515 
VAL HB     H N N 516 
VAL HG11   H N N 517 
VAL HG12   H N N 518 
VAL HG13   H N N 519 
VAL HG21   H N N 520 
VAL HG22   H N N 521 
VAL HG23   H N N 522 
VAL HXT    H N N 523 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
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  
FMN N1    C2     sing N N 83  
FMN N1    C10    doub N N 84  
FMN C2    O2     doub N N 85  
FMN C2    N3     sing N N 86  
FMN N3    C4     sing N N 87  
FMN N3    HN3    sing N N 88  
FMN C4    O4     doub N N 89  
FMN C4    C4A    sing N N 90  
FMN C4A   N5     doub N N 91  
FMN C4A   C10    sing N N 92  
FMN N5    C5A    sing N N 93  
FMN C5A   C6     doub Y N 94  
FMN C5A   C9A    sing Y N 95  
FMN C6    C7     sing Y N 96  
FMN C6    H6     sing N N 97  
FMN C7    C7M    sing N N 98  
FMN C7    C8     doub Y N 99  
FMN C7M   HM71   sing N N 100 
FMN C7M   HM72   sing N N 101 
FMN C7M   HM73   sing N N 102 
FMN C8    C8M    sing N N 103 
FMN C8    C9     sing Y N 104 
FMN C8M   HM81   sing N N 105 
FMN C8M   HM82   sing N N 106 
FMN C8M   HM83   sing N N 107 
FMN C9    C9A    doub Y N 108 
FMN C9    H9     sing N N 109 
FMN C9A   N10    sing N N 110 
FMN N10   C10    sing N N 111 
FMN N10   "C1'"  sing N N 112 
FMN "C1'" "C2'"  sing N N 113 
FMN "C1'" "H1'1" sing N N 114 
FMN "C1'" "H1'2" sing N N 115 
FMN "C2'" "O2'"  sing N N 116 
FMN "C2'" "C3'"  sing N N 117 
FMN "C2'" "H2'"  sing N N 118 
FMN "O2'" "HO2'" sing N N 119 
FMN "C3'" "O3'"  sing N N 120 
FMN "C3'" "C4'"  sing N N 121 
FMN "C3'" "H3'"  sing N N 122 
FMN "O3'" "HO3'" sing N N 123 
FMN "C4'" "O4'"  sing N N 124 
FMN "C4'" "C5'"  sing N N 125 
FMN "C4'" "H4'"  sing N N 126 
FMN "O4'" "HO4'" sing N N 127 
FMN "C5'" "O5'"  sing N N 128 
FMN "C5'" "H5'1" sing N N 129 
FMN "C5'" "H5'2" sing N N 130 
FMN "O5'" P      sing N N 131 
FMN P     O1P    doub N N 132 
FMN P     O2P    sing N N 133 
FMN P     O3P    sing N N 134 
FMN O2P   HOP2   sing N N 135 
FMN O3P   HOP3   sing N N 136 
GLN N     CA     sing N N 137 
GLN N     H      sing N N 138 
GLN N     H2     sing N N 139 
GLN CA    C      sing N N 140 
GLN CA    CB     sing N N 141 
GLN CA    HA     sing N N 142 
GLN C     O      doub N N 143 
GLN C     OXT    sing N N 144 
GLN CB    CG     sing N N 145 
GLN CB    HB2    sing N N 146 
GLN CB    HB3    sing N N 147 
GLN CG    CD     sing N N 148 
GLN CG    HG2    sing N N 149 
GLN CG    HG3    sing N N 150 
GLN CD    OE1    doub N N 151 
GLN CD    NE2    sing N N 152 
GLN NE2   HE21   sing N N 153 
GLN NE2   HE22   sing N N 154 
GLN OXT   HXT    sing N N 155 
GLU N     CA     sing N N 156 
GLU N     H      sing N N 157 
GLU N     H2     sing N N 158 
GLU CA    C      sing N N 159 
GLU CA    CB     sing N N 160 
GLU CA    HA     sing N N 161 
GLU C     O      doub N N 162 
GLU C     OXT    sing N N 163 
GLU CB    CG     sing N N 164 
GLU CB    HB2    sing N N 165 
GLU CB    HB3    sing N N 166 
GLU CG    CD     sing N N 167 
GLU CG    HG2    sing N N 168 
GLU CG    HG3    sing N N 169 
GLU CD    OE1    doub N N 170 
GLU CD    OE2    sing N N 171 
GLU OE2   HE2    sing N N 172 
GLU OXT   HXT    sing N N 173 
GLY N     CA     sing N N 174 
GLY N     H      sing N N 175 
GLY N     H2     sing N N 176 
GLY CA    C      sing N N 177 
GLY CA    HA2    sing N N 178 
GLY CA    HA3    sing N N 179 
GLY C     O      doub N N 180 
GLY C     OXT    sing N N 181 
GLY OXT   HXT    sing N N 182 
HIS N     CA     sing N N 183 
HIS N     H      sing N N 184 
HIS N     H2     sing N N 185 
HIS CA    C      sing N N 186 
HIS CA    CB     sing N N 187 
HIS CA    HA     sing N N 188 
HIS C     O      doub N N 189 
HIS C     OXT    sing N N 190 
HIS CB    CG     sing N N 191 
HIS CB    HB2    sing N N 192 
HIS CB    HB3    sing N N 193 
HIS CG    ND1    sing Y N 194 
HIS CG    CD2    doub Y N 195 
HIS ND1   CE1    doub Y N 196 
HIS ND1   HD1    sing N N 197 
HIS CD2   NE2    sing Y N 198 
HIS CD2   HD2    sing N N 199 
HIS CE1   NE2    sing Y N 200 
HIS CE1   HE1    sing N N 201 
HIS NE2   HE2    sing N N 202 
HIS OXT   HXT    sing N N 203 
HOH O     H1     sing N N 204 
HOH O     H2     sing N N 205 
ILE N     CA     sing N N 206 
ILE N     H      sing N N 207 
ILE N     H2     sing N N 208 
ILE CA    C      sing N N 209 
ILE CA    CB     sing N N 210 
ILE CA    HA     sing N N 211 
ILE C     O      doub N N 212 
ILE C     OXT    sing N N 213 
ILE CB    CG1    sing N N 214 
ILE CB    CG2    sing N N 215 
ILE CB    HB     sing N N 216 
ILE CG1   CD1    sing N N 217 
ILE CG1   HG12   sing N N 218 
ILE CG1   HG13   sing N N 219 
ILE CG2   HG21   sing N N 220 
ILE CG2   HG22   sing N N 221 
ILE CG2   HG23   sing N N 222 
ILE CD1   HD11   sing N N 223 
ILE CD1   HD12   sing N N 224 
ILE CD1   HD13   sing N N 225 
ILE OXT   HXT    sing N N 226 
LEU N     CA     sing N N 227 
LEU N     H      sing N N 228 
LEU N     H2     sing N N 229 
LEU CA    C      sing N N 230 
LEU CA    CB     sing N N 231 
LEU CA    HA     sing N N 232 
LEU C     O      doub N N 233 
LEU C     OXT    sing N N 234 
LEU CB    CG     sing N N 235 
LEU CB    HB2    sing N N 236 
LEU CB    HB3    sing N N 237 
LEU CG    CD1    sing N N 238 
LEU CG    CD2    sing N N 239 
LEU CG    HG     sing N N 240 
LEU CD1   HD11   sing N N 241 
LEU CD1   HD12   sing N N 242 
LEU CD1   HD13   sing N N 243 
LEU CD2   HD21   sing N N 244 
LEU CD2   HD22   sing N N 245 
LEU CD2   HD23   sing N N 246 
LEU OXT   HXT    sing N N 247 
LYS N     CA     sing N N 248 
LYS N     H      sing N N 249 
LYS N     H2     sing N N 250 
LYS CA    C      sing N N 251 
LYS CA    CB     sing N N 252 
LYS CA    HA     sing N N 253 
LYS C     O      doub N N 254 
LYS C     OXT    sing N N 255 
LYS CB    CG     sing N N 256 
LYS CB    HB2    sing N N 257 
LYS CB    HB3    sing N N 258 
LYS CG    CD     sing N N 259 
LYS CG    HG2    sing N N 260 
LYS CG    HG3    sing N N 261 
LYS CD    CE     sing N N 262 
LYS CD    HD2    sing N N 263 
LYS CD    HD3    sing N N 264 
LYS CE    NZ     sing N N 265 
LYS CE    HE2    sing N N 266 
LYS CE    HE3    sing N N 267 
LYS NZ    HZ1    sing N N 268 
LYS NZ    HZ2    sing N N 269 
LYS NZ    HZ3    sing N N 270 
LYS OXT   HXT    sing N N 271 
MET N     CA     sing N N 272 
MET N     H      sing N N 273 
MET N     H2     sing N N 274 
MET CA    C      sing N N 275 
MET CA    CB     sing N N 276 
MET CA    HA     sing N N 277 
MET C     O      doub N N 278 
MET C     OXT    sing N N 279 
MET CB    CG     sing N N 280 
MET CB    HB2    sing N N 281 
MET CB    HB3    sing N N 282 
MET CG    SD     sing N N 283 
MET CG    HG2    sing N N 284 
MET CG    HG3    sing N N 285 
MET SD    CE     sing N N 286 
MET CE    HE1    sing N N 287 
MET CE    HE2    sing N N 288 
MET CE    HE3    sing N N 289 
MET OXT   HXT    sing N N 290 
NAP PA    O1A    doub N N 291 
NAP PA    O2A    sing N N 292 
NAP PA    O5B    sing N N 293 
NAP PA    O3     sing N N 294 
NAP O2A   HOA2   sing N N 295 
NAP O5B   C5B    sing N N 296 
NAP C5B   C4B    sing N N 297 
NAP C5B   H51A   sing N N 298 
NAP C5B   H52A   sing N N 299 
NAP C4B   O4B    sing N N 300 
NAP C4B   C3B    sing N N 301 
NAP C4B   H4B    sing N N 302 
NAP O4B   C1B    sing N N 303 
NAP C3B   O3B    sing N N 304 
NAP C3B   C2B    sing N N 305 
NAP C3B   H3B    sing N N 306 
NAP O3B   HO3A   sing N N 307 
NAP C2B   O2B    sing N N 308 
NAP C2B   C1B    sing N N 309 
NAP C2B   H2B    sing N N 310 
NAP O2B   P2B    sing N N 311 
NAP C1B   N9A    sing N N 312 
NAP C1B   H1B    sing N N 313 
NAP N9A   C8A    sing Y N 314 
NAP N9A   C4A    sing Y N 315 
NAP C8A   N7A    doub Y N 316 
NAP C8A   H8A    sing N N 317 
NAP N7A   C5A    sing Y N 318 
NAP C5A   C6A    sing Y N 319 
NAP C5A   C4A    doub Y N 320 
NAP C6A   N6A    sing N N 321 
NAP C6A   N1A    doub Y N 322 
NAP N6A   H61A   sing N N 323 
NAP N6A   H62A   sing N N 324 
NAP N1A   C2A    sing Y N 325 
NAP C2A   N3A    doub Y N 326 
NAP C2A   H2A    sing N N 327 
NAP N3A   C4A    sing Y N 328 
NAP O3    PN     sing N N 329 
NAP PN    O1N    doub N N 330 
NAP PN    O2N    sing N N 331 
NAP PN    O5D    sing N N 332 
NAP O5D   C5D    sing N N 333 
NAP C5D   C4D    sing N N 334 
NAP C5D   H51N   sing N N 335 
NAP C5D   H52N   sing N N 336 
NAP C4D   O4D    sing N N 337 
NAP C4D   C3D    sing N N 338 
NAP C4D   H4D    sing N N 339 
NAP O4D   C1D    sing N N 340 
NAP C3D   O3D    sing N N 341 
NAP C3D   C2D    sing N N 342 
NAP C3D   H3D    sing N N 343 
NAP O3D   HO3N   sing N N 344 
NAP C2D   O2D    sing N N 345 
NAP C2D   C1D    sing N N 346 
NAP C2D   H2D    sing N N 347 
NAP O2D   HO2N   sing N N 348 
NAP C1D   N1N    sing N N 349 
NAP C1D   H1D    sing N N 350 
NAP N1N   C2N    sing Y N 351 
NAP N1N   C6N    doub Y N 352 
NAP C2N   C3N    doub Y N 353 
NAP C2N   H2N    sing N N 354 
NAP C3N   C7N    sing N N 355 
NAP C3N   C4N    sing Y N 356 
NAP C7N   O7N    doub N N 357 
NAP C7N   N7N    sing N N 358 
NAP N7N   H71N   sing N N 359 
NAP N7N   H72N   sing N N 360 
NAP C4N   C5N    doub Y N 361 
NAP C4N   H4N    sing N N 362 
NAP C5N   C6N    sing Y N 363 
NAP C5N   H5N    sing N N 364 
NAP C6N   H6N    sing N N 365 
NAP P2B   O1X    doub N N 366 
NAP P2B   O2X    sing N N 367 
NAP P2B   O3X    sing N N 368 
NAP O2X   HOP2   sing N N 369 
NAP O3X   HOP3   sing N N 370 
PHE N     CA     sing N N 371 
PHE N     H      sing N N 372 
PHE N     H2     sing N N 373 
PHE CA    C      sing N N 374 
PHE CA    CB     sing N N 375 
PHE CA    HA     sing N N 376 
PHE C     O      doub N N 377 
PHE C     OXT    sing N N 378 
PHE CB    CG     sing N N 379 
PHE CB    HB2    sing N N 380 
PHE CB    HB3    sing N N 381 
PHE CG    CD1    doub Y N 382 
PHE CG    CD2    sing Y N 383 
PHE CD1   CE1    sing Y N 384 
PHE CD1   HD1    sing N N 385 
PHE CD2   CE2    doub Y N 386 
PHE CD2   HD2    sing N N 387 
PHE CE1   CZ     doub Y N 388 
PHE CE1   HE1    sing N N 389 
PHE CE2   CZ     sing Y N 390 
PHE CE2   HE2    sing N N 391 
PHE CZ    HZ     sing N N 392 
PHE OXT   HXT    sing N N 393 
PRO N     CA     sing N N 394 
PRO N     CD     sing N N 395 
PRO N     H      sing N N 396 
PRO CA    C      sing N N 397 
PRO CA    CB     sing N N 398 
PRO CA    HA     sing N N 399 
PRO C     O      doub N N 400 
PRO C     OXT    sing N N 401 
PRO CB    CG     sing N N 402 
PRO CB    HB2    sing N N 403 
PRO CB    HB3    sing N N 404 
PRO CG    CD     sing N N 405 
PRO CG    HG2    sing N N 406 
PRO CG    HG3    sing N N 407 
PRO CD    HD2    sing N N 408 
PRO CD    HD3    sing N N 409 
PRO OXT   HXT    sing N N 410 
SER N     CA     sing N N 411 
SER N     H      sing N N 412 
SER N     H2     sing N N 413 
SER CA    C      sing N N 414 
SER CA    CB     sing N N 415 
SER CA    HA     sing N N 416 
SER C     O      doub N N 417 
SER C     OXT    sing N N 418 
SER CB    OG     sing N N 419 
SER CB    HB2    sing N N 420 
SER CB    HB3    sing N N 421 
SER OG    HG     sing N N 422 
SER OXT   HXT    sing N N 423 
SO4 S     O1     doub N N 424 
SO4 S     O2     doub N N 425 
SO4 S     O3     sing N N 426 
SO4 S     O4     sing N N 427 
THR N     CA     sing N N 428 
THR N     H      sing N N 429 
THR N     H2     sing N N 430 
THR CA    C      sing N N 431 
THR CA    CB     sing N N 432 
THR CA    HA     sing N N 433 
THR C     O      doub N N 434 
THR C     OXT    sing N N 435 
THR CB    OG1    sing N N 436 
THR CB    CG2    sing N N 437 
THR CB    HB     sing N N 438 
THR OG1   HG1    sing N N 439 
THR CG2   HG21   sing N N 440 
THR CG2   HG22   sing N N 441 
THR CG2   HG23   sing N N 442 
THR OXT   HXT    sing N N 443 
TRP N     CA     sing N N 444 
TRP N     H      sing N N 445 
TRP N     H2     sing N N 446 
TRP CA    C      sing N N 447 
TRP CA    CB     sing N N 448 
TRP CA    HA     sing N N 449 
TRP C     O      doub N N 450 
TRP C     OXT    sing N N 451 
TRP CB    CG     sing N N 452 
TRP CB    HB2    sing N N 453 
TRP CB    HB3    sing N N 454 
TRP CG    CD1    doub Y N 455 
TRP CG    CD2    sing Y N 456 
TRP CD1   NE1    sing Y N 457 
TRP CD1   HD1    sing N N 458 
TRP CD2   CE2    doub Y N 459 
TRP CD2   CE3    sing Y N 460 
TRP NE1   CE2    sing Y N 461 
TRP NE1   HE1    sing N N 462 
TRP CE2   CZ2    sing Y N 463 
TRP CE3   CZ3    doub Y N 464 
TRP CE3   HE3    sing N N 465 
TRP CZ2   CH2    doub Y N 466 
TRP CZ2   HZ2    sing N N 467 
TRP CZ3   CH2    sing Y N 468 
TRP CZ3   HZ3    sing N N 469 
TRP CH2   HH2    sing N N 470 
TRP OXT   HXT    sing N N 471 
TYR N     CA     sing N N 472 
TYR N     H      sing N N 473 
TYR N     H2     sing N N 474 
TYR CA    C      sing N N 475 
TYR CA    CB     sing N N 476 
TYR CA    HA     sing N N 477 
TYR C     O      doub N N 478 
TYR C     OXT    sing N N 479 
TYR CB    CG     sing N N 480 
TYR CB    HB2    sing N N 481 
TYR CB    HB3    sing N N 482 
TYR CG    CD1    doub Y N 483 
TYR CG    CD2    sing Y N 484 
TYR CD1   CE1    sing Y N 485 
TYR CD1   HD1    sing N N 486 
TYR CD2   CE2    doub Y N 487 
TYR CD2   HD2    sing N N 488 
TYR CE1   CZ     doub Y N 489 
TYR CE1   HE1    sing N N 490 
TYR CE2   CZ     sing Y N 491 
TYR CE2   HE2    sing N N 492 
TYR CZ    OH     sing N N 493 
TYR OH    HH     sing N N 494 
TYR OXT   HXT    sing N N 495 
VAL N     CA     sing N N 496 
VAL N     H      sing N N 497 
VAL N     H2     sing N N 498 
VAL CA    C      sing N N 499 
VAL CA    CB     sing N N 500 
VAL CA    HA     sing N N 501 
VAL C     O      doub N N 502 
VAL C     OXT    sing N N 503 
VAL CB    CG1    sing N N 504 
VAL CB    CG2    sing N N 505 
VAL CB    HB     sing N N 506 
VAL CG1   HG11   sing N N 507 
VAL CG1   HG12   sing N N 508 
VAL CG1   HG13   sing N N 509 
VAL CG2   HG21   sing N N 510 
VAL CG2   HG22   sing N N 511 
VAL CG2   HG23   sing N N 512 
VAL OXT   HXT    sing N N 513 
# 
_pdbx_audit_support.funding_organization   'Austrian Science Fund' 
_pdbx_audit_support.country                Austria 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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   2hs6 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8QNA 
_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]   0.011331 
_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]   0.011071 
_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]   0.020338 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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     . ASN A 1 16  ? -7.04500  9.87200  -23.74700 1.000 29.30734 ? 10  ASN A N     1 
ATOM   2    C CA    . ASN A 1 16  ? -7.38900  10.45100 -22.44900 1.000 26.89811 ? 10  ASN A CA    1 
ATOM   3    C C     . ASN A 1 16  ? -8.83300  10.08700 -22.10700 1.000 26.16562 ? 10  ASN A C     1 
ATOM   4    O O     . ASN A 1 16  ? -9.76800  10.55400 -22.76100 1.000 26.00623 ? 10  ASN A O     1 
ATOM   5    C CB    . ASN A 1 16  ? -7.18800  11.97300 -22.47100 1.000 26.35633 ? 10  ASN A CB    1 
ATOM   6    C CG    . ASN A 1 16  ? -7.42300  12.63200 -21.11100 1.000 26.54547 ? 10  ASN A CG    1 
ATOM   7    O OD1   . ASN A 1 16  ? -8.13200  12.10700 -20.25900 1.000 25.47928 ? 10  ASN A OD1   1 
ATOM   8    N ND2   . ASN A 1 16  ? -6.82400  13.80200 -20.91500 1.000 28.17458 ? 10  ASN A ND2   1 
ATOM   9    N N     . PRO A 1 17  ? -9.01600  9.25300  -21.07900 1.000 24.30259 ? 11  PRO A N     1 
ATOM   10   C CA    . PRO A 1 17  ? -10.37600 8.79700  -20.74400 1.000 22.89558 ? 11  PRO A CA    1 
ATOM   11   C C     . PRO A 1 17  ? -11.29300 9.91100  -20.29100 1.000 20.59599 ? 11  PRO A C     1 
ATOM   12   O O     . PRO A 1 17  ? -12.51500 9.73100  -20.33100 1.000 20.92851 ? 11  PRO A O     1 
ATOM   13   C CB    . PRO A 1 17  ? -10.14600 7.77400  -19.62400 1.000 23.48258 ? 11  PRO A CB    1 
ATOM   14   C CG    . PRO A 1 17  ? -8.81200  8.16000  -19.03400 1.000 24.44619 ? 11  PRO A CG    1 
ATOM   15   C CD    . PRO A 1 17  ? -7.99600  8.68300  -20.18200 1.000 24.92924 ? 11  PRO A CD    1 
ATOM   16   N N     . LEU A 1 18  ? -10.76000 11.06300 -19.87500 1.000 19.40552 ? 12  LEU A N     1 
ATOM   17   C CA    . LEU A 1 18  ? -11.65200 12.16100 -19.51800 1.000 19.34232 ? 12  LEU A CA    1 
ATOM   18   C C     . LEU A 1 18  ? -12.38400 12.72300 -20.72500 1.000 19.08233 ? 12  LEU A C     1 
ATOM   19   O O     . LEU A 1 18  ? -13.35700 13.46500 -20.55800 1.000 19.99132 ? 12  LEU A O     1 
ATOM   20   C CB    . LEU A 1 18  ? -10.88200 13.28900 -18.82800 1.000 18.23953 ? 12  LEU A CB    1 
ATOM   21   C CG    . LEU A 1 18  ? -10.39600 13.01000 -17.40300 1.000 18.90098 ? 12  LEU A CG    1 
ATOM   22   C CD1   . LEU A 1 18  ? -9.53400  14.16100 -16.89800 1.000 18.48629 ? 12  LEU A CD1   1 
ATOM   23   C CD2   . LEU A 1 18  ? -11.56900 12.74800 -16.45100 1.000 17.74698 ? 12  LEU A CD2   1 
ATOM   24   N N     . PHE A 1 19  ? -11.93900 12.40000 -21.92900 1.000 19.75488 ? 13  PHE A N     1 
ATOM   25   C CA    . PHE A 1 19  ? -12.57100 12.89800 -23.14100 1.000 19.90160 ? 13  PHE A CA    1 
ATOM   26   C C     . PHE A 1 19  ? -13.21000 11.77000 -23.92800 1.000 22.69989 ? 13  PHE A C     1 
ATOM   27   O O     . PHE A 1 19  ? -13.42600 11.88700 -25.14000 1.000 24.49137 ? 13  PHE A O     1 
ATOM   28   C CB    . PHE A 1 19  ? -11.55200 13.70100 -23.94500 1.000 21.12363 ? 13  PHE A CB    1 
ATOM   29   C CG    . PHE A 1 19  ? -11.16200 14.95400 -23.23100 1.000 23.25989 ? 13  PHE A CG    1 
ATOM   30   C CD1   . PHE A 1 19  ? -10.10200 14.95600 -22.33900 1.000 24.28395 ? 13  PHE A CD1   1 
ATOM   31   C CD2   . PHE A 1 19  ? -11.94200 16.09400 -23.34000 1.000 23.90672 ? 13  PHE A CD2   1 
ATOM   32   C CE1   . PHE A 1 19  ? -9.79300  16.09100 -21.62100 1.000 25.59545 ? 13  PHE A CE1   1 
ATOM   33   C CE2   . PHE A 1 19  ? -11.63500 17.23500 -22.62300 1.000 24.60323 ? 13  PHE A CE2   1 
ATOM   34   C CZ    . PHE A 1 19  ? -10.56100 17.23300 -21.76400 1.000 24.67319 ? 13  PHE A CZ    1 
ATOM   35   N N     . SER A 1 20  ? -13.50600 10.67000 -23.24700 1.000 22.41383 ? 14  SER A N     1 
ATOM   36   C CA    . SER A 1 20  ? -14.44800 9.80800  -23.94000 1.000 24.96423 ? 14  SER A CA    1 
ATOM   37   C C     . SER A 1 20  ? -15.87300 10.22800 -23.59300 1.000 23.53807 ? 14  SER A C     1 
ATOM   38   O O     . SER A 1 20  ? -16.14200 10.63000 -22.45400 1.000 23.92715 ? 14  SER A O     1 
ATOM   39   C CB    . SER A 1 20  ? -14.22600 8.35400  -23.56500 1.000 27.98907 ? 14  SER A CB    1 
ATOM   40   O OG    . SER A 1 20  ? -14.54700 8.14400  -22.21900 1.000 30.17120 ? 14  SER A OG    1 
ATOM   41   N N     . PRO A 1 21  ? -16.78000 10.18700 -24.56900 1.000 23.30396 ? 15  PRO A N     1 
ATOM   42   C CA    . PRO A 1 21  ? -18.15400 10.63000 -24.32000 1.000 22.66949 ? 15  PRO A CA    1 
ATOM   43   C C     . PRO A 1 21  ? -18.82700 9.75100  -23.27900 1.000 22.15483 ? 15  PRO A C     1 
ATOM   44   O O     . PRO A 1 21  ? -18.42700 8.61100  -23.03000 1.000 23.13384 ? 15  PRO A O     1 
ATOM   45   C CB    . PRO A 1 21  ? -18.82800 10.49500 -25.69100 1.000 23.87414 ? 15  PRO A CB    1 
ATOM   46   C CG    . PRO A 1 21  ? -17.96700 9.53000  -26.43600 1.000 26.10724 ? 15  PRO A CG    1 
ATOM   47   C CD    . PRO A 1 21  ? -16.57200 9.81300  -25.97300 1.000 24.66659 ? 15  PRO A CD    1 
ATOM   48   N N     . TYR A 1 22  ? -19.84800 10.31000 -22.64100 1.000 19.87676 ? 16  TYR A N     1 
ATOM   49   C CA    . TYR A 1 22  ? -20.56000 9.59600  -21.59300 1.000 19.20991 ? 16  TYR A CA    1 
ATOM   50   C C     . TYR A 1 22  ? -22.03600 9.93600  -21.67800 1.000 20.87212 ? 16  TYR A C     1 
ATOM   51   O O     . TYR A 1 22  ? -22.39900 11.10600 -21.82200 1.000 22.76253 ? 16  TYR A O     1 
ATOM   52   C CB    . TYR A 1 22  ? -20.01600 9.95100  -20.20600 1.000 19.39107 ? 16  TYR A CB    1 
ATOM   53   C CG    . TYR A 1 22  ? -20.69100 9.12700  -19.14100 1.000 17.65669 ? 16  TYR A CG    1 
ATOM   54   C CD1   . TYR A 1 22  ? -20.35500 7.79400  -18.96100 1.000 18.29418 ? 16  TYR A CD1   1 
ATOM   55   C CD2   . TYR A 1 22  ? -21.69200 9.66800  -18.34300 1.000 19.29997 ? 16  TYR A CD2   1 
ATOM   56   C CE1   . TYR A 1 22  ? -20.98900 7.01700  -18.01800 1.000 18.68962 ? 16  TYR A CE1   1 
ATOM   57   C CE2   . TYR A 1 22  ? -22.32700 8.89800  -17.38200 1.000 20.10654 ? 16  TYR A CE2   1 
ATOM   58   C CZ    . TYR A 1 22  ? -21.97200 7.57200  -17.22700 1.000 18.90773 ? 16  TYR A CZ    1 
ATOM   59   O OH    . TYR A 1 22  ? -22.60100 6.80500  -16.27500 1.000 18.82371 ? 16  TYR A OH    1 
ATOM   60   N N     . LYS A 1 23  ? -22.88200 8.91400  -21.58700 1.000 20.78240 ? 17  LYS A N     1 
ATOM   61   C CA    . LYS A 1 23  ? -24.33300 9.08800  -21.61400 1.000 22.97454 ? 17  LYS A CA    1 
ATOM   62   C C     . LYS A 1 23  ? -24.83200 9.16000  -20.17100 1.000 23.62556 ? 17  LYS A C     1 
ATOM   63   O O     . LYS A 1 23  ? -24.96300 8.13000  -19.50300 1.000 25.04577 ? 17  LYS A O     1 
ATOM   64   C CB    . LYS A 1 23  ? -24.97500 7.93900  -22.38700 1.000 26.29983 ? 17  LYS A CB    1 
ATOM   65   C CG    . LYS A 1 23  ? -26.49900 7.92500  -22.43000 1.000 29.15380 ? 17  LYS A CG    1 
ATOM   66   C CD    . LYS A 1 23  ? -27.02700 9.13800  -23.14900 1.000 33.34118 ? 17  LYS A CD    1 
ATOM   67   C CE    . LYS A 1 23  ? -28.14600 8.78100  -24.12800 1.000 36.36902 ? 17  LYS A CE    1 
ATOM   68   N NZ    . LYS A 1 23  ? -29.06600 9.94300  -24.34900 1.000 37.63533 ? 17  LYS A NZ    1 
ATOM   69   N N     . MET A 1 24  ? -25.06600 10.38700 -19.67300 1.000 23.69521 ? 18  MET A N     1 
ATOM   70   C CA    . MET A 1 24  ? -25.74600 10.63100 -18.39400 1.000 22.77001 ? 18  MET A CA    1 
ATOM   71   C C     . MET A 1 24  ? -27.25700 10.54700 -18.56700 1.000 25.04209 ? 18  MET A C     1 
ATOM   72   O O     . MET A 1 24  ? -27.95800 11.55900 -18.52200 1.000 27.06717 ? 18  MET A O     1 
ATOM   73   C CB    . MET A 1 24  ? -25.46800 12.01400 -17.81700 1.000 23.02632 ? 18  MET A CB    1 
ATOM   74   C CG    . MET A 1 24  ? -25.61200 12.08000 -16.29700 1.000 23.02191 ? 18  MET A CG    1 
ATOM   75   S SD    . MET A 1 24  ? -24.72200 13.42200 -15.50900 1.000 24.68836 ? 18  MET A SD    1 
ATOM   76   C CE    . MET A 1 24  ? -25.43800 14.82700 -16.38300 1.000 26.45977 ? 18  MET A CE    1 
ATOM   77   N N     . GLY A 1 25  ? -27.76000 9.32500  -18.72000 1.000 24.62159 ? 19  GLY A N     1 
ATOM   78   C CA    . GLY A 1 25  ? -29.18700 9.15600  -18.90300 1.000 24.75062 ? 19  GLY A CA    1 
ATOM   79   C C     . GLY A 1 25  ? -29.68000 9.94800  -20.09400 1.000 25.03980 ? 19  GLY A C     1 
ATOM   80   O O     . GLY A 1 25  ? -29.31200 9.64200  -21.22400 1.000 25.96085 ? 19  GLY A O     1 
ATOM   81   N N     . LYS A 1 26  ? -30.48300 10.99000 -19.85900 1.000 25.18053 ? 20  LYS A N     1 
ATOM   82   C CA    . LYS A 1 26  ? -31.00400 11.79100 -20.96400 1.000 24.38840 ? 20  LYS A CA    1 
ATOM   83   C C     . LYS A 1 26  ? -29.93300 12.63900 -21.64300 1.000 23.11760 ? 20  LYS A C     1 
ATOM   84   O O     . LYS A 1 26  ? -30.15700 13.12000 -22.76200 1.000 25.54386 ? 20  LYS A O     1 
ATOM   85   C CB    . LYS A 1 26  ? -32.13300 12.70000 -20.46000 1.000 25.95327 ? 20  LYS A CB    1 
ATOM   86   N N     . PHE A 1 27  ? -28.78000 12.83100 -21.01000 1.000 21.36757 ? 21  PHE A N     1 
ATOM   87   C CA    . PHE A 1 27  ? -27.81800 13.84800 -21.42400 1.000 22.55701 ? 21  PHE A CA    1 
ATOM   88   C C     . PHE A 1 27  ? -26.58500 13.21900 -22.05900 1.000 22.27516 ? 21  PHE A C     1 
ATOM   89   O O     . PHE A 1 27  ? -25.91800 12.38300 -21.44200 1.000 23.82326 ? 21  PHE A O     1 
ATOM   90   C CB    . PHE A 1 27  ? -27.42200 14.71700 -20.22300 1.000 21.74932 ? 21  PHE A CB    1 
ATOM   91   C CG    . PHE A 1 27  ? -28.60000 15.33400 -19.53600 1.000 21.60925 ? 21  PHE A CG    1 
ATOM   92   C CD1   . PHE A 1 27  ? -29.33600 16.32400 -20.16200 1.000 22.57966 ? 21  PHE A CD1   1 
ATOM   93   C CD2   . PHE A 1 27  ? -29.01000 14.88200 -18.29000 1.000 22.08666 ? 21  PHE A CD2   1 
ATOM   94   C CE1   . PHE A 1 27  ? -30.44000 16.87900 -19.54700 1.000 21.99962 ? 21  PHE A CE1   1 
ATOM   95   C CE2   . PHE A 1 27  ? -30.11400 15.42800 -17.66900 1.000 22.90010 ? 21  PHE A CE2   1 
ATOM   96   C CZ    . PHE A 1 27  ? -30.83000 16.43300 -18.29900 1.000 23.12026 ? 21  PHE A CZ    1 
ATOM   97   N N     . ASN A 1 28  ? -26.26000 13.65900 -23.27300 1.000 20.95190 ? 22  ASN A N     1 
ATOM   98   C CA    . ASN A 1 28  ? -25.08000 13.17200 -23.99500 1.000 19.84010 ? 22  ASN A CA    1 
ATOM   99   C C     . ASN A 1 28  ? -23.91300 14.09800 -23.69700 1.000 20.16227 ? 22  ASN A C     1 
ATOM   100  O O     . ASN A 1 28  ? -23.83100 15.19700 -24.25000 1.000 22.98977 ? 22  ASN A O     1 
ATOM   101  C CB    . ASN A 1 28  ? -25.35100 13.11300 -25.49700 1.000 21.41722 ? 22  ASN A CB    1 
ATOM   102  C CG    . ASN A 1 28  ? -26.47300 12.17300 -25.83400 1.000 26.33375 ? 22  ASN A CG    1 
ATOM   103  O OD1   . ASN A 1 28  ? -26.44400 11.01300 -25.43700 1.000 26.96587 ? 22  ASN A OD1   1 
ATOM   104  N ND2   . ASN A 1 28  ? -27.48000 12.66500 -26.55100 1.000 29.07898 ? 22  ASN A ND2   1 
ATOM   105  N N     . LEU A 1 29  ? -22.99500 13.66100 -22.83800 1.000 18.27393 ? 23  LEU A N     1 
ATOM   106  C CA    . LEU A 1 29  ? -21.82700 14.47200 -22.51200 1.000 16.33960 ? 23  LEU A CA    1 
ATOM   107  C C     . LEU A 1 29  ? -20.66600 14.11800 -23.43400 1.000 17.68967 ? 23  LEU A C     1 
ATOM   108  O O     . LEU A 1 29  ? -20.47500 12.95500 -23.79700 1.000 19.55630 ? 23  LEU A O     1 
ATOM   109  C CB    . LEU A 1 29  ? -21.40500 14.28400 -21.05300 1.000 16.97526 ? 23  LEU A CB    1 
ATOM   110  C CG    . LEU A 1 29  ? -22.50900 14.57300 -20.03000 1.000 17.54986 ? 23  LEU A CG    1 
ATOM   111  C CD1   . LEU A 1 29  ? -22.00300 14.39000 -18.60100 1.000 17.01573 ? 23  LEU A CD1   1 
ATOM   112  C CD2   . LEU A 1 29  ? -23.12100 15.96900 -20.24100 1.000 17.88742 ? 23  LEU A CD2   1 
ATOM   113  N N     . SER A 1 30  ? -19.88600 15.13300 -23.80200 1.000 17.40583 ? 24  SER A N     1 
ATOM   114  C CA    . SER A 1 30  ? -18.75000 14.92100 -24.69000 1.000 18.71386 ? 24  SER A CA    1 
ATOM   115  C C     . SER A 1 30  ? -17.45300 14.66500 -23.93300 1.000 18.34555 ? 24  SER A C     1 
ATOM   116  O O     . SER A 1 30  ? -16.47500 14.20000 -24.53800 1.000 18.10889 ? 24  SER A O     1 
ATOM   117  C CB    . SER A 1 30  ? -18.58700 16.13000 -25.62100 1.000 21.55072 ? 24  SER A CB    1 
ATOM   118  O OG    . SER A 1 30  ? -18.14000 17.25500 -24.88400 1.000 26.49196 ? 24  SER A OG    1 
ATOM   119  N N     . HIS A 1 31  ? -17.42400 14.96200 -22.63500 1.000 17.26429 ? 25  HIS A N     1 
ATOM   120  C CA    . HIS A 1 31  ? -16.25100 14.72600 -21.80200 1.000 15.68936 ? 25  HIS A CA    1 
ATOM   121  C C     . HIS A 1 31  ? -16.71000 14.63700 -20.35700 1.000 15.16614 ? 25  HIS A C     1 
ATOM   122  O O     . HIS A 1 31  ? -17.87500 14.90100 -20.03300 1.000 15.80190 ? 25  HIS A O     1 
ATOM   123  C CB    . HIS A 1 31  ? -15.19600 15.82400 -21.97700 1.000 15.82404 ? 25  HIS A CB    1 
ATOM   124  C CG    . HIS A 1 31  ? -15.67000 17.18100 -21.55300 1.000 16.93636 ? 25  HIS A CG    1 
ATOM   125  N ND1   . HIS A 1 31  ? -15.72500 17.57500 -20.23200 1.000 16.71404 ? 25  HIS A ND1   1 
ATOM   126  C CD2   . HIS A 1 31  ? -16.14800 18.22000 -22.27700 1.000 16.38751 ? 25  HIS A CD2   1 
ATOM   127  C CE1   . HIS A 1 31  ? -16.19600 18.80900 -20.16500 1.000 16.83489 ? 25  HIS A CE1   1 
ATOM   128  N NE2   . HIS A 1 31  ? -16.46300 19.22200 -21.39200 1.000 16.87630 ? 25  HIS A NE2   1 
ATOM   129  N N     . ARG A 1 32  ? -15.77500 14.27700 -19.48000 1.000 15.62502 ? 26  ARG A N     1 
ATOM   130  C CA    . ARG A 1 32  ? -16.13000 13.89400 -18.12000 1.000 15.43329 ? 26  ARG A CA    1 
ATOM   131  C C     . ARG A 1 32  ? -15.66900 14.89100 -17.07200 1.000 14.58838 ? 26  ARG A C     1 
ATOM   132  O O     . ARG A 1 32  ? -15.73200 14.58600 -15.87200 1.000 14.75107 ? 26  ARG A O     1 
ATOM   133  C CB    . ARG A 1 32  ? -15.57100 12.50400 -17.82200 1.000 17.26408 ? 26  ARG A CB    1 
ATOM   134  C CG    . ARG A 1 32  ? -16.20100 11.49700 -18.77900 1.000 19.75397 ? 26  ARG A CG    1 
ATOM   135  C CD    . ARG A 1 32  ? -15.41700 10.25200 -18.88100 1.000 21.27565 ? 26  ARG A CD    1 
ATOM   136  N NE    . ARG A 1 32  ? -16.02800 9.33500  -19.83600 1.000 22.05179 ? 26  ARG A NE    1 
ATOM   137  C CZ    . ARG A 1 32  ? -16.59400 8.18400  -19.50800 1.000 20.81845 ? 26  ARG A CZ    1 
ATOM   138  N NH1   . ARG A 1 32  ? -16.78800 7.84900  -18.24500 1.000 20.06601 ? 26  ARG A NH1   1 
ATOM   139  N NH2   . ARG A 1 32  ? -16.94800 7.33900  -20.47300 1.000 21.04497 ? 26  ARG A NH2   1 
ATOM   140  N N     . VAL A 1 33  ? -15.25100 16.08300 -17.49000 1.000 14.76181 ? 27  VAL A N     1 
ATOM   141  C CA    . VAL A 1 33  ? -14.79400 17.12300 -16.57500 1.000 15.91243 ? 27  VAL A CA    1 
ATOM   142  C C     . VAL A 1 33  ? -16.00700 17.95600 -16.19000 1.000 14.74451 ? 27  VAL A C     1 
ATOM   143  O O     . VAL A 1 33  ? -16.63200 18.58600 -17.05100 1.000 16.74073 ? 27  VAL A O     1 
ATOM   144  C CB    . VAL A 1 33  ? -13.70400 17.99800 -17.21600 1.000 16.26485 ? 27  VAL A CB    1 
ATOM   145  C CG1   . VAL A 1 33  ? -13.23900 19.08400 -16.24000 1.000 16.61003 ? 27  VAL A CG1   1 
ATOM   146  C CG2   . VAL A 1 33  ? -12.52300 17.14400 -17.62900 1.000 17.65943 ? 27  VAL A CG2   1 
ATOM   147  N N     . VAL A 1 34  ? -16.35400 17.94300 -14.90700 1.000 13.91045 ? 28  VAL A N     1 
ATOM   148  C CA    . VAL A 1 34  ? -17.56500 18.58300 -14.40200 1.000 12.77012 ? 28  VAL A CA    1 
ATOM   149  C C     . VAL A 1 34  ? -17.18600 19.79300 -13.54900 1.000 11.91999 ? 28  VAL A C     1 
ATOM   150  O O     . VAL A 1 34  ? -16.23600 19.73500 -12.75300 1.000 13.68950 ? 28  VAL A O     1 
ATOM   151  C CB    . VAL A 1 34  ? -18.40100 17.57100 -13.58400 1.000 12.52326 ? 28  VAL A CB    1 
ATOM   152  C CG1   . VAL A 1 34  ? -19.65400 18.22900 -12.95700 1.000 12.84638 ? 28  VAL A CG1   1 
ATOM   153  C CG2   . VAL A 1 34  ? -18.77000 16.36200 -14.45000 1.000 12.68029 ? 28  VAL A CG2   1 
ATOM   154  N N     . LEU A 1 35  ? -17.95100 20.87700 -13.68100 1.000 13.07315 ? 29  LEU A N     1 
ATOM   155  C CA    . LEU A 1 35  ? -17.81700 22.01100 -12.76200 1.000 12.46643 ? 29  LEU A CA    1 
ATOM   156  C C     . LEU A 1 35  ? -18.52400 21.67500 -11.45000 1.000 13.19419 ? 29  LEU A C     1 
ATOM   157  O O     . LEU A 1 35  ? -19.75200 21.53400 -11.41700 1.000 13.90937 ? 29  LEU A O     1 
ATOM   158  C CB    . LEU A 1 35  ? -18.39800 23.28900 -13.37300 1.000 13.30229 ? 29  LEU A CB    1 
ATOM   159  C CG    . LEU A 1 35  ? -18.50500 24.51900 -12.44300 1.000 13.02922 ? 29  LEU A CG    1 
ATOM   160  C CD1   . LEU A 1 35  ? -17.12500 25.00800 -11.97600 1.000 14.40940 ? 29  LEU A CD1   1 
ATOM   161  C CD2   . LEU A 1 35  ? -19.26400 25.67600 -13.08500 1.000 13.92582 ? 29  LEU A CD2   1 
ATOM   162  N N     . ALA A 1 36  ? -17.75700 21.52500 -10.37400 1.000 11.89722 ? 30  ALA A N     1 
ATOM   163  C CA    . ALA A 1 36  ? -18.33000 21.28300 -9.05900  1.000 12.25114 ? 30  ALA A CA    1 
ATOM   164  C C     . ALA A 1 36  ? -19.12000 22.50400 -8.58300  1.000 13.40365 ? 30  ALA A C     1 
ATOM   165  O O     . ALA A 1 36  ? -18.76600 23.64300 -8.90200  1.000 13.13440 ? 30  ALA A O     1 
ATOM   166  C CB    . ALA A 1 36  ? -17.22600 20.94900 -8.05100  1.000 13.69549 ? 30  ALA A CB    1 
ATOM   167  N N     . PRO A 1 37  ? -20.19500 22.28900 -7.81700  1.000 14.04628 ? 31  PRO A N     1 
ATOM   168  C CA    . PRO A 1 37  ? -20.96000 23.42300 -7.27000  1.000 12.57058 ? 31  PRO A CA    1 
ATOM   169  C C     . PRO A 1 37  ? -20.12100 24.23900 -6.29600  1.000 12.64690 ? 31  PRO A C     1 
ATOM   170  O O     . PRO A 1 37  ? -19.51500 23.68600 -5.37700  1.000 14.94233 ? 31  PRO A O     1 
ATOM   171  C CB    . PRO A 1 37  ? -22.13700 22.73400 -6.55400  1.000 13.57898 ? 31  PRO A CB    1 
ATOM   172  C CG    . PRO A 1 37  ? -21.59700 21.35700 -6.19000  1.000 13.90050 ? 31  PRO A CG    1 
ATOM   173  C CD    . PRO A 1 37  ? -20.71300 20.98600 -7.35100  1.000 13.17775 ? 31  PRO A CD    1 
ATOM   174  N N     . MET A 1 38  ? -20.10100 25.56600 -6.47600  1.000 13.48588 ? 32  MET A N     1 
ATOM   175  C CA    . MET A 1 38  ? -19.23700 26.41300 -5.64600  1.000 13.88812 ? 32  MET A CA    1 
ATOM   176  C C     . MET A 1 38  ? -19.91800 27.73700 -5.31700  1.000 14.51621 ? 32  MET A C     1 
ATOM   177  O O     . MET A 1 38  ? -20.13100 28.57500 -6.20300  1.000 13.90307 ? 32  MET A O     1 
ATOM   178  C CB    . MET A 1 38  ? -17.90800 26.66900 -6.34700  1.000 14.45106 ? 32  MET A CB    1 
ATOM   179  C CG    . MET A 1 38  ? -16.95500 25.51300 -6.20000  1.000 14.82169 ? 32  MET A CG    1 
ATOM   180  S SD    . MET A 1 38  ? -15.37300 25.91900 -6.93900  1.000 16.06433 ? 32  MET A SD    1 
ATOM   181  C CE    . MET A 1 38  ? -15.89800 26.02700 -8.66500  1.000 17.52382 ? 32  MET A CE    1 
ATOM   182  N N     . THR A 1 39  ? -20.22500 27.91800 -4.03800  1.000 13.60881 ? 33  THR A N     1 
ATOM   183  C CA    . THR A 1 39  ? -20.65800 29.20000 -3.49300  1.000 13.36284 ? 33  THR A CA    1 
ATOM   184  C C     . THR A 1 39  ? -19.60500 30.26900 -3.73100  1.000 13.41977 ? 33  THR A C     1 
ATOM   185  O O     . THR A 1 39  ? -18.44500 30.09800 -3.35000  1.000 15.08084 ? 33  THR A O     1 
ATOM   186  C CB    . THR A 1 39  ? -20.90700 29.03500 -1.98700  1.000 13.41731 ? 33  THR A CB    1 
ATOM   187  O OG1   . THR A 1 39  ? -22.00900 28.14100 -1.78800  1.000 15.96002 ? 33  THR A OG1   1 
ATOM   188  C CG2   . THR A 1 39  ? -21.21600 30.35600 -1.30500  1.000 13.49218 ? 33  THR A CG2   1 
ATOM   189  N N     . ARG A 1 40  ? -20.00900 31.38400 -4.35700  1.000 13.34799 ? 34  ARG A N     1 
ATOM   190  C CA    . ARG A 1 40  ? -19.09200 32.49400 -4.62000  1.000 12.23280 ? 34  ARG A CA    1 
ATOM   191  C C     . ARG A 1 40  ? -19.59700 33.85100 -4.13400  1.000 14.34786 ? 34  ARG A C     1 
ATOM   192  O O     . ARG A 1 40  ? -18.80200 34.80600 -4.09700  1.000 13.75871 ? 34  ARG A O     1 
ATOM   193  C CB    . ARG A 1 40  ? -18.75500 32.58700 -6.12200  1.000 14.16603 ? 34  ARG A CB    1 
ATOM   194  C CG    . ARG A 1 40  ? -18.20900 31.28700 -6.71300  1.000 13.73054 ? 34  ARG A CG    1 
ATOM   195  C CD    . ARG A 1 40  ? -16.87600 30.86500 -6.09400  1.000 13.54957 ? 34  ARG A CD    1 
ATOM   196  N NE    . ARG A 1 40  ? -15.86500 31.92200 -6.08400  1.000 13.73760 ? 34  ARG A NE    1 
ATOM   197  C CZ    . ARG A 1 40  ? -15.15500 32.29900 -7.14400  1.000 14.94636 ? 34  ARG A CZ    1 
ATOM   198  N NH1   . ARG A 1 40  ? -15.29600 31.70500 -8.32400  1.000 13.35646 ? 34  ARG A NH1   1 
ATOM   199  N NH2   . ARG A 1 40  ? -14.27000 33.29100 -7.01600  1.000 15.71501 ? 34  ARG A NH2   1 
ATOM   200  N N     . CYS A 1 41  ? -20.88000 33.97600 -3.77200  1.000 14.54586 ? 35  CYS A N     1 
ATOM   201  C CA    . CYS A 1 41  ? -21.39100 35.14300 -3.05600  1.000 12.33776 ? 35  CYS A CA    1 
ATOM   202  C C     . CYS A 1 41  ? -21.43800 36.39500 -3.93300  1.000 13.30829 ? 35  CYS A C     1 
ATOM   203  O O     . CYS A 1 41  ? -21.30000 37.51400 -3.42900  1.000 14.07134 ? 35  CYS A O     1 
ATOM   204  C CB    . CYS A 1 41  ? -20.56100 35.41100 -1.79000  1.000 13.42605 ? 35  CYS A CB    1 
ATOM   205  S SG    . CYS A 1 41  ? -20.49100 33.97500 -0.68900  1.000 15.71216 ? 35  CYS A SG    1 
ATOM   206  N N     . ARG A 1 42  ? -21.62400 36.23500 -5.24700  1.000 13.50676 ? 36  ARG A N     1 
ATOM   207  C CA    . ARG A 1 42  ? -21.79000 37.37800 -6.13300  1.000 13.35710 ? 36  ARG A CA    1 
ATOM   208  C C     . ARG A 1 42  ? -23.24700 37.65500 -6.45600  1.000 14.85656 ? 36  ARG A C     1 
ATOM   209  O O     . ARG A 1 42  ? -23.53500 38.62600 -7.16900  1.000 15.36476 ? 36  ARG A O     1 
ATOM   210  C CB    . ARG A 1 42  ? -21.00500 37.17600 -7.44400  1.000 13.62253 ? 36  ARG A CB    1 
ATOM   211  C CG    . ARG A 1 42  ? -19.59900 37.76100 -7.44200  1.000 14.40854 ? 36  ARG A CG    1 
ATOM   212  C CD    . ARG A 1 42  ? -18.66700 36.95600 -6.55000  1.000 14.60441 ? 36  ARG A CD    1 
ATOM   213  N NE    . ARG A 1 42  ? -17.28600 37.42500 -6.66300  1.000 13.17893 ? 36  ARG A NE    1 
ATOM   214  C CZ    . ARG A 1 42  ? -16.25500 36.81400 -6.10600  1.000 11.96563 ? 36  ARG A CZ    1 
ATOM   215  N NH1   . ARG A 1 42  ? -16.41600 35.71800 -5.37600  1.000 11.79888 ? 36  ARG A NH1   1 
ATOM   216  N NH2   . ARG A 1 42  ? -15.02900 37.30000 -6.30600  1.000 13.45122 ? 36  ARG A NH2   1 
ATOM   217  N N     . ALA A 1 43  ? -24.17000 36.83000 -5.95700  1.000 13.86538 ? 37  ALA A N     1 
ATOM   218  C CA    . ALA A 1 43  ? -25.59300 36.98000 -6.28300  1.000 15.06310 ? 37  ALA A CA    1 
ATOM   219  C C     . ALA A 1 43  ? -26.22400 37.95400 -5.29000  1.000 15.25671 ? 37  ALA A C     1 
ATOM   220  O O     . ALA A 1 43  ? -26.93500 37.57300 -4.35800  1.000 16.16382 ? 37  ALA A O     1 
ATOM   221  C CB    . ALA A 1 43  ? -26.28600 35.62300 -6.27300  1.000 15.40632 ? 37  ALA A CB    1 
ATOM   222  N N     . LEU A 1 44  ? -25.96200 39.24100 -5.51500  1.000 15.26426 ? 38  LEU A N     1 
ATOM   223  C CA    . LEU A 1 44  ? -26.30800 40.27300 -4.54300  1.000 16.17234 ? 38  LEU A CA    1 
ATOM   224  C C     . LEU A 1 44  ? -27.79600 40.24200 -4.19500  1.000 16.16722 ? 38  LEU A C     1 
ATOM   225  O O     . LEU A 1 44  ? -28.65700 40.18400 -5.08200  1.000 16.53089 ? 38  LEU A O     1 
ATOM   226  C CB    . LEU A 1 44  ? -25.90900 41.64300 -5.09800  1.000 15.98642 ? 38  LEU A CB    1 
ATOM   227  C CG    . LEU A 1 44  ? -24.43300 41.85700 -5.46200  1.000 17.37848 ? 38  LEU A CG    1 
ATOM   228  C CD1   . LEU A 1 44  ? -24.17100 43.33700 -5.68900  1.000 19.62248 ? 38  LEU A CD1   1 
ATOM   229  C CD2   . LEU A 1 44  ? -23.46400 41.33400 -4.41100  1.000 16.78290 ? 38  LEU A CD2   1 
ATOM   230  N N     . ASN A 1 45  ? -28.08800 40.26500 -2.88700  1.000 16.81785 ? 39  ASN A N     1 
ATOM   231  C CA    . ASN A 1 45  ? -29.45900 40.26400 -2.36000  1.000 17.50235 ? 39  ASN A CA    1 
ATOM   232  C C     . ASN A 1 45  ? -30.21400 39.00300 -2.77300  1.000 16.75331 ? 39  ASN A C     1 
ATOM   233  O O     . ASN A 1 45  ? -31.44400 39.00900 -2.87100  1.000 17.71436 ? 39  ASN A O     1 
ATOM   234  C CB    . ASN A 1 45  ? -30.23100 41.51800 -2.78200  1.000 19.83286 ? 39  ASN A CB    1 
ATOM   235  C CG    . ASN A 1 45  ? -29.53700 42.80600 -2.35900  1.000 20.58660 ? 39  ASN A CG    1 
ATOM   236  O OD1   . ASN A 1 45  ? -29.29700 43.67600 -3.19000  1.000 23.02536 ? 39  ASN A OD1   1 
ATOM   237  N ND2   . ASN A 1 45  ? -29.24200 42.94700 -1.05900  1.000 20.47338 ? 39  ASN A ND2   1 
ATOM   238  N N     . ASN A 1 46  ? -29.46400 37.91600 -2.97400  1.000 16.20516 ? 40  ASN A N     1 
ATOM   239  C CA    . ASN A 1 46  ? -29.95500 36.59300 -3.35500  1.000 14.69934 ? 40  ASN A CA    1 
ATOM   240  C C     . ASN A 1 46  ? -30.55000 36.55300 -4.76000  1.000 15.68927 ? 40  ASN A C     1 
ATOM   241  O O     . ASN A 1 46  ? -31.24900 35.59700 -5.11200  1.000 15.11127 ? 40  ASN A O     1 
ATOM   242  C CB    . ASN A 1 46  ? -30.96200 36.03600 -2.33900  1.000 16.94482 ? 40  ASN A CB    1 
ATOM   243  C CG    . ASN A 1 46  ? -30.50600 36.21900 -0.90800  1.000 18.07312 ? 40  ASN A CG    1 
ATOM   244  O OD1   . ASN A 1 46  ? -31.19500 36.83300 -0.10200  1.000 19.35862 ? 40  ASN A OD1   1 
ATOM   245  N ND2   . ASN A 1 46  ? -29.33900 35.69200 -0.58800  1.000 17.11175 ? 40  ASN A ND2   1 
ATOM   246  N N     . ILE A 1 47  ? -30.26500 37.54200 -5.59000  1.000 15.73687 ? 41  ILE A N     1 
ATOM   247  C CA    . ILE A 1 47  ? -30.73800 37.58100 -6.97100  1.000 15.98281 ? 41  ILE A CA    1 
ATOM   248  C C     . ILE A 1 47  ? -29.56000 37.26800 -7.88500  1.000 16.19933 ? 41  ILE A C     1 
ATOM   249  O O     . ILE A 1 47  ? -28.52100 37.93300 -7.78500  1.000 16.41270 ? 41  ILE A O     1 
ATOM   250  C CB    . ILE A 1 47  ? -31.36100 38.94400 -7.32200  1.000 17.87545 ? 41  ILE A CB    1 
ATOM   251  C CG1   . ILE A 1 47  ? -32.47500 39.27500 -6.32400  1.000 21.27650 ? 41  ILE A CG1   1 
ATOM   252  C CG2   . ILE A 1 47  ? -31.91500 38.92100 -8.74200  1.000 17.34065 ? 41  ILE A CG2   1 
ATOM   253  C CD1   . ILE A 1 47  ? -32.88200 40.73000 -6.33700  1.000 24.68162 ? 41  ILE A CD1   1 
ATOM   254  N N     . PRO A 1 48  ? -29.67300 36.28500 -8.77600  1.000 16.89940 ? 42  PRO A N     1 
ATOM   255  C CA    . PRO A 1 48  ? -28.60200 36.05700 -9.75100  1.000 18.69557 ? 42  PRO A CA    1 
ATOM   256  C C     . PRO A 1 48  ? -28.32800 37.32900 -10.54200 1.000 18.95512 ? 42  PRO A C     1 
ATOM   257  O O     . PRO A 1 48  ? -29.24700 38.04800 -10.93800 1.000 20.25109 ? 42  PRO A O     1 
ATOM   258  C CB    . PRO A 1 48  ? -29.16100 34.93900 -10.63900 1.000 18.57077 ? 42  PRO A CB    1 
ATOM   259  C CG    . PRO A 1 48  ? -30.17700 34.24700 -9.78400  1.000 18.33551 ? 42  PRO A CG    1 
ATOM   260  C CD    . PRO A 1 48  ? -30.80200 35.35200 -8.96400  1.000 17.23127 ? 42  PRO A CD    1 
ATOM   261  N N     . GLN A 1 49  ? -27.05000 37.62400 -10.73000 1.000 18.85600 ? 43  GLN A N     1 
ATOM   262  C CA    . GLN A 1 49  ? -26.59800 38.84400 -11.38100 1.000 17.58024 ? 43  GLN A CA    1 
ATOM   263  C C     . GLN A 1 49  ? -25.91700 38.52100 -12.70200 1.000 17.79888 ? 43  GLN A C     1 
ATOM   264  O O     . GLN A 1 49  ? -25.52200 37.38100 -12.95500 1.000 18.48829 ? 43  GLN A O     1 
ATOM   265  C CB    . GLN A 1 49  ? -25.62300 39.60900 -10.47500 1.000 19.64919 ? 43  GLN A CB    1 
ATOM   266  C CG    . GLN A 1 49  ? -26.18300 39.89800 -9.09100  1.000 20.88880 ? 43  GLN A CG    1 
ATOM   267  C CD    . GLN A 1 49  ? -27.28300 40.94900 -9.14500  1.000 23.01116 ? 43  GLN A CD    1 
ATOM   268  O OE1   . GLN A 1 49  ? -27.25100 41.85200 -9.99500  1.000 25.80205 ? 43  GLN A OE1   1 
ATOM   269  N NE2   . GLN A 1 49  ? -28.26300 40.83500 -8.25000  1.000 21.84170 ? 43  GLN A NE2   1 
ATOM   270  N N     . ALA A 1 50  ? -25.74700 39.56300 -13.52700 1.000 18.67780 ? 44  ALA A N     1 
ATOM   271  C CA    . ALA A 1 50  ? -25.06500 39.41200 -14.81300 1.000 18.72398 ? 44  ALA A CA    1 
ATOM   272  C C     . ALA A 1 50  ? -23.68500 38.79200 -14.65600 1.000 19.56289 ? 44  ALA A C     1 
ATOM   273  O O     . ALA A 1 50  ? -23.23400 38.05300 -15.53900 1.000 19.46284 ? 44  ALA A O     1 
ATOM   274  C CB    . ALA A 1 50  ? -24.94400 40.76700 -15.51600 1.000 20.01629 ? 44  ALA A CB    1 
ATOM   275  N N     . ALA A 1 51  ? -23.00400 39.07700 -13.54500 1.000 18.80476 ? 45  ALA A N     1 
ATOM   276  C CA    . ALA A 1 51  ? -21.67700 38.50700 -13.32800 1.000 18.93523 ? 45  ALA A CA    1 
ATOM   277  C C     . ALA A 1 51  ? -21.72500 36.98400 -13.31800 1.000 17.07548 ? 45  ALA A C     1 
ATOM   278  O O     . ALA A 1 51  ? -20.80800 36.32900 -13.82600 1.000 16.41661 ? 45  ALA A O     1 
ATOM   279  C CB    . ALA A 1 51  ? -21.07800 39.03700 -12.02800 1.000 19.29963 ? 45  ALA A CB    1 
ATOM   280  N N     . LEU A 1 52  ? -22.78300 36.39900 -12.74900 1.000 16.87112 ? 46  LEU A N     1 
ATOM   281  C CA    . LEU A 1 52  ? -22.89000 34.94000 -12.76700 1.000 14.91472 ? 46  LEU A CA    1 
ATOM   282  C C     . LEU A 1 52  ? -22.97800 34.42500 -14.19700 1.000 15.80414 ? 46  LEU A C     1 
ATOM   283  O O     . LEU A 1 52  ? -22.40300 33.38300 -14.52500 1.000 16.31210 ? 46  LEU A O     1 
ATOM   284  C CB    . LEU A 1 52  ? -24.10600 34.46900 -11.97500 1.000 13.77795 ? 46  LEU A CB    1 
ATOM   285  C CG    . LEU A 1 52  ? -23.98400 34.33100 -10.45400 1.000 14.40194 ? 46  LEU A CG    1 
ATOM   286  C CD1   . LEU A 1 52  ? -23.66200 35.65100 -9.78100  1.000 17.96997 ? 46  LEU A CD1   1 
ATOM   287  C CD2   . LEU A 1 52  ? -25.25300 33.70100 -9.86600  1.000 15.10817 ? 46  LEU A CD2   1 
ATOM   288  N N     . GLY A 1 53  ? -23.71300 35.13500 -15.05600 1.000 15.43914 ? 47  GLY A N     1 
ATOM   289  C CA    . GLY A 1 53  ? -23.77500 34.74700 -16.45400 1.000 16.18558 ? 47  GLY A CA    1 
ATOM   290  C C     . GLY A 1 53  ? -22.40600 34.72500 -17.10900 1.000 17.45084 ? 47  GLY A C     1 
ATOM   291  O O     . GLY A 1 53  ? -22.05200 33.77100 -17.80400 1.000 18.18199 ? 47  GLY A O     1 
ATOM   292  N N     . GLU A 1 54  ? -21.61300 35.77700 -16.89100 1.000 17.47282 ? 48  GLU A N     1 
ATOM   293  C CA    . GLU A 1 54  ? -20.25600 35.78900 -17.44100 1.000 18.93154 ? 48  GLU A CA    1 
ATOM   294  C C     . GLU A 1 54  ? -19.43400 34.62000 -16.90800 1.000 16.14491 ? 48  GLU A C     1 
ATOM   295  O O     . GLU A 1 54  ? -18.74600 33.92700 -17.66800 1.000 15.88029 ? 48  GLU A O     1 
ATOM   296  C CB    . GLU A 1 54  ? -19.55500 37.10900 -17.11400 1.000 24.06069 ? 48  GLU A CB    1 
ATOM   297  C CG    . GLU A 1 54  ? -18.22500 37.25700 -17.84900 1.000 31.68190 ? 48  GLU A CG    1 
ATOM   298  C CD    . GLU A 1 54  ? -17.81500 38.69500 -18.10600 1.000 39.16408 ? 48  GLU A CD    1 
ATOM   299  O OE1   . GLU A 1 54  ? -18.00200 39.54400 -17.20500 1.000 42.34357 ? 48  GLU A OE1   1 
ATOM   300  O OE2   . GLU A 1 54  ? -17.26900 38.96800 -19.20100 1.000 42.29436 ? 48  GLU A OE2   1 
ATOM   301  N N     . TYR A 1 55  ? -19.52600 34.37300 -15.60400 1.000 15.00222 ? 49  TYR A N     1 
ATOM   302  C CA    . TYR A 1 55  ? -18.73300 33.33300 -14.95600 1.000 13.41494 ? 49  TYR A CA    1 
ATOM   303  C C     . TYR A 1 55  ? -19.06900 31.94500 -15.48900 1.000 13.86073 ? 49  TYR A C     1 
ATOM   304  O O     . TYR A 1 55  ? -18.16900 31.16000 -15.81700 1.000 14.73422 ? 49  TYR A O     1 
ATOM   305  C CB    . TYR A 1 55  ? -18.99200 33.41500 -13.46100 1.000 14.24758 ? 49  TYR A CB    1 
ATOM   306  C CG    . TYR A 1 55  ? -18.46900 32.32200 -12.58800 1.000 14.47562 ? 49  TYR A CG    1 
ATOM   307  C CD1   . TYR A 1 55  ? -17.16300 32.33900 -12.14100 1.000 15.09088 ? 49  TYR A CD1   1 
ATOM   308  C CD2   . TYR A 1 55  ? -19.32200 31.32400 -12.11600 1.000 15.55435 ? 49  TYR A CD2   1 
ATOM   309  C CE1   . TYR A 1 55  ? -16.68800 31.37300 -11.28000 1.000 17.00466 ? 49  TYR A CE1   1 
ATOM   310  C CE2   . TYR A 1 55  ? -18.86600 30.35800 -11.25500 1.000 16.15727 ? 49  TYR A CE2   1 
ATOM   311  C CZ    . TYR A 1 55  ? -17.54400 30.39400 -10.82800 1.000 17.38786 ? 49  TYR A CZ    1 
ATOM   312  O OH    . TYR A 1 55  ? -17.09300 29.43900 -9.95300  1.000 18.68234 ? 49  TYR A OH    1 
ATOM   313  N N     . TYR A 1 56  ? -20.36100 31.59700 -15.54800 1.000 13.37789 ? 50  TYR A N     1 
ATOM   314  C CA    . TYR A 1 56  ? -20.70400 30.25700 -16.02700 1.000 14.04103 ? 50  TYR A CA    1 
ATOM   315  C C     . TYR A 1 56  ? -20.46100 30.11500 -17.52300 1.000 15.31462 ? 50  TYR A C     1 
ATOM   316  O O     . TYR A 1 56  ? -20.05400 29.04300 -17.99200 1.000 15.47692 ? 50  TYR A O     1 
ATOM   317  C CB    . TYR A 1 56  ? -22.15300 29.91500 -15.68500 1.000 13.48674 ? 50  TYR A CB    1 
ATOM   318  C CG    . TYR A 1 56  ? -22.34800 29.62700 -14.19700 1.000 13.95170 ? 50  TYR A CG    1 
ATOM   319  C CD1   . TYR A 1 56  ? -21.78400 28.49500 -13.59600 1.000 13.38249 ? 50  TYR A CD1   1 
ATOM   320  C CD2   . TYR A 1 56  ? -23.07800 30.49800 -13.39600 1.000 15.18791 ? 50  TYR A CD2   1 
ATOM   321  C CE1   . TYR A 1 56  ? -21.97600 28.23300 -12.23600 1.000 14.81770 ? 50  TYR A CE1   1 
ATOM   322  C CE2   . TYR A 1 56  ? -23.25600 30.26200 -12.04500 1.000 15.78202 ? 50  TYR A CE2   1 
ATOM   323  C CZ    . TYR A 1 56  ? -22.70300 29.12600 -11.46300 1.000 16.34631 ? 50  TYR A CZ    1 
ATOM   324  O OH    . TYR A 1 56  ? -22.88600 28.89500 -10.11500 1.000 18.11570 ? 50  TYR A OH    1 
ATOM   325  N N     . GLU A 1 57  ? -20.70600 31.17500 -18.29400 1.000 15.18749 ? 51  GLU A N     1 
ATOM   326  C CA    . GLU A 1 57  ? -20.43800 31.09500 -19.72500 1.000 15.79187 ? 51  GLU A CA    1 
ATOM   327  C C     . GLU A 1 57  ? -18.95400 30.85300 -19.98800 1.000 16.29281 ? 51  GLU A C     1 
ATOM   328  O O     . GLU A 1 57  ? -18.59400 30.08100 -20.88800 1.000 17.91135 ? 51  GLU A O     1 
ATOM   329  C CB    . GLU A 1 57  ? -20.93000 32.36700 -20.42400 1.000 19.35600 ? 51  GLU A CB    1 
ATOM   330  C CG    . GLU A 1 57  ? -20.49600 32.53300 -21.88800 1.000 23.94958 ? 51  GLU A CG    1 
ATOM   331  C CD    . GLU A 1 57  ? -20.94000 33.86800 -22.46700 1.000 28.62657 ? 51  GLU A CD    1 
ATOM   332  O OE1   . GLU A 1 57  ? -20.56400 34.91700 -21.89300 1.000 31.00401 ? 51  GLU A OE1   1 
ATOM   333  O OE2   . GLU A 1 57  ? -21.67400 33.88100 -23.48400 1.000 30.78687 ? 51  GLU A OE2   1 
ATOM   334  N N     . GLN A 1 58  ? -18.08000 31.48400 -19.19200 1.000 16.40134 ? 52  GLN A N     1 
ATOM   335  C CA    . GLN A 1 58  ? -16.63500 31.30900 -19.35100 1.000 16.50601 ? 52  GLN A CA    1 
ATOM   336  C C     . GLN A 1 58  ? -16.22800 29.84900 -19.20700 1.000 16.26499 ? 52  GLN A C     1 
ATOM   337  O O     . GLN A 1 58  ? -15.28900 29.39100 -19.87000 1.000 16.68820 ? 52  GLN A O     1 
ATOM   338  C CB    . GLN A 1 58  ? -15.89000 32.14700 -18.30500 1.000 17.35925 ? 52  GLN A CB    1 
ATOM   339  C CG    . GLN A 1 58  ? -15.70800 33.60900 -18.66000 1.000 18.63719 ? 52  GLN A CG    1 
ATOM   340  C CD    . GLN A 1 58  ? -14.85400 34.33400 -17.63600 1.000 18.38217 ? 52  GLN A CD    1 
ATOM   341  O OE1   . GLN A 1 58  ? -14.59900 33.81700 -16.54400 1.000 18.30306 ? 52  GLN A OE1   1 
ATOM   342  N NE2   . GLN A 1 58  ? -14.40300 35.53100 -17.98200 1.000 19.26350 ? 52  GLN A NE2   1 
ATOM   343  N N     . ARG A 1 59  ? -16.90500 29.11500 -18.32000 1.000 15.32035 ? 53  ARG A N     1 
ATOM   344  C CA    . ARG A 1 59  ? -16.54400 27.75000 -17.95900 1.000 14.61776 ? 53  ARG A CA    1 
ATOM   345  C C     . ARG A 1 59  ? -17.29300 26.70400 -18.77400 1.000 15.74271 ? 53  ARG A C     1 
ATOM   346  O O     . ARG A 1 59  ? -16.85400 25.54600 -18.84000 1.000 15.73222 ? 53  ARG A O     1 
ATOM   347  C CB    . ARG A 1 59  ? -16.78400 27.57000 -16.45300 1.000 13.81624 ? 53  ARG A CB    1 
ATOM   348  C CG    . ARG A 1 59  ? -15.67200 28.27800 -15.66200 1.000 13.81418 ? 53  ARG A CG    1 
ATOM   349  C CD    . ARG A 1 59  ? -16.03200 28.82300 -14.27400 1.000 14.32113 ? 53  ARG A CD    1 
ATOM   350  N NE    . ARG A 1 59  ? -14.88200 29.55400 -13.74800 1.000 15.34072 ? 53  ARG A NE    1 
ATOM   351  C CZ    . ARG A 1 59  ? -14.52400 30.76700 -14.15100 1.000 14.95330 ? 53  ARG A CZ    1 
ATOM   352  N NH1   . ARG A 1 59  ? -15.31200 31.50200 -14.93300 1.000 14.41235 ? 53  ARG A NH1   1 
ATOM   353  N NH2   . ARG A 1 59  ? -13.34200 31.25500 -13.77200 1.000 14.63148 ? 53  ARG A NH2   1 
ATOM   354  N N     . ALA A 1 60  ? -18.39100 27.09600 -19.40600 1.000 15.11131 ? 54  ALA A N     1 
ATOM   355  C CA    . ALA A 1 60  ? -19.19500 26.17200 -20.19300 1.000 15.73393 ? 54  ALA A CA    1 
ATOM   356  C C     . ALA A 1 60  ? -18.45200 25.71500 -21.44400 1.000 16.14003 ? 54  ALA A C     1 
ATOM   357  O O     . ALA A 1 60  ? -17.74000 26.49600 -22.08400 1.000 18.15004 ? 54  ALA A O     1 
ATOM   358  C CB    . ALA A 1 60  ? -20.51400 26.84000 -20.58400 1.000 14.26121 ? 54  ALA A CB    1 
ATOM   359  N N     . THR A 1 61  ? -18.63900 24.44100 -21.79400 1.000 16.43425 ? 55  THR A N     1 
ATOM   360  C CA    . THR A 1 61  ? -18.10000 23.84400 -23.01200 1.000 14.91406 ? 55  THR A CA    1 
ATOM   361  C C     . THR A 1 61  ? -19.18300 23.00700 -23.67800 1.000 16.86979 ? 55  THR A C     1 
ATOM   362  O O     . THR A 1 61  ? -20.12900 22.54900 -23.02700 1.000 16.17457 ? 55  THR A O     1 
ATOM   363  C CB    . THR A 1 61  ? -16.88800 22.95000 -22.74200 1.000 15.29152 ? 55  THR A CB    1 
ATOM   364  O OG1   . THR A 1 61  ? -17.21500 21.99900 -21.71700 1.000 17.48269 ? 55  THR A OG1   1 
ATOM   365  C CG2   . THR A 1 61  ? -15.68700 23.78800 -22.31600 1.000 15.90092 ? 55  THR A CG2   1 
ATOM   366  N N     . ALA A 1 62  ? -19.02800 22.80600 -24.98700 1.000 17.69575 ? 56  ALA A N     1 
ATOM   367  C CA    . ALA A 1 62  ? -19.95800 21.97600 -25.75100 1.000 17.96975 ? 56  ALA A CA    1 
ATOM   368  C C     . ALA A 1 62  ? -19.97000 20.54700 -25.21400 1.000 18.12309 ? 56  ALA A C     1 
ATOM   369  O O     . ALA A 1 62  ? -18.93600 19.87100 -25.19900 1.000 19.66960 ? 56  ALA A O     1 
ATOM   370  C CB    . ALA A 1 62  ? -19.56600 21.98500 -27.22600 1.000 18.80521 ? 56  ALA A CB    1 
ATOM   371  N N     . GLY A 1 63  ? -21.14200 20.08200 -24.77600 1.000 16.37619 ? 57  GLY A N     1 
ATOM   372  C CA    . GLY A 1 63  ? -21.23100 18.75600 -24.19300 1.000 17.08650 ? 57  GLY A CA    1 
ATOM   373  C C     . GLY A 1 63  ? -20.62900 18.61300 -22.81300 1.000 16.02626 ? 57  GLY A C     1 
ATOM   374  O O     . GLY A 1 63  ? -20.46100 17.48600 -22.34600 1.000 17.03471 ? 57  GLY A O     1 
ATOM   375  N N     . GLY A 1 64  ? -20.28300 19.71700 -22.15100 1.000 14.13301 ? 58  GLY A N     1 
ATOM   376  C CA    . GLY A 1 64  ? -19.79900 19.66900 -20.78200 1.000 13.55807 ? 58  GLY A CA    1 
ATOM   377  C C     . GLY A 1 64  ? -20.92500 19.86600 -19.77900 1.000 15.17238 ? 58  GLY A C     1 
ATOM   378  O O     . GLY A 1 64  ? -21.93300 20.50700 -20.06900 1.000 16.97491 ? 58  GLY A O     1 
ATOM   379  N N     . PHE A 1 65  ? -20.73300 19.30900 -18.58700 1.000 13.63629 ? 59  PHE A N     1 
ATOM   380  C CA    . PHE A 1 65  ? -21.71400 19.35800 -17.50900 1.000 13.41601 ? 59  PHE A CA    1 
ATOM   381  C C     . PHE A 1 65  ? -21.26400 20.34600 -16.43500 1.000 13.78692 ? 59  PHE A C     1 
ATOM   382  O O     . PHE A 1 65  ? -20.12100 20.27700 -15.96000 1.000 13.72178 ? 59  PHE A O     1 
ATOM   383  C CB    . PHE A 1 65  ? -21.91600 17.96600 -16.90300 1.000 14.31585 ? 59  PHE A CB    1 
ATOM   384  C CG    . PHE A 1 65  ? -22.94000 17.91600 -15.78800 1.000 13.38842 ? 59  PHE A CG    1 
ATOM   385  C CD1   . PHE A 1 65  ? -24.10300 18.67200 -15.83900 1.000 15.09999 ? 59  PHE A CD1   1 
ATOM   386  C CD2   . PHE A 1 65  ? -22.72700 17.10700 -14.68000 1.000 12.38032 ? 59  PHE A CD2   1 
ATOM   387  C CE1   . PHE A 1 65  ? -25.02400 18.60600 -14.80600 1.000 16.02987 ? 59  PHE A CE1   1 
ATOM   388  C CE2   . PHE A 1 65  ? -23.65700 17.03400 -13.65100 1.000 13.64362 ? 59  PHE A CE2   1 
ATOM   389  C CZ    . PHE A 1 65  ? -24.79800 17.78900 -13.71200 1.000 15.97403 ? 59  PHE A CZ    1 
ATOM   390  N N     . LEU A 1 66  ? -22.17500 21.24400 -16.03400 1.000 13.70714 ? 60  LEU A N     1 
ATOM   391  C CA    . LEU A 1 66  ? -21.92800 22.27300 -15.02800 1.000 12.59814 ? 60  LEU A CA    1 
ATOM   392  C C     . LEU A 1 66  ? -22.95700 22.14200 -13.91600 1.000 12.64217 ? 60  LEU A C     1 
ATOM   393  O O     . LEU A 1 66  ? -24.13400 21.89800 -14.18100 1.000 14.86869 ? 60  LEU A O     1 
ATOM   394  C CB    . LEU A 1 66  ? -22.03800 23.69400 -15.60300 1.000 15.10552 ? 60  LEU A CB    1 
ATOM   395  C CG    . LEU A 1 66  ? -21.27900 24.13700 -16.85000 1.000 19.42365 ? 60  LEU A CG    1 
ATOM   396  C CD1   . LEU A 1 66  ? -21.56700 25.62100 -17.08500 1.000 20.76915 ? 60  LEU A CD1   1 
ATOM   397  C CD2   . LEU A 1 66  ? -19.79300 23.92100 -16.70200 1.000 22.14872 ? 60  LEU A CD2   1 
ATOM   398  N N     . ILE A 1 67  ? -22.52900 22.33900 -12.67400 1.000 11.91299 ? 61  ILE A N     1 
ATOM   399  C CA    . ILE A 1 67  ? -23.43700 22.39800 -11.53800 1.000 11.72984 ? 61  ILE A CA    1 
ATOM   400  C C     . ILE A 1 67  ? -23.26500 23.77400 -10.90900 1.000 12.73642 ? 61  ILE A C     1 
ATOM   401  O O     . ILE A 1 67  ? -22.12900 24.22100 -10.69400 1.000 13.88063 ? 61  ILE A O     1 
ATOM   402  C CB    . ILE A 1 67  ? -23.17100 21.26700 -10.52500 1.000 13.14798 ? 61  ILE A CB    1 
ATOM   403  C CG1   . ILE A 1 67  ? -23.20100 19.88500 -11.22900 1.000 12.40170 ? 61  ILE A CG1   1 
ATOM   404  C CG2   . ILE A 1 67  ? -24.18900 21.32300 -9.37800  1.000 13.81491 ? 61  ILE A CG2   1 
ATOM   405  C CD1   . ILE A 1 67  ? -22.48500 18.80800 -10.39800 1.000 15.29122 ? 61  ILE A CD1   1 
ATOM   406  N N     . THR A 1 68  ? -24.37900 24.46300 -10.65300 1.000 13.55432 ? 62  THR A N     1 
ATOM   407  C CA    . THR A 1 68  ? -24.28200 25.79900 -10.07500 1.000 13.96515 ? 62  THR A CA    1 
ATOM   408  C C     . THR A 1 68  ? -23.86900 25.75600 -8.60900  1.000 14.25630 ? 62  THR A C     1 
ATOM   409  O O     . THR A 1 68  ? -23.98400 24.74200 -7.91700  1.000 13.36055 ? 62  THR A O     1 
ATOM   410  C CB    . THR A 1 68  ? -25.61200 26.56000 -10.11900 1.000 14.69501 ? 62  THR A CB    1 
ATOM   411  O OG1   . THR A 1 68  ? -26.53900 25.96100 -9.18300  1.000 14.87676 ? 62  THR A OG1   1 
ATOM   412  C CG2   . THR A 1 68  ? -26.19400 26.62800 -11.53300 1.000 15.02528 ? 62  THR A CG2   1 
ATOM   413  N N     . GLU A 1 69  ? -23.44100 26.91800 -8.12900  1.000 14.10053 ? 63  GLU A N     1 
ATOM   414  C CA    . GLU A 1 69  ? -23.40000 27.18500 -6.70100  1.000 14.33898 ? 63  GLU A CA    1 
ATOM   415  C C     . GLU A 1 69  ? -24.69400 26.78000 -5.99900  1.000 13.65460 ? 63  GLU A C     1 
ATOM   416  O O     . GLU A 1 69  ? -25.77600 26.77900 -6.59100  1.000 15.00743 ? 63  GLU A O     1 
ATOM   417  C CB    . GLU A 1 69  ? -23.11400 28.67000 -6.47600  1.000 16.40506 ? 63  GLU A CB    1 
ATOM   418  C CG    . GLU A 1 69  ? -24.26300 29.64600 -6.71700  1.000 18.47116 ? 63  GLU A CG    1 
ATOM   419  C CD    . GLU A 1 69  ? -23.79500 30.90300 -7.47900  1.000 19.10606 ? 63  GLU A CD    1 
ATOM   420  O OE1   . GLU A 1 69  ? -23.38400 30.89000 -8.67700  1.000 19.35738 ? 63  GLU A OE1   1 
ATOM   421  O OE2   . GLU A 1 69  ? -23.87300 31.95400 -6.83600  1.000 18.94742 ? 63  GLU A OE2   1 
ATOM   422  N N     . GLY A 1 70  ? -24.56800 26.42700 -4.72000  1.000 12.86590 ? 64  GLY A N     1 
ATOM   423  C CA    . GLY A 1 70  ? -25.73800 26.13600 -3.90500  1.000 12.26421 ? 64  GLY A CA    1 
ATOM   424  C C     . GLY A 1 70  ? -26.75300 27.26300 -3.94900  1.000 13.58713 ? 64  GLY A C     1 
ATOM   425  O O     . GLY A 1 70  ? -26.39000 28.43000 -3.82500  1.000 14.57315 ? 64  GLY A O     1 
ATOM   426  N N     . THR A 1 71  ? -28.03100 26.93600 -4.13600  1.000 13.26980 ? 65  THR A N     1 
ATOM   427  C CA    . THR A 1 71  ? -29.05600 27.93900 -4.40600  1.000 13.07822 ? 65  THR A CA    1 
ATOM   428  C C     . THR A 1 71  ? -30.16900 27.77700 -3.38400  1.000 14.12288 ? 65  THR A C     1 
ATOM   429  O O     . THR A 1 71  ? -30.59500 26.64400 -3.12600  1.000 14.61793 ? 65  THR A O     1 
ATOM   430  C CB    . THR A 1 71  ? -29.56700 27.76100 -5.84300  1.000 14.35092 ? 65  THR A CB    1 
ATOM   431  O OG1   . THR A 1 71  ? -28.47900 27.99000 -6.74800  1.000 15.50006 ? 65  THR A OG1   1 
ATOM   432  C CG2   . THR A 1 71  ? -30.69900 28.72100 -6.16300  1.000 16.50662 ? 65  THR A CG2   1 
ATOM   433  N N     . MET A 1 72  ? -30.63100 28.88500 -2.78400  1.000 14.41832 ? 66  MET A N     1 
ATOM   434  C CA    . MET A 1 72  ? -31.62700 28.72600 -1.72200  1.000 15.05764 ? 66  MET A CA    1 
ATOM   435  C C     . MET A 1 72  ? -32.97900 28.25200 -2.22500  1.000 14.64735 ? 66  MET A C     1 
ATOM   436  O O     . MET A 1 72  ? -33.43200 28.61000 -3.31400  1.000 14.27564 ? 66  MET A O     1 
ATOM   437  C CB    . MET A 1 72  ? -31.85800 29.96000 -0.82100  1.000 16.51818 ? 66  MET A CB    1 
ATOM   438  C CG    . MET A 1 72  ? -30.70500 30.85800 -0.35800  1.000 15.59557 ? 66  MET A CG    1 
ATOM   439  S SD    . MET A 1 72  ? -31.04200 32.62500 -0.26600  1.000 16.75118 ? 66  MET A SD    1 
ATOM   440  C CE    . MET A 1 72  ? -32.18800 32.62700 1.14400   1.000 16.90914 ? 66  MET A CE    1 
ATOM   441  N N     . ILE A 1 73  ? -33.62000 27.42900 -1.39300  1.000 13.16310 ? 67  ILE A N     1 
ATOM   442  C CA    . ILE A 1 73  ? -34.95200 26.90400 -1.67400  1.000 13.23953 ? 67  ILE A CA    1 
ATOM   443  C C     . ILE A 1 73  ? -36.03600 27.63700 -0.90500  1.000 14.54369 ? 67  ILE A C     1 
ATOM   444  O O     . ILE A 1 73  ? -37.22900 27.38600 -1.15200  1.000 15.52950 ? 67  ILE A O     1 
ATOM   445  C CB    . ILE A 1 73  ? -35.03800 25.39700 -1.35700  1.000 12.72114 ? 67  ILE A CB    1 
ATOM   446  C CG1   . ILE A 1 73  ? -34.78900 25.14700 0.13900   1.000 14.04737 ? 67  ILE A CG1   1 
ATOM   447  C CG2   . ILE A 1 73  ? -34.05000 24.62000 -2.23800  1.000 13.60938 ? 67  ILE A CG2   1 
ATOM   448  C CD1   . ILE A 1 73  ? -35.15700 23.74000 0.60200   1.000 14.55344 ? 67  ILE A CD1   1 
ATOM   449  N N     . SER A 1 74  ? -35.67300 28.54500 -0.01000  1.000 15.70988 ? 68  SER A N     1 
ATOM   450  C CA    . SER A 1 74  ? -36.63800 29.22000 0.85000   1.000 16.28464 ? 68  SER A CA    1 
ATOM   451  C C     . SER A 1 74  ? -35.93400 30.38300 1.54100   1.000 17.12164 ? 68  SER A C     1 
ATOM   452  O O     . SER A 1 74  ? -34.70300 30.41500 1.59300   1.000 16.91959 ? 68  SER A O     1 
ATOM   453  C CB    . SER A 1 74  ? -37.20600 28.25700 1.90000   1.000 17.68669 ? 68  SER A CB    1 
ATOM   454  O OG    . SER A 1 74  ? -36.23200 28.06300 2.90700   1.000 18.90171 ? 68  SER A OG    1 
ATOM   455  N N     . PRO A 1 75  ? -36.69900 31.31900 2.11300   1.000 17.27438 ? 69  PRO A N     1 
ATOM   456  C CA    . PRO A 1 75  ? -36.07700 32.44400 2.83300   1.000 20.22712 ? 69  PRO A CA    1 
ATOM   457  C C     . PRO A 1 75  ? -35.22700 32.04400 4.03100   1.000 20.20883 ? 69  PRO A C     1 
ATOM   458  O O     . PRO A 1 75  ? -34.42500 32.86700 4.49400   1.000 21.77956 ? 69  PRO A O     1 
ATOM   459  C CB    . PRO A 1 75  ? -37.28700 33.28600 3.27300   1.000 21.59038 ? 69  PRO A CB    1 
ATOM   460  C CG    . PRO A 1 75  ? -38.33800 32.98900 2.22900   1.000 20.21196 ? 69  PRO A CG    1 
ATOM   461  C CD    . PRO A 1 75  ? -38.14900 31.53100 1.90100   1.000 17.97029 ? 69  PRO A CD    1 
ATOM   462  N N     . THR A 1 76  ? -35.37200 30.82800 4.56000   1.000 20.80518 ? 70  THR A N     1 
ATOM   463  C CA    . THR A 1 76  ? -34.63100 30.40900 5.74700   1.000 21.32271 ? 70  THR A CA    1 
ATOM   464  C C     . THR A 1 76  ? -33.42400 29.54800 5.41700   1.000 19.31526 ? 70  THR A C     1 
ATOM   465  O O     . THR A 1 76  ? -32.74100 29.07300 6.33100   1.000 19.69437 ? 70  THR A O     1 
ATOM   466  C CB    . THR A 1 76  ? -35.53300 29.62100 6.69500   1.000 23.92532 ? 70  THR A CB    1 
ATOM   467  O OG1   . THR A 1 76  ? -35.99800 28.44100 6.03100   1.000 25.02947 ? 70  THR A OG1   1 
ATOM   468  C CG2   . THR A 1 76  ? -36.71400 30.46100 7.12300   1.000 25.85941 ? 70  THR A CG2   1 
ATOM   469  N N     . SER A 1 77  ? -33.13700 29.33300 4.14700   1.000 17.51791 ? 71  SER A N     1 
ATOM   470  C CA    . SER A 1 77  ? -32.19100 28.28800 3.80300   1.000 17.27297 ? 71  SER A CA    1 
ATOM   471  C C     . SER A 1 77  ? -30.74900 28.76800 3.63400   1.000 15.83855 ? 71  SER A C     1 
ATOM   472  O O     . SER A 1 77  ? -29.88200 27.93400 3.36600   1.000 14.41332 ? 71  SER A O     1 
ATOM   473  C CB    . SER A 1 77  ? -32.67400 27.57000 2.54200   1.000 20.81181 ? 71  SER A CB    1 
ATOM   474  O OG    . SER A 1 77  ? -32.70500 28.46000 1.47400   1.000 22.43079 ? 71  SER A OG    1 
ATOM   475  N N     . ALA A 1 78  ? -30.44600 30.05700 3.82200   1.000 16.93905 ? 72  ALA A N     1 
ATOM   476  C CA    . ALA A 1 78  ? -29.09900 30.57100 3.55700   1.000 16.70254 ? 72  ALA A CA    1 
ATOM   477  C C     . ALA A 1 78  ? -28.24500 30.68600 4.82200   1.000 16.53869 ? 72  ALA A C     1 
ATOM   478  O O     . ALA A 1 78  ? -28.73200 31.02200 5.90500   1.000 16.99008 ? 72  ALA A O     1 
ATOM   479  C CB    . ALA A 1 78  ? -29.15100 31.94500 2.88100   1.000 16.99158 ? 72  ALA A CB    1 
ATOM   480  N N     . GLY A 1 79  ? -26.93700 30.44600 4.65400   1.000 15.76391 ? 73  GLY A N     1 
ATOM   481  C CA    . GLY A 1 79  ? -25.95200 30.68400 5.70200   1.000 15.01168 ? 73  GLY A CA    1 
ATOM   482  C C     . GLY A 1 79  ? -24.67600 31.32400 5.16300   1.000 15.17665 ? 73  GLY A C     1 
ATOM   483  O O     . GLY A 1 79  ? -23.61000 31.21500 5.77900   1.000 15.92332 ? 73  GLY A O     1 
ATOM   484  N N     . PHE A 1 80  ? -24.77400 31.97000 4.00100   1.000 16.16157 ? 74  PHE A N     1 
ATOM   485  C CA    . PHE A 1 80  ? -23.70300 32.71800 3.34700   1.000 16.34087 ? 74  PHE A CA    1 
ATOM   486  C C     . PHE A 1 80  ? -24.30500 33.99800 2.78700   1.000 15.78863 ? 74  PHE A C     1 
ATOM   487  O O     . PHE A 1 80  ? -25.49600 34.02800 2.45300   1.000 16.02230 ? 74  PHE A O     1 
ATOM   488  C CB    . PHE A 1 80  ? -23.04400 31.93700 2.18800   1.000 15.68069 ? 74  PHE A CB    1 
ATOM   489  C CG    . PHE A 1 80  ? -21.93700 30.99000 2.61000   1.000 17.47254 ? 74  PHE A CG    1 
ATOM   490  C CD1   . PHE A 1 80  ? -22.23800 29.73600 3.13500   1.000 18.24281 ? 74  PHE A CD1   1 
ATOM   491  C CD2   . PHE A 1 80  ? -20.60000 31.33800 2.44200   1.000 16.97004 ? 74  PHE A CD2   1 
ATOM   492  C CE1   . PHE A 1 80  ? -21.23100 28.85700 3.51300   1.000 18.44374 ? 74  PHE A CE1   1 
ATOM   493  C CE2   . PHE A 1 80  ? -19.58100 30.45800 2.82300   1.000 18.86111 ? 74  PHE A CE2   1 
ATOM   494  C CZ    . PHE A 1 80  ? -19.90300 29.21800 3.36300   1.000 18.28280 ? 74  PHE A CZ    1 
ATOM   495  N N     . PRO A 1 81  ? -23.51300 35.05500 2.63800   1.000 15.45304 ? 75  PRO A N     1 
ATOM   496  C CA    . PRO A 1 81  ? -24.05100 36.29600 2.05900   1.000 15.56286 ? 75  PRO A CA    1 
ATOM   497  C C     . PRO A 1 81  ? -24.18400 36.20300 0.54600   1.000 14.75189 ? 75  PRO A C     1 
ATOM   498  O O     . PRO A 1 81  ? -23.34200 35.61900 -0.13500  1.000 16.11347 ? 75  PRO A O     1 
ATOM   499  C CB    . PRO A 1 81  ? -23.00200 37.34400 2.44500   1.000 16.06791 ? 75  PRO A CB    1 
ATOM   500  C CG    . PRO A 1 81  ? -21.71000 36.55400 2.45800   1.000 17.62272 ? 75  PRO A CG    1 
ATOM   501  C CD    . PRO A 1 81  ? -22.06600 35.15500 2.92300   1.000 16.60857 ? 75  PRO A CD    1 
ATOM   502  N N     . HIS A 1 82  ? -25.25900 36.79300 0.01900   1.000 13.77163 ? 76  HIS A N     1 
ATOM   503  C CA    . HIS A 1 82  ? -25.39100 37.03000 -1.42100  1.000 14.73474 ? 76  HIS A CA    1 
ATOM   504  C C     . HIS A 1 82  ? -25.25700 35.74500 -2.23900  1.000 15.39895 ? 76  HIS A C     1 
ATOM   505  O O     . HIS A 1 82  ? -24.60900 35.70400 -3.29600  1.000 15.98066 ? 76  HIS A O     1 
ATOM   506  C CB    . HIS A 1 82  ? -24.39700 38.10200 -1.86000  1.000 16.53308 ? 76  HIS A CB    1 
ATOM   507  C CG    . HIS A 1 82  ? -24.56800 39.37000 -1.08600  1.000 18.48457 ? 76  HIS A CG    1 
ATOM   508  N ND1   . HIS A 1 82  ? -25.76400 40.05400 -1.06500  1.000 18.98707 ? 76  HIS A ND1   1 
ATOM   509  C CD2   . HIS A 1 82  ? -23.74400 40.02600 -0.23500  1.000 18.63766 ? 76  HIS A CD2   1 
ATOM   510  C CE1   . HIS A 1 82  ? -25.65800 41.10100 -0.26700  1.000 17.77387 ? 76  HIS A CE1   1 
ATOM   511  N NE2   . HIS A 1 82  ? -24.44500 41.10300 0.25600   1.000 18.74129 ? 76  HIS A NE2   1 
ATOM   512  N N     . VAL A 1 83  ? -25.89000 34.68600 -1.74800  1.000 15.16321 ? 77  VAL A N     1 
ATOM   513  C CA    . VAL A 1 83  ? -26.04600 33.44400 -2.50100  1.000 14.51837 ? 77  VAL A CA    1 
ATOM   514  C C     . VAL A 1 83  ? -27.37900 33.51700 -3.23300  1.000 13.82235 ? 77  VAL A C     1 
ATOM   515  O O     . VAL A 1 83  ? -28.33700 34.10800 -2.72100  1.000 14.42926 ? 77  VAL A O     1 
ATOM   516  C CB    . VAL A 1 83  ? -25.96700 32.22100 -1.57700  1.000 16.31946 ? 77  VAL A CB    1 
ATOM   517  C CG1   . VAL A 1 83  ? -24.58500 32.18500 -0.89400  1.000 16.68905 ? 77  VAL A CG1   1 
ATOM   518  C CG2   . VAL A 1 83  ? -27.08400 32.26000 -0.54000  1.000 17.08077 ? 77  VAL A CG2   1 
ATOM   519  N N     . PRO A 1 84  ? -27.48600 32.95800 -4.42800  1.000 13.77844 ? 78  PRO A N     1 
ATOM   520  C CA    . PRO A 1 84  ? -28.74200 33.07700 -5.17600  1.000 14.24186 ? 78  PRO A CA    1 
ATOM   521  C C     . PRO A 1 84  ? -29.81800 32.19500 -4.58000  1.000 13.38624 ? 78  PRO A C     1 
ATOM   522  O O     . PRO A 1 84  ? -29.53800 31.16300 -3.97000  1.000 14.42715 ? 78  PRO A O     1 
ATOM   523  C CB    . PRO A 1 84  ? -28.36900 32.58500 -6.57200  1.000 13.98503 ? 78  PRO A CB    1 
ATOM   524  C CG    . PRO A 1 84  ? -27.20700 31.61600 -6.30200  1.000 12.19039 ? 78  PRO A CG    1 
ATOM   525  C CD    . PRO A 1 84  ? -26.45800 32.18700 -5.14600  1.000 13.83724 ? 78  PRO A CD    1 
ATOM   526  N N     . GLY A 1 85  ? -31.07200 32.59100 -4.79800  1.000 14.32179 ? 79  GLY A N     1 
ATOM   527  C CA    . GLY A 1 85  ? -32.19800 31.72400 -4.55000  1.000 13.80220 ? 79  GLY A CA    1 
ATOM   528  C C     . GLY A 1 85  ? -32.87300 31.32700 -5.85300  1.000 13.85868 ? 79  GLY A C     1 
ATOM   529  O O     . GLY A 1 85  ? -32.55600 31.82100 -6.94300  1.000 13.70831 ? 79  GLY A O     1 
ATOM   530  N N     . ILE A 1 86  ? -33.81700 30.39900 -5.72600  1.000 14.23929 ? 80  ILE A N     1 
ATOM   531  C CA    . ILE A 1 86  ? -34.67400 30.05300 -6.85900  1.000 15.72258 ? 80  ILE A CA    1 
ATOM   532  C C     . ILE A 1 86  ? -36.08700 29.82300 -6.33400  1.000 17.66852 ? 80  ILE A C     1 
ATOM   533  O O     . ILE A 1 86  ? -36.84700 29.01700 -6.88500  1.000 17.66325 ? 80  ILE A O     1 
ATOM   534  C CB    . ILE A 1 86  ? -34.11500 28.84600 -7.65200  1.000 16.53793 ? 80  ILE A CB    1 
ATOM   535  C CG1   . ILE A 1 86  ? -34.76300 28.75200 -9.05200  1.000 18.32615 ? 80  ILE A CG1   1 
ATOM   536  C CG2   . ILE A 1 86  ? -34.21300 27.52300 -6.85500  1.000 18.59734 ? 80  ILE A CG2   1 
ATOM   537  C CD1   . ILE A 1 86  ? -33.85200 28.14600 -10.09700 1.000 18.92868 ? 80  ILE A CD1   1 
ATOM   538  N N     . PHE A 1 87  ? -36.46400 30.55900 -5.28100  1.000 17.34413 ? 81  PHE A N     1 
ATOM   539  C CA    . PHE A 1 87  ? -37.81400 30.46200 -4.71900  1.000 17.81152 ? 81  PHE A CA    1 
ATOM   540  C C     . PHE A 1 87  ? -38.71600 31.64900 -5.06700  1.000 18.86598 ? 81  PHE A C     1 
ATOM   541  O O     . PHE A 1 87  ? -39.90600 31.61200 -4.73800  1.000 19.94013 ? 81  PHE A O     1 
ATOM   542  C CB    . PHE A 1 87  ? -37.75900 30.27600 -3.18900  1.000 18.18360 ? 81  PHE A CB    1 
ATOM   543  C CG    . PHE A 1 87  ? -37.01800 31.37200 -2.44900  1.000 19.11576 ? 81  PHE A CG    1 
ATOM   544  C CD1   . PHE A 1 87  ? -35.64000 31.30200 -2.27000  1.000 18.61950 ? 81  PHE A CD1   1 
ATOM   545  C CD2   . PHE A 1 87  ? -37.70100 32.45300 -1.91700  1.000 20.13379 ? 81  PHE A CD2   1 
ATOM   546  C CE1   . PHE A 1 87  ? -34.95600 32.30300 -1.59600  1.000 19.15385 ? 81  PHE A CE1   1 
ATOM   547  C CE2   . PHE A 1 87  ? -37.03200 33.45600 -1.23500  1.000 21.14138 ? 81  PHE A CE2   1 
ATOM   548  C CZ    . PHE A 1 87  ? -35.65500 33.38700 -1.07100  1.000 20.49284 ? 81  PHE A CZ    1 
ATOM   549  N N     . THR A 1 88  ? -38.20600 32.68300 -5.73900  1.000 19.88812 ? 82  THR A N     1 
ATOM   550  C CA    . THR A 1 88  ? -39.04100 33.79600 -6.17800  1.000 19.83583 ? 82  THR A CA    1 
ATOM   551  C C     . THR A 1 88  ? -39.07300 33.87600 -7.69900  1.000 20.39014 ? 82  THR A C     1 
ATOM   552  O O     . THR A 1 88  ? -38.15400 33.42100 -8.38800  1.000 19.32638 ? 82  THR A O     1 
ATOM   553  C CB    . THR A 1 88  ? -38.55600 35.14700 -5.63500  1.000 20.53174 ? 82  THR A CB    1 
ATOM   554  O OG1   . THR A 1 88  ? -37.39300 35.55400 -6.36800  1.000 20.52386 ? 82  THR A OG1   1 
ATOM   555  C CG2   . THR A 1 88  ? -38.24300 35.07400 -4.13700  1.000 20.19841 ? 82  THR A CG2   1 
ATOM   556  N N     . LYS A 1 89  ? -40.14000 34.50400 -8.21100  1.000 21.21337 ? 83  LYS A N     1 
ATOM   557  C CA    . LYS A 1 89  ? -40.28500 34.68800 -9.65400  1.000 22.11346 ? 83  LYS A CA    1 
ATOM   558  C C     . LYS A 1 89  ? -39.15500 35.54300 -10.21400 1.000 22.36034 ? 83  LYS A C     1 
ATOM   559  O O     . LYS A 1 89  ? -38.65500 35.27800 -11.31400 1.000 21.60408 ? 83  LYS A O     1 
ATOM   560  C CB    . LYS A 1 89  ? -41.65000 35.31500 -9.97100  1.000 23.50786 ? 83  LYS A CB    1 
ATOM   561  N N     . GLU A 1 90  ? -38.74500 36.57700 -9.47000  1.000 22.80383 ? 84  GLU A N     1 
ATOM   562  C CA    . GLU A 1 90  ? -37.60700 37.40200 -9.87300  1.000 22.46100 ? 84  GLU A CA    1 
ATOM   563  C C     . GLU A 1 90  ? -36.33800 36.57000 -10.03500 1.000 20.16339 ? 84  GLU A C     1 
ATOM   564  O O     . GLU A 1 90  ? -35.58000 36.75300 -10.99700 1.000 19.34954 ? 84  GLU A O     1 
ATOM   565  C CB    . GLU A 1 90  ? -37.36900 38.49900 -8.83900  1.000 24.50564 ? 84  GLU A CB    1 
ATOM   566  C CG    . GLU A 1 90  ? -36.16400 39.36300 -9.16000  1.000 27.93060 ? 84  GLU A CG    1 
ATOM   567  C CD    . GLU A 1 90  ? -36.02400 40.54400 -8.22600  1.000 32.04709 ? 84  GLU A CD    1 
ATOM   568  O OE1   . GLU A 1 90  ? -36.37100 40.39700 -7.02900  1.000 33.42532 ? 84  GLU A OE1   1 
ATOM   569  O OE2   . GLU A 1 90  ? -35.57000 41.61600 -8.68200  1.000 34.08535 ? 84  GLU A OE2   1 
ATOM   570  N N     . GLN A 1 91  ? -36.07400 35.67000 -9.08800  1.000 18.23113 ? 85  GLN A N     1 
ATOM   571  C CA    . GLN A 1 91  ? -34.88300 34.83500 -9.19500  1.000 16.76713 ? 85  GLN A CA    1 
ATOM   572  C C     . GLN A 1 91  ? -34.95800 33.92600 -10.41400 1.000 17.20986 ? 85  GLN A C     1 
ATOM   573  O O     . GLN A 1 91  ? -33.95400 33.72800 -11.10700 1.000 17.38789 ? 85  GLN A O     1 
ATOM   574  C CB    . GLN A 1 91  ? -34.68900 34.01700 -7.91500  1.000 15.56364 ? 85  GLN A CB    1 
ATOM   575  C CG    . GLN A 1 91  ? -34.30400 34.85100 -6.70000  1.000 15.66342 ? 85  GLN A CG    1 
ATOM   576  C CD    . GLN A 1 91  ? -34.70200 34.18300 -5.39500  1.000 16.58152 ? 85  GLN A CD    1 
ATOM   577  O OE1   . GLN A 1 91  ? -35.36400 33.15000 -5.40100  1.000 16.81793 ? 85  GLN A OE1   1 
ATOM   578  N NE2   . GLN A 1 91  ? -34.30500 34.77500 -4.27000  1.000 17.42223 ? 85  GLN A NE2   1 
ATOM   579  N N     . VAL A 1 92  ? -36.14000 33.36700 -10.69300 1.000 15.73616 ? 86  VAL A N     1 
ATOM   580  C CA    . VAL A 1 92  ? -36.30900 32.51400 -11.86900 1.000 17.53723 ? 86  VAL A CA    1 
ATOM   581  C C     . VAL A 1 92  ? -35.99600 33.29200 -13.14400 1.000 18.12704 ? 86  VAL A C     1 
ATOM   582  O O     . VAL A 1 92  ? -35.28100 32.80400 -14.02600 1.000 18.82312 ? 86  VAL A O     1 
ATOM   583  C CB    . VAL A 1 92  ? -37.73200 31.92600 -11.90600 1.000 19.26604 ? 86  VAL A CB    1 
ATOM   584  C CG1   . VAL A 1 92  ? -38.03800 31.31300 -13.28400 1.000 19.66386 ? 86  VAL A CG1   1 
ATOM   585  C CG2   . VAL A 1 92  ? -37.90800 30.89500 -10.80000 1.000 19.69764 ? 86  VAL A CG2   1 
ATOM   586  N N     . ARG A 1 93  ? -36.53500 34.51300 -13.26600 1.000 20.24242 ? 87  ARG A N     1 
ATOM   587  C CA    . ARG A 1 93  ? -36.28700 35.30700 -14.47000 1.000 22.25698 ? 87  ARG A CA    1 
ATOM   588  C C     . ARG A 1 93  ? -34.80700 35.60200 -14.65300 1.000 20.72990 ? 87  ARG A C     1 
ATOM   589  O O     . ARG A 1 93  ? -34.30400 35.58600 -15.78000 1.000 19.11076 ? 87  ARG A O     1 
ATOM   590  C CB    . ARG A 1 93  ? -37.05900 36.62700 -14.44300 1.000 25.91899 ? 87  ARG A CB    1 
ATOM   591  C CG    . ARG A 1 93  ? -38.52800 36.51400 -14.20100 1.000 31.07108 ? 87  ARG A CG    1 
ATOM   592  C CD    . ARG A 1 93  ? -39.19900 37.85700 -14.49500 1.000 35.28760 ? 87  ARG A CD    1 
ATOM   593  N NE    . ARG A 1 93  ? -38.83400 38.86700 -13.50900 1.000 38.14447 ? 87  ARG A NE    1 
ATOM   594  C CZ    . ARG A 1 93  ? -39.58600 39.18800 -12.46600 1.000 39.74399 ? 87  ARG A CZ    1 
ATOM   595  N NH1   . ARG A 1 93  ? -40.74200 38.58600 -12.23800 1.000 40.76221 ? 87  ARG A NH1   1 
ATOM   596  N NH2   . ARG A 1 93  ? -39.16800 40.13700 -11.63100 1.000 40.06177 ? 87  ARG A NH2   1 
ATOM   597  N N     . GLU A 1 94  ? -34.09400 35.89800 -13.56300 1.000 18.13318 ? 88  GLU A N     1 
ATOM   598  C CA    . GLU A 1 94  ? -32.67500 36.20900 -13.70600 1.000 18.92436 ? 88  GLU A CA    1 
ATOM   599  C C     . GLU A 1 94  ? -31.86300 34.95000 -13.99100 1.000 18.10062 ? 88  GLU A C     1 
ATOM   600  O O     . GLU A 1 94  ? -30.90300 34.99000 -14.76900 1.000 19.86262 ? 88  GLU A O     1 
ATOM   601  C CB    . GLU A 1 94  ? -32.15400 36.93100 -12.46000 1.000 21.07629 ? 88  GLU A CB    1 
ATOM   602  C CG    . GLU A 1 94  ? -32.76200 38.32500 -12.25700 1.000 22.79807 ? 88  GLU A CG    1 
ATOM   603  C CD    . GLU A 1 94  ? -32.72600 39.19500 -13.51100 1.000 28.64438 ? 88  GLU A CD    1 
ATOM   604  O OE1   . GLU A 1 94  ? -31.64600 39.34700 -14.13100 1.000 29.11321 ? 88  GLU A OE1   1 
ATOM   605  O OE2   . GLU A 1 94  ? -33.78800 39.75000 -13.86900 1.000 31.78140 ? 88  GLU A OE2   1 
ATOM   606  N N     . TRP A 1 95  ? -32.25000 33.81600 -13.39600 1.000 16.43935 ? 89  TRP A N     1 
ATOM   607  C CA    . TRP A 1 95  ? -31.56000 32.56100 -13.68600 1.000 14.59224 ? 89  TRP A CA    1 
ATOM   608  C C     . TRP A 1 95  ? -31.70600 32.18400 -15.16100 1.000 15.21247 ? 89  TRP A C     1 
ATOM   609  O O     . TRP A 1 95  ? -30.77900 31.63000 -15.76500 1.000 16.62414 ? 89  TRP A O     1 
ATOM   610  C CB    . TRP A 1 95  ? -32.11600 31.44400 -12.80800 1.000 14.36632 ? 89  TRP A CB    1 
ATOM   611  C CG    . TRP A 1 95  ? -31.41400 31.23000 -11.47100 1.000 15.62108 ? 89  TRP A CG    1 
ATOM   612  C CD1   . TRP A 1 95  ? -31.99600 31.26500 -10.22600 1.000 15.61917 ? 89  TRP A CD1   1 
ATOM   613  C CD2   . TRP A 1 95  ? -30.03500 30.88300 -11.25300 1.000 15.84010 ? 89  TRP A CD2   1 
ATOM   614  N NE1   . TRP A 1 95  ? -31.06700 30.98800 -9.25800  1.000 14.83547 ? 89  TRP A NE1   1 
ATOM   615  C CE2   . TRP A 1 95  ? -29.85900 30.73500 -9.86100  1.000 14.94208 ? 89  TRP A CE2   1 
ATOM   616  C CE3   . TRP A 1 95  ? -28.93400 30.68700 -12.09700 1.000 16.47872 ? 89  TRP A CE3   1 
ATOM   617  C CZ2   . TRP A 1 95  ? -28.62600 30.40700 -9.29600  1.000 15.44769 ? 89  TRP A CZ2   1 
ATOM   618  C CZ3   . TRP A 1 95  ? -27.70200 30.36200 -11.52500 1.000 15.03560 ? 89  TRP A CZ3   1 
ATOM   619  C CH2   . TRP A 1 95  ? -27.56400 30.21900 -10.14600 1.000 15.26168 ? 89  TRP A CH2   1 
ATOM   620  N N     . LYS A 1 96  ? -32.86600 32.47800 -15.76000 1.000 16.99894 ? 90  LYS A N     1 
ATOM   621  C CA    . LYS A 1 96  ? -33.09200 32.10800 -17.15500 1.000 19.07402 ? 90  LYS A CA    1 
ATOM   622  C C     . LYS A 1 96  ? -32.06400 32.74300 -18.08300 1.000 18.52773 ? 90  LYS A C     1 
ATOM   623  O O     . LYS A 1 96  ? -31.64600 32.11600 -19.06500 1.000 19.72556 ? 90  LYS A O     1 
ATOM   624  C CB    . LYS A 1 96  ? -34.50900 32.49000 -17.58400 1.000 23.18518 ? 90  LYS A CB    1 
ATOM   625  C CG    . LYS A 1 96  ? -34.88300 31.90900 -18.93800 1.000 30.21293 ? 90  LYS A CG    1 
ATOM   626  C CD    . LYS A 1 96  ? -36.06700 32.61900 -19.56200 1.000 35.54574 ? 90  LYS A CD    1 
ATOM   627  C CE    . LYS A 1 96  ? -37.16700 32.85900 -18.52900 1.000 39.93253 ? 90  LYS A CE    1 
ATOM   628  N NZ    . LYS A 1 96  ? -37.82300 31.60300 -18.03300 1.000 42.18329 ? 90  LYS A NZ    1 
ATOM   629  N N     . LYS A 1 97  ? -31.62400 33.96800 -17.77500 1.000 18.57442 ? 91  LYS A N     1 
ATOM   630  C CA    . LYS A 1 97  ? -30.63200 34.62900 -18.61700 1.000 18.19912 ? 91  LYS A CA    1 
ATOM   631  C C     . LYS A 1 97  ? -29.28400 33.93500 -18.53500 1.000 18.69656 ? 91  LYS A C     1 
ATOM   632  O O     . LYS A 1 97  ? -28.53500 33.89700 -19.52300 1.000 19.54262 ? 91  LYS A O     1 
ATOM   633  C CB    . LYS A 1 97  ? -30.49800 36.09800 -18.21900 1.000 19.62227 ? 91  LYS A CB    1 
ATOM   634  C CG    . LYS A 1 97  ? -31.81600 36.86700 -18.21600 1.000 20.63847 ? 91  LYS A CG    1 
ATOM   635  C CD    . LYS A 1 97  ? -31.58100 38.32100 -17.83500 1.000 24.92875 ? 91  LYS A CD    1 
ATOM   636  C CE    . LYS A 1 97  ? -32.87200 39.02100 -17.50400 1.000 29.01413 ? 91  LYS A CE    1 
ATOM   637  N NZ    . LYS A 1 97  ? -32.61200 40.14300 -16.55900 1.000 32.69480 ? 91  LYS A NZ    1 
ATOM   638  N N     . ILE A 1 98  ? -28.97400 33.36400 -17.38000 1.000 17.85304 ? 92  ILE A N     1 
ATOM   639  C CA    . ILE A 1 98  ? -27.71100 32.65700 -17.19100 1.000 18.35888 ? 92  ILE A CA    1 
ATOM   640  C C     . ILE A 1 98  ? -27.74800 31.29300 -17.86700 1.000 17.26562 ? 92  ILE A C     1 
ATOM   641  O O     . ILE A 1 98  ? -26.80000 30.88700 -18.55800 1.000 17.68934 ? 92  ILE A O     1 
ATOM   642  C CB    . ILE A 1 98  ? -27.42300 32.54400 -15.68200 1.000 18.53490 ? 92  ILE A CB    1 
ATOM   643  C CG1   . ILE A 1 98  ? -27.23200 33.95100 -15.09300 1.000 20.32151 ? 92  ILE A CG1   1 
ATOM   644  C CG2   . ILE A 1 98  ? -26.24200 31.59600 -15.41600 1.000 20.46987 ? 92  ILE A CG2   1 
ATOM   645  C CD1   . ILE A 1 98  ? -27.51600 34.05500 -13.60300 1.000 22.28021 ? 92  ILE A CD1   1 
ATOM   646  N N     . VAL A 1 99  ? -28.84100 30.55400 -17.66700 1.000 16.06509 ? 93  VAL A N     1 
ATOM   647  C CA    . VAL A 1 99  ? -28.99400 29.26500 -18.33800 1.000 15.72499 ? 93  VAL A CA    1 
ATOM   648  C C     . VAL A 1 99  ? -28.90900 29.43500 -19.85200 1.000 17.23753 ? 93  VAL A C     1 
ATOM   649  O O     . VAL A 1 99  ? -28.31700 28.60400 -20.55200 1.000 18.05454 ? 93  VAL A O     1 
ATOM   650  C CB    . VAL A 1 99  ? -30.31600 28.59800 -17.91300 1.000 16.38054 ? 93  VAL A CB    1 
ATOM   651  C CG1   . VAL A 1 99  ? -30.52100 27.29700 -18.68500 1.000 18.80799 ? 93  VAL A CG1   1 
ATOM   652  C CG2   . VAL A 1 99  ? -30.32700 28.34700 -16.42200 1.000 17.21020 ? 93  VAL A CG2   1 
ATOM   653  N N     . ASP A 1 100 ? -29.48800 30.51700 -20.37900 1.000 18.26620 ? 94  ASP A N     1 
ATOM   654  C CA    . ASP A 1 100 ? -29.48400 30.72100 -21.82200 1.000 19.63623 ? 94  ASP A CA    1 
ATOM   655  C C     . ASP A 1 100 ? -28.06400 30.86900 -22.36600 1.000 18.89378 ? 94  ASP A C     1 
ATOM   656  O O     . ASP A 1 100 ? -27.73100 30.27600 -23.39900 1.000 18.78312 ? 94  ASP A O     1 
ATOM   657  C CB    . ASP A 1 100 ? -30.33700 31.93600 -22.19100 1.000 22.55867 ? 94  ASP A CB    1 
ATOM   658  C CG    . ASP A 1 100 ? -31.84300 31.65400 -22.09300 1.000 26.13105 ? 94  ASP A CG    1 
ATOM   659  O OD1   . ASP A 1 100 ? -32.23400 30.49200 -21.86600 1.000 28.11343 ? 94  ASP A OD1   1 
ATOM   660  O OD2   . ASP A 1 100 ? -32.64400 32.59800 -22.25100 1.000 27.84991 ? 94  ASP A OD2   1 
ATOM   661  N N     . VAL A 1 101 ? -27.20400 31.64100 -21.69000 1.000 18.80981 ? 95  VAL A N     1 
ATOM   662  C CA    . VAL A 1 101 ? -25.84900 31.79500 -22.22100 1.000 18.32064 ? 95  VAL A CA    1 
ATOM   663  C C     . VAL A 1 101 ? -25.04900 30.50000 -22.06400 1.000 17.77598 ? 95  VAL A C     1 
ATOM   664  O O     . VAL A 1 101 ? -24.16000 30.21000 -22.87800 1.000 18.95421 ? 95  VAL A O     1 
ATOM   665  C CB    . VAL A 1 101 ? -25.11900 33.01200 -21.59500 1.000 20.91493 ? 95  VAL A CB    1 
ATOM   666  C CG1   . VAL A 1 101 ? -25.92800 34.28800 -21.79300 1.000 23.02690 ? 95  VAL A CG1   1 
ATOM   667  C CG2   . VAL A 1 101 ? -24.80600 32.81200 -20.12500 1.000 21.60974 ? 95  VAL A CG2   1 
ATOM   668  N N     . VAL A 1 102 ? -25.36100 29.68300 -21.05500 1.000 16.15388 ? 96  VAL A N     1 
ATOM   669  C CA    . VAL A 1 102 ? -24.67800 28.40100 -20.91500 1.000 14.91006 ? 96  VAL A CA    1 
ATOM   670  C C     . VAL A 1 102 ? -25.14400 27.42500 -21.99200 1.000 16.67696 ? 96  VAL A C     1 
ATOM   671  O O     . VAL A 1 102 ? -24.33200 26.73400 -22.62700 1.000 16.40444 ? 96  VAL A O     1 
ATOM   672  C CB    . VAL A 1 102 ? -24.90200 27.85300 -19.49200 1.000 15.81004 ? 96  VAL A CB    1 
ATOM   673  C CG1   . VAL A 1 102 ? -24.53000 26.38000 -19.41400 1.000 18.35526 ? 96  VAL A CG1   1 
ATOM   674  C CG2   . VAL A 1 102 ? -24.09500 28.69100 -18.48000 1.000 15.96030 ? 96  VAL A CG2   1 
ATOM   675  N N     . HIS A 1 103 ? -26.45500 27.36300 -22.23500 1.000 17.12067 ? 97  HIS A N     1 
ATOM   676  C CA    . HIS A 1 103 ? -26.95300 26.52000 -23.32000 1.000 16.25382 ? 97  HIS A CA    1 
ATOM   677  C C     . HIS A 1 103 ? -26.47900 26.99100 -24.69000 1.000 16.38657 ? 97  HIS A C     1 
ATOM   678  O O     . HIS A 1 103 ? -26.34600 26.17300 -25.60700 1.000 18.30241 ? 97  HIS A O     1 
ATOM   679  C CB    . HIS A 1 103 ? -28.47700 26.43800 -23.31500 1.000 16.18182 ? 97  HIS A CB    1 
ATOM   680  C CG    . HIS A 1 103 ? -29.02800 25.56700 -22.24000 1.000 16.36719 ? 97  HIS A CG    1 
ATOM   681  N ND1   . HIS A 1 103 ? -30.34200 25.63200 -21.82800 1.000 18.66422 ? 97  HIS A ND1   1 
ATOM   682  C CD2   . HIS A 1 103 ? -28.43500 24.62700 -21.46400 1.000 15.27176 ? 97  HIS A CD2   1 
ATOM   683  C CE1   . HIS A 1 103 ? -30.54100 24.74000 -20.87000 1.000 18.24490 ? 97  HIS A CE1   1 
ATOM   684  N NE2   . HIS A 1 103 ? -29.39800 24.12100 -20.63000 1.000 16.91642 ? 97  HIS A NE2   1 
ATOM   685  N N     . ALA A 1 104 ? -26.22400 28.29200 -24.85600 1.000 17.35726 ? 98  ALA A N     1 
ATOM   686  C CA    . ALA A 1 104 ? -25.69200 28.76500 -26.12900 1.000 18.47395 ? 98  ALA A CA    1 
ATOM   687  C C     . ALA A 1 104 ? -24.31800 28.17800 -26.42000 1.000 20.34394 ? 98  ALA A C     1 
ATOM   688  O O     . ALA A 1 104 ? -23.89900 28.14100 -27.58500 1.000 21.76625 ? 98  ALA A O     1 
ATOM   689  C CB    . ALA A 1 104 ? -25.61800 30.29000 -26.14600 1.000 18.92488 ? 98  ALA A CB    1 
ATOM   690  N N     . LYS A 1 105 ? -23.60700 27.72900 -25.39100 1.000 20.04563 ? 99  LYS A N     1 
ATOM   691  C CA    . LYS A 1 105 ? -22.33000 27.06900 -25.58900 1.000 21.09178 ? 99  LYS A CA    1 
ATOM   692  C C     . LYS A 1 105 ? -22.46900 25.55900 -25.72000 1.000 19.49184 ? 99  LYS A C     1 
ATOM   693  O O     . LYS A 1 105 ? -21.46300 24.87800 -25.93700 1.000 20.49175 ? 99  LYS A O     1 
ATOM   694  C CB    . LYS A 1 105 ? -21.37300 27.41700 -24.44300 1.000 24.22757 ? 99  LYS A CB    1 
ATOM   695  C CG    . LYS A 1 105 ? -20.73900 28.79900 -24.56400 1.000 27.62029 ? 99  LYS A CG    1 
ATOM   696  C CD    . LYS A 1 105 ? -19.23200 28.65900 -24.74000 1.000 30.02142 ? 99  LYS A CD    1 
ATOM   697  C CE    . LYS A 1 105 ? -18.48100 29.80100 -24.10100 1.000 31.61849 ? 99  LYS A CE    1 
ATOM   698  N NZ    . LYS A 1 105 ? -17.32400 29.26700 -23.35300 1.000 31.32452 ? 99  LYS A NZ    1 
ATOM   699  N N     . GLY A 1 106 ? -23.68200 25.02100 -25.60700 1.000 18.41126 ? 100 GLY A N     1 
ATOM   700  C CA    . GLY A 1 106 ? -23.86700 23.58900 -25.73000 1.000 19.68607 ? 100 GLY A CA    1 
ATOM   701  C C     . GLY A 1 106 ? -23.60400 22.80700 -24.46200 1.000 18.47375 ? 100 GLY A C     1 
ATOM   702  O O     . GLY A 1 106 ? -23.44700 21.58300 -24.52200 1.000 18.11913 ? 100 GLY A O     1 
ATOM   703  N N     . ALA A 1 107 ? -23.53700 23.47400 -23.31700 1.000 17.06547 ? 101 ALA A N     1 
ATOM   704  C CA    . ALA A 1 107 ? -23.34300 22.80400 -22.04100 1.000 16.28932 ? 101 ALA A CA    1 
ATOM   705  C C     . ALA A 1 107 ? -24.68200 22.35900 -21.45000 1.000 15.91080 ? 101 ALA A C     1 
ATOM   706  O O     . ALA A 1 107 ? -25.75600 22.84900 -21.82300 1.000 16.83659 ? 101 ALA A O     1 
ATOM   707  C CB    . ALA A 1 107 ? -22.61600 23.71700 -21.04600 1.000 17.51272 ? 101 ALA A CB    1 
ATOM   708  N N     . VAL A 1 108 ? -24.59300 21.40200 -20.52600 1.000 14.09825 ? 102 VAL A N     1 
ATOM   709  C CA    . VAL A 1 108 ? -25.70100 20.95300 -19.68800 1.000 13.68768 ? 102 VAL A CA    1 
ATOM   710  C C     . VAL A 1 108 ? -25.48700 21.54400 -18.30400 1.000 13.19650 ? 102 VAL A C     1 
ATOM   711  O O     . VAL A 1 108 ? -24.35200 21.55600 -17.80700 1.000 14.74776 ? 102 VAL A O     1 
ATOM   712  C CB    . VAL A 1 108 ? -25.73800 19.41000 -19.62800 1.000 14.30803 ? 102 VAL A CB    1 
ATOM   713  C CG1   . VAL A 1 108 ? -26.78100 18.92500 -18.62900 1.000 15.49828 ? 102 VAL A CG1   1 
ATOM   714  C CG2   . VAL A 1 108 ? -25.96200 18.82300 -21.02000 1.000 16.12168 ? 102 VAL A CG2   1 
ATOM   715  N N     . ILE A 1 109 ? -26.54900 22.03100 -17.66000 1.000 12.97919 ? 103 ILE A N     1 
ATOM   716  C CA    . ILE A 1 109 ? -26.36800 22.70700 -16.37700 1.000 12.41906 ? 103 ILE A CA    1 
ATOM   717  C C     . ILE A 1 109 ? -27.48300 22.31600 -15.41000 1.000 12.55615 ? 103 ILE A C     1 
ATOM   718  O O     . ILE A 1 109 ? -28.67100 22.35400 -15.76100 1.000 14.01721 ? 103 ILE A O     1 
ATOM   719  C CB    . ILE A 1 109 ? -26.27100 24.24300 -16.53000 1.000 14.62008 ? 103 ILE A CB    1 
ATOM   720  C CG1   . ILE A 1 109 ? -26.10400 24.92100 -15.17000 1.000 16.99915 ? 103 ILE A CG1   1 
ATOM   721  C CG2   . ILE A 1 109 ? -27.47200 24.83600 -17.29000 1.000 16.00143 ? 103 ILE A CG2   1 
ATOM   722  C CD1   . ILE A 1 109 ? -25.54200 26.32400 -15.29400 1.000 17.45832 ? 103 ILE A CD1   1 
ATOM   723  N N     . PHE A 1 110 ? -27.08500 21.91500 -14.20200 1.000 12.11345 ? 104 PHE A N     1 
ATOM   724  C CA    . PHE A 1 110 ? -27.98100 21.60900 -13.08900 1.000 13.19087 ? 104 PHE A CA    1 
ATOM   725  C C     . PHE A 1 110 ? -27.88300 22.69700 -12.02600 1.000 14.38957 ? 104 PHE A C     1 
ATOM   726  O O     . PHE A 1 110 ? -26.79700 23.20700 -11.74200 1.000 13.85592 ? 104 PHE A O     1 
ATOM   727  C CB    . PHE A 1 110 ? -27.64200 20.25500 -12.42900 1.000 13.00619 ? 104 PHE A CB    1 
ATOM   728  C CG    . PHE A 1 110 ? -28.22800 19.04600 -13.13200 1.000 12.88786 ? 104 PHE A CG    1 
ATOM   729  C CD1   . PHE A 1 110 ? -28.48200 19.05200 -14.51000 1.000 13.39677 ? 104 PHE A CD1   1 
ATOM   730  C CD2   . PHE A 1 110 ? -28.50700 17.89600 -12.41100 1.000 13.25882 ? 104 PHE A CD2   1 
ATOM   731  C CE1   . PHE A 1 110 ? -29.00700 17.91600 -15.14600 1.000 13.18818 ? 104 PHE A CE1   1 
ATOM   732  C CE2   . PHE A 1 110 ? -29.04000 16.76400 -13.03200 1.000 14.74854 ? 104 PHE A CE2   1 
ATOM   733  C CZ    . PHE A 1 110 ? -29.28900 16.77800 -14.40100 1.000 14.33776 ? 104 PHE A CZ    1 
ATOM   734  N N     . CYS A 1 111 ? -29.00900 23.01100 -11.39500 1.000 12.17824 ? 105 CYS A N     1 
ATOM   735  C CA    . CYS A 1 111 ? -29.03000 23.92600 -10.25900 1.000 13.33128 ? 105 CYS A CA    1 
ATOM   736  C C     . CYS A 1 111 ? -28.93800 23.13800 -8.95700  1.000 14.15893 ? 105 CYS A C     1 
ATOM   737  O O     . CYS A 1 111 ? -29.77500 22.25900 -8.70800  1.000 13.01709 ? 105 CYS A O     1 
ATOM   738  C CB    . CYS A 1 111 ? -30.31400 24.75300 -10.27900 1.000 15.28449 ? 105 CYS A CB    1 
ATOM   739  S SG    . CYS A 1 111 ? -30.47400 25.90200 -8.90200  1.000 15.79778 ? 105 CYS A SG    1 
ATOM   740  N N     . GLN A 1 112 ? -27.94900 23.46100 -8.10800  1.000 13.58578 ? 106 GLN A N     1 
ATOM   741  C CA    . GLN A 1 112 ? -27.85800 22.80600 -6.80400  1.000 13.28752 ? 106 GLN A CA    1 
ATOM   742  C C     . GLN A 1 112 ? -28.80400 23.46200 -5.79700  1.000 14.04331 ? 106 GLN A C     1 
ATOM   743  O O     . GLN A 1 112 ? -28.68100 24.65700 -5.50400  1.000 15.73222 ? 106 GLN A O     1 
ATOM   744  C CB    . GLN A 1 112 ? -26.43200 22.82100 -6.25100  1.000 11.96450 ? 106 GLN A CB    1 
ATOM   745  C CG    . GLN A 1 112 ? -26.33700 21.94800 -4.99700  1.000 12.91562 ? 106 GLN A CG    1 
ATOM   746  C CD    . GLN A 1 112 ? -25.01900 22.06100 -4.28000  1.000 13.09118 ? 106 GLN A CD    1 
ATOM   747  O OE1   . GLN A 1 112 ? -24.67200 23.12300 -3.75200  1.000 12.98595 ? 106 GLN A OE1   1 
ATOM   748  N NE2   . GLN A 1 112 ? -24.29300 20.95300 -4.21600  1.000 13.57801 ? 106 GLN A NE2   1 
ATOM   749  N N     . LEU A 1 113 ? -29.71500 22.67100 -5.23100  1.000 12.45941 ? 107 LEU A N     1 
ATOM   750  C CA    . LEU A 1 113 ? -30.66800 23.15400 -4.23200  1.000 12.15070 ? 107 LEU A CA    1 
ATOM   751  C C     . LEU A 1 113 ? -30.08900 22.95300 -2.83800  1.000 12.92503 ? 107 LEU A C     1 
ATOM   752  O O     . LEU A 1 113 ? -29.80200 21.81700 -2.44900  1.000 12.60168 ? 107 LEU A O     1 
ATOM   753  C CB    . LEU A 1 113 ? -31.98800 22.40200 -4.36300  1.000 12.11194 ? 107 LEU A CB    1 
ATOM   754  C CG    . LEU A 1 113 ? -32.62200 22.49100 -5.75300  1.000 13.56697 ? 107 LEU A CG    1 
ATOM   755  C CD1   . LEU A 1 113 ? -34.00600 21.83700 -5.70000  1.000 13.85654 ? 107 LEU A CD1   1 
ATOM   756  C CD2   . LEU A 1 113 ? -32.75300 23.95000 -6.22300  1.000 14.02689 ? 107 LEU A CD2   1 
ATOM   757  N N     . TRP A 1 114 ? -29.96800 24.03500 -2.07000  1.000 13.53415 ? 108 TRP A N     1 
ATOM   758  C CA    . TRP A 1 114 ? -29.13400 24.05300 -0.87100  1.000 13.47756 ? 108 TRP A CA    1 
ATOM   759  C C     . TRP A 1 114 ? -29.90600 24.66100 0.28900   1.000 15.63452 ? 108 TRP A C     1 
ATOM   760  O O     . TRP A 1 114 ? -30.35600 25.80800 0.20200   1.000 17.40843 ? 108 TRP A O     1 
ATOM   761  C CB    . TRP A 1 114 ? -27.85900 24.86200 -1.14300  1.000 15.25224 ? 108 TRP A CB    1 
ATOM   762  C CG    . TRP A 1 114 ? -26.84300 24.92700 -0.05400  1.000 15.77622 ? 108 TRP A CG    1 
ATOM   763  C CD1   . TRP A 1 114 ? -26.62300 24.01500 0.93600   1.000 17.32476 ? 108 TRP A CD1   1 
ATOM   764  C CD2   . TRP A 1 114 ? -25.87000 25.95700 0.12200   1.000 16.89169 ? 108 TRP A CD2   1 
ATOM   765  N NE1   . TRP A 1 114 ? -25.56300 24.41600 1.72300   1.000 16.99722 ? 108 TRP A NE1   1 
ATOM   766  C CE2   . TRP A 1 114 ? -25.09000 25.61100 1.24300   1.000 17.12988 ? 108 TRP A CE2   1 
ATOM   767  C CE3   . TRP A 1 114 ? -25.58000 27.14500 -0.56100  1.000 17.59406 ? 108 TRP A CE3   1 
ATOM   768  C CZ2   . TRP A 1 114 ? -24.04000 26.41200 1.69800   1.000 18.24780 ? 108 TRP A CZ2   1 
ATOM   769  C CZ3   . TRP A 1 114 ? -24.53200 27.94700 -0.10100  1.000 17.86214 ? 108 TRP A CZ3   1 
ATOM   770  C CH2   . TRP A 1 114 ? -23.77600 27.57100 1.01300   1.000 19.02328 ? 108 TRP A CH2   1 
ATOM   771  N N     . HIS A 1 115 ? -30.04200 23.90200 1.37500   1.000 13.03149 ? 109 HIS A N     1 
ATOM   772  C CA    . HIS A 1 115 ? -30.52900 24.41300 2.65400   1.000 13.99291 ? 109 HIS A CA    1 
ATOM   773  C C     . HIS A 1 115 ? -29.46500 24.14800 3.71600   1.000 14.91010 ? 109 HIS A C     1 
ATOM   774  O O     . HIS A 1 115 ? -29.05700 22.99600 3.91300   1.000 13.96302 ? 109 HIS A O     1 
ATOM   775  C CB    . HIS A 1 115 ? -31.86800 23.76200 3.03500   1.000 13.39614 ? 109 HIS A CB    1 
ATOM   776  C CG    . HIS A 1 115 ? -32.59700 24.48100 4.12700   1.000 13.45626 ? 109 HIS A CG    1 
ATOM   777  N ND1   . HIS A 1 115 ? -31.99100 24.84000 5.31200   1.000 12.60375 ? 109 HIS A ND1   1 
ATOM   778  C CD2   . HIS A 1 115 ? -33.87400 24.92900 4.20700   1.000 14.47364 ? 109 HIS A CD2   1 
ATOM   779  C CE1   . HIS A 1 115 ? -32.86600 25.46900 6.08100   1.000 13.82255 ? 109 HIS A CE1   1 
ATOM   780  N NE2   . HIS A 1 115 ? -34.01600 25.53500 5.43200   1.000 15.00468 ? 109 HIS A NE2   1 
ATOM   781  N N     . VAL A 1 116 ? -29.02100 25.21100 4.40500   1.000 13.48570 ? 110 VAL A N     1 
ATOM   782  C CA    . VAL A 1 116 ? -27.90400 25.07700 5.34700   1.000 12.04388 ? 110 VAL A CA    1 
ATOM   783  C C     . VAL A 1 116 ? -28.31200 24.55800 6.71600   1.000 13.73884 ? 110 VAL A C     1 
ATOM   784  O O     . VAL A 1 116 ? -27.43700 24.20800 7.51400   1.000 13.64813 ? 110 VAL A O     1 
ATOM   785  C CB    . VAL A 1 116 ? -27.16400 26.40900 5.56700   1.000 11.58962 ? 110 VAL A CB    1 
ATOM   786  C CG1   . VAL A 1 116 ? -26.55300 26.88300 4.23600   1.000 12.16856 ? 110 VAL A CG1   1 
ATOM   787  C CG2   . VAL A 1 116 ? -28.10700 27.46000 6.13500   1.000 10.98243 ? 110 VAL A CG2   1 
ATOM   788  N N     . GLY A 1 117 ? -29.60300 24.51500 7.02000   1.000 13.50893 ? 111 GLY A N     1 
ATOM   789  C CA    . GLY A 1 117 ? -30.00900 24.10700 8.35300   1.000 14.26603 ? 111 GLY A CA    1 
ATOM   790  C C     . GLY A 1 117 ? -29.37900 24.98700 9.42200   1.000 13.84292 ? 111 GLY A C     1 
ATOM   791  O O     . GLY A 1 117 ? -29.43600 26.22500 9.35800   1.000 14.13633 ? 111 GLY A O     1 
ATOM   792  N N     . ARG A 1 118 ? -28.76200 24.34200 10.41700  1.000 13.85599 ? 112 ARG A N     1 
ATOM   793  C CA    . ARG A 1 118 ? -28.20900 25.05500 11.56300  1.000 14.20810 ? 112 ARG A CA    1 
ATOM   794  C C     . ARG A 1 118 ? -26.95000 25.83800 11.22400  1.000 14.74828 ? 112 ARG A C     1 
ATOM   795  O O     . ARG A 1 118 ? -26.49700 26.64100 12.05300  1.000 14.90846 ? 112 ARG A O     1 
ATOM   796  C CB    . ARG A 1 118 ? -27.90700 24.08600 12.71400  1.000 13.12360 ? 112 ARG A CB    1 
ATOM   797  C CG    . ARG A 1 118 ? -26.72700 23.15800 12.48400  1.000 13.51614 ? 112 ARG A CG    1 
ATOM   798  C CD    . ARG A 1 118 ? -26.55100 22.20500 13.66000  1.000 14.34218 ? 112 ARG A CD    1 
ATOM   799  N NE    . ARG A 1 118 ? -25.32900 21.41400 13.52400  1.000 14.15269 ? 112 ARG A NE    1 
ATOM   800  C CZ    . ARG A 1 118 ? -24.76300 20.70600 14.49900  1.000 16.20228 ? 112 ARG A CZ    1 
ATOM   801  N NH1   . ARG A 1 118 ? -25.28400 20.65100 15.71900  1.000 15.86453 ? 112 ARG A NH1   1 
ATOM   802  N NH2   . ARG A 1 118 ? -23.64000 20.04200 14.25000  1.000 16.67842 ? 112 ARG A NH2   1 
ATOM   803  N N     . ALA A 1 119 ? -26.38400 25.64000 10.03700  1.000 13.19137 ? 113 ALA A N     1 
ATOM   804  C CA    . ALA A 1 119 ? -25.18200 26.36800 9.63800   1.000 13.65289 ? 113 ALA A CA    1 
ATOM   805  C C     . ALA A 1 119 ? -25.55400 27.75400 9.11100   1.000 15.09484 ? 113 ALA A C     1 
ATOM   806  O O     . ALA A 1 119 ? -25.32900 28.10100 7.95000   1.000 15.16911 ? 113 ALA A O     1 
ATOM   807  C CB    . ALA A 1 119 ? -24.40000 25.56800 8.60500   1.000 13.66107 ? 113 ALA A CB    1 
ATOM   808  N N     . SER A 1 120 ? -26.16100 28.54600 9.99000   1.000 14.37381 ? 114 SER A N     1 
ATOM   809  C CA    . SER A 1 120 ? -26.61000 29.88400 9.62100   1.000 15.29470 ? 114 SER A CA    1 
ATOM   810  C C     . SER A 1 120 ? -26.40700 30.80800 10.82200  1.000 15.35057 ? 114 SER A C     1 
ATOM   811  O O     . SER A 1 120 ? -25.68600 30.48100 11.77000  1.000 15.49695 ? 114 SER A O     1 
ATOM   812  C CB    . SER A 1 120 ? -28.06600 29.84200 9.12700   1.000 16.53967 ? 114 SER A CB    1 
ATOM   813  O OG    . SER A 1 120 ? -28.44500 31.09300 8.56000   1.000 15.67374 ? 114 SER A OG    1 
ATOM   814  N N     . HIS A 1 121 ? -27.03900 31.97900 10.76800  1.000 16.70109 ? 115 HIS A N     1 
ATOM   815  C CA    . HIS A 1 121 ? -26.87700 33.03100 11.75700  1.000 17.59347 ? 115 HIS A CA    1 
ATOM   816  C C     . HIS A 1 121 ? -28.11200 33.91300 11.68100  1.000 16.93505 ? 115 HIS A C     1 
ATOM   817  O O     . HIS A 1 121 ? -28.76200 33.98100 10.63200  1.000 16.67279 ? 115 HIS A O     1 
ATOM   818  C CB    . HIS A 1 121 ? -25.60100 33.83600 11.47600  1.000 16.69246 ? 115 HIS A CB    1 
ATOM   819  C CG    . HIS A 1 121 ? -25.22200 34.80600 12.55600  1.000 17.73651 ? 115 HIS A CG    1 
ATOM   820  N ND1   . HIS A 1 121 ? -25.84400 36.02600 12.71800  1.000 19.42103 ? 115 HIS A ND1   1 
ATOM   821  C CD2   . HIS A 1 121 ? -24.25400 34.74900 13.50400  1.000 19.60481 ? 115 HIS A CD2   1 
ATOM   822  C CE1   . HIS A 1 121 ? -25.29000 36.66900 13.73200  1.000 20.92333 ? 115 HIS A CE1   1 
ATOM   823  N NE2   . HIS A 1 121 ? -24.32100 35.91700 14.22500  1.000 21.36680 ? 115 HIS A NE2   1 
ATOM   824  N N     . GLU A 1 122 ? -28.43300 34.58500 12.80000  1.000 17.15016 ? 116 GLU A N     1 
ATOM   825  C CA    . GLU A 1 122 ? -29.55400 35.52400 12.79600  1.000 19.38058 ? 116 GLU A CA    1 
ATOM   826  C C     . GLU A 1 122 ? -29.46800 36.53100 11.64700  1.000 19.50702 ? 116 GLU A C     1 
ATOM   827  O O     . GLU A 1 122 ? -30.49700 36.91700 11.08600  1.000 18.87768 ? 116 GLU A O     1 
ATOM   828  C CB    . GLU A 1 122 ? -29.63600 36.26600 14.13600  1.000 21.14720 ? 116 GLU A CB    1 
ATOM   829  N N     . VAL A 1 123 ? -28.25900 36.95800 11.26500  1.000 19.21358 ? 117 VAL A N     1 
ATOM   830  C CA    . VAL A 1 123 ? -28.14300 37.96200 10.20900  1.000 19.67740 ? 117 VAL A CA    1 
ATOM   831  C C     . VAL A 1 123 ? -28.62800 37.43300 8.85900   1.000 18.14951 ? 117 VAL A C     1 
ATOM   832  O O     . VAL A 1 123 ? -28.93600 38.23200 7.95900   1.000 18.25518 ? 117 VAL A O     1 
ATOM   833  C CB    . VAL A 1 123 ? -26.69000 38.48500 10.10300  1.000 20.87044 ? 117 VAL A CB    1 
ATOM   834  C CG1   . VAL A 1 123 ? -25.75900 37.45300 9.46000   1.000 19.73178 ? 117 VAL A CG1   1 
ATOM   835  C CG2   . VAL A 1 123 ? -26.64400 39.79400 9.32400   1.000 24.12418 ? 117 VAL A CG2   1 
ATOM   836  N N     . TYR A 1 124 ? -28.69800 36.10800 8.68600   1.000 17.91236 ? 118 TYR A N     1 
ATOM   837  C CA    . TYR A 1 124 ? -29.14500 35.49400 7.44000   1.000 16.97277 ? 118 TYR A CA    1 
ATOM   838  C C     . TYR A 1 124 ? -30.58800 35.02800 7.49300   1.000 18.37121 ? 118 TYR A C     1 
ATOM   839  O O     . TYR A 1 124 ? -31.08200 34.48600 6.50100   1.000 19.35857 ? 118 TYR A O     1 
ATOM   840  C CB    . TYR A 1 124 ? -28.25000 34.29900 7.08200   1.000 16.17236 ? 118 TYR A CB    1 
ATOM   841  C CG    . TYR A 1 124 ? -26.83200 34.70600 6.77400   1.000 14.63292 ? 118 TYR A CG    1 
ATOM   842  C CD1   . TYR A 1 124 ? -26.56300 35.66400 5.80000   1.000 15.11246 ? 118 TYR A CD1   1 
ATOM   843  C CD2   . TYR A 1 124 ? -25.76000 34.14700 7.47800   1.000 13.66654 ? 118 TYR A CD2   1 
ATOM   844  C CE1   . TYR A 1 124 ? -25.24800 36.06000 5.52700   1.000 16.09011 ? 118 TYR A CE1   1 
ATOM   845  C CE2   . TYR A 1 124 ? -24.45300 34.53300 7.22100   1.000 13.95106 ? 118 TYR A CE2   1 
ATOM   846  C CZ    . TYR A 1 124 ? -24.20000 35.48600 6.23800   1.000 15.29258 ? 118 TYR A CZ    1 
ATOM   847  O OH    . TYR A 1 124 ? -22.89800 35.87900 5.97100   1.000 16.12047 ? 118 TYR A OH    1 
ATOM   848  N N     . GLN A 1 125 ? -31.26900 35.20700 8.62700   1.000 19.05972 ? 119 GLN A N     1 
ATOM   849  C CA    . GLN A 1 125 ? -32.58300 34.61400 8.80100   1.000 18.80184 ? 119 GLN A CA    1 
ATOM   850  C C     . GLN A 1 125 ? -33.65100 35.69100 8.80600   1.000 20.92547 ? 119 GLN A C     1 
ATOM   851  O O     . GLN A 1 125 ? -33.41500 36.78700 9.32500   1.000 22.14492 ? 119 GLN A O     1 
ATOM   852  C CB    . GLN A 1 125 ? -32.65400 33.82900 10.11600  1.000 19.59375 ? 119 GLN A CB    1 
ATOM   853  C CG    . GLN A 1 125 ? -31.86900 32.52600 10.08100  1.000 19.48913 ? 119 GLN A CG    1 
ATOM   854  C CD    . GLN A 1 125 ? -32.39700 31.58000 9.02100   1.000 18.82218 ? 119 GLN A CD    1 
ATOM   855  O OE1   . GLN A 1 125 ? -33.60400 31.44800 8.85500   1.000 19.92239 ? 119 GLN A OE1   1 
ATOM   856  N NE2   . GLN A 1 125 ? -31.50000 30.92400 8.29600   1.000 18.10654 ? 119 GLN A NE2   1 
ATOM   857  N N     . PRO A 1 126 ? -34.82400 35.42500 8.24100   1.000 23.28763 ? 120 PRO A N     1 
ATOM   858  C CA    . PRO A 1 126 ? -35.88600 36.43300 8.29200   1.000 26.20369 ? 120 PRO A CA    1 
ATOM   859  C C     . PRO A 1 126 ? -36.25300 36.72100 9.73800   1.000 27.27644 ? 120 PRO A C     1 
ATOM   860  O O     . PRO A 1 126 ? -36.29300 35.81800 10.57800  1.000 27.50612 ? 120 PRO A O     1 
ATOM   861  C CB    . PRO A 1 126 ? -37.04100 35.79200 7.51300   1.000 26.86478 ? 120 PRO A CB    1 
ATOM   862  C CG    . PRO A 1 126 ? -36.72100 34.35800 7.40600   1.000 27.28511 ? 120 PRO A CG    1 
ATOM   863  C CD    . PRO A 1 126 ? -35.24800 34.18100 7.57300   1.000 24.05747 ? 120 PRO A CD    1 
ATOM   864  N N     . ALA A 1 127 ? -36.45400 38.00500 10.03100  1.000 27.05797 ? 121 ALA A N     1 
ATOM   865  C CA    . ALA A 1 127 ? -36.76300 38.49300 11.37100  1.000 27.55843 ? 121 ALA A CA    1 
ATOM   866  C C     . ALA A 1 127 ? -35.71200 38.08900 12.40000  1.000 26.63506 ? 121 ALA A C     1 
ATOM   867  O O     . ALA A 1 127 ? -35.99100 38.08700 13.60200  1.000 27.43593 ? 121 ALA A O     1 
ATOM   868  C CB    . ALA A 1 127 ? -38.15000 38.02200 11.82500  1.000 28.75459 ? 121 ALA A CB    1 
ATOM   869  N N     . GLY A 1 128 ? -34.50400 37.73700 11.96000  1.000 26.69635 ? 122 GLY A N     1 
ATOM   870  C CA    . GLY A 1 128 ? -33.46500 37.32700 12.89500  1.000 27.83197 ? 122 GLY A CA    1 
ATOM   871  C C     . GLY A 1 128 ? -33.80800 36.08600 13.68900  1.000 26.50845 ? 122 GLY A C     1 
ATOM   872  O O     . GLY A 1 128 ? -33.32100 35.91800 14.81500  1.000 27.20801 ? 122 GLY A O     1 
ATOM   873  N N     . ALA A 1 129 ? -34.63700 35.21100 13.13100  1.000 25.08989 ? 123 ALA A N     1 
ATOM   874  C CA    . ALA A 1 129 ? -35.06200 34.00300 13.81600  1.000 25.33975 ? 123 ALA A CA    1 
ATOM   875  C C     . ALA A 1 129 ? -33.93600 32.97700 13.85300  1.000 23.76275 ? 123 ALA A C     1 
ATOM   876  O O     . ALA A 1 129 ? -32.97200 33.03900 13.08200  1.000 22.81128 ? 123 ALA A O     1 
ATOM   877  C CB    . ALA A 1 129 ? -36.28100 33.39500 13.12300  1.000 26.38229 ? 123 ALA A CB    1 
ATOM   878  N N     . ALA A 1 130 ? -34.08800 32.00200 14.75000  1.000 21.75741 ? 124 ALA A N     1 
ATOM   879  C CA    . ALA A 1 130 ? -33.11600 30.92100 14.84600  1.000 20.25732 ? 124 ALA A CA    1 
ATOM   880  C C     . ALA A 1 130 ? -33.16200 30.04300 13.59400  1.000 18.74474 ? 124 ALA A C     1 
ATOM   881  O O     . ALA A 1 130 ? -34.24500 29.76500 13.06300  1.000 18.51828 ? 124 ALA A O     1 
ATOM   882  C CB    . ALA A 1 130 ? -33.38200 30.06200 16.08200  1.000 20.41315 ? 124 ALA A CB    1 
ATOM   883  N N     . PRO A 1 131 ? -32.00900 29.58600 13.10800  1.000 18.02027 ? 125 PRO A N     1 
ATOM   884  C CA    . PRO A 1 131 ? -31.98500 28.59300 12.02700  1.000 16.98267 ? 125 PRO A CA    1 
ATOM   885  C C     . PRO A 1 131 ? -32.67900 27.30500 12.45000  1.000 17.37771 ? 125 PRO A C     1 
ATOM   886  O O     . PRO A 1 131 ? -32.84800 27.02700 13.63800  1.000 19.07002 ? 125 PRO A O     1 
ATOM   887  C CB    . PRO A 1 131 ? -30.48500 28.35400 11.79800  1.000 18.06079 ? 125 PRO A CB    1 
ATOM   888  C CG    . PRO A 1 131 ? -29.77300 29.46000 12.54800  1.000 19.30428 ? 125 PRO A CG    1 
ATOM   889  C CD    . PRO A 1 131 ? -30.67000 29.86600 13.65800  1.000 18.37577 ? 125 PRO A CD    1 
ATOM   890  N N     . ILE A 1 132 ? -33.06500 26.49600 11.46100  1.000 17.02530 ? 126 ILE A N     1 
ATOM   891  C CA    . ILE A 1 132 ? -33.78400 25.24800 11.71800  1.000 17.03166 ? 126 ILE A CA    1 
ATOM   892  C C     . ILE A 1 132 ? -32.83200 24.07400 11.55200  1.000 15.73671 ? 126 ILE A C     1 
ATOM   893  O O     . ILE A 1 132 ? -31.84400 24.14100 10.80800  1.000 15.96438 ? 126 ILE A O     1 
ATOM   894  C CB    . ILE A 1 132 ? -35.01100 25.08000 10.79400  1.000 17.59869 ? 126 ILE A CB    1 
ATOM   895  C CG1   . ILE A 1 132 ? -34.59800 25.03000 9.32100   1.000 18.00609 ? 126 ILE A CG1   1 
ATOM   896  C CG2   . ILE A 1 132 ? -36.03000 26.18000 11.03700  1.000 20.45003 ? 126 ILE A CG2   1 
ATOM   897  C CD1   . ILE A 1 132 ? -35.68000 24.42800 8.45900   1.000 20.86085 ? 126 ILE A CD1   1 
ATOM   898  N N     . SER A 1 133 ? -33.14500 22.96200 12.21800  1.000 15.12819 ? 127 SER A N     1 
ATOM   899  C CA    . SER A 1 133 ? -32.27500 21.79300 12.13300  1.000 14.34565 ? 127 SER A CA    1 
ATOM   900  C C     . SER A 1 133 ? -33.03200 20.54400 12.57200  1.000 15.70773 ? 127 SER A C     1 
ATOM   901  O O     . SER A 1 133 ? -34.18400 20.60200 13.01000  1.000 16.34337 ? 127 SER A O     1 
ATOM   902  C CB    . SER A 1 133 ? -31.01000 21.99100 12.98100  1.000 15.54672 ? 127 SER A CB    1 
ATOM   903  O OG    . SER A 1 133 ? -30.09100 20.93700 12.77400  1.000 16.58969 ? 127 SER A OG    1 
ATOM   904  N N     . SER A 1 134 ? -32.35300 19.39900 12.45800  1.000 14.25971 ? 128 SER A N     1 
ATOM   905  C CA    . SER A 1 134 ? -32.84000 18.17800 13.09500  1.000 15.59172 ? 128 SER A CA    1 
ATOM   906  C C     . SER A 1 134 ? -32.78300 18.28900 14.61000  1.000 17.78054 ? 128 SER A C     1 
ATOM   907  O O     . SER A 1 134 ? -33.55400 17.62900 15.32100  1.000 17.23339 ? 128 SER A O     1 
ATOM   908  C CB    . SER A 1 134 ? -31.98700 16.99500 12.65600  1.000 15.05371 ? 128 SER A CB    1 
ATOM   909  O OG    . SER A 1 134 ? -30.63800 17.23300 13.04600  1.000 16.02051 ? 128 SER A OG    1 
ATOM   910  N N     . THR A 1 135 ? -31.87800 19.11900 15.11000  1.000 18.61932 ? 129 THR A N     1 
ATOM   911  C CA    . THR A 1 135 ? -31.44200 19.12700 16.49300  1.000 19.73780 ? 129 THR A CA    1 
ATOM   912  C C     . THR A 1 135 ? -31.59000 20.53500 17.04900  1.000 17.41768 ? 129 THR A C     1 
ATOM   913  O O     . THR A 1 135 ? -31.72500 21.50100 16.29500  1.000 16.44211 ? 129 THR A O     1 
ATOM   914  C CB    . THR A 1 135 ? -29.96600 18.65700 16.58500  1.000 20.86061 ? 129 THR A CB    1 
ATOM   915  O OG1   . THR A 1 135 ? -29.55200 18.57600 17.95000  1.000 21.44480 ? 129 THR A OG1   1 
ATOM   916  C CG2   . THR A 1 135 ? -29.01700 19.62400 15.83200  1.000 21.11369 ? 129 THR A CG2   1 
ATOM   917  N N     . GLU A 1 136 ? -31.56300 20.65100 18.38000  1.000 18.34924 ? 130 GLU A N     1 
ATOM   918  C CA    . GLU A 1 136 ? -31.42100 21.95700 19.01800  1.000 19.94873 ? 130 GLU A CA    1 
ATOM   919  C C     . GLU A 1 136 ? -29.98300 22.28500 19.39700  1.000 19.40927 ? 130 GLU A C     1 
ATOM   920  O O     . GLU A 1 136 ? -29.75500 23.31500 20.02800  1.000 19.99275 ? 130 GLU A O     1 
ATOM   921  C CB    . GLU A 1 136 ? -32.30500 22.07200 20.27200  1.000 26.59007 ? 130 GLU A CB    1 
ATOM   922  C CG    . GLU A 1 136 ? -33.72000 21.56000 20.12500  1.000 33.47104 ? 130 GLU A CG    1 
ATOM   923  C CD    . GLU A 1 136 ? -34.51500 21.68900 21.42400  1.000 39.48465 ? 130 GLU A CD    1 
ATOM   924  O OE1   . GLU A 1 136 ? -33.91500 21.51700 22.50900  1.000 41.79199 ? 130 GLU A OE1   1 
ATOM   925  O OE2   . GLU A 1 136 ? -35.73800 21.95000 21.36100  1.000 42.39006 ? 130 GLU A OE2   1 
ATOM   926  N N     . LYS A 1 137 ? -29.02700 21.59300 19.08700  1.000 18.94921 ? 131 LYS A N     1 
ATOM   927  C CA    . LYS A 1 137 ? -27.62000 21.81400 19.41400  1.000 19.70239 ? 131 LYS A CA    1 
ATOM   928  C C     . LYS A 1 137 ? -26.94800 22.65200 18.32700  1.000 18.35098 ? 131 LYS A C     1 
ATOM   929  O O     . LYS A 1 137 ? -27.12900 22.37700 17.12800  1.000 17.81095 ? 131 LYS A O     1 
ATOM   930  C CB    . LYS A 1 137 ? -26.87300 20.48700 19.51500  1.000 22.29876 ? 131 LYS A CB    1 
ATOM   931  C CG    . LYS A 1 137 ? -27.34400 19.51000 20.56800  1.000 27.34006 ? 131 LYS A CG    1 
ATOM   932  C CD    . LYS A 1 137 ? -27.13200 20.11600 21.96700  1.000 31.49217 ? 131 LYS A CD    1 
ATOM   933  C CE    . LYS A 1 137 ? -27.51300 19.17000 23.13900  1.000 34.34018 ? 131 LYS A CE    1 
ATOM   934  N NZ    . LYS A 1 137 ? -27.35900 19.69100 24.53100  1.000 37.37428 ? 131 LYS A NZ    1 
ATOM   935  N N     . PRO A 1 138 ? -26.17000 23.58000 18.84200  1.000 16.18612 ? 132 PRO A N     1 
ATOM   936  C CA    . PRO A 1 138 ? -25.38900 24.40200 17.91000  1.000 16.35240 ? 132 PRO A CA    1 
ATOM   937  C C     . PRO A 1 138 ? -24.17700 23.66200 17.37100  1.000 16.66294 ? 132 PRO A C     1 
ATOM   938  O O     . PRO A 1 138 ? -23.64000 22.74700 17.99800  1.000 17.69701 ? 132 PRO A O     1 
ATOM   939  C CB    . PRO A 1 138 ? -24.92100 25.58400 18.77200  1.000 18.20134 ? 132 PRO A CB    1 
ATOM   940  C CG    . PRO A 1 138 ? -25.24700 25.21600 20.21500  1.000 18.68381 ? 132 PRO A CG    1 
ATOM   941  C CD    . PRO A 1 138 ? -25.79100 23.82600 20.24400  1.000 18.18259 ? 132 PRO A CD    1 
ATOM   942  N N     . ILE A 1 139 ? -23.73500 24.09000 16.18600  1.000 14.83661 ? 133 ILE A N     1 
ATOM   943  C CA    . ILE A 1 139 ? -22.36400 23.79600 15.78400  1.000 14.52684 ? 133 ILE A CA    1 
ATOM   944  C C     . ILE A 1 139 ? -21.42600 24.35800 16.84800  1.000 16.91381 ? 133 ILE A C     1 
ATOM   945  O O     . ILE A 1 139 ? -21.65100 25.45100 17.38200  1.000 17.44118 ? 133 ILE A O     1 
ATOM   946  C CB    . ILE A 1 139 ? -22.07300 24.38700 14.39300  1.000 15.18116 ? 133 ILE A CB    1 
ATOM   947  C CG1   . ILE A 1 139 ? -22.97500 23.74100 13.32100  1.000 14.82834 ? 133 ILE A CG1   1 
ATOM   948  C CG2   . ILE A 1 139 ? -20.58900 24.23400 14.03400  1.000 17.18314 ? 133 ILE A CG2   1 
ATOM   949  C CD1   . ILE A 1 139 ? -23.08700 24.54300 12.02600  1.000 17.05690 ? 133 ILE A CD1   1 
ATOM   950  N N     . SER A 1 140 ? -20.36800 23.61300 17.16900  1.000 17.68567 ? 134 SER A N     1 
ATOM   951  C CA    . SER A 1 140 ? -19.46500 24.04000 18.23000  1.000 17.66180 ? 134 SER A CA    1 
ATOM   952  C C     . SER A 1 140 ? -18.60900 25.21700 17.76900  1.000 19.33869 ? 134 SER A C     1 
ATOM   953  O O     . SER A 1 140 ? -18.50700 25.51600 16.58200  1.000 18.54625 ? 134 SER A O     1 
ATOM   954  C CB    . SER A 1 140 ? -18.56900 22.88600 18.67900  1.000 18.47187 ? 134 SER A CB    1 
ATOM   955  O OG    . SER A 1 140 ? -17.61100 22.56700 17.67400  1.000 20.20445 ? 134 SER A OG    1 
ATOM   956  N N     . ASN A 1 141 ? -17.98600 25.90100 18.73100  1.000 22.08964 ? 135 ASN A N     1 
ATOM   957  C CA    . ASN A 1 141 ? -17.16100 27.04500 18.35500  1.000 26.33575 ? 135 ASN A CA    1 
ATOM   958  C C     . ASN A 1 141 ? -15.81800 26.64000 17.74900  1.000 25.79850 ? 135 ASN A C     1 
ATOM   959  O O     . ASN A 1 141 ? -14.97900 27.51300 17.50100  1.000 28.24642 ? 135 ASN A O     1 
ATOM   960  C CB    . ASN A 1 141 ? -16.95600 27.98300 19.55000  1.000 30.27340 ? 135 ASN A CB    1 
ATOM   961  C CG    . ASN A 1 141 ? -16.20700 27.33200 20.69800  1.000 33.14942 ? 135 ASN A CG    1 
ATOM   962  O OD1   . ASN A 1 141 ? -15.81300 26.16300 20.63300  1.000 33.69661 ? 135 ASN A OD1   1 
ATOM   963  N ND2   . ASN A 1 141 ? -16.01300 28.09300 21.76900  1.000 34.55309 ? 135 ASN A ND2   1 
ATOM   964  N N     . ARG A 1 142 ? -15.60200 25.34900 17.48900  1.000 23.70557 ? 136 ARG A N     1 
ATOM   965  C CA    . ARG A 1 142 ? -14.52100 24.93900 16.59500  1.000 24.11774 ? 136 ARG A CA    1 
ATOM   966  C C     . ARG A 1 142 ? -14.70700 25.48900 15.18400  1.000 22.49196 ? 136 ARG A C     1 
ATOM   967  O O     . ARG A 1 142 ? -13.75200 25.51400 14.40000  1.000 25.20205 ? 136 ARG A O     1 
ATOM   968  C CB    . ARG A 1 142 ? -14.43600 23.41000 16.54400  1.000 25.86289 ? 136 ARG A CB    1 
ATOM   969  N N     . TRP A 1 143 ? -15.91000 25.93000 14.85000  1.000 19.81960 ? 137 TRP A N     1 
ATOM   970  C CA    . TRP A 1 143 ? -16.25100 26.41900 13.52800  1.000 18.33172 ? 137 TRP A CA    1 
ATOM   971  C C     . TRP A 1 143 ? -16.82200 27.82100 13.66000  1.000 19.57372 ? 137 TRP A C     1 
ATOM   972  O O     . TRP A 1 143 ? -17.47800 28.13800 14.65600  1.000 21.01166 ? 137 TRP A O     1 
ATOM   973  C CB    . TRP A 1 143 ? -17.28500 25.50100 12.86200  1.000 19.42404 ? 137 TRP A CB    1 
ATOM   974  C CG    . TRP A 1 143 ? -16.88200 24.06200 12.82600  1.000 21.44651 ? 137 TRP A CG    1 
ATOM   975  C CD1   . TRP A 1 143 ? -17.15400 23.10700 13.76800  1.000 21.04697 ? 137 TRP A CD1   1 
ATOM   976  C CD2   . TRP A 1 143 ? -16.13500 23.40500 11.79100  1.000 24.01387 ? 137 TRP A CD2   1 
ATOM   977  N NE1   . TRP A 1 143 ? -16.61300 21.89900 13.38500  1.000 22.77224 ? 137 TRP A NE1   1 
ATOM   978  C CE2   . TRP A 1 143 ? -15.99200 22.05300 12.17200  1.000 24.34218 ? 137 TRP A CE2   1 
ATOM   979  C CE3   . TRP A 1 143 ? -15.57800 23.82600 10.57700  1.000 26.58254 ? 137 TRP A CE3   1 
ATOM   980  C CZ2   . TRP A 1 143 ? -15.30900 21.12500 11.38900  1.000 24.79118 ? 137 TRP A CZ2   1 
ATOM   981  C CZ3   . TRP A 1 143 ? -14.90400 22.89800 9.79600   1.000 27.56578 ? 137 TRP A CZ3   1 
ATOM   982  C CH2   . TRP A 1 143 ? -14.77800 21.56400 10.20600  1.000 27.24929 ? 137 TRP A CH2   1 
ATOM   983  N N     . ARG A 1 144 ? -16.56400 28.66600 12.65800  1.000 18.76374 ? 138 ARG A N     1 
ATOM   984  C CA    . ARG A 1 144 ? -17.10500 30.02200 12.62800  1.000 21.15971 ? 138 ARG A CA    1 
ATOM   985  C C     . ARG A 1 144 ? -17.73600 30.30300 11.27600  1.000 19.53282 ? 138 ARG A C     1 
ATOM   986  O O     . ARG A 1 144 ? -17.29200 29.78400 10.25200  1.000 20.98939 ? 138 ARG A O     1 
ATOM   987  C CB    . ARG A 1 144 ? -16.03000 31.09400 12.88700  1.000 23.86957 ? 138 ARG A CB    1 
ATOM   988  C CG    . ARG A 1 144 ? -15.29900 30.95500 14.20600  1.000 27.11994 ? 138 ARG A CG    1 
ATOM   989  C CD    . ARG A 1 144 ? -16.21700 31.30400 15.36900  1.000 31.12577 ? 138 ARG A CD    1 
ATOM   990  N NE    . ARG A 1 144 ? -15.75000 30.71300 16.61700  1.000 35.48293 ? 138 ARG A NE    1 
ATOM   991  C CZ    . ARG A 1 144 ? -14.89600 31.30300 17.44100  1.000 37.94221 ? 138 ARG A CZ    1 
ATOM   992  N NH1   . ARG A 1 144 ? -14.42000 32.51300 17.19000  1.000 38.26868 ? 138 ARG A NH1   1 
ATOM   993  N NH2   . ARG A 1 144 ? -14.51000 30.66300 18.54400  1.000 39.73809 ? 138 ARG A NH2   1 
ATOM   994  N N     . ILE A 1 145 ? -18.75900 31.15900 11.27100  1.000 16.33491 ? 139 ILE A N     1 
ATOM   995  C CA    . ILE A 1 145 ? -19.51300 31.45500 10.05800  1.000 15.59961 ? 139 ILE A CA    1 
ATOM   996  C C     . ILE A 1 145 ? -19.01900 32.76400 9.45400   1.000 17.12127 ? 139 ILE A C     1 
ATOM   997  O O     . ILE A 1 145 ? -18.78500 33.75200 10.16400  1.000 17.98774 ? 139 ILE A O     1 
ATOM   998  C CB    . ILE A 1 145 ? -21.03300 31.50300 10.34600  1.000 15.59827 ? 139 ILE A CB    1 
ATOM   999  C CG1   . ILE A 1 145 ? -21.83000 31.62000 9.04100   1.000 15.06053 ? 139 ILE A CG1   1 
ATOM   1000 C CG2   . ILE A 1 145 ? -21.38900 32.64700 11.30600  1.000 17.31971 ? 139 ILE A CG2   1 
ATOM   1001 C CD1   . ILE A 1 145 ? -23.32500 31.48500 9.20500   1.000 16.02359 ? 139 ILE A CD1   1 
ATOM   1002 N N     . LEU A 1 146 ? -18.86600 32.77500 8.13300   1.000 16.20461 ? 140 LEU A N     1 
ATOM   1003 C CA    . LEU A 1 146 ? -18.58000 34.01400 7.41200   1.000 15.46332 ? 140 LEU A CA    1 
ATOM   1004 C C     . LEU A 1 146 ? -19.78900 34.95500 7.49400   1.000 15.49631 ? 140 LEU A C     1 
ATOM   1005 O O     . LEU A 1 146 ? -20.89900 34.59100 7.09400   1.000 16.98164 ? 140 LEU A O     1 
ATOM   1006 C CB    . LEU A 1 146 ? -18.22800 33.70200 5.95900   1.000 16.67578 ? 140 LEU A CB    1 
ATOM   1007 C CG    . LEU A 1 146 ? -17.97000 34.90800 5.05300   1.000 16.04103 ? 140 LEU A CG    1 
ATOM   1008 C CD1   . LEU A 1 146 ? -16.72900 35.65900 5.51000   1.000 17.45208 ? 140 LEU A CD1   1 
ATOM   1009 C CD2   . LEU A 1 146 ? -17.86900 34.46800 3.57600   1.000 17.93042 ? 140 LEU A CD2   1 
ATOM   1010 N N     . MET A 1 147 ? -19.58300 36.14300 8.04400   1.000 15.53343 ? 141 MET A N     1 
ATOM   1011 C CA    . MET A 1 147 ? -20.52200 37.25900 8.15700   1.000 15.16302 ? 141 MET A CA    1 
ATOM   1012 C C     . MET A 1 147 ? -20.54600 38.12200 6.90400   1.000 16.25379 ? 141 MET A C     1 
ATOM   1013 O O     . MET A 1 147 ? -19.60000 38.11800 6.11500   1.000 15.32966 ? 141 MET A O     1 
ATOM   1014 C CB    . MET A 1 147 ? -20.16600 38.11300 9.37400   1.000 15.58082 ? 141 MET A CB    1 
ATOM   1015 C CG    . MET A 1 147 ? -20.24400 37.48800 10.78600  1.000 18.48744 ? 141 MET A CG    1 
ATOM   1016 S SD    . MET A 1 147 ? -21.77100 36.53400 11.08400  1.000 21.12400 ? 141 MET A SD    1 
ATOM   1017 C CE    . MET A 1 147 ? -22.79200 37.89300 11.64800  1.000 22.73095 ? 141 MET A CE    1 
ATOM   1018 N N     . PRO A 1 148 ? -21.62600 38.88200 6.69200   1.000 16.92126 ? 142 PRO A N     1 
ATOM   1019 C CA    . PRO A 1 148 ? -21.68600 39.74000 5.49600   1.000 17.93348 ? 142 PRO A CA    1 
ATOM   1020 C C     . PRO A 1 148 ? -20.58000 40.77700 5.43800   1.000 17.18710 ? 142 PRO A C     1 
ATOM   1021 O O     . PRO A 1 148 ? -20.22900 41.21100 4.33200   1.000 18.23565 ? 142 PRO A O     1 
ATOM   1022 C CB    . PRO A 1 148 ? -23.07200 40.39700 5.60200   1.000 19.58946 ? 142 PRO A CB    1 
ATOM   1023 C CG    . PRO A 1 148 ? -23.86500 39.46400 6.45100   1.000 19.15551 ? 142 PRO A CG    1 
ATOM   1024 C CD    . PRO A 1 148 ? -22.89000 38.91100 7.44700   1.000 17.71601 ? 142 PRO A CD    1 
ATOM   1025 N N     . ASP A 1 149 ? -20.00900 41.18400 6.57900   1.000 14.97378 ? 143 ASP A N     1 
ATOM   1026 C CA    . ASP A 1 149 ? -18.93700 42.17300 6.55100   1.000 16.52541 ? 143 ASP A CA    1 
ATOM   1027 C C     . ASP A 1 149 ? -17.55300 41.54700 6.42300   1.000 17.42154 ? 143 ASP A C     1 
ATOM   1028 O O     . ASP A 1 149 ? -16.55500 42.26300 6.51300   1.000 20.47220 ? 143 ASP A O     1 
ATOM   1029 C CB    . ASP A 1 149 ? -18.99100 43.08400 7.79100   1.000 18.88709 ? 143 ASP A CB    1 
ATOM   1030 C CG    . ASP A 1 149 ? -18.80500 42.33500 9.10400   1.000 20.48741 ? 143 ASP A CG    1 
ATOM   1031 O OD1   . ASP A 1 149 ? -18.48100 41.12400 9.10500   1.000 21.28842 ? 143 ASP A OD1   1 
ATOM   1032 O OD2   . ASP A 1 149 ? -18.96400 42.98500 10.15900  1.000 22.04741 ? 143 ASP A OD2   1 
ATOM   1033 N N     . GLY A 1 150 ? -17.46900 40.24000 6.20200   1.000 18.62982 ? 144 GLY A N     1 
ATOM   1034 C CA    . GLY A 1 150 ? -16.19500 39.58500 6.02500   1.000 19.43614 ? 144 GLY A CA    1 
ATOM   1035 C C     . GLY A 1 150 ? -15.53300 39.11800 7.29900   1.000 19.40522 ? 144 GLY A C     1 
ATOM   1036 O O     . GLY A 1 150 ? -14.45800 38.50300 7.22900   1.000 21.15636 ? 144 GLY A O     1 
ATOM   1037 N N     . THR A 1 151 ? -16.12600 39.39000 8.46000   1.000 19.55150 ? 145 THR A N     1 
ATOM   1038 C CA    . THR A 1 151 ? -15.62400 38.82300 9.69900   1.000 19.92295 ? 145 THR A CA    1 
ATOM   1039 C C     . THR A 1 151 ? -16.19300 37.41800 9.88200   1.000 19.75997 ? 145 THR A C     1 
ATOM   1040 O O     . THR A 1 151 ? -16.99100 36.92700 9.07600   1.000 18.85168 ? 145 THR A O     1 
ATOM   1041 C CB    . THR A 1 151 ? -15.99100 39.69200 10.90200  1.000 21.87543 ? 145 THR A CB    1 
ATOM   1042 O OG1   . THR A 1 151 ? -17.41500 39.69300 11.08400  1.000 20.01951 ? 145 THR A OG1   1 
ATOM   1043 C CG2   . THR A 1 151 ? -15.49400 41.12300 10.71800  1.000 24.41388 ? 145 THR A CG2   1 
ATOM   1044 N N     . HIS A 1 152 ? -15.81500 36.76800 10.97500  1.000 19.66653 ? 146 HIS A N     1 
ATOM   1045 C CA    . HIS A 1 152 ? -16.34000 35.44900 11.27700  1.000 20.28557 ? 146 HIS A CA    1 
ATOM   1046 C C     . HIS A 1 152 ? -17.08900 35.49700 12.59100  1.000 20.17518 ? 146 HIS A C     1 
ATOM   1047 O O     . HIS A 1 152 ? -16.59100 36.04700 13.57300  1.000 23.34138 ? 146 HIS A O     1 
ATOM   1048 C CB    . HIS A 1 152 ? -15.22000 34.40900 11.27900  1.000 23.23361 ? 146 HIS A CB    1 
ATOM   1049 C CG    . HIS A 1 152 ? -14.75700 34.08600 9.89500   1.000 26.30507 ? 146 HIS A CG    1 
ATOM   1050 N ND1   . HIS A 1 152 ? -13.87900 34.89100 9.20300   1.000 28.26354 ? 146 HIS A ND1   1 
ATOM   1051 C CD2   . HIS A 1 152 ? -15.13100 33.10900 9.03600   1.000 27.90183 ? 146 HIS A CD2   1 
ATOM   1052 C CE1   . HIS A 1 152 ? -13.68900 34.39300 7.99500   1.000 29.26925 ? 146 HIS A CE1   1 
ATOM   1053 N NE2   . HIS A 1 152 ? -14.44000 33.31400 7.86700   1.000 29.23530 ? 146 HIS A NE2   1 
ATOM   1054 N N     . GLY A 1 153 ? -18.29600 34.93200 12.59200  1.000 17.36163 ? 147 GLY A N     1 
ATOM   1055 C CA    . GLY A 1 153 ? -19.16700 34.96200 13.74200  1.000 17.09109 ? 147 GLY A CA    1 
ATOM   1056 C C     . GLY A 1 153 ? -19.41600 33.57400 14.30900  1.000 18.76141 ? 147 GLY A C     1 
ATOM   1057 O O     . GLY A 1 153 ? -18.84400 32.57300 13.86900  1.000 18.34177 ? 147 GLY A O     1 
ATOM   1058 N N     . ILE A 1 154 ? -20.29200 33.54300 15.30800  1.000 18.74827 ? 148 ILE A N     1 
ATOM   1059 C CA    . ILE A 1 154 ? -20.60900 32.33300 16.05200  1.000 19.17140 ? 148 ILE A CA    1 
ATOM   1060 C C     . ILE A 1 154 ? -21.90800 31.73300 15.54100  1.000 18.07553 ? 148 ILE A C     1 
ATOM   1061 O O     . ILE A 1 154 ? -22.92400 32.43600 15.41800  1.000 18.87135 ? 148 ILE A O     1 
ATOM   1062 C CB    . ILE A 1 154 ? -20.69500 32.62400 17.56000  1.000 21.92827 ? 148 ILE A CB    1 
ATOM   1063 C CG1   . ILE A 1 154 ? -19.49100 33.44500 18.01000  1.000 24.25430 ? 148 ILE A CG1   1 
ATOM   1064 C CG2   . ILE A 1 154 ? -20.91200 31.36000 18.36800  1.000 20.05230 ? 148 ILE A CG2   1 
ATOM   1065 C CD1   . ILE A 1 154 ? -19.84600 34.58000 18.94800  1.000 28.44415 ? 148 ILE A CD1   1 
ATOM   1066 N N     . TYR A 1 155 ? -21.87900 30.42900 15.27500  1.000 17.55576 ? 149 TYR A N     1 
ATOM   1067 C CA    . TYR A 1 155 ? -23.10400 29.69500 14.94200  1.000 17.56150 ? 149 TYR A CA    1 
ATOM   1068 C C     . TYR A 1 155 ? -24.03200 29.66800 16.15200  1.000 18.38131 ? 149 TYR A C     1 
ATOM   1069 O O     . TYR A 1 155 ? -23.60300 29.29000 17.24800  1.000 17.96418 ? 149 TYR A O     1 
ATOM   1070 C CB    . TYR A 1 155 ? -22.79500 28.26900 14.51600  1.000 16.88426 ? 149 TYR A CB    1 
ATOM   1071 C CG    . TYR A 1 155 ? -22.11700 28.14800 13.17300  1.000 15.92562 ? 149 TYR A CG    1 
ATOM   1072 C CD1   . TYR A 1 155 ? -22.82100 28.34000 11.98600  1.000 15.63235 ? 149 TYR A CD1   1 
ATOM   1073 C CD2   . TYR A 1 155 ? -20.76800 27.83600 13.09000  1.000 16.73826 ? 149 TYR A CD2   1 
ATOM   1074 C CE1   . TYR A 1 155 ? -22.19500 28.21200 10.75300  1.000 17.03792 ? 149 TYR A CE1   1 
ATOM   1075 C CE2   . TYR A 1 155 ? -20.13100 27.72600 11.86400  1.000 16.24119 ? 149 TYR A CE2   1 
ATOM   1076 C CZ    . TYR A 1 155 ? -20.84900 27.91700 10.70000  1.000 17.70074 ? 149 TYR A CZ    1 
ATOM   1077 O OH    . TYR A 1 155 ? -20.22300 27.80700 9.48100   1.000 18.41622 ? 149 TYR A OH    1 
ATOM   1078 N N     . PRO A 1 156 ? -25.29900 30.02300 15.99200  1.000 19.57084 ? 150 PRO A N     1 
ATOM   1079 C CA    . PRO A 1 156 ? -26.24200 30.03600 17.11200  1.000 18.91427 ? 150 PRO A CA    1 
ATOM   1080 C C     . PRO A 1 156 ? -26.89400 28.67500 17.33600  1.000 18.83470 ? 150 PRO A C     1 
ATOM   1081 O O     . PRO A 1 156 ? -26.74200 27.74300 16.54400  1.000 19.65928 ? 150 PRO A O     1 
ATOM   1082 C CB    . PRO A 1 156 ? -27.29200 31.04600 16.65100  1.000 19.51463 ? 150 PRO A CB    1 
ATOM   1083 C CG    . PRO A 1 156 ? -27.34100 30.82900 15.15100  1.000 20.40408 ? 150 PRO A CG    1 
ATOM   1084 C CD    . PRO A 1 156 ? -25.91000 30.51500 14.74200  1.000 19.83207 ? 150 PRO A CD    1 
ATOM   1085 N N     . LYS A 1 157 ? -27.63400 28.59100 18.43700  1.000 17.90023 ? 151 LYS A N     1 
ATOM   1086 C CA    . LYS A 1 157 ? -28.47100 27.43200 18.72200  1.000 18.06243 ? 151 LYS A CA    1 
ATOM   1087 C C     . LYS A 1 157 ? -29.61200 27.35900 17.71000  1.000 19.14583 ? 151 LYS A C     1 
ATOM   1088 O O     . LYS A 1 157 ? -30.32300 28.35200 17.52500  1.000 20.30344 ? 151 LYS A O     1 
ATOM   1089 C CB    . LYS A 1 157 ? -29.02300 27.56000 20.14500  1.000 21.30885 ? 151 LYS A CB    1 
ATOM   1090 C CG    . LYS A 1 157 ? -29.59900 26.30000 20.71700  1.000 24.83752 ? 151 LYS A CG    1 
ATOM   1091 C CD    . LYS A 1 157 ? -30.10200 26.53800 22.13200  1.000 25.09104 ? 151 LYS A CD    1 
ATOM   1092 C CE    . LYS A 1 157 ? -30.86100 25.32100 22.68000  1.000 27.53548 ? 151 LYS A CE    1 
ATOM   1093 N NZ    . LYS A 1 157 ? -30.09100 24.01700 22.64800  1.000 28.30851 ? 151 LYS A NZ    1 
ATOM   1094 N N     . PRO A 1 158 ? -29.81100 26.23100 17.03000  1.000 18.51273 ? 152 PRO A N     1 
ATOM   1095 C CA    . PRO A 1 158 ? -30.91800 26.11300 16.07800  1.000 17.08835 ? 152 PRO A CA    1 
ATOM   1096 C C     . PRO A 1 158 ? -32.19600 25.68400 16.78400  1.000 17.53342 ? 152 PRO A C     1 
ATOM   1097 O O     . PRO A 1 158 ? -32.19800 25.31700 17.95700  1.000 18.82495 ? 152 PRO A O     1 
ATOM   1098 C CB    . PRO A 1 158 ? -30.45600 25.00400 15.12600  1.000 18.16880 ? 152 PRO A CB    1 
ATOM   1099 C CG    . PRO A 1 158 ? -29.61900 24.11900 15.98500  1.000 18.32569 ? 152 PRO A CG    1 
ATOM   1100 C CD    . PRO A 1 158 ? -28.94500 25.03800 17.01400  1.000 18.90490 ? 152 PRO A CD    1 
ATOM   1101 N N     . ARG A 1 159 ? -33.28100 25.68600 16.01700  1.000 17.52986 ? 153 ARG A N     1 
ATOM   1102 C CA    . ARG A 1 159 ? -34.56800 25.17500 16.46300  1.000 19.17256 ? 153 ARG A CA    1 
ATOM   1103 C C     . ARG A 1 159 ? -34.82400 23.83200 15.78800  1.000 18.52051 ? 153 ARG A C     1 
ATOM   1104 O O     . ARG A 1 159 ? -34.68500 23.71000 14.56400  1.000 16.85169 ? 153 ARG A O     1 
ATOM   1105 C CB    . ARG A 1 159 ? -35.66100 26.19200 16.13200  1.000 20.83003 ? 153 ARG A CB    1 
ATOM   1106 C CG    . ARG A 1 159 ? -37.07100 25.72600 16.31000  1.000 23.14244 ? 153 ARG A CG    1 
ATOM   1107 C CD    . ARG A 1 159 ? -38.01800 26.92900 16.16400  1.000 23.91527 ? 153 ARG A CD    1 
ATOM   1108 N NE    . ARG A 1 159 ? -38.15100 27.39000 14.78600  1.000 22.82461 ? 153 ARG A NE    1 
ATOM   1109 C CZ    . ARG A 1 159 ? -38.81100 26.72900 13.84000  1.000 24.24600 ? 153 ARG A CZ    1 
ATOM   1110 N NH1   . ARG A 1 159 ? -39.39200 25.56500 14.08700  1.000 25.49621 ? 153 ARG A NH1   1 
ATOM   1111 N NH2   . ARG A 1 159 ? -38.91400 27.26000 12.62500  1.000 24.26733 ? 153 ARG A NH2   1 
ATOM   1112 N N     . ALA A 1 160 ? -35.16100 22.81700 16.58300  1.000 18.29328 ? 154 ALA A N     1 
ATOM   1113 C CA    . ALA A 1 160 ? -35.43600 21.49500 16.02900  1.000 19.09116 ? 154 ALA A CA    1 
ATOM   1114 C C     . ALA A 1 160 ? -36.86200 21.45400 15.50700  1.000 18.84801 ? 154 ALA A C     1 
ATOM   1115 O O     . ALA A 1 160 ? -37.80300 21.79400 16.23000  1.000 20.14567 ? 154 ALA A O     1 
ATOM   1116 C CB    . ALA A 1 160 ? -35.22600 20.40700 17.08000  1.000 18.94155 ? 154 ALA A CB    1 
ATOM   1117 N N     . ILE A 1 161 ? -37.02700 21.04000 14.26000  1.000 17.41651 ? 155 ILE A N     1 
ATOM   1118 C CA    . ILE A 1 161 ? -38.33200 21.12300 13.60900  1.000 16.23365 ? 155 ILE A CA    1 
ATOM   1119 C C     . ILE A 1 161 ? -39.10700 19.82400 13.77500  1.000 17.18539 ? 155 ILE A C     1 
ATOM   1120 O O     . ILE A 1 161 ? -38.53900 18.73200 13.84400  1.000 19.60511 ? 155 ILE A O     1 
ATOM   1121 C CB    . ILE A 1 161 ? -38.16300 21.48800 12.12100  1.000 16.54382 ? 155 ILE A CB    1 
ATOM   1122 C CG1   . ILE A 1 161 ? -37.30500 20.44100 11.39500  1.000 17.19566 ? 155 ILE A CG1   1 
ATOM   1123 C CG2   . ILE A 1 161 ? -37.51600 22.87200 12.00400  1.000 17.99309 ? 155 ILE A CG2   1 
ATOM   1124 C CD1   . ILE A 1 161 ? -37.19800 20.68800 9.88300   1.000 18.83460 ? 155 ILE A CD1   1 
ATOM   1125 N N     . GLY A 1 162 ? -40.43500 19.94900 13.81600  1.000 16.19295 ? 156 GLY A N     1 
ATOM   1126 C CA    . GLY A 1 162 ? -41.31300 18.79700 13.84100  1.000 15.52789 ? 156 GLY A CA    1 
ATOM   1127 C C     . GLY A 1 162 ? -41.58100 18.23600 12.45100  1.000 15.70577 ? 156 GLY A C     1 
ATOM   1128 O O     . GLY A 1 162 ? -41.07900 18.72200 11.43100  1.000 15.64219 ? 156 GLY A O     1 
ATOM   1129 N N     . THR A 1 163 ? -42.39800 17.17500 12.41300  1.000 15.50997 ? 157 THR A N     1 
ATOM   1130 C CA    . THR A 1 163 ? -42.59200 16.46800 11.14400  1.000 15.01790 ? 157 THR A CA    1 
ATOM   1131 C C     . THR A 1 163 ? -43.46200 17.25000 10.16200  1.000 15.10429 ? 157 THR A C     1 
ATOM   1132 O O     . THR A 1 163 ? -43.26000 17.12700 8.94700   1.000 15.92206 ? 157 THR A O     1 
ATOM   1133 C CB    . THR A 1 163 ? -43.17400 15.06200 11.35900  1.000 14.79534 ? 157 THR A CB    1 
ATOM   1134 O OG1   . THR A 1 163 ? -44.53500 15.14100 11.80500  1.000 16.41700 ? 157 THR A OG1   1 
ATOM   1135 C CG2   . THR A 1 163 ? -42.37000 14.28600 12.36600  1.000 14.61395 ? 157 THR A CG2   1 
ATOM   1136 N N     . TYR A 1 164 ? -44.41900 18.06200 10.63900  1.000 14.87199 ? 158 TYR A N     1 
ATOM   1137 C CA    . TYR A 1 164 ? -45.10900 18.96800 9.71900   1.000 15.86893 ? 158 TYR A CA    1 
ATOM   1138 C C     . TYR A 1 164 ? -44.10800 19.89200 9.03600   1.000 15.24523 ? 158 TYR A C     1 
ATOM   1139 O O     . TYR A 1 164 ? -44.09500 20.03100 7.80300   1.000 14.97033 ? 158 TYR A O     1 
ATOM   1140 C CB    . TYR A 1 164 ? -46.13700 19.82500 10.46200  1.000 16.51565 ? 158 TYR A CB    1 
ATOM   1141 C CG    . TYR A 1 164 ? -46.73600 20.91900 9.59600   1.000 18.07528 ? 158 TYR A CG    1 
ATOM   1142 C CD1   . TYR A 1 164 ? -47.31700 20.64200 8.35800   1.000 18.82655 ? 158 TYR A CD1   1 
ATOM   1143 C CD2   . TYR A 1 164 ? -46.55700 22.25200 9.94100   1.000 19.29378 ? 158 TYR A CD2   1 
ATOM   1144 C CE1   . TYR A 1 164 ? -47.81800 21.66500 7.56000   1.000 19.42255 ? 158 TYR A CE1   1 
ATOM   1145 C CE2   . TYR A 1 164 ? -47.02900 23.26800 9.15000   1.000 19.90876 ? 158 TYR A CE2   1 
ATOM   1146 C CZ    . TYR A 1 164 ? -47.66400 22.98100 7.96800   1.000 20.88427 ? 158 TYR A CZ    1 
ATOM   1147 O OH    . TYR A 1 164 ? -48.13600 24.03900 7.20300   1.000 24.99134 ? 158 TYR A OH    1 
ATOM   1148 N N     . GLU A 1 165 ? -43.26000 20.54100 9.83400   1.000 14.07780 ? 159 GLU A N     1 
ATOM   1149 C CA    . GLU A 1 165 ? -42.27500 21.44900 9.26000   1.000 14.89941 ? 159 GLU A CA    1 
ATOM   1150 C C     . GLU A 1 165 ? -41.31200 20.73700 8.31900   1.000 14.43825 ? 159 GLU A C     1 
ATOM   1151 O O     . GLU A 1 165 ? -40.93600 21.29200 7.27500   1.000 14.75777 ? 159 GLU A O     1 
ATOM   1152 C CB    . GLU A 1 165 ? -41.50600 22.16700 10.35900  1.000 17.28690 ? 159 GLU A CB    1 
ATOM   1153 C CG    . GLU A 1 165 ? -40.76600 23.36900 9.79700   1.000 21.35270 ? 159 GLU A CG    1 
ATOM   1154 C CD    . GLU A 1 165 ? -40.37600 24.38000 10.84000  1.000 24.74904 ? 159 GLU A CD    1 
ATOM   1155 O OE1   . GLU A 1 165 ? -40.80500 24.22600 12.00700  1.000 26.40379 ? 159 GLU A OE1   1 
ATOM   1156 O OE2   . GLU A 1 165 ? -39.68600 25.35900 10.46800  1.000 26.35626 ? 159 GLU A OE2   1 
ATOM   1157 N N     . ILE A 1 166 ? -40.88100 19.52600 8.67800   1.000 15.73730 ? 160 ILE A N     1 
ATOM   1158 C CA    . ILE A 1 166 ? -40.06500 18.72800 7.75900   1.000 15.81375 ? 160 ILE A CA    1 
ATOM   1159 C C     . ILE A 1 166 ? -40.77500 18.57300 6.41900   1.000 15.42146 ? 160 ILE A C     1 
ATOM   1160 O O     . ILE A 1 166 ? -40.17400 18.74700 5.34800   1.000 16.35595 ? 160 ILE A O     1 
ATOM   1161 C CB    . ILE A 1 166 ? -39.74800 17.35400 8.37100   1.000 15.77202 ? 160 ILE A CB    1 
ATOM   1162 C CG1   . ILE A 1 166 ? -38.74200 17.49300 9.52400   1.000 15.87750 ? 160 ILE A CG1   1 
ATOM   1163 C CG2   . ILE A 1 166 ? -39.28700 16.37400 7.27000   1.000 16.45939 ? 160 ILE A CG2   1 
ATOM   1164 C CD1   . ILE A 1 166 ? -38.53200 16.22400 10.33500  1.000 16.24546 ? 160 ILE A CD1   1 
ATOM   1165 N N     . SER A 1 167 ? -42.06900 18.23400 6.46100   1.000 14.33596 ? 161 SER A N     1 
ATOM   1166 C CA    . SER A 1 167 ? -42.81200 18.07100 5.21500   1.000 15.80630 ? 161 SER A CA    1 
ATOM   1167 C C     . SER A 1 167 ? -42.87800 19.37300 4.42000   1.000 15.92464 ? 161 SER A C     1 
ATOM   1168 O O     . SER A 1 167 ? -42.89700 19.33800 3.18400   1.000 15.18087 ? 161 SER A O     1 
ATOM   1169 C CB    . SER A 1 167 ? -44.21900 17.51900 5.49700   1.000 15.92583 ? 161 SER A CB    1 
ATOM   1170 O OG    . SER A 1 167 ? -45.12300 18.50300 5.98700   1.000 15.86215 ? 161 SER A OG    1 
ATOM   1171 N N     . GLN A 1 168 ? -42.88100 20.52900 5.09900   1.000 14.38697 ? 162 GLN A N     1 
ATOM   1172 C CA    . GLN A 1 168 ? -42.89600 21.79200 4.37400   1.000 16.05535 ? 162 GLN A CA    1 
ATOM   1173 C C     . GLN A 1 168 ? -41.53200 22.12400 3.77700   1.000 15.61955 ? 162 GLN A C     1 
ATOM   1174 O O     . GLN A 1 168 ? -41.47400 22.70700 2.69300   1.000 16.98078 ? 162 GLN A O     1 
ATOM   1175 C CB    . GLN A 1 168 ? -43.38700 22.92000 5.28800   1.000 17.14361 ? 162 GLN A CB    1 
ATOM   1176 C CG    . GLN A 1 168 ? -44.82500 22.66500 5.79300   1.000 20.12228 ? 162 GLN A CG    1 
ATOM   1177 C CD    . GLN A 1 168 ? -45.79500 22.38700 4.65000   1.000 25.56446 ? 162 GLN A CD    1 
ATOM   1178 O OE1   . GLN A 1 168 ? -46.15700 23.29200 3.89900   1.000 28.59149 ? 162 GLN A OE1   1 
ATOM   1179 N NE2   . GLN A 1 168 ? -46.20800 21.12300 4.50400   1.000 25.97995 ? 162 GLN A NE2   1 
ATOM   1180 N N     . VAL A 1 169 ? -40.43100 21.73200 4.43000   1.000 14.11701 ? 163 VAL A N     1 
ATOM   1181 C CA    . VAL A 1 169 ? -39.12400 21.89800 3.79800   1.000 14.39094 ? 163 VAL A CA    1 
ATOM   1182 C C     . VAL A 1 169 ? -39.02300 21.02000 2.55200   1.000 14.39932 ? 163 VAL A C     1 
ATOM   1183 O O     . VAL A 1 169 ? -38.47600 21.43400 1.51800   1.000 13.85322 ? 163 VAL A O     1 
ATOM   1184 C CB    . VAL A 1 169 ? -37.99200 21.58300 4.78700   1.000 13.93087 ? 163 VAL A CB    1 
ATOM   1185 C CG1   . VAL A 1 169 ? -36.65100 21.70900 4.08100   1.000 14.66906 ? 163 VAL A CG1   1 
ATOM   1186 C CG2   . VAL A 1 169 ? -38.03500 22.52300 6.01600   1.000 14.51217 ? 163 VAL A CG2   1 
ATOM   1187 N N     . VAL A 1 170 ? -39.53000 19.78800 2.63400   1.000 14.46016 ? 164 VAL A N     1 
ATOM   1188 C CA    . VAL A 1 170 ? -39.57300 18.93000 1.45200   1.000 15.45664 ? 164 VAL A CA    1 
ATOM   1189 C C     . VAL A 1 170 ? -40.34700 19.61800 0.33300   1.000 16.79784 ? 164 VAL A C     1 
ATOM   1190 O O     . VAL A 1 170 ? -39.93500 19.60600 -0.83300  1.000 16.87098 ? 164 VAL A O     1 
ATOM   1191 C CB    . VAL A 1 170 ? -40.18400 17.55700 1.80000   1.000 15.69889 ? 164 VAL A CB    1 
ATOM   1192 C CG1   . VAL A 1 170 ? -40.38400 16.72500 0.53700   1.000 15.31676 ? 164 VAL A CG1   1 
ATOM   1193 C CG2   . VAL A 1 170 ? -39.30900 16.80300 2.77200   1.000 15.24737 ? 164 VAL A CG2   1 
ATOM   1194 N N     . GLU A 1 171 ? -41.47500 20.24800 0.67200   1.000 16.99613 ? 165 GLU A N     1 
ATOM   1195 C CA    . GLU A 1 171 ? -42.22400 20.98500 -0.33900  1.000 18.73193 ? 165 GLU A CA    1 
ATOM   1196 C C     . GLU A 1 171 ? -41.42300 22.15200 -0.92000  1.000 18.14070 ? 165 GLU A C     1 
ATOM   1197 O O     . GLU A 1 171 ? -41.56500 22.46300 -2.11100  1.000 17.88444 ? 165 GLU A O     1 
ATOM   1198 C CB    . GLU A 1 171 ? -43.54700 21.45200 0.25800   1.000 20.18744 ? 165 GLU A CB    1 
ATOM   1199 C CG    . GLU A 1 171 ? -44.43600 22.21100 -0.70400  1.000 24.75290 ? 165 GLU A CG    1 
ATOM   1200 C CD    . GLU A 1 171 ? -44.86600 21.38900 -1.91800  1.000 30.10818 ? 165 GLU A CD    1 
ATOM   1201 O OE1   . GLU A 1 171 ? -44.85500 20.13700 -1.84100  1.000 31.96579 ? 165 GLU A OE1   1 
ATOM   1202 O OE2   . GLU A 1 171 ? -45.23900 22.01400 -2.94500  1.000 32.62795 ? 165 GLU A OE2   1 
ATOM   1203 N N     . ASP A 1 172 ? -40.55300 22.78400 -0.11800  1.000 16.06022 ? 166 ASP A N     1 
ATOM   1204 C CA    . ASP A 1 172 ? -39.69600 23.84300 -0.66000  1.000 15.05852 ? 166 ASP A CA    1 
ATOM   1205 C C     . ASP A 1 172 ? -38.70800 23.28600 -1.68000  1.000 14.67706 ? 166 ASP A C     1 
ATOM   1206 O O     . ASP A 1 172 ? -38.39200 23.94700 -2.67600  1.000 14.25857 ? 166 ASP A O     1 
ATOM   1207 C CB    . ASP A 1 172 ? -38.92500 24.54800 0.46200   1.000 14.96286 ? 166 ASP A CB    1 
ATOM   1208 C CG    . ASP A 1 172 ? -39.82100 25.40800 1.34800   1.000 20.19251 ? 166 ASP A CG    1 
ATOM   1209 O OD1   . ASP A 1 172 ? -40.84000 25.92200 0.84600   1.000 23.03168 ? 166 ASP A OD1   1 
ATOM   1210 O OD2   . ASP A 1 172 ? -39.49700 25.58000 2.54500   1.000 22.41557 ? 166 ASP A OD2   1 
ATOM   1211 N N     . TYR A 1 173 ? -38.16500 22.09200 -1.42300  1.000 14.32188 ? 167 TYR A N     1 
ATOM   1212 C CA    . TYR A 1 173 ? -37.31600 21.45600 -2.43100  1.000 14.55689 ? 167 TYR A CA    1 
ATOM   1213 C C     . TYR A 1 173 ? -38.10600 21.16700 -3.69900  1.000 14.86684 ? 167 TYR A C     1 
ATOM   1214 O O     . TYR A 1 173 ? -37.61900 21.39200 -4.81000  1.000 15.28420 ? 167 TYR A O     1 
ATOM   1215 C CB    . TYR A 1 173 ? -36.72800 20.15400 -1.89800  1.000 14.92347 ? 167 TYR A CB    1 
ATOM   1216 C CG    . TYR A 1 173 ? -35.52900 20.29000 -1.00400  1.000 14.03807 ? 167 TYR A CG    1 
ATOM   1217 C CD1   . TYR A 1 173 ? -34.26100 20.52300 -1.53700  1.000 14.23044 ? 167 TYR A CD1   1 
ATOM   1218 C CD2   . TYR A 1 173 ? -35.65000 20.12300 0.36700   1.000 12.96246 ? 167 TYR A CD2   1 
ATOM   1219 C CE1   . TYR A 1 173 ? -33.14500 20.62400 -0.71200  1.000 14.55213 ? 167 TYR A CE1   1 
ATOM   1220 C CE2   . TYR A 1 173 ? -34.54500 20.22100 1.21000   1.000 13.09528 ? 167 TYR A CE2   1 
ATOM   1221 C CZ    . TYR A 1 173 ? -33.29500 20.47300 0.66100   1.000 13.76572 ? 167 TYR A CZ    1 
ATOM   1222 O OH    . TYR A 1 173 ? -32.20200 20.55800 1.48900   1.000 14.59585 ? 167 TYR A OH    1 
ATOM   1223 N N     . ARG A 1 174 ? -39.32600 20.64800 -3.54300  1.000 14.26213 ? 168 ARG A N     1 
ATOM   1224 C CA    . ARG A 1 174 ? -40.16800 20.32700 -4.69000  1.000 16.10525 ? 168 ARG A CA    1 
ATOM   1225 C C     . ARG A 1 174 ? -40.47000 21.56600 -5.52400  1.000 15.99073 ? 168 ARG A C     1 
ATOM   1226 O O     . ARG A 1 174 ? -40.34700 21.54000 -6.75600  1.000 16.64245 ? 168 ARG A O     1 
ATOM   1227 C CB    . ARG A 1 174 ? -41.46400 19.67400 -4.20900  1.000 18.67274 ? 168 ARG A CB    1 
ATOM   1228 C CG    . ARG A 1 174 ? -42.11500 18.77000 -5.26000  1.000 22.02903 ? 168 ARG A CG    1 
ATOM   1229 C CD    . ARG A 1 174 ? -43.46000 18.27300 -4.79200  1.000 26.21693 ? 168 ARG A CD    1 
ATOM   1230 N NE    . ARG A 1 174 ? -44.35500 19.40900 -4.68100  1.000 29.30016 ? 168 ARG A NE    1 
ATOM   1231 C CZ    . ARG A 1 174 ? -45.10600 19.85500 -5.67600  1.000 32.76040 ? 168 ARG A CZ    1 
ATOM   1232 N NH1   . ARG A 1 174 ? -45.18000 19.20500 -6.82900  1.000 33.81946 ? 168 ARG A NH1   1 
ATOM   1233 N NH2   . ARG A 1 174 ? -45.78700 20.98800 -5.51700  1.000 33.94109 ? 168 ARG A NH2   1 
ATOM   1234 N N     . ARG A 1 175 ? -40.88000 22.66100 -4.86700  1.000 16.75414 ? 169 ARG A N     1 
ATOM   1235 C CA    . ARG A 1 175 ? -41.20800 23.88500 -5.59500  1.000 15.97247 ? 169 ARG A CA    1 
ATOM   1236 C C     . ARG A 1 175 ? -39.96900 24.47800 -6.24900  1.000 14.77740 ? 169 ARG A C     1 
ATOM   1237 O O     . ARG A 1 175 ? -40.03800 24.98800 -7.37700  1.000 16.61831 ? 169 ARG A O     1 
ATOM   1238 C CB    . ARG A 1 175 ? -41.84700 24.91100 -4.66100  1.000 18.59623 ? 169 ARG A CB    1 
ATOM   1239 N N     . SER A 1 176 ? -38.82500 24.41500 -5.56400  1.000 14.60553 ? 170 SER A N     1 
ATOM   1240 C CA    . SER A 1 176 ? -37.61700 24.96900 -6.16500  1.000 15.31150 ? 170 SER A CA    1 
ATOM   1241 C C     . SER A 1 176 ? -37.18900 24.15400 -7.37800  1.000 15.82887 ? 170 SER A C     1 
ATOM   1242 O O     . SER A 1 176 ? -36.67400 24.71100 -8.35100  1.000 15.84570 ? 170 SER A O     1 
ATOM   1243 C CB    . SER A 1 176 ? -36.49000 25.03900 -5.13400  1.000 17.32198 ? 170 SER A CB    1 
ATOM   1244 O OG    . SER A 1 176 ? -36.77100 26.01600 -4.14200  1.000 18.24526 ? 170 SER A OG    1 
ATOM   1245 N N     . ALA A 1 177 ? -37.36600 22.83000 -7.32400  1.000 15.36003 ? 171 ALA A N     1 
ATOM   1246 C CA    . ALA A 1 177 ? -37.04200 21.99900 -8.47900  1.000 15.08084 ? 171 ALA A CA    1 
ATOM   1247 C C     . ALA A 1 177 ? -37.89400 22.38900 -9.68000  1.000 16.19596 ? 171 ALA A C     1 
ATOM   1248 O O     . ALA A 1 177 ? -37.38700 22.51800 -10.80100 1.000 16.81145 ? 171 ALA A O     1 
ATOM   1249 C CB    . ALA A 1 177 ? -37.23500 20.52000 -8.14100  1.000 15.80472 ? 171 ALA A CB    1 
ATOM   1250 N N     . LEU A 1 178 ? -39.19300 22.59900 -9.45600  1.000 14.68335 ? 172 LEU A N     1 
ATOM   1251 C CA    . LEU A 1 178 ? -40.07400 23.05400 -10.52700 1.000 14.94471 ? 172 LEU A CA    1 
ATOM   1252 C C     . LEU A 1 178 ? -39.65700 24.43100 -11.03500 1.000 16.20471 ? 172 LEU A C     1 
ATOM   1253 O O     . LEU A 1 178 ? -39.69700 24.69500 -12.24400 1.000 17.56863 ? 172 LEU A O     1 
ATOM   1254 C CB    . LEU A 1 178 ? -41.52200 23.06500 -10.02100 1.000 14.99417 ? 172 LEU A CB    1 
ATOM   1255 C CG    . LEU A 1 178 ? -42.14600 21.67200 -9.87300  1.000 16.08710 ? 172 LEU A CG    1 
ATOM   1256 C CD1   . LEU A 1 178 ? -43.40500 21.75400 -9.03200  1.000 17.31961 ? 172 LEU A CD1   1 
ATOM   1257 C CD2   . LEU A 1 178 ? -42.45200 21.07400 -11.23700 1.000 18.58570 ? 172 LEU A CD2   1 
ATOM   1258 N N     . ASN A 1 179 ? -39.23400 25.31800 -10.12800 1.000 15.88173 ? 173 ASN A N     1 
ATOM   1259 C CA    . ASN A 1 179 ? -38.77400 26.63600 -10.55700 1.000 15.90204 ? 173 ASN A CA    1 
ATOM   1260 C C     . ASN A 1 179 ? -37.50300 26.52800 -11.38300 1.000 15.30735 ? 173 ASN A C     1 
ATOM   1261 O O     . ASN A 1 179 ? -37.31700 27.27600 -12.35500 1.000 15.58123 ? 173 ASN A O     1 
ATOM   1262 C CB    . ASN A 1 179 ? -38.54300 27.53400 -9.34400  1.000 14.80836 ? 173 ASN A CB    1 
ATOM   1263 C CG    . ASN A 1 179 ? -39.84100 27.97200 -8.67200  1.000 18.05632 ? 173 ASN A CG    1 
ATOM   1264 O OD1   . ASN A 1 179 ? -40.93600 27.82500 -9.23200  1.000 19.22122 ? 173 ASN A OD1   1 
ATOM   1265 N ND2   . ASN A 1 179 ? -39.72100 28.51600 -7.47400  1.000 19.04067 ? 173 ASN A ND2   1 
ATOM   1266 N N     . ALA A 1 180 ? -36.61000 25.61200 -11.00400 1.000 13.23063 ? 174 ALA A N     1 
ATOM   1267 C CA    . ALA A 1 180 ? -35.38900 25.41700 -11.77600 1.000 14.66411 ? 174 ALA A CA    1 
ATOM   1268 C C     . ALA A 1 180 ? -35.71000 25.00300 -13.20400 1.000 15.42230 ? 174 ALA A C     1 
ATOM   1269 O O     . ALA A 1 180 ? -35.11800 25.52100 -14.15800 1.000 15.64444 ? 174 ALA A O     1 
ATOM   1270 C CB    . ALA A 1 180 ? -34.50200 24.37800 -11.09800 1.000 14.67831 ? 174 ALA A CB    1 
ATOM   1271 N N     . ILE A 1 181 ? -36.66400 24.08400 -13.37000 1.000 15.04331 ? 175 ILE A N     1 
ATOM   1272 C CA    . ILE A 1 181 ? -37.07600 23.67200 -14.70500 1.000 17.04974 ? 175 ILE A CA    1 
ATOM   1273 C C     . ILE A 1 181 ? -37.68500 24.84400 -15.46400 1.000 18.60803 ? 175 ILE A C     1 
ATOM   1274 O O     . ILE A 1 181 ? -37.42200 25.03100 -16.65900 1.000 17.86663 ? 175 ILE A O     1 
ATOM   1275 C CB    . ILE A 1 181 ? -38.04500 22.47900 -14.60700 1.000 18.42940 ? 175 ILE A CB    1 
ATOM   1276 C CG1   . ILE A 1 181 ? -37.30700 21.27600 -14.02200 1.000 18.85675 ? 175 ILE A CG1   1 
ATOM   1277 C CG2   . ILE A 1 181 ? -38.66300 22.18000 -15.96900 1.000 21.11002 ? 175 ILE A CG2   1 
ATOM   1278 C CD1   . ILE A 1 181 ? -36.09100 20.84500 -14.82700 1.000 20.35783 ? 175 ILE A CD1   1 
ATOM   1279 N N     . GLU A 1 182 ? -38.47700 25.67600 -14.77900 1.000 19.51235 ? 176 GLU A N     1 
ATOM   1280 C CA    . GLU A 1 182 ? -39.04600 26.84400 -15.44500 1.000 19.66206 ? 176 GLU A CA    1 
ATOM   1281 C C     . GLU A 1 182 ? -37.96000 27.81700 -15.90900 1.000 18.73289 ? 176 GLU A C     1 
ATOM   1282 O O     . GLU A 1 182 ? -38.09900 28.44500 -16.97100 1.000 18.89638 ? 176 GLU A O     1 
ATOM   1283 C CB    . GLU A 1 182 ? -40.05000 27.53400 -14.51600 1.000 24.41968 ? 176 GLU A CB    1 
ATOM   1284 C CG    . GLU A 1 182 ? -40.45800 28.92700 -14.96200 1.000 30.29755 ? 176 GLU A CG    1 
ATOM   1285 C CD    . GLU A 1 182 ? -41.53200 29.53600 -14.08100 1.000 36.59486 ? 176 GLU A CD    1 
ATOM   1286 O OE1   . GLU A 1 182 ? -41.97900 28.85400 -13.13100 1.000 39.47460 ? 176 GLU A OE1   1 
ATOM   1287 O OE2   . GLU A 1 182 ? -41.92000 30.69800 -14.33000 1.000 39.47714 ? 176 GLU A OE2   1 
ATOM   1288 N N     . ALA A 1 183 ? -36.86200 27.93700 -15.15300 1.000 16.92118 ? 177 ALA A N     1 
ATOM   1289 C CA    . ALA A 1 183 ? -35.75600 28.78500 -15.59100 1.000 18.37473 ? 177 ALA A CA    1 
ATOM   1290 C C     . ALA A 1 183 ? -34.97500 28.16800 -16.74200 1.000 19.00558 ? 177 ALA A C     1 
ATOM   1291 O O     . ALA A 1 183 ? -34.11400 28.84400 -17.32300 1.000 20.60720 ? 177 ALA A O     1 
ATOM   1292 C CB    . ALA A 1 183 ? -34.80800 29.08100 -14.42100 1.000 16.89615 ? 177 ALA A CB    1 
ATOM   1293 N N     . GLY A 1 184 ? -35.22800 26.90500 -17.07100 1.000 16.97898 ? 178 GLY A N     1 
ATOM   1294 C CA    . GLY A 1 184 ? -34.54500 26.26600 -18.17000 1.000 15.92835 ? 178 GLY A CA    1 
ATOM   1295 C C     . GLY A 1 184 ? -33.43200 25.31500 -17.78400 1.000 15.84662 ? 178 GLY A C     1 
ATOM   1296 O O     . GLY A 1 184 ? -32.84000 24.69900 -18.68300 1.000 15.73745 ? 178 GLY A O     1 
ATOM   1297 N N     . PHE A 1 185 ? -33.11500 25.18300 -16.49500 1.000 14.88440 ? 179 PHE A N     1 
ATOM   1298 C CA    . PHE A 1 185 ? -32.10100 24.21800 -16.07800 1.000 13.53557 ? 179 PHE A CA    1 
ATOM   1299 C C     . PHE A 1 185 ? -32.44200 22.83700 -16.61200 1.000 14.58283 ? 179 PHE A C     1 
ATOM   1300 O O     . PHE A 1 185 ? -33.61400 22.46100 -16.73000 1.000 15.86667 ? 179 PHE A O     1 
ATOM   1301 C CB    . PHE A 1 185 ? -31.98300 24.14700 -14.54400 1.000 12.53934 ? 179 PHE A CB    1 
ATOM   1302 C CG    . PHE A 1 185 ? -31.24900 25.31600 -13.93200 1.000 12.95309 ? 179 PHE A CG    1 
ATOM   1303 C CD1   . PHE A 1 185 ? -29.86300 25.35900 -13.92600 1.000 13.62181 ? 179 PHE A CD1   1 
ATOM   1304 C CD2   . PHE A 1 185 ? -31.95600 26.37100 -13.35800 1.000 14.27775 ? 179 PHE A CD2   1 
ATOM   1305 C CE1   . PHE A 1 185 ? -29.18200 26.43600 -13.35700 1.000 14.36442 ? 179 PHE A CE1   1 
ATOM   1306 C CE2   . PHE A 1 185 ? -31.29800 27.44800 -12.79400 1.000 15.29861 ? 179 PHE A CE2   1 
ATOM   1307 C CZ    . PHE A 1 185 ? -29.89400 27.48300 -12.77900 1.000 15.22285 ? 179 PHE A CZ    1 
ATOM   1308 N N     . ASP A 1 186 ? -31.39700 22.06900 -16.92000 1.000 14.63061 ? 180 ASP A N     1 
ATOM   1309 C CA    . ASP A 1 186 ? -31.58900 20.68600 -17.33300 1.000 15.25563 ? 180 ASP A CA    1 
ATOM   1310 C C     . ASP A 1 186 ? -31.97400 19.78200 -16.17200 1.000 13.59618 ? 180 ASP A C     1 
ATOM   1311 O O     . ASP A 1 186 ? -32.53600 18.70100 -16.40200 1.000 15.47484 ? 180 ASP A O     1 
ATOM   1312 C CB    . ASP A 1 186 ? -30.31600 20.19600 -17.99300 1.000 16.33275 ? 180 ASP A CB    1 
ATOM   1313 C CG    . ASP A 1 186 ? -29.96700 21.02300 -19.20800 1.000 17.79188 ? 180 ASP A CG    1 
ATOM   1314 O OD1   . ASP A 1 186 ? -30.69800 20.91400 -20.20900 1.000 20.45633 ? 180 ASP A OD1   1 
ATOM   1315 O OD2   . ASP A 1 186 ? -29.01400 21.82400 -19.14600 1.000 18.65116 ? 180 ASP A OD2   1 
ATOM   1316 N N     . GLY A 1 187 ? -31.68300 20.19800 -14.94700 1.000 12.72457 ? 181 GLY A N     1 
ATOM   1317 C CA    . GLY A 1 187 ? -32.00000 19.39300 -13.78500 1.000 11.86776 ? 181 GLY A CA    1 
ATOM   1318 C C     . GLY A 1 187 ? -31.54500 20.10000 -12.52900 1.000 14.16619 ? 181 GLY A C     1 
ATOM   1319 O O     . GLY A 1 187 ? -31.12800 21.26800 -12.55700 1.000 12.69925 ? 181 GLY A O     1 
ATOM   1320 N N     . ILE A 1 188 ? -31.64100 19.37800 -11.41400 1.000 13.18637 ? 182 ILE A N     1 
ATOM   1321 C CA    . ILE A 1 188 ? -31.22400 19.90500 -10.12500 1.000 12.06961 ? 182 ILE A CA    1 
ATOM   1322 C C     . ILE A 1 188 ? -30.36000 18.86300 -9.42700  1.000 12.57566 ? 182 ILE A C     1 
ATOM   1323 O O     . ILE A 1 188 ? -30.45800 17.66200 -9.69000  1.000 13.40106 ? 182 ILE A O     1 
ATOM   1324 C CB    . ILE A 1 188 ? -32.42400 20.31300 -9.22100  1.000 13.79359 ? 182 ILE A CB    1 
ATOM   1325 C CG1   . ILE A 1 188 ? -33.28600 19.10500 -8.82500  1.000 14.96965 ? 182 ILE A CG1   1 
ATOM   1326 C CG2   . ILE A 1 188 ? -33.29300 21.35600 -9.91100  1.000 13.40270 ? 182 ILE A CG2   1 
ATOM   1327 C CD1   . ILE A 1 188 ? -32.87000 18.42500 -7.50200  1.000 16.53521 ? 182 ILE A CD1   1 
ATOM   1328 N N     . GLU A 1 189 ? -29.52100 19.34800 -8.50900  1.000 13.30656 ? 183 GLU A N     1 
ATOM   1329 C CA    . GLU A 1 189 ? -28.75300 18.50700 -7.60100  1.000 14.04067 ? 183 GLU A CA    1 
ATOM   1330 C C     . GLU A 1 189 ? -29.20500 18.77300 -6.17100  1.000 13.44172 ? 183 GLU A C     1 
ATOM   1331 O O     . GLU A 1 189 ? -29.27700 19.93300 -5.74900  1.000 14.48358 ? 183 GLU A O     1 
ATOM   1332 C CB    . GLU A 1 189 ? -27.25100 18.77400 -7.71900  1.000 15.16089 ? 183 GLU A CB    1 
ATOM   1333 C CG    . GLU A 1 189 ? -26.41600 17.90000 -6.77200  1.000 14.97832 ? 183 GLU A CG    1 
ATOM   1334 C CD    . GLU A 1 189 ? -24.92700 18.09400 -6.93200  1.000 15.30200 ? 183 GLU A CD    1 
ATOM   1335 O OE1   . GLU A 1 189 ? -24.30900 17.37700 -7.75000  1.000 16.47296 ? 183 GLU A OE1   1 
ATOM   1336 O OE2   . GLU A 1 189 ? -24.36300 18.95300 -6.21900  1.000 16.46541 ? 183 GLU A OE2   1 
ATOM   1337 N N     . ILE A 1 190 ? -29.50900 17.71100 -5.42800  1.000 13.00970 ? 184 ILE A N     1 
ATOM   1338 C CA    . ILE A 1 190 ? -29.83000 17.85000 -4.00700  1.000 12.21069 ? 184 ILE A CA    1 
ATOM   1339 C C     . ILE A 1 190 ? -28.52600 17.92800 -3.22100  1.000 12.90174 ? 184 ILE A C     1 
ATOM   1340 O O     . ILE A 1 190 ? -27.72600 16.98800 -3.23800  1.000 12.67740 ? 184 ILE A O     1 
ATOM   1341 C CB    . ILE A 1 190 ? -30.70600 16.68400 -3.51500  1.000 12.85128 ? 184 ILE A CB    1 
ATOM   1342 C CG1   . ILE A 1 190 ? -32.06100 16.69200 -4.23300  1.000 13.93009 ? 184 ILE A CG1   1 
ATOM   1343 C CG2   . ILE A 1 190 ? -30.91300 16.73500 -1.99400  1.000 14.02811 ? 184 ILE A CG2   1 
ATOM   1344 C CD1   . ILE A 1 190 ? -32.91400 17.91300 -3.88300  1.000 15.29328 ? 184 ILE A CD1   1 
ATOM   1345 N N     . HIS A 1 191 ? -28.30300 19.04900 -2.53100  1.000 13.24321 ? 185 HIS A N     1 
ATOM   1346 C CA    . HIS A 1 191 ? -27.11100 19.18800 -1.68400  1.000 12.36616 ? 185 HIS A CA    1 
ATOM   1347 C C     . HIS A 1 191 ? -27.40400 18.46200 -0.37800  1.000 14.11849 ? 185 HIS A C     1 
ATOM   1348 O O     . HIS A 1 191 ? -28.06500 19.00100 0.51600   1.000 14.60428 ? 185 HIS A O     1 
ATOM   1349 C CB    . HIS A 1 191 ? -26.76600 20.65900 -1.45900  1.000 14.05413 ? 185 HIS A CB    1 
ATOM   1350 C CG    . HIS A 1 191 ? -25.44500 20.89400 -0.78400  1.000 15.42791 ? 185 HIS A CG    1 
ATOM   1351 N ND1   . HIS A 1 191 ? -24.78100 19.92100 -0.06700  1.000 15.40919 ? 185 HIS A ND1   1 
ATOM   1352 C CD2   . HIS A 1 191 ? -24.66400 22.00400 -0.72400  1.000 14.86550 ? 185 HIS A CD2   1 
ATOM   1353 C CE1   . HIS A 1 191 ? -23.65000 20.42100 0.40900   1.000 15.41875 ? 185 HIS A CE1   1 
ATOM   1354 N NE2   . HIS A 1 191 ? -23.55500 21.68400 0.02600   1.000 15.33579 ? 185 HIS A NE2   1 
ATOM   1355 N N     . GLY A 1 192 ? -26.92200 17.22400 -0.27100  1.000 13.83665 ? 186 GLY A N     1 
ATOM   1356 C CA    . GLY A 1 192 ? -27.08700 16.48600 0.96400   1.000 14.14589 ? 186 GLY A CA    1 
ATOM   1357 C C     . GLY A 1 192 ? -25.77800 16.23700 1.67900   1.000 14.22166 ? 186 GLY A C     1 
ATOM   1358 O O     . GLY A 1 192 ? -25.63500 15.23100 2.38800   1.000 16.03005 ? 186 GLY A O     1 
ATOM   1359 N N     . ALA A 1 193 ? -24.82200 17.15200 1.51400   1.000 13.67028 ? 187 ALA A N     1 
ATOM   1360 C CA    . ALA A 1 193 ? -23.46500 16.95300 1.99700   1.000 13.60359 ? 187 ALA A CA    1 
ATOM   1361 C C     . ALA A 1 193 ? -23.07000 18.01800 3.02500   1.000 13.69064 ? 187 ALA A C     1 
ATOM   1362 O O     . ALA A 1 193 ? -23.83400 18.94100 3.34800   1.000 14.84361 ? 187 ALA A O     1 
ATOM   1363 C CB    . ALA A 1 193 ? -22.48200 16.94900 0.81800   1.000 12.93824 ? 187 ALA A CB    1 
ATOM   1364 N N     . HIS A 1 194 ? -21.86700 17.82200 3.58000   1.000 14.61998 ? 188 HIS A N     1 
ATOM   1365 C CA    . HIS A 1 194 ? -21.04700 18.86800 4.21200   1.000 16.21223 ? 188 HIS A CA    1 
ATOM   1366 C C     . HIS A 1 194 ? -21.69100 19.46700 5.46200   1.000 15.86064 ? 188 HIS A C     1 
ATOM   1367 O O     . HIS A 1 194 ? -21.45000 20.62900 5.79100   1.000 16.00280 ? 188 HIS A O     1 
ATOM   1368 C CB    . HIS A 1 194 ? -20.69200 19.98200 3.21900   1.000 16.33962 ? 188 HIS A CB    1 
ATOM   1369 C CG    . HIS A 1 194 ? -20.02100 19.49300 1.97300   1.000 17.23752 ? 188 HIS A CG    1 
ATOM   1370 N ND1   . HIS A 1 194 ? -20.11100 20.15900 0.77300   1.000 18.61167 ? 188 HIS A ND1   1 
ATOM   1371 C CD2   . HIS A 1 194 ? -19.27200 18.39100 1.73600   1.000 18.69486 ? 188 HIS A CD2   1 
ATOM   1372 C CE1   . HIS A 1 194 ? -19.42900 19.50100 -0.14800  1.000 19.97727 ? 188 HIS A CE1   1 
ATOM   1373 N NE2   . HIS A 1 194 ? -18.90800 18.42500 0.41300   1.000 19.66315 ? 188 HIS A NE2   1 
ATOM   1374 N N     . GLY A 1 195 ? -22.48300 18.68400 6.19500   1.000 15.64108 ? 189 GLY A N     1 
ATOM   1375 C CA    . GLY A 1 195 ? -23.00000 19.15900 7.46600   1.000 14.18247 ? 189 GLY A CA    1 
ATOM   1376 C C     . GLY A 1 195 ? -24.14100 20.14900 7.37500   1.000 13.66142 ? 189 GLY A C     1 
ATOM   1377 O O     . GLY A 1 195 ? -24.47400 20.77000 8.39000   1.000 14.38444 ? 189 GLY A O     1 
ATOM   1378 N N     . TYR A 1 196 ? -24.75600 20.31100 6.20000   1.000 12.84051 ? 190 TYR A N     1 
ATOM   1379 C CA    . TYR A 1 196 ? -25.89100 21.21300 6.03300   1.000 12.14496 ? 190 TYR A CA    1 
ATOM   1380 C C     . TYR A 1 196 ? -27.17600 20.44800 6.38900   1.000 12.40113 ? 190 TYR A C     1 
ATOM   1381 O O     . TYR A 1 196 ? -27.10500 19.40400 7.03600   1.000 12.66353 ? 190 TYR A O     1 
ATOM   1382 C CB    . TYR A 1 196 ? -25.83200 21.82700 4.62900   1.000 12.44761 ? 190 TYR A CB    1 
ATOM   1383 C CG    . TYR A 1 196 ? -24.62200 22.73000 4.49200   1.000 13.48197 ? 190 TYR A CG    1 
ATOM   1384 C CD1   . TYR A 1 196 ? -24.47400 23.85900 5.30400   1.000 14.97744 ? 190 TYR A CD1   1 
ATOM   1385 C CD2   . TYR A 1 196 ? -23.61400 22.43300 3.59700   1.000 13.72261 ? 190 TYR A CD2   1 
ATOM   1386 C CE1   . TYR A 1 196 ? -23.36000 24.68300 5.19600   1.000 15.41672 ? 190 TYR A CE1   1 
ATOM   1387 C CE2   . TYR A 1 196 ? -22.50200 23.24700 3.48000   1.000 16.74257 ? 190 TYR A CE2   1 
ATOM   1388 C CZ    . TYR A 1 196 ? -22.38100 24.36500 4.27000   1.000 17.75479 ? 190 TYR A CZ    1 
ATOM   1389 O OH    . TYR A 1 196 ? -21.25700 25.15300 4.12200   1.000 20.49654 ? 190 TYR A OH    1 
ATOM   1390 N N     . LEU A 1 197 ? -28.36100 20.94700 6.01000   1.000 12.45276 ? 191 LEU A N     1 
ATOM   1391 C CA    . LEU A 1 197 ? -29.59900 20.46500 6.64100   1.000 13.92769 ? 191 LEU A CA    1 
ATOM   1392 C C     . LEU A 1 197 ? -29.77500 18.95600 6.49200   1.000 13.96630 ? 191 LEU A C     1 
ATOM   1393 O O     . LEU A 1 197 ? -30.06200 18.25300 7.47000   1.000 13.11731 ? 191 LEU A O     1 
ATOM   1394 C CB    . LEU A 1 197 ? -30.82100 21.18200 6.06300   1.000 13.38880 ? 191 LEU A CB    1 
ATOM   1395 C CG    . LEU A 1 197 ? -32.15600 20.76700 6.69600   1.000 14.58626 ? 191 LEU A CG    1 
ATOM   1396 C CD1   . LEU A 1 197 ? -32.22400 21.07600 8.21700   1.000 14.21223 ? 191 LEU A CD1   1 
ATOM   1397 C CD2   . LEU A 1 197 ? -33.33100 21.39800 5.96000   1.000 16.41938 ? 191 LEU A CD2   1 
ATOM   1398 N N     . ILE A 1 198 ? -29.64700 18.44200 5.27100   1.000 13.10987 ? 192 ILE A N     1 
ATOM   1399 C CA    . ILE A 1 198 ? -29.87800 17.01900 5.06200   1.000 12.43922 ? 192 ILE A CA    1 
ATOM   1400 C C     . ILE A 1 198 ? -28.86000 16.20300 5.84100   1.000 13.60040 ? 192 ILE A C     1 
ATOM   1401 O O     . ILE A 1 198 ? -29.19700 15.18700 6.45400   1.000 13.75592 ? 192 ILE A O     1 
ATOM   1402 C CB    . ILE A 1 198 ? -29.85700 16.69300 3.55900   1.000 12.60342 ? 192 ILE A CB    1 
ATOM   1403 C CG1   . ILE A 1 198 ? -31.11100 17.28900 2.90600   1.000 13.15304 ? 192 ILE A CG1   1 
ATOM   1404 C CG2   . ILE A 1 198 ? -29.75600 15.18100 3.32600   1.000 15.76914 ? 192 ILE A CG2   1 
ATOM   1405 C CD1   . ILE A 1 198 ? -31.06900 17.32300 1.41200   1.000 14.74311 ? 192 ILE A CD1   1 
ATOM   1406 N N     . ASP A 1 199 ? -27.60900 16.66300 5.87400   1.000 14.65986 ? 193 ASP A N     1 
ATOM   1407 C CA    . ASP A 1 199 ? -26.57800 15.90600 6.56500   1.000 15.58630 ? 193 ASP A CA    1 
ATOM   1408 C C     . ASP A 1 199 ? -26.78500 15.97200 8.08500   1.000 14.88041 ? 193 ASP A C     1 
ATOM   1409 O O     . ASP A 1 199 ? -26.34800 15.06800 8.81400   1.000 15.53731 ? 193 ASP A O     1 
ATOM   1410 C CB    . ASP A 1 199 ? -25.20900 16.48100 6.17000   1.000 16.55109 ? 193 ASP A CB    1 
ATOM   1411 C CG    . ASP A 1 199 ? -24.07100 15.50700 6.37100   1.000 19.50123 ? 193 ASP A CG    1 
ATOM   1412 O OD1   . ASP A 1 199 ? -24.31800 14.30300 6.13700   1.000 21.02967 ? 193 ASP A OD1   1 
ATOM   1413 O OD2   . ASP A 1 199 ? -22.90300 15.95000 6.54000   1.000 19.75243 ? 193 ASP A OD2   1 
ATOM   1414 N N     . GLN A 1 200 ? -27.46200 17.02200 8.57800   1.000 13.70157 ? 194 GLN A N     1 
ATOM   1415 C CA    . GLN A 1 200 ? -27.82200 17.11400 9.98900   1.000 13.00001 ? 194 GLN A CA    1 
ATOM   1416 C C     . GLN A 1 200 ? -28.86000 16.07300 10.38400  1.000 13.07730 ? 194 GLN A C     1 
ATOM   1417 O O     . GLN A 1 200 ? -28.96900 15.74400 11.57000  1.000 14.07271 ? 194 GLN A O     1 
ATOM   1418 C CB    . GLN A 1 200 ? -28.34000 18.52400 10.31800  1.000 12.50391 ? 194 GLN A CB    1 
ATOM   1419 C CG    . GLN A 1 200 ? -27.23900 19.58700 10.20000  1.000 13.10847 ? 194 GLN A CG    1 
ATOM   1420 C CD    . GLN A 1 200 ? -27.76300 20.97700 9.89100   1.000 13.22887 ? 194 GLN A CD    1 
ATOM   1421 O OE1   . GLN A 1 200 ? -28.84700 21.35900 10.32800  1.000 13.46218 ? 194 GLN A OE1   1 
ATOM   1422 N NE2   . GLN A 1 200 ? -26.97400 21.75600 9.14400   1.000 14.11304 ? 194 GLN A NE2   1 
ATOM   1423 N N     . PHE A 1 201 ? -29.62100 15.55000 9.42200   1.000 13.02495 ? 195 PHE A N     1 
ATOM   1424 C CA    . PHE A 1 201 ? -30.48100 14.40500 9.68200   1.000 12.87738 ? 195 PHE A CA    1 
ATOM   1425 C C     . PHE A 1 201 ? -29.73400 13.08600 9.51200   1.000 13.52270 ? 195 PHE A C     1 
ATOM   1426 O O     . PHE A 1 201 ? -29.95800 12.14200 10.27900  1.000 15.38356 ? 195 PHE A O     1 
ATOM   1427 C CB    . PHE A 1 201 ? -31.70600 14.44800 8.75700   1.000 13.84236 ? 195 PHE A CB    1 
ATOM   1428 C CG    . PHE A 1 201 ? -32.79900 15.35900 9.24000   1.000 15.13567 ? 195 PHE A CG    1 
ATOM   1429 C CD1   . PHE A 1 201 ? -32.81000 16.70500 8.89700   1.000 16.11937 ? 195 PHE A CD1   1 
ATOM   1430 C CD2   . PHE A 1 201 ? -33.80600 14.86900 10.04900  1.000 14.40409 ? 195 PHE A CD2   1 
ATOM   1431 C CE1   . PHE A 1 201 ? -33.81300 17.55200 9.35700   1.000 15.29229 ? 195 PHE A CE1   1 
ATOM   1432 C CE2   . PHE A 1 201 ? -34.81300 15.70000 10.49500  1.000 13.94410 ? 195 PHE A CE2   1 
ATOM   1433 C CZ    . PHE A 1 201 ? -34.82100 17.03900 10.15000  1.000 15.27464 ? 195 PHE A CZ    1 
ATOM   1434 N N     . LEU A 1 202 ? -28.82000 13.01900 8.53200   1.000 13.72343 ? 196 LEU A N     1 
ATOM   1435 C CA    . LEU A 1 202 ? -28.13900 11.76800 8.21800   1.000 14.17873 ? 196 LEU A CA    1 
ATOM   1436 C C     . LEU A 1 202 ? -27.18700 11.33800 9.32500   1.000 15.45384 ? 196 LEU A C     1 
ATOM   1437 O O     . LEU A 1 202 ? -27.11400 10.14800 9.65900   1.000 16.17629 ? 196 LEU A O     1 
ATOM   1438 C CB    . LEU A 1 202 ? -27.35100 11.91200 6.91500   1.000 14.71440 ? 196 LEU A CB    1 
ATOM   1439 C CG    . LEU A 1 202 ? -28.13800 11.90200 5.61800   1.000 13.52814 ? 196 LEU A CG    1 
ATOM   1440 C CD1   . LEU A 1 202 ? -27.21100 12.21900 4.44400   1.000 15.75064 ? 196 LEU A CD1   1 
ATOM   1441 C CD2   . LEU A 1 202 ? -28.83800 10.54600 5.41600   1.000 14.93494 ? 196 LEU A CD2   1 
ATOM   1442 N N     . LYS A 1 203 ? -26.40000 12.27600 9.85300   1.000 16.10546 ? 197 LYS A N     1 
ATOM   1443 C CA    . LYS A 1 203 ? -25.21800 11.94100 10.63600  1.000 15.33941 ? 197 LYS A CA    1 
ATOM   1444 C C     . LYS A 1 203 ? -25.61000 11.69800 12.08600  1.000 15.57004 ? 197 LYS A C     1 
ATOM   1445 O O     . LYS A 1 203 ? -26.26000 12.54600 12.70800  1.000 15.94796 ? 197 LYS A O     1 
ATOM   1446 C CB    . LYS A 1 203 ? -24.17700 13.06500 10.55800  1.000 13.98293 ? 197 LYS A CB    1 
ATOM   1447 C CG    . LYS A 1 203 ? -23.59500 13.31000 9.14200   1.000 16.43600 ? 197 LYS A CG    1 
ATOM   1448 C CD    . LYS A 1 203 ? -22.63100 12.20800 8.75200   1.000 18.61909 ? 197 LYS A CD    1 
ATOM   1449 C CE    . LYS A 1 203 ? -22.10000 12.39500 7.32300   1.000 20.04131 ? 197 LYS A CE    1 
ATOM   1450 N NZ    . LYS A 1 203 ? -21.23800 13.60800 7.17400   1.000 19.95808 ? 197 LYS A NZ    1 
ATOM   1451 N N     . ASP A 1 204 ? -25.19400 10.55500 12.63600  1.000 15.00268 ? 198 ASP A N     1 
ATOM   1452 C CA    . ASP A 1 204 ? -25.58100 10.28700 14.01700  1.000 18.17924 ? 198 ASP A CA    1 
ATOM   1453 C C     . ASP A 1 204 ? -24.78700 11.11300 15.02000  1.000 18.59173 ? 198 ASP A C     1 
ATOM   1454 O O     . ASP A 1 204 ? -25.16000 11.14700 16.19600  1.000 20.76114 ? 198 ASP A O     1 
ATOM   1455 C CB    . ASP A 1 204 ? -25.52400 8.77800  14.35300  1.000 20.53395 ? 198 ASP A CB    1 
ATOM   1456 C CG    . ASP A 1 204 ? -24.11800 8.18500  14.36100  1.000 24.09200 ? 198 ASP A CG    1 
ATOM   1457 O OD1   . ASP A 1 204 ? -23.10700 8.90700  14.26500  1.000 24.13139 ? 198 ASP A OD1   1 
ATOM   1458 O OD2   . ASP A 1 204 ? -24.03700 6.94000  14.48900  1.000 27.28271 ? 198 ASP A OD2   1 
ATOM   1459 N N     . GLY A 1 205 ? -23.75300 11.82900 14.57200  1.000 18.05299 ? 199 GLY A N     1 
ATOM   1460 C CA    . GLY A 1 205 ? -23.10400 12.83500 15.38600  1.000 20.88468 ? 199 GLY A CA    1 
ATOM   1461 C C     . GLY A 1 205 ? -23.87800 14.12400 15.53900  1.000 20.95524 ? 199 GLY A C     1 
ATOM   1462 O O     . GLY A 1 205 ? -23.51200 14.95000 16.38500  1.000 24.62722 ? 199 GLY A O     1 
ATOM   1463 N N     . ILE A 1 206 ? -24.94400 14.32000 14.75300  1.000 18.21182 ? 200 ILE A N     1 
ATOM   1464 C CA    . ILE A 1 206 ? -25.79600 15.50100 14.85000  1.000 19.55695 ? 200 ILE A CA    1 
ATOM   1465 C C     . ILE A 1 206 ? -27.21500 15.12900 15.25100  1.000 19.57359 ? 200 ILE A C     1 
ATOM   1466 O O     . ILE A 1 206 ? -27.80400 15.73900 16.15400  1.000 20.98196 ? 200 ILE A O     1 
ATOM   1467 C CB    . ILE A 1 206 ? -25.80200 16.30200 13.52900  1.000 20.08523 ? 200 ILE A CB    1 
ATOM   1468 C CG1   . ILE A 1 206 ? -24.38700 16.73000 13.14100  1.000 20.87123 ? 200 ILE A CG1   1 
ATOM   1469 C CG2   . ILE A 1 206 ? -26.70000 17.52900 13.64300  1.000 19.00020 ? 200 ILE A CG2   1 
ATOM   1470 C CD1   . ILE A 1 206 ? -24.32200 17.34700 11.73600  1.000 20.28932 ? 200 ILE A CD1   1 
ATOM   1471 N N     . ASN A 1 207 ? -27.79400 14.15000 14.57000  1.000 19.11814 ? 201 ASN A N     1 
ATOM   1472 C CA    . ASN A 1 207 ? -29.20500 13.81300 14.73300  1.000 18.67626 ? 201 ASN A CA    1 
ATOM   1473 C C     . ASN A 1 207 ? -29.38800 13.09700 16.06600  1.000 20.86562 ? 201 ASN A C     1 
ATOM   1474 O O     . ASN A 1 207 ? -29.10000 11.90400 16.18800  1.000 23.03088 ? 201 ASN A O     1 
ATOM   1475 C CB    . ASN A 1 207 ? -29.66600 12.96400 13.55100  1.000 17.84802 ? 201 ASN A CB    1 
ATOM   1476 C CG    . ASN A 1 207 ? -31.13800 12.63800 13.60500  1.000 17.03842 ? 201 ASN A CG    1 
ATOM   1477 O OD1   . ASN A 1 207 ? -31.76100 12.69200 14.67200  1.000 17.45879 ? 201 ASN A OD1   1 
ATOM   1478 N ND2   . ASN A 1 207 ? -31.70500 12.27700 12.45800  1.000 16.82091 ? 201 ASN A ND2   1 
ATOM   1479 N N     . ASP A 1 208 ? -29.87400 13.82700 17.07600  1.000 22.23189 ? 202 ASP A N     1 
ATOM   1480 C CA    . ASP A 1 208 ? -30.17800 13.25700 18.38300  1.000 23.80113 ? 202 ASP A CA    1 
ATOM   1481 C C     . ASP A 1 208 ? -31.68400 13.12200 18.61700  1.000 23.40787 ? 202 ASP A C     1 
ATOM   1482 O O     . ASP A 1 208 ? -32.13800 13.12300 19.76700  1.000 22.38325 ? 202 ASP A O     1 
ATOM   1483 C CB    . ASP A 1 208 ? -29.52900 14.07700 19.50600  1.000 23.76098 ? 202 ASP A CB    1 
ATOM   1484 C CG    . ASP A 1 208 ? -29.97100 15.54900 19.53300  1.000 25.47359 ? 202 ASP A CG    1 
ATOM   1485 O OD1   . ASP A 1 208 ? -30.61400 16.02300 18.57100  1.000 25.32753 ? 202 ASP A OD1   1 
ATOM   1486 O OD2   . ASP A 1 208 ? -29.66300 16.23800 20.54400  1.000 25.93057 ? 202 ASP A OD2   1 
ATOM   1487 N N     . ARG A 1 209 ? -32.46300 12.98700 17.53800  1.000 22.44881 ? 203 ARG A N     1 
ATOM   1488 C CA    . ARG A 1 209 ? -33.91800 12.92800 17.65700  1.000 22.32078 ? 203 ARG A CA    1 
ATOM   1489 C C     . ARG A 1 209 ? -34.37300 11.58000 18.19100  1.000 23.92142 ? 203 ARG A C     1 
ATOM   1490 O O     . ARG A 1 209 ? -33.70300 10.55800 18.02200  1.000 24.87866 ? 203 ARG A O     1 
ATOM   1491 C CB    . ARG A 1 209 ? -34.59700 13.16600 16.31100  1.000 20.73171 ? 203 ARG A CB    1 
ATOM   1492 C CG    . ARG A 1 209 ? -34.29000 14.50400 15.63700  1.000 19.08172 ? 203 ARG A CG    1 
ATOM   1493 C CD    . ARG A 1 209 ? -34.89200 14.54000 14.23600  1.000 16.90075 ? 203 ARG A CD    1 
ATOM   1494 N NE    . ARG A 1 209 ? -36.34300 14.70000 14.24400  1.000 16.74801 ? 203 ARG A NE    1 
ATOM   1495 C CZ    . ARG A 1 209 ? -36.95500 15.87200 14.14500  1.000 17.21750 ? 203 ARG A CZ    1 
ATOM   1496 N NH1   . ARG A 1 209 ? -36.27100 17.00500 14.08600  1.000 16.81016 ? 203 ARG A NH1   1 
ATOM   1497 N NH2   . ARG A 1 209 ? -38.28500 15.90700 14.07700  1.000 18.07706 ? 203 ARG A NH2   1 
ATOM   1498 N N     . THR A 1 210 ? -35.54500 11.58300 18.82500  1.000 25.47749 ? 204 THR A N     1 
ATOM   1499 C CA    . THR A 1 210 ? -36.15400 10.36000 19.33000  1.000 28.02759 ? 204 THR A CA    1 
ATOM   1500 C C     . THR A 1 210 ? -37.50900 10.08600 18.69000  1.000 28.12061 ? 204 THR A C     1 
ATOM   1501 O O     . THR A 1 210 ? -38.24900 9.22700  19.18200  1.000 29.50672 ? 204 THR A O     1 
ATOM   1502 C CB    . THR A 1 210 ? -36.29600 10.41400 20.85600  1.000 29.90378 ? 204 THR A CB    1 
ATOM   1503 O OG1   . THR A 1 210 ? -37.04800 11.57300 21.22700  1.000 30.38046 ? 204 THR A OG1   1 
ATOM   1504 C CG2   . THR A 1 210 ? -34.92500 10.48200 21.52200  1.000 31.00625 ? 204 THR A CG2   1 
ATOM   1505 N N     . ASP A 1 211 ? -37.86000 10.79900 17.62200  1.000 25.89819 ? 205 ASP A N     1 
ATOM   1506 C CA    . ASP A 1 211 ? -39.06600 10.52800 16.86300  1.000 24.63724 ? 205 ASP A CA    1 
ATOM   1507 C C     . ASP A 1 211 ? -38.70500 9.69000  15.63000  1.000 23.88847 ? 205 ASP A C     1 
ATOM   1508 O O     . ASP A 1 211 ? -37.61800 9.10500  15.55700  1.000 24.19703 ? 205 ASP A O     1 
ATOM   1509 C CB    . ASP A 1 211 ? -39.77300 11.85300 16.52300  1.000 24.22781 ? 205 ASP A CB    1 
ATOM   1510 C CG    . ASP A 1 211 ? -39.09400 12.63500 15.39500  1.000 22.85917 ? 205 ASP A CG    1 
ATOM   1511 O OD1   . ASP A 1 211 ? -37.95600 12.30900 14.99800  1.000 21.57201 ? 205 ASP A OD1   1 
ATOM   1512 O OD2   . ASP A 1 211 ? -39.71000 13.60500 14.91000  1.000 22.45270 ? 205 ASP A OD2   1 
ATOM   1513 N N     . GLU A 1 212 ? -39.60400 9.64200  14.64500  1.000 23.95954 ? 206 GLU A N     1 
ATOM   1514 C CA    . GLU A 1 212 ? -39.42900 8.75400  13.50300  1.000 25.51869 ? 206 GLU A CA    1 
ATOM   1515 C C     . GLU A 1 212 ? -38.30300 9.17900  12.57300  1.000 22.52769 ? 206 GLU A C     1 
ATOM   1516 O O     . GLU A 1 212 ? -37.97700 8.42200  11.65500  1.000 20.93440 ? 206 GLU A O     1 
ATOM   1517 C CB    . GLU A 1 212 ? -40.73600 8.64800  12.70700  1.000 30.77147 ? 206 GLU A CB    1 
ATOM   1518 C CG    . GLU A 1 212 ? -41.01200 9.87400  11.85200  1.000 36.92556 ? 206 GLU A CG    1 
ATOM   1519 C CD    . GLU A 1 212 ? -42.48200 10.08300 11.56000  1.000 42.30502 ? 206 GLU A CD    1 
ATOM   1520 O OE1   . GLU A 1 212 ? -43.04700 9.28400  10.78700  1.000 45.59942 ? 206 GLU A OE1   1 
ATOM   1521 O OE2   . GLU A 1 212 ? -43.06200 11.07200 12.05700  1.000 43.33914 ? 206 GLU A OE2   1 
ATOM   1522 N N     . TYR A 1 213 ? -37.70400 10.35400 12.77600  1.000 20.50598 ? 207 TYR A N     1 
ATOM   1523 C CA    . TYR A 1 213 ? -36.59000 10.79900 11.95200  1.000 18.87494 ? 207 TYR A CA    1 
ATOM   1524 C C     . TYR A 1 213 ? -35.24700 10.64200 12.63700  1.000 18.65736 ? 207 TYR A C     1 
ATOM   1525 O O     . TYR A 1 213 ? -34.24000 11.11400 12.10300  1.000 19.27921 ? 207 TYR A O     1 
ATOM   1526 C CB    . TYR A 1 213 ? -36.77700 12.25900 11.53900  1.000 19.20257 ? 207 TYR A CB    1 
ATOM   1527 C CG    . TYR A 1 213 ? -37.84100 12.44700 10.49300  1.000 18.36704 ? 207 TYR A CG    1 
ATOM   1528 C CD1   . TYR A 1 213 ? -39.17100 12.58800 10.85500  1.000 18.30322 ? 207 TYR A CD1   1 
ATOM   1529 C CD2   . TYR A 1 213 ? -37.51700 12.49500 9.14100   1.000 17.57685 ? 207 TYR A CD2   1 
ATOM   1530 C CE1   . TYR A 1 213 ? -40.15200 12.74900 9.90000   1.000 17.93630 ? 207 TYR A CE1   1 
ATOM   1531 C CE2   . TYR A 1 213 ? -38.48800 12.65800 8.17500   1.000 18.35065 ? 207 TYR A CE2   1 
ATOM   1532 C CZ    . TYR A 1 213 ? -39.80800 12.79000 8.56200   1.000 18.77967 ? 207 TYR A CZ    1 
ATOM   1533 O OH    . TYR A 1 213 ? -40.79100 12.95600 7.61600   1.000 21.82640 ? 207 TYR A OH    1 
ATOM   1534 N N     . GLY A 1 214 ? -35.20100 9.99300  13.80400  1.000 18.67577 ? 208 GLY A N     1 
ATOM   1535 C CA    . GLY A 1 214 ? -33.96500 9.84100  14.53300  1.000 20.78116 ? 208 GLY A CA    1 
ATOM   1536 C C     . GLY A 1 214 ? -33.78900 8.42200  15.03900  1.000 22.66014 ? 208 GLY A C     1 
ATOM   1537 O O     . GLY A 1 214 ? -34.72100 7.61300  15.04400  1.000 22.58859 ? 208 GLY A O     1 
ATOM   1538 N N     . GLY A 1 215 ? -32.56300 8.14700  15.47200  1.000 23.91689 ? 209 GLY A N     1 
ATOM   1539 C CA    . GLY A 1 215 ? -32.19400 6.87000  16.03900  1.000 25.88642 ? 209 GLY A CA    1 
ATOM   1540 C C     . GLY A 1 215 ? -31.56700 5.95000  15.01600  1.000 27.89411 ? 209 GLY A C     1 
ATOM   1541 O O     . GLY A 1 215 ? -30.36100 6.02500  14.72900  1.000 30.84239 ? 209 GLY A O     1 
ATOM   1542 N N     . SER A 1 216 ? -32.38700 5.07500  14.45600  1.000 23.14873 ? 210 SER A N     1 
ATOM   1543 C CA    . SER A 1 216 ? -31.87900 4.04800  13.57700  1.000 22.65048 ? 210 SER A CA    1 
ATOM   1544 C C     . SER A 1 216 ? -31.35000 4.67000  12.29300  1.000 21.19344 ? 210 SER A C     1 
ATOM   1545 O O     . SER A 1 216 ? -31.68000 5.80100  11.93400  1.000 19.20296 ? 210 SER A O     1 
ATOM   1546 C CB    . SER A 1 216 ? -32.97200 3.03600  13.25700  1.000 22.43069 ? 210 SER A CB    1 
ATOM   1547 O OG    . SER A 1 216 ? -33.99400 3.64700  12.49100  1.000 20.48770 ? 210 SER A OG    1 
ATOM   1548 N N     . LEU A 1 217 ? -30.51900 3.89700  11.59900  1.000 22.18467 ? 211 LEU A N     1 
ATOM   1549 C CA    . LEU A 1 217 ? -30.03100 4.30700  10.29100  1.000 22.79168 ? 211 LEU A CA    1 
ATOM   1550 C C     . LEU A 1 217 ? -31.19000 4.56200  9.32800   1.000 21.56949 ? 211 LEU A C     1 
ATOM   1551 O O     . LEU A 1 217 ? -31.20200 5.57000  8.60800   1.000 20.41276 ? 211 LEU A O     1 
ATOM   1552 C CB    . LEU A 1 217 ? -29.09000 3.22200  9.77300   1.000 25.39483 ? 211 LEU A CB    1 
ATOM   1553 C CG    . LEU A 1 217 ? -28.11500 3.46400  8.63600   1.000 25.36635 ? 211 LEU A CG    1 
ATOM   1554 C CD1   . LEU A 1 217 ? -27.48300 4.83300  8.74900   1.000 25.31402 ? 211 LEU A CD1   1 
ATOM   1555 C CD2   . LEU A 1 217 ? -27.06900 2.36100  8.68500   1.000 26.26450 ? 211 LEU A CD2   1 
ATOM   1556 N N     . ALA A 1 218 ? -32.20000 3.68600  9.34000   1.000 20.98528 ? 212 ALA A N     1 
ATOM   1557 C CA    . ALA A 1 218 ? -33.36900 3.89300  8.49000   1.000 19.42294 ? 212 ALA A CA    1 
ATOM   1558 C C     . ALA A 1 218 ? -34.05500 5.21000  8.81200   1.000 19.02748 ? 212 ALA A C     1 
ATOM   1559 O O     . ALA A 1 218 ? -34.42400 5.96700  7.90300   1.000 20.19609 ? 212 ALA A O     1 
ATOM   1560 C CB    . ALA A 1 218 ? -34.35600 2.73200  8.64300   1.000 19.95711 ? 212 ALA A CB    1 
ATOM   1561 N N     . ASN A 1 219 ? -34.23000 5.50100  10.10100  1.000 17.58503 ? 213 ASN A N     1 
ATOM   1562 C CA    . ASN A 1 219 ? -34.88400 6.74200  10.50600  1.000 17.04581 ? 213 ASN A CA    1 
ATOM   1563 C C     . ASN A 1 219 ? -34.06900 7.95900  10.07900  1.000 16.31706 ? 213 ASN A C     1 
ATOM   1564 O O     . ASN A 1 219 ? -34.63000 8.96400  9.62300   1.000 16.04962 ? 213 ASN A O     1 
ATOM   1565 C CB    . ASN A 1 219 ? -35.10700 6.73600  12.02200  1.000 17.57314 ? 213 ASN A CB    1 
ATOM   1566 C CG    . ASN A 1 219 ? -36.30200 5.89500  12.43200  1.000 21.44058 ? 213 ASN A CG    1 
ATOM   1567 O OD1   . ASN A 1 219 ? -36.92700 5.23300  11.60000  1.000 23.56988 ? 213 ASN A OD1   1 
ATOM   1568 N ND2   . ASN A 1 219 ? -36.62600 5.91700  13.71900  1.000 22.27202 ? 213 ASN A ND2   1 
ATOM   1569 N N     . ARG A 1 220 ? -32.74000 7.88600  10.20300  1.000 16.22440 ? 214 ARG A N     1 
ATOM   1570 C CA    . ARG A 1 220 ? -31.90200 9.01300  9.80500   1.000 15.99929 ? 214 ARG A CA    1 
ATOM   1571 C C     . ARG A 1 220 ? -31.88400 9.22500  8.29300   1.000 15.66171 ? 214 ARG A C     1 
ATOM   1572 O O     . ARG A 1 220 ? -31.66000 10.35300 7.84300   1.000 16.37063 ? 214 ARG A O     1 
ATOM   1573 C CB    . ARG A 1 220 ? -30.47100 8.82400  10.33100  1.000 16.56806 ? 214 ARG A CB    1 
ATOM   1574 C CG    . ARG A 1 220 ? -30.34700 8.96000  11.84200  1.000 18.82353 ? 214 ARG A CG    1 
ATOM   1575 C CD    . ARG A 1 220 ? -28.88900 8.87700  12.27400  1.000 21.19695 ? 214 ARG A CD    1 
ATOM   1576 N NE    . ARG A 1 220 ? -28.44600 7.49300  12.40900  1.000 24.65919 ? 214 ARG A NE    1 
ATOM   1577 C CZ    . ARG A 1 220 ? -27.33800 7.00200  11.87000  1.000 28.23140 ? 214 ARG A CZ    1 
ATOM   1578 N NH1   . ARG A 1 220 ? -26.57800 7.72700  11.06200  1.000 28.86288 ? 214 ARG A NH1   1 
ATOM   1579 N NH2   . ARG A 1 220 ? -26.97700 5.75400  12.15700  1.000 28.71834 ? 214 ARG A NH2   1 
ATOM   1580 N N     . CYS A 1 221 ? -32.15900 8.19600  7.50000   1.000 15.10890 ? 215 CYS A N     1 
ATOM   1581 C CA    . CYS A 1 221 ? -32.21800 8.36100  6.05500   1.000 14.85261 ? 215 CYS A CA    1 
ATOM   1582 C C     . CYS A 1 221 ? -33.58100 8.80600  5.54400   1.000 13.99077 ? 215 CYS A C     1 
ATOM   1583 O O     . CYS A 1 221 ? -33.72600 9.00400  4.33100   1.000 15.55574 ? 215 CYS A O     1 
ATOM   1584 C CB    . CYS A 1 221 ? -31.84500 7.05500  5.34800   1.000 16.84400 ? 215 CYS A CB    1 
ATOM   1585 S SG    . CYS A 1 221 ? -30.12200 6.58100  5.53100   1.000 20.07091 ? 215 CYS A SG    1 
ATOM   1586 N N     . LYS A 1 222 ? -34.57700 8.94700  6.42200   1.000 15.26529 ? 216 LYS A N     1 
ATOM   1587 C CA    . LYS A 1 222 ? -35.92700 9.26600  5.96700   1.000 15.75326 ? 216 LYS A CA    1 
ATOM   1588 C C     . LYS A 1 222 ? -35.98500 10.63600 5.30100   1.000 16.27279 ? 216 LYS A C     1 
ATOM   1589 O O     . LYS A 1 222 ? -36.62200 10.79400 4.25300   1.000 16.30635 ? 216 LYS A O     1 
ATOM   1590 C CB    . LYS A 1 222 ? -36.91600 9.19900  7.13600   1.000 19.96421 ? 216 LYS A CB    1 
ATOM   1591 C CG    . LYS A 1 222 ? -37.29600 7.79700  7.53900   1.000 24.37165 ? 216 LYS A CG    1 
ATOM   1592 C CD    . LYS A 1 222 ? -38.53400 7.80200  8.43000   1.000 28.77704 ? 216 LYS A CD    1 
ATOM   1593 C CE    . LYS A 1 222 ? -38.85800 6.39600  8.92900   1.000 30.45418 ? 216 LYS A CE    1 
ATOM   1594 N NZ    . LYS A 1 222 ? -39.40500 6.39400  10.30700  1.000 31.25676 ? 216 LYS A NZ    1 
ATOM   1595 N N     . PHE A 1 223 ? -35.31900 11.64000 5.88000   1.000 14.66100 ? 217 PHE A N     1 
ATOM   1596 C CA    . PHE A 1 223 ? -35.42000 12.98600 5.32100   1.000 14.78635 ? 217 PHE A CA    1 
ATOM   1597 C C     . PHE A 1 223 ? -34.86600 13.04800 3.89700   1.000 14.07144 ? 217 PHE A C     1 
ATOM   1598 O O     . PHE A 1 223 ? -35.53700 13.55100 2.98800   1.000 14.91371 ? 217 PHE A O     1 
ATOM   1599 C CB    . PHE A 1 223 ? -34.71200 13.99600 6.22300   1.000 15.64685 ? 217 PHE A CB    1 
ATOM   1600 C CG    . PHE A 1 223 ? -34.87200 15.43000 5.77600   1.000 16.78607 ? 217 PHE A CG    1 
ATOM   1601 C CD1   . PHE A 1 223 ? -36.12700 15.98600 5.59500   1.000 20.15124 ? 217 PHE A CD1   1 
ATOM   1602 C CD2   . PHE A 1 223 ? -33.75400 16.21200 5.50900   1.000 16.94130 ? 217 PHE A CD2   1 
ATOM   1603 C CE1   . PHE A 1 223 ? -36.26600 17.30700 5.17800   1.000 20.09753 ? 217 PHE A CE1   1 
ATOM   1604 C CE2   . PHE A 1 223 ? -33.87900 17.52900 5.10400   1.000 16.65807 ? 217 PHE A CE2   1 
ATOM   1605 C CZ    . PHE A 1 223 ? -35.13100 18.07700 4.93300   1.000 16.75922 ? 217 PHE A CZ    1 
ATOM   1606 N N     . ILE A 1 224 ? -33.64500 12.54800 3.66600   1.000 15.70028 ? 218 ILE A N     1 
ATOM   1607 C CA    . ILE A 1 224 ? -33.11300 12.61400 2.30000   1.000 14.94951 ? 218 ILE A CA    1 
ATOM   1608 C C     . ILE A 1 224 ? -33.97200 11.78800 1.34100   1.000 16.12406 ? 218 ILE A C     1 
ATOM   1609 O O     . ILE A 1 224 ? -34.17500 12.17000 0.17800   1.000 15.07857 ? 218 ILE A O     1 
ATOM   1610 C CB    . ILE A 1 224 ? -31.62800 12.19300 2.24400   1.000 15.10788 ? 218 ILE A CB    1 
ATOM   1611 C CG1   . ILE A 1 224 ? -31.03800 12.63600 0.89400   1.000 12.61117 ? 218 ILE A CG1   1 
ATOM   1612 C CG2   . ILE A 1 224 ? -31.45200 10.68900 2.48000   1.000 15.49300 ? 218 ILE A CG2   1 
ATOM   1613 C CD1   . ILE A 1 224 ? -29.52200 12.41100 0.74800   1.000 14.64394 ? 218 ILE A CD1   1 
ATOM   1614 N N     . THR A 1 225 ? -34.50200 10.65400 1.81200   1.000 14.58719 ? 219 THR A N     1 
ATOM   1615 C CA    . THR A 1 225 ? -35.36600 9.84200  0.96100   1.000 15.84681 ? 219 THR A CA    1 
ATOM   1616 C C     . THR A 1 225 ? -36.59800 10.62900 0.53400   1.000 15.08531 ? 219 THR A C     1 
ATOM   1617 O O     . THR A 1 225 ? -36.96900 10.62700 -0.64200  1.000 14.59032 ? 219 THR A O     1 
ATOM   1618 C CB    . THR A 1 225 ? -35.77400 8.56000  1.68700   1.000 16.59028 ? 219 THR A CB    1 
ATOM   1619 O OG1   . THR A 1 225 ? -34.60100 7.81900  2.04800   1.000 16.90326 ? 219 THR A OG1   1 
ATOM   1620 C CG2   . THR A 1 225 ? -36.65000 7.69700  0.78200   1.000 16.91504 ? 219 THR A CG2   1 
ATOM   1621 N N     . GLN A 1 226 ? -37.23300 11.32900 1.48400   1.000 13.60213 ? 220 GLN A N     1 
ATOM   1622 C CA    . GLN A 1 226 ? -38.43700 12.09100 1.16000   1.000 14.19148 ? 220 GLN A CA    1 
ATOM   1623 C C     . GLN A 1 226 ? -38.12100 13.28100 0.25900   1.000 13.99406 ? 220 GLN A C     1 
ATOM   1624 O O     . GLN A 1 226 ? -38.92000 13.63000 -0.62000  1.000 16.24259 ? 220 GLN A O     1 
ATOM   1625 C CB    . GLN A 1 226 ? -39.12800 12.54300 2.45100   1.000 14.56124 ? 220 GLN A CB    1 
ATOM   1626 C CG    . GLN A 1 226 ? -39.75500 11.36800 3.20900   1.000 17.08249 ? 220 GLN A CG    1 
ATOM   1627 C CD    . GLN A 1 226 ? -40.09200 11.66600 4.65800   1.000 20.21110 ? 220 GLN A CD    1 
ATOM   1628 O OE1   . GLN A 1 226 ? -40.03900 12.80600 5.10300   1.000 20.67488 ? 220 GLN A OE1   1 
ATOM   1629 N NE2   . GLN A 1 226 ? -40.47600 10.62400 5.39800   1.000 23.87956 ? 220 GLN A NE2   1 
ATOM   1630 N N     . VAL A 1 227 ? -36.96100 13.91600 0.44600   1.000 14.91116 ? 221 VAL A N     1 
ATOM   1631 C CA    . VAL A 1 227 ? -36.57700 15.02000 -0.43600  1.000 14.93283 ? 221 VAL A CA    1 
ATOM   1632 C C     . VAL A 1 227 ? -36.39500 14.51200 -1.86500  1.000 14.75032 ? 221 VAL A C     1 
ATOM   1633 O O     . VAL A 1 227 ? -36.94600 15.07100 -2.82100  1.000 14.76137 ? 221 VAL A O     1 
ATOM   1634 C CB    . VAL A 1 227 ? -35.30400 15.71300 0.09000   1.000 14.81625 ? 221 VAL A CB    1 
ATOM   1635 C CG1   . VAL A 1 227 ? -34.66400 16.61200 -1.00100  1.000 15.34418 ? 221 VAL A CG1   1 
ATOM   1636 C CG2   . VAL A 1 227 ? -35.59600 16.49600 1.35900   1.000 14.35196 ? 221 VAL A CG2   1 
ATOM   1637 N N     . VAL A 1 228 ? -35.63400 13.42500 -2.03200  1.000 13.56869 ? 222 VAL A N     1 
ATOM   1638 C CA    . VAL A 1 228 ? -35.40600 12.88300 -3.36700  1.000 13.79674 ? 222 VAL A CA    1 
ATOM   1639 C C     . VAL A 1 228 ? -36.71800 12.40300 -3.99100  1.000 13.42664 ? 222 VAL A C     1 
ATOM   1640 O O     . VAL A 1 228 ? -36.97500 12.64000 -5.18100  1.000 14.69452 ? 222 VAL A O     1 
ATOM   1641 C CB    . VAL A 1 228 ? -34.34600 11.76100 -3.31800  1.000 14.88491 ? 222 VAL A CB    1 
ATOM   1642 C CG1   . VAL A 1 228 ? -34.15400 11.14900 -4.70400  1.000 16.53277 ? 222 VAL A CG1   1 
ATOM   1643 C CG2   . VAL A 1 228 ? -33.00600 12.31500 -2.81600  1.000 16.14774 ? 222 VAL A CG2   1 
ATOM   1644 N N     . GLN A 1 229 ? -37.56100 11.70800 -3.21400  1.000 14.34204 ? 223 GLN A N     1 
ATOM   1645 C CA    . GLN A 1 229 ? -38.83300 11.25900 -3.77100  1.000 14.92140 ? 223 GLN A CA    1 
ATOM   1646 C C     . GLN A 1 229 ? -39.66800 12.44100 -4.24500  1.000 16.03830 ? 223 GLN A C     1 
ATOM   1647 O O     . GLN A 1 229 ? -40.32700 12.36300 -5.28900  1.000 17.14786 ? 223 GLN A O     1 
ATOM   1648 C CB    . GLN A 1 229 ? -39.61700 10.42200 -2.75000  1.000 14.89586 ? 223 GLN A CB    1 
ATOM   1649 C CG    . GLN A 1 229 ? -39.01900 9.03500  -2.47500  1.000 17.31613 ? 223 GLN A CG    1 
ATOM   1650 C CD    . GLN A 1 229 ? -39.65000 8.32100  -1.27600  1.000 19.58361 ? 223 GLN A CD    1 
ATOM   1651 O OE1   . GLN A 1 229 ? -40.01500 8.95100  -0.26800  1.000 20.40492 ? 223 GLN A OE1   1 
ATOM   1652 N NE2   . GLN A 1 229 ? -39.75500 6.98700  -1.37100  1.000 20.22065 ? 223 GLN A NE2   1 
ATOM   1653 N N     . ALA A 1 230 ? -39.63800 13.55800 -3.51000  1.000 15.51483 ? 224 ALA A N     1 
ATOM   1654 C CA    . ALA A 1 230 ? -40.48400 14.68300 -3.89400  1.000 15.00557 ? 224 ALA A CA    1 
ATOM   1655 C C     . ALA A 1 230 ? -40.00700 15.31000 -5.19500  1.000 16.25928 ? 224 ALA A C     1 
ATOM   1656 O O     . ALA A 1 230 ? -40.81600 15.61500 -6.07900  1.000 15.93262 ? 224 ALA A O     1 
ATOM   1657 C CB    . ALA A 1 230 ? -40.52900 15.73300 -2.78900  1.000 15.04023 ? 224 ALA A CB    1 
ATOM   1658 N N     . VAL A 1 231 ? -38.69600 15.54200 -5.32200  1.000 15.52501 ? 225 VAL A N     1 
ATOM   1659 C CA    . VAL A 1 231 ? -38.21800 16.16700 -6.55100  1.000 15.93595 ? 225 VAL A CA    1 
ATOM   1660 C C     . VAL A 1 231 ? -38.29000 15.18400 -7.72200  1.000 15.91952 ? 225 VAL A C     1 
ATOM   1661 O O     . VAL A 1 231 ? -38.52500 15.59400 -8.86300  1.000 17.33066 ? 225 VAL A O     1 
ATOM   1662 C CB    . VAL A 1 231 ? -36.79900 16.75500 -6.37900  1.000 15.75428 ? 225 VAL A CB    1 
ATOM   1663 C CG1   . VAL A 1 231 ? -36.79000 17.88400 -5.32900  1.000 16.55558 ? 225 VAL A CG1   1 
ATOM   1664 C CG2   . VAL A 1 231 ? -35.76100 15.67600 -6.04100  1.000 16.60035 ? 225 VAL A CG2   1 
ATOM   1665 N N     . VAL A 1 232 ? -38.10100 13.88300 -7.46900  1.000 14.70928 ? 226 VAL A N     1 
ATOM   1666 C CA    . VAL A 1 232 ? -38.27100 12.89400 -8.53100  1.000 16.83098 ? 226 VAL A CA    1 
ATOM   1667 C C     . VAL A 1 232 ? -39.70300 12.92100 -9.04300  1.000 18.24004 ? 226 VAL A C     1 
ATOM   1668 O O     . VAL A 1 232 ? -39.95300 12.90500 -10.25600 1.000 18.28511 ? 226 VAL A O     1 
ATOM   1669 C CB    . VAL A 1 232 ? -37.87900 11.48800 -8.02900  1.000 16.00013 ? 226 VAL A CB    1 
ATOM   1670 C CG1   . VAL A 1 232 ? -38.45700 10.39900 -8.94400  1.000 18.67981 ? 226 VAL A CG1   1 
ATOM   1671 C CG2   . VAL A 1 232 ? -36.35300 11.35900 -7.90400  1.000 16.51298 ? 226 VAL A CG2   1 
ATOM   1672 N N     . SER A 1 233 ? -40.66800 12.99200 -8.12500  1.000 18.26183 ? 227 SER A N     1 
ATOM   1673 C CA    . SER A 1 233 ? -42.05700 13.02200 -8.55700  1.000 19.55038 ? 227 SER A CA    1 
ATOM   1674 C C     . SER A 1 233 ? -42.36500 14.29100 -9.34500  1.000 20.03728 ? 227 SER A C     1 
ATOM   1675 O O     . SER A 1 233 ? -43.15300 14.24900 -10.29700 1.000 22.01369 ? 227 SER A O     1 
ATOM   1676 C CB    . SER A 1 233 ? -42.97800 12.88800 -7.34300  1.000 24.08950 ? 227 SER A CB    1 
ATOM   1677 O OG    . SER A 1 233 ? -44.26700 13.38100 -7.64900  1.000 30.31449 ? 227 SER A OG    1 
ATOM   1678 N N     . ALA A 1 234 ? -41.72400 15.41300 -9.00100  1.000 17.76844 ? 228 ALA A N     1 
ATOM   1679 C CA    . ALA A 1 234 ? -42.05300 16.68400 -9.64500  1.000 17.72743 ? 228 ALA A CA    1 
ATOM   1680 C C     . ALA A 1 234 ? -41.43400 16.82000 -11.03100 1.000 17.48641 ? 228 ALA A C     1 
ATOM   1681 O O     . ALA A 1 234 ? -42.10600 17.29000 -11.95700 1.000 19.24765 ? 228 ALA A O     1 
ATOM   1682 C CB    . ALA A 1 234 ? -41.61100 17.86200 -8.77300  1.000 19.78265 ? 228 ALA A CB    1 
ATOM   1683 N N     . ILE A 1 235 ? -40.16300 16.44700 -11.20600 1.000 17.39390 ? 229 ILE A N     1 
ATOM   1684 C CA    . ILE A 1 235 ? -39.46700 16.73400 -12.45900 1.000 15.20901 ? 229 ILE A CA    1 
ATOM   1685 C C     . ILE A 1 235 ? -38.87300 15.49600 -13.11800 1.000 16.46358 ? 229 ILE A C     1 
ATOM   1686 O O     . ILE A 1 235 ? -38.30200 15.60900 -14.21100 1.000 18.31693 ? 229 ILE A O     1 
ATOM   1687 C CB    . ILE A 1 235 ? -38.37900 17.82000 -12.27800 1.000 16.27391 ? 229 ILE A CB    1 
ATOM   1688 C CG1   . ILE A 1 235 ? -37.14100 17.26100 -11.56300 1.000 17.47910 ? 229 ILE A CG1   1 
ATOM   1689 C CG2   . ILE A 1 235 ? -38.95700 19.07900 -11.56800 1.000 17.47089 ? 229 ILE A CG2   1 
ATOM   1690 C CD1   . ILE A 1 235 ? -35.99400 18.26700 -11.47400 1.000 19.32386 ? 229 ILE A CD1   1 
ATOM   1691 N N     . GLY A 1 236 ? -39.00000 14.31700 -12.50500 1.000 15.80634 ? 230 GLY A N     1 
ATOM   1692 C CA    . GLY A 1 236 ? -38.49000 13.08700 -13.09100 1.000 15.78896 ? 230 GLY A CA    1 
ATOM   1693 C C     . GLY A 1 236 ? -37.09700 12.74400 -12.60100 1.000 14.92933 ? 230 GLY A C     1 
ATOM   1694 O O     . GLY A 1 236 ? -36.26300 13.63600 -12.42800 1.000 17.27694 ? 230 GLY A O     1 
ATOM   1695 N N     . ALA A 1 237 ? -36.82700 11.45200 -12.39600 1.000 14.30390 ? 231 ALA A N     1 
ATOM   1696 C CA    . ALA A 1 237 ? -35.55200 11.04300 -11.81200 1.000 15.86947 ? 231 ALA A CA    1 
ATOM   1697 C C     . ALA A 1 237 ? -34.37600 11.41200 -12.70200 1.000 14.34321 ? 231 ALA A C     1 
ATOM   1698 O O     . ALA A 1 237 ? -33.29400 11.72400 -12.18900 1.000 14.35925 ? 231 ALA A O     1 
ATOM   1699 C CB    . ALA A 1 237 ? -35.54800 9.53600  -11.53300 1.000 16.15705 ? 231 ALA A CB    1 
ATOM   1700 N N     . ASP A 1 238 ? -34.56400 11.40400 -14.03000 1.000 15.64477 ? 232 ASP A N     1 
ATOM   1701 C CA    . ASP A 1 238 ? -33.43300 11.65000 -14.91400 1.000 17.31021 ? 232 ASP A CA    1 
ATOM   1702 C C     . ASP A 1 238 ? -32.96900 13.10000 -14.87200 1.000 16.45611 ? 232 ASP A C     1 
ATOM   1703 O O     . ASP A 1 238 ? -31.91300 13.40900 -15.43400 1.000 16.72191 ? 232 ASP A O     1 
ATOM   1704 C CB    . ASP A 1 238 ? -33.75400 11.20100 -16.35100 1.000 22.42149 ? 232 ASP A CB    1 
ATOM   1705 C CG    . ASP A 1 238 ? -34.99100 11.86200 -16.93200 1.000 28.04386 ? 232 ASP A CG    1 
ATOM   1706 O OD1   . ASP A 1 238 ? -35.67400 12.63700 -16.24200 1.000 30.46532 ? 232 ASP A OD1   1 
ATOM   1707 O OD2   . ASP A 1 238 ? -35.29700 11.58000 -18.11000 1.000 32.90814 ? 232 ASP A OD2   1 
ATOM   1708 N N     . ARG A 1 239 ? -33.69600 13.97600 -14.17500 1.000 15.83494 ? 233 ARG A N     1 
ATOM   1709 C CA    A ARG A 1 239 ? -33.29400 15.36500 -14.00000 0.520 13.63435 ? 233 ARG A CA    1 
ATOM   1710 C CA    B ARG A 1 239 ? -33.28700 15.36400 -13.99800 0.480 13.39724 ? 233 ARG A CA    1 
ATOM   1711 C C     . ARG A 1 239 ? -32.83800 15.65800 -12.57300 1.000 13.88857 ? 233 ARG A C     1 
ATOM   1712 O O     . ARG A 1 239 ? -32.72800 16.83100 -12.19200 1.000 13.35643 ? 233 ARG A O     1 
ATOM   1713 C CB    A ARG A 1 239 ? -34.43600 16.29700 -14.39900 0.520 14.81193 ? 233 ARG A CB    1 
ATOM   1714 C CB    B ARG A 1 239 ? -34.41900 16.30300 -14.39800 0.480 13.87632 ? 233 ARG A CB    1 
ATOM   1715 C CG    A ARG A 1 239 ? -34.82300 16.16100 -15.86700 0.520 16.16025 ? 233 ARG A CG    1 
ATOM   1716 C CG    B ARG A 1 239 ? -34.67000 16.27300 -15.88300 0.480 14.32320 ? 233 ARG A CG    1 
ATOM   1717 C CD    A ARG A 1 239 ? -35.66300 17.33400 -16.35600 0.520 18.15772 ? 233 ARG A CD    1 
ATOM   1718 C CD    B ARG A 1 239 ? -35.53800 17.42100 -16.34600 0.480 16.42419 ? 233 ARG A CD    1 
ATOM   1719 N NE    A ARG A 1 239 ? -37.04900 17.26600 -15.90900 0.520 18.36614 ? 233 ARG A NE    1 
ATOM   1720 N NE    B ARG A 1 239 ? -35.97500 17.17600 -17.71200 0.480 15.90520 ? 233 ARG A NE    1 
ATOM   1721 C CZ    A ARG A 1 239 ? -38.04500 17.95400 -16.45800 0.520 18.31179 ? 233 ARG A CZ    1 
ATOM   1722 C CZ    B ARG A 1 239 ? -35.29700 17.52700 -18.79800 0.480 15.59398 ? 233 ARG A CZ    1 
ATOM   1723 N NH1   A ARG A 1 239 ? -37.84500 18.76000 -17.48900 0.520 19.53081 ? 233 ARG A NH1   1 
ATOM   1724 N NH1   B ARG A 1 239 ? -34.17700 18.23900 -18.72000 0.480 12.49783 ? 233 ARG A NH1   1 
ATOM   1725 N NH2   A ARG A 1 239 ? -39.27000 17.83300 -15.95700 0.520 16.40416 ? 233 ARG A NH2   1 
ATOM   1726 N NH2   B ARG A 1 239 ? -35.74700 17.14900 -19.98900 0.480 17.84242 ? 233 ARG A NH2   1 
ATOM   1727 N N     . VAL A 1 240 ? -32.55800 14.61900 -11.78500 1.000 14.91968 ? 234 VAL A N     1 
ATOM   1728 C CA    . VAL A 1 240 ? -32.22500 14.76100 -10.36600 1.000 14.39186 ? 234 VAL A CA    1 
ATOM   1729 C C     . VAL A 1 240 ? -30.87800 14.10300 -10.09900 1.000 14.92267 ? 234 VAL A C     1 
ATOM   1730 O O     . VAL A 1 240 ? -30.70500 12.90300 -10.34800 1.000 15.51876 ? 234 VAL A O     1 
ATOM   1731 C CB    . VAL A 1 240 ? -33.31100 14.15200 -9.46100  1.000 13.31053 ? 234 VAL A CB    1 
ATOM   1732 C CG1   . VAL A 1 240 ? -32.88000 14.21900 -7.98600  1.000 14.71604 ? 234 VAL A CG1   1 
ATOM   1733 C CG2   . VAL A 1 240 ? -34.62600 14.88700 -9.65900  1.000 12.56446 ? 234 VAL A CG2   1 
ATOM   1734 N N     . GLY A 1 241 ? -29.93200 14.88900 -9.58800  1.000 13.18390 ? 235 GLY A N     1 
ATOM   1735 C CA    . GLY A 1 241 ? -28.70000 14.36600 -9.02600  1.000 12.70430 ? 235 GLY A CA    1 
ATOM   1736 C C     . GLY A 1 241 ? -28.69900 14.52700 -7.51300  1.000 12.88585 ? 235 GLY A C     1 
ATOM   1737 O O     . GLY A 1 241 ? -29.42300 15.37900 -6.98100  1.000 13.67346 ? 235 GLY A O     1 
ATOM   1738 N N     . VAL A 1 242 ? -27.91800 13.71000 -6.79800  1.000 12.50869 ? 236 VAL A N     1 
ATOM   1739 C CA    . VAL A 1 242 ? -27.87400 13.72700 -5.33800  1.000 12.83078 ? 236 VAL A CA    1 
ATOM   1740 C C     . VAL A 1 242 ? -26.41800 13.76500 -4.89900  1.000 12.69920 ? 236 VAL A C     1 
ATOM   1741 O O     . VAL A 1 242 ? -25.61700 12.92800 -5.33000  1.000 15.71683 ? 236 VAL A O     1 
ATOM   1742 C CB    . VAL A 1 242 ? -28.57500 12.49700 -4.72900  1.000 12.64860 ? 236 VAL A CB    1 
ATOM   1743 C CG1   . VAL A 1 242 ? -28.56400 12.57000 -3.18800  1.000 13.95461 ? 236 VAL A CG1   1 
ATOM   1744 C CG2   . VAL A 1 242 ? -30.01500 12.37000 -5.25600  1.000 13.83636 ? 236 VAL A CG2   1 
ATOM   1745 N N     . ARG A 1 243 ? -26.08100 14.70900 -4.02400  1.000 12.69547 ? 237 ARG A N     1 
ATOM   1746 C CA    . ARG A 1 243 ? -24.71500 14.86100 -3.53400  1.000 13.39703 ? 237 ARG A CA    1 
ATOM   1747 C C     . ARG A 1 243 ? -24.66800 14.57100 -2.03700  1.000 13.50892 ? 237 ARG A C     1 
ATOM   1748 O O     . ARG A 1 243 ? -25.42600 15.17000 -1.26000  1.000 14.40498 ? 237 ARG A O     1 
ATOM   1749 C CB    . ARG A 1 243 ? -24.17200 16.26600 -3.82800  1.000 13.43148 ? 237 ARG A CB    1 
ATOM   1750 C CG    . ARG A 1 243 ? -22.67200 16.36800 -3.58800  1.000 15.72818 ? 237 ARG A CG    1 
ATOM   1751 C CD    . ARG A 1 243 ? -22.08600 17.74400 -3.86600  1.000 17.14345 ? 237 ARG A CD    1 
ATOM   1752 N NE    . ARG A 1 243 ? -20.79300 17.61500 -4.54100  1.000 19.28203 ? 237 ARG A NE    1 
ATOM   1753 C CZ    . ARG A 1 243 ? -19.81300 18.50900 -4.49700  1.000 19.10370 ? 237 ARG A CZ    1 
ATOM   1754 N NH1   . ARG A 1 243 ? -19.88400 19.57600 -3.72800  1.000 16.64529 ? 237 ARG A NH1   1 
ATOM   1755 N NH2   . ARG A 1 243 ? -18.71800 18.31000 -5.23100  1.000 20.25058 ? 237 ARG A NH2   1 
ATOM   1756 N N     . VAL A 1 244 ? -23.77200 13.66800 -1.62200  1.000 14.25474 ? 238 VAL A N     1 
ATOM   1757 C CA    . VAL A 1 244 ? -23.60000 13.33600 -0.20500  1.000 13.81699 ? 238 VAL A CA    1 
ATOM   1758 C C     . VAL A 1 244 ? -22.11000 13.25900 0.11700   1.000 14.20891 ? 238 VAL A C     1 
ATOM   1759 O O     . VAL A 1 244 ? -21.25500 13.24700 -0.76900  1.000 15.50398 ? 238 VAL A O     1 
ATOM   1760 C CB    . VAL A 1 244 ? -24.30300 12.01300 0.20700   1.000 14.38119 ? 238 VAL A CB    1 
ATOM   1761 C CG1   . VAL A 1 244 ? -25.84500 12.15200 0.11300   1.000 14.30105 ? 238 VAL A CG1   1 
ATOM   1762 C CG2   . VAL A 1 244 ? -23.78100 10.81900 -0.60900  1.000 16.60586 ? 238 VAL A CG2   1 
ATOM   1763 N N     . SER A 1 245 ? -21.79900 13.21800 1.41000   1.000 13.61306 ? 239 SER A N     1 
ATOM   1764 C CA    . SER A 1 245 ? -20.40900 13.18300 1.87100   1.000 13.75015 ? 239 SER A CA    1 
ATOM   1765 C C     . SER A 1 245 ? -20.34900 12.46100 3.21300   1.000 16.08442 ? 239 SER A C     1 
ATOM   1766 O O     . SER A 1 245 ? -20.12900 13.07500 4.26600   1.000 16.89678 ? 239 SER A O     1 
ATOM   1767 C CB    . SER A 1 245 ? -19.83800 14.60100 1.96800   1.000 14.31136 ? 239 SER A CB    1 
ATOM   1768 O OG    . SER A 1 245 ? -20.45000 15.35600 3.01400   1.000 16.32399 ? 239 SER A OG    1 
ATOM   1769 N N     . PRO A 1 246 ? -20.54200 11.13900 3.20900   1.000 16.97931 ? 240 PRO A N     1 
ATOM   1770 C CA    . PRO A 1 246 ? -20.60100 10.40600 4.48800   1.000 17.22350 ? 240 PRO A CA    1 
ATOM   1771 C C     . PRO A 1 246 ? -19.31800 10.46200 5.28900   1.000 18.59735 ? 240 PRO A C     1 
ATOM   1772 O O     . PRO A 1 246 ? -19.37100 10.28200 6.50700   1.000 20.01173 ? 240 PRO A O     1 
ATOM   1773 C CB    . PRO A 1 246 ? -20.91600 8.95600  4.07800   1.000 18.90667 ? 240 PRO A CB    1 
ATOM   1774 C CG    . PRO A 1 246 ? -20.94400 8.90800  2.60400   1.000 19.21455 ? 240 PRO A CG    1 
ATOM   1775 C CD    . PRO A 1 246 ? -20.66500 10.26500 2.02700   1.000 18.01777 ? 240 PRO A CD    1 
ATOM   1776 N N     . ALA A 1 247 ? -18.17200 10.69300 4.65000   1.000 19.49548 ? 241 ALA A N     1 
ATOM   1777 C CA    . ALA A 1 247 ? -16.88000 10.63600 5.31800   1.000 20.99523 ? 241 ALA A CA    1 
ATOM   1778 C C     . ALA A 1 247 ? -16.28500 12.01300 5.58600   1.000 22.37090 ? 241 ALA A C     1 
ATOM   1779 O O     . ALA A 1 247 ? -15.13400 12.10500 6.02200   1.000 24.01647 ? 241 ALA A O     1 
ATOM   1780 C CB    . ALA A 1 247 ? -15.90500 9.80300  4.48400   1.000 22.27699 ? 241 ALA A CB    1 
ATOM   1781 N N     . ILE A 1 248 ? -17.03100 13.08200 5.33900   1.000 22.71299 ? 242 ILE A N     1 
ATOM   1782 C CA    . ILE A 1 248 ? -16.57000 14.44200 5.59500   1.000 22.21935 ? 242 ILE A CA    1 
ATOM   1783 C C     . ILE A 1 248 ? -17.24900 14.93300 6.86700   1.000 21.74041 ? 242 ILE A C     1 
ATOM   1784 O O     . ILE A 1 248 ? -18.47800 14.83700 6.98900   1.000 22.27733 ? 242 ILE A O     1 
ATOM   1785 C CB    . ILE A 1 248 ? -16.88100 15.35700 4.39700   1.000 22.30131 ? 242 ILE A CB    1 
ATOM   1786 C CG1   . ILE A 1 248 ? -15.99200 14.98100 3.20000   1.000 23.85128 ? 242 ILE A CG1   1 
ATOM   1787 C CG2   . ILE A 1 248 ? -16.69400 16.81700 4.76800   1.000 21.97212 ? 242 ILE A CG2   1 
ATOM   1788 C CD1   . ILE A 1 248 ? -16.06700 15.95000 2.01300   1.000 26.13680 ? 242 ILE A CD1   1 
ATOM   1789 N N     . ASP A 1 249 ? -16.45400 15.44400 7.82200   1.000 23.82834 ? 243 ASP A N     1 
ATOM   1790 C CA    . ASP A 1 249 ? -16.92400 15.79300 9.16200   1.000 23.84710 ? 243 ASP A CA    1 
ATOM   1791 C C     . ASP A 1 249 ? -17.14500 17.29900 9.36400   1.000 24.94595 ? 243 ASP A C     1 
ATOM   1792 O O     . ASP A 1 249 ? -17.21600 17.76200 10.51200  1.000 29.02799 ? 243 ASP A O     1 
ATOM   1793 C CB    . ASP A 1 249 ? -15.94300 15.26900 10.21500  1.000 24.85027 ? 243 ASP A CB    1 
ATOM   1794 N N     . HIS A 1 250 ? -17.28900 18.04800 8.27600   1.000 21.29231 ? 244 HIS A N     1 
ATOM   1795 C CA    . HIS A 1 250 ? -17.48300 19.49800 8.27300   1.000 20.48847 ? 244 HIS A CA    1 
ATOM   1796 C C     . HIS A 1 250 ? -18.61600 19.93500 9.20400   1.000 19.14289 ? 244 HIS A C     1 
ATOM   1797 O O     . HIS A 1 250 ? -19.69700 19.35500 9.18300   1.000 20.01332 ? 244 HIS A O     1 
ATOM   1798 C CB    . HIS A 1 250 ? -17.80900 19.90200 6.83200   1.000 21.17631 ? 244 HIS A CB    1 
ATOM   1799 C CG    . HIS A 1 250 ? -17.80000 21.37700 6.57400   1.000 22.61762 ? 244 HIS A CG    1 
ATOM   1800 N ND1   . HIS A 1 250 ? -16.72500 22.18500 6.87700   1.000 25.70602 ? 244 HIS A ND1   1 
ATOM   1801 C CD2   . HIS A 1 250 ? -18.75600 22.19600 6.07500   1.000 21.67334 ? 244 HIS A CD2   1 
ATOM   1802 C CE1   . HIS A 1 250 ? -17.00400 23.43300 6.54200   1.000 24.67685 ? 244 HIS A CE1   1 
ATOM   1803 N NE2   . HIS A 1 250 ? -18.23200 23.46900 6.05900   1.000 24.48478 ? 244 HIS A NE2   1 
ATOM   1804 N N     . LEU A 1 251 ? -18.37400 20.98600 9.99600   1.000 17.43992 ? 245 LEU A N     1 
ATOM   1805 C CA    . LEU A 1 251 ? -19.38500 21.56100 10.89900  1.000 15.34930 ? 245 LEU A CA    1 
ATOM   1806 C C     . LEU A 1 251 ? -19.92700 20.52000 11.88000  1.000 16.81318 ? 245 LEU A C     1 
ATOM   1807 O O     . LEU A 1 251 ? -21.13300 20.45300 12.14800  1.000 17.12443 ? 245 LEU A O     1 
ATOM   1808 C CB    . LEU A 1 251 ? -20.52200 22.21400 10.10500  1.000 15.76321 ? 245 LEU A CB    1 
ATOM   1809 C CG    . LEU A 1 251 ? -20.07500 23.27900 9.09800   1.000 16.36874 ? 245 LEU A CG    1 
ATOM   1810 C CD1   . LEU A 1 251 ? -21.21900 23.71500 8.19300   1.000 17.99214 ? 245 LEU A CD1   1 
ATOM   1811 C CD2   . LEU A 1 251 ? -19.45200 24.50200 9.79900   1.000 17.22265 ? 245 LEU A CD2   1 
ATOM   1812 N N     . ASP A 1 252 ? -19.01900 19.71200 12.42700  1.000 16.69558 ? 246 ASP A N     1 
ATOM   1813 C CA    . ASP A 1 252 ? -19.33500 18.69800 13.44000  1.000 19.15995 ? 246 ASP A CA    1 
ATOM   1814 C C     . ASP A 1 252 ? -20.29200 17.63900 12.90300  1.000 21.05610 ? 246 ASP A C     1 
ATOM   1815 O O     . ASP A 1 252 ? -21.17900 17.17100 13.61500  1.000 24.21094 ? 246 ASP A O     1 
ATOM   1816 C CB    . ASP A 1 252 ? -19.90500 19.33500 14.71100  1.000 21.01732 ? 246 ASP A CB    1 
ATOM   1817 C CG    . ASP A 1 252 ? -18.90100 20.21300 15.42000  1.000 22.90684 ? 246 ASP A CG    1 
ATOM   1818 O OD1   . ASP A 1 252 ? -17.68300 20.04400 15.18200  1.000 23.09692 ? 246 ASP A OD1   1 
ATOM   1819 O OD2   . ASP A 1 252 ? -19.32900 21.05800 16.22700  1.000 24.38384 ? 246 ASP A OD2   1 
ATOM   1820 N N     . ALA A 1 253 ? -20.10500 17.25300 11.64600  1.000 20.69466 ? 247 ALA A N     1 
ATOM   1821 C CA    . ALA A 1 253 ? -21.00900 16.31700 10.99200  1.000 21.35125 ? 247 ALA A CA    1 
ATOM   1822 C C     . ALA A 1 253 ? -20.37800 14.94100 10.86400  1.000 22.13386 ? 247 ALA A C     1 
ATOM   1823 O O     . ALA A 1 253 ? -20.16100 14.45300 9.75000   1.000 24.20957 ? 247 ALA A O     1 
ATOM   1824 C CB    . ALA A 1 253 ? -21.40800 16.82900 9.60700   1.000 22.26461 ? 247 ALA A CB    1 
ATOM   1825 N N     . MET A 1 254 ? -20.09000 14.30200 11.98600  1.000 21.10321 ? 248 MET A N     1 
ATOM   1826 C CA    . MET A 1 254 ? -19.45600 12.99500 11.96200  1.000 22.23450 ? 248 MET A CA    1 
ATOM   1827 C C     . MET A 1 254 ? -20.50200 11.90100 12.11600  1.000 20.97893 ? 248 MET A C     1 
ATOM   1828 O O     . MET A 1 254 ? -21.56200 12.10900 12.71200  1.000 19.88814 ? 248 MET A O     1 
ATOM   1829 C CB    . MET A 1 254 ? -18.40000 12.89200 13.06700  1.000 27.25605 ? 248 MET A CB    1 
ATOM   1830 N N     . ASP A 1 255 ? -20.20700 10.73100 11.56200  1.000 21.54975 ? 249 ASP A N     1 
ATOM   1831 C CA    . ASP A 1 255 ? -21.04200 9.56700  11.80900  1.000 23.16014 ? 249 ASP A CA    1 
ATOM   1832 C C     . ASP A 1 255 ? -20.16700 8.43900  12.32400  1.000 22.87724 ? 249 ASP A C     1 
ATOM   1833 O O     . ASP A 1 255 ? -19.00200 8.30500  11.93700  1.000 23.46225 ? 249 ASP A O     1 
ATOM   1834 C CB    . ASP A 1 255 ? -21.81400 9.12400  10.56000  1.000 24.24146 ? 249 ASP A CB    1 
ATOM   1835 C CG    . ASP A 1 255 ? -22.82000 8.01900  10.86200  1.000 26.80092 ? 249 ASP A CG    1 
ATOM   1836 O OD1   . ASP A 1 255 ? -22.45900 6.81100  10.92700  1.000 28.53304 ? 249 ASP A OD1   1 
ATOM   1837 O OD2   . ASP A 1 255 ? -24.01600 8.38000  10.96300  1.000 25.93947 ? 249 ASP A OD2   1 
ATOM   1838 N N     . SER A 1 256 ? -20.74700 7.63100  13.21000  1.000 22.14233 ? 250 SER A N     1 
ATOM   1839 C CA    . SER A 1 256 ? -20.00900 6.54000  13.82600  1.000 22.38722 ? 250 SER A CA    1 
ATOM   1840 C C     . SER A 1 256 ? -19.63400 5.43900  12.83900  1.000 22.33468 ? 250 SER A C     1 
ATOM   1841 O O     . SER A 1 256 ? -18.72000 4.66100  13.12700  1.000 25.10743 ? 250 SER A O     1 
ATOM   1842 C CB    . SER A 1 256 ? -20.83300 5.94600  14.96500  1.000 23.74062 ? 250 SER A CB    1 
ATOM   1843 O OG    . SER A 1 256 ? -22.04600 5.42100  14.45500  1.000 25.21310 ? 250 SER A OG    1 
ATOM   1844 N N     . ASN A 1 257 ? -20.32200 5.33100  11.70400  1.000 21.59021 ? 251 ASN A N     1 
ATOM   1845 C CA    . ASN A 1 257 ? -20.01200 4.31900  10.69200  1.000 19.95655 ? 251 ASN A CA    1 
ATOM   1846 C C     . ASN A 1 257 ? -20.25300 4.91800  9.31900   1.000 18.52661 ? 251 ASN A C     1 
ATOM   1847 O O     . ASN A 1 257 ? -21.27300 4.64400  8.67700   1.000 18.23659 ? 251 ASN A O     1 
ATOM   1848 C CB    . ASN A 1 257 ? -20.85400 3.06200  10.89800  1.000 21.93597 ? 251 ASN A CB    1 
ATOM   1849 C CG    . ASN A 1 257 ? -20.32200 1.87600  10.13800  1.000 25.43616 ? 251 ASN A CG    1 
ATOM   1850 O OD1   . ASN A 1 257 ? -19.67400 2.02500  9.10100   1.000 25.01053 ? 251 ASN A OD1   1 
ATOM   1851 N ND2   . ASN A 1 257 ? -20.59200 0.67500  10.65400  1.000 28.78737 ? 251 ASN A ND2   1 
ATOM   1852 N N     . PRO A 1 258 ? -19.31900 5.74200  8.83200   1.000 19.00860 ? 252 PRO A N     1 
ATOM   1853 C CA    . PRO A 1 258 ? -19.54100 6.44000  7.55100   1.000 18.89125 ? 252 PRO A CA    1 
ATOM   1854 C C     . PRO A 1 258 ? -19.85500 5.52200  6.38400   1.000 17.17643 ? 252 PRO A C     1 
ATOM   1855 O O     . PRO A 1 258 ? -20.71300 5.85800  5.55300   1.000 17.51951 ? 252 PRO A O     1 
ATOM   1856 C CB    . PRO A 1 258 ? -18.21900 7.19300  7.33900   1.000 20.00670 ? 252 PRO A CB    1 
ATOM   1857 C CG    . PRO A 1 258 ? -17.71200 7.41800  8.73900   1.000 21.54644 ? 252 PRO A CG    1 
ATOM   1858 C CD    . PRO A 1 258 ? -18.07400 6.17700  9.49000   1.000 21.84738 ? 252 PRO A CD    1 
ATOM   1859 N N     . LEU A 1 259 ? -19.17200 4.38000  6.27300   1.000 16.22731 ? 253 LEU A N     1 
ATOM   1860 C CA    . LEU A 1 259 ? -19.43900 3.49600  5.14500   1.000 15.43371 ? 253 LEU A CA    1 
ATOM   1861 C C     . LEU A 1 259 ? -20.85200 2.94000  5.21600   1.000 15.72231 ? 253 LEU A C     1 
ATOM   1862 O O     . LEU A 1 259 ? -21.57000 2.94800  4.21200   1.000 16.51801 ? 253 LEU A O     1 
ATOM   1863 C CB    . LEU A 1 259 ? -18.41200 2.36600  5.09600   1.000 18.55749 ? 253 LEU A CB    1 
ATOM   1864 C CG    . LEU A 1 259 ? -18.62600 1.32700  3.98800   1.000 20.01924 ? 253 LEU A CG    1 
ATOM   1865 C CD1   . LEU A 1 259 ? -18.69900 1.98800  2.59500   1.000 20.76573 ? 253 LEU A CD1   1 
ATOM   1866 C CD2   . LEU A 1 259 ? -17.52700 0.26600  4.02800   1.000 21.44440 ? 253 LEU A CD2   1 
ATOM   1867 N N     . SER A 1 260 ? -21.28500 2.49000  6.40200   1.000 16.82980 ? 254 SER A N     1 
ATOM   1868 C CA    . SER A 1 260 ? -22.64900 1.97300  6.53200   1.000 17.40691 ? 254 SER A CA    1 
ATOM   1869 C C     . SER A 1 260 ? -23.67300 3.05900  6.23900   1.000 17.39436 ? 254 SER A C     1 
ATOM   1870 O O     . SER A 1 260 ? -24.71000 2.79500  5.61500   1.000 18.07628 ? 254 SER A O     1 
ATOM   1871 C CB    . SER A 1 260 ? -22.87500 1.39400  7.93400   1.000 20.97378 ? 254 SER A CB    1 
ATOM   1872 O OG    . SER A 1 260 ? -22.42600 0.04900  7.98400   1.000 24.95540 ? 254 SER A OG    1 
ATOM   1873 N N     . LEU A 1 261 ? -23.41000 4.28800  6.68900   1.000 15.57061 ? 255 LEU A N     1 
ATOM   1874 C CA    . LEU A 1 261 ? -24.32300 5.38300  6.37400   1.000 14.92554 ? 255 LEU A CA    1 
ATOM   1875 C C     . LEU A 1 261 ? -24.40800 5.60000  4.87200   1.000 15.39763 ? 255 LEU A C     1 
ATOM   1876 O O     . LEU A 1 261 ? -25.50300 5.71600  4.31100   1.000 15.83522 ? 255 LEU A O     1 
ATOM   1877 C CB    . LEU A 1 261 ? -23.88400 6.66900  7.07100   1.000 14.89351 ? 255 LEU A CB    1 
ATOM   1878 C CG    . LEU A 1 261 ? -24.69500 7.91600  6.69400   1.000 16.95245 ? 255 LEU A CG    1 
ATOM   1879 C CD1   . LEU A 1 261 ? -26.17100 7.75000  7.08200   1.000 18.72082 ? 255 LEU A CD1   1 
ATOM   1880 C CD2   . LEU A 1 261 ? -24.10000 9.14600  7.36900   1.000 16.77176 ? 255 LEU A CD2   1 
ATOM   1881 N N     . GLY A 1 262 ? -23.25700 5.65200  4.19800   1.000 15.02355 ? 256 GLY A N     1 
ATOM   1882 C CA    . GLY A 1 262 ? -23.26800 5.82700  2.75400   1.000 15.64948 ? 256 GLY A CA    1 
ATOM   1883 C C     . GLY A 1 262 ? -23.97600 4.69900  2.02800   1.000 15.17381 ? 256 GLY A C     1 
ATOM   1884 O O     . GLY A 1 262 ? -24.72600 4.93600  1.07700   1.000 16.08574 ? 256 GLY A O     1 
ATOM   1885 N N     . LEU A 1 263 ? -23.75400 3.45900  2.46300   1.000 14.82147 ? 257 LEU A N     1 
ATOM   1886 C CA    . LEU A 1 263 ? -24.43100 2.33600  1.81600   1.000 15.89150 ? 257 LEU A CA    1 
ATOM   1887 C C     . LEU A 1 263 ? -25.92700 2.36400  2.08200   1.000 15.81018 ? 257 LEU A C     1 
ATOM   1888 O O     . LEU A 1 263 ? -26.71000 1.91000  1.23700   1.000 16.11287 ? 257 LEU A O     1 
ATOM   1889 C CB    . LEU A 1 263 ? -23.84000 0.99800  2.28000   1.000 14.56007 ? 257 LEU A CB    1 
ATOM   1890 C CG    . LEU A 1 263 ? -22.42100 0.71300  1.78600   1.000 14.44600 ? 257 LEU A CG    1 
ATOM   1891 C CD1   . LEU A 1 263 ? -21.82800 -0.51200 2.46300   1.000 15.01502 ? 257 LEU A CD1   1 
ATOM   1892 C CD2   . LEU A 1 263 ? -22.38800 0.58100  0.26100   1.000 16.31379 ? 257 LEU A CD2   1 
ATOM   1893 N N     . ALA A 1 264 ? -26.34200 2.87600  3.24700   1.000 15.41787 ? 258 ALA A N     1 
ATOM   1894 C CA    . ALA A 1 264 ? -27.77300 2.99600  3.52000   1.000 15.85624 ? 258 ALA A CA    1 
ATOM   1895 C C     . ALA A 1 264 ? -28.41900 4.01900  2.59300   1.000 15.29794 ? 258 ALA A C     1 
ATOM   1896 O O     . ALA A 1 264 ? -29.49700 3.77100  2.04200   1.000 15.70535 ? 258 ALA A O     1 
ATOM   1897 C CB    . ALA A 1 264 ? -28.01300 3.36000  4.98900   1.000 15.49684 ? 258 ALA A CB    1 
ATOM   1898 N N     . VAL A 1 265 ? -27.76800 5.16700  2.39300   1.000 13.84119 ? 259 VAL A N     1 
ATOM   1899 C CA    . VAL A 1 265 ? -28.27700 6.14000  1.42800   1.000 14.51461 ? 259 VAL A CA    1 
ATOM   1900 C C     . VAL A 1 265 ? -28.32100 5.53800  0.02500   1.000 14.10266 ? 259 VAL A C     1 
ATOM   1901 O O     . VAL A 1 265 ? -29.30300 5.70900  -0.71100  1.000 14.87757 ? 259 VAL A O     1 
ATOM   1902 C CB    . VAL A 1 265 ? -27.43200 7.42700  1.45900   1.000 15.31932 ? 259 VAL A CB    1 
ATOM   1903 C CG1   . VAL A 1 265 ? -27.84400 8.36000  0.30300   1.000 14.88636 ? 259 VAL A CG1   1 
ATOM   1904 C CG2   . VAL A 1 265 ? -27.55200 8.13600  2.83200   1.000 14.74330 ? 259 VAL A CG2   1 
ATOM   1905 N N     . VAL A 1 266 ? -27.26000 4.83100  -0.37500  1.000 14.38110 ? 260 VAL A N     1 
ATOM   1906 C CA    . VAL A 1 266 ? -27.21600 4.27000  -1.72400  1.000 16.46535 ? 260 VAL A CA    1 
ATOM   1907 C C     . VAL A 1 266 ? -28.35500 3.27100  -1.91800  1.000 16.72955 ? 260 VAL A C     1 
ATOM   1908 O O     . VAL A 1 266 ? -29.02200 3.26000  -2.96100  1.000 15.95307 ? 260 VAL A O     1 
ATOM   1909 C CB    . VAL A 1 266 ? -25.83900 3.62700  -1.99200  1.000 17.92531 ? 260 VAL A CB    1 
ATOM   1910 C CG1   . VAL A 1 266 ? -25.89600 2.73600  -3.23100  1.000 17.90680 ? 260 VAL A CG1   1 
ATOM   1911 C CG2   . VAL A 1 266 ? -24.77000 4.68700  -2.16100  1.000 17.48284 ? 260 VAL A CG2   1 
ATOM   1912 N N     . GLU A 1 267 ? -28.61600 2.43400  -0.90500  1.000 15.72144 ? 261 GLU A N     1 
ATOM   1913 C CA    . GLU A 1 267 ? -29.68400 1.45100  -1.04700  1.000 18.26339 ? 261 GLU A CA    1 
ATOM   1914 C C     . GLU A 1 267 ? -31.02700 2.13900  -1.25800  1.000 18.32303 ? 261 GLU A C     1 
ATOM   1915 O O     . GLU A 1 267 ? -31.84100 1.69800  -2.07400  1.000 18.83621 ? 261 GLU A O     1 
ATOM   1916 C CB    . GLU A 1 267 ? -29.73200 0.53700  0.17200   1.000 24.24511 ? 261 GLU A CB    1 
ATOM   1917 C CG    . GLU A 1 267 ? -30.89100 -0.42500 0.12000   1.000 31.13041 ? 261 GLU A CG    1 
ATOM   1918 C CD    . GLU A 1 267 ? -31.60100 -0.54200 1.44100   1.000 38.57192 ? 261 GLU A CD    1 
ATOM   1919 O OE1   . GLU A 1 267 ? -32.45800 0.32500  1.72700   1.000 42.18872 ? 261 GLU A OE1   1 
ATOM   1920 O OE2   . GLU A 1 267 ? -31.30100 -1.49700 2.18800   1.000 40.44624 ? 261 GLU A OE2   1 
ATOM   1921 N N     . ARG A 1 268 ? -31.25300 3.24700  -0.56400  1.000 17.61764 ? 262 ARG A N     1 
ATOM   1922 C CA    . ARG A 1 268 ? -32.51300 3.96200  -0.72700  1.000 17.03503 ? 262 ARG A CA    1 
ATOM   1923 C C     . ARG A 1 268 ? -32.59500 4.62300  -2.10100  1.000 14.76053 ? 262 ARG A C     1 
ATOM   1924 O O     . ARG A 1 268 ? -33.65700 4.61200  -2.73800  1.000 17.12724 ? 262 ARG A O     1 
ATOM   1925 C CB    . ARG A 1 268 ? -32.65800 4.94200  0.43000   1.000 19.86299 ? 262 ARG A CB    1 
ATOM   1926 C CG    . ARG A 1 268 ? -33.09300 4.10100  1.65900   1.000 23.12771 ? 262 ARG A CG    1 
ATOM   1927 C CD    . ARG A 1 268 ? -33.06300 4.79100  2.97600   1.000 28.77145 ? 262 ARG A CD    1 
ATOM   1928 N NE    . ARG A 1 268 ? -33.42000 3.86800  4.05300   1.000 29.98291 ? 262 ARG A NE    1 
ATOM   1929 C CZ    . ARG A 1 268 ? -32.63900 2.89900  4.53000   1.000 30.51079 ? 262 ARG A CZ    1 
ATOM   1930 N NH1   . ARG A 1 268 ? -31.47300 2.59500  3.96900   1.000 29.01685 ? 262 ARG A NH1   1 
ATOM   1931 N NH2   . ARG A 1 268 ? -33.05200 2.19000  5.58000   1.000 31.80286 ? 262 ARG A NH2   1 
ATOM   1932 N N     . LEU A 1 269 ? -31.48400 5.16900  -2.60000  1.000 14.71311 ? 263 LEU A N     1 
ATOM   1933 C CA    . LEU A 1 269 ? -31.49200 5.69500  -3.96500  1.000 14.43807 ? 263 LEU A CA    1 
ATOM   1934 C C     . LEU A 1 269 ? -31.83000 4.60200  -4.97500  1.000 14.42027 ? 263 LEU A C     1 
ATOM   1935 O O     . LEU A 1 269 ? -32.65600 4.81300  -5.86600  1.000 16.08970 ? 263 LEU A O     1 
ATOM   1936 C CB    . LEU A 1 269 ? -30.15100 6.35300  -4.30300  1.000 15.09149 ? 263 LEU A CB    1 
ATOM   1937 C CG    . LEU A 1 269 ? -29.78500 7.56900  -3.46100  1.000 15.15449 ? 263 LEU A CG    1 
ATOM   1938 C CD1   . LEU A 1 269 ? -28.46300 8.15400  -3.96100  1.000 15.66516 ? 263 LEU A CD1   1 
ATOM   1939 C CD2   . LEU A 1 269 ? -30.89100 8.60700  -3.51200  1.000 15.34764 ? 263 LEU A CD2   1 
ATOM   1940 N N     . ASN A 1 270 ? -31.20300 3.42100  -4.84600  1.000 13.81639 ? 264 ASN A N     1 
ATOM   1941 C CA    . ASN A 1 270 ? -31.50700 2.30700  -5.74200  1.000 14.00171 ? 264 ASN A CA    1 
ATOM   1942 C C     . ASN A 1 270 ? -32.98800 1.95500  -5.69000  1.000 16.13838 ? 264 ASN A C     1 
ATOM   1943 O O     . ASN A 1 270 ? -33.60200 1.65800  -6.72400  1.000 16.12122 ? 264 ASN A O     1 
ATOM   1944 C CB    . ASN A 1 270 ? -30.68100 1.07000  -5.36500  1.000 14.76059 ? 264 ASN A CB    1 
ATOM   1945 C CG    . ASN A 1 270 ? -29.21800 1.19300  -5.73500  1.000 15.97689 ? 264 ASN A CG    1 
ATOM   1946 O OD1   . ASN A 1 270 ? -28.83100 2.06200  -6.51400  1.000 17.25814 ? 264 ASN A OD1   1 
ATOM   1947 N ND2   . ASN A 1 270 ? -28.39000 0.31700  -5.16500  1.000 15.91569 ? 264 ASN A ND2   1 
ATOM   1948 N N     . LYS A 1 271 ? -33.57700 1.97500  -4.48900  1.000 16.71520 ? 265 LYS A N     1 
ATOM   1949 C CA    . LYS A 1 271 ? -34.98100 1.59200  -4.34700  1.000 18.36820 ? 265 LYS A CA    1 
ATOM   1950 C C     . LYS A 1 271 ? -35.90700 2.63800  -4.95100  1.000 17.24863 ? 265 LYS A C     1 
ATOM   1951 O O     . LYS A 1 271 ? -36.93100 2.29300  -5.54800  1.000 17.32831 ? 265 LYS A O     1 
ATOM   1952 C CB    . LYS A 1 271 ? -35.32100 1.36400  -2.87800  1.000 21.33305 ? 265 LYS A CB    1 
ATOM   1953 C CG    . LYS A 1 271 ? -34.80800 0.03600  -2.34700  1.000 25.40835 ? 265 LYS A CG    1 
ATOM   1954 C CD    . LYS A 1 271 ? -34.98800 -0.07300 -0.83600  1.000 29.21890 ? 265 LYS A CD    1 
ATOM   1955 C CE    . LYS A 1 271 ? -34.52200 -1.44200 -0.33000  1.000 32.45002 ? 265 LYS A CE    1 
ATOM   1956 N NZ    . LYS A 1 271 ? -35.02900 -1.73300 1.03700   1.000 35.34848 ? 265 LYS A NZ    1 
ATOM   1957 N N     . ILE A 1 272 ? -35.57800 3.92000  -4.78600  1.000 15.90642 ? 266 ILE A N     1 
ATOM   1958 C CA    . ILE A 1 272 ? -36.36700 4.97500  -5.41000  1.000 15.68468 ? 266 ILE A CA    1 
ATOM   1959 C C     . ILE A 1 272 ? -36.36900 4.80400  -6.92200  1.000 14.51531 ? 266 ILE A C     1 
ATOM   1960 O O     . ILE A 1 272 ? -37.40500 4.95100  -7.57300  1.000 17.01197 ? 266 ILE A O     1 
ATOM   1961 C CB    . ILE A 1 272 ? -35.82900 6.36200  -5.00800  1.000 15.56446 ? 266 ILE A CB    1 
ATOM   1962 C CG1   . ILE A 1 272 ? -36.07100 6.62700  -3.51600  1.000 15.61824 ? 266 ILE A CG1   1 
ATOM   1963 C CG2   . ILE A 1 272 ? -36.48000 7.45800  -5.87900  1.000 16.41752 ? 266 ILE A CG2   1 
ATOM   1964 C CD1   . ILE A 1 272 ? -35.40700 7.91700  -2.99900  1.000 17.91493 ? 266 ILE A CD1   1 
ATOM   1965 N N     . GLN A 1 273 ? -35.20500 4.50300  -7.50000  1.000 15.18820 ? 267 GLN A N     1 
ATOM   1966 C CA    . GLN A 1 273 ? -35.10200 4.28400  -8.94200  1.000 15.23109 ? 267 GLN A CA    1 
ATOM   1967 C C     . GLN A 1 273 ? -35.94800 3.10100  -9.38700  1.000 18.33599 ? 267 GLN A C     1 
ATOM   1968 O O     . GLN A 1 273 ? -36.65600 3.17100  -10.40000 1.000 19.46673 ? 267 GLN A O     1 
ATOM   1969 C CB    . GLN A 1 273 ? -33.63600 4.06300  -9.33600  1.000 13.99312 ? 267 GLN A CB    1 
ATOM   1970 C CG    . GLN A 1 273 ? -32.76200 5.29100  -9.06800  1.000 14.88468 ? 267 GLN A CG    1 
ATOM   1971 C CD    . GLN A 1 273 ? -31.30500 5.11600  -9.47700  1.000 16.20581 ? 267 GLN A CD    1 
ATOM   1972 O OE1   . GLN A 1 273 ? -30.60200 6.10200  -9.70100  1.000 17.01161 ? 267 GLN A OE1   1 
ATOM   1973 N NE2   . GLN A 1 273 ? -30.84200 3.86900  -9.55700  1.000 15.88903 ? 267 GLN A NE2   1 
ATOM   1974 N N     . LEU A 1 274 ? -35.86900 1.98700  -8.66100  1.000 18.19756 ? 268 LEU A N     1 
ATOM   1975 C CA    . LEU A 1 274 ? -36.66300 0.82600  -9.05400  1.000 20.68734 ? 268 LEU A CA    1 
ATOM   1976 C C     . LEU A 1 274 ? -38.15500 1.10900  -8.92400  1.000 21.70039 ? 268 LEU A C     1 
ATOM   1977 O O     . LEU A 1 274 ? -38.94800 0.68800  -9.77100  1.000 22.96676 ? 268 LEU A O     1 
ATOM   1978 C CB    . LEU A 1 274 ? -36.26900 -0.39000 -8.22200  1.000 23.92569 ? 268 LEU A CB    1 
ATOM   1979 C CG    . LEU A 1 274 ? -34.89900 -0.94400 -8.61400  1.000 27.03118 ? 268 LEU A CG    1 
ATOM   1980 C CD1   . LEU A 1 274 ? -34.35100 -1.86800 -7.52700  1.000 29.20026 ? 268 LEU A CD1   1 
ATOM   1981 C CD2   . LEU A 1 274 ? -34.92200 -1.62300 -9.99000  1.000 27.93317 ? 268 LEU A CD2   1 
ATOM   1982 N N     . HIS A 1 275 ? -38.55900 1.83400  -7.87700  1.000 21.17209 ? 269 HIS A N     1 
ATOM   1983 C CA    . HIS A 1 275 ? -39.98600 2.08900  -7.68800  1.000 22.43279 ? 269 HIS A CA    1 
ATOM   1984 C C     . HIS A 1 275 ? -40.51100 3.07400  -8.72300  1.000 23.03352 ? 269 HIS A C     1 
ATOM   1985 O O     . HIS A 1 275 ? -41.63000 2.91800  -9.22300  1.000 24.65833 ? 269 HIS A O     1 
ATOM   1986 C CB    . HIS A 1 275 ? -40.24800 2.60200  -6.27200  1.000 22.47734 ? 269 HIS A CB    1 
ATOM   1987 C CG    . HIS A 1 275 ? -41.70000 2.67600  -5.91000  1.000 25.13569 ? 269 HIS A CG    1 
ATOM   1988 N ND1   . HIS A 1 275 ? -42.49700 1.55700  -5.79800  1.000 25.93664 ? 269 HIS A ND1   1 
ATOM   1989 C CD2   . HIS A 1 275 ? -42.49100 3.73300  -5.61300  1.000 25.51897 ? 269 HIS A CD2   1 
ATOM   1990 C CE1   . HIS A 1 275 ? -43.71800 1.92100  -5.45000  1.000 25.97713 ? 269 HIS A CE1   1 
ATOM   1991 N NE2   . HIS A 1 275 ? -43.74300 3.23600  -5.33400  1.000 26.03823 ? 269 HIS A NE2   1 
ATOM   1992 N N     . SER A 1 276 ? -39.72200 4.09200  -9.05900  1.000 22.81174 ? 270 SER A N     1 
ATOM   1993 C CA    . SER A 1 276 ? -40.16300 5.09000  -10.02100 1.000 22.86766 ? 270 SER A CA    1 
ATOM   1994 C C     . SER A 1 276 ? -39.98700 4.62000  -11.45400 1.000 24.73453 ? 270 SER A C     1 
ATOM   1995 O O     . SER A 1 276 ? -40.58300 5.21000  -12.36100 1.000 27.04889 ? 270 SER A O     1 
ATOM   1996 C CB    . SER A 1 276 ? -39.40400 6.40300  -9.81400  1.000 25.77977 ? 270 SER A CB    1 
ATOM   1997 O OG    . SER A 1 276 ? -38.02800 6.22900  -10.08500 1.000 27.95479 ? 270 SER A OG    1 
ATOM   1998 N N     . GLY A 1 277 ? -39.19500 3.57100  -11.67200 1.000 25.69907 ? 271 GLY A N     1 
ATOM   1999 C CA    . GLY A 1 277 ? -38.95100 3.06700  -13.00700 1.000 25.67137 ? 271 GLY A CA    1 
ATOM   2000 C C     . GLY A 1 277 ? -37.96800 3.87700  -13.82000 1.000 25.63185 ? 271 GLY A C     1 
ATOM   2001 O O     . GLY A 1 277 ? -37.97400 3.78200  -15.04700 1.000 26.18704 ? 271 GLY A O     1 
ATOM   2002 N N     . SER A 1 278 ? -37.11700 4.66900  -13.17200 1.000 25.82863 ? 272 SER A N     1 
ATOM   2003 C CA    . SER A 1 278 ? -36.18000 5.53200  -13.87400 1.000 27.20278 ? 272 SER A CA    1 
ATOM   2004 C C     . SER A 1 278 ? -34.95900 5.76900  -13.00100 1.000 23.99961 ? 272 SER A C     1 
ATOM   2005 O O     . SER A 1 278 ? -35.06200 5.82700  -11.77500 1.000 24.12242 ? 272 SER A O     1 
ATOM   2006 C CB    . SER A 1 278 ? -36.80500 6.88200  -14.23800 1.000 32.55670 ? 272 SER A CB    1 
ATOM   2007 O OG    . SER A 1 278 ? -35.85900 7.68300  -14.93400 1.000 36.79864 ? 272 SER A OG    1 
ATOM   2008 N N     . LYS A 1 279 ? -33.80900 5.94200  -13.64600 1.000 22.01342 ? 273 LYS A N     1 
ATOM   2009 C CA    . LYS A 1 279 ? -32.56700 6.18500  -12.92800 1.000 21.52102 ? 273 LYS A CA    1 
ATOM   2010 C C     . LYS A 1 279 ? -32.39400 7.67800  -12.66700 1.000 19.47534 ? 273 LYS A C     1 
ATOM   2011 O O     . LYS A 1 279 ? -32.78700 8.51300  -13.48900 1.000 18.68591 ? 273 LYS A O     1 
ATOM   2012 C CB    . LYS A 1 279 ? -31.37300 5.64000  -13.72200 1.000 23.47769 ? 273 LYS A CB    1 
ATOM   2013 C CG    . LYS A 1 279 ? -31.14100 4.12100  -13.53900 1.000 27.62724 ? 273 LYS A CG    1 
ATOM   2014 C CD    . LYS A 1 279 ? -29.69700 3.73800  -13.83900 1.000 30.35217 ? 273 LYS A CD    1 
ATOM   2015 C CE    . LYS A 1 279 ? -29.45400 2.23300  -13.81700 1.000 32.95234 ? 273 LYS A CE    1 
ATOM   2016 N NZ    . LYS A 1 279 ? -30.60800 1.45900  -13.29300 1.000 34.30816 ? 273 LYS A NZ    1 
ATOM   2017 N N     . LEU A 1 280 ? -31.82000 8.00600  -11.50600 1.000 17.70827 ? 274 LEU A N     1 
ATOM   2018 C CA    . LEU A 1 280 ? -31.36900 9.36900  -11.24400 1.000 15.58166 ? 274 LEU A CA    1 
ATOM   2019 C C     . LEU A 1 280 ? -30.31900 9.77700  -12.27500 1.000 14.80482 ? 274 LEU A C     1 
ATOM   2020 O O     . LEU A 1 280 ? -29.70000 8.93800  -12.93800 1.000 15.27958 ? 274 LEU A O     1 
ATOM   2021 C CB    . LEU A 1 280 ? -30.77300 9.48900  -9.83900  1.000 16.10132 ? 274 LEU A CB    1 
ATOM   2022 C CG    . LEU A 1 280 ? -31.74200 9.22100  -8.68100  1.000 16.48555 ? 274 LEU A CG    1 
ATOM   2023 C CD1   . LEU A 1 280 ? -30.98900 8.94100  -7.36400  1.000 19.26468 ? 274 LEU A CD1   1 
ATOM   2024 C CD2   . LEU A 1 280 ? -32.71000 10.38900 -8.54600  1.000 17.07980 ? 274 LEU A CD2   1 
ATOM   2025 N N     . ALA A 1 281 ? -30.12400 11.08700 -12.41900 1.000 13.00915 ? 275 ALA A N     1 
ATOM   2026 C CA    . ALA A 1 281 ? -29.03100 11.55600 -13.26500 1.000 14.44540 ? 275 ALA A CA    1 
ATOM   2027 C C     . ALA A 1 281 ? -27.69400 11.01800 -12.76300 1.000 13.62402 ? 275 ALA A C     1 
ATOM   2028 O O     . ALA A 1 281 ? -26.87400 10.52000 -13.55100 1.000 14.63792 ? 275 ALA A O     1 
ATOM   2029 C CB    . ALA A 1 281 ? -29.01900 13.08300 -13.31900 1.000 14.76998 ? 275 ALA A CB    1 
ATOM   2030 N N     . TYR A 1 282 ? -27.46000 11.09800 -11.45400 1.000 13.95116 ? 276 TYR A N     1 
ATOM   2031 C CA    . TYR A 1 282 ? -26.19600 10.62800 -10.88800 1.000 12.36816 ? 276 TYR A CA    1 
ATOM   2032 C C     . TYR A 1 282 ? -26.23700 10.68400 -9.37300  1.000 12.34192 ? 276 TYR A C     1 
ATOM   2033 O O     . TYR A 1 282 ? -27.09400 11.33900 -8.76800  1.000 13.76444 ? 276 TYR A O     1 
ATOM   2034 C CB    . TYR A 1 282 ? -25.02100 11.47000 -11.36600 1.000 12.27354 ? 276 TYR A CB    1 
ATOM   2035 C CG    . TYR A 1 282 ? -25.19100 12.94500 -11.01700 1.000 13.65509 ? 276 TYR A CG    1 
ATOM   2036 C CD1   . TYR A 1 282 ? -24.83700 13.44400 -9.75900  1.000 12.93849 ? 276 TYR A CD1   1 
ATOM   2037 C CD2   . TYR A 1 282 ? -25.72000 13.83500 -11.94400 1.000 13.90304 ? 276 TYR A CD2   1 
ATOM   2038 C CE1   . TYR A 1 282 ? -25.00300 14.79000 -9.44800  1.000 13.40759 ? 276 TYR A CE1   1 
ATOM   2039 C CE2   . TYR A 1 282 ? -25.89500 15.17200 -11.63700 1.000 13.90267 ? 276 TYR A CE2   1 
ATOM   2040 C CZ    . TYR A 1 282 ? -25.52500 15.64600 -10.39200 1.000 14.62313 ? 276 TYR A CZ    1 
ATOM   2041 O OH    . TYR A 1 282 ? -25.68100 16.98300 -10.09000 1.000 14.00856 ? 276 TYR A OH    1 
ATOM   2042 N N     . LEU A 1 283 ? -25.24500 10.02600 -8.78500  1.000 12.80810 ? 277 LEU A N     1 
ATOM   2043 C CA    . LEU A 1 283 ? -24.84400 10.17100 -7.39700  1.000 12.51563 ? 277 LEU A CA    1 
ATOM   2044 C C     . LEU A 1 283 ? -23.48300 10.85500 -7.38400  1.000 13.11206 ? 277 LEU A C     1 
ATOM   2045 O O     . LEU A 1 283 ? -22.58300 10.46000 -8.13500  1.000 14.08590 ? 277 LEU A O     1 
ATOM   2046 C CB    . LEU A 1 283 ? -24.74200 8.80500  -6.72200  1.000 13.29155 ? 277 LEU A CB    1 
ATOM   2047 C CG    . LEU A 1 283 ? -24.09400 8.79000  -5.33500  1.000 12.89442 ? 277 LEU A CG    1 
ATOM   2048 C CD1   . LEU A 1 283 ? -24.96400 9.57300  -4.36000  1.000 13.10451 ? 277 LEU A CD1   1 
ATOM   2049 C CD2   . LEU A 1 283 ? -23.88600 7.35300  -4.87500  1.000 15.58895 ? 277 LEU A CD2   1 
ATOM   2050 N N     . HIS A 1 284 ? -23.33400 11.86700 -6.53500  1.000 13.32246 ? 278 HIS A N     1 
ATOM   2051 C CA    . HIS A 1 284 ? -22.16000 12.73000 -6.49400  1.000 12.15621 ? 278 HIS A CA    1 
ATOM   2052 C C     . HIS A 1 284 ? -21.61900 12.64200 -5.07400  1.000 13.23098 ? 278 HIS A C     1 
ATOM   2053 O O     . HIS A 1 284 ? -22.33000 12.97500 -4.12700  1.000 14.05950 ? 278 HIS A O     1 
ATOM   2054 C CB    . HIS A 1 284 ? -22.59800 14.15800 -6.85300  1.000 12.33099 ? 278 HIS A CB    1 
ATOM   2055 C CG    . HIS A 1 284 ? -21.49900 15.14400 -7.12500  1.000 13.15963 ? 278 HIS A CG    1 
ATOM   2056 N ND1   . HIS A 1 284 ? -21.77900 16.42900 -7.54300  1.000 14.84031 ? 278 HIS A ND1   1 
ATOM   2057 C CD2   . HIS A 1 284 ? -20.14600 15.05800 -7.04800  1.000 14.59177 ? 278 HIS A CD2   1 
ATOM   2058 C CE1   . HIS A 1 284 ? -20.64600 17.08900 -7.72800  1.000 15.81096 ? 278 HIS A CE1   1 
ATOM   2059 N NE2   . HIS A 1 284 ? -19.63900 16.28100 -7.43200  1.000 15.60184 ? 278 HIS A NE2   1 
ATOM   2060 N N     . VAL A 1 285 ? -20.39300 12.14700 -4.89700  1.000 14.09570 ? 279 VAL A N     1 
ATOM   2061 C CA    . VAL A 1 285 ? -19.83700 11.99900 -3.55500  1.000 14.50713 ? 279 VAL A CA    1 
ATOM   2062 C C     . VAL A 1 285 ? -18.53300 12.77400 -3.47800  1.000 13.94765 ? 279 VAL A C     1 
ATOM   2063 O O     . VAL A 1 285 ? -17.66800 12.63100 -4.34700  1.000 15.07571 ? 279 VAL A O     1 
ATOM   2064 C CB    . VAL A 1 285 ? -19.61800 10.52300 -3.16500  1.000 14.90650 ? 279 VAL A CB    1 
ATOM   2065 C CG1   . VAL A 1 285 ? -19.07700 10.43900 -1.73900  1.000 17.74549 ? 279 VAL A CG1   1 
ATOM   2066 C CG2   . VAL A 1 285 ? -20.92600 9.72200  -3.29100  1.000 16.73331 ? 279 VAL A CG2   1 
ATOM   2067 N N     . THR A 1 286 ? -18.39500 13.58800 -2.43900  1.000 14.36645 ? 280 THR A N     1 
ATOM   2068 C CA    . THR A 1 286 ? -17.12900 14.25200 -2.15800  1.000 17.11531 ? 280 THR A CA    1 
ATOM   2069 C C     . THR A 1 286 ? -16.38200 13.50500 -1.06800  1.000 20.25122 ? 280 THR A C     1 
ATOM   2070 O O     . THR A 1 286 ? -16.97000 13.09000 -0.06200  1.000 19.56838 ? 280 THR A O     1 
ATOM   2071 C CB    . THR A 1 286 ? -17.33300 15.69800 -1.72200  1.000 22.96477 ? 280 THR A CB    1 
ATOM   2072 O OG1   . THR A 1 286 ? -18.16000 15.71900 -0.55800  1.000 27.50728 ? 280 THR A OG1   1 
ATOM   2073 C CG2   . THR A 1 286 ? -18.02800 16.44300 -2.78300  1.000 25.39854 ? 280 THR A CG2   1 
ATOM   2074 N N     . GLN A 1 287 ? -15.09400 13.34100 -1.27600  1.000 21.86665 ? 281 GLN A N     1 
ATOM   2075 C CA    . GLN A 1 287 ? -14.27300 12.64000 -0.32100  1.000 24.49989 ? 281 GLN A CA    1 
ATOM   2076 C C     . GLN A 1 287 ? -13.34000 13.61800 0.37800   1.000 26.33339 ? 281 GLN A C     1 
ATOM   2077 O O     . GLN A 1 287 ? -12.98800 14.66300 -0.18100  1.000 26.40924 ? 281 GLN A O     1 
ATOM   2078 C CB    . GLN A 1 287 ? -13.43200 11.55400 -1.00600  1.000 25.22570 ? 281 GLN A CB    1 
ATOM   2079 C CG    . GLN A 1 287 ? -12.45800 12.09700 -2.05200  1.000 27.43831 ? 281 GLN A CG    1 
ATOM   2080 C CD    . GLN A 1 287 ? -11.56400 11.01500 -2.64300  1.000 30.92685 ? 281 GLN A CD    1 
ATOM   2081 O OE1   . GLN A 1 287 ? -11.86500 10.46400 -3.69700  1.000 32.60518 ? 281 GLN A OE1   1 
ATOM   2082 N NE2   . GLN A 1 287 ? -10.45300 10.71700 -1.97100  1.000 32.66390 ? 281 GLN A NE2   1 
ATOM   2083 N N     . PRO A 1 288 ? -12.92300 13.30900 1.59800   1.000 27.25803 ? 282 PRO A N     1 
ATOM   2084 C CA    . PRO A 1 288 ? -11.83500 14.06500 2.21400   1.000 30.29477 ? 282 PRO A CA    1 
ATOM   2085 C C     . PRO A 1 288 ? -10.50400 13.62500 1.62300   1.000 34.30876 ? 282 PRO A C     1 
ATOM   2086 O O     . PRO A 1 288 ? -10.39100 12.57000 0.99600   1.000 36.14628 ? 282 PRO A O     1 
ATOM   2087 C CB    . PRO A 1 288 ? -11.94400 13.69300 3.69600   1.000 29.58997 ? 282 PRO A CB    1 
ATOM   2088 C CG    . PRO A 1 288 ? -12.50500 12.29800 3.67700   1.000 28.89151 ? 282 PRO A CG    1 
ATOM   2089 C CD    . PRO A 1 288 ? -13.37100 12.18200 2.43700   1.000 28.26216 ? 282 PRO A CD    1 
ATOM   2090 N N     . ARG A 1 289 ? -9.49500  14.46600 1.80900   1.000 36.53884 ? 283 ARG A N     1 
ATOM   2091 C CA    . ARG A 1 289 ? -8.15700  14.12400 1.33400   1.000 38.14627 ? 283 ARG A CA    1 
ATOM   2092 C C     . ARG A 1 289 ? -7.18100  13.97800 2.49500   1.000 40.58090 ? 283 ARG A C     1 
ATOM   2093 O O     . ARG A 1 289 ? -6.89600  14.94400 3.19800   1.000 42.08315 ? 283 ARG A O     1 
ATOM   2094 C CB    . ARG A 1 289 ? -7.65000  15.17200 0.34500   1.000 36.72426 ? 283 ARG A CB    1 
ATOM   2095 C CG    . ARG A 1 289 ? -8.28800  15.06000 -1.02700  1.000 34.15113 ? 283 ARG A CG    1 
ATOM   2096 C CD    . ARG A 1 289 ? -7.70800  13.88100 -1.80500  1.000 32.61219 ? 283 ARG A CD    1 
ATOM   2097 N NE    . ARG A 1 289 ? -8.41200  13.68600 -3.06500  1.000 31.95401 ? 283 ARG A NE    1 
ATOM   2098 C CZ    . ARG A 1 289 ? -8.23300  12.66000 -3.88500  1.000 31.07247 ? 283 ARG A CZ    1 
ATOM   2099 N NH1   . ARG A 1 289 ? -7.35300  11.70900 -3.62100  1.000 30.84538 ? 283 ARG A NH1   1 
ATOM   2100 N NH2   . ARG A 1 289 ? -8.95000  12.58900 -5.00200  1.000 32.03916 ? 283 ARG A NH2   1 
ATOM   2101 N N     . SER A 1 303 ? -4.73000  5.81800  4.95900   1.000 47.58985 ? 297 SER A N     1 
ATOM   2102 C CA    . SER A 1 303 ? -5.90000  6.69000  4.95700   1.000 47.21022 ? 297 SER A CA    1 
ATOM   2103 C C     . SER A 1 303 ? -6.28900  7.08600  3.53300   1.000 46.91785 ? 297 SER A C     1 
ATOM   2104 O O     . SER A 1 303 ? -7.47200  7.10400  3.19500   1.000 47.75798 ? 297 SER A O     1 
ATOM   2105 C CB    . SER A 1 303 ? -5.64800  7.93700  5.80300   1.000 47.33199 ? 297 SER A CB    1 
ATOM   2106 N N     . GLU A 1 304 ? -5.29700  7.40700  2.69700   1.000 44.62835 ? 298 GLU A N     1 
ATOM   2107 C CA    . GLU A 1 304 ? -5.58800  7.66600  1.28900   1.000 43.86372 ? 298 GLU A CA    1 
ATOM   2108 C C     . GLU A 1 304 ? -6.15700  6.42000  0.62000   1.000 41.13359 ? 298 GLU A C     1 
ATOM   2109 O O     . GLU A 1 304 ? -7.15400  6.49100  -0.11100  1.000 39.98912 ? 298 GLU A O     1 
ATOM   2110 C CB    . GLU A 1 304 ? -4.32800  8.14100  0.56500   1.000 45.54547 ? 298 GLU A CB    1 
ATOM   2111 N N     . GLU A 1 305 ? -5.54100  5.26100  0.87200   1.000 38.91835 ? 299 GLU A N     1 
ATOM   2112 C CA    . GLU A 1 305 ? -6.06300  4.01400  0.32400   1.000 35.99100 ? 299 GLU A CA    1 
ATOM   2113 C C     . GLU A 1 305 ? -7.41400  3.65900  0.94100   1.000 33.67715 ? 299 GLU A C     1 
ATOM   2114 O O     . GLU A 1 305 ? -8.30200  3.14700  0.24800   1.000 32.30060 ? 299 GLU A O     1 
ATOM   2115 C CB    . GLU A 1 305 ? -5.05600  2.88300  0.53900   1.000 35.82546 ? 299 GLU A CB    1 
ATOM   2116 N N     . GLU A 1 306 ? -7.59200  3.92900  2.23800   1.000 31.79991 ? 300 GLU A N     1 
ATOM   2117 C CA    . GLU A 1 306 ? -8.87700  3.64700  2.87500   1.000 30.25914 ? 300 GLU A CA    1 
ATOM   2118 C C     . GLU A 1 306 ? -9.97300  4.56200  2.34000   1.000 27.70751 ? 300 GLU A C     1 
ATOM   2119 O O     . GLU A 1 306 ? -11.11500 4.12600  2.13500   1.000 27.00812 ? 300 GLU A O     1 
ATOM   2120 C CB    . GLU A 1 306 ? -8.75100  3.78700  4.39300   1.000 31.29961 ? 300 GLU A CB    1 
ATOM   2121 N N     . GLU A 1 307 ? -9.65200  5.83800  2.12200   1.000 26.57143 ? 301 GLU A N     1 
ATOM   2122 C CA    . GLU A 1 307 ? -10.64200 6.76400  1.58000   1.000 28.13194 ? 301 GLU A CA    1 
ATOM   2123 C C     . GLU A 1 307 ? -11.03000 6.37600  0.16000   1.000 27.32291 ? 301 GLU A C     1 
ATOM   2124 O O     . GLU A 1 307 ? -12.20900 6.45400  -0.21100  1.000 26.70017 ? 301 GLU A O     1 
ATOM   2125 C CB    . GLU A 1 307 ? -10.10500 8.19700  1.62100   1.000 29.89871 ? 301 GLU A CB    1 
ATOM   2126 N N     . ALA A 1 308 ? -10.05200 5.95400  -0.64800  1.000 26.39102 ? 302 ALA A N     1 
ATOM   2127 C CA    . ALA A 1 308 ? -10.35600 5.50300  -2.00000  1.000 25.54627 ? 302 ALA A CA    1 
ATOM   2128 C C     . ALA A 1 308 ? -11.21300 4.24400  -1.97500  1.000 24.82288 ? 302 ALA A C     1 
ATOM   2129 O O     . ALA A 1 308 ? -12.11300 4.08000  -2.81100  1.000 24.62319 ? 302 ALA A O     1 
ATOM   2130 C CB    . ALA A 1 308 ? -9.06200  5.25700  -2.78200  1.000 25.56543 ? 302 ALA A CB    1 
ATOM   2131 N N     . ARG A 1 309 ? -10.95100 3.34100  -1.02500  1.000 22.30719 ? 303 ARG A N     1 
ATOM   2132 C CA    . ARG A 1 309 ? -11.72900 2.11000  -0.97400  1.000 21.87607 ? 303 ARG A CA    1 
ATOM   2133 C C     . ARG A 1 309 ? -13.17200 2.40200  -0.58300  1.000 21.04508 ? 303 ARG A C     1 
ATOM   2134 O O     . ARG A 1 309 ? -14.10300 1.77100  -1.09300  1.000 20.88226 ? 303 ARG A O     1 
ATOM   2135 C CB    . ARG A 1 309 ? -11.10700 1.12300  0.01000   1.000 23.17054 ? 303 ARG A CB    1 
ATOM   2136 C CG    . ARG A 1 309 ? -11.99200 -0.09300 0.23100   1.000 25.03815 ? 303 ARG A CG    1 
ATOM   2137 C CD    . ARG A 1 309 ? -11.29200 -1.18600 0.98600   1.000 28.28107 ? 303 ARG A CD    1 
ATOM   2138 N NE    . ARG A 1 309 ? -11.15900 -0.83100 2.39100   1.000 31.81229 ? 303 ARG A NE    1 
ATOM   2139 C CZ    . ARG A 1 309 ? -10.41600 -1.49900 3.26300   1.000 35.86077 ? 303 ARG A CZ    1 
ATOM   2140 N NH1   . ARG A 1 309 ? -9.72500  -2.57200 2.90400   1.000 38.33991 ? 303 ARG A NH1   1 
ATOM   2141 N NH2   . ARG A 1 309 ? -10.37800 -1.09300 4.52800   1.000 35.31568 ? 303 ARG A NH2   1 
ATOM   2142 N N     . LEU A 1 310 ? -13.38100 3.37400  0.30200   1.000 18.92735 ? 304 LEU A N     1 
ATOM   2143 C CA    . LEU A 1 310 ? -14.74800 3.69300  0.69400   1.000 20.31962 ? 304 LEU A CA    1 
ATOM   2144 C C     . LEU A 1 310 ? -15.51100 4.31200  -0.47500  1.000 18.91053 ? 304 LEU A C     1 
ATOM   2145 O O     . LEU A 1 310 ? -16.66800 3.94900  -0.72600  1.000 18.46651 ? 304 LEU A O     1 
ATOM   2146 C CB    . LEU A 1 310 ? -14.72900 4.58300  1.94500   1.000 22.80582 ? 304 LEU A CB    1 
ATOM   2147 C CG    . LEU A 1 310 ? -15.99400 5.07100  2.67600   1.000 25.67566 ? 304 LEU A CG    1 
ATOM   2148 C CD1   . LEU A 1 310 ? -15.60100 5.84800  3.93900   1.000 27.78384 ? 304 LEU A CD1   1 
ATOM   2149 C CD2   . LEU A 1 310 ? -16.88500 5.95600  1.84000   1.000 27.20649 ? 304 LEU A CD2   1 
ATOM   2150 N N     . MET A 1 311 ? -14.86900 5.20300  -1.23900  1.000 19.17538 ? 305 MET A N     1 
ATOM   2151 C CA    . MET A 1 311 ? -15.52300 5.76100  -2.42400  1.000 19.03437 ? 305 MET A CA    1 
ATOM   2152 C C     . MET A 1 311 ? -15.86900 4.68600  -3.44500  1.000 18.82553 ? 305 MET A C     1 
ATOM   2153 O O     . MET A 1 311 ? -16.96900 4.69400  -4.01700  1.000 19.64949 ? 305 MET A O     1 
ATOM   2154 C CB    . MET A 1 311 ? -14.65400 6.83700  -3.07200  1.000 20.56249 ? 305 MET A CB    1 
ATOM   2155 C CG    . MET A 1 311 ? -14.51400 8.03000  -2.18600  1.000 23.49230 ? 305 MET A CG    1 
ATOM   2156 S SD    . MET A 1 311 ? -15.94000 9.07700  -2.54500  1.000 24.78232 ? 305 MET A SD    1 
ATOM   2157 C CE    . MET A 1 311 ? -15.57900 9.71700  -4.18900  1.000 22.76545 ? 305 MET A CE    1 
ATOM   2158 N N     . ARG A 1 312 ? -14.93600 3.76700  -3.70800  1.000 18.79572 ? 306 ARG A N     1 
ATOM   2159 C CA    . ARG A 1 312 ? -15.21900 2.68600  -4.64300  1.000 18.11251 ? 306 ARG A CA    1 
ATOM   2160 C C     . ARG A 1 312 ? -16.32900 1.78600  -4.12600  1.000 17.74579 ? 306 ARG A C     1 
ATOM   2161 O O     . ARG A 1 312 ? -17.12700 1.26800  -4.91600  1.000 19.53022 ? 306 ARG A O     1 
ATOM   2162 C CB    . ARG A 1 312 ? -13.94600 1.87200  -4.89900  1.000 20.20679 ? 306 ARG A CB    1 
ATOM   2163 C CG    . ARG A 1 312 ? -13.99500 0.94400  -6.10700  1.000 23.10979 ? 306 ARG A CG    1 
ATOM   2164 C CD    . ARG A 1 312 ? -14.59400 1.60600  -7.34700  1.000 25.22336 ? 306 ARG A CD    1 
ATOM   2165 N NE    . ARG A 1 312 ? -14.90700 0.60400  -8.36200  1.000 27.39368 ? 306 ARG A NE    1 
ATOM   2166 C CZ    . ARG A 1 312 ? -14.08400 0.23500  -9.33400  1.000 29.20660 ? 306 ARG A CZ    1 
ATOM   2167 N NH1   . ARG A 1 312 ? -12.91300 0.82300  -9.50900  1.000 29.85760 ? 306 ARG A NH1   1 
ATOM   2168 N NH2   . ARG A 1 312 ? -14.44700 -0.74600 -10.15200 1.000 30.52426 ? 306 ARG A NH2   1 
ATOM   2169 N N     . THR A 1 313 ? -16.40700 1.59500  -2.80900  1.000 16.66043 ? 307 THR A N     1 
ATOM   2170 C CA    . THR A 1 313 ? -17.46600 0.74700  -2.26100  1.000 16.56670 ? 307 THR A CA    1 
ATOM   2171 C C     . THR A 1 313 ? -18.84000 1.36500  -2.49900  1.000 16.68178 ? 307 THR A C     1 
ATOM   2172 O O     . THR A 1 313 ? -19.79500 0.66000  -2.85500  1.000 17.08209 ? 307 THR A O     1 
ATOM   2173 C CB    . THR A 1 313 ? -17.22500 0.49500  -0.76800  1.000 18.33519 ? 307 THR A CB    1 
ATOM   2174 O OG1   . THR A 1 313 ? -15.91000 -0.05600 -0.58100  1.000 19.19922 ? 307 THR A OG1   1 
ATOM   2175 C CG2   . THR A 1 313 ? -18.25200 -0.48700 -0.21800  1.000 19.29792 ? 307 THR A CG2   1 
ATOM   2176 N N     . LEU A 1 314 ? -18.95800 2.68100  -2.31200  1.000 15.33797 ? 308 LEU A N     1 
ATOM   2177 C CA    . LEU A 1 314 ? -20.20700 3.37200  -2.61200  1.000 15.48050 ? 308 LEU A CA    1 
ATOM   2178 C C     . LEU A 1 314 ? -20.53200 3.30200  -4.09700  1.000 14.39803 ? 308 LEU A C     1 
ATOM   2179 O O     . LEU A 1 314 ? -21.68600 3.05700  -4.48300  1.000 15.02117 ? 308 LEU A O     1 
ATOM   2180 C CB    . LEU A 1 314 ? -20.11000 4.82900  -2.15500  1.000 15.68177 ? 308 LEU A CB    1 
ATOM   2181 C CG    . LEU A 1 314 ? -19.87300 5.02700  -0.65800  1.000 16.59095 ? 308 LEU A CG    1 
ATOM   2182 C CD1   . LEU A 1 314 ? -19.76100 6.51600  -0.32600  1.000 18.87504 ? 308 LEU A CD1   1 
ATOM   2183 C CD2   . LEU A 1 314 ? -20.97400 4.35500  0.16900   1.000 16.88080 ? 308 LEU A CD2   1 
ATOM   2184 N N     . ARG A 1 315 ? -19.52800 3.53000  -4.94400  1.000 13.44964 ? 309 ARG A N     1 
ATOM   2185 C CA    . ARG A 1 315 ? -19.73400 3.48200  -6.39000  1.000 14.38870 ? 309 ARG A CA    1 
ATOM   2186 C C     . ARG A 1 315 ? -20.24300 2.11200  -6.81600  1.000 15.67403 ? 309 ARG A C     1 
ATOM   2187 O O     . ARG A 1 315 ? -21.23200 2.00300  -7.55100  1.000 16.29975 ? 309 ARG A O     1 
ATOM   2188 C CB    . ARG A 1 315 ? -18.42300 3.82000  -7.10700  1.000 16.78955 ? 309 ARG A CB    1 
ATOM   2189 C CG    . ARG A 1 315 ? -18.54000 4.03800  -8.62200  1.000 17.32258 ? 309 ARG A CG    1 
ATOM   2190 C CD    . ARG A 1 315 ? -18.53700 2.72900  -9.45200  1.000 18.50697 ? 309 ARG A CD    1 
ATOM   2191 N NE    . ARG A 1 315 ? -17.97600 2.96300  -10.77700 1.000 18.91754 ? 309 ARG A NE    1 
ATOM   2192 C CZ    . ARG A 1 315 ? -18.57500 3.64500  -11.75000 1.000 17.99024 ? 309 ARG A CZ    1 
ATOM   2193 N NH1   . ARG A 1 315 ? -19.83300 4.05600  -11.64000 1.000 16.35621 ? 309 ARG A NH1   1 
ATOM   2194 N NH2   . ARG A 1 315 ? -17.89200 3.92700  -12.85800 1.000 18.02495 ? 309 ARG A NH2   1 
ATOM   2195 N N     . ASN A 1 316 ? -19.58500 1.04600  -6.33800  1.000 15.03333 ? 310 ASN A N     1 
ATOM   2196 C CA    . ASN A 1 316 ? -19.99900 -0.30300 -6.72400  1.000 15.10822 ? 310 ASN A CA    1 
ATOM   2197 C C     . ASN A 1 316 ? -21.40500 -0.61200 -6.23400  1.000 16.67389 ? 310 ASN A C     1 
ATOM   2198 O O     . ASN A 1 316 ? -22.10700 -1.44100 -6.82900  1.000 17.05374 ? 310 ASN A O     1 
ATOM   2199 C CB    . ASN A 1 316 ? -19.02300 -1.34500 -6.16800  1.000 17.38598 ? 310 ASN A CB    1 
ATOM   2200 C CG    . ASN A 1 316 ? -17.67700 -1.33100 -6.86000  1.000 19.80552 ? 310 ASN A CG    1 
ATOM   2201 O OD1   . ASN A 1 316 ? -17.50100 -0.71300 -7.90800  1.000 21.75357 ? 310 ASN A OD1   1 
ATOM   2202 N ND2   . ASN A 1 316 ? -16.72000 -2.04200 -6.28100  1.000 19.22208 ? 310 ASN A ND2   1 
ATOM   2203 N N     . ALA A 1 317 ? -21.82900 0.03900  -5.15300  1.000 14.90843 ? 311 ALA A N     1 
ATOM   2204 C CA    . ALA A 1 317 ? -23.13800 -0.25100 -4.58500  1.000 14.64200 ? 311 ALA A CA    1 
ATOM   2205 C C     . ALA A 1 317 ? -24.26200 0.47300  -5.30400  1.000 14.99365 ? 311 ALA A C     1 
ATOM   2206 O O     . ALA A 1 317 ? -25.42200 0.05600  -5.18300  1.000 14.65873 ? 311 ALA A O     1 
ATOM   2207 C CB    . ALA A 1 317 ? -23.17400 0.12800  -3.10500  1.000 15.96705 ? 311 ALA A CB    1 
ATOM   2208 N N     . TYR A 1 318 ? -23.95200 1.52400  -6.05500  1.000 13.79946 ? 312 TYR A N     1 
ATOM   2209 C CA    . TYR A 1 318 ? -24.97400 2.39600  -6.62100  1.000 13.62146 ? 312 TYR A CA    1 
ATOM   2210 C C     . TYR A 1 318 ? -25.27700 2.00400  -8.06900  1.000 14.10324 ? 312 TYR A C     1 
ATOM   2211 O O     . TYR A 1 318 ? -24.36100 1.83400  -8.88600  1.000 13.75859 ? 312 TYR A O     1 
ATOM   2212 C CB    . TYR A 1 318 ? -24.55300 3.87100  -6.53400  1.000 14.95130 ? 312 TYR A CB    1 
ATOM   2213 C CG    . TYR A 1 318 ? -25.51900 4.74600  -7.27800  1.000 14.31295 ? 312 TYR A CG    1 
ATOM   2214 C CD1   . TYR A 1 318 ? -26.88000 4.73600  -6.95600  1.000 14.87883 ? 312 TYR A CD1   1 
ATOM   2215 C CD2   . TYR A 1 318 ? -25.09900 5.52400  -8.35400  1.000 14.97539 ? 312 TYR A CD2   1 
ATOM   2216 C CE1   . TYR A 1 318 ? -27.78600 5.50500  -7.67800  1.000 14.61594 ? 312 TYR A CE1   1 
ATOM   2217 C CE2   . TYR A 1 318 ? -25.99400 6.29600  -9.07500  1.000 13.22153 ? 312 TYR A CE2   1 
ATOM   2218 C CZ    . TYR A 1 318 ? -27.33100 6.27600  -8.73800  1.000 14.37728 ? 312 TYR A CZ    1 
ATOM   2219 O OH    . TYR A 1 318 ? -28.20900 7.02500  -9.47500  1.000 15.86039 ? 312 TYR A OH    1 
ATOM   2220 N N     . GLN A 1 319 ? -26.57000 1.85800  -8.38000  1.000 13.76918 ? 313 GLN A N     1 
ATOM   2221 C CA    . GLN A 1 319 ? -27.03300 1.47900  -9.71600  1.000 14.90477 ? 313 GLN A CA    1 
ATOM   2222 C C     . GLN A 1 319 ? -27.16400 2.73400  -10.57700 1.000 15.61837 ? 313 GLN A C     1 
ATOM   2223 O O     . GLN A 1 319 ? -28.26100 3.26300  -10.79600 1.000 17.61045 ? 313 GLN A O     1 
ATOM   2224 C CB    . GLN A 1 319 ? -28.36700 0.74100  -9.62600  1.000 16.34804 ? 313 GLN A CB    1 
ATOM   2225 C CG    . GLN A 1 319 ? -28.31800 -0.62100 -8.97500  1.000 18.27388 ? 313 GLN A CG    1 
ATOM   2226 C CD    . GLN A 1 319 ? -29.68600 -1.27800 -8.90800  1.000 19.37964 ? 313 GLN A CD    1 
ATOM   2227 O OE1   . GLN A 1 319 ? -30.54000 -1.04400 -9.77500  1.000 20.11002 ? 313 GLN A OE1   1 
ATOM   2228 N NE2   . GLN A 1 319 ? -29.89400 -2.13300 -7.89900  1.000 18.39202 ? 313 GLN A NE2   1 
ATOM   2229 N N     . GLY A 1 320 ? -26.03200 3.23500  -11.06400 1.000 15.29093 ? 314 GLY A N     1 
ATOM   2230 C CA    . GLY A 1 320 ? -26.09400 4.40100  -11.93200 1.000 15.45680 ? 314 GLY A CA    1 
ATOM   2231 C C     . GLY A 1 320 ? -24.76300 5.14000  -12.01500 1.000 15.79696 ? 314 GLY A C     1 
ATOM   2232 O O     . GLY A 1 320 ? -23.70900 4.60000  -11.67900 1.000 15.88381 ? 314 GLY A O     1 
ATOM   2233 N N     . THR A 1 321 ? -24.86100 6.38000  -12.49900 1.000 15.82072 ? 315 THR A N     1 
ATOM   2234 C CA    . THR A 1 321 ? -23.71000 7.24500  -12.75100 1.000 14.01622 ? 315 THR A CA    1 
ATOM   2235 C C     . THR A 1 321 ? -23.12100 7.78700  -11.45600 1.000 14.09488 ? 315 THR A C     1 
ATOM   2236 O O     . THR A 1 321 ? -23.84200 8.24900  -10.58000 1.000 13.49802 ? 315 THR A O     1 
ATOM   2237 C CB    . THR A 1 321 ? -24.14300 8.41600  -13.63400 1.000 15.54355 ? 315 THR A CB    1 
ATOM   2238 O OG1   . THR A 1 321 ? -24.53200 7.92400  -14.92200 1.000 17.15765 ? 315 THR A OG1   1 
ATOM   2239 C CG2   . THR A 1 321 ? -23.01700 9.44300  -13.79800 1.000 15.25124 ? 315 THR A CG2   1 
ATOM   2240 N N     . PHE A 1 322 ? -21.79300 7.77000  -11.35700 1.000 14.89332 ? 316 PHE A N     1 
ATOM   2241 C CA    . PHE A 1 322 ? -21.08800 8.17500  -10.14800 1.000 14.31523 ? 316 PHE A CA    1 
ATOM   2242 C C     . PHE A 1 322 ? -20.14400 9.31800  -10.48700 1.000 13.23870 ? 316 PHE A C     1 
ATOM   2243 O O     . PHE A 1 322 ? -19.28100 9.17300  -11.36900 1.000 15.08627 ? 316 PHE A O     1 
ATOM   2244 C CB    . PHE A 1 322 ? -20.31300 6.98900  -9.56300  1.000 15.17914 ? 316 PHE A CB    1 
ATOM   2245 C CG    . PHE A 1 322 ? -19.79500 7.21300  -8.16600  1.000 15.16203 ? 316 PHE A CG    1 
ATOM   2246 C CD1   . PHE A 1 322 ? -20.61400 6.99400  -7.06900  1.000 16.39263 ? 316 PHE A CD1   1 
ATOM   2247 C CD2   . PHE A 1 322 ? -18.48300 7.62200  -7.95300  1.000 16.00637 ? 316 PHE A CD2   1 
ATOM   2248 C CE1   . PHE A 1 322 ? -20.13700 7.17000  -5.77800  1.000 16.71738 ? 316 PHE A CE1   1 
ATOM   2249 C CE2   . PHE A 1 322 ? -17.98900 7.80500  -6.66500  1.000 16.97977 ? 316 PHE A CE2   1 
ATOM   2250 C CZ    . PHE A 1 322 ? -18.83100 7.58100  -5.56900  1.000 16.76842 ? 316 PHE A CZ    1 
ATOM   2251 N N     . ILE A 1 323 ? -20.31300 10.44400 -9.79400  1.000 13.01628 ? 317 ILE A N     1 
ATOM   2252 C CA    . ILE A 1 323 ? -19.42700 11.59800 -9.88700  1.000 13.02992 ? 317 ILE A CA    1 
ATOM   2253 C C     . ILE A 1 323 ? -18.59400 11.66100 -8.61900  1.000 13.32254 ? 317 ILE A C     1 
ATOM   2254 O O     . ILE A 1 323 ? -19.13300 11.75100 -7.51500  1.000 13.47317 ? 317 ILE A O     1 
ATOM   2255 C CB    . ILE A 1 323 ? -20.20200 12.91300 -10.06900 1.000 13.59713 ? 317 ILE A CB    1 
ATOM   2256 C CG1   . ILE A 1 323 ? -21.28400 12.77100 -11.14100 1.000 13.63018 ? 317 ILE A CG1   1 
ATOM   2257 C CG2   . ILE A 1 323 ? -19.21700 14.06500 -10.38500 1.000 13.70112 ? 317 ILE A CG2   1 
ATOM   2258 C CD1   . ILE A 1 323 ? -21.93000 14.12000 -11.57600 1.000 14.62087 ? 317 ILE A CD1   1 
ATOM   2259 N N     . CYS A 1 324 ? -17.28700 11.63900 -8.77400  1.000 14.02394 ? 318 CYS A N     1 
ATOM   2260 C CA    . CYS A 1 324 ? -16.36000 11.77300 -7.66100  1.000 16.91091 ? 318 CYS A CA    1 
ATOM   2261 C C     . CYS A 1 324 ? -15.80400 13.19100 -7.57800  1.000 16.30059 ? 318 CYS A C     1 
ATOM   2262 O O     . CYS A 1 324 ? -15.68100 13.88300 -8.58600  1.000 15.95429 ? 318 CYS A O     1 
ATOM   2263 C CB    . CYS A 1 324 ? -15.27300 10.71000 -7.81800  1.000 20.39302 ? 318 CYS A CB    1 
ATOM   2264 S SG    . CYS A 1 324 ? -14.10800 11.08200 -9.12300  1.000 23.52168 ? 318 CYS A SG    1 
ATOM   2265 N N     . SER A 1 325 ? -15.51000 13.63700 -6.35600  1.000 15.58630 ? 319 SER A N     1 
ATOM   2266 C CA    . SER A 1 325 ? -15.10200 15.01800 -6.14100  1.000 16.56477 ? 319 SER A CA    1 
ATOM   2267 C C     . SER A 1 325 ? -14.24000 15.09500 -4.89600  1.000 17.16160 ? 319 SER A C     1 
ATOM   2268 O O     . SER A 1 325 ? -14.41500 14.31800 -3.95100  1.000 18.40106 ? 319 SER A O     1 
ATOM   2269 C CB    . SER A 1 325 ? -16.31300 15.95600 -5.98500  1.000 20.55033 ? 319 SER A CB    1 
ATOM   2270 O OG    . SER A 1 325 ? -15.92200 17.32800 -5.98800  1.000 22.77829 ? 319 SER A OG    1 
ATOM   2271 N N     . GLY A 1 326 ? -13.31800 16.05500 -4.90400  1.000 16.91165 ? 320 GLY A N     1 
ATOM   2272 C CA    . GLY A 1 326 ? -12.52900 16.37400 -3.73200  1.000 18.41414 ? 320 GLY A CA    1 
ATOM   2273 C C     . GLY A 1 326 ? -11.04500 16.18600 -3.95900  1.000 18.56188 ? 320 GLY A C     1 
ATOM   2274 O O     . GLY A 1 326 ? -10.53800 15.06300 -3.88200  1.000 19.91148 ? 320 GLY A O     1 
ATOM   2275 N N     . GLY A 1 327 ? -10.34200 17.28200 -4.23900  1.000 17.39215 ? 321 GLY A N     1 
ATOM   2276 C CA    . GLY A 1 327 ? -8.90500  17.22700 -4.40000  1.000 19.60690 ? 321 GLY A CA    1 
ATOM   2277 C C     . GLY A 1 327 ? -8.44000  16.62100 -5.70100  1.000 20.46699 ? 321 GLY A C     1 
ATOM   2278 O O     . GLY A 1 327 ? -7.28000  16.21300 -5.79700  1.000 21.44794 ? 321 GLY A O     1 
ATOM   2279 N N     . TYR A 1 328 ? -9.30100  16.54000 -6.71200  1.000 20.75595 ? 322 TYR A N     1 
ATOM   2280 C CA    . TYR A 1 328 ? -8.88700  15.90600 -7.95100  1.000 21.12287 ? 322 TYR A CA    1 
ATOM   2281 C C     . TYR A 1 328 ? -7.97700  16.82600 -8.75800  1.000 22.84574 ? 322 TYR A C     1 
ATOM   2282 O O     . TYR A 1 328 ? -8.03100  18.05700 -8.65900  1.000 23.33335 ? 322 TYR A O     1 
ATOM   2283 C CB    . TYR A 1 328 ? -10.10500 15.45100 -8.77100  1.000 20.16646 ? 322 TYR A CB    1 
ATOM   2284 C CG    . TYR A 1 328 ? -10.62500 14.14600 -8.21400  1.000 21.82613 ? 322 TYR A CG    1 
ATOM   2285 C CD1   . TYR A 1 328 ? -11.52100 14.13500 -7.14800  1.000 21.95400 ? 322 TYR A CD1   1 
ATOM   2286 C CD2   . TYR A 1 328 ? -10.14900 12.92300 -8.68200  1.000 23.38647 ? 322 TYR A CD2   1 
ATOM   2287 C CE1   . TYR A 1 328 ? -11.96600 12.94400 -6.59000  1.000 23.49007 ? 322 TYR A CE1   1 
ATOM   2288 C CE2   . TYR A 1 328 ? -10.59100 11.72600 -8.12900  1.000 24.09200 ? 322 TYR A CE2   1 
ATOM   2289 C CZ    . TYR A 1 328 ? -11.49600 11.74700 -7.07300  1.000 24.94280 ? 322 TYR A CZ    1 
ATOM   2290 O OH    . TYR A 1 328 ? -11.93700 10.56600 -6.50100  1.000 26.53180 ? 322 TYR A OH    1 
ATOM   2291 N N     . THR A 1 329 ? -7.08700  16.19700 -9.50400  1.000 22.31836 ? 323 THR A N     1 
ATOM   2292 C CA    . THR A 1 329 ? -6.16900  16.83100 -10.43100 1.000 22.66212 ? 323 THR A CA    1 
ATOM   2293 C C     . THR A 1 329 ? -6.38600  16.19000 -11.79000 1.000 21.54170 ? 323 THR A C     1 
ATOM   2294 O O     . THR A 1 329 ? -7.20000  15.27300 -11.93500 1.000 22.45726 ? 323 THR A O     1 
ATOM   2295 C CB    . THR A 1 329 ? -4.72000  16.65600 -9.98000  1.000 23.52919 ? 323 THR A CB    1 
ATOM   2296 O OG1   . THR A 1 329 ? -4.43000  15.25700 -9.90400  1.000 23.66922 ? 323 THR A OG1   1 
ATOM   2297 C CG2   . THR A 1 329 ? -4.49100  17.29700 -8.61300  1.000 24.00951 ? 323 THR A CG2   1 
ATOM   2298 N N     . ARG A 1 330 ? -5.65900  16.66900 -12.80000 1.000 21.04981 ? 324 ARG A N     1 
ATOM   2299 C CA    . ARG A 1 330 ? -5.73600  16.01500 -14.10100 1.000 19.67732 ? 324 ARG A CA    1 
ATOM   2300 C C     . ARG A 1 330 ? -5.35900  14.54400 -13.97700 1.000 20.79387 ? 324 ARG A C     1 
ATOM   2301 O O     . ARG A 1 330 ? -6.08500  13.66000 -14.44200 1.000 21.68930 ? 324 ARG A O     1 
ATOM   2302 C CB    . ARG A 1 330 ? -4.83600  16.72800 -15.10900 1.000 19.35932 ? 324 ARG A CB    1 
ATOM   2303 C CG    . ARG A 1 330 ? -4.79700  16.04000 -16.48300 1.000 20.17581 ? 324 ARG A CG    1 
ATOM   2304 C CD    . ARG A 1 330 ? -3.93800  16.82700 -17.45600 1.000 21.00046 ? 324 ARG A CD    1 
ATOM   2305 N NE    . ARG A 1 330 ? -4.05300  16.36900 -18.83600 1.000 24.98558 ? 324 ARG A NE    1 
ATOM   2306 C CZ    . ARG A 1 330 ? -3.38800  15.34200 -19.34700 1.000 26.14129 ? 324 ARG A CZ    1 
ATOM   2307 N NH1   . ARG A 1 330 ? -2.56700  14.61300 -18.60600 1.000 27.50294 ? 324 ARG A NH1   1 
ATOM   2308 N NH2   . ARG A 1 330 ? -3.55400  15.03400 -20.63100 1.000 26.77904 ? 324 ARG A NH2   1 
ATOM   2309 N N     . GLU A 1 331 ? -4.25400  14.26500 -13.28300 1.000 21.02093 ? 325 GLU A N     1 
ATOM   2310 C CA    . GLU A 1 331 ? -3.76500  12.89600 -13.16100 1.000 22.89181 ? 325 GLU A CA    1 
ATOM   2311 C C     . GLU A 1 331 ? -4.72700  12.02900 -12.35400 1.000 21.58038 ? 325 GLU A C     1 
ATOM   2312 O O     . GLU A 1 331 ? -5.01900  10.89100 -12.74400 1.000 21.08360 ? 325 GLU A O     1 
ATOM   2313 C CB    . GLU A 1 331 ? -2.36900  12.88700 -12.51800 1.000 25.16949 ? 325 GLU A CB    1 
ATOM   2314 N N     . LEU A 1 332 ? -5.22600  12.53900 -11.22100 1.000 21.62270 ? 326 LEU A N     1 
ATOM   2315 C CA    . LEU A 1 332 ? -6.14800  11.73600 -10.41800 1.000 20.91822 ? 326 LEU A CA    1 
ATOM   2316 C C     . LEU A 1 332 ? -7.49100  11.56100 -11.11500 1.000 20.76771 ? 326 LEU A C     1 
ATOM   2317 O O     . LEU A 1 332 ? -8.15100  10.53200 -10.93000 1.000 20.88129 ? 326 LEU A O     1 
ATOM   2318 C CB    . LEU A 1 332 ? -6.34700  12.35500 -9.02700  1.000 21.37867 ? 326 LEU A CB    1 
ATOM   2319 C CG    . LEU A 1 332 ? -5.14900  12.33900 -8.06200  1.000 24.13052 ? 326 LEU A CG    1 
ATOM   2320 C CD1   . LEU A 1 332 ? -5.40700  13.24800 -6.85900  1.000 24.53758 ? 326 LEU A CD1   1 
ATOM   2321 C CD2   . LEU A 1 332 ? -4.84000  10.92300 -7.60100  1.000 25.36499 ? 326 LEU A CD2   1 
ATOM   2322 N N     . GLY A 1 333 ? -7.91300  12.54800 -11.91000 1.000 19.28541 ? 327 GLY A N     1 
ATOM   2323 C CA    . GLY A 1 333 ? -9.16000  12.40300 -12.64800 1.000 19.48551 ? 327 GLY A CA    1 
ATOM   2324 C C     . GLY A 1 333 ? -9.04900  11.37400 -13.75500 1.000 19.82947 ? 327 GLY A C     1 
ATOM   2325 O O     . GLY A 1 333 ? -9.95100  10.55000 -13.94800 1.000 19.54607 ? 327 GLY A O     1 
ATOM   2326 N N     . ILE A 1 334 ? -7.94200  11.40400 -14.49500 1.000 19.62836 ? 328 ILE A N     1 
ATOM   2327 C CA    . ILE A 1 334 ? -7.69600  10.38500 -15.50700 1.000 20.29822 ? 328 ILE A CA    1 
ATOM   2328 C C     . ILE A 1 334 ? -7.71100  8.99500  -14.87800 1.000 21.09697 ? 328 ILE A C     1 
ATOM   2329 O O     . ILE A 1 334 ? -8.34800  8.06900  -15.39600 1.000 21.46962 ? 328 ILE A O     1 
ATOM   2330 C CB    . ILE A 1 334 ? -6.36800  10.67200 -16.22800 1.000 20.91057 ? 328 ILE A CB    1 
ATOM   2331 C CG1   . ILE A 1 334 ? -6.52300  11.90900 -17.11000 1.000 21.08728 ? 328 ILE A CG1   1 
ATOM   2332 C CG2   . ILE A 1 334 ? -5.92400  9.46700  -17.05500 1.000 21.95983 ? 328 ILE A CG2   1 
ATOM   2333 C CD1   . ILE A 1 334 ? -5.21100  12.38900 -17.75400 1.000 22.26527 ? 328 ILE A CD1   1 
ATOM   2334 N N     . GLU A 1 335 ? -7.01500  8.82700  -13.74500 1.000 20.98942 ? 329 GLU A N     1 
ATOM   2335 C CA    . GLU A 1 335 ? -6.96900  7.50800  -13.11000 1.000 22.47504 ? 329 GLU A CA    1 
ATOM   2336 C C     . GLU A 1 335 ? -8.35200  7.05800  -12.64800 1.000 22.68419 ? 329 GLU A C     1 
ATOM   2337 O O     . GLU A 1 335 ? -8.71100  5.88700  -12.80200 1.000 22.96415 ? 329 GLU A O     1 
ATOM   2338 C CB    . GLU A 1 335 ? -5.98700  7.50800  -11.93700 1.000 23.11374 ? 329 GLU A CB    1 
ATOM   2339 N N     . ALA A 1 336 ? -9.14400  7.97300  -12.07600 1.000 22.43270 ? 330 ALA A N     1 
ATOM   2340 C CA    . ALA A 1 336 ? -10.46700 7.59300  -11.58100 1.000 21.15696 ? 330 ALA A CA    1 
ATOM   2341 C C     . ALA A 1 336 ? -11.32900 7.02300  -12.70600 1.000 20.93933 ? 330 ALA A C     1 
ATOM   2342 O O     . ALA A 1 336 ? -11.98800 5.98900  -12.54100 1.000 20.78468 ? 330 ALA A O     1 
ATOM   2343 C CB    . ALA A 1 336 ? -11.14900 8.79500  -10.92700 1.000 20.83107 ? 330 ALA A CB    1 
ATOM   2344 N N     . VAL A 1 337 ? -11.33200 7.67800  -13.86500 1.000 20.47789 ? 331 VAL A N     1 
ATOM   2345 C CA    . VAL A 1 337 ? -12.13700 7.16800  -14.97200 1.000 20.76169 ? 331 VAL A CA    1 
ATOM   2346 C C     . VAL A 1 337 ? -11.51100 5.90200  -15.55500 1.000 22.42193 ? 331 VAL A C     1 
ATOM   2347 O O     . VAL A 1 337 ? -12.21200 4.92200  -15.82900 1.000 22.66200 ? 331 VAL A O     1 
ATOM   2348 C CB    . VAL A 1 337 ? -12.33500 8.25900  -16.03800 1.000 20.75577 ? 331 VAL A CB    1 
ATOM   2349 C CG1   . VAL A 1 337 ? -13.10400 7.70600  -17.23900 1.000 19.71937 ? 331 VAL A CG1   1 
ATOM   2350 C CG2   . VAL A 1 337 ? -13.06600 9.45600  -15.44100 1.000 22.30857 ? 331 VAL A CG2   1 
ATOM   2351 N N     . ALA A 1 338 ? -10.18300 5.89300  -15.73500 1.000 21.65972 ? 332 ALA A N     1 
ATOM   2352 C CA    . ALA A 1 338 ? -9.51600  4.73000  -16.31400 1.000 22.59561 ? 332 ALA A CA    1 
ATOM   2353 C C     . ALA A 1 338 ? -9.68300  3.47800  -15.45200 1.000 24.02194 ? 332 ALA A C     1 
ATOM   2354 O O     . ALA A 1 338 ? -9.81900  2.37200  -15.98600 1.000 26.21188 ? 332 ALA A O     1 
ATOM   2355 C CB    . ALA A 1 338 ? -8.03300  5.03400  -16.53200 1.000 23.71276 ? 332 ALA A CB    1 
ATOM   2356 N N     . GLN A 1 339 ? -9.65200  3.61900  -14.12300 1.000 22.97644 ? 333 GLN A N     1 
ATOM   2357 C CA    . GLN A 1 339 ? -9.78800  2.46000  -13.23800 1.000 25.04215 ? 333 GLN A CA    1 
ATOM   2358 C C     . GLN A 1 339 ? -11.23700 2.07600  -12.95500 1.000 24.74866 ? 333 GLN A C     1 
ATOM   2359 O O     . GLN A 1 339 ? -11.46800 1.09800  -12.23100 1.000 27.73595 ? 333 GLN A O     1 
ATOM   2360 C CB    . GLN A 1 339 ? -9.05900  2.69900  -11.90500 1.000 28.86656 ? 333 GLN A CB    1 
ATOM   2361 C CG    . GLN A 1 339 ? -7.55200  2.96900  -12.02800 1.000 33.95288 ? 333 GLN A CG    1 
ATOM   2362 C CD    . GLN A 1 339 ? -6.94200  3.57500  -10.76100 1.000 39.50333 ? 333 GLN A CD    1 
ATOM   2363 O OE1   . GLN A 1 339 ? -7.57000  3.58900  -9.69300  1.000 41.80158 ? 333 GLN A OE1   1 
ATOM   2364 N NE2   . GLN A 1 339 ? -5.70800  4.07300  -10.87500 1.000 41.24451 ? 333 GLN A NE2   1 
ATOM   2365 N N     . GLY A 1 340 ? -12.21400 2.80500  -13.49700 1.000 22.47209 ? 334 GLY A N     1 
ATOM   2366 C CA    . GLY A 1 340 ? -13.60700 2.51700  -13.24100 1.000 22.43737 ? 334 GLY A CA    1 
ATOM   2367 C C     . GLY A 1 340 ? -14.12400 3.04000  -11.92400 1.000 22.06876 ? 334 GLY A C     1 
ATOM   2368 O O     . GLY A 1 340 ? -15.23900 2.68600  -11.53300 1.000 23.73182 ? 334 GLY A O     1 
ATOM   2369 N N     . ASP A 1 341 ? -13.33900 3.85800  -11.21900 1.000 21.65737 ? 335 ASP A N     1 
ATOM   2370 C CA    . ASP A 1 341 ? -13.72900 4.36500  -9.91000  1.000 21.31156 ? 335 ASP A CA    1 
ATOM   2371 C C     . ASP A 1 341 ? -14.84800 5.39600  -9.99500  1.000 19.37315 ? 335 ASP A C     1 
ATOM   2372 O O     . ASP A 1 341 ? -15.56300 5.61100  -9.00900  1.000 19.47062 ? 335 ASP A O     1 
ATOM   2373 C CB    . ASP A 1 341 ? -12.51200 4.98000  -9.21200  1.000 24.11576 ? 335 ASP A CB    1 
ATOM   2374 C CG    . ASP A 1 341 ? -11.38600 3.97700  -9.01000  1.000 28.79134 ? 335 ASP A CG    1 
ATOM   2375 O OD1   . ASP A 1 341 ? -11.68000 2.79000  -8.75600  1.000 29.36726 ? 335 ASP A OD1   1 
ATOM   2376 O OD2   . ASP A 1 341 ? -10.20100 4.37900  -9.08700  1.000 30.68942 ? 335 ASP A OD2   1 
ATOM   2377 N N     . ALA A 1 342 ? -15.00900 6.04400  -11.14000 1.000 18.26400 ? 336 ALA A N     1 
ATOM   2378 C CA    . ALA A 1 342 ? -16.04900 7.04800  -11.31000 1.000 16.87115 ? 336 ALA A CA    1 
ATOM   2379 C C     . ALA A 1 342 ? -16.34700 7.17700  -12.79000 1.000 16.36849 ? 336 ALA A C     1 
ATOM   2380 O O     . ALA A 1 342 ? -15.52100 6.83300  -13.63900 1.000 18.60805 ? 336 ALA A O     1 
ATOM   2381 C CB    . ALA A 1 342 ? -15.63000 8.40500  -10.73400 1.000 18.75037 ? 336 ALA A CB    1 
ATOM   2382 N N     . ASP A 1 343 ? -17.53800 7.68900  -13.09200 1.000 16.07934 ? 337 ASP A N     1 
ATOM   2383 C CA    . ASP A 1 343 ? -17.87700 7.99900  -14.47400 1.000 16.33585 ? 337 ASP A CA    1 
ATOM   2384 C C     . ASP A 1 343 ? -17.55100 9.43800  -14.83400 1.000 16.46367 ? 337 ASP A C     1 
ATOM   2385 O O     . ASP A 1 343 ? -17.15100 9.70800  -15.96700 1.000 17.07605 ? 337 ASP A O     1 
ATOM   2386 C CB    . ASP A 1 343 ? -19.35800 7.71600  -14.72600 1.000 16.92466 ? 337 ASP A CB    1 
ATOM   2387 C CG    . ASP A 1 343 ? -19.73900 6.30900  -14.33300 1.000 17.32877 ? 337 ASP A CG    1 
ATOM   2388 O OD1   . ASP A 1 343 ? -19.22700 5.37700  -14.99600 1.000 16.87157 ? 337 ASP A OD1   1 
ATOM   2389 O OD2   . ASP A 1 343 ? -20.53100 6.13200  -13.36800 1.000 15.70914 ? 337 ASP A OD2   1 
ATOM   2390 N N     . LEU A 1 344 ? -17.73300 10.36600 -13.89700 1.000 15.30656 ? 338 LEU A N     1 
ATOM   2391 C CA    . LEU A 1 344 ? -17.44000 11.77400 -14.11500 1.000 14.81103 ? 338 LEU A CA    1 
ATOM   2392 C C     . LEU A 1 344 ? -16.62900 12.27300 -12.92900 1.000 14.12043 ? 338 LEU A C     1 
ATOM   2393 O O     . LEU A 1 344 ? -16.70000 11.70700 -11.83800 1.000 15.96486 ? 338 LEU A O     1 
ATOM   2394 C CB    . LEU A 1 344 ? -18.73200 12.60900 -14.27700 1.000 15.07595 ? 338 LEU A CB    1 
ATOM   2395 C CG    . LEU A 1 344 ? -19.76600 12.07800 -15.27100 1.000 16.01759 ? 338 LEU A CG    1 
ATOM   2396 C CD1   . LEU A 1 344 ? -21.10700 12.76400 -15.04100 1.000 15.22536 ? 338 LEU A CD1   1 
ATOM   2397 C CD2   . LEU A 1 344 ? -19.26100 12.35800 -16.68000 1.000 17.00765 ? 338 LEU A CD2   1 
ATOM   2398 N N     . VAL A 1 345 ? -15.83100 13.31800 -13.15700 1.000 14.66282 ? 339 VAL A N     1 
ATOM   2399 C CA    . VAL A 1 345 ? -14.98700 13.89900 -12.12000 1.000 15.28667 ? 339 VAL A CA    1 
ATOM   2400 C C     . VAL A 1 345 ? -15.30500 15.38800 -12.03800 1.000 15.13212 ? 339 VAL A C     1 
ATOM   2401 O O     . VAL A 1 345 ? -15.19100 16.09900 -13.04400 1.000 14.31106 ? 339 VAL A O     1 
ATOM   2402 C CB    . VAL A 1 345 ? -13.48900 13.68000 -12.41600 1.000 16.08488 ? 339 VAL A CB    1 
ATOM   2403 C CG1   . VAL A 1 345 ? -12.62100 14.30000 -11.32500 1.000 16.14953 ? 339 VAL A CG1   1 
ATOM   2404 C CG2   . VAL A 1 345 ? -13.16400 12.20400 -12.59400 1.000 17.19221 ? 339 VAL A CG2   1 
ATOM   2405 N N     . SER A 1 346 ? -15.69700 15.86900 -10.85300 1.000 13.82338 ? 340 SER A N     1 
ATOM   2406 C CA    . SER A 1 346 ? -15.94400 17.30100 -10.70900 1.000 14.06802 ? 340 SER A CA    1 
ATOM   2407 C C     . SER A 1 346 ? -14.75100 17.98900 -10.06400 1.000 14.02575 ? 340 SER A C     1 
ATOM   2408 O O     . SER A 1 346 ? -14.07400 17.42800 -9.18800  1.000 15.41165 ? 340 SER A O     1 
ATOM   2409 C CB    . SER A 1 346 ? -17.22400 17.62100 -9.92300  1.000 15.36206 ? 340 SER A CB    1 
ATOM   2410 O OG    . SER A 1 346 ? -17.17200 17.20800 -8.57600  1.000 16.03465 ? 340 SER A OG    1 
ATOM   2411 N N     . TYR A 1 347 ? -14.49900 19.20400 -10.52900 1.000 14.29620 ? 341 TYR A N     1 
ATOM   2412 C CA    . TYR A 1 347 ? -13.39700 20.04500 -10.09200 1.000 14.29009 ? 341 TYR A CA    1 
ATOM   2413 C C     . TYR A 1 347 ? -13.96600 21.33800 -9.54800  1.000 14.91973 ? 341 TYR A C     1 
ATOM   2414 O O     . TYR A 1 347 ? -14.80300 21.96900 -10.20200 1.000 14.90132 ? 341 TYR A O     1 
ATOM   2415 C CB    . TYR A 1 347 ? -12.45300 20.36000 -11.25100 1.000 14.66446 ? 341 TYR A CB    1 
ATOM   2416 C CG    . TYR A 1 347 ? -11.69000 19.16500 -11.74300 1.000 15.09785 ? 341 TYR A CG    1 
ATOM   2417 C CD1   . TYR A 1 347 ? -12.25000 18.30400 -12.68300 1.000 14.57969 ? 341 TYR A CD1   1 
ATOM   2418 C CD2   . TYR A 1 347 ? -10.42000 18.88000 -11.25100 1.000 15.51521 ? 341 TYR A CD2   1 
ATOM   2419 C CE1   . TYR A 1 347 ? -11.56000 17.21000 -13.14300 1.000 15.05308 ? 341 TYR A CE1   1 
ATOM   2420 C CE2   . TYR A 1 347 ? -9.72000  17.78200 -11.70200 1.000 15.84487 ? 341 TYR A CE2   1 
ATOM   2421 C CZ    . TYR A 1 347 ? -10.29600 16.94800 -12.64600 1.000 16.10938 ? 341 TYR A CZ    1 
ATOM   2422 O OH    . TYR A 1 347 ? -9.61900  15.85500 -13.10400 1.000 16.10968 ? 341 TYR A OH    1 
ATOM   2423 N N     . GLY A 1 348 ? -13.49400 21.74100 -8.37400  1.000 14.70049 ? 342 GLY A N     1 
ATOM   2424 C CA    . GLY A 1 348 ? -13.90600 22.97600 -7.74600  1.000 15.45889 ? 342 GLY A CA    1 
ATOM   2425 C C     . GLY A 1 348 ? -12.85000 24.04400 -7.93800  1.000 15.32318 ? 342 GLY A C     1 
ATOM   2426 O O     . GLY A 1 348 ? -12.90800 24.84400 -8.89200  1.000 16.56172 ? 342 GLY A O     1 
ATOM   2427 N N     . ARG A 1 349 ? -11.86400 24.09100 -7.03700  1.000 13.18090 ? 343 ARG A N     1 
ATOM   2428 C CA    . ARG A 1 349 ? -10.95400 25.23200 -6.99500  1.000 13.95185 ? 343 ARG A CA    1 
ATOM   2429 C C     . ARG A 1 349 ? -10.21200 25.43600 -8.31500  1.000 14.47061 ? 343 ARG A C     1 
ATOM   2430 O O     . ARG A 1 349 ? -10.01500 26.57900 -8.74700  1.000 15.09451 ? 343 ARG A O     1 
ATOM   2431 C CB    . ARG A 1 349 ? -9.98100  25.06600 -5.83700  1.000 15.75908 ? 343 ARG A CB    1 
ATOM   2432 C CG    . ARG A 1 349 ? -10.68000 25.24300 -4.50000  1.000 16.22459 ? 343 ARG A CG    1 
ATOM   2433 C CD    . ARG A 1 349 ? -9.82600  24.77500 -3.33300  1.000 18.94951 ? 343 ARG A CD    1 
ATOM   2434 N NE    . ARG A 1 349 ? -9.62700  23.33400 -3.39900  1.000 20.06606 ? 343 ARG A NE    1 
ATOM   2435 C CZ    . ARG A 1 349 ? -8.68600  22.68200 -2.73500  1.000 22.57810 ? 343 ARG A CZ    1 
ATOM   2436 N NH1   . ARG A 1 349 ? -7.86700  23.31000 -1.90700  1.000 24.17050 ? 343 ARG A NH1   1 
ATOM   2437 N NH2   . ARG A 1 349 ? -8.56400  21.37000 -2.90400  1.000 24.33159 ? 343 ARG A NH2   1 
ATOM   2438 N N     . LEU A 1 350 ? -9.80100  24.35500 -8.98600  1.000 14.71442 ? 344 LEU A N     1 
ATOM   2439 C CA    . LEU A 1 350 ? -9.09900  24.55200 -10.25200 1.000 15.99949 ? 344 LEU A CA    1 
ATOM   2440 C C     . LEU A 1 350 ? -9.99400  25.20400 -11.30000 1.000 15.23959 ? 344 LEU A C     1 
ATOM   2441 O O     . LEU A 1 350 ? -9.49400  25.89100 -12.19500 1.000 15.78638 ? 344 LEU A O     1 
ATOM   2442 C CB    . LEU A 1 350 ? -8.53600  23.23100 -10.78100 1.000 15.93994 ? 344 LEU A CB    1 
ATOM   2443 C CG    . LEU A 1 350 ? -7.23900  22.76200 -10.11100 1.000 16.43132 ? 344 LEU A CG    1 
ATOM   2444 C CD1   . LEU A 1 350 ? -6.89000  21.33800 -10.52700 1.000 18.73430 ? 344 LEU A CD1   1 
ATOM   2445 C CD2   . LEU A 1 350 ? -6.09300  23.72900 -10.42500 1.000 15.33121 ? 344 LEU A CD2   1 
ATOM   2446 N N     . PHE A 1 351 ? -11.31900 25.01600 -11.20300 1.000 14.35296 ? 345 PHE A N     1 
ATOM   2447 C CA    . PHE A 1 351 ? -12.23500 25.69200 -12.11600 1.000 15.21133 ? 345 PHE A CA    1 
ATOM   2448 C C     . PHE A 1 351 ? -12.42100 27.16500 -11.75700 1.000 15.56246 ? 345 PHE A C     1 
ATOM   2449 O O     . PHE A 1 351 ? -12.77400 27.97000 -12.62800 1.000 15.92066 ? 345 PHE A O     1 
ATOM   2450 C CB    . PHE A 1 351 ? -13.59200 24.96900 -12.11400 1.000 14.69140 ? 345 PHE A CB    1 
ATOM   2451 C CG    . PHE A 1 351 ? -14.01200 24.41400 -13.46400 1.000 14.40372 ? 345 PHE A CG    1 
ATOM   2452 C CD1   . PHE A 1 351 ? -13.94300 25.20100 -14.61800 1.000 14.55980 ? 345 PHE A CD1   1 
ATOM   2453 C CD2   . PHE A 1 351 ? -14.49900 23.10300 -13.57600 1.000 15.42568 ? 345 PHE A CD2   1 
ATOM   2454 C CE1   . PHE A 1 351 ? -14.34300 24.69800 -15.84000 1.000 16.03646 ? 345 PHE A CE1   1 
ATOM   2455 C CE2   . PHE A 1 351 ? -14.90900 22.58900 -14.82700 1.000 14.33711 ? 345 PHE A CE2   1 
ATOM   2456 C CZ    . PHE A 1 351 ? -14.83100 23.39500 -15.94800 1.000 15.56229 ? 345 PHE A CZ    1 
ATOM   2457 N N     . ILE A 1 352 ? -12.19300 27.53800 -10.49500 1.000 15.05408 ? 346 ILE A N     1 
ATOM   2458 C CA    . ILE A 1 352 ? -12.23400 28.95100 -10.13200 1.000 14.77936 ? 346 ILE A CA    1 
ATOM   2459 C C     . ILE A 1 352 ? -11.19800 29.72900 -10.93400 1.000 14.76335 ? 346 ILE A C     1 
ATOM   2460 O O     . ILE A 1 352 ? -11.49600 30.77900 -11.51600 1.000 14.79276 ? 346 ILE A O     1 
ATOM   2461 C CB    . ILE A 1 352 ? -12.02000 29.12400 -8.61800  1.000 15.15518 ? 346 ILE A CB    1 
ATOM   2462 C CG1   . ILE A 1 352 ? -13.23600 28.58200 -7.86900  1.000 15.60476 ? 346 ILE A CG1   1 
ATOM   2463 C CG2   . ILE A 1 352 ? -11.69000 30.58100 -8.28600  1.000 14.62710 ? 346 ILE A CG2   1 
ATOM   2464 C CD1   . ILE A 1 352 ? -13.15600 28.75600 -6.35800  1.000 17.88171 ? 346 ILE A CD1   1 
ATOM   2465 N N     . SER A 1 353 ? -9.96800  29.21400 -10.99400 1.000 14.47536 ? 347 SER A N     1 
ATOM   2466 C CA    . SER A 1 353 ? -8.86200  29.97500 -11.55100 1.000 14.51251 ? 347 SER A CA    1 
ATOM   2467 C C     . SER A 1 353 ? -8.53100  29.59800 -12.98500 1.000 14.70517 ? 347 SER A C     1 
ATOM   2468 O O     . SER A 1 353 ? -7.66100  30.22900 -13.58800 1.000 15.67092 ? 347 SER A O     1 
ATOM   2469 C CB    . SER A 1 353 ? -7.61700  29.80600 -10.68400 1.000 14.76906 ? 347 SER A CB    1 
ATOM   2470 O OG    . SER A 1 353 ? -7.28500  28.42900 -10.52900 1.000 15.52312 ? 347 SER A OG    1 
ATOM   2471 N N     . ASN A 1 354 ? -9.20200  28.59800 -13.55200 1.000 14.22748 ? 348 ASN A N     1 
ATOM   2472 C CA    . ASN A 1 354 ? -8.97700  28.19500 -14.93800 1.000 14.15219 ? 348 ASN A CA    1 
ATOM   2473 C C     . ASN A 1 354 ? -10.33500 28.12200 -15.60300 1.000 15.19155 ? 348 ASN A C     1 
ATOM   2474 O O     . ASN A 1 354 ? -10.95700 27.05200 -15.63900 1.000 15.01643 ? 348 ASN A O     1 
ATOM   2475 C CB    . ASN A 1 354 ? -8.25000  26.85700 -15.03300 1.000 15.15246 ? 348 ASN A CB    1 
ATOM   2476 C CG    . ASN A 1 354 ? -6.87800  26.89100 -14.37900 1.000 16.21627 ? 348 ASN A CG    1 
ATOM   2477 O OD1   . ASN A 1 354 ? -5.87700  27.19600 -15.04700 1.000 15.82954 ? 348 ASN A OD1   1 
ATOM   2478 N ND2   . ASN A 1 354 ? -6.81800  26.57200 -13.07300 1.000 14.73110 ? 348 ASN A ND2   1 
ATOM   2479 N N     . PRO A 1 355 ? -10.81900 29.23400 -16.15300 1.000 15.67908 ? 349 PRO A N     1 
ATOM   2480 C CA    . PRO A 1 355 ? -12.11700 29.18300 -16.84100 1.000 15.06249 ? 349 PRO A CA    1 
ATOM   2481 C C     . PRO A 1 355 ? -12.13700 28.11000 -17.90900 1.000 15.23807 ? 349 PRO A C     1 
ATOM   2482 O O     . PRO A 1 355 ? -13.16000 27.43400 -18.09900 1.000 14.67212 ? 349 PRO A O     1 
ATOM   2483 C CB    . PRO A 1 355 ? -12.26700 30.57800 -17.45800 1.000 17.94043 ? 349 PRO A CB    1 
ATOM   2484 C CG    . PRO A 1 355 ? -11.03400 31.33900 -17.10100 1.000 20.16217 ? 349 PRO A CG    1 
ATOM   2485 C CD    . PRO A 1 355 ? -10.07000 30.47700 -16.40600 1.000 17.07189 ? 349 PRO A CD    1 
ATOM   2486 N N     . ASP A 1 356 ? -11.01900 27.93300 -18.61200 1.000 15.34019 ? 350 ASP A N     1 
ATOM   2487 C CA    . ASP A 1 356 ? -10.89000 26.91900 -19.66000 1.000 15.84214 ? 350 ASP A CA    1 
ATOM   2488 C C     . ASP A 1 356 ? -10.22900 25.65000 -19.13100 1.000 15.70843 ? 350 ASP A C     1 
ATOM   2489 O O     . ASP A 1 356 ? -9.39400  25.04500 -19.81000 1.000 16.40735 ? 350 ASP A O     1 
ATOM   2490 C CB    . ASP A 1 356 ? -10.12300 27.47300 -20.86700 1.000 17.72690 ? 350 ASP A CB    1 
ATOM   2491 C CG    . ASP A 1 356 ? -8.80800  28.16000 -20.49600 1.000 19.59875 ? 350 ASP A CG    1 
ATOM   2492 O OD1   . ASP A 1 356 ? -8.49700  28.34400 -19.30100 1.000 20.50684 ? 350 ASP A OD1   1 
ATOM   2493 O OD2   . ASP A 1 356 ? -8.07800  28.51600 -21.43900 1.000 21.32575 ? 350 ASP A OD2   1 
ATOM   2494 N N     . LEU A 1 357 ? -10.61600 25.22400 -17.92400 1.000 14.95734 ? 351 LEU A N     1 
ATOM   2495 C CA    . LEU A 1 357 ? -10.03200 24.02800 -17.32600 1.000 15.32395 ? 351 LEU A CA    1 
ATOM   2496 C C     . LEU A 1 357 ? -10.16700 22.81700 -18.24200 1.000 14.70133 ? 351 LEU A C     1 
ATOM   2497 O O     . LEU A 1 357 ? -9.24700  22.00500 -18.35300 1.000 15.82597 ? 351 LEU A O     1 
ATOM   2498 C CB    . LEU A 1 357 ? -10.68800 23.73500 -15.98400 1.000 14.66416 ? 351 LEU A CB    1 
ATOM   2499 C CG    . LEU A 1 357 ? -10.09900 22.50600 -15.27800 1.000 15.45805 ? 351 LEU A CG    1 
ATOM   2500 C CD1   . LEU A 1 357 ? -8.59800  22.66800 -14.95300 1.000 16.00145 ? 351 LEU A CD1   1 
ATOM   2501 C CD2   . LEU A 1 357 ? -10.90600 22.22000 -14.02000 1.000 15.21147 ? 351 LEU A CD2   1 
ATOM   2502 N N     . VAL A 1 358 ? -11.31000 22.67000 -18.89800 1.000 14.35063 ? 352 VAL A N     1 
ATOM   2503 C CA    . VAL A 1 358 ? -11.50200 21.50300 -19.75800 1.000 14.33469 ? 352 VAL A CA    1 
ATOM   2504 C C     . VAL A 1 358 ? -10.45200 21.48300 -20.86200 1.000 16.65782 ? 352 VAL A C     1 
ATOM   2505 O O     . VAL A 1 358 ? -9.81400  20.45600 -21.11400 1.000 17.31855 ? 352 VAL A O     1 
ATOM   2506 C CB    . VAL A 1 358 ? -12.92300 21.48100 -20.34500 1.000 15.58045 ? 352 VAL A CB    1 
ATOM   2507 C CG1   . VAL A 1 358 ? -13.09000 20.23300 -21.19400 1.000 17.81201 ? 352 VAL A CG1   1 
ATOM   2508 C CG2   . VAL A 1 358 ? -13.97000 21.48800 -19.24500 1.000 15.33899 ? 352 VAL A CG2   1 
ATOM   2509 N N     . MET A 1 359 ? -10.27100 22.62000 -21.55000 1.000 17.27082 ? 353 MET A N     1 
ATOM   2510 C CA    . MET A 1 359 ? -9.26700  22.70700 -22.60800 1.000 18.37154 ? 353 MET A CA    1 
ATOM   2511 C C     . MET A 1 359 ? -7.85700  22.50200 -22.07000 1.000 17.48772 ? 353 MET A C     1 
ATOM   2512 O O     . MET A 1 359 ? -7.02700  21.86300 -22.72500 1.000 17.85634 ? 353 MET A O     1 
ATOM   2513 C CB    . MET A 1 359 ? -9.37500  24.05500 -23.31900 1.000 23.82315 ? 353 MET A CB    1 
ATOM   2514 C CG    . MET A 1 359 ? -8.45700  24.21600 -24.52900 1.000 29.92197 ? 353 MET A CG    1 
ATOM   2515 S SD    . MET A 1 359 ? -8.79400  23.06400 -25.89300 1.000 35.57114 ? 353 MET A SD    1 
ATOM   2516 C CE    . MET A 1 359 ? -10.59500 23.01400 -25.85700 1.000 36.01367 ? 353 MET A CE    1 
ATOM   2517 N N     . ARG A 1 360 ? -7.56000  23.04600 -20.89100 1.000 17.18376 ? 354 ARG A N     1 
ATOM   2518 C CA    . ARG A 1 360 ? -6.22700  22.85300 -20.32200 1.000 18.09424 ? 354 ARG A CA    1 
ATOM   2519 C C     . ARG A 1 360 ? -5.97100  21.38200 -20.01500 1.000 18.84957 ? 354 ARG A C     1 
ATOM   2520 O O     . ARG A 1 360 ? -4.88200  20.86000 -20.28400 1.000 19.09446 ? 354 ARG A O     1 
ATOM   2521 C CB    . ARG A 1 360 ? -6.06100  23.71200 -19.07100 1.000 16.88493 ? 354 ARG A CB    1 
ATOM   2522 C CG    . ARG A 1 360 ? -6.00800  25.19800 -19.37900 1.000 17.85495 ? 354 ARG A CG    1 
ATOM   2523 C CD    . ARG A 1 360 ? -5.72800  25.99200 -18.14400 1.000 19.29367 ? 354 ARG A CD    1 
ATOM   2524 N NE    . ARG A 1 360 ? -5.94400  27.41300 -18.36000 1.000 19.04219 ? 354 ARG A NE    1 
ATOM   2525 C CZ    . ARG A 1 360 ? -5.02900  28.35200 -18.15900 1.000 20.92730 ? 354 ARG A CZ    1 
ATOM   2526 N NH1   . ARG A 1 360 ? -3.79300  28.05100 -17.79000 1.000 21.00372 ? 354 ARG A NH1   1 
ATOM   2527 N NH2   . ARG A 1 360 ? -5.36700  29.62700 -18.31300 1.000 22.51824 ? 354 ARG A NH2   1 
ATOM   2528 N N     . ILE A 1 361 ? -6.97200  20.68900 -19.47800 1.000 18.77455 ? 355 ILE A N     1 
ATOM   2529 C CA    . ILE A 1 361 ? -6.81700  19.26500 -19.20900 1.000 18.84040 ? 355 ILE A CA    1 
ATOM   2530 C C     . ILE A 1 361 ? -6.64500  18.49400 -20.51800 1.000 19.38635 ? 355 ILE A C     1 
ATOM   2531 O O     . ILE A 1 361 ? -5.80500  17.58800 -20.62000 1.000 20.61400 ? 355 ILE A O     1 
ATOM   2532 C CB    . ILE A 1 361 ? -8.01800  18.77200 -18.37700 1.000 18.82695 ? 355 ILE A CB    1 
ATOM   2533 C CG1   . ILE A 1 361 ? -7.93500  19.36200 -16.95800 1.000 20.20216 ? 355 ILE A CG1   1 
ATOM   2534 C CG2   . ILE A 1 361 ? -8.09100  17.24500 -18.35700 1.000 20.39141 ? 355 ILE A CG2   1 
ATOM   2535 C CD1   . ILE A 1 361 ? -9.02900  18.89300 -15.99200 1.000 19.23765 ? 355 ILE A CD1   1 
ATOM   2536 N N     . LYS A 1 362 ? -7.39300  18.87600 -21.55400 1.000 18.22475 ? 356 LYS A N     1 
ATOM   2537 C CA    . LYS A 1 362 ? -7.25300  18.22600 -22.85600 1.000 20.68601 ? 356 LYS A CA    1 
ATOM   2538 C C     . LYS A 1 362 ? -5.84000  18.37400 -23.40700 1.000 21.55159 ? 356 LYS A C     1 
ATOM   2539 O O     . LYS A 1 362 ? -5.25400  17.41000 -23.91600 1.000 23.25748 ? 356 LYS A O     1 
ATOM   2540 C CB    . LYS A 1 362 ? -8.26400  18.81000 -23.84200 1.000 22.63687 ? 356 LYS A CB    1 
ATOM   2541 C CG    . LYS A 1 362 ? -8.76100  17.83000 -24.90700 1.000 28.27459 ? 356 LYS A CG    1 
ATOM   2542 C CD    . LYS A 1 362 ? -9.99800  18.38900 -25.62500 1.000 31.84300 ? 356 LYS A CD    1 
ATOM   2543 C CE    . LYS A 1 362 ? -10.26300 17.65600 -26.93500 1.000 35.02691 ? 356 LYS A CE    1 
ATOM   2544 N NZ    . LYS A 1 362 ? -9.05700  16.89300 -27.37500 1.000 36.86811 ? 356 LYS A NZ    1 
ATOM   2545 N N     . LEU A 1 363 ? -5.28700  19.57900 -23.34100 1.000 22.90506 ? 357 LEU A N     1 
ATOM   2546 C CA    . LEU A 1 363 ? -3.98300  19.86900 -23.92700 1.000 22.05823 ? 357 LEU A CA    1 
ATOM   2547 C C     . LEU A 1 363 ? -2.82900  19.55300 -22.99000 1.000 21.49199 ? 357 LEU A C     1 
ATOM   2548 O O     . LEU A 1 363 ? -1.66900  19.67100 -23.40100 1.000 21.84116 ? 357 LEU A O     1 
ATOM   2549 C CB    . LEU A 1 363 ? -3.89600  21.34500 -24.32900 1.000 21.39861 ? 357 LEU A CB    1 
ATOM   2550 C CG    . LEU A 1 363 ? -4.94000  21.89200 -25.29700 1.000 23.71609 ? 357 LEU A CG    1 
ATOM   2551 C CD1   . LEU A 1 363 ? -4.79200  23.39900 -25.44800 1.000 24.04097 ? 357 LEU A CD1   1 
ATOM   2552 C CD2   . LEU A 1 363 ? -4.76900  21.20700 -26.63300 1.000 24.36638 ? 357 LEU A CD2   1 
ATOM   2553 N N     . ASN A 1 364 ? -3.12400  19.14900 -21.75500 1.000 20.79342 ? 358 ASN A N     1 
ATOM   2554 C CA    . ASN A 1 364 ? -2.14600  19.07000 -20.66800 1.000 21.05826 ? 358 ASN A CA    1 
ATOM   2555 C C     . ASN A 1 364 ? -1.35000  20.37300 -20.55000 1.000 20.81408 ? 358 ASN A C     1 
ATOM   2556 O O     . ASN A 1 364 ? -0.11900  20.38700 -20.43100 1.000 22.30050 ? 358 ASN A O     1 
ATOM   2557 C CB    . ASN A 1 364 ? -1.22700  17.86100 -20.83000 1.000 22.76519 ? 358 ASN A CB    1 
ATOM   2558 C CG    . ASN A 1 364 ? -0.50700  17.52100 -19.54900 1.000 25.81835 ? 358 ASN A CG    1 
ATOM   2559 O OD1   . ASN A 1 364 ? -0.90000  17.96900 -18.47000 1.000 25.36577 ? 358 ASN A OD1   1 
ATOM   2560 N ND2   . ASN A 1 364 ? 0.56000   16.73800 -19.65500 1.000 28.84974 ? 358 ASN A ND2   1 
ATOM   2561 N N     . ALA A 1 365 ? -2.07600  21.47800 -20.58500 1.000 18.85651 ? 359 ALA A N     1 
ATOM   2562 C CA    . ALA A 1 365 ? -1.50900  22.80200 -20.41900 1.000 19.49447 ? 359 ALA A CA    1 
ATOM   2563 C C     . ALA A 1 365 ? -1.38600  23.12000 -18.93300 1.000 21.15921 ? 359 ALA A C     1 
ATOM   2564 O O     . ALA A 1 365 ? -2.20200  22.66800 -18.12900 1.000 22.18870 ? 359 ALA A O     1 
ATOM   2565 C CB    . ALA A 1 365 ? -2.39100  23.84600 -21.09900 1.000 20.74146 ? 359 ALA A CB    1 
ATOM   2566 N N     . PRO A 1 366 ? -0.38500  23.90100 -18.53900 1.000 22.01564 ? 360 PRO A N     1 
ATOM   2567 C CA    . PRO A 1 366 ? -0.24400  24.23800 -17.11300 1.000 21.59173 ? 360 PRO A CA    1 
ATOM   2568 C C     . PRO A 1 366 ? -1.46900  24.97100 -16.58700 1.000 20.46043 ? 360 PRO A C     1 
ATOM   2569 O O     . PRO A 1 366 ? -2.08000  25.78500 -17.28100 1.000 22.05339 ? 360 PRO A O     1 
ATOM   2570 C CB    . PRO A 1 366 ? 1.00000   25.12800 -17.06200 1.000 23.46113 ? 360 PRO A CB    1 
ATOM   2571 C CG    . PRO A 1 366 ? 1.48100   25.26800 -18.46200 1.000 26.46289 ? 360 PRO A CG    1 
ATOM   2572 C CD    . PRO A 1 366 ? 0.72900   24.38800 -19.36900 1.000 24.37525 ? 360 PRO A CD    1 
ATOM   2573 N N     . LEU A 1 367 ? -1.81600  24.67200 -15.34700 1.000 18.53515 ? 361 LEU A N     1 
ATOM   2574 C CA    . LEU A 1 367 ? -2.96800  25.27600 -14.69000 1.000 15.83690 ? 361 LEU A CA    1 
ATOM   2575 C C     . LEU A 1 367 ? -2.53300  26.47900 -13.86800 1.000 16.21513 ? 361 LEU A C     1 
ATOM   2576 O O     . LEU A 1 367 ? -1.40400  26.54100 -13.36500 1.000 15.79079 ? 361 LEU A O     1 
ATOM   2577 C CB    . LEU A 1 367 ? -3.66300  24.26200 -13.78400 1.000 15.57024 ? 361 LEU A CB    1 
ATOM   2578 C CG    . LEU A 1 367 ? -4.05200  22.95700 -14.48600 1.000 16.46815 ? 361 LEU A CG    1 
ATOM   2579 C CD1   . LEU A 1 367 ? -4.84400  22.09200 -13.53200 1.000 18.76000 ? 361 LEU A CD1   1 
ATOM   2580 C CD2   . LEU A 1 367 ? -4.87700  23.24300 -15.74200 1.000 16.16924 ? 361 LEU A CD2   1 
ATOM   2581 N N     . ASN A 1 368 ? -3.44500  27.43100 -13.71700 1.000 15.46355 ? 362 ASN A N     1 
ATOM   2582 C CA    . ASN A 1 368 ? -3.15300  28.65000 -12.97900 1.000 17.06350 ? 362 ASN A CA    1 
ATOM   2583 C C     . ASN A 1 368 ? -3.65300  28.55600 -11.54100 1.000 15.99790 ? 362 ASN A C     1 
ATOM   2584 O O     . ASN A 1 368 ? -4.67000  27.91600 -11.25300 1.000 15.30687 ? 362 ASN A O     1 
ATOM   2585 C CB    . ASN A 1 368 ? -3.77000  29.86100 -13.67300 1.000 17.65142 ? 362 ASN A CB    1 
ATOM   2586 C CG    . ASN A 1 368 ? -3.02100  30.24600 -14.95000 1.000 21.12140 ? 362 ASN A CG    1 
ATOM   2587 O OD1   . ASN A 1 368 ? -1.87100  29.84100 -15.16400 1.000 23.74084 ? 362 ASN A OD1   1 
ATOM   2588 N ND2   . ASN A 1 368 ? -3.66900  31.02900 -15.80000 1.000 22.68746 ? 362 ASN A ND2   1 
ATOM   2589 N N     . LYS A 1 369 ? -2.90800  29.18800 -10.63400 1.000 15.36849 ? 363 LYS A N     1 
ATOM   2590 C CA    . LYS A 1 369 ? -3.24200  29.13200 -9.21700  1.000 16.40888 ? 363 LYS A CA    1 
ATOM   2591 C C     . LYS A 1 369 ? -4.52300  29.91500 -8.91900  1.000 16.84810 ? 363 LYS A C     1 
ATOM   2592 O O     . LYS A 1 369 ? -4.89600  30.84900 -9.63800  1.000 17.23814 ? 363 LYS A O     1 
ATOM   2593 C CB    . LYS A 1 369 ? -2.09600  29.68300 -8.37100  1.000 17.75727 ? 363 LYS A CB    1 
ATOM   2594 C CG    . LYS A 1 369 ? -1.79600  31.13800 -8.60400  1.000 20.85229 ? 363 LYS A CG    1 
ATOM   2595 C CD    . LYS A 1 369 ? -0.52600  31.53800 -7.86200  1.000 26.62893 ? 363 LYS A CD    1 
ATOM   2596 C CE    . LYS A 1 369 ? -0.32700  33.04000 -7.88700  1.000 32.67919 ? 363 LYS A CE    1 
ATOM   2597 N NZ    . LYS A 1 369 ? 1.02700   33.39300 -8.38900  1.000 36.76039 ? 363 LYS A NZ    1 
ATOM   2598 N N     . TYR A 1 370 ? -5.18600  29.53700 -7.82200  1.000 16.96997 ? 364 TYR A N     1 
ATOM   2599 C CA    . TYR A 1 370 ? -6.38700  30.22000 -7.35200  1.000 17.48554 ? 364 TYR A CA    1 
ATOM   2600 C C     . TYR A 1 370 ? -6.08200  31.03600 -6.10200  1.000 18.57350 ? 364 TYR A C     1 
ATOM   2601 O O     . TYR A 1 370 ? -5.16800  30.70900 -5.33700  1.000 20.19167 ? 364 TYR A O     1 
ATOM   2602 C CB    . TYR A 1 370 ? -7.52700  29.23100 -7.04900  1.000 18.81395 ? 364 TYR A CB    1 
ATOM   2603 C CG    . TYR A 1 370 ? -7.10600  27.92900 -6.38900  1.000 20.32644 ? 364 TYR A CG    1 
ATOM   2604 C CD1   . TYR A 1 370 ? -6.90300  27.84600 -5.01000  1.000 21.59515 ? 364 TYR A CD1   1 
ATOM   2605 C CD2   . TYR A 1 370 ? -6.93900  26.77600 -7.14500  1.000 21.36529 ? 364 TYR A CD2   1 
ATOM   2606 C CE1   . TYR A 1 370 ? -6.53000  26.64700 -4.41500  1.000 22.93330 ? 364 TYR A CE1   1 
ATOM   2607 C CE2   . TYR A 1 370 ? -6.56800  25.57900 -6.56300  1.000 22.63162 ? 364 TYR A CE2   1 
ATOM   2608 C CZ    . TYR A 1 370 ? -6.36900  25.51200 -5.20200  1.000 24.37572 ? 364 TYR A CZ    1 
ATOM   2609 O OH    . TYR A 1 370 ? -5.99900  24.29900 -4.64100  1.000 26.41520 ? 364 TYR A OH    1 
ATOM   2610 N N     . ASN A 1 371 ? -6.85200  32.11000 -5.94000  1.000 18.77971 ? 365 ASN A N     1 
ATOM   2611 C CA    A ASN A 1 371 ? -6.73300  33.02600 -4.76800  0.500 18.79102 ? 365 ASN A CA    1 
ATOM   2612 C CA    B ASN A 1 371 ? -6.71600  33.00600 -4.75400  0.500 19.58800 ? 365 ASN A CA    1 
ATOM   2613 C C     . ASN A 1 371 ? -7.92700  32.97000 -3.76800  1.000 17.91953 ? 365 ASN A C     1 
ATOM   2614 O O     . ASN A 1 371 ? -9.09400  33.53300 -3.93200  1.000 19.01247 ? 365 ASN A O     1 
ATOM   2615 C CB    A ASN A 1 371 ? -6.59200  34.46500 -5.24100  0.500 19.82612 ? 365 ASN A CB    1 
ATOM   2616 C CB    B ASN A 1 371 ? -6.50200  34.44000 -5.22100  0.500 21.81508 ? 365 ASN A CB    1 
ATOM   2617 C CG    A ASN A 1 371 ? -6.35800  35.43300 -4.07600  0.500 23.24619 ? 365 ASN A CG    1 
ATOM   2618 C CG    B ASN A 1 371 ? -5.42600  34.53300 -6.28300  0.500 25.02475 ? 365 ASN A CG    1 
ATOM   2619 O OD1   A ASN A 1 371 ? -5.93000  35.02100 -2.98000  0.500 24.60609 ? 365 ASN A OD1   1 
ATOM   2620 O OD1   B ASN A 1 371 ? -4.29900  34.09000 -6.07000  0.500 26.40965 ? 365 ASN A OD1   1 
ATOM   2621 N ND2   A ASN A 1 371 ? -6.63200  36.72800 -4.30600  0.500 25.44304 ? 365 ASN A ND2   1 
ATOM   2622 N ND2   B ASN A 1 371 ? -5.76500  35.09000 -7.43400  0.500 27.07605 ? 365 ASN A ND2   1 
ATOM   2623 N N     . ALA A 1 372 ? -7.71800  32.19700 -2.71800  1.000 17.99931 ? 366 ALA A N     1 
ATOM   2624 C CA    . ALA A 1 372 ? -8.79800  31.96300 -1.76800  1.000 17.61956 ? 366 ALA A CA    1 
ATOM   2625 C C     . ALA A 1 372 ? -9.35900  33.25200 -1.17100  1.000 17.42180 ? 366 ALA A C     1 
ATOM   2626 O O     . ALA A 1 372 ? -10.51900 33.26300 -0.74200  1.000 16.79427 ? 366 ALA A O     1 
ATOM   2627 C CB    . ALA A 1 372 ? -8.31500  31.02000 -0.66600  1.000 19.71034 ? 366 ALA A CB    1 
ATOM   2628 N N     . LYS A 1 373 ? -8.58900  34.34600 -1.15300  1.000 16.79729 ? 367 LYS A N     1 
ATOM   2629 C CA    . LYS A 1 373 ? -9.12600  35.57600 -0.57200  1.000 16.49463 ? 367 LYS A CA    1 
ATOM   2630 C C     . LYS A 1 373 ? -10.34400 36.08700 -1.33400  1.000 16.04111 ? 367 LYS A C     1 
ATOM   2631 O O     . LYS A 1 373 ? -11.18100 36.78800 -0.74900  1.000 17.54616 ? 367 LYS A O     1 
ATOM   2632 C CB    . LYS A 1 373 ? -8.04400  36.65800 -0.51500  1.000 18.29288 ? 367 LYS A CB    1 
ATOM   2633 C CG    . LYS A 1 373 ? -7.00300  36.41200 0.57400   1.000 22.16479 ? 367 LYS A CG    1 
ATOM   2634 C CD    . LYS A 1 373 ? -6.06300  37.59500 0.70200   1.000 26.19413 ? 367 LYS A CD    1 
ATOM   2635 C CE    . LYS A 1 373 ? -5.12300  37.41900 1.87800   1.000 29.63340 ? 367 LYS A CE    1 
ATOM   2636 N NZ    . LYS A 1 373 ? -4.22700  38.58400 2.00800   1.000 31.92413 ? 367 LYS A NZ    1 
ATOM   2637 N N     . THR A 1 374 ? -10.48400 35.74300 -2.61500  1.000 15.40723 ? 368 THR A N     1 
ATOM   2638 C CA    . THR A 1 374 ? -11.61600 36.23000 -3.39400  1.000 15.90243 ? 368 THR A CA    1 
ATOM   2639 C C     . THR A 1 374 ? -12.61000 35.11900 -3.72200  1.000 16.52568 ? 368 THR A C     1 
ATOM   2640 O O     . THR A 1 374 ? -13.44100 35.27700 -4.62700  1.000 17.80562 ? 368 THR A O     1 
ATOM   2641 C CB    . THR A 1 374 ? -11.13800 36.94500 -4.66600  1.000 16.84280 ? 368 THR A CB    1 
ATOM   2642 O OG1   . THR A 1 374 ? -10.20700 36.13100 -5.40000  1.000 17.26388 ? 368 THR A OG1   1 
ATOM   2643 C CG2   . THR A 1 374 ? -10.43400 38.26100 -4.29200  1.000 18.38618 ? 368 THR A CG2   1 
ATOM   2644 N N     . PHE A 1 375 ? -12.56400 34.00900 -2.98000  1.000 15.74883 ? 369 PHE A N     1 
ATOM   2645 C CA    . PHE A 1 375 ? -13.57500 32.97500 -3.16700  1.000 13.98001 ? 369 PHE A CA    1 
ATOM   2646 C C     . PHE A 1 375 ? -14.97200 33.51200 -2.86300  1.000 13.90420 ? 369 PHE A C     1 
ATOM   2647 O O     . PHE A 1 375 ? -15.92600 33.18100 -3.57300  1.000 12.95263 ? 369 PHE A O     1 
ATOM   2648 C CB    . PHE A 1 375 ? -13.30000 31.76300 -2.27000  1.000 14.90243 ? 369 PHE A CB    1 
ATOM   2649 C CG    . PHE A 1 375 ? -12.20300 30.85700 -2.74600  1.000 16.42585 ? 369 PHE A CG    1 
ATOM   2650 C CD1   . PHE A 1 375 ? -11.51300 31.10700 -3.92600  1.000 17.02014 ? 369 PHE A CD1   1 
ATOM   2651 C CD2   . PHE A 1 375 ? -11.86700 29.73800 -1.99600  1.000 16.88929 ? 369 PHE A CD2   1 
ATOM   2652 C CE1   . PHE A 1 375 ? -10.48700 30.25500 -4.34100  1.000 16.87249 ? 369 PHE A CE1   1 
ATOM   2653 C CE2   . PHE A 1 375 ? -10.84900 28.87600 -2.40500  1.000 17.11512 ? 369 PHE A CE2   1 
ATOM   2654 C CZ    . PHE A 1 375 ? -10.16700 29.13200 -3.58400  1.000 18.69281 ? 369 PHE A CZ    1 
ATOM   2655 N N     . TYR A 1 376 ? -15.12300 34.29900 -1.77700  1.000 14.24107 ? 370 TYR A N     1 
ATOM   2656 C CA    . TYR A 1 376 ? -16.44400 34.67200 -1.26200  1.000 13.62203 ? 370 TYR A CA    1 
ATOM   2657 C C     . TYR A 1 376 ? -16.69700 36.17800 -1.21500  1.000 16.31767 ? 370 TYR A C     1 
ATOM   2658 O O     . TYR A 1 376 ? -17.61300 36.62400 -0.50900  1.000 17.05383 ? 370 TYR A O     1 
ATOM   2659 C CB    . TYR A 1 376 ? -16.66100 34.10100 0.13400   1.000 15.89988 ? 370 TYR A CB    1 
ATOM   2660 C CG    . TYR A 1 376 ? -16.47200 32.61300 0.25300   1.000 18.44360 ? 370 TYR A CG    1 
ATOM   2661 C CD1   . TYR A 1 376 ? -17.28200 31.72700 -0.44700  1.000 19.09994 ? 370 TYR A CD1   1 
ATOM   2662 C CD2   . TYR A 1 376 ? -15.51900 32.08700 1.12500   1.000 20.37942 ? 370 TYR A CD2   1 
ATOM   2663 C CE1   . TYR A 1 376 ? -17.12400 30.36000 -0.30800  1.000 20.09992 ? 370 TYR A CE1   1 
ATOM   2664 C CE2   . TYR A 1 376 ? -15.35200 30.72500 1.25800   1.000 22.85055 ? 370 TYR A CE2   1 
ATOM   2665 C CZ    . TYR A 1 376 ? -16.15700 29.86900 0.54700   1.000 23.36344 ? 370 TYR A CZ    1 
ATOM   2666 O OH    . TYR A 1 376 ? -15.98900 28.50900 0.70000   1.000 25.69535 ? 370 TYR A OH    1 
ATOM   2667 N N     . THR A 1 377 ? -15.91700 36.97200 -1.93100  1.000 16.02299 ? 371 THR A N     1 
ATOM   2668 C CA    . THR A 1 377 ? -16.12100 38.40900 -1.97200  1.000 17.83302 ? 371 THR A CA    1 
ATOM   2669 C C     . THR A 1 377 ? -17.24900 38.74600 -2.95300  1.000 17.69531 ? 371 THR A C     1 
ATOM   2670 O O     . THR A 1 377 ? -17.78600 37.87300 -3.64200  1.000 17.69791 ? 371 THR A O     1 
ATOM   2671 C CB    . THR A 1 377 ? -14.80700 39.10000 -2.34700  1.000 19.39550 ? 371 THR A CB    1 
ATOM   2672 O OG1   . THR A 1 377 ? -14.21600 38.41100 -3.45600  1.000 20.73574 ? 371 THR A OG1   1 
ATOM   2673 C CG2   . THR A 1 377 ? -13.83100 39.03200 -1.17900  1.000 20.07847 ? 371 THR A CG2   1 
ATOM   2674 N N     . GLN A 1 378 ? -17.64000 40.02300 -2.99300  1.000 17.25712 ? 372 GLN A N     1 
ATOM   2675 C CA    . GLN A 1 378 ? -18.80900 40.42100 -3.77200  1.000 16.75749 ? 372 GLN A CA    1 
ATOM   2676 C C     . GLN A 1 378 ? -18.46000 41.06100 -5.10700  1.000 17.22095 ? 372 GLN A C     1 
ATOM   2677 O O     . GLN A 1 378 ? -19.36800 41.38100 -5.88000  1.000 17.43719 ? 372 GLN A O     1 
ATOM   2678 C CB    . GLN A 1 378 ? -19.69100 41.37400 -2.96100  1.000 16.92260 ? 372 GLN A CB    1 
ATOM   2679 C CG    . GLN A 1 378 ? -20.60700 40.63600 -2.00100  1.000 17.11560 ? 372 GLN A CG    1 
ATOM   2680 C CD    . GLN A 1 378 ? -19.82700 39.84000 -0.98300  1.000 17.45109 ? 372 GLN A CD    1 
ATOM   2681 O OE1   . GLN A 1 378 ? -19.18700 40.41500 -0.08600  1.000 20.60350 ? 372 GLN A OE1   1 
ATOM   2682 N NE2   . GLN A 1 378 ? -19.86900 38.50800 -1.10400  1.000 16.23071 ? 372 GLN A NE2   1 
ATOM   2683 N N     . ASP A 1 379 ? -17.18500 41.26300 -5.39900  1.000 16.72157 ? 373 ASP A N     1 
ATOM   2684 C CA    . ASP A 1 379 ? -16.82600 41.98400 -6.61100  1.000 17.93283 ? 373 ASP A CA    1 
ATOM   2685 C C     . ASP A 1 379 ? -17.26600 41.18200 -7.83400  1.000 17.09372 ? 373 ASP A C     1 
ATOM   2686 O O     . ASP A 1 379 ? -16.99100 39.97600 -7.91000  1.000 16.97835 ? 373 ASP A O     1 
ATOM   2687 C CB    . ASP A 1 379 ? -15.31800 42.23700 -6.65800  1.000 21.10146 ? 373 ASP A CB    1 
ATOM   2688 C CG    . ASP A 1 379 ? -14.94600 43.33900 -7.63100  1.000 24.08349 ? 373 ASP A CG    1 
ATOM   2689 O OD1   . ASP A 1 379 ? -15.02700 43.10300 -8.85100  1.000 22.87548 ? 373 ASP A OD1   1 
ATOM   2690 O OD2   . ASP A 1 379 ? -14.58600 44.44700 -7.17600  1.000 27.33898 ? 373 ASP A OD2   1 
ATOM   2691 N N     . PRO A 1 380 ? -17.95200 41.80100 -8.80000  1.000 18.12840 ? 374 PRO A N     1 
ATOM   2692 C CA    . PRO A 1 380 ? -18.43000 41.04600 -9.97200  1.000 17.48986 ? 374 PRO A CA    1 
ATOM   2693 C C     . PRO A 1 380 ? -17.32500 40.61300 -10.91900 1.000 17.92397 ? 374 PRO A C     1 
ATOM   2694 O O     . PRO A 1 380 ? -17.58100 39.77800 -11.79900 1.000 19.84448 ? 374 PRO A O     1 
ATOM   2695 C CB    . PRO A 1 380 ? -19.39500 42.02400 -10.65600 1.000 17.73332 ? 374 PRO A CB    1 
ATOM   2696 C CG    . PRO A 1 380 ? -18.91600 43.38900 -10.21800 1.000 18.31663 ? 374 PRO A CG    1 
ATOM   2697 C CD    . PRO A 1 380 ? -18.39600 43.20700 -8.81000  1.000 18.23773 ? 374 PRO A CD    1 
ATOM   2698 N N     . VAL A 1 381 ? -16.10900 41.13500 -10.77300 1.000 17.02523 ? 375 VAL A N     1 
ATOM   2699 C CA    . VAL A 1 381 ? -15.00800 40.83700 -11.68200 1.000 19.29530 ? 375 VAL A CA    1 
ATOM   2700 C C     . VAL A 1 381 ? -13.81500 40.23000 -10.94500 1.000 18.41518 ? 375 VAL A C     1 
ATOM   2701 O O     . VAL A 1 381 ? -13.34100 39.14300 -11.29400 1.000 17.56568 ? 375 VAL A O     1 
ATOM   2702 C CB    . VAL A 1 381 ? -14.58000 42.09600 -12.47500 1.000 20.07462 ? 375 VAL A CB    1 
ATOM   2703 C CG1   . VAL A 1 381 ? -13.35400 41.81500 -13.32800 1.000 21.15530 ? 375 VAL A CG1   1 
ATOM   2704 C CG2   . VAL A 1 381 ? -15.71800 42.59100 -13.36500 1.000 19.67284 ? 375 VAL A CG2   1 
ATOM   2705 N N     . VAL A 1 382 ? -13.32900 40.91000 -9.90900  1.000 18.92473 ? 376 VAL A N     1 
ATOM   2706 C CA    . VAL A 1 382 ? -12.04500 40.56000 -9.30400  1.000 19.04498 ? 376 VAL A CA    1 
ATOM   2707 C C     . VAL A 1 382 ? -12.11900 39.18900 -8.63900  1.000 18.09450 ? 376 VAL A C     1 
ATOM   2708 O O     . VAL A 1 382 ? -12.91900 38.96100 -7.72400  1.000 18.60888 ? 376 VAL A O     1 
ATOM   2709 C CB    . VAL A 1 382 ? -11.60500 41.63200 -8.30500  1.000 19.75635 ? 376 VAL A CB    1 
ATOM   2710 C CG1   . VAL A 1 382 ? -10.30100 41.19600 -7.61000  1.000 19.33826 ? 376 VAL A CG1   1 
ATOM   2711 C CG2   . VAL A 1 382 ? -11.39900 42.93300 -9.03200  1.000 21.98816 ? 376 VAL A CG2   1 
ATOM   2712 N N     . GLY A 1 383 ? -11.26400 38.27200 -9.08600  1.000 17.47475 ? 377 GLY A N     1 
ATOM   2713 C CA    . GLY A 1 383 ? -11.24000 36.92700 -8.53900  1.000 16.05783 ? 377 GLY A CA    1 
ATOM   2714 C C     . GLY A 1 383 ? -12.42900 36.08800 -8.93600  1.000 16.00180 ? 377 GLY A C     1 
ATOM   2715 O O     . GLY A 1 383 ? -12.67600 35.04400 -8.32300  1.000 15.51246 ? 377 GLY A O     1 
ATOM   2716 N N     . TYR A 1 384 ? -13.16600 36.50900 -9.96400  1.000 14.59013 ? 378 TYR A N     1 
ATOM   2717 C CA    . TYR A 1 384 ? -14.40200 35.84300 -10.35300 1.000 14.21202 ? 378 TYR A CA    1 
ATOM   2718 C C     . TYR A 1 384 ? -14.37100 35.59300 -11.85400 1.000 14.68698 ? 378 TYR A C     1 
ATOM   2719 O O     . TYR A 1 384 ? -14.40000 34.44000 -12.31400 1.000 15.52619 ? 378 TYR A O     1 
ATOM   2720 C CB    . TYR A 1 384 ? -15.61200 36.69800 -9.94900  1.000 14.66161 ? 378 TYR A CB    1 
ATOM   2721 C CG    . TYR A 1 384 ? -16.94300 35.97700 -9.99200  1.000 15.89806 ? 378 TYR A CG    1 
ATOM   2722 C CD1   . TYR A 1 384 ? -17.12900 34.76500 -9.34600  1.000 15.46601 ? 378 TYR A CD1   1 
ATOM   2723 C CD2   . TYR A 1 384 ? -18.01900 36.51900 -10.68300 1.000 16.37067 ? 378 TYR A CD2   1 
ATOM   2724 C CE1   . TYR A 1 384 ? -18.35500 34.10500 -9.39300  1.000 15.27063 ? 378 TYR A CE1   1 
ATOM   2725 C CE2   . TYR A 1 384 ? -19.23300 35.87100 -10.73500 1.000 17.14649 ? 378 TYR A CE2   1 
ATOM   2726 C CZ    . TYR A 1 384 ? -19.39200 34.66400 -10.09400 1.000 15.99174 ? 378 TYR A CZ    1 
ATOM   2727 O OH    . TYR A 1 384 ? -20.60800 34.02400 -10.14900 1.000 19.13930 ? 378 TYR A OH    1 
ATOM   2728 N N     . THR A 1 385 ? -14.28900 36.66600 -12.63500 1.000 15.62448 ? 379 THR A N     1 
ATOM   2729 C CA    . THR A 1 385 ? -14.25300 36.52300 -14.08000 1.000 16.01998 ? 379 THR A CA    1 
ATOM   2730 C C     . THR A 1 385 ? -12.95700 37.02800 -14.69700 1.000 15.90500 ? 379 THR A C     1 
ATOM   2731 O O     . THR A 1 385 ? -12.82400 36.97900 -15.92800 1.000 17.40228 ? 379 THR A O     1 
ATOM   2732 C CB    . THR A 1 385 ? -15.45400 37.23000 -14.74000 1.000 17.39281 ? 379 THR A CB    1 
ATOM   2733 O OG1   . THR A 1 385 ? -15.43700 38.63700 -14.46500 1.000 18.30332 ? 379 THR A OG1   1 
ATOM   2734 C CG2   . THR A 1 385 ? -16.77500 36.63500 -14.24300 1.000 18.39765 ? 379 THR A CG2   1 
ATOM   2735 N N     . ASP A 1 386 ? -11.98500 37.48400 -13.89800 1.000 15.90711 ? 380 ASP A N     1 
ATOM   2736 C CA    . ASP A 1 386 ? -10.76400 38.02200 -14.48900 1.000 16.34912 ? 380 ASP A CA    1 
ATOM   2737 C C     . ASP A 1 386 ? -9.60400  37.03700 -14.45600 1.000 16.92485 ? 380 ASP A C     1 
ATOM   2738 O O     . ASP A 1 386 ? -8.46200  37.45100 -14.67400 1.000 19.17145 ? 380 ASP A O     1 
ATOM   2739 C CB    . ASP A 1 386 ? -10.29000 39.32700 -13.82800 1.000 19.50568 ? 380 ASP A CB    1 
ATOM   2740 C CG    . ASP A 1 386 ? -10.16200 39.23800 -12.31400 1.000 22.01535 ? 380 ASP A CG    1 
ATOM   2741 O OD1   . ASP A 1 386 ? -10.20900 38.12800 -11.74200 1.000 21.58339 ? 380 ASP A OD1   1 
ATOM   2742 O OD2   . ASP A 1 386 ? -9.84900  40.29200 -11.71200 1.000 23.43055 ? 380 ASP A OD2   1 
ATOM   2743 N N     . TYR A 1 387 ? -9.85100  35.76700 -14.16900 1.000 16.04139 ? 381 TYR A N     1 
ATOM   2744 C CA    . TYR A 1 387 ? -8.80900  34.77400 -14.38200 1.000 16.40636 ? 381 TYR A CA    1 
ATOM   2745 C C     . TYR A 1 387 ? -8.67400  34.51500 -15.88000 1.000 17.90995 ? 381 TYR A C     1 
ATOM   2746 O O     . TYR A 1 387 ? -9.66900  34.21000 -16.54100 1.000 18.89032 ? 381 TYR A O     1 
ATOM   2747 C CB    . TYR A 1 387 ? -9.14300  33.48000 -13.66600 1.000 15.15191 ? 381 TYR A CB    1 
ATOM   2748 C CG    . TYR A 1 387 ? -8.99900  33.47800 -12.15600 1.000 15.23642 ? 381 TYR A CG    1 
ATOM   2749 C CD1   . TYR A 1 387 ? -7.76100  33.29600 -11.54700 1.000 15.33567 ? 381 TYR A CD1   1 
ATOM   2750 C CD2   . TYR A 1 387 ? -10.11300 33.57400 -11.34000 1.000 15.89192 ? 381 TYR A CD2   1 
ATOM   2751 C CE1   . TYR A 1 387 ? -7.64200  33.24400 -10.16200 1.000 15.45483 ? 381 TYR A CE1   1 
ATOM   2752 C CE2   . TYR A 1 387 ? -10.01200 33.51200 -9.95600  1.000 15.65832 ? 381 TYR A CE2   1 
ATOM   2753 C CZ    . TYR A 1 387 ? -8.78100  33.34700 -9.36900  1.000 16.90933 ? 381 TYR A CZ    1 
ATOM   2754 O OH    . TYR A 1 387 ? -8.71100  33.27400 -7.99300  1.000 19.02240 ? 381 TYR A OH    1 
ATOM   2755 N N     . PRO A 1 388 ? -7.47800  34.60900 -16.44600 1.000 19.29681 ? 382 PRO A N     1 
ATOM   2756 C CA    . PRO A 1 388 ? -7.34100  34.57000 -17.90300 1.000 21.11742 ? 382 PRO A CA    1 
ATOM   2757 C C     . PRO A 1 388 ? -7.48800  33.17200 -18.48600 1.000 21.29809 ? 382 PRO A C     1 
ATOM   2758 O O     . PRO A 1 388 ? -7.24800  32.15300 -17.83700 1.000 20.28176 ? 382 PRO A O     1 
ATOM   2759 C CB    . PRO A 1 388 ? -5.92000  35.09400 -18.13400 1.000 21.75005 ? 382 PRO A CB    1 
ATOM   2760 C CG    . PRO A 1 388 ? -5.18900  34.71700 -16.86600 1.000 22.71769 ? 382 PRO A CG    1 
ATOM   2761 C CD    . PRO A 1 388 ? -6.20700  34.91800 -15.77100 1.000 20.68483 ? 382 PRO A CD    1 
ATOM   2762 N N     . PHE A 1 389 ? -7.88400  33.15700 -19.75400 1.000 21.20435 ? 383 PHE A N     1 
ATOM   2763 C CA    . PHE A 1 389 ? -7.82400  31.97300 -20.58500 1.000 21.91097 ? 383 PHE A CA    1 
ATOM   2764 C C     . PHE A 1 389 ? -6.38300  31.71600 -21.01800 1.000 23.15451 ? 383 PHE A C     1 
ATOM   2765 O O     . PHE A 1 389 ? -5.50400  32.57300 -20.87700 1.000 23.61992 ? 383 PHE A O     1 
ATOM   2766 C CB    . PHE A 1 389 ? -8.71600  32.14900 -21.81400 1.000 20.12839 ? 383 PHE A CB    1 
ATOM   2767 C CG    . PHE A 1 389 ? -10.18800 32.10300 -21.50800 1.000 21.00314 ? 383 PHE A CG    1 
ATOM   2768 C CD1   . PHE A 1 389 ? -10.84800 33.22400 -21.01600 1.000 22.83019 ? 383 PHE A CD1   1 
ATOM   2769 C CD2   . PHE A 1 389 ? -10.91000 30.94200 -21.71500 1.000 21.24265 ? 383 PHE A CD2   1 
ATOM   2770 C CE1   . PHE A 1 389 ? -12.20200 33.17700 -20.73900 1.000 23.81413 ? 383 PHE A CE1   1 
ATOM   2771 C CE2   . PHE A 1 389 ? -12.26800 30.88400 -21.43500 1.000 21.59337 ? 383 PHE A CE2   1 
ATOM   2772 C CZ    . PHE A 1 389 ? -12.91100 31.99900 -20.94500 1.000 22.77411 ? 383 PHE A CZ    1 
ATOM   2773 N N     . LEU A 1 390 ? -6.14000  30.51600 -21.54200 1.000 22.38808 ? 384 LEU A N     1 
ATOM   2774 C CA    . LEU A 1 390 ? -4.87500  30.23900 -22.21600 1.000 26.30865 ? 384 LEU A CA    1 
ATOM   2775 C C     . LEU A 1 390 ? -4.62100  31.28500 -23.29200 1.000 29.35979 ? 384 LEU A C     1 
ATOM   2776 O O     . LEU A 1 390 ? -5.54300  31.70700 -23.99300 1.000 29.18500 ? 384 LEU A O     1 
ATOM   2777 C CB    . LEU A 1 390 ? -4.90000  28.85200 -22.85900 1.000 29.18308 ? 384 LEU A CB    1 
ATOM   2778 C CG    . LEU A 1 390 ? -4.63600  27.63600 -21.98300 1.000 31.19120 ? 384 LEU A CG    1 
ATOM   2779 C CD1   . LEU A 1 390 ? -5.06700  26.37200 -22.72900 1.000 31.62132 ? 384 LEU A CD1   1 
ATOM   2780 C CD2   . LEU A 1 390 ? -3.16400  27.56700 -21.61000 1.000 32.53849 ? 384 LEU A CD2   1 
ATOM   2781 N N     . GLN A 1 391 ? -3.36400  31.69400 -23.42600 1.000 32.58310 ? 385 GLN A N     1 
ATOM   2782 C CA    . GLN A 1 391 ? -2.99900  32.76800 -24.35300 1.000 37.17688 ? 385 GLN A CA    1 
ATOM   2783 C C     . GLN A 1 391 ? -3.39100  32.45500 -25.79600 1.000 38.60204 ? 385 GLN A C     1 
ATOM   2784 O O     . GLN A 1 391 ? -3.06500  31.39200 -26.31900 1.000 39.63891 ? 385 GLN A O     1 
ATOM   2785 C CB    . GLN A 1 391 ? -1.49400  33.04700 -24.27900 1.000 39.17551 ? 385 GLN A CB    1 
HETATM 2786 N N1    . FMN B 2 .   ? -19.95400 22.20600 -2.54500  1.000 12.87122 ? 401 FMN A N1    1 
HETATM 2787 C C2    . FMN B 2 .   ? -21.32000 22.17500 -2.57600  1.000 13.52631 ? 401 FMN A C2    1 
HETATM 2788 O O2    . FMN B 2 .   ? -21.88500 21.08100 -2.61400  1.000 13.21282 ? 401 FMN A O2    1 
HETATM 2789 N N3    . FMN B 2 .   ? -22.04000 23.35400 -2.59900  1.000 15.20039 ? 401 FMN A N3    1 
HETATM 2790 C C4    . FMN B 2 .   ? -21.42400 24.58300 -2.58000  1.000 15.50443 ? 401 FMN A C4    1 
HETATM 2791 O O4    . FMN B 2 .   ? -22.09000 25.62200 -2.61200  1.000 17.87500 ? 401 FMN A O4    1 
HETATM 2792 C C4A   . FMN B 2 .   ? -20.04000 24.61300 -2.53800  1.000 15.19274 ? 401 FMN A C4A   1 
HETATM 2793 N N5    . FMN B 2 .   ? -19.36300 25.81000 -2.49900  1.000 16.65775 ? 401 FMN A N5    1 
HETATM 2794 C C5A   . FMN B 2 .   ? -17.98100 25.84000 -2.52400  1.000 14.48208 ? 401 FMN A C5A   1 
HETATM 2795 C C6    . FMN B 2 .   ? -17.32800 27.07100 -2.52300  1.000 14.46676 ? 401 FMN A C6    1 
HETATM 2796 C C7    . FMN B 2 .   ? -15.94700 27.10700 -2.55200  1.000 15.12658 ? 401 FMN A C7    1 
HETATM 2797 C C7M   . FMN B 2 .   ? -15.20900 28.41600 -2.55100  1.000 16.71334 ? 401 FMN A C7M   1 
HETATM 2798 C C8    . FMN B 2 .   ? -15.23300 25.91500 -2.54500  1.000 16.17327 ? 401 FMN A C8    1 
HETATM 2799 C C8M   . FMN B 2 .   ? -13.72800 25.94500 -2.54300  1.000 20.17689 ? 401 FMN A C8M   1 
HETATM 2800 C C9    . FMN B 2 .   ? -15.89200 24.69300 -2.55400  1.000 14.93789 ? 401 FMN A C9    1 
HETATM 2801 C C9A   . FMN B 2 .   ? -17.27600 24.64800 -2.53900  1.000 13.57670 ? 401 FMN A C9A   1 
HETATM 2802 N N10   . FMN B 2 .   ? -17.94500 23.43400 -2.51700  1.000 11.88276 ? 401 FMN A N10   1 
HETATM 2803 C C10   . FMN B 2 .   ? -19.32000 23.41800 -2.53900  1.000 13.93103 ? 401 FMN A C10   1 
HETATM 2804 C "C1'" . FMN B 2 .   ? -17.21000 22.12700 -2.55500  1.000 13.18741 ? 401 FMN A "C1'" 1 
HETATM 2805 C "C2'" . FMN B 2 .   ? -16.91100 21.86000 -4.03200  1.000 14.25642 ? 401 FMN A "C2'" 1 
HETATM 2806 O "O2'" . FMN B 2 .   ? -18.11100 21.53900 -4.71100  1.000 14.46586 ? 401 FMN A "O2'" 1 
HETATM 2807 C "C3'" . FMN B 2 .   ? -16.00200 20.66800 -4.26000  1.000 16.45607 ? 401 FMN A "C3'" 1 
HETATM 2808 O "O3'" . FMN B 2 .   ? -16.50700 19.52100 -3.61700  1.000 16.97745 ? 401 FMN A "O3'" 1 
HETATM 2809 C "C4'" . FMN B 2 .   ? -14.57600 20.85400 -3.80900  1.000 19.58403 ? 401 FMN A "C4'" 1 
HETATM 2810 O "O4'" . FMN B 2 .   ? -14.12200 22.17100 -4.03600  1.000 20.77624 ? 401 FMN A "O4'" 1 
HETATM 2811 C "C5'" . FMN B 2 .   ? -13.86100 19.88900 -4.74000  1.000 18.15155 ? 401 FMN A "C5'" 1 
HETATM 2812 O "O5'" . FMN B 2 .   ? -12.53700 19.84300 -4.37900  1.000 19.09865 ? 401 FMN A "O5'" 1 
HETATM 2813 P P     . FMN B 2 .   ? -11.48900 20.62000 -5.29600  1.000 17.40770 ? 401 FMN A P     1 
HETATM 2814 O O1P   . FMN B 2 .   ? -11.67900 22.09100 -4.97400  1.000 16.48400 ? 401 FMN A O1P   1 
HETATM 2815 O O2P   . FMN B 2 .   ? -11.73100 20.28200 -6.76700  1.000 17.06626 ? 401 FMN A O2P   1 
HETATM 2816 O O3P   . FMN B 2 .   ? -10.12000 20.18400 -4.83400  1.000 18.82637 ? 401 FMN A O3P   1 
HETATM 2817 P PA    . NAP C 3 .   ? -46.83300 6.16800  0.89700   1.000 45.37566 ? 402 NAP A PA    1 
HETATM 2818 O O1A   . NAP C 3 .   ? -47.22400 7.73800  0.75600   1.000 47.20302 ? 402 NAP A O1A   1 
HETATM 2819 O O2A   . NAP C 3 .   ? -47.82400 5.26400  0.07700   1.000 45.99000 ? 402 NAP A O2A   1 
HETATM 2820 O O5B   . NAP C 3 .   ? -45.29200 5.94500  0.33500   1.000 39.01356 ? 402 NAP A O5B   1 
HETATM 2821 C C5B   . NAP C 3 .   ? -44.23200 6.66400  0.89400   1.000 33.45087 ? 402 NAP A C5B   1 
HETATM 2822 C C4B   . NAP C 3 .   ? -43.14700 6.93200  -0.22400  1.000 29.81098 ? 402 NAP A C4B   1 
HETATM 2823 O O4B   . NAP C 3 .   ? -42.50900 5.80500  -0.54500  1.000 27.34264 ? 402 NAP A O4B   1 
HETATM 2824 C C3B   . NAP C 3 .   ? -43.81400 7.41700  -1.53600  1.000 29.40375 ? 402 NAP A C3B   1 
HETATM 2825 O O3B   . NAP C 3 .   ? -43.00600 8.22800  -2.15300  1.000 30.48356 ? 402 NAP A O3B   1 
HETATM 2826 C C2B   . NAP C 3 .   ? -43.95200 6.07300  -2.37600  1.000 27.63780 ? 402 NAP A C2B   1 
HETATM 2827 O O2B   . NAP C 3 .   ? -43.97000 6.44500  -3.76500  1.000 28.33508 ? 402 NAP A O2B   1 
HETATM 2828 C C1B   . NAP C 3 .   ? -42.84800 5.45200  -2.11600  1.000 26.52001 ? 402 NAP A C1B   1 
HETATM 2829 N N9A   . NAP C 3 .   ? -42.96200 3.98600  -2.17300  1.000 24.91135 ? 402 NAP A N9A   1 
HETATM 2830 C C8A   . NAP C 3 .   ? -44.07400 3.22600  -1.95600  1.000 25.14703 ? 402 NAP A C8A   1 
HETATM 2831 N N7A   . NAP C 3 .   ? -43.74800 1.93700  -2.07200  1.000 25.30069 ? 402 NAP A N7A   1 
HETATM 2832 C C5A   . NAP C 3 .   ? -42.43400 1.84900  -2.36500  1.000 25.43212 ? 402 NAP A C5A   1 
HETATM 2833 C C6A   . NAP C 3 .   ? -41.53600 0.77300  -2.61100  1.000 26.79374 ? 402 NAP A C6A   1 
HETATM 2834 N N6A   . NAP C 3 .   ? -41.96300 -0.55500 -2.57700  1.000 28.19598 ? 402 NAP A N6A   1 
HETATM 2835 N N1A   . NAP C 3 .   ? -40.28500 1.03900  -2.86400  1.000 25.68074 ? 402 NAP A N1A   1 
HETATM 2836 C C2A   . NAP C 3 .   ? -39.84000 2.32600  -2.91100  1.000 24.51965 ? 402 NAP A C2A   1 
HETATM 2837 N N3A   . NAP C 3 .   ? -40.66200 3.36200  -2.69000  1.000 23.91059 ? 402 NAP A N3A   1 
HETATM 2838 C C4A   . NAP C 3 .   ? -41.93900 3.17500  -2.41400  1.000 24.19993 ? 402 NAP A C4A   1 
HETATM 2839 O O3    . NAP C 3 .   ? -46.94600 5.73800  2.44100   1.000 48.40923 ? 402 NAP A O3    1 
HETATM 2840 P PN    . NAP C 3 .   ? -46.11000 4.44400  3.04500   1.000 51.00866 ? 402 NAP A PN    1 
HETATM 2841 O O1N   . NAP C 3 .   ? -45.01700 4.97500  4.01800   1.000 51.36260 ? 402 NAP A O1N   1 
HETATM 2842 O O2N   . NAP C 3 .   ? -45.44900 3.69200  1.88600   1.000 49.89653 ? 402 NAP A O2N   1 
HETATM 2843 O O5D   . NAP C 3 .   ? -47.03400 3.58500  3.72000   1.000 51.73653 ? 402 NAP A O5D   1 
HETATM 2844 P P2B   . NAP C 3 .   ? -45.40600 6.45500  -4.62200  1.000 30.52502 ? 402 NAP A P2B   1 
HETATM 2845 O O1X   . NAP C 3 .   ? -46.47300 7.18200  -3.80400  1.000 29.46447 ? 402 NAP A O1X   1 
HETATM 2846 O O2X   . NAP C 3 .   ? -45.09100 7.18500  -5.88100  1.000 31.99970 ? 402 NAP A O2X   1 
HETATM 2847 O O3X   . NAP C 3 .   ? -45.83700 4.99100  -4.91900  1.000 31.39997 ? 402 NAP A O3X   1 
HETATM 2848 S S     . SO4 D 4 .   ? -15.78100 21.84700 2.31000   1.000 61.65021 ? 403 SO4 A S     1 
HETATM 2849 O O1    . SO4 D 4 .   ? -15.40600 21.39600 0.99500   1.000 57.30002 ? 403 SO4 A O1    1 
HETATM 2850 O O2    . SO4 D 4 .   ? -14.68100 22.54500 2.91200   1.000 62.62676 ? 403 SO4 A O2    1 
HETATM 2851 O O3    . SO4 D 4 .   ? -16.90700 22.73300 2.21400   1.000 62.96739 ? 403 SO4 A O3    1 
HETATM 2852 O O4    . SO4 D 4 .   ? -16.12800 20.71700 3.12700   1.000 60.44630 ? 403 SO4 A O4    1 
HETATM 2853 O O     . HOH E 5 .   ? -36.88700 26.44200 6.30500   1.000 38.48946 ? 501 HOH A O     1 
HETATM 2854 O O     . HOH E 5 .   ? -5.72800  8.94400  -25.45700 1.000 68.17053 ? 502 HOH A O     1 
HETATM 2855 O O     . HOH E 5 .   ? -20.22600 16.13400 5.87800   1.000 35.59217 ? 503 HOH A O     1 
HETATM 2856 O O     . HOH E 5 .   ? -18.33000 40.17700 2.20400   1.000 34.69247 ? 504 HOH A O     1 
HETATM 2857 O O     . HOH E 5 .   ? -18.33300 39.21300 13.33500  1.000 39.28855 ? 505 HOH A O     1 
HETATM 2858 O O     . HOH E 5 .   ? -50.08000 23.72200 5.69200   1.000 26.87868 ? 506 HOH A O     1 
HETATM 2859 O O     . HOH E 5 .   ? -30.04500 -1.02700 -12.21000 1.000 52.81788 ? 507 HOH A O     1 
HETATM 2860 O O     . HOH E 5 .   ? -13.31000 40.01800 -5.12200  1.000 19.93614 ? 508 HOH A O     1 
HETATM 2861 O O     . HOH E 5 .   ? -27.360   21.943   25.599    1.000 24.87769 ? 509 HOH A O     1 
HETATM 2862 O O     . HOH E 5 .   ? -25.06900 17.35300 -24.51300 1.000 42.99601 ? 510 HOH A O     1 
HETATM 2863 O O     . HOH E 5 .   ? -36.14700 23.44500 19.39200  1.000 39.30960 ? 511 HOH A O     1 
HETATM 2864 O O     . HOH E 5 .   ? -39.07300 26.06900 8.13500   1.000 42.04506 ? 512 HOH A O     1 
HETATM 2865 O O     . HOH E 5 .   ? -26.93600 9.04300  -15.59300 1.000 22.76718 ? 513 HOH A O     1 
HETATM 2866 O O     . HOH E 5 .   ? -12.609   45.955   -7.642    1.000 32.03923 ? 514 HOH A O     1 
HETATM 2867 O O     . HOH E 5 .   ? -21.57200 16.57500 16.37400  1.000 48.04027 ? 515 HOH A O     1 
HETATM 2868 O O     . HOH E 5 .   ? -37.74900 2.84200  11.44600  1.000 42.26955 ? 516 HOH A O     1 
HETATM 2869 O O     . HOH E 5 .   ? -35.22200 30.36700 10.47700  1.000 32.23035 ? 517 HOH A O     1 
HETATM 2870 O O     . HOH E 5 .   ? -23.09000 4.38600  -16.87000 1.000 45.24440 ? 518 HOH A O     1 
HETATM 2871 O O     . HOH E 5 .   ? -44.59000 17.82700 -12.05500 1.000 36.00805 ? 519 HOH A O     1 
HETATM 2872 O O     . HOH E 5 .   ? -23.06900 32.11100 -24.66900 1.000 23.30581 ? 520 HOH A O     1 
HETATM 2873 O O     . HOH E 5 .   ? -2.31700  14.70900 -8.58300  1.000 37.14509 ? 521 HOH A O     1 
HETATM 2874 O O     . HOH E 5 .   ? -12.10700 2.16000  3.42600   1.000 38.55190 ? 522 HOH A O     1 
HETATM 2875 O O     . HOH E 5 .   ? -20.77600 28.08000 7.00100   1.000 27.35214 ? 523 HOH A O     1 
HETATM 2876 O O     . HOH E 5 .   ? -14.71000 44.93300 -10.61000 1.000 38.99564 ? 524 HOH A O     1 
HETATM 2877 O O     . HOH E 5 .   ? -20.83900 3.43900  -15.43600 1.000 37.13072 ? 525 HOH A O     1 
HETATM 2878 O O     . HOH E 5 .   ? -38.95300 26.89300 -3.11800  1.000 35.75255 ? 526 HOH A O     1 
HETATM 2879 O O     . HOH E 5 .   ? -35.20800 32.52100 -22.19400 1.000 58.31863 ? 527 HOH A O     1 
HETATM 2880 O O     . HOH E 5 .   ? -21.22500 27.91500 17.97000  1.000 17.25314 ? 528 HOH A O     1 
HETATM 2881 O O     . HOH E 5 .   ? -30.22500 9.60300  15.97900  1.000 39.22405 ? 529 HOH A O     1 
HETATM 2882 O O     . HOH E 5 .   ? -10.81500 33.71800 -6.58500  1.000 18.47766 ? 530 HOH A O     1 
HETATM 2883 O O     . HOH E 5 .   ? -17.71900 22.90300 -19.36000 1.000 18.21441 ? 531 HOH A O     1 
HETATM 2884 O O     . HOH E 5 .   ? -24.03900 30.03100 -29.33200 1.000 24.83731 ? 532 HOH A O     1 
HETATM 2885 O O     . HOH E 5 .   ? -30.49800 41.48800 0.66700   1.000 42.49225 ? 533 HOH A O     1 
HETATM 2886 O O     . HOH E 5 .   ? -40.43500 4.38900  11.57400  1.000 52.13576 ? 534 HOH A O     1 
HETATM 2887 O O     . HOH E 5 .   ? -29.95600 21.45000 -22.63100 1.000 28.35868 ? 535 HOH A O     1 
HETATM 2888 O O     . HOH E 5 .   ? -41.49100 22.72800 14.00600  1.000 22.61037 ? 536 HOH A O     1 
HETATM 2889 O O     . HOH E 5 .   ? -4.37200  24.39100 -2.62600  1.000 32.80086 ? 537 HOH A O     1 
HETATM 2890 O O     . HOH E 5 .   ? -8.72800  28.18000 -23.92700 1.000 30.84861 ? 538 HOH A O     1 
HETATM 2891 O O     . HOH E 5 .   ? -28.70100 38.69900 5.41800   1.000 29.71854 ? 539 HOH A O     1 
HETATM 2892 O O     . HOH E 5 .   ? -27.17900 10.66700 17.75300  1.000 48.69865 ? 540 HOH A O     1 
HETATM 2893 O O     . HOH E 5 .   ? -5.11000  16.51100 -4.38800  1.000 40.33036 ? 541 HOH A O     1 
HETATM 2894 O O     . HOH E 5 .   ? -35.92300 1.89000  12.47400  1.000 26.67891 ? 542 HOH A O     1 
HETATM 2895 O O     . HOH E 5 .   ? -15.10100 27.73600 -21.88700 1.000 33.04666 ? 543 HOH A O     1 
HETATM 2896 O O     . HOH E 5 .   ? -23.59300 -1.26400 6.04400   1.000 27.84443 ? 544 HOH A O     1 
HETATM 2897 O O     . HOH E 5 .   ? -33.39000 22.86900 -20.47200 1.000 43.28946 ? 545 HOH A O     1 
HETATM 2898 O O     . HOH E 5 .   ? -35.41000 5.20200  5.11700   1.000 49.53469 ? 546 HOH A O     1 
HETATM 2899 O O     . HOH E 5 .   ? -46.37200 9.64300  -2.90200  1.000 38.66376 ? 547 HOH A O     1 
HETATM 2900 O O     . HOH E 5 .   ? -42.54700 10.54800 14.57700  1.000 48.20083 ? 548 HOH A O     1 
HETATM 2901 O O     . HOH E 5 .   ? -36.68300 29.70700 14.03900  1.000 30.63967 ? 549 HOH A O     1 
HETATM 2902 O O     . HOH E 5 .   ? -22.19900 2.80400  14.66300  1.000 42.48302 ? 550 HOH A O     1 
HETATM 2903 O O     . HOH E 5 .   ? -7.73200  30.72800 -25.07600 1.000 41.14643 ? 551 HOH A O     1 
HETATM 2904 O O     . HOH E 5 .   ? -11.61000 32.62800 1.56900   1.000 38.90918 ? 552 HOH A O     1 
HETATM 2905 O O     . HOH E 5 .   ? -29.89200 20.93800 0.28300   1.000 16.41413 ? 553 HOH A O     1 
HETATM 2906 O O     . HOH E 5 .   ? -20.84800 31.53500 -8.98100  1.000 24.41616 ? 554 HOH A O     1 
HETATM 2907 O O     . HOH E 5 .   ? -11.17600 37.94300 1.62000   1.000 36.14972 ? 555 HOH A O     1 
HETATM 2908 O O     . HOH E 5 .   ? -32.30900 34.56500 16.83800  1.000 36.53402 ? 556 HOH A O     1 
HETATM 2909 O O     . HOH E 5 .   ? -32.11300 27.47800 -22.47500 1.000 40.13009 ? 557 HOH A O     1 
HETATM 2910 O O     . HOH E 5 .   ? -22.08900 33.88400 -7.07100  1.000 19.19478 ? 558 HOH A O     1 
HETATM 2911 O O     . HOH E 5 .   ? -9.61900  42.67900 -12.81500 1.000 28.06069 ? 559 HOH A O     1 
HETATM 2912 O O     . HOH E 5 .   ? -36.23600 42.37500 -5.28600  1.000 42.46057 ? 560 HOH A O     1 
HETATM 2913 O O     . HOH E 5 .   ? -45.36000 12.72900 12.50400  1.000 30.03503 ? 561 HOH A O     1 
HETATM 2914 O O     . HOH E 5 .   ? -32.88400 19.55300 -20.81700 1.000 35.82220 ? 562 HOH A O     1 
HETATM 2915 O O     . HOH E 5 .   ? -37.05300 25.75600 3.91000   1.000 21.61693 ? 563 HOH A O     1 
HETATM 2916 O O     . HOH E 5 .   ? -7.90700  1.88300  -2.04500  1.000 40.55689 ? 564 HOH A O     1 
HETATM 2917 O O     . HOH E 5 .   ? -19.25600 26.09700 5.57800   1.000 32.36218 ? 565 HOH A O     1 
HETATM 2918 O O     . HOH E 5 .   ? -18.28300 34.86500 -20.54500 1.000 37.15791 ? 566 HOH A O     1 
HETATM 2919 O O     . HOH E 5 .   ? -35.70100 2.18100  5.49200   1.000 45.82047 ? 567 HOH A O     1 
HETATM 2920 O O     . HOH E 5 .   ? -33.57900 29.23300 -19.96000 1.000 34.72869 ? 568 HOH A O     1 
HETATM 2921 O O     . HOH E 5 .   ? -21.17700 32.26900 5.62500   1.000 20.33925 ? 569 HOH A O     1 
HETATM 2922 O O     . HOH E 5 .   ? -24.33800 5.00900  11.45400  1.000 47.38067 ? 570 HOH A O     1 
HETATM 2923 O O     . HOH E 5 .   ? -8.25800  36.64600 -10.71000 1.000 30.93048 ? 571 HOH A O     1 
HETATM 2924 O O     . HOH E 5 .   ? -40.82200 25.44300 4.84800   1.000 36.07741 ? 572 HOH A O     1 
HETATM 2925 O O     . HOH E 5 .   ? -17.47000 27.22300 9.55200   1.000 27.53777 ? 573 HOH A O     1 
HETATM 2926 O O     . HOH E 5 .   ? -27.45100 3.99300  14.10200  1.000 52.14620 ? 574 HOH A O     1 
HETATM 2927 O O     . HOH E 5 .   ? -19.70200 42.95900 0.52900   1.000 26.20241 ? 575 HOH A O     1 
HETATM 2928 O O     . HOH E 5 .   ? -22.76600 21.46500 20.16800  1.000 41.99966 ? 576 HOH A O     1 
HETATM 2929 O O     . HOH E 5 .   ? -6.19100  31.77600 -15.34000 1.000 24.19584 ? 577 HOH A O     1 
HETATM 2930 O O     . HOH E 5 .   ? -26.89800 17.25800 18.15600  1.000 27.91294 ? 578 HOH A O     1 
HETATM 2931 O O     . HOH E 5 .   ? -19.38800 29.14600 16.22900  1.000 20.13566 ? 579 HOH A O     1 
HETATM 2932 O O     . HOH E 5 .   ? -42.12200 10.55400 0.09400   1.000 30.16934 ? 580 HOH A O     1 
HETATM 2933 O O     . HOH E 5 .   ? -37.83500 14.15300 -16.66600 1.000 33.66647 ? 581 HOH A O     1 
HETATM 2934 O O     . HOH E 5 .   ? -18.27300 39.71700 -14.38200 1.000 32.19251 ? 582 HOH A O     1 
HETATM 2935 O O     . HOH E 5 .   ? -32.02100 35.19000 -21.99300 1.000 40.79610 ? 583 HOH A O     1 
HETATM 2936 O O     . HOH E 5 .   ? -43.81000 17.78100 -1.09900  1.000 30.89075 ? 584 HOH A O     1 
HETATM 2937 O O     . HOH E 5 .   ? -17.53300 5.34200  -17.07900 1.000 21.28811 ? 585 HOH A O     1 
HETATM 2938 O O     . HOH E 5 .   ? -42.03200 14.36800 16.03800  1.000 31.81025 ? 586 HOH A O     1 
HETATM 2939 O O     . HOH E 5 .   ? -22.06500 11.71600 -25.58200 1.000 29.50608 ? 587 HOH A O     1 
HETATM 2940 O O     . HOH E 5 .   ? -23.68600 38.58800 -18.13900 1.000 35.88769 ? 588 HOH A O     1 
HETATM 2941 O O     . HOH E 5 .   ? -1.39900  31.23500 -21.63900 1.000 53.76844 ? 589 HOH A O     1 
HETATM 2942 O O     . HOH E 5 .   ? -23.77800 20.37500 -26.91100 1.000 37.45393 ? 590 HOH A O     1 
HETATM 2943 O O     . HOH E 5 .   ? -24.74400 33.67800 16.97500  1.000 27.75386 ? 591 HOH A O     1 
HETATM 2944 O O     . HOH E 5 .   ? -24.05600 29.60900 -3.15800  1.000 17.39577 ? 592 HOH A O     1 
HETATM 2945 O O     . HOH E 5 .   ? -28.40200 7.32700  16.06100  1.000 46.40180 ? 593 HOH A O     1 
HETATM 2946 O O     . HOH E 5 .   ? -40.48600 7.79300  2.12900   1.000 33.41633 ? 594 HOH A O     1 
HETATM 2947 O O     . HOH E 5 .   ? -23.95300 10.03300 -25.04800 1.000 49.32344 ? 595 HOH A O     1 
HETATM 2948 O O     . HOH E 5 .   ? -17.79900 21.00000 -17.41100 1.000 15.88448 ? 596 HOH A O     1 
HETATM 2949 O O     . HOH E 5 .   ? -20.01100 -2.03300 -2.68000  1.000 18.14821 ? 597 HOH A O     1 
HETATM 2950 O O     . HOH E 5 .   ? -19.46700 28.48600 -8.82700  1.000 18.46367 ? 598 HOH A O     1 
HETATM 2951 O O     . HOH E 5 .   ? -19.92400 24.87200 1.78100   1.000 31.11499 ? 599 HOH A O     1 
HETATM 2952 O O     . HOH E 5 .   ? -23.14700 28.49000 6.39300   1.000 21.45460 ? 600 HOH A O     1 
HETATM 2953 O O     . HOH E 5 .   ? -16.28400 13.18300 -27.04700 1.000 47.43592 ? 601 HOH A O     1 
HETATM 2954 O O     . HOH E 5 .   ? -3.07200  29.60200 -4.01100  1.000 32.19467 ? 602 HOH A O     1 
HETATM 2955 O O     . HOH E 5 .   ? -12.48500 8.20900  -7.73800  1.000 34.52286 ? 603 HOH A O     1 
HETATM 2956 O O     . HOH E 5 .   ? -9.744    -1.443   7.150     1.000 43.84313 ? 604 HOH A O     1 
HETATM 2957 O O     . HOH E 5 .   ? -23.28200 -0.14700 -10.40800 1.000 30.11250 ? 605 HOH A O     1 
HETATM 2958 O O     . HOH E 5 .   ? -31.85100 32.21100 5.09900   1.000 20.86275 ? 606 HOH A O     1 
HETATM 2959 O O     . HOH E 5 .   ? -14.53600 45.14700 -4.54000  1.000 31.53064 ? 607 HOH A O     1 
HETATM 2960 O O     . HOH E 5 .   ? -41.41900 -0.89900 -6.30000  1.000 44.11308 ? 608 HOH A O     1 
HETATM 2961 O O     . HOH E 5 .   ? -27.45600 15.62600 22.02900  1.000 30.06899 ? 609 HOH A O     1 
HETATM 2962 O O     . HOH E 5 .   ? -12.17800 17.61200 -7.13900  1.000 19.15394 ? 610 HOH A O     1 
HETATM 2963 O O     . HOH E 5 .   ? -9.96000  21.60400 -8.37500  1.000 16.49760 ? 611 HOH A O     1 
HETATM 2964 O O     . HOH E 5 .   ? -27.54500 7.46700  -12.12200 1.000 17.05760 ? 612 HOH A O     1 
HETATM 2965 O O     . HOH E 5 .   ? -31.97800 36.41200 2.48400   1.000 35.12931 ? 613 HOH A O     1 
HETATM 2966 O O     . HOH E 5 .   ? -31.69500 12.24300 5.86200   1.000 18.52644 ? 614 HOH A O     1 
HETATM 2967 O O     . HOH E 5 .   ? -8.09200  20.25800 -6.67300  1.000 25.56463 ? 615 HOH A O     1 
HETATM 2968 O O     . HOH E 5 .   ? -42.57200 26.25900 12.50700  1.000 42.67151 ? 616 HOH A O     1 
HETATM 2969 O O     . HOH E 5 .   ? -2.87000  20.12600 -17.34900 1.000 25.38172 ? 617 HOH A O     1 
HETATM 2970 O O     . HOH E 5 .   ? -33.59700 26.19800 20.14500  1.000 37.58210 ? 618 HOH A O     1 
HETATM 2971 O O     . HOH E 5 .   ? -36.30400 39.88100 8.03600   1.000 38.86185 ? 619 HOH A O     1 
HETATM 2972 O O     . HOH E 5 .   ? -30.29300 15.67300 -23.75600 1.000 39.91216 ? 620 HOH A O     1 
HETATM 2973 O O     . HOH E 5 .   ? -25.87000 5.77300  16.16500  1.000 42.24734 ? 621 HOH A O     1 
HETATM 2974 O O     . HOH E 5 .   ? -18.54000 11.31700 8.91100   1.000 28.80484 ? 622 HOH A O     1 
HETATM 2975 O O     . HOH E 5 .   ? -43.02800 6.77300  -7.65300  1.000 32.64833 ? 623 HOH A O     1 
HETATM 2976 O O     . HOH E 5 .   ? -18.53700 38.41900 3.59500   1.000 36.30973 ? 624 HOH A O     1 
HETATM 2977 O O     . HOH E 5 .   ? -23.00900 31.90800 -4.22400  1.000 16.55130 ? 625 HOH A O     1 
HETATM 2978 O O     . HOH E 5 .   ? -41.18100 29.18400 -4.96700  1.000 39.34648 ? 626 HOH A O     1 
HETATM 2979 O O     . HOH E 5 .   ? -20.89400 22.78000 0.46900   1.000 21.29980 ? 627 HOH A O     1 
HETATM 2980 O O     . HOH E 5 .   ? -32.02400 1.16200  -9.05800  1.000 22.13116 ? 628 HOH A O     1 
HETATM 2981 O O     . HOH E 5 .   ? -5.74400  14.75000 -23.39800 1.000 39.92273 ? 629 HOH A O     1 
HETATM 2982 O O     . HOH E 5 .   ? -30.67200 12.09500 21.86100  1.000 50.87601 ? 630 HOH A O     1 
HETATM 2983 O O     . HOH E 5 .   ? 0.42000   24.56600 -12.74600 1.000 18.47203 ? 631 HOH A O     1 
HETATM 2984 O O     . HOH E 5 .   ? -9.98200  0.61900  -8.60400  1.000 43.01899 ? 632 HOH A O     1 
HETATM 2985 O O     . HOH E 5 .   ? -20.28400 25.89100 -9.49900  1.000 15.96875 ? 633 HOH A O     1 
HETATM 2986 O O     . HOH E 5 .   ? -41.59700 13.11300 -0.17900  1.000 21.92290 ? 634 HOH A O     1 
HETATM 2987 O O     . HOH E 5 .   ? -37.11500 10.09400 -15.42600 1.000 35.20960 ? 635 HOH A O     1 
HETATM 2988 O O     . HOH E 5 .   ? -13.25100 37.27400 5.06900   1.000 44.81186 ? 636 HOH A O     1 
HETATM 2989 O O     . HOH E 5 .   ? -29.68000 46.37900 -2.75200  1.000 36.74730 ? 637 HOH A O     1 
HETATM 2990 O O     . HOH E 5 .   ? -42.44100 7.25500  -12.47000 1.000 41.85615 ? 638 HOH A O     1 
HETATM 2991 O O     . HOH E 5 .   ? -15.07000 4.79000  -15.44700 1.000 25.78788 ? 639 HOH A O     1 
HETATM 2992 O O     . HOH E 5 .   ? -39.83600 23.78500 16.15700  1.000 35.49911 ? 640 HOH A O     1 
HETATM 2993 O O     . HOH E 5 .   ? -19.08700 -1.01700 9.06200   1.000 42.52044 ? 641 HOH A O     1 
HETATM 2994 O O     . HOH E 5 .   ? -13.92000 24.99900 -19.17500 1.000 17.39298 ? 642 HOH A O     1 
HETATM 2995 O O     . HOH E 5 .   ? -8.21500  37.50500 -6.74500  1.000 34.68691 ? 643 HOH A O     1 
HETATM 2996 O O     . HOH E 5 .   ? -13.19100 35.18200 0.27600   1.000 21.36022 ? 644 HOH A O     1 
HETATM 2997 O O     . HOH E 5 .   ? -32.35800 3.78300  16.90600  1.000 56.24344 ? 645 HOH A O     1 
HETATM 2998 O O     . HOH E 5 .   ? -21.78500 41.83900 2.12700   1.000 19.00780 ? 646 HOH A O     1 
HETATM 2999 O O     . HOH E 5 .   ? -7.53100  40.52400 -10.20900 1.000 36.75046 ? 647 HOH A O     1 
HETATM 3000 O O     . HOH E 5 .   ? -17.52900 11.21400 1.90200   1.000 25.15170 ? 648 HOH A O     1 
HETATM 3001 O O     . HOH E 5 .   ? -3.71700  32.82300 -11.18800 1.000 23.72393 ? 649 HOH A O     1 
HETATM 3002 O O     . HOH E 5 .   ? -36.32700 6.94500  17.20400  1.000 43.52381 ? 650 HOH A O     1 
HETATM 3003 O O     . HOH E 5 .   ? -30.48300 30.89800 18.61300  1.000 25.48370 ? 651 HOH A O     1 
HETATM 3004 O O     . HOH E 5 .   ? -30.46900 11.51300 -16.85300 1.000 26.20616 ? 652 HOH A O     1 
HETATM 3005 O O     . HOH E 5 .   ? -33.84000 37.42700 -0.69600  1.000 41.16411 ? 653 HOH A O     1 
HETATM 3006 O O     . HOH E 5 .   ? -41.68700 23.78600 -13.95300 1.000 24.62083 ? 654 HOH A O     1 
HETATM 3007 O O     . HOH E 5 .   ? -25.54600 26.01300 14.73000  1.000 18.58871 ? 655 HOH A O     1 
HETATM 3008 O O     . HOH E 5 .   ? -32.23400 -2.88500 4.41300   1.000 40.62131 ? 656 HOH A O     1 
HETATM 3009 O O     . HOH E 5 .   ? -23.82900 13.42500 3.50400   1.000 16.68723 ? 657 HOH A O     1 
HETATM 3010 O O     . HOH E 5 .   ? -7.60600  7.97600  -25.71300 1.000 52.91947 ? 658 HOH A O     1 
HETATM 3011 O O     . HOH E 5 .   ? -29.78300 40.52300 -12.11100 1.000 38.26773 ? 659 HOH A O     1 
HETATM 3012 O O     . HOH E 5 .   ? -12.24600 33.81800 -15.04000 1.000 19.50441 ? 660 HOH A O     1 
HETATM 3013 O O     . HOH E 5 .   ? -13.59200 32.50500 -10.46900 1.000 13.53788 ? 661 HOH A O     1 
HETATM 3014 O O     . HOH E 5 .   ? -31.93800 27.32600 8.77700   1.000 18.72198 ? 662 HOH A O     1 
HETATM 3015 O O     . HOH E 5 .   ? -18.72200 17.22700 -18.31400 1.000 15.62933 ? 663 HOH A O     1 
HETATM 3016 O O     . HOH E 5 .   ? -38.13900 -0.92300 -11.90700 1.000 38.85814 ? 664 HOH A O     1 
HETATM 3017 O O     . HOH E 5 .   ? -44.92000 16.50500 -7.50800  1.000 34.19531 ? 665 HOH A O     1 
HETATM 3018 O O     . HOH E 5 .   ? -47.77300 17.64300 6.23300   1.000 20.89133 ? 666 HOH A O     1 
HETATM 3019 O O     . HOH E 5 .   ? -18.86900 -0.87100 -10.34300 1.000 42.66907 ? 667 HOH A O     1 
HETATM 3020 O O     . HOH E 5 .   ? -16.02100 19.00800 -0.91000  1.000 25.98599 ? 668 HOH A O     1 
HETATM 3021 O O     . HOH E 5 .   ? -40.01300 27.67100 -1.22900  1.000 43.73420 ? 669 HOH A O     1 
HETATM 3022 O O     . HOH E 5 .   ? -14.50700 6.24900  -6.49500  1.000 34.56162 ? 670 HOH A O     1 
HETATM 3023 O O     . HOH E 5 .   ? -16.23600 20.38700 -25.74000 1.000 50.91988 ? 671 HOH A O     1 
HETATM 3024 O O     . HOH E 5 .   ? -29.57600 29.30200 -25.27900 1.000 28.87621 ? 672 HOH A O     1 
HETATM 3025 O O     . HOH E 5 .   ? -35.13400 2.11200  -12.51000 1.000 39.56926 ? 673 HOH A O     1 
HETATM 3026 O O     . HOH E 5 .   ? -29.24900 35.71800 -21.53900 1.000 29.97969 ? 674 HOH A O     1 
HETATM 3027 O O     . HOH E 5 .   ? 0.62500   28.55400 -15.09100 1.000 21.53881 ? 675 HOH A O     1 
HETATM 3028 O O     . HOH E 5 .   ? -42.34300 26.65200 -11.42400 1.000 48.68474 ? 676 HOH A O     1 
HETATM 3029 O O     . HOH E 5 .   ? -41.01600 9.77000  -6.12400  1.000 24.09934 ? 677 HOH A O     1 
HETATM 3030 O O     . HOH E 5 .   ? -31.82600 39.23000 10.20100  1.000 41.07740 ? 678 HOH A O     1 
HETATM 3031 O O     . HOH E 5 .   ? -35.66100 36.26800 -18.14500 1.000 27.07096 ? 679 HOH A O     1 
HETATM 3032 O O     . HOH E 5 .   ? -33.42000 5.26400  -16.34600 1.000 37.03765 ? 680 HOH A O     1 
HETATM 3033 O O     . HOH E 5 .   ? -27.92900 35.42200 2.25700   1.000 18.78638 ? 681 HOH A O     1 
HETATM 3034 O O     . HOH E 5 .   ? -41.69000 18.84900 -14.26500 1.000 37.51034 ? 682 HOH A O     1 
HETATM 3035 O O     . HOH E 5 .   ? -22.27000 15.87700 -26.49900 1.000 31.77023 ? 683 HOH A O     1 
HETATM 3036 O O     . HOH E 5 .   ? -43.27400 24.91700 1.86200   1.000 36.42188 ? 684 HOH A O     1 
HETATM 3037 O O     . HOH E 5 .   ? -43.84000 4.67400  -9.33000  1.000 42.77317 ? 685 HOH A O     1 
HETATM 3038 O O     . HOH E 5 .   ? -41.04600 28.39200 2.20900   1.000 43.77388 ? 686 HOH A O     1 
HETATM 3039 O O     . HOH E 5 .   ? -17.48600 43.86400 12.40800  1.000 48.08035 ? 687 HOH A O     1 
HETATM 3040 O O     . HOH E 5 .   ? -43.97800 17.23800 1.61200   1.000 22.62538 ? 688 HOH A O     1 
HETATM 3041 O O     . HOH E 5 .   ? -27.389   23.522   23.359    1.000 25.86098 ? 689 HOH A O     1 
HETATM 3042 O O     . HOH E 5 .   ? -16.79100 37.60500 2.02400   1.000 24.40465 ? 690 HOH A O     1 
HETATM 3043 O O     . HOH E 5 .   ? -21.92000 3.89600  -9.55300  1.000 17.02834 ? 691 HOH A O     1 
HETATM 3044 O O     . HOH E 5 .   ? -40.31400 34.06500 -13.27600 1.000 41.24646 ? 692 HOH A O     1 
HETATM 3045 O O     . HOH E 5 .   ? -38.30700 -0.11000 -4.90700  1.000 36.33199 ? 693 HOH A O     1 
HETATM 3046 O O     . HOH E 5 .   ? -26.41800 -1.41000 -2.96000  1.000 30.61205 ? 694 HOH A O     1 
HETATM 3047 O O     . HOH E 5 .   ? -35.95900 23.02100 -18.23800 1.000 29.70164 ? 695 HOH A O     1 
HETATM 3048 O O     . HOH E 5 .   ? -33.95800 37.85600 -3.54200  1.000 27.73823 ? 696 HOH A O     1 
HETATM 3049 O O     . HOH E 5 .   ? -40.04900 20.03300 -18.76400 1.000 49.28481 ? 697 HOH A O     1 
HETATM 3050 O O     . HOH E 5 .   ? -36.18000 37.93300 -5.37800  1.000 24.15534 ? 698 HOH A O     1 
HETATM 3051 O O     . HOH E 5 .   ? -23.77400 21.01800 11.14000  1.000 15.54700 ? 699 HOH A O     1 
HETATM 3052 O O     . HOH E 5 .   ? -29.783   40.836   8.751     1.000 34.24545 ? 700 HOH A O     1 
HETATM 3053 O O     . HOH E 5 .   ? -7.78100  8.95400  -8.58400  1.000 23.05562 ? 701 HOH A O     1 
HETATM 3054 O O     . HOH E 5 .   ? -8.05900  10.09400 -6.05700  1.000 31.44417 ? 702 HOH A O     1 
HETATM 3055 O O     . HOH E 5 .   ? -23.16700 18.61800 16.67500  1.000 37.69615 ? 703 HOH A O     1 
HETATM 3056 O O     . HOH E 5 .   ? -29.11800 37.21400 -14.70100 1.000 28.86712 ? 704 HOH A O     1 
HETATM 3057 O O     . HOH E 5 .   ? -26.62600 18.63300 3.85600   1.000 15.59632 ? 705 HOH A O     1 
HETATM 3058 O O     . HOH E 5 .   ? -7.96700  8.84800  -1.50300  1.000 42.44325 ? 706 HOH A O     1 
HETATM 3059 O O     . HOH E 5 .   ? -21.69500 20.29300 17.64200  1.000 40.33205 ? 707 HOH A O     1 
HETATM 3060 O O     . HOH E 5 .   ? -25.85200 0.17200  5.69500   1.000 25.59431 ? 708 HOH A O     1 
HETATM 3061 O O     . HOH E 5 .   ? -26.20400 -0.49600 -0.22800  1.000 28.93206 ? 709 HOH A O     1 
HETATM 3062 O O     . HOH E 5 .   ? -40.38100 37.88000 -7.51400  1.000 33.99290 ? 710 HOH A O     1 
HETATM 3063 O O     . HOH E 5 .   ? -22.52800 2.89200  -13.65100 1.000 34.03082 ? 711 HOH A O     1 
HETATM 3064 O O     . HOH E 5 .   ? -19.32400 30.47400 6.48600   1.000 22.50887 ? 712 HOH A O     1 
HETATM 3065 O O     . HOH E 5 .   ? -39.51600 5.67400  -3.94400  1.000 23.40439 ? 713 HOH A O     1 
HETATM 3066 O O     . HOH E 5 .   ? -21.69600 40.74600 -7.77600  1.000 18.33993 ? 714 HOH A O     1 
HETATM 3067 O O     . HOH E 5 .   ? -27.44500 34.30900 15.48400  1.000 24.44920 ? 715 HOH A O     1 
HETATM 3068 O O     . HOH E 5 .   ? -28.69800 20.17500 3.06300   1.000 18.19492 ? 716 HOH A O     1 
HETATM 3069 O O     . HOH E 5 .   ? -9.92700  7.08300  -8.14100  1.000 31.17760 ? 717 HOH A O     1 
HETATM 3070 O O     . HOH E 5 .   ? -32.98900 1.13100  -11.71000 1.000 37.61616 ? 718 HOH A O     1 
HETATM 3071 O O     . HOH E 5 .   ? -31.05800 9.51600  18.47500  1.000 54.69721 ? 719 HOH A O     1 
HETATM 3072 O O     . HOH E 5 .   ? -8.22500  35.67700 -21.11100 1.000 24.56792 ? 720 HOH A O     1 
HETATM 3073 O O     . HOH E 5 .   ? -15.74100 36.49600 -20.34700 1.000 51.73219 ? 721 HOH A O     1 
HETATM 3074 O O     . HOH E 5 .   ? -28.11200 30.94500 20.03300  1.000 25.20418 ? 722 HOH A O     1 
HETATM 3075 O O     . HOH E 5 .   ? -38.78200 34.36000 10.57100  1.000 45.41665 ? 723 HOH A O     1 
HETATM 3076 O O     . HOH E 5 .   ? -43.00300 26.11300 -8.17000  1.000 49.70553 ? 724 HOH A O     1 
HETATM 3077 O O     . HOH E 5 .   ? -41.98000 11.84300 -12.01600 1.000 38.95919 ? 725 HOH A O     1 
HETATM 3078 O O     . HOH E 5 .   ? -13.68600 15.36100 7.00400   1.000 38.65165 ? 726 HOH A O     1 
HETATM 3079 O O     . HOH E 5 .   ? -34.73400 4.43800  16.01400  1.000 37.74377 ? 727 HOH A O     1 
HETATM 3080 O O     . HOH E 5 .   ? -42.13600 14.69400 4.48600   1.000 28.58960 ? 728 HOH A O     1 
HETATM 3081 O O     . HOH E 5 .   ? -27.24000 38.06300 1.70300   1.000 19.16240 ? 729 HOH A O     1 
HETATM 3082 O O     . HOH E 5 .   ? -3.48900  31.79700 -18.69900 1.000 32.51960 ? 730 HOH A O     1 
HETATM 3083 O O     . HOH E 5 .   ? 1.38400   20.63100 -17.96700 1.000 56.20586 ? 731 HOH A O     1 
HETATM 3084 O O     . HOH E 5 .   ? -12.27300 5.18800  -5.48400  1.000 30.90045 ? 732 HOH A O     1 
HETATM 3085 O O     . HOH E 5 .   ? -0.39000  17.75900 -15.62400 1.000 53.16675 ? 733 HOH A O     1 
HETATM 3086 O O     . HOH E 5 .   ? -33.61300 16.80300 18.10100  1.000 28.92777 ? 734 HOH A O     1 
HETATM 3087 O O     . HOH E 5 .   ? -38.96700 9.49400  -12.54200 1.000 23.15043 ? 735 HOH A O     1 
HETATM 3088 O O     . HOH E 5 .   ? -28.61100 28.35300 0.78600   1.000 20.89329 ? 736 HOH A O     1 
HETATM 3089 O O     . HOH E 5 .   ? -10.85300 36.45800 -18.00400 1.000 30.82115 ? 737 HOH A O     1 
HETATM 3090 O O     . HOH E 5 .   ? -22.04500 6.12700  -21.69000 1.000 30.08610 ? 738 HOH A O     1 
HETATM 3091 O O     . HOH E 5 .   ? -33.20300 -0.71300 5.76300   1.000 46.72871 ? 739 HOH A O     1 
HETATM 3092 O O     . HOH E 5 .   ? -34.15900 11.65200 8.58700   1.000 15.98735 ? 740 HOH A O     1 
HETATM 3093 O O     . HOH E 5 .   ? -20.73500 10.06000 15.53400  1.000 43.25606 ? 741 HOH A O     1 
HETATM 3094 O O     . HOH E 5 .   ? -33.59300 41.82600 -10.83000 1.000 50.26722 ? 742 HOH A O     1 
HETATM 3095 O O     . HOH E 5 .   ? -31.76100 -4.36300 -8.22900  1.000 40.46034 ? 743 HOH A O     1 
HETATM 3096 O O     . HOH E 5 .   ? -5.29200  30.61500 -2.27400  1.000 29.20356 ? 744 HOH A O     1 
HETATM 3097 O O     . HOH E 5 .   ? -10.693   -4.546   0.967     1.000 46.45272 ? 745 HOH A O     1 
HETATM 3098 O O     . HOH E 5 .   ? -13.16500 27.82600 1.09300   1.000 45.48290 ? 746 HOH A O     1 
HETATM 3099 O O     . HOH E 5 .   ? -34.12200 35.51000 3.26100   1.000 30.67987 ? 747 HOH A O     1 
HETATM 3100 O O     . HOH E 5 .   ? -27.62700 41.76000 -13.03700 1.000 36.88820 ? 748 HOH A O     1 
HETATM 3101 O O     . HOH E 5 .   ? -27.57700 16.11900 -24.19500 1.000 32.35761 ? 749 HOH A O     1 
HETATM 3102 O O     . HOH E 5 .   ? -29.51700 1.47400  12.93600  1.000 40.06322 ? 750 HOH A O     1 
HETATM 3103 O O     . HOH E 5 .   ? -13.72600 8.32100  1.49200   1.000 38.47485 ? 751 HOH A O     1 
HETATM 3104 O O     . HOH E 5 .   ? -40.87500 -3.28200 -2.84300  1.000 40.53219 ? 752 HOH A O     1 
HETATM 3105 O O     . HOH E 5 .   ? -32.03100 0.92900  10.38200  1.000 26.91022 ? 753 HOH A O     1 
HETATM 3106 O O     . HOH E 5 .   ? -31.31900 18.72600 20.60600  1.000 32.12471 ? 754 HOH A O     1 
HETATM 3107 O O     . HOH E 5 .   ? -13.90200 -2.60900 -6.96500  1.000 27.14697 ? 755 HOH A O     1 
HETATM 3108 O O     . HOH E 5 .   ? -23.80200 5.41100  -19.57400 1.000 41.13191 ? 756 HOH A O     1 
HETATM 3109 O O     . HOH E 5 .   ? -6.74700  39.35200 -2.93700  1.000 44.63006 ? 757 HOH A O     1 
HETATM 3110 O O     . HOH E 5 .   ? -14.10100 40.12200 -16.65400 1.000 36.02370 ? 758 HOH A O     1 
HETATM 3111 O O     . HOH E 5 .   ? -26.46600 35.77200 -18.52500 1.000 33.59923 ? 759 HOH A O     1 
HETATM 3112 O O     . HOH E 5 .   ? -29.35000 42.96600 -6.06900  1.000 37.77940 ? 760 HOH A O     1 
HETATM 3113 O O     . HOH E 5 .   ? -29.93700 35.61900 4.00600   1.000 26.27857 ? 761 HOH A O     1 
HETATM 3114 O O     . HOH E 5 .   ? -14.40600 27.73400 10.84200  1.000 32.10516 ? 762 HOH A O     1 
HETATM 3115 O O     . HOH E 5 .   ? -31.04600 8.98800  -15.85200 1.000 23.07528 ? 763 HOH A O     1 
HETATM 3116 O O     . HOH E 5 .   ? -3.36200  9.35000  -14.67300 1.000 41.87974 ? 764 HOH A O     1 
HETATM 3117 O O     . HOH E 5 .   ? -26.38300 29.47300 1.89700   1.000 17.60004 ? 765 HOH A O     1 
HETATM 3118 O O     . HOH E 5 .   ? -19.31400 25.85800 -27.74700 1.000 26.65567 ? 766 HOH A O     1 
HETATM 3119 O O     . HOH E 5 .   ? -23.27200 41.71100 -12.18500 1.000 23.48879 ? 767 HOH A O     1 
HETATM 3120 O O     . HOH E 5 .   ? -28.55900 44.48700 -10.45800 1.000 41.94185 ? 768 HOH A O     1 
HETATM 3121 O O     . HOH E 5 .   ? -13.53200 37.84900 12.55900  1.000 34.51895 ? 769 HOH A O     1 
HETATM 3122 O O     . HOH E 5 .   ? -9.08200  1.85200  -18.83100 1.000 52.51949 ? 770 HOH A O     1 
HETATM 3123 O O     . HOH E 5 .   ? -16.915   24.554   22.899    1.000 28.20334 ? 771 HOH A O     1 
HETATM 3124 O O     . HOH E 5 .   ? -12.36200 24.75600 -21.64800 1.000 20.36217 ? 772 HOH A O     1 
HETATM 3125 O O     . HOH E 5 .   ? -2.69800  4.92100  1.73600   1.000 53.65615 ? 773 HOH A O     1 
HETATM 3126 O O     . HOH E 5 .   ? -22.81600 0.57200  12.65800  1.000 39.60386 ? 774 HOH A O     1 
HETATM 3127 O O     . HOH E 5 .   ? 2.46800   36.00500 -8.10600  1.000 62.31872 ? 775 HOH A O     1 
HETATM 3128 O O     . HOH E 5 .   ? -9.70000  8.42100  -4.10100  1.000 47.81264 ? 776 HOH A O     1 
HETATM 3129 O O     . HOH E 5 .   ? -42.30300 35.51900 -6.36000  1.000 35.34820 ? 777 HOH A O     1 
HETATM 3130 O O     . HOH E 5 .   ? -3.62500  18.88500 -12.49600 1.000 26.23948 ? 778 HOH A O     1 
HETATM 3131 O O     . HOH E 5 .   ? -16.53200 3.73600  7.62400   1.000 33.99983 ? 779 HOH A O     1 
HETATM 3132 O O     . HOH E 5 .   ? -16.47400 42.25600 -1.30000  1.000 34.03605 ? 780 HOH A O     1 
HETATM 3133 O O     . HOH E 5 .   ? -37.23500 20.85700 -19.60600 1.000 45.75179 ? 781 HOH A O     1 
HETATM 3134 O O     . HOH E 5 .   ? -43.40000 9.52400  -4.88500  1.000 33.16340 ? 782 HOH A O     1 
HETATM 3135 O O     . HOH E 5 .   ? -16.63900 0.29300  -12.81500 1.000 42.19445 ? 783 HOH A O     1 
HETATM 3136 O O     . HOH E 5 .   ? -1.30600  29.93100 -18.16600 1.000 42.71139 ? 784 HOH A O     1 
HETATM 3137 O O     . HOH E 5 .   ? -17.75500 -3.29800 -3.68900  1.000 21.27436 ? 785 HOH A O     1 
HETATM 3138 O O     . HOH E 5 .   ? -29.72200 -2.24600 -4.15100  1.000 42.11268 ? 786 HOH A O     1 
HETATM 3139 O O     . HOH E 5 .   ? -20.76700 41.20800 11.89500  1.000 51.25317 ? 787 HOH A O     1 
HETATM 3140 O O     . HOH E 5 .   ? -39.26200 4.42300  14.32000  1.000 48.53914 ? 788 HOH A O     1 
HETATM 3141 O O     . HOH E 5 .   ? -40.25400 28.11800 4.14000   1.000 46.43359 ? 789 HOH A O     1 
HETATM 3142 O O     . HOH E 5 .   ? -21.65500 36.25800 15.90200  1.000 24.97111 ? 790 HOH A O     1 
HETATM 3143 O O     . HOH E 5 .   ? -13.79400 17.65700 -0.08000  1.000 44.35713 ? 791 HOH A O     1 
HETATM 3144 O O     . HOH E 5 .   ? -25.78600 42.84400 -12.55200 1.000 40.23004 ? 792 HOH A O     1 
HETATM 3145 O O     . HOH E 5 .   ? -0.46400  22.21600 -13.95000 1.000 21.63896 ? 793 HOH A O     1 
HETATM 3146 O O     . HOH E 5 .   ? -13.85000 -0.85100 -2.80900  1.000 45.65704 ? 794 HOH A O     1 
HETATM 3147 O O     . HOH E 5 .   ? -16.33900 27.98200 3.78400   1.000 45.60179 ? 795 HOH A O     1 
HETATM 3148 O O     . HOH E 5 .   ? -37.22000 14.29500 19.04400  1.000 36.34494 ? 796 HOH A O     1 
HETATM 3149 O O     . HOH E 5 .   ? -15.85800 20.63400 19.53400  1.000 42.68928 ? 797 HOH A O     1 
HETATM 3150 O O     . HOH E 5 .   ? -3.21200  34.87100 -9.36600  1.000 51.95802 ? 798 HOH A O     1 
HETATM 3151 O O     . HOH E 5 .   ? -45.55400 25.94300 7.05600   1.000 44.30094 ? 799 HOH A O     1 
HETATM 3152 O O     . HOH E 5 .   ? -14.75600 31.90700 4.96900   1.000 39.70235 ? 800 HOH A O     1 
HETATM 3153 O O     . HOH E 5 .   ? -19.49000 27.13100 0.45800   1.000 35.48771 ? 801 HOH A O     1 
HETATM 3154 O O     . HOH E 5 .   ? -8.09700  26.37100 -0.78200  1.000 35.69782 ? 802 HOH A O     1 
HETATM 3155 O O     . HOH E 5 .   ? -25.89000 5.03500  -15.77600 1.000 42.33506 ? 803 HOH A O     1 
HETATM 3156 O O     . HOH E 5 .   ? -5.34500  12.09900 3.90700   1.000 58.14706 ? 804 HOH A O     1 
HETATM 3157 O O     . HOH E 5 .   ? -15.41100 -2.69600 -2.55300  1.000 32.80009 ? 805 HOH A O     1 
HETATM 3158 O O     . HOH E 5 .   ? -38.87400 29.66500 4.84700   1.000 36.09901 ? 806 HOH A O     1 
HETATM 3159 O O     . HOH E 5 .   ? -39.14200 7.91300  3.96500   1.000 48.95178 ? 807 HOH A O     1 
HETATM 3160 O O     . HOH E 5 .   ? -21.10800 -2.60500 9.55000   1.000 27.37437 ? 808 HOH A O     1 
HETATM 3161 O O     . HOH E 5 .   ? -37.69700 29.70600 10.65500  1.000 36.22556 ? 809 HOH A O     1 
HETATM 3162 O O     . HOH E 5 .   ? -19.37800 5.15300  -21.29700 1.000 49.51717 ? 810 HOH A O     1 
HETATM 3163 O O     . HOH E 5 .   ? -27.61500 5.95200  -14.42600 1.000 49.62128 ? 811 HOH A O     1 
HETATM 3164 O O     . HOH E 5 .   ? -18.494   30.373   21.301    1.000 50.10247 ? 812 HOH A O     1 
HETATM 3165 O O     . HOH E 5 .   ? -44.92800 10.20500 -8.79000  1.000 42.19158 ? 813 HOH A O     1 
HETATM 3166 O O     . HOH E 5 .   ? -18.51000 4.46600  -19.37500 1.000 44.38147 ? 814 HOH A O     1 
HETATM 3167 O O     . HOH E 5 .   ? -27.76400 33.13200 -25.34500 1.000 36.73267 ? 815 HOH A O     1 
HETATM 3168 O O     . HOH E 5 .   ? -28.82600 7.44700  -16.01100 1.000 38.90650 ? 816 HOH A O     1 
HETATM 3169 O O     . HOH E 5 .   ? -42.48700 40.76400 -14.30700 1.000 55.11063 ? 817 HOH A O     1 
HETATM 3170 O O     . HOH E 5 .   ? -10.16200 1.47500  -4.04700  1.000 38.68683 ? 818 HOH A O     1 
HETATM 3171 O O     . HOH E 5 .   ? -24.04300 1.06600  -12.95700 1.000 52.01483 ? 819 HOH A O     1 
HETATM 3172 O O     . HOH E 5 .   ? 0.152     32.717   -15.481   1.000 41.24305 ? 820 HOH A O     1 
HETATM 3173 O O     . HOH E 5 .   ? -39.46200 28.48100 8.74100   1.000 58.99953 ? 821 HOH A O     1 
HETATM 3174 O O     . HOH E 5 .   ? -44.12200 25.08700 10.97200  1.000 34.92151 ? 822 HOH A O     1 
HETATM 3175 O O     . HOH E 5 .   ? -16.985   44.455   -3.769    1.000 33.43019 ? 823 HOH A O     1 
HETATM 3176 O O     . HOH E 5 .   ? -29.22000 39.61300 1.07300   1.000 35.43419 ? 824 HOH A O     1 
HETATM 3177 O O     . HOH E 5 .   ? -27.50600 44.82000 -7.92000  1.000 49.98828 ? 825 HOH A O     1 
HETATM 3178 O O     . HOH E 5 .   ? -34.76600 2.13000  -15.48500 1.000 52.14921 ? 826 HOH A O     1 
HETATM 3179 O O     . HOH E 5 .   ? -4.68600  33.52600 -13.34800 1.000 39.60821 ? 827 HOH A O     1 
HETATM 3180 O O     . HOH E 5 .   ? -40.70100 42.30600 -14.13400 1.000 54.04375 ? 828 HOH A O     1 
HETATM 3181 O O     . HOH E 5 .   ? -20.39400 28.32100 -28.60100 1.000 28.60785 ? 829 HOH A O     1 
HETATM 3182 O O     . HOH E 5 .   ? -5.647    19.433   -3.978    1.000 51.92196 ? 830 HOH A O     1 
HETATM 3183 O O     . HOH E 5 .   ? -14.187   -4.188   -4.730    1.000 42.29956 ? 831 HOH A O     1 
HETATM 3184 O O     . HOH E 5 .   ? -8.80300  33.56900 2.51100   1.000 41.45135 ? 832 HOH A O     1 
HETATM 3185 O O     . HOH E 5 .   ? -36.68700 30.60300 16.99200  1.000 54.67965 ? 833 HOH A O     1 
HETATM 3186 O O     . HOH E 5 .   ? -40.20000 6.78600  -5.96400  1.000 41.37624 ? 834 HOH A O     1 
HETATM 3187 O O     . HOH E 5 .   ? -37.26400 6.08000  3.98200   1.000 34.37996 ? 835 HOH A O     1 
HETATM 3188 O O     . HOH E 5 .   ? -35.65800 24.15200 -21.06600 1.000 59.21024 ? 836 HOH A O     1 
HETATM 3189 O O     . HOH E 5 .   ? -41.50600 24.51100 -16.63000 1.000 39.41351 ? 837 HOH A O     1 
HETATM 3190 O O     . HOH E 5 .   ? -41.85700 39.73300 -8.83800  1.000 61.26149 ? 838 HOH A O     1 
HETATM 3191 O O     . HOH E 5 .   ? -11.37200 -1.24400 -6.68600  1.000 42.14082 ? 839 HOH A O     1 
HETATM 3192 O O     . HOH E 5 .   ? -11.985   -1.299   7.999     1.000 56.28536 ? 840 HOH A O     1 
HETATM 3193 O O     . HOH E 5 .   ? -35.387   -0.637   6.756     1.000 41.00045 ? 841 HOH A O     1 
HETATM 3194 O O     . HOH E 5 .   ? -16.07000 9.40400  0.63000   1.000 30.35860 ? 842 HOH A O     1 
HETATM 3195 O O     . HOH E 5 .   ? -29.23700 31.31700 -26.80900 1.000 38.07570 ? 843 HOH A O     1 
HETATM 3196 O O     . HOH E 5 .   ? -31.64100 6.91800  -19.76200 1.000 47.43716 ? 844 HOH A O     1 
HETATM 3197 O O     . HOH E 5 .   ? -24.02700 36.79100 -19.74900 1.000 42.73913 ? 845 HOH A O     1 
HETATM 3198 O O     . HOH E 5 .   ? -14.42400 20.34300 17.41800  1.000 57.80563 ? 846 HOH A O     1 
HETATM 3199 O O     . HOH E 5 .   ? -44.03600 11.64700 -3.70900  1.000 53.56334 ? 847 HOH A O     1 
HETATM 3200 O O     . HOH E 5 .   ? -21.95000 31.51700 -27.26600 1.000 34.68236 ? 848 HOH A O     1 
HETATM 3201 O O     . HOH E 5 .   ? -25.76200 16.09300 20.28700  1.000 54.99217 ? 849 HOH A O     1 
HETATM 3202 O O     . HOH E 5 .   ? -38.44100 35.51000 -17.93200 1.000 43.63752 ? 850 HOH A O     1 
HETATM 3203 O O     . HOH E 5 .   ? -34.523   -0.069   11.218    1.000 26.77552 ? 851 HOH A O     1 
HETATM 3204 O O     . HOH E 5 .   ? -14.36400 18.17000 -25.75900 1.000 48.44468 ? 852 HOH A O     1 
HETATM 3205 O O     . HOH E 5 .   ? -41.06000 5.95200  15.10700  1.000 59.76744 ? 853 HOH A O     1 
HETATM 3206 O O     . HOH E 5 .   ? -44.57100 16.00000 -2.60600  1.000 37.24800 ? 854 HOH A O     1 
HETATM 3207 O O     . HOH E 5 .   ? -15.69200 41.22400 1.69300   1.000 58.46216 ? 855 HOH A O     1 
HETATM 3208 O O     . HOH E 5 .   ? -43.38700 13.80400 -2.09300  1.000 52.86037 ? 856 HOH A O     1 
HETATM 3209 O O     . HOH E 5 .   ? -16.12500 26.54300 7.55600   1.000 47.21698 ? 857 HOH A O     1 
HETATM 3210 O O     . HOH E 5 .   ? -41.30700 9.25000  -11.25800 1.000 34.99328 ? 858 HOH A O     1 
HETATM 3211 O O     . HOH E 5 .   ? -43.38400 9.95000  2.64900   1.000 37.86759 ? 859 HOH A O     1 
HETATM 3212 O O     . HOH E 5 .   ? -5.62400  35.89000 -12.22900 1.000 54.85447 ? 860 HOH A O     1 
HETATM 3213 O O     . HOH E 5 .   ? -12.64200 8.17000  3.67300   1.000 42.18800 ? 861 HOH A O     1 
HETATM 3214 O O     . HOH E 5 .   ? -27.40000 37.56300 -16.70600 1.000 34.39945 ? 862 HOH A O     1 
HETATM 3215 O O     . HOH E 5 .   ? -30.35600 32.59600 16.37000  1.000 35.54351 ? 863 HOH A O     1 
HETATM 3216 O O     . HOH E 5 .   ? -5.68800  10.66500 -27.55100 1.000 65.30352 ? 864 HOH A O     1 
HETATM 3217 O O     . HOH E 5 .   ? -34.98600 21.27200 -21.38600 1.000 50.63011 ? 865 HOH A O     1 
HETATM 3218 O O     . HOH E 5 .   ? -25.05100 33.62100 -25.83700 1.000 31.53209 ? 866 HOH A O     1 
HETATM 3219 O O     . HOH E 5 .   ? -42.15600 9.17800  -8.66400  1.000 31.65594 ? 867 HOH A O     1 
HETATM 3220 O O     . HOH E 5 .   ? -34.71000 35.81000 -20.68000 1.000 42.02881 ? 868 HOH A O     1 
HETATM 3221 O O     . HOH E 5 .   ? -35.23300 36.67300 0.89700   1.000 58.40883 ? 869 HOH A O     1 
HETATM 3222 O O     . HOH E 5 .   ? -24.51000 1.93400  11.32700  1.000 49.30662 ? 870 HOH A O     1 
HETATM 3223 O O     . HOH E 5 .   ? -7.35100  39.54700 -7.29600  1.000 46.73413 ? 871 HOH A O     1 
HETATM 3224 O O     . HOH E 5 .   ? -32.23300 1.90000  -17.12300 1.000 47.95875 ? 872 HOH A O     1 
HETATM 3225 O O     . HOH E 5 .   ? -40.31100 30.03000 -0.13900  1.000 43.56148 ? 873 HOH A O     1 
HETATM 3226 O O     . HOH E 5 .   ? -37.70800 3.62200  6.79000   1.000 41.89928 ? 874 HOH A O     1 
HETATM 3227 O O     . HOH E 5 .   ? -36.77900 3.57700  1.56900   1.000 38.35179 ? 875 HOH A O     1 
HETATM 3228 O O     . HOH E 5 .   ? -39.35800 17.46400 17.83900  1.000 59.28483 ? 876 HOH A O     1 
HETATM 3229 O O     . HOH E 5 .   ? -25.18500 32.41700 19.62000  1.000 34.49684 ? 877 HOH A O     1 
HETATM 3230 O O     . HOH E 5 .   ? -36.52500 39.21300 -17.88500 1.000 61.10054 ? 878 HOH A O     1 
HETATM 3231 O O     . HOH E 5 .   ? -46.60300 17.25400 2.22000   1.000 37.28762 ? 879 HOH A O     1 
HETATM 3232 O O     . HOH E 5 .   ? -5.54000  7.43900  -8.30600  1.000 45.01947 ? 880 HOH A O     1 
HETATM 3233 O O     . HOH E 5 .   ? -34.44000 26.57800 -22.37800 1.000 51.94690 ? 881 HOH A O     1 
HETATM 3234 O O     . HOH E 5 .   ? -32.49500 7.81100  -17.69400 1.000 34.87035 ? 882 HOH A O     1 
HETATM 3235 O O     . HOH E 5 .   ? -23.454   16.371   -28.366   1.000 59.51762 ? 883 HOH A O     1 
HETATM 3236 O O     . HOH E 5 .   ? -37.39700 16.47800 18.24700  1.000 47.15455 ? 884 HOH A O     1 
HETATM 3237 O O     . HOH E 5 .   ? -1.70100  18.51800 -10.61100 1.000 39.37750 ? 885 HOH A O     1 
HETATM 3238 O O     . HOH E 5 .   ? -22.502   -1.918   13.549    1.000 39.32010 ? 886 HOH A O     1 
HETATM 3239 O O     . HOH E 5 .   ? -4.045    26.426   -1.411    1.000 45.03700 ? 887 HOH A O     1 
HETATM 3240 O O     . HOH E 5 .   ? -32.43100 31.18900 20.09500  1.000 52.80384 ? 888 HOH A O     1 
HETATM 3241 O O     . HOH E 5 .   ? -13.44900 33.93100 3.65000   1.000 37.93483 ? 889 HOH A O     1 
HETATM 3242 O O     . HOH E 5 .   ? -39.71000 34.67000 13.07600  1.000 53.56251 ? 890 HOH A O     1 
HETATM 3243 O O     . HOH E 5 .   ? -14.42300 36.39200 2.50100   1.000 30.76539 ? 891 HOH A O     1 
HETATM 3244 O O     . HOH E 5 .   ? -36.25400 27.83500 -21.26600 1.000 54.57791 ? 892 HOH A O     1 
HETATM 3245 O O     . HOH E 5 .   ? -16.72900 30.10400 5.33000   1.000 34.75023 ? 893 HOH A O     1 
HETATM 3246 O O     . HOH E 5 .   ? -7.96600  40.85500 -5.19000  1.000 41.59269 ? 894 HOH A O     1 
HETATM 3247 O O     . HOH E 5 .   ? -11.25400 28.30300 -24.53400 1.000 39.55443 ? 895 HOH A O     1 
HETATM 3248 O O     . HOH E 5 .   ? -2.32800  19.70000 -14.61200 1.000 27.51613 ? 896 HOH A O     1 
HETATM 3249 O O     . HOH E 5 .   ? -43.56300 24.82700 8.30100   1.000 39.55600 ? 897 HOH A O     1 
HETATM 3250 O O     . HOH E 5 .   ? -2.53800  15.78800 -5.85700  1.000 58.28789 ? 898 HOH A O     1 
HETATM 3251 O O     . HOH E 5 .   ? -11.627   39.988   10.432    1.000 52.32805 ? 899 HOH A O     1 
HETATM 3252 O O     . HOH E 5 .   ? -28.54400 35.32700 -24.03300 1.000 43.75886 ? 900 HOH A O     1 
HETATM 3253 O O     . HOH E 5 .   ? -12.490   30.075   23.937    1.000 57.17122 ? 901 HOH A O     1 
HETATM 3254 O O     . HOH E 5 .   ? -26.28100 39.15000 4.01400   1.000 22.61543 ? 902 HOH A O     1 
HETATM 3255 O O     . HOH E 5 .   ? -20.58300 38.53400 14.95200  1.000 36.27463 ? 903 HOH A O     1 
HETATM 3256 O O     . HOH E 5 .   ? -5.82200  28.35500 -0.98600  1.000 43.75162 ? 904 HOH A O     1 
HETATM 3257 O O     . HOH E 5 .   ? -29.84500 5.42600  -17.35800 1.000 48.79318 ? 905 HOH A O     1 
HETATM 3258 O O     . HOH E 5 .   ? -42.25400 21.27000 -14.97700 1.000 36.21841 ? 906 HOH A O     1 
HETATM 3259 O O     . HOH E 5 .   ? -42.93000 14.55900 1.86200   1.000 28.21197 ? 907 HOH A O     1 
HETATM 3260 O O     . HOH E 5 .   ? -29.296   47.319   -6.230    1.000 45.51382 ? 908 HOH A O     1 
HETATM 3261 O O     . HOH E 5 .   ? -26.901   0.885    12.268    1.000 35.66581 ? 909 HOH A O     1 
HETATM 3262 O O     . HOH E 5 .   ? -14.63600 5.52600  7.47400   1.000 52.65427 ? 910 HOH A O     1 
HETATM 3263 O O     . HOH E 5 .   ? -44.76500 20.76000 -14.04200 1.000 52.72009 ? 911 HOH A O     1 
HETATM 3264 O O     . HOH E 5 .   ? -39.88200 31.86600 6.02800   1.000 47.85517 ? 912 HOH A O     1 
HETATM 3265 O O     . HOH E 5 .   ? -13.03800 26.47500 -23.45200 1.000 27.11638 ? 913 HOH A O     1 
HETATM 3266 O O     . HOH E 5 .   ? -11.30400 -0.89200 -4.14800  1.000 41.84652 ? 914 HOH A O     1 
HETATM 3267 O O     . HOH E 5 .   ? -30.92600 0.23600  14.93900  1.000 35.79911 ? 915 HOH A O     1 
HETATM 3268 O O     . HOH E 5 .   ? -27.60900 39.97000 -18.13800 1.000 50.74399 ? 916 HOH A O     1 
HETATM 3269 O O     . HOH E 5 .   ? -10.32000 31.52500 -25.50300 1.000 55.88642 ? 917 HOH A O     1 
HETATM 3270 O O     . HOH E 5 .   ? -37.99100 36.38100 1.07700   1.000 53.03103 ? 918 HOH A O     1 
HETATM 3271 O O     . HOH E 5 .   ? -8.09700  44.59500 -9.07800  1.000 36.23779 ? 919 HOH A O     1 
HETATM 3272 O O     . HOH E 5 .   ? -30.26300 46.39900 -9.96200  1.000 50.88788 ? 920 HOH A O     1 
HETATM 3273 O O     . HOH E 5 .   ? -18.21000 44.80700 -14.34200 1.000 36.92533 ? 921 HOH A O     1 
HETATM 3274 O O     . HOH E 5 .   ? -39.99700 35.44500 0.07900   1.000 51.85918 ? 922 HOH A O     1 
HETATM 3275 O O     . HOH E 5 .   ? -40.01400 34.52400 5.46500   1.000 52.62390 ? 923 HOH A O     1 
HETATM 3276 O O     . HOH E 5 .   ? -39.06600 36.21100 4.12300   1.000 46.43378 ? 924 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . ASN A 16  ? 0.26030 0.40297 0.45028 0.01820  0.08742  0.03540  10  ASN A N     
2    C CA    . ASN A 16  ? 0.24376 0.37754 0.40071 0.03624  0.08572  0.02065  10  ASN A CA    
3    C C     . ASN A 16  ? 0.25405 0.36550 0.37461 0.05857  0.06172  0.02995  10  ASN A C     
4    O O     . ASN A 16  ? 0.26153 0.36679 0.35979 0.06788  0.06305  0.00616  10  ASN A O     
5    C CB    . ASN A 16  ? 0.22234 0.37937 0.39971 0.01918  0.07916  -0.00105 10  ASN A CB    
6    C CG    . ASN A 16  ? 0.21695 0.39534 0.39631 0.00505  0.02804  0.00192  10  ASN A CG    
7    O OD1   . ASN A 16  ? 0.19560 0.39520 0.37730 0.01006  0.00377  0.00542  10  ASN A OD1   
8    N ND2   . ASN A 16  ? 0.23001 0.40724 0.43325 0.01146  0.01413  -0.01954 10  ASN A ND2   
9    N N     . PRO A 17  ? 0.24759 0.34182 0.33399 0.06528  0.02894  0.04858  11  PRO A N     
10   C CA    . PRO A 17  ? 0.23183 0.32142 0.31668 0.05458  0.03955  0.03804  11  PRO A CA    
11   C C     . PRO A 17  ? 0.21322 0.29287 0.27647 0.02917  0.05819  -0.00474 11  PRO A C     
12   O O     . PRO A 17  ? 0.19487 0.28816 0.31216 0.01511  0.04718  0.02751  11  PRO A O     
13   C CB    . PRO A 17  ? 0.24516 0.32786 0.31920 0.06134  -0.00011 0.03509  11  PRO A CB    
14   C CG    . PRO A 17  ? 0.25785 0.33961 0.33138 0.05819  -0.01708 0.05000  11  PRO A CG    
15   C CD    . PRO A 17  ? 0.25878 0.34668 0.34174 0.06247  0.00083  0.02750  11  PRO A CD    
16   N N     . LEU A 18  ? 0.21267 0.28298 0.24168 0.02164  0.04890  -0.03921 12  LEU A N     
17   C CA    . LEU A 18  ? 0.20467 0.25710 0.27315 0.01180  0.05916  -0.01205 12  LEU A CA    
18   C C     . LEU A 18  ? 0.20154 0.24481 0.27870 0.00666  0.06405  -0.00350 12  LEU A C     
19   O O     . LEU A 18  ? 0.20987 0.24031 0.30940 0.03665  0.08298  -0.00496 12  LEU A O     
20   C CB    . LEU A 18  ? 0.19116 0.24861 0.25325 -0.01077 0.05353  -0.02536 12  LEU A CB    
21   C CG    . LEU A 18  ? 0.19873 0.24693 0.27248 -0.02506 0.05389  -0.01035 12  LEU A CG    
22   C CD1   . LEU A 18  ? 0.19566 0.22587 0.28086 -0.03572 0.05991  -0.01378 12  LEU A CD1   
23   C CD2   . LEU A 18  ? 0.20445 0.23870 0.23116 -0.02624 0.04768  0.03616  12  LEU A CD2   
24   N N     . PHE A 19  ? 0.20944 0.25048 0.29067 -0.00771 0.07707  0.01305  13  PHE A N     
25   C CA    . PHE A 19  ? 0.23021 0.25051 0.27545 -0.00762 0.06112  -0.01596 13  PHE A CA    
26   C C     . PHE A 19  ? 0.26119 0.29505 0.30626 0.00472  0.05264  -0.01339 13  PHE A C     
27   O O     . PHE A 19  ? 0.28678 0.30938 0.33440 0.00501  0.05360  0.00086  13  PHE A O     
28   C CB    . PHE A 19  ? 0.22890 0.24719 0.32651 -0.02013 0.04996  -0.02367 13  PHE A CB    
29   C CG    . PHE A 19  ? 0.24226 0.25774 0.38376 -0.03509 0.07262  -0.02074 13  PHE A CG    
30   C CD1   . PHE A 19  ? 0.24092 0.25981 0.42195 -0.04604 0.07206  -0.02577 13  PHE A CD1   
31   C CD2   . PHE A 19  ? 0.23890 0.26303 0.40642 -0.04475 0.11017  -0.01481 13  PHE A CD2   
32   C CE1   . PHE A 19  ? 0.25582 0.25930 0.45739 -0.03942 0.07839  -0.01797 13  PHE A CE1   
33   C CE2   . PHE A 19  ? 0.24323 0.25888 0.43271 -0.04803 0.13175  -0.02157 13  PHE A CE2   
34   C CZ    . PHE A 19  ? 0.24776 0.25549 0.43421 -0.03170 0.10350  -0.03856 13  PHE A CZ    
35   N N     . SER A 20  ? 0.27643 0.30338 0.27182 0.01483  0.06334  -0.02128 14  SER A N     
36   C CA    . SER A 20  ? 0.30216 0.32390 0.32247 0.00923  0.04009  -0.01491 14  SER A CA    
37   C C     . SER A 20  ? 0.29126 0.33231 0.27076 -0.01904 0.03017  -0.01122 14  SER A C     
38   O O     . SER A 20  ? 0.28063 0.34730 0.28119 -0.02587 -0.00370 -0.01598 14  SER A O     
39   C CB    . SER A 20  ? 0.34606 0.35562 0.36178 0.03607  0.05670  0.02930  14  SER A CB    
40   O OG    . SER A 20  ? 0.37160 0.37146 0.40330 0.05458  0.07407  0.06002  14  SER A OG    
41   N N     . PRO A 21  ? 0.28917 0.33602 0.26025 -0.01623 0.00954  -0.01217 15  PRO A N     
42   C CA    . PRO A 21  ? 0.28822 0.32642 0.24670 -0.01120 0.00907  -0.01571 15  PRO A CA    
43   C C     . PRO A 21  ? 0.26521 0.28730 0.28927 -0.01848 0.03181  -0.00536 15  PRO A C     
44   O O     . PRO A 21  ? 0.27278 0.27028 0.33593 0.00740  0.06619  -0.02058 15  PRO A O     
45   C CB    . PRO A 21  ? 0.30674 0.34548 0.25489 0.00584  0.01796  -0.02400 15  PRO A CB    
46   C CG    . PRO A 21  ? 0.31184 0.36089 0.31922 0.00368  -0.01089 -0.03690 15  PRO A CG    
47   C CD    . PRO A 21  ? 0.29625 0.35276 0.28821 -0.00631 -0.00537 -0.03840 15  PRO A CD    
48   N N     . TYR A 22  ? 0.23537 0.27148 0.24837 -0.03229 0.00590  0.01867  16  TYR A N     
49   C CA    . TYR A 22  ? 0.23036 0.26004 0.23949 -0.02915 0.00836  0.02533  16  TYR A CA    
50   C C     . TYR A 22  ? 0.25740 0.26214 0.27351 -0.03705 0.00509  0.02641  16  TYR A C     
51   O O     . TYR A 22  ? 0.27001 0.25155 0.34331 -0.02008 0.01735  0.03146  16  TYR A O     
52   C CB    . TYR A 22  ? 0.21347 0.25849 0.26481 -0.02497 0.00642  0.02827  16  TYR A CB    
53   C CG    . TYR A 22  ? 0.19336 0.25448 0.22303 -0.01440 0.02785  0.02001  16  TYR A CG    
54   C CD1   . TYR A 22  ? 0.18449 0.25078 0.25982 -0.00596 0.01387  0.01294  16  TYR A CD1   
55   C CD2   . TYR A 22  ? 0.18007 0.27018 0.28305 -0.00603 0.01797  0.03255  16  TYR A CD2   
56   C CE1   . TYR A 22  ? 0.19156 0.26902 0.24954 0.03059  0.02384  0.02087  16  TYR A CE1   
57   C CE2   . TYR A 22  ? 0.18178 0.27664 0.30553 0.01913  0.02289  0.03412  16  TYR A CE2   
58   C CZ    . TYR A 22  ? 0.18240 0.26271 0.27329 0.03022  0.03936  0.02760  16  TYR A CZ    
59   O OH    . TYR A 22  ? 0.18921 0.25297 0.27303 0.03217  0.02198  0.02846  16  TYR A OH    
60   N N     . LYS A 23  ? 0.26548 0.27336 0.25079 -0.05614 -0.03494 0.00283  17  LYS A N     
61   C CA    . LYS A 23  ? 0.29219 0.31645 0.26429 -0.04557 -0.04321 -0.00396 17  LYS A CA    
62   C C     . LYS A 23  ? 0.29375 0.32887 0.27504 -0.05774 -0.01701 -0.02974 17  LYS A C     
63   O O     . LYS A 23  ? 0.30555 0.33161 0.31447 -0.07274 0.00868  -0.00839 17  LYS A O     
64   C CB    . LYS A 23  ? 0.32471 0.36051 0.31405 -0.03567 -0.05863 -0.00089 17  LYS A CB    
65   C CG    . LYS A 23  ? 0.37377 0.40460 0.32934 -0.00917 -0.05436 0.01132  17  LYS A CG    
66   C CD    . LYS A 23  ? 0.40980 0.44684 0.41017 -0.00860 -0.05864 0.01150  17  LYS A CD    
67   C CE    . LYS A 23  ? 0.43266 0.47238 0.47682 -0.00254 -0.06934 0.03185  17  LYS A CE    
68   N NZ    . LYS A 23  ? 0.44610 0.47095 0.51292 -0.00111 -0.06706 0.06514  17  LYS A NZ    
69   N N     . MET A 24  ? 0.26798 0.34553 0.28680 -0.03341 -0.02080 -0.02441 18  MET A N     
70   C CA    . MET A 24  ? 0.25380 0.37081 0.24055 -0.02593 0.01153  -0.02991 18  MET A CA    
71   C C     . MET A 24  ? 0.26448 0.39064 0.29637 -0.01749 0.03318  -0.04045 18  MET A C     
72   O O     . MET A 24  ? 0.26946 0.39881 0.36016 -0.00237 0.02839  -0.05864 18  MET A O     
73   C CB    . MET A 24  ? 0.26334 0.40012 0.21144 -0.03295 -0.00238 -0.03239 18  MET A CB    
74   C CG    . MET A 24  ? 0.24707 0.41361 0.21405 -0.03671 -0.03583 -0.05884 18  MET A CG    
75   S SD    . MET A 24  ? 0.23922 0.44260 0.25623 -0.02453 -0.00151 -0.05861 18  MET A SD    
76   C CE    . MET A 24  ? 0.25424 0.44121 0.30991 -0.02769 -0.02702 -0.09841 18  MET A CE    
77   N N     . GLY A 25  ? 0.25824 0.38448 0.29279 -0.03083 0.04706  -0.04671 19  GLY A N     
78   C CA    . GLY A 25  ? 0.25650 0.37821 0.30570 -0.04004 0.04667  -0.04685 19  GLY A CA    
79   C C     . GLY A 25  ? 0.24848 0.36879 0.33413 -0.05512 0.05491  -0.06150 19  GLY A C     
80   O O     . GLY A 25  ? 0.27017 0.39414 0.32208 -0.05218 0.05396  -0.08017 19  GLY A O     
81   N N     . LYS A 26  ? 0.22817 0.34665 0.38193 -0.06579 0.05443  -0.04933 20  LYS A N     
82   C CA    . LYS A 26  ? 0.22272 0.33747 0.36646 -0.04327 0.04552  -0.04853 20  LYS A CA    
83   C C     . LYS A 26  ? 0.23078 0.33439 0.31319 -0.03692 0.02564  -0.05176 20  LYS A C     
84   O O     . LYS A 26  ? 0.23818 0.37935 0.35302 -0.05091 -0.01827 -0.01010 20  LYS A O     
85   C CB    . LYS A 26  ? 0.22834 0.34622 0.41154 -0.04066 0.07305  -0.00970 20  LYS A CB    
86   N N     . PHE A 27  ? 0.22001 0.30529 0.28657 -0.02797 0.02694  -0.05174 21  PHE A N     
87   C CA    . PHE A 27  ? 0.24412 0.31128 0.30167 -0.04004 0.01660  -0.06759 21  PHE A CA    
88   C C     . PHE A 27  ? 0.25727 0.30937 0.27971 -0.03157 0.01457  -0.04283 21  PHE A C     
89   O O     . PHE A 27  ? 0.27646 0.32000 0.30872 -0.03534 0.03047  0.00060  21  PHE A O     
90   C CB    . PHE A 27  ? 0.24712 0.31012 0.26913 -0.05503 0.01955  -0.10591 21  PHE A CB    
91   C CG    . PHE A 27  ? 0.25589 0.29531 0.26985 -0.06656 0.01297  -0.11073 21  PHE A CG    
92   C CD1   . PHE A 27  ? 0.27121 0.29227 0.29444 -0.06845 0.03249  -0.09788 21  PHE A CD1   
93   C CD2   . PHE A 27  ? 0.26685 0.30122 0.27112 -0.05403 0.01086  -0.10844 21  PHE A CD2   
94   C CE1   . PHE A 27  ? 0.27433 0.27716 0.28439 -0.06242 0.06058  -0.09740 21  PHE A CE1   
95   C CE2   . PHE A 27  ? 0.27184 0.29754 0.30072 -0.06152 0.02162  -0.09800 21  PHE A CE2   
96   C CZ    . PHE A 27  ? 0.27798 0.28409 0.31640 -0.06187 0.02826  -0.09749 21  PHE A CZ    
97   N N     . ASN A 28  ? 0.24790 0.31071 0.23747 -0.02677 -0.01381 -0.02796 22  ASN A N     
98   C CA    . ASN A 28  ? 0.24110 0.29891 0.21383 -0.03998 -0.04275 -0.03244 22  ASN A CA    
99   C C     . ASN A 28  ? 0.21428 0.26818 0.28361 -0.05197 -0.03620 0.01397  22  ASN A C     
100  O O     . ASN A 28  ? 0.22345 0.27483 0.37522 -0.04414 -0.04499 0.04352  22  ASN A O     
101  C CB    . ASN A 28  ? 0.27172 0.32209 0.21995 -0.04540 -0.06516 -0.02472 22  ASN A CB    
102  C CG    . ASN A 28  ? 0.31175 0.35127 0.33754 -0.03607 -0.08096 -0.02813 22  ASN A CG    
103  O OD1   . ASN A 28  ? 0.32007 0.34209 0.36242 -0.03858 -0.07382 -0.03163 22  ASN A OD1   
104  N ND2   . ASN A 28  ? 0.33919 0.37526 0.39042 -0.02428 -0.10430 -0.02082 22  ASN A ND2   
105  N N     . LEU A 29  ? 0.19258 0.23846 0.26328 -0.05462 -0.00886 0.01047  23  LEU A N     
106  C CA    . LEU A 29  ? 0.18933 0.23969 0.19181 -0.03203 0.01451  -0.02405 23  LEU A CA    
107  C C     . LEU A 29  ? 0.20373 0.24685 0.22154 -0.04243 0.03417  -0.00566 23  LEU A C     
108  O O     . LEU A 29  ? 0.24312 0.25658 0.24335 -0.03939 0.06981  -0.00851 23  LEU A O     
109  C CB    . LEU A 29  ? 0.18065 0.24794 0.21640 0.01430  0.01674  -0.01988 23  LEU A CB    
110  C CG    . LEU A 29  ? 0.16445 0.24769 0.25468 0.03829  0.03678  -0.01136 23  LEU A CG    
111  C CD1   . LEU A 29  ? 0.13956 0.24678 0.26018 0.02335  0.05216  0.02227  23  LEU A CD1   
112  C CD2   . LEU A 29  ? 0.16748 0.24210 0.27006 0.06049  0.01554  0.00721  23  LEU A CD2   
113  N N     . SER A 30  ? 0.18432 0.24468 0.23234 -0.05549 0.04653  0.01823  24  SER A N     
114  C CA    . SER A 30  ? 0.21304 0.24164 0.25636 -0.03498 0.06726  -0.00594 24  SER A CA    
115  C C     . SER A 30  ? 0.20000 0.23671 0.26034 -0.00389 0.05959  -0.01859 24  SER A C     
116  O O     . SER A 30  ? 0.20524 0.24003 0.24279 0.00760  0.06385  -0.03187 24  SER A O     
117  C CB    . SER A 30  ? 0.25602 0.23388 0.32893 -0.05384 0.11573  -0.03781 24  SER A CB    
118  O OG    . SER A 30  ? 0.29582 0.28097 0.42978 -0.04461 0.08276  0.00372  24  SER A OG    
119  N N     . HIS A 31  ? 0.18578 0.22763 0.24255 0.01023  0.02710  0.00613  25  HIS A N     
120  C CA    . HIS A 31  ? 0.18093 0.22411 0.19108 -0.00800 -0.01253 -0.00815 25  HIS A CA    
121  C C     . HIS A 31  ? 0.17195 0.22507 0.17922 -0.00032 0.02860  -0.00428 25  HIS A C     
122  O O     . HIS A 31  ? 0.17335 0.23129 0.19575 0.02050  0.06468  -0.02101 25  HIS A O     
123  C CB    . HIS A 31  ? 0.16125 0.23378 0.20622 -0.01653 0.00146  -0.00509 25  HIS A CB    
124  C CG    . HIS A 31  ? 0.15252 0.24328 0.24771 -0.00733 -0.00398 -0.00772 25  HIS A CG    
125  N ND1   . HIS A 31  ? 0.13497 0.25043 0.24966 0.00668  -0.01539 -0.01221 25  HIS A ND1   
126  C CD2   . HIS A 31  ? 0.14602 0.24224 0.23438 -0.00504 -0.01119 0.00692  25  HIS A CD2   
127  C CE1   . HIS A 31  ? 0.13558 0.26080 0.24327 -0.01908 0.00418  0.00712  25  HIS A CE1   
128  N NE2   . HIS A 31  ? 0.12940 0.25769 0.25413 -0.02481 0.02227  0.02150  25  HIS A NE2   
129  N N     . ARG A 32  ? 0.17859 0.21790 0.19719 -0.00396 0.01338  0.01258  26  ARG A N     
130  C CA    . ARG A 32  ? 0.19652 0.19724 0.19264 0.01446  0.01584  0.00411  26  ARG A CA    
131  C C     . ARG A 32  ? 0.15680 0.20757 0.18992 0.01112  -0.02463 -0.00955 26  ARG A C     
132  O O     . ARG A 32  ? 0.15580 0.21266 0.19202 0.02741  0.01682  -0.03192 26  ARG A O     
133  C CB    . ARG A 32  ? 0.22316 0.20054 0.23225 0.01362  0.03524  -0.00669 26  ARG A CB    
134  C CG    . ARG A 32  ? 0.24890 0.22754 0.27412 0.01361  0.03269  -0.02702 26  ARG A CG    
135  C CD    . ARG A 32  ? 0.25101 0.26704 0.29033 -0.00437 0.03885  -0.04490 26  ARG A CD    
136  N NE    . ARG A 32  ? 0.25387 0.27771 0.30629 -0.03496 0.03781  -0.03310 26  ARG A NE    
137  C CZ    . ARG A 32  ? 0.21576 0.29098 0.28427 -0.03763 0.04331  -0.04423 26  ARG A CZ    
138  N NH1   . ARG A 32  ? 0.20461 0.29914 0.25866 -0.03405 0.03836  -0.04380 26  ARG A NH1   
139  N NH2   . ARG A 32  ? 0.22455 0.30081 0.27425 -0.02745 0.04147  -0.04667 26  ARG A NH2   
140  N N     . VAL A 33  ? 0.11914 0.20379 0.23795 -0.00425 -0.00596 0.00147  27  VAL A N     
141  C CA    . VAL A 33  ? 0.11779 0.21338 0.27343 -0.00154 0.00080  -0.01976 27  VAL A CA    
142  C C     . VAL A 33  ? 0.11828 0.20310 0.23884 0.00546  0.01123  -0.01671 27  VAL A C     
143  O O     . VAL A 33  ? 0.16379 0.21785 0.25444 0.01043  -0.00374 0.01996  27  VAL A O     
144  C CB    . VAL A 33  ? 0.10005 0.20502 0.31292 -0.00403 0.01430  -0.04300 27  VAL A CB    
145  C CG1   . VAL A 33  ? 0.11190 0.21452 0.30468 0.02206  0.01315  -0.04327 27  VAL A CG1   
146  C CG2   . VAL A 33  ? 0.09983 0.22162 0.34953 0.00230  0.03563  -0.04282 27  VAL A CG2   
147  N N     . VAL A 34  ? 0.10266 0.18225 0.24362 0.00027  0.01275  0.00160  28  VAL A N     
148  C CA    . VAL A 34  ? 0.08663 0.15020 0.24838 0.00174  0.04429  -0.02754 28  VAL A CA    
149  C C     . VAL A 34  ? 0.08764 0.13678 0.22848 -0.02109 0.00275  -0.04402 28  VAL A C     
150  O O     . VAL A 34  ? 0.08697 0.17251 0.26066 -0.01799 -0.01566 -0.01808 28  VAL A O     
151  C CB    . VAL A 34  ? 0.08463 0.13659 0.25461 0.01701  0.04520  -0.00203 28  VAL A CB    
152  C CG1   . VAL A 34  ? 0.08990 0.14548 0.25273 0.01215  0.05735  0.00712  28  VAL A CG1   
153  C CG2   . VAL A 34  ? 0.09385 0.13664 0.25130 0.02698  0.02452  -0.04744 28  VAL A CG2   
154  N N     . LEU A 35  ? 0.11776 0.14250 0.23646 -0.00589 0.01065  -0.04076 29  LEU A N     
155  C CA    . LEU A 35  ? 0.10650 0.14518 0.22199 0.00266  0.01103  -0.02568 29  LEU A CA    
156  C C     . LEU A 35  ? 0.10166 0.18717 0.21248 0.01400  0.00542  0.00305  29  LEU A C     
157  O O     . LEU A 35  ? 0.08060 0.21364 0.23426 0.02664  0.00025  0.00928  29  LEU A O     
158  C CB    . LEU A 35  ? 0.11124 0.13848 0.25571 0.03019  0.00790  -0.02522 29  LEU A CB    
159  C CG    . LEU A 35  ? 0.07849 0.15662 0.25994 0.00803  -0.01423 -0.00228 29  LEU A CG    
160  C CD1   . LEU A 35  ? 0.08077 0.17324 0.29348 -0.01715 -0.00328 -0.02677 29  LEU A CD1   
161  C CD2   . LEU A 35  ? 0.08186 0.18769 0.25956 0.01930  0.00709  0.00737  29  LEU A CD2   
162  N N     . ALA A 36  ? 0.10212 0.17251 0.17741 0.00206  0.00601  -0.00600 30  ALA A N     
163  C CA    . ALA A 36  ? 0.09557 0.17653 0.19338 0.00251  0.00055  0.02033  30  ALA A CA    
164  C C     . ALA A 36  ? 0.09445 0.18563 0.22920 -0.00785 0.02109  0.01517  30  ALA A C     
165  O O     . ALA A 36  ? 0.10398 0.20724 0.18783 0.00669  0.00475  0.02705  30  ALA A O     
166  C CB    . ALA A 36  ? 0.12093 0.19441 0.20503 -0.00401 -0.02560 0.05093  30  ALA A CB    
167  N N     . PRO A 37  ? 0.09247 0.19191 0.24931 -0.01526 0.01328  -0.00480 31  PRO A N     
168  C CA    . PRO A 37  ? 0.06473 0.18519 0.22770 -0.01573 0.00452  -0.02555 31  PRO A CA    
169  C C     . PRO A 37  ? 0.08575 0.19419 0.20059 0.01590  0.00343  -0.03151 31  PRO A C     
170  O O     . PRO A 37  ? 0.11488 0.21393 0.23894 0.03501  -0.04258 -0.02028 31  PRO A O     
171  C CB    . PRO A 37  ? 0.10550 0.19006 0.22038 -0.01372 0.02490  0.04171  31  PRO A CB    
172  C CG    . PRO A 37  ? 0.09954 0.19124 0.23737 -0.01827 0.02742  0.01616  31  PRO A CG    
173  C CD    . PRO A 37  ? 0.09185 0.20263 0.20622 -0.02631 0.03698  0.00305  31  PRO A CD    
174  N N     . MET A 38  ? 0.08626 0.19605 0.23009 0.01369  -0.02589 -0.01308 32  MET A N     
175  C CA    . MET A 38  ? 0.09162 0.18657 0.24950 0.00814  0.00358  -0.03955 32  MET A CA    
176  C C     . MET A 38  ? 0.10573 0.18160 0.26422 0.01865  0.02132  -0.03416 32  MET A C     
177  O O     . MET A 38  ? 0.11257 0.18695 0.22873 0.01659  0.00130  -0.03364 32  MET A O     
178  C CB    . MET A 38  ? 0.07641 0.20707 0.26559 -0.01391 0.02221  0.00321  32  MET A CB    
179  C CG    . MET A 38  ? 0.09628 0.21545 0.25143 -0.02548 0.00732  -0.00005 32  MET A CG    
180  S SD    . MET A 38  ? 0.12839 0.23116 0.25082 -0.01657 0.00266  -0.00679 32  MET A SD    
181  C CE    . MET A 38  ? 0.13173 0.24556 0.28853 -0.01287 0.01264  -0.03613 32  MET A CE    
182  N N     . THR A 39  ? 0.10520 0.17073 0.24115 0.01648  0.00916  -0.04419 33  THR A N     
183  C CA    . THR A 39  ? 0.11073 0.17091 0.22609 0.00566  0.02294  -0.01468 33  THR A CA    
184  C C     . THR A 39  ? 0.10243 0.17170 0.23576 0.01041  0.00013  0.00522  33  THR A C     
185  O O     . THR A 39  ? 0.10552 0.17590 0.29159 0.02075  -0.00973 0.01047  33  THR A O     
186  C CB    . THR A 39  ? 0.11782 0.17731 0.21466 0.00115  0.03368  -0.01927 33  THR A CB    
187  O OG1   . THR A 39  ? 0.11096 0.20943 0.28601 0.00345  0.03538  -0.00416 33  THR A OG1   
188  C CG2   . THR A 39  ? 0.11785 0.15850 0.23630 0.01482  0.03487  -0.04273 33  THR A CG2   
189  N N     . ARG A 40  ? 0.11734 0.15554 0.23429 0.00531  0.00229  -0.00437 34  ARG A N     
190  C CA    . ARG A 40  ? 0.08761 0.17021 0.20697 0.00998  -0.00761 -0.01164 34  ARG A CA    
191  C C     . ARG A 40  ? 0.10493 0.16546 0.27477 -0.00576 -0.01981 -0.02848 34  ARG A C     
192  O O     . ARG A 40  ? 0.12145 0.14396 0.25735 -0.00705 -0.02252 -0.03927 34  ARG A O     
193  C CB    . ARG A 40  ? 0.08433 0.20302 0.25089 0.03079  0.00627  -0.00808 34  ARG A CB    
194  C CG    . ARG A 40  ? 0.08668 0.21611 0.21891 0.00532  0.01516  0.00366  34  ARG A CG    
195  C CD    . ARG A 40  ? 0.08013 0.21348 0.22121 0.01763  0.00810  0.01058  34  ARG A CD    
196  N NE    . ARG A 40  ? 0.07701 0.21767 0.22729 0.00695  0.02427  0.03819  34  ARG A NE    
197  C CZ    . ARG A 40  ? 0.08047 0.23240 0.25502 0.00233  0.00209  -0.00341 34  ARG A CZ    
198  N NH1   . ARG A 40  ? 0.07790 0.22945 0.20013 0.02419  -0.01068 0.00236  34  ARG A NH1   
199  N NH2   . ARG A 40  ? 0.07886 0.23673 0.28152 -0.01580 -0.02606 -0.00621 34  ARG A NH2   
200  N N     . CYS A 41  ? 0.12119 0.17386 0.25762 0.00129  -0.01128 0.00233  35  CYS A N     
201  C CA    . CYS A 41  ? 0.11247 0.17465 0.18166 0.00092  -0.02649 0.01300  35  CYS A CA    
202  C C     . CYS A 41  ? 0.12165 0.17034 0.21366 -0.00358 -0.00673 -0.00217 35  CYS A C     
203  O O     . CYS A 41  ? 0.14651 0.16314 0.22500 -0.00016 -0.01940 -0.01429 35  CYS A O     
204  C CB    . CYS A 41  ? 0.11919 0.17461 0.21633 -0.00202 -0.01794 0.00990  35  CYS A CB    
205  S SG    . CYS A 41  ? 0.13626 0.18461 0.27612 0.02159  -0.01476 -0.00076 35  CYS A SG    
206  N N     . ARG A 42  ? 0.11567 0.17651 0.22101 -0.00671 0.02448  0.01792  36  ARG A N     
207  C CA    . ARG A 42  ? 0.10927 0.19569 0.20256 -0.01739 0.01542  0.01560  36  ARG A CA    
208  C C     . ARG A 42  ? 0.10494 0.19346 0.26608 -0.00731 0.00601  0.00377  36  ARG A C     
209  O O     . ARG A 42  ? 0.10872 0.18695 0.28812 0.00020  -0.00735 0.00211  36  ARG A O     
210  C CB    . ARG A 42  ? 0.10599 0.20182 0.20978 -0.04156 -0.00689 0.00194  36  ARG A CB    
211  C CG    . ARG A 42  ? 0.10128 0.20776 0.23842 -0.03012 -0.01617 0.03230  36  ARG A CG    
212  C CD    . ARG A 42  ? 0.08591 0.19535 0.27364 -0.02297 0.03478  0.00716  36  ARG A CD    
213  N NE    . ARG A 42  ? 0.09145 0.16509 0.24420 -0.02860 0.04369  0.02636  36  ARG A NE    
214  C CZ    . ARG A 42  ? 0.09029 0.15579 0.20856 -0.03708 0.04295  0.00001  36  ARG A CZ    
215  N NH1   . ARG A 42  ? 0.11889 0.15258 0.17684 -0.00851 0.01578  0.00308  36  ARG A NH1   
216  N NH2   . ARG A 42  ? 0.09453 0.16164 0.25492 -0.04703 0.02476  -0.02287 36  ARG A NH2   
217  N N     . ALA A 43  ? 0.08446 0.18649 0.25587 -0.00106 0.00105  -0.01296 37  ALA A N     
218  C CA    . ALA A 43  ? 0.10238 0.17978 0.29017 -0.01676 0.00544  0.00389  37  ALA A CA    
219  C C     . ALA A 43  ? 0.11370 0.15848 0.30751 0.00649  -0.02266 0.01509  37  ALA A C     
220  O O     . ALA A 43  ? 0.10462 0.15468 0.35486 0.00363  -0.05047 -0.00774 37  ALA A O     
221  C CB    . ALA A 43  ? 0.12014 0.18094 0.28429 -0.03313 0.00519  0.05420  37  ALA A CB    
222  N N     . LEU A 44  ? 0.13015 0.15768 0.29214 0.01073  -0.01505 0.00613  38  LEU A N     
223  C CA    . LEU A 44  ? 0.14257 0.18312 0.28879 -0.00751 0.01195  0.02394  38  LEU A CA    
224  C C     . LEU A 44  ? 0.15729 0.20169 0.25531 0.00415  0.01757  0.01838  38  LEU A C     
225  O O     . LEU A 44  ? 0.16680 0.21272 0.24858 0.02433  0.01373  0.03525  38  LEU A O     
226  C CB    . LEU A 44  ? 0.13569 0.18929 0.28243 -0.01661 0.01317  -0.01039 38  LEU A CB    
227  C CG    . LEU A 44  ? 0.13486 0.20764 0.31780 -0.01667 0.01071  0.03515  38  LEU A CG    
228  C CD1   . LEU A 44  ? 0.15339 0.20874 0.38344 -0.01437 0.02003  0.02760  38  LEU A CD1   
229  C CD2   . LEU A 44  ? 0.12655 0.21572 0.29540 -0.02383 0.01770  0.04476  38  LEU A CD2   
230  N N     . ASN A 45  ? 0.16433 0.19469 0.27999 -0.02594 0.01289  0.01548  39  ASN A N     
231  C CA    . ASN A 45  ? 0.17276 0.19087 0.30138 -0.00936 0.02231  0.00448  39  ASN A CA    
232  C C     . ASN A 45  ? 0.15957 0.18882 0.28816 -0.00444 -0.01825 -0.01376 39  ASN A C     
233  O O     . ASN A 45  ? 0.17466 0.18933 0.30908 0.00087  -0.01787 -0.00154 39  ASN A O     
234  C CB    . ASN A 45  ? 0.20606 0.22206 0.32544 -0.02233 0.01802  -0.00038 39  ASN A CB    
235  C CG    . ASN A 45  ? 0.21056 0.23194 0.33970 -0.03015 0.02727  -0.02943 39  ASN A CG    
236  O OD1   . ASN A 45  ? 0.23045 0.24062 0.40379 -0.06600 0.03710  -0.02726 39  ASN A OD1   
237  N ND2   . ASN A 45  ? 0.20689 0.23890 0.33211 -0.01291 0.00620  -0.11408 39  ASN A ND2   
238  N N     . ASN A 46  ? 0.15530 0.18377 0.27666 0.00778  -0.01543 -0.03376 40  ASN A N     
239  C CA    . ASN A 46  ? 0.13260 0.17838 0.24753 -0.01276 -0.00635 -0.03090 40  ASN A CA    
240  C C     . ASN A 46  ? 0.13034 0.18410 0.28168 -0.00944 -0.01196 -0.00878 40  ASN A C     
241  O O     . ASN A 46  ? 0.09285 0.18329 0.29802 -0.01724 -0.02024 -0.01021 40  ASN A O     
242  C CB    . ASN A 46  ? 0.13852 0.20612 0.29918 0.00865  0.01217  -0.04416 40  ASN A CB    
243  C CG    . ASN A 46  ? 0.15137 0.21933 0.31599 0.00987  0.01277  -0.03597 40  ASN A CG    
244  O OD1   . ASN A 46  ? 0.16667 0.26306 0.30582 0.03715  0.01548  -0.05408 40  ASN A OD1   
245  N ND2   . ASN A 46  ? 0.14559 0.20230 0.30227 -0.01796 -0.01892 -0.01608 40  ASN A ND2   
246  N N     . ILE A 47  ? 0.17049 0.21067 0.21677 0.00767  -0.02145 -0.01319 41  ILE A N     
247  C CA    . ILE A 47  ? 0.16059 0.21177 0.23491 0.01635  -0.01142 0.01903  41  ILE A CA    
248  C C     . ILE A 47  ? 0.15600 0.20928 0.25022 0.00602  -0.02551 -0.00197 41  ILE A C     
249  O O     . ILE A 47  ? 0.14945 0.23153 0.24262 0.00530  -0.00680 -0.00080 41  ILE A O     
250  C CB    . ILE A 47  ? 0.17493 0.24372 0.26054 0.04318  -0.00914 0.02768  41  ILE A CB    
251  C CG1   . ILE A 47  ? 0.20230 0.25441 0.35170 0.05409  -0.00910 0.02055  41  ILE A CG1   
252  C CG2   . ILE A 47  ? 0.18705 0.26109 0.21072 0.05812  -0.01797 0.02641  41  ILE A CG2   
253  C CD1   . ILE A 47  ? 0.22849 0.27418 0.43513 0.03861  0.00965  0.01688  41  ILE A CD1   
254  N N     . PRO A 48  ? 0.16041 0.19903 0.28266 -0.01750 -0.00927 0.00803  42  PRO A N     
255  C CA    . PRO A 48  ? 0.16611 0.22021 0.32403 -0.01769 -0.00977 0.00312  42  PRO A CA    
256  C C     . PRO A 48  ? 0.15581 0.25493 0.30946 -0.00571 -0.00073 0.04731  42  PRO A C     
257  O O     . PRO A 48  ? 0.17428 0.28842 0.30674 0.00536  -0.02694 0.03776  42  PRO A O     
258  C CB    . PRO A 48  ? 0.16973 0.21193 0.32394 -0.04026 -0.02415 -0.01650 42  PRO A CB    
259  C CG    . PRO A 48  ? 0.17851 0.20119 0.31696 -0.03959 -0.01724 -0.01489 42  PRO A CG    
260  C CD    . PRO A 48  ? 0.16438 0.20826 0.28207 -0.03375 -0.02872 -0.03706 42  PRO A CD    
261  N N     . GLN A 49  ? 0.14366 0.25763 0.31515 -0.00511 0.00644  0.05467  43  GLN A N     
262  C CA    . GLN A 49  ? 0.15709 0.24393 0.26695 -0.01250 0.00546  0.04545  43  GLN A CA    
263  C C     . GLN A 49  ? 0.17415 0.22925 0.27288 -0.00368 -0.01135 0.04122  43  GLN A C     
264  O O     . GLN A 49  ? 0.17113 0.19920 0.33214 0.01278  0.00250  0.06186  43  GLN A O     
265  C CB    . GLN A 49  ? 0.17568 0.26509 0.30582 -0.01459 0.01333  0.02970  43  GLN A CB    
266  C CG    . GLN A 49  ? 0.20801 0.27017 0.31549 -0.00275 0.01849  0.02848  43  GLN A CG    
267  C CD    . GLN A 49  ? 0.24989 0.27571 0.34871 0.01138  0.04388  0.01779  43  GLN A CD    
268  O OE1   . GLN A 49  ? 0.29075 0.28017 0.40944 0.03270  0.01497  0.00380  43  GLN A OE1   
269  N NE2   . GLN A 49  ? 0.24493 0.27837 0.30658 0.00564  0.08121  0.00941  43  GLN A NE2   
270  N N     . ALA A 50  ? 0.18956 0.24433 0.27578 0.00318  -0.01403 0.03626  44  ALA A N     
271  C CA    . ALA A 50  ? 0.18805 0.23660 0.28678 0.02444  0.02194  0.03274  44  ALA A CA    
272  C C     . ALA A 50  ? 0.20005 0.23422 0.30903 0.01123  0.02918  0.02297  44  ALA A C     
273  O O     . ALA A 50  ? 0.21356 0.24166 0.28428 0.02552  0.04291  0.02789  44  ALA A O     
274  C CB    . ALA A 50  ? 0.19089 0.24557 0.32407 0.04285  0.01175  0.04616  44  ALA A CB    
275  N N     . ALA A 51  ? 0.18612 0.21132 0.31706 0.00584  0.00747  0.02720  45  ALA A N     
276  C CA    . ALA A 51  ? 0.19010 0.21556 0.31379 -0.00535 -0.03140 -0.01022 45  ALA A CA    
277  C C     . ALA A 51  ? 0.17237 0.20385 0.27256 -0.01041 -0.00398 0.00906  45  ALA A C     
278  O O     . ALA A 51  ? 0.18188 0.19603 0.24585 0.00222  -0.01401 -0.00589 45  ALA A O     
279  C CB    . ALA A 51  ? 0.20903 0.22702 0.29725 -0.00738 -0.06128 0.01082  45  ALA A CB    
280  N N     . LEU A 52  ? 0.13725 0.20349 0.30029 -0.03790 0.01623  -0.04783 46  LEU A N     
281  C CA    . LEU A 52  ? 0.11448 0.20004 0.25218 -0.02957 0.02566  -0.02336 46  LEU A CA    
282  C C     . LEU A 52  ? 0.13150 0.22630 0.24268 -0.00830 0.00383  -0.01440 46  LEU A C     
283  O O     . LEU A 52  ? 0.14380 0.22139 0.25460 -0.01359 -0.00957 -0.03443 46  LEU A O     
284  C CB    . LEU A 52  ? 0.10526 0.21643 0.20181 -0.02812 0.04380  -0.01087 46  LEU A CB    
285  C CG    . LEU A 52  ? 0.11147 0.23886 0.19688 -0.03410 0.01920  0.00452  46  LEU A CG    
286  C CD1   . LEU A 52  ? 0.12987 0.25302 0.29988 -0.02304 0.00226  0.01913  46  LEU A CD1   
287  C CD2   . LEU A 52  ? 0.11175 0.26198 0.20031 -0.03710 -0.00562 0.02583  46  LEU A CD2   
288  N N     . GLY A 53  ? 0.12365 0.24532 0.21765 -0.01142 -0.02495 -0.00335 47  GLY A N     
289  C CA    . GLY A 53  ? 0.11276 0.25772 0.24450 0.00272  0.01822  -0.00584 47  GLY A CA    
290  C C     . GLY A 53  ? 0.12100 0.25863 0.28342 -0.00107 0.00913  0.00291  47  GLY A C     
291  O O     . GLY A 53  ? 0.14505 0.26535 0.28043 -0.01439 -0.01517 -0.01816 47  GLY A O     
292  N N     . GLU A 54  ? 0.12804 0.23209 0.30376 0.00708  -0.02259 0.00424  48  GLU A N     
293  C CA    . GLU A 54  ? 0.16627 0.25473 0.29831 0.00056  0.01371  0.02735  48  GLU A CA    
294  C C     . GLU A 54  ? 0.13145 0.22868 0.25330 -0.00751 0.01765  0.01327  48  GLU A C     
295  O O     . GLU A 54  ? 0.13775 0.22857 0.23706 -0.00754 0.01961  0.00336  48  GLU A O     
296  C CB    . GLU A 54  ? 0.26044 0.28729 0.36646 -0.00996 0.03175  -0.00553 48  GLU A CB    
297  C CG    . GLU A 54  ? 0.36704 0.35505 0.48168 -0.00116 0.06107  -0.01170 48  GLU A CG    
298  C CD    . GLU A 54  ? 0.44734 0.44884 0.59187 -0.00041 0.09419  -0.02456 48  GLU A CD    
299  O OE1   . GLU A 54  ? 0.46924 0.46664 0.67297 0.00819  0.11383  -0.04556 48  GLU A OE1   
300  O OE2   . GLU A 54  ? 0.47824 0.48975 0.63900 -0.00386 0.09247  -0.00449 48  GLU A OE2   
301  N N     . TYR A 55  ? 0.13290 0.20823 0.22888 -0.02442 -0.00159 -0.00269 49  TYR A N     
302  C CA    . TYR A 55  ? 0.12935 0.20276 0.17760 -0.00367 -0.01460 0.02255  49  TYR A CA    
303  C C     . TYR A 55  ? 0.12046 0.19964 0.20655 0.00509  -0.00635 0.01370  49  TYR A C     
304  O O     . TYR A 55  ? 0.13995 0.20022 0.21967 0.01901  0.00387  0.01880  49  TYR A O     
305  C CB    . TYR A 55  ? 0.14140 0.18890 0.21104 -0.00425 -0.02777 0.04688  49  TYR A CB    
306  C CG    . TYR A 55  ? 0.13673 0.18459 0.22869 -0.01468 -0.02890 0.04101  49  TYR A CG    
307  C CD1   . TYR A 55  ? 0.13770 0.19040 0.24528 -0.00934 -0.03214 0.00516  49  TYR A CD1   
308  C CD2   . TYR A 55  ? 0.14254 0.18753 0.26092 0.00173  -0.02001 0.02256  49  TYR A CD2   
309  C CE1   . TYR A 55  ? 0.14593 0.19879 0.30138 0.00423  -0.01514 -0.00930 49  TYR A CE1   
310  C CE2   . TYR A 55  ? 0.14750 0.19814 0.26826 0.01166  -0.03447 0.01403  49  TYR A CE2   
311  C CZ    . TYR A 55  ? 0.15266 0.19362 0.31438 0.00135  -0.03176 -0.00948 49  TYR A CZ    
312  O OH    . TYR A 55  ? 0.17189 0.21482 0.32313 -0.00086 -0.03057 0.01551  49  TYR A OH    
313  N N     . TYR A 56  ? 0.11911 0.20847 0.18071 -0.00485 -0.01377 0.01959  50  TYR A N     
314  C CA    . TYR A 56  ? 0.12865 0.21989 0.18495 -0.00094 -0.00289 0.03050  50  TYR A CA    
315  C C     . TYR A 56  ? 0.14582 0.23388 0.20218 0.01229  -0.01986 0.02259  50  TYR A C     
316  O O     . TYR A 56  ? 0.13957 0.23461 0.21387 0.02423  -0.00333 -0.01234 50  TYR A O     
317  C CB    . TYR A 56  ? 0.11767 0.22988 0.16489 0.01825  0.00425  0.03951  50  TYR A CB    
318  C CG    . TYR A 56  ? 0.13091 0.23510 0.16410 0.01496  -0.00575 0.03829  50  TYR A CG    
319  C CD1   . TYR A 56  ? 0.14242 0.23001 0.13604 0.00189  0.00949  0.07093  50  TYR A CD1   
320  C CD2   . TYR A 56  ? 0.13205 0.22985 0.21517 0.00453  0.01302  0.01423  50  TYR A CD2   
321  C CE1   . TYR A 56  ? 0.13288 0.23793 0.19220 0.01963  0.01503  0.06087  50  TYR A CE1   
322  C CE2   . TYR A 56  ? 0.14163 0.22253 0.23549 -0.00495 -0.00396 0.04688  50  TYR A CE2   
323  C CZ    . TYR A 56  ? 0.13951 0.23353 0.24805 0.01255  0.00282  0.05966  50  TYR A CZ    
324  O OH    . TYR A 56  ? 0.15441 0.23477 0.29913 -0.00030 0.00003  0.03718  50  TYR A OH    
325  N N     . GLU A 57  ? 0.17288 0.24775 0.15643 0.01115  -0.03701 0.03583  51  GLU A N     
326  C CA    . GLU A 57  ? 0.19181 0.27854 0.12967 0.01368  -0.01327 0.05092  51  GLU A CA    
327  C C     . GLU A 57  ? 0.15031 0.27006 0.19868 -0.03431 -0.02309 0.03255  51  GLU A C     
328  O O     . GLU A 57  ? 0.14682 0.26987 0.26385 -0.04171 -0.06139 0.03137  51  GLU A O     
329  C CB    . GLU A 57  ? 0.24583 0.31044 0.17917 0.04273  -0.03624 0.04488  51  GLU A CB    
330  C CG    . GLU A 57  ? 0.31132 0.34028 0.25838 0.01640  -0.06181 0.06153  51  GLU A CG    
331  C CD    . GLU A 57  ? 0.35459 0.39071 0.34238 -0.02455 -0.06221 0.04421  51  GLU A CD    
332  O OE1   . GLU A 57  ? 0.38858 0.40069 0.38874 -0.01977 -0.05235 0.03835  51  GLU A OE1   
333  O OE2   . GLU A 57  ? 0.35571 0.41689 0.39716 -0.04203 -0.04215 0.05339  51  GLU A OE2   
334  N N     . GLN A 58  ? 0.11786 0.26221 0.24310 -0.04231 -0.02764 0.01276  52  GLN A N     
335  C CA    . GLN A 58  ? 0.12559 0.23330 0.26826 -0.03059 -0.00868 -0.00479 52  GLN A CA    
336  C C     . GLN A 58  ? 0.13034 0.22163 0.26603 -0.00640 0.02019  -0.01204 52  GLN A C     
337  O O     . GLN A 58  ? 0.12942 0.22663 0.27802 -0.01290 0.02389  0.02409  52  GLN A O     
338  C CB    . GLN A 58  ? 0.13766 0.22188 0.30003 -0.04780 -0.03709 -0.00874 52  GLN A CB    
339  C CG    . GLN A 58  ? 0.15762 0.22101 0.32949 -0.03766 -0.03371 -0.00722 52  GLN A CG    
340  C CD    . GLN A 58  ? 0.17036 0.21867 0.30941 -0.03686 -0.00404 -0.01178 52  GLN A CD    
341  O OE1   . GLN A 58  ? 0.16993 0.22466 0.30084 -0.01492 0.01899  -0.02255 52  GLN A OE1   
342  N NE2   . GLN A 58  ? 0.18485 0.20815 0.33893 -0.05542 -0.00964 -0.02724 52  GLN A NE2   
343  N N     . ARG A 59  ? 0.13650 0.19711 0.24849 0.00164  -0.00798 -0.00192 53  ARG A N     
344  C CA    . ARG A 59  ? 0.13523 0.20011 0.22007 -0.00555 -0.00088 -0.02671 53  ARG A CA    
345  C C     . ARG A 59  ? 0.14121 0.20868 0.24826 -0.00076 -0.01487 -0.01265 53  ARG A C     
346  O O     . ARG A 59  ? 0.12132 0.21116 0.26528 -0.00706 -0.00739 0.01501  53  ARG A O     
347  C CB    . ARG A 59  ? 0.13133 0.19989 0.19374 -0.00454 -0.00583 -0.03262 53  ARG A CB    
348  C CG    . ARG A 59  ? 0.10567 0.21375 0.20545 0.00862  -0.01006 -0.04189 53  ARG A CG    
349  C CD    . ARG A 59  ? 0.11623 0.21357 0.21434 0.00044  -0.03897 -0.01467 53  ARG A CD    
350  N NE    . ARG A 59  ? 0.12455 0.22068 0.23765 0.00684  -0.02435 -0.00660 53  ARG A NE    
351  C CZ    . ARG A 59  ? 0.11182 0.20552 0.25081 0.01230  -0.05458 0.00241  53  ARG A CZ    
352  N NH1   . ARG A 59  ? 0.11054 0.19371 0.24335 0.02467  -0.03849 0.00554  53  ARG A NH1   
353  N NH2   . ARG A 59  ? 0.11406 0.21581 0.22607 0.01897  -0.03277 0.00440  53  ARG A NH2   
354  N N     . ALA A 60  ? 0.14760 0.22411 0.20245 -0.00995 -0.02056 -0.02507 54  ALA A N     
355  C CA    . ALA A 60  ? 0.14961 0.22220 0.22600 0.00526  0.01571  -0.00033 54  ALA A CA    
356  C C     . ALA A 60  ? 0.16800 0.22565 0.21960 0.01097  0.01786  -0.01558 54  ALA A C     
357  O O     . ALA A 60  ? 0.20482 0.24303 0.24177 0.02433  0.05832  -0.03624 54  ALA A O     
358  C CB    . ALA A 60  ? 0.11757 0.19174 0.23255 0.03505  0.01524  0.02603  54  ALA A CB    
359  N N     . THR A 61  ? 0.17028 0.21299 0.24115 0.00477  -0.01618 -0.02444 55  THR A N     
360  C CA    . THR A 61  ? 0.15299 0.20147 0.21221 0.00308  -0.01507 -0.02138 55  THR A CA    
361  C C     . THR A 61  ? 0.17003 0.22014 0.25080 -0.00280 -0.01281 0.00844  55  THR A C     
362  O O     . THR A 61  ? 0.14880 0.20956 0.25620 0.02022  0.01526  0.02025  55  THR A O     
363  C CB    . THR A 61  ? 0.14843 0.21174 0.22084 -0.00671 -0.00404 0.00128  55  THR A CB    
364  O OG1   . THR A 61  ? 0.15111 0.21407 0.29908 0.00933  0.00744  0.01640  55  THR A OG1   
365  C CG2   . THR A 61  ? 0.14395 0.23390 0.22631 -0.00195 0.01177  0.00365  55  THR A CG2   
366  N N     . ALA A 62  ? 0.19395 0.23201 0.24639 -0.01456 -0.01194 0.01877  56  ALA A N     
367  C CA    . ALA A 62  ? 0.21753 0.24176 0.22347 -0.02038 -0.02469 0.02347  56  ALA A CA    
368  C C     . ALA A 62  ? 0.21771 0.24236 0.22852 -0.01331 -0.03085 0.02846  56  ALA A C     
369  O O     . ALA A 62  ? 0.22536 0.24304 0.27896 0.00869  -0.02796 0.03831  56  ALA A O     
370  C CB    . ALA A 62  ? 0.23134 0.25038 0.23279 -0.01381 -0.02788 0.01631  56  ALA A CB    
371  N N     . GLY A 63  ? 0.20555 0.22994 0.18674 -0.02783 -0.04816 0.05231  57  GLY A N     
372  C CA    . GLY A 63  ? 0.19264 0.23748 0.21909 0.00462  -0.04568 0.02703  57  GLY A CA    
373  C C     . GLY A 63  ? 0.17900 0.22760 0.20233 0.00424  0.00169  0.03757  57  GLY A C     
374  O O     . GLY A 63  ? 0.19339 0.20971 0.24414 -0.00805 0.01589  0.03665  57  GLY A O     
375  N N     . GLY A 64  ? 0.16394 0.23966 0.13339 -0.00301 0.00713  -0.02113 58  GLY A N     
376  C CA    . GLY A 64  ? 0.14103 0.24223 0.13189 0.01814  0.03081  -0.01304 58  GLY A CA    
377  C C     . GLY A 64  ? 0.12594 0.25435 0.19618 0.00905  0.01560  -0.00734 58  GLY A C     
378  O O     . GLY A 64  ? 0.15559 0.28191 0.20748 0.03786  0.02374  0.04990  58  GLY A O     
379  N N     . PHE A 65  ? 0.09839 0.23389 0.18583 -0.00745 0.01875  -0.02196 59  PHE A N     
380  C CA    . PHE A 65  ? 0.08960 0.23115 0.18900 -0.00070 0.02720  -0.00145 59  PHE A CA    
381  C C     . PHE A 65  ? 0.09835 0.22445 0.20104 -0.00519 -0.01308 -0.01587 59  PHE A C     
382  O O     . PHE A 65  ? 0.08513 0.22365 0.21259 -0.01008 -0.03021 -0.00404 59  PHE A O     
383  C CB    . PHE A 65  ? 0.07874 0.22128 0.24392 0.00943  0.04390  -0.01146 59  PHE A CB    
384  C CG    . PHE A 65  ? 0.07237 0.21061 0.22573 0.01220  0.03751  -0.01329 59  PHE A CG    
385  C CD1   . PHE A 65  ? 0.08549 0.24050 0.24774 -0.00086 0.05475  0.00121  59  PHE A CD1   
386  C CD2   . PHE A 65  ? 0.06902 0.20508 0.19630 -0.01251 0.02521  -0.01194 59  PHE A CD2   
387  C CE1   . PHE A 65  ? 0.09426 0.23474 0.28006 -0.02123 0.03089  0.00513  59  PHE A CE1   
388  C CE2   . PHE A 65  ? 0.06710 0.21027 0.24103 0.00481  0.01271  -0.02025 59  PHE A CE2   
389  C CZ    . PHE A 65  ? 0.08905 0.22768 0.29021 -0.01074 -0.00604 -0.02971 59  PHE A CZ    
390  N N     . LEU A 66  ? 0.11687 0.22418 0.17976 0.00695  0.01638  -0.00872 60  LEU A N     
391  C CA    . LEU A 66  ? 0.13267 0.21066 0.13534 -0.01217 0.02425  0.03792  60  LEU A CA    
392  C C     . LEU A 66  ? 0.13428 0.20528 0.14079 -0.02173 0.00973  0.00088  60  LEU A C     
393  O O     . LEU A 66  ? 0.13872 0.21954 0.20668 -0.02196 -0.02429 -0.02615 60  LEU A O     
394  C CB    . LEU A 66  ? 0.16695 0.22783 0.17916 -0.01023 0.01545  0.07715  60  LEU A CB    
395  C CG    . LEU A 66  ? 0.20343 0.24911 0.28547 -0.00890 0.05503  0.11653  60  LEU A CG    
396  C CD1   . LEU A 66  ? 0.23453 0.24492 0.30969 -0.00370 0.08072  0.09518  60  LEU A CD1   
397  C CD2   . LEU A 66  ? 0.21724 0.27580 0.34851 -0.01428 0.03112  0.10252  60  LEU A CD2   
398  N N     . ILE A 67  ? 0.11740 0.18205 0.15319 -0.00350 0.00114  -0.02164 61  ILE A N     
399  C CA    . ILE A 67  ? 0.10476 0.18617 0.15475 -0.01048 -0.00827 0.03874  61  ILE A CA    
400  C C     . ILE A 67  ? 0.11319 0.19336 0.17738 -0.00943 -0.00338 -0.01417 61  ILE A C     
401  O O     . ILE A 67  ? 0.11653 0.21390 0.19698 -0.01942 -0.02533 -0.02323 61  ILE A O     
402  C CB    . ILE A 67  ? 0.11381 0.16164 0.22412 -0.00772 0.02868  0.00858  61  ILE A CB    
403  C CG1   . ILE A 67  ? 0.11300 0.14964 0.20857 -0.00393 0.02830  0.01038  61  ILE A CG1   
404  C CG2   . ILE A 67  ? 0.13018 0.18731 0.20742 0.00574  -0.00741 -0.00625 61  ILE A CG2   
405  C CD1   . ILE A 67  ? 0.11423 0.15868 0.30809 -0.00676 0.01699  -0.01752 61  ILE A CD1   
406  N N     . THR A 68  ? 0.13825 0.17890 0.19786 0.01367  -0.02628 0.00754  62  THR A N     
407  C CA    . THR A 68  ? 0.12208 0.17946 0.22907 0.01267  -0.01610 -0.02840 62  THR A CA    
408  C C     . THR A 68  ? 0.12596 0.17367 0.24204 0.01605  -0.00306 -0.02601 62  THR A C     
409  O O     . THR A 68  ? 0.11037 0.17828 0.21899 0.03476  -0.01417 -0.01524 62  THR A O     
410  C CB    . THR A 68  ? 0.11300 0.20197 0.24337 -0.00668 -0.00787 0.00343  62  THR A CB    
411  O OG1   . THR A 68  ? 0.10737 0.19532 0.26256 -0.01563 -0.02893 0.00223  62  THR A OG1   
412  C CG2   . THR A 68  ? 0.12589 0.20518 0.23982 -0.00271 -0.03097 -0.00220 62  THR A CG2   
413  N N     . GLU A 69  ? 0.11343 0.18507 0.23725 -0.01574 -0.00284 -0.05277 63  GLU A N     
414  C CA    . GLU A 69  ? 0.12277 0.18106 0.24099 -0.01389 0.00458  -0.00480 63  GLU A CA    
415  C C     . GLU A 69  ? 0.12293 0.18456 0.21132 0.00468  0.02294  -0.00919 63  GLU A C     
416  O O     . GLU A 69  ? 0.14852 0.19128 0.23041 0.01162  -0.02193 0.01512  63  GLU A O     
417  C CB    . GLU A 69  ? 0.12804 0.17796 0.31732 0.03169  -0.00927 -0.02600 63  GLU A CB    
418  C CG    . GLU A 69  ? 0.15936 0.20413 0.33833 0.02706  0.02063  -0.02346 63  GLU A CG    
419  C CD    . GLU A 69  ? 0.17044 0.22775 0.32775 0.04113  0.02349  -0.02006 63  GLU A CD    
420  O OE1   . GLU A 69  ? 0.20201 0.23239 0.30110 0.02595  -0.01000 -0.03011 63  GLU A OE1   
421  O OE2   . GLU A 69  ? 0.15424 0.22132 0.34435 0.01787  0.01084  -0.04933 63  GLU A OE2   
422  N N     . GLY A 70  ? 0.10248 0.17713 0.20923 0.01080  0.01686  0.01309  64  GLY A N     
423  C CA    . GLY A 70  ? 0.07485 0.16681 0.22432 -0.00441 0.02205  0.01116  64  GLY A CA    
424  C C     . GLY A 70  ? 0.08250 0.17733 0.25641 -0.00242 -0.00734 -0.00061 64  GLY A C     
425  O O     . GLY A 70  ? 0.10782 0.18625 0.25964 -0.02535 0.00602  0.02766  64  GLY A O     
426  N N     . THR A 71  ? 0.08107 0.17078 0.25234 0.02055  -0.04074 -0.00127 65  THR A N     
427  C CA    . THR A 71  ? 0.08569 0.19510 0.21612 0.02429  -0.00327 0.01865  65  THR A CA    
428  C C     . THR A 71  ? 0.11154 0.19526 0.22981 0.00716  -0.01030 0.00008  65  THR A C     
429  O O     . THR A 71  ? 0.13664 0.17251 0.24627 0.00423  -0.02520 -0.00425 65  THR A O     
430  C CB    . THR A 71  ? 0.09236 0.20773 0.24517 0.00916  0.00401  0.00371  65  THR A CB    
431  O OG1   . THR A 71  ? 0.12849 0.21003 0.25041 -0.01097 0.01992  -0.00114 65  THR A OG1   
432  C CG2   . THR A 71  ? 0.13321 0.20601 0.28795 0.03738  0.00446  -0.00080 65  THR A CG2   
433  N N     . MET A 72  ? 0.12130 0.20718 0.21935 0.02634  -0.00115 -0.02665 66  MET A N     
434  C CA    . MET A 72  ? 0.12808 0.20572 0.23831 -0.00557 0.01286  -0.04322 66  MET A CA    
435  C C     . MET A 72  ? 0.12499 0.19452 0.23702 -0.01401 -0.00013 0.00073  66  MET A C     
436  O O     . MET A 72  ? 0.13164 0.19403 0.21674 -0.00014 -0.01689 0.00236  66  MET A O     
437  C CB    . MET A 72  ? 0.13624 0.22144 0.26993 0.00291  0.02233  -0.04759 66  MET A CB    
438  C CG    . MET A 72  ? 0.13924 0.18658 0.26674 -0.00638 0.01327  -0.02885 66  MET A CG    
439  S SD    . MET A 72  ? 0.15056 0.20100 0.28491 -0.00463 0.01298  -0.00143 66  MET A SD    
440  C CE    . MET A 72  ? 0.11879 0.21154 0.31214 -0.00744 -0.01314 -0.03348 66  MET A CE    
441  N N     . ILE A 73  ? 0.10909 0.16965 0.22140 -0.00049 -0.01200 0.02829  67  ILE A N     
442  C CA    . ILE A 73  ? 0.07652 0.17448 0.25204 0.00163  -0.03460 -0.00658 67  ILE A CA    
443  C C     . ILE A 73  ? 0.09221 0.20920 0.25118 0.00222  -0.03687 0.00417  67  ILE A C     
444  O O     . ILE A 73  ? 0.08251 0.22234 0.28521 -0.00751 -0.03683 0.00732  67  ILE A O     
445  C CB    . ILE A 73  ? 0.07717 0.16348 0.24270 0.01378  -0.00961 0.00465  67  ILE A CB    
446  C CG1   . ILE A 73  ? 0.09784 0.17049 0.26541 -0.01450 0.01071  -0.01755 67  ILE A CG1   
447  C CG2   . ILE A 73  ? 0.08083 0.17562 0.26065 0.03129  0.00512  -0.03140 67  ILE A CG2   
448  C CD1   . ILE A 73  ? 0.10737 0.19345 0.25215 -0.02772 0.01372  -0.00332 67  ILE A CD1   
449  N N     . SER A 74  ? 0.11890 0.20743 0.27057 0.00278  -0.00011 -0.02079 68  SER A N     
450  C CA    . SER A 74  ? 0.11872 0.22895 0.27107 0.00616  -0.00876 -0.00873 68  SER A CA    
451  C C     . SER A 74  ? 0.11706 0.23825 0.29523 0.01136  -0.01228 -0.02937 68  SER A C     
452  O O     . SER A 74  ? 0.11140 0.23841 0.29306 0.01317  -0.01630 -0.03738 68  SER A O     
453  C CB    . SER A 74  ? 0.13149 0.23714 0.30338 -0.01827 -0.01155 0.02947  68  SER A CB    
454  O OG    . SER A 74  ? 0.15551 0.26181 0.30085 -0.02047 -0.00634 0.04525  68  SER A OG    
455  N N     . PRO A 75  ? 0.11039 0.23632 0.30964 0.02735  -0.03342 -0.06723 69  PRO A N     
456  C CA    . PRO A 75  ? 0.13082 0.25478 0.38293 0.02086  -0.00070 -0.07229 69  PRO A CA    
457  C C     . PRO A 75  ? 0.14032 0.25603 0.37150 -0.00998 0.02078  -0.04356 69  PRO A C     
458  O O     . PRO A 75  ? 0.15603 0.25619 0.41530 0.00032  0.01715  -0.03612 69  PRO A O     
459  C CB    . PRO A 75  ? 0.14191 0.27921 0.39921 0.02123  -0.02525 -0.08697 69  PRO A CB    
460  C CG    . PRO A 75  ? 0.14587 0.27581 0.34628 0.00508  -0.03956 -0.09550 69  PRO A CG    
461  C CD    . PRO A 75  ? 0.12143 0.25518 0.30618 0.02860  -0.02986 -0.08103 69  PRO A CD    
462  N N     . THR A 76  ? 0.14696 0.26093 0.38261 -0.05081 0.02028  -0.03210 70  THR A N     
463  C CA    . THR A 76  ? 0.19508 0.27862 0.33646 -0.08272 0.01562  -0.04247 70  THR A CA    
464  C C     . THR A 76  ? 0.19038 0.25975 0.28376 -0.05757 -0.01639 -0.00665 70  THR A C     
465  O O     . THR A 76  ? 0.20229 0.27157 0.27443 -0.05464 -0.05082 -0.00487 70  THR A O     
466  C CB    . THR A 76  ? 0.24454 0.31148 0.35303 -0.13724 0.01260  -0.07513 70  THR A CB    
467  O OG1   . THR A 76  ? 0.28292 0.34208 0.32600 -0.16283 0.02409  -0.03905 70  THR A OG1   
468  C CG2   . THR A 76  ? 0.23554 0.33422 0.41278 -0.13523 0.01627  -0.08324 70  THR A CG2   
469  N N     . SER A 77  ? 0.18721 0.23788 0.24051 -0.02803 -0.01105 -0.01899 71  SER A N     
470  C CA    . SER A 77  ? 0.19707 0.24042 0.21880 0.01154  -0.02097 0.01558  71  SER A CA    
471  C C     . SER A 77  ? 0.17062 0.21975 0.21143 0.00120  -0.01085 0.02443  71  SER A C     
472  O O     . SER A 77  ? 0.14888 0.20293 0.19583 0.02820  -0.00907 0.00655  71  SER A O     
473  C CB    . SER A 77  ? 0.23835 0.28748 0.26492 0.04993  0.00794  0.02923  71  SER A CB    
474  O OG    . SER A 77  ? 0.25166 0.34861 0.25200 0.04505  0.00186  -0.01282 71  SER A OG    
475  N N     . ALA A 78  ? 0.16463 0.22987 0.24911 -0.01646 -0.00454 0.00853  72  ALA A N     
476  C CA    . ALA A 78  ? 0.15728 0.21691 0.26044 -0.00469 -0.00204 0.02234  72  ALA A CA    
477  C C     . ALA A 78  ? 0.16252 0.21552 0.25036 0.00360  -0.02529 0.02385  72  ALA A C     
478  O O     . ALA A 78  ? 0.18366 0.21050 0.25139 0.00192  -0.05325 0.01333  72  ALA A O     
479  C CB    . ALA A 78  ? 0.16452 0.21772 0.26336 0.00545  0.02975  0.02242  72  ALA A CB    
480  N N     . GLY A 79  ? 0.15367 0.21463 0.23066 -0.00171 0.00130  0.00827  73  GLY A N     
481  C CA    . GLY A 79  ? 0.13471 0.22290 0.21277 -0.02833 -0.00368 0.02277  73  GLY A CA    
482  C C     . GLY A 79  ? 0.14792 0.21299 0.21573 -0.02081 -0.00585 0.01699  73  GLY A C     
483  O O     . GLY A 79  ? 0.15693 0.22153 0.22654 -0.00222 -0.02715 0.03184  73  GLY A O     
484  N N     . PHE A 80  ? 0.16126 0.20483 0.24798 -0.01521 0.03160  -0.00131 74  PHE A N     
485  C CA    . PHE A 80  ? 0.15063 0.20636 0.26389 -0.01550 -0.01269 -0.01491 74  PHE A CA    
486  C C     . PHE A 80  ? 0.14858 0.19714 0.25418 -0.01632 -0.02078 0.00469  74  PHE A C     
487  O O     . PHE A 80  ? 0.14797 0.21205 0.24875 -0.00477 -0.02331 0.03462  74  PHE A O     
488  C CB    . PHE A 80  ? 0.15366 0.19991 0.24223 0.01042  -0.01769 -0.03776 74  PHE A CB    
489  C CG    . PHE A 80  ? 0.17332 0.21773 0.27282 0.01723  -0.03643 -0.00307 74  PHE A CG    
490  C CD1   . PHE A 80  ? 0.19018 0.22463 0.27834 0.02526  -0.01977 -0.01856 74  PHE A CD1   
491  C CD2   . PHE A 80  ? 0.16043 0.22449 0.25987 0.03809  -0.07293 0.01798  74  PHE A CD2   
492  C CE1   . PHE A 80  ? 0.17975 0.24220 0.27883 0.02109  -0.02480 -0.03535 74  PHE A CE1   
493  C CE2   . PHE A 80  ? 0.16929 0.23788 0.30946 0.02124  -0.06226 0.01794  74  PHE A CE2   
494  C CZ    . PHE A 80  ? 0.17713 0.24691 0.27062 0.01184  -0.03900 -0.01041 74  PHE A CZ    
495  N N     . PRO A 81  ? 0.14571 0.20218 0.23925 -0.02477 -0.02805 0.00800  75  PRO A N     
496  C CA    . PRO A 81  ? 0.13641 0.19914 0.25578 -0.02070 -0.04218 -0.00640 75  PRO A CA    
497  C C     . PRO A 81  ? 0.12620 0.18798 0.24633 -0.00686 -0.03382 0.00337  75  PRO A C     
498  O O     . PRO A 81  ? 0.12281 0.19973 0.28970 -0.00234 0.01337  0.01627  75  PRO A O     
499  C CB    . PRO A 81  ? 0.15332 0.20797 0.24922 -0.02435 -0.05941 -0.02546 75  PRO A CB    
500  C CG    . PRO A 81  ? 0.17581 0.21190 0.28188 -0.03026 -0.02990 -0.01105 75  PRO A CG    
501  C CD    . PRO A 81  ? 0.16828 0.21046 0.25231 -0.03479 -0.05542 0.01743  75  PRO A CD    
502  N N     . HIS A 82  ? 0.12052 0.17228 0.23046 -0.00374 -0.03257 0.01788  76  HIS A N     
503  C CA    . HIS A 82  ? 0.14292 0.17150 0.24543 -0.00569 -0.02927 -0.02103 76  HIS A CA    
504  C C     . HIS A 82  ? 0.12025 0.20410 0.26073 0.02082  0.00491  -0.02463 76  HIS A C     
505  O O     . HIS A 82  ? 0.09567 0.23586 0.27566 0.03331  0.02086  -0.01678 76  HIS A O     
506  C CB    . HIS A 82  ? 0.17798 0.17690 0.27331 -0.01649 -0.02464 -0.00988 76  HIS A CB    
507  C CG    . HIS A 82  ? 0.22080 0.17037 0.31117 -0.02982 -0.02492 -0.01764 76  HIS A CG    
508  N ND1   . HIS A 82  ? 0.23012 0.17011 0.32119 -0.03301 -0.03541 -0.02014 76  HIS A ND1   
509  C CD2   . HIS A 82  ? 0.23785 0.16745 0.30284 -0.03616 -0.03180 -0.00315 76  HIS A CD2   
510  C CE1   . HIS A 82  ? 0.22847 0.14475 0.30210 -0.06647 -0.03546 -0.03557 76  HIS A CE1   
511  N NE2   . HIS A 82  ? 0.23552 0.16538 0.31118 -0.04710 -0.04681 -0.04944 76  HIS A NE2   
512  N N     . VAL A 83  ? 0.11194 0.19268 0.27151 0.01070  0.01856  -0.00488 77  VAL A N     
513  C CA    . VAL A 83  ? 0.12040 0.19141 0.23981 0.01327  -0.06106 -0.00497 77  VAL A CA    
514  C C     . VAL A 83  ? 0.11091 0.17028 0.24400 0.02869  -0.03248 -0.01309 77  VAL A C     
515  O O     . VAL A 83  ? 0.11641 0.15502 0.27681 0.04382  -0.01700 -0.01158 77  VAL A O     
516  C CB    . VAL A 83  ? 0.12648 0.21255 0.28104 0.03233  -0.05303 0.02182  77  VAL A CB    
517  C CG1   . VAL A 83  ? 0.14211 0.21708 0.27491 0.05794  -0.05783 0.03154  77  VAL A CG1   
518  C CG2   . VAL A 83  ? 0.17199 0.23565 0.24136 0.02542  -0.02814 0.02988  77  VAL A CG2   
519  N N     . PRO A 84  ? 0.10350 0.17190 0.24812 0.01714  -0.02561 0.01284  78  PRO A N     
520  C CA    . PRO A 84  ? 0.10559 0.18963 0.24590 -0.00521 -0.02774 0.01516  78  PRO A CA    
521  C C     . PRO A 84  ? 0.08787 0.19379 0.22696 -0.00041 -0.01434 -0.00473 78  PRO A C     
522  O O     . PRO A 84  ? 0.10853 0.19592 0.24372 0.01740  -0.02702 -0.00499 78  PRO A O     
523  C CB    . PRO A 84  ? 0.10913 0.19305 0.22918 0.01455  -0.02458 -0.00638 78  PRO A CB    
524  C CG    . PRO A 84  ? 0.08326 0.18486 0.19505 0.01235  -0.05192 -0.01746 78  PRO A CG    
525  C CD    . PRO A 84  ? 0.09647 0.18872 0.24056 0.01821  -0.03503 -0.01046 78  PRO A CD    
526  N N     . GLY A 85  ? 0.09922 0.20826 0.23668 -0.01566 -0.01387 0.00857  79  GLY A N     
527  C CA    . GLY A 85  ? 0.10079 0.19053 0.23310 -0.01149 -0.01357 0.01272  79  GLY A CA    
528  C C     . GLY A 85  ? 0.09961 0.19833 0.22862 0.00939  -0.00876 0.00792  79  GLY A C     
529  O O     . GLY A 85  ? 0.11733 0.21663 0.18689 0.01794  0.00630  0.00749  79  GLY A O     
530  N N     . ILE A 86  ? 0.09915 0.17989 0.26198 0.00394  -0.00598 -0.01041 80  ILE A N     
531  C CA    . ILE A 86  ? 0.11858 0.19577 0.28304 0.00020  0.01191  -0.03622 80  ILE A CA    
532  C C     . ILE A 86  ? 0.12300 0.22322 0.32510 -0.01038 0.02720  -0.02881 80  ILE A C     
533  O O     . ILE A 86  ? 0.09960 0.23769 0.33383 0.00415  0.00101  -0.02777 80  ILE A O     
534  C CB    . ILE A 86  ? 0.16102 0.20144 0.26591 -0.02393 -0.01810 -0.03836 80  ILE A CB    
535  C CG1   . ILE A 86  ? 0.17311 0.23249 0.29071 -0.01148 -0.01691 -0.08711 80  ILE A CG1   
536  C CG2   . ILE A 86  ? 0.19217 0.20227 0.31217 -0.00073 -0.03993 -0.02405 80  ILE A CG2   
537  C CD1   . ILE A 86  ? 0.18825 0.26557 0.26539 -0.02165 -0.02641 -0.06371 80  ILE A CD1   
538  N N     . PHE A 87  ? 0.12971 0.24300 0.28629 -0.00881 0.02011  -0.02316 81  PHE A N     
539  C CA    . PHE A 87  ? 0.13838 0.25077 0.28761 0.00096  0.00655  -0.01390 81  PHE A CA    
540  C C     . PHE A 87  ? 0.13445 0.27874 0.30363 0.00796  0.01416  -0.00445 81  PHE A C     
541  O O     . PHE A 87  ? 0.13819 0.31051 0.30893 0.00671  0.04879  0.01591  81  PHE A O     
542  C CB    . PHE A 87  ? 0.15549 0.24269 0.29272 0.00015  -0.00782 -0.00827 81  PHE A CB    
543  C CG    . PHE A 87  ? 0.15476 0.24879 0.32276 0.00712  0.00138  -0.03095 81  PHE A CG    
544  C CD1   . PHE A 87  ? 0.15168 0.24564 0.31013 0.00489  0.00448  -0.03386 81  PHE A CD1   
545  C CD2   . PHE A 87  ? 0.17091 0.25571 0.33838 0.00405  0.03019  -0.04675 81  PHE A CD2   
546  C CE1   . PHE A 87  ? 0.18405 0.24373 0.29997 0.02428  0.03559  -0.04260 81  PHE A CE1   
547  C CE2   . PHE A 87  ? 0.18346 0.25640 0.36341 0.01888  0.05253  -0.04640 81  PHE A CE2   
548  C CZ    . PHE A 87  ? 0.17982 0.25296 0.34585 0.02364  0.05774  -0.04050 81  PHE A CZ    
549  N N     . THR A 88  ? 0.15242 0.27909 0.32415 0.02236  -0.02676 0.01151  82  THR A N     
550  C CA    . THR A 88  ? 0.14439 0.28544 0.32384 0.03202  -0.01781 0.02403  82  THR A CA    
551  C C     . THR A 88  ? 0.14342 0.30756 0.32376 0.03236  -0.03762 0.02857  82  THR A C     
552  O O     . THR A 88  ? 0.13573 0.32128 0.27730 0.01515  -0.04452 0.02693  82  THR A O     
553  C CB    . THR A 88  ? 0.17251 0.28109 0.32652 0.02020  -0.01147 0.02806  82  THR A CB    
554  O OG1   . THR A 88  ? 0.14843 0.27126 0.36012 0.00174  -0.01329 0.00908  82  THR A OG1   
555  C CG2   . THR A 88  ? 0.19710 0.26687 0.30347 0.02047  -0.00960 0.03185  82  THR A CG2   
556  N N     . LYS A 89  ? 0.14247 0.32543 0.33811 0.02924  -0.04381 0.05164  83  LYS A N     
557  C CA    . LYS A 89  ? 0.16286 0.32358 0.35377 0.04286  -0.03580 0.07610  83  LYS A CA    
558  C C     . LYS A 89  ? 0.18632 0.28807 0.37521 0.03611  -0.02790 0.04664  83  LYS A C     
559  O O     . LYS A 89  ? 0.18841 0.26908 0.36336 0.03837  -0.03455 -0.00613 83  LYS A O     
560  C CB    . LYS A 89  ? 0.18991 0.35558 0.34770 0.03420  -0.05539 0.08365  83  LYS A CB    
561  N N     . GLU A 90  ? 0.19224 0.27134 0.40286 0.03166  -0.02426 0.03904  84  GLU A N     
562  C CA    . GLU A 90  ? 0.19365 0.26017 0.39959 0.02546  -0.01434 0.02567  84  GLU A CA    
563  C C     . GLU A 90  ? 0.17786 0.23794 0.35032 0.01993  -0.00616 0.02681  84  GLU A C     
564  O O     . GLU A 90  ? 0.17181 0.20078 0.36261 0.01061  -0.02431 0.07448  84  GLU A O     
565  C CB    . GLU A 90  ? 0.22313 0.27496 0.43302 0.02329  -0.00076 -0.01649 84  GLU A CB    
566  C CG    . GLU A 90  ? 0.27895 0.29696 0.48532 0.01357  0.00078  -0.02585 84  GLU A CG    
567  C CD    . GLU A 90  ? 0.32548 0.33111 0.56106 0.01080  -0.01034 0.00361  84  GLU A CD    
568  O OE1   . GLU A 90  ? 0.33534 0.34334 0.59132 0.03334  -0.01343 -0.00924 84  GLU A OE1   
569  O OE2   . GLU A 90  ? 0.34425 0.35570 0.59514 -0.02677 -0.02248 0.02148  84  GLU A OE2   
570  N N     . GLN A 91  ? 0.16599 0.23444 0.29227 0.02063  -0.02636 0.01238  85  GLN A N     
571  C CA    . GLN A 91  ? 0.17037 0.23525 0.23146 0.02552  -0.02444 -0.01819 85  GLN A CA    
572  C C     . GLN A 91  ? 0.15453 0.24836 0.25101 0.02125  -0.01779 0.00135  85  GLN A C     
573  O O     . GLN A 91  ? 0.12472 0.25328 0.28267 0.02712  -0.01509 -0.00441 85  GLN A O     
574  C CB    . GLN A 91  ? 0.17382 0.21949 0.19804 0.02026  -0.02774 -0.00935 85  GLN A CB    
575  C CG    . GLN A 91  ? 0.17024 0.22040 0.20450 0.00558  -0.00422 -0.00308 85  GLN A CG    
576  C CD    . GLN A 91  ? 0.15486 0.23644 0.23871 -0.00436 -0.00001 0.00381  85  GLN A CD    
577  O OE1   . GLN A 91  ? 0.11830 0.24896 0.27174 -0.02101 0.02959  0.00474  85  GLN A OE1   
578  N NE2   . GLN A 91  ? 0.17982 0.25459 0.22755 -0.00471 0.01718  0.01722  85  GLN A NE2   
579  N N     . VAL A 92  ? 0.12631 0.24155 0.23004 0.02189  -0.03324 0.01525  86  VAL A N     
580  C CA    . VAL A 92  ? 0.13964 0.26672 0.25998 0.02923  0.00133  -0.01317 86  VAL A CA    
581  C C     . VAL A 92  ? 0.15542 0.26824 0.26509 0.04089  -0.02243 -0.00528 86  VAL A C     
582  O O     . VAL A 92  ? 0.14856 0.27239 0.29425 0.04560  -0.03963 0.00685  86  VAL A O     
583  C CB    . VAL A 92  ? 0.16250 0.27820 0.29132 0.01769  0.02112  -0.02991 86  VAL A CB    
584  C CG1   . VAL A 92  ? 0.16702 0.28659 0.29353 0.02306  0.01721  -0.01473 86  VAL A CG1   
585  C CG2   . VAL A 92  ? 0.16742 0.26684 0.31416 0.03859  0.03803  -0.02457 86  VAL A CG2   
586  N N     . ARG A 93  ? 0.18754 0.27512 0.30646 0.03777  -0.05042 -0.01996 87  ARG A N     
587  C CA    . ARG A 93  ? 0.21831 0.28401 0.34335 0.06328  -0.05003 -0.01508 87  ARG A CA    
588  C C     . ARG A 93  ? 0.19733 0.27282 0.31749 0.05331  -0.04230 -0.00752 87  ARG A C     
589  O O     . ARG A 93  ? 0.18405 0.26384 0.27823 0.04902  -0.03544 0.01022  87  ARG A O     
590  C CB    . ARG A 93  ? 0.27543 0.30465 0.40472 0.10853  -0.05007 -0.04684 87  ARG A CB    
591  C CG    . ARG A 93  ? 0.34957 0.32593 0.50506 0.13238  -0.06518 -0.04289 87  ARG A CG    
592  C CD    . ARG A 93  ? 0.41216 0.35026 0.57835 0.13531  -0.07819 -0.05704 87  ARG A CD    
593  N NE    . ARG A 93  ? 0.44836 0.37229 0.62866 0.12707  -0.09242 -0.05716 87  ARG A NE    
594  C CZ    . ARG A 93  ? 0.47392 0.39384 0.64232 0.11667  -0.09825 -0.04590 87  ARG A CZ    
595  N NH1   . ARG A 93  ? 0.48066 0.40899 0.65913 0.10344  -0.09833 -0.03029 87  ARG A NH1   
596  N NH2   . ARG A 93  ? 0.48385 0.39411 0.64420 0.11921  -0.10538 -0.04502 87  ARG A NH2   
597  N N     . GLU A 94  ? 0.18946 0.26721 0.23231 0.05117  -0.05847 -0.00582 88  GLU A N     
598  C CA    . GLU A 94  ? 0.20575 0.25190 0.26139 0.04225  -0.03240 -0.00167 88  GLU A CA    
599  C C     . GLU A 94  ? 0.18056 0.25500 0.25218 0.03717  -0.00540 0.02012  88  GLU A C     
600  O O     . GLU A 94  ? 0.17283 0.27867 0.30319 0.02192  0.00039  0.05636  88  GLU A O     
601  C CB    . GLU A 94  ? 0.24116 0.23835 0.32129 0.04565  -0.02398 -0.00897 88  GLU A CB    
602  C CG    . GLU A 94  ? 0.26618 0.22961 0.37043 0.04394  -0.00827 0.02068  88  GLU A CG    
603  C CD    . GLU A 94  ? 0.31219 0.26834 0.50782 0.05195  0.00247  0.06350  88  GLU A CD    
604  O OE1   . GLU A 94  ? 0.33096 0.25726 0.51795 0.02370  0.03860  0.10543  88  GLU A OE1   
605  O OE2   . GLU A 94  ? 0.33566 0.30564 0.56624 0.05492  -0.01207 0.10105  88  GLU A OE2   
606  N N     . TRP A 95  ? 0.16586 0.21936 0.23939 0.01935  0.01282  -0.01405 89  TRP A N     
607  C CA    . TRP A 95  ? 0.14357 0.20349 0.20738 0.02389  0.04034  0.01014  89  TRP A CA    
608  C C     . TRP A 95  ? 0.13235 0.21396 0.23169 0.02440  0.03148  0.00836  89  TRP A C     
609  O O     . TRP A 95  ? 0.12654 0.22033 0.28477 0.02562  0.03100  0.02583  89  TRP A O     
610  C CB    . TRP A 95  ? 0.15596 0.20230 0.18760 0.01731  0.00379  0.00125  89  TRP A CB    
611  C CG    . TRP A 95  ? 0.15248 0.20200 0.23905 0.01753  -0.00631 0.01096  89  TRP A CG    
612  C CD1   . TRP A 95  ? 0.15311 0.18845 0.25189 0.00939  -0.01012 -0.02646 89  TRP A CD1   
613  C CD2   . TRP A 95  ? 0.14428 0.20170 0.25587 0.01609  -0.00428 -0.02494 89  TRP A CD2   
614  N NE1   . TRP A 95  ? 0.13821 0.18857 0.23690 -0.00832 -0.01543 -0.02045 89  TRP A NE1   
615  C CE2   . TRP A 95  ? 0.13364 0.19893 0.23516 0.00731  -0.01399 -0.02072 89  TRP A CE2   
616  C CE3   . TRP A 95  ? 0.14262 0.19487 0.28862 0.01095  -0.01172 -0.01681 89  TRP A CE3   
617  C CZ2   . TRP A 95  ? 0.14848 0.19907 0.23939 0.01311  -0.02344 -0.01005 89  TRP A CZ2   
618  C CZ3   . TRP A 95  ? 0.15467 0.20287 0.21374 -0.01476 -0.01187 -0.03612 89  TRP A CZ3   
619  C CH2   . TRP A 95  ? 0.16345 0.19817 0.21826 -0.00431 -0.03136 -0.04572 89  TRP A CH2   
620  N N     . LYS A 96  ? 0.14910 0.22864 0.26814 0.00718  0.01348  0.00597  90  LYS A N     
621  C CA    . LYS A 96  ? 0.17526 0.25739 0.29208 0.02963  -0.01071 -0.01617 90  LYS A CA    
622  C C     . LYS A 96  ? 0.19854 0.24767 0.25776 0.03676  -0.02671 0.00123  90  LYS A C     
623  O O     . LYS A 96  ? 0.21078 0.25721 0.28150 0.04424  -0.02902 -0.02934 90  LYS A O     
624  C CB    . LYS A 96  ? 0.22541 0.30342 0.35211 0.05775  -0.07026 -0.01873 90  LYS A CB    
625  C CG    . LYS A 96  ? 0.27445 0.35716 0.51635 0.05851  -0.08411 -0.00144 90  LYS A CG    
626  C CD    . LYS A 96  ? 0.31625 0.40133 0.63299 0.04315  -0.08643 -0.00104 90  LYS A CD    
627  C CE    . LYS A 96  ? 0.35591 0.43158 0.72976 0.01990  -0.07867 0.00348  90  LYS A CE    
628  N NZ    . LYS A 96  ? 0.37334 0.45165 0.77778 0.01797  -0.07994 0.01290  90  LYS A NZ    
629  N N     . LYS A 97  ? 0.18923 0.23091 0.28561 0.02720  -0.01724 0.00296  91  LYS A N     
630  C CA    . LYS A 97  ? 0.18853 0.23055 0.27240 0.01452  -0.01559 0.02862  91  LYS A CA    
631  C C     . LYS A 97  ? 0.17841 0.25317 0.27880 -0.00959 0.00262  0.03793  91  LYS A C     
632  O O     . LYS A 97  ? 0.18919 0.27660 0.27674 -0.01876 0.01261  0.05804  91  LYS A O     
633  C CB    . LYS A 97  ? 0.21091 0.21839 0.31626 0.03315  -0.01283 0.00852  91  LYS A CB    
634  C CG    . LYS A 97  ? 0.23056 0.22648 0.32713 0.05365  -0.02685 0.01567  91  LYS A CG    
635  C CD    . LYS A 97  ? 0.27023 0.25280 0.42415 0.05286  -0.02083 0.00140  91  LYS A CD    
636  C CE    . LYS A 97  ? 0.31892 0.26770 0.51579 0.04186  -0.01110 -0.03689 91  LYS A CE    
637  N NZ    . LYS A 97  ? 0.35787 0.30310 0.58128 0.03568  0.00189  -0.03604 91  LYS A NZ    
638  N N     . ILE A 98  ? 0.16358 0.26927 0.24548 -0.01604 -0.03577 0.04065  92  ILE A N     
639  C CA    . ILE A 98  ? 0.15357 0.26501 0.27898 -0.01756 -0.03420 0.00455  92  ILE A CA    
640  C C     . ILE A 98  ? 0.14586 0.25391 0.25624 -0.00727 0.00855  0.00745  92  ILE A C     
641  O O     . ILE A 98  ? 0.15360 0.24735 0.27116 0.01521  0.03924  -0.00797 92  ILE A O     
642  C CB    . ILE A 98  ? 0.17562 0.28642 0.24220 -0.01434 -0.03962 -0.03515 92  ILE A CB    
643  C CG1   . ILE A 98  ? 0.21153 0.31650 0.24409 -0.03317 -0.04776 -0.02867 92  ILE A CG1   
644  C CG2   . ILE A 98  ? 0.18514 0.30899 0.28363 -0.00910 -0.05181 -0.03843 92  ILE A CG2   
645  C CD1   . ILE A 98  ? 0.22815 0.33042 0.28798 -0.03410 -0.06955 -0.01821 92  ILE A CD1   
646  N N     . VAL A 99  ? 0.14328 0.23809 0.22903 -0.02122 -0.00487 0.00640  93  VAL A N     
647  C CA    . VAL A 99  ? 0.16396 0.23253 0.20099 -0.02918 0.00335  -0.01231 93  VAL A CA    
648  C C     . VAL A 99  ? 0.17462 0.24234 0.23799 -0.01589 -0.02456 0.00919  93  VAL A C     
649  O O     . VAL A 99  ? 0.17878 0.26649 0.24072 -0.00124 -0.03059 0.01942  93  VAL A O     
650  C CB    . VAL A 99  ? 0.17310 0.21703 0.23225 -0.03726 -0.00001 -0.00805 93  VAL A CB    
651  C CG1   . VAL A 99  ? 0.20765 0.23490 0.27207 -0.03451 0.02533  0.00355  93  VAL A CG1   
652  C CG2   . VAL A 99  ? 0.17337 0.21537 0.26517 -0.03083 0.01697  -0.00252 93  VAL A CG2   
653  N N     . ASP A 100 ? 0.18720 0.24390 0.26293 0.00419  -0.03552 0.03307  94  ASP A N     
654  C CA    . ASP A 100 ? 0.20862 0.25577 0.28170 0.00934  -0.03524 0.00939  94  ASP A CA    
655  C C     . ASP A 100 ? 0.20684 0.24376 0.26728 -0.02372 -0.03808 0.04617  94  ASP A C     
656  O O     . ASP A 100 ? 0.20719 0.23457 0.27191 -0.02303 -0.02228 0.05879  94  ASP A O     
657  C CB    . ASP A 100 ? 0.23974 0.28045 0.33694 0.02248  -0.06552 0.01745  94  ASP A CB    
658  C CG    . ASP A 100 ? 0.27528 0.31467 0.40291 0.03230  -0.05571 0.01410  94  ASP A CG    
659  O OD1   . ASP A 100 ? 0.28428 0.33980 0.44411 0.01944  -0.07106 -0.01000 94  ASP A OD1   
660  O OD2   . ASP A 100 ? 0.30048 0.33648 0.42122 0.03804  -0.02112 -0.00011 94  ASP A OD2   
661  N N     . VAL A 101 ? 0.21567 0.24756 0.25145 -0.03287 -0.05316 0.04073  95  VAL A N     
662  C CA    . VAL A 101 ? 0.18421 0.22716 0.28473 -0.03407 -0.06494 0.04578  95  VAL A CA    
663  C C     . VAL A 101 ? 0.19149 0.21873 0.26519 -0.03754 -0.01947 0.03306  95  VAL A C     
664  O O     . VAL A 101 ? 0.18315 0.23524 0.30178 -0.02070 0.01410  0.02869  95  VAL A O     
665  C CB    . VAL A 101 ? 0.19289 0.24431 0.35748 -0.02053 -0.09354 0.06635  95  VAL A CB    
666  C CG1   . VAL A 101 ? 0.21202 0.25957 0.40332 -0.01742 -0.11051 0.07714  95  VAL A CG1   
667  C CG2   . VAL A 101 ? 0.18139 0.26203 0.37766 -0.04638 -0.05721 0.02098  95  VAL A CG2   
668  N N     . VAL A 102 ? 0.18763 0.20577 0.22037 -0.03124 -0.03380 0.01334  96  VAL A N     
669  C CA    . VAL A 102 ? 0.18670 0.21363 0.16619 -0.03047 -0.03012 0.03336  96  VAL A CA    
670  C C     . VAL A 102 ? 0.19013 0.23743 0.20608 -0.01555 0.01887  0.02664  96  VAL A C     
671  O O     . VAL A 102 ? 0.19798 0.22718 0.19814 -0.02201 0.01906  -0.00712 96  VAL A O     
672  C CB    . VAL A 102 ? 0.21677 0.21072 0.17322 -0.01461 -0.04971 0.01587  96  VAL A CB    
673  C CG1   . VAL A 102 ? 0.23472 0.22867 0.23404 -0.02646 -0.02479 0.03448  96  VAL A CG1   
674  C CG2   . VAL A 102 ? 0.21774 0.21424 0.17444 -0.01854 -0.04858 -0.00673 96  VAL A CG2   
675  N N     . HIS A 103 ? 0.17570 0.25716 0.21765 -0.03401 -0.00507 0.02056  97  HIS A N     
676  C CA    . HIS A 103 ? 0.16111 0.24370 0.21277 -0.03437 -0.00917 0.00072  97  HIS A CA    
677  C C     . HIS A 103 ? 0.19588 0.23845 0.18828 -0.01862 -0.01371 0.01052  97  HIS A C     
678  O O     . HIS A 103 ? 0.21116 0.25257 0.23167 -0.00464 0.00408  0.00424  97  HIS A O     
679  C CB    . HIS A 103 ? 0.13118 0.24220 0.24146 -0.04170 0.03391  0.01396  97  HIS A CB    
680  C CG    . HIS A 103 ? 0.10856 0.25226 0.26105 -0.02767 0.04909  0.03244  97  HIS A CG    
681  N ND1   . HIS A 103 ? 0.13185 0.27911 0.29820 -0.00976 0.03562  0.05352  97  HIS A ND1   
682  C CD2   . HIS A 103 ? 0.09993 0.25046 0.22986 -0.02897 -0.00140 0.02738  97  HIS A CD2   
683  C CE1   . HIS A 103 ? 0.13749 0.26722 0.28851 0.01127  -0.02740 0.07353  97  HIS A CE1   
684  N NE2   . HIS A 103 ? 0.11415 0.26157 0.26703 -0.00065 -0.03434 0.05339  97  HIS A NE2   
685  N N     . ALA A 104 ? 0.21652 0.23069 0.21229 -0.01058 0.00271  0.04473  98  ALA A N     
686  C CA    . ALA A 104 ? 0.23402 0.22724 0.24067 0.01327  0.01848  0.03581  98  ALA A CA    
687  C C     . ALA A 104 ? 0.25982 0.23782 0.27534 0.01497  0.02954  0.03688  98  ALA A C     
688  O O     . ALA A 104 ? 0.29046 0.24263 0.29393 0.02048  0.02003  0.02676  98  ALA A O     
689  C CB    . ALA A 104 ? 0.24485 0.21701 0.25719 0.02755  0.01093  0.03621  98  ALA A CB    
690  N N     . LYS A 105 ? 0.24160 0.24694 0.27310 0.01072  0.02163  0.03870  99  LYS A N     
691  C CA    . LYS A 105 ? 0.24947 0.26993 0.28199 0.00227  0.02054  0.06629  99  LYS A CA    
692  C C     . LYS A 105 ? 0.23077 0.26006 0.24977 0.00991  0.02066  0.05589  99  LYS A C     
693  O O     . LYS A 105 ? 0.22460 0.26593 0.28807 0.03233  0.05644  0.02592  99  LYS A O     
694  C CB    . LYS A 105 ? 0.26631 0.30602 0.34820 -0.01595 0.03528  0.10744  99  LYS A CB    
695  C CG    . LYS A 105 ? 0.30480 0.34099 0.40366 -0.00554 0.03879  0.10310  99  LYS A CG    
696  C CD    . LYS A 105 ? 0.33129 0.37798 0.43141 -0.03359 0.05689  0.08858  99  LYS A CD    
697  C CE    . LYS A 105 ? 0.33340 0.40533 0.46264 -0.02620 0.06947  0.07274  99  LYS A CE    
698  N NZ    . LYS A 105 ? 0.32792 0.41042 0.45185 -0.00406 0.06364  0.07255  99  LYS A NZ    
699  N N     . GLY A 106 ? 0.23327 0.25040 0.21588 -0.00449 -0.00548 0.06868  100 GLY A N     
700  C CA    . GLY A 106 ? 0.22818 0.26693 0.25287 0.00123  0.00171  0.06978  100 GLY A CA    
701  C C     . GLY A 106 ? 0.19188 0.27073 0.23931 -0.00772 -0.00106 0.05268  100 GLY A C     
702  O O     . GLY A 106 ? 0.18204 0.28199 0.22441 -0.00758 -0.01899 0.02957  100 GLY A O     
703  N N     . ALA A 107 ? 0.15835 0.26183 0.22823 -0.01410 -0.01027 0.02958  101 ALA A N     
704  C CA    . ALA A 107 ? 0.14333 0.23401 0.24158 -0.02677 0.00408  0.02466  101 ALA A CA    
705  C C     . ALA A 107 ? 0.12288 0.23895 0.24270 -0.01657 0.00192  0.02302  101 ALA A C     
706  O O     . ALA A 107 ? 0.11803 0.27279 0.24890 0.02125  -0.00674 0.04826  101 ALA A O     
707  C CB    . ALA A 107 ? 0.15070 0.23310 0.28161 -0.03037 0.00851  -0.01791 101 ALA A CB    
708  N N     . VAL A 108 ? 0.12947 0.20085 0.20535 -0.04176 0.02941  0.00173  102 VAL A N     
709  C CA    . VAL A 108 ? 0.12013 0.19805 0.20189 -0.04275 0.00955  -0.00124 102 VAL A CA    
710  C C     . VAL A 108 ? 0.11114 0.20368 0.18659 -0.02799 0.01023  -0.00095 102 VAL A C     
711  O O     . VAL A 108 ? 0.11710 0.22028 0.22297 -0.03439 -0.01747 -0.02418 102 VAL A O     
712  C CB    . VAL A 108 ? 0.13324 0.21650 0.19390 -0.03563 0.00235  -0.03759 102 VAL A CB    
713  C CG1   . VAL A 108 ? 0.11750 0.22612 0.24524 -0.02518 -0.02936 -0.00232 102 VAL A CG1   
714  C CG2   . VAL A 108 ? 0.15756 0.23649 0.21850 -0.02032 -0.00635 -0.05202 102 VAL A CG2   
715  N N     . ILE A 109 ? 0.10924 0.18543 0.19849 -0.00353 0.00271  0.00780  103 ILE A N     
716  C CA    . ILE A 109 ? 0.10115 0.18589 0.18482 -0.00370 0.00228  0.00389  103 ILE A CA    
717  C C     . ILE A 109 ? 0.07425 0.18210 0.22073 -0.00923 0.00468  -0.00352 103 ILE A C     
718  O O     . ILE A 109 ? 0.09145 0.18897 0.25217 -0.01264 0.01128  0.00447  103 ILE A O     
719  C CB    . ILE A 109 ? 0.11331 0.20362 0.23857 -0.02592 -0.05248 0.00147  103 ILE A CB    
720  C CG1   . ILE A 109 ? 0.14798 0.20274 0.29517 -0.02384 -0.03864 0.00501  103 ILE A CG1   
721  C CG2   . ILE A 109 ? 0.11133 0.22769 0.26896 -0.04112 -0.05962 0.00172  103 ILE A CG2   
722  C CD1   . ILE A 109 ? 0.17108 0.21491 0.27735 -0.03735 -0.04302 -0.03566 103 ILE A CD1   
723  N N     . PHE A 110 ? 0.08441 0.18515 0.19070 0.00661  -0.00852 0.00997  104 PHE A N     
724  C CA    . PHE A 110 ? 0.10073 0.18620 0.21426 0.01263  0.00473  -0.01358 104 PHE A CA    
725  C C     . PHE A 110 ? 0.10697 0.18838 0.25139 0.01337  -0.00620 -0.03943 104 PHE A C     
726  O O     . PHE A 110 ? 0.09552 0.19437 0.23658 -0.00432 -0.00882 -0.05680 104 PHE A O     
727  C CB    . PHE A 110 ? 0.10766 0.18409 0.20243 -0.00972 -0.00468 -0.00836 104 PHE A CB    
728  C CG    . PHE A 110 ? 0.10707 0.19215 0.19047 -0.02100 0.01893  -0.00090 104 PHE A CG    
729  C CD1   . PHE A 110 ? 0.10904 0.20146 0.19851 -0.03992 -0.00550 -0.01909 104 PHE A CD1   
730  C CD2   . PHE A 110 ? 0.13203 0.19205 0.17970 -0.00516 -0.01937 0.01341  104 PHE A CD2   
731  C CE1   . PHE A 110 ? 0.12162 0.18896 0.19051 -0.03588 -0.01419 0.00182  104 PHE A CE1   
732  C CE2   . PHE A 110 ? 0.14248 0.18827 0.22962 -0.01267 -0.01739 -0.00965 104 PHE A CE2   
733  C CZ    . PHE A 110 ? 0.13380 0.18952 0.22145 -0.02350 -0.01761 -0.02710 104 PHE A CZ    
734  N N     . CYS A 111 ? 0.11616 0.18130 0.16525 0.03742  0.00355  -0.04389 105 CYS A N     
735  C CA    . CYS A 111 ? 0.11041 0.17471 0.22141 0.02280  -0.03199 -0.04851 105 CYS A CA    
736  C C     . CYS A 111 ? 0.10829 0.18097 0.24871 0.01299  -0.04234 -0.00551 105 CYS A C     
737  O O     . CYS A 111 ? 0.11482 0.15099 0.22877 0.00026  -0.03512 0.00418  105 CYS A O     
738  C CB    . CYS A 111 ? 0.12114 0.17959 0.28000 0.02212  -0.05088 -0.04823 105 CYS A CB    
739  S SG    . CYS A 111 ? 0.12518 0.20126 0.27380 0.01044  -0.02530 -0.02073 105 CYS A SG    
740  N N     . GLN A 112 ? 0.08075 0.18790 0.24754 0.04146  -0.01602 -0.01074 106 GLN A N     
741  C CA    . GLN A 112 ? 0.07643 0.19509 0.23335 0.02937  -0.03238 0.01139  106 GLN A CA    
742  C C     . GLN A 112 ? 0.09750 0.19444 0.24164 0.01649  -0.01737 -0.00869 106 GLN A C     
743  O O     . GLN A 112 ? 0.11644 0.20237 0.27894 0.01170  0.00345  0.01173  106 GLN A O     
744  C CB    . GLN A 112 ? 0.08181 0.19528 0.17751 0.02555  -0.05288 0.01141  106 GLN A CB    
745  C CG    . GLN A 112 ? 0.07900 0.20882 0.20291 0.03330  -0.04397 0.01092  106 GLN A CG    
746  C CD    . GLN A 112 ? 0.09297 0.19721 0.20723 0.03052  -0.01783 0.00702  106 GLN A CD    
747  O OE1   . GLN A 112 ? 0.12433 0.17909 0.18999 0.03186  -0.01513 0.00135  106 GLN A OE1   
748  N NE2   . GLN A 112 ? 0.07927 0.17615 0.26048 0.03155  -0.01890 -0.00193 106 GLN A NE2   
749  N N     . LEU A 113 ? 0.09069 0.18880 0.19390 0.01119  -0.01094 -0.02344 107 LEU A N     
750  C CA    . LEU A 113 ? 0.07970 0.19301 0.18897 0.00471  -0.02645 -0.02394 107 LEU A CA    
751  C C     . LEU A 113 ? 0.10250 0.18924 0.19935 -0.01016 -0.01347 0.00034  107 LEU A C     
752  O O     . LEU A 113 ? 0.09615 0.19265 0.19001 0.01830  -0.01218 0.02852  107 LEU A O     
753  C CB    . LEU A 113 ? 0.07744 0.19823 0.18453 0.00447  -0.00308 -0.01553 107 LEU A CB    
754  C CG    . LEU A 113 ? 0.09629 0.21156 0.20763 -0.00842 -0.00955 0.01297  107 LEU A CG    
755  C CD1   . LEU A 113 ? 0.07183 0.22915 0.22550 -0.02922 -0.02886 -0.00627 107 LEU A CD1   
756  C CD2   . LEU A 113 ? 0.12185 0.19852 0.21259 0.03079  0.00041  0.04532  107 LEU A CD2   
757  N N     . TRP A 114 ? 0.11696 0.18965 0.20763 -0.03172 0.02770  -0.00337 108 TRP A N     
758  C CA    . TRP A 114 ? 0.11391 0.19959 0.19859 -0.02680 0.01974  -0.00384 108 TRP A CA    
759  C C     . TRP A 114 ? 0.16132 0.20949 0.22323 0.01429  0.00254  -0.01877 108 TRP A C     
760  O O     . TRP A 114 ? 0.21905 0.20408 0.23830 0.05723  0.03969  0.01721  108 TRP A O     
761  C CB    . TRP A 114 ? 0.09314 0.22796 0.25842 -0.02683 -0.01904 -0.00827 108 TRP A CB    
762  C CG    . TRP A 114 ? 0.10627 0.23490 0.25826 -0.01310 -0.01672 -0.02771 108 TRP A CG    
763  C CD1   . TRP A 114 ? 0.13603 0.25126 0.27097 -0.02441 -0.02016 -0.05068 108 TRP A CD1   
764  C CD2   . TRP A 114 ? 0.11109 0.24927 0.28145 -0.02095 -0.01407 -0.02289 108 TRP A CD2   
765  N NE1   . TRP A 114 ? 0.12165 0.25064 0.27353 -0.01621 -0.01713 -0.01547 108 TRP A NE1   
766  C CE2   . TRP A 114 ? 0.11418 0.25363 0.28305 -0.02633 -0.02648 -0.01740 108 TRP A CE2   
767  C CE3   . TRP A 114 ? 0.11111 0.25219 0.30520 -0.04059 -0.03918 -0.02838 108 TRP A CE3   
768  C CZ2   . TRP A 114 ? 0.12742 0.26831 0.29760 -0.02338 -0.03862 -0.01775 108 TRP A CZ2   
769  C CZ3   . TRP A 114 ? 0.12690 0.28147 0.27032 -0.03208 -0.06603 -0.04754 108 TRP A CZ3   
770  C CH2   . TRP A 114 ? 0.13753 0.28611 0.29916 -0.01478 -0.04179 -0.01993 108 TRP A CH2   
771  N N     . HIS A 115 ? 0.13395 0.19636 0.16482 -0.00747 0.01760  -0.00963 109 HIS A N     
772  C CA    . HIS A 115 ? 0.09965 0.22253 0.20949 -0.01086 0.01979  -0.01470 109 HIS A CA    
773  C C     . HIS A 115 ? 0.09759 0.21591 0.25302 -0.00934 -0.00988 -0.00131 109 HIS A C     
774  O O     . HIS A 115 ? 0.09446 0.20340 0.23267 0.00234  -0.01903 0.01794  109 HIS A O     
775  C CB    . HIS A 115 ? 0.08197 0.22801 0.19901 -0.00744 0.01437  -0.03176 109 HIS A CB    
776  C CG    . HIS A 115 ? 0.09946 0.20959 0.20223 0.00997  0.01465  0.00155  109 HIS A CG    
777  N ND1   . HIS A 115 ? 0.09695 0.18153 0.20041 0.01568  0.02878  -0.03785 109 HIS A ND1   
778  C CD2   . HIS A 115 ? 0.12015 0.21982 0.20996 0.01473  0.00932  0.00698  109 HIS A CD2   
779  C CE1   . HIS A 115 ? 0.08470 0.20542 0.23507 0.01983  0.00667  -0.02054 109 HIS A CE1   
780  N NE2   . HIS A 115 ? 0.10477 0.22529 0.24005 -0.00095 0.00699  -0.00797 109 HIS A NE2   
781  N N     . VAL A 116 ? 0.07308 0.20036 0.23896 -0.02360 -0.00579 0.01057  110 VAL A N     
782  C CA    . VAL A 116 ? 0.08974 0.18011 0.18776 -0.02607 0.00491  0.02512  110 VAL A CA    
783  C C     . VAL A 116 ? 0.11134 0.19386 0.21682 -0.00587 0.01340  0.01062  110 VAL A C     
784  O O     . VAL A 116 ? 0.13176 0.19109 0.19571 0.01261  0.00742  0.03052  110 VAL A O     
785  C CB    . VAL A 116 ? 0.10551 0.15925 0.17559 -0.00478 0.02459  -0.00781 110 VAL A CB    
786  C CG1   . VAL A 116 ? 0.09670 0.16577 0.19988 -0.01905 0.01104  -0.02821 110 VAL A CG1   
787  C CG2   . VAL A 116 ? 0.13086 0.15168 0.13474 0.00479  0.02678  0.00909  110 VAL A CG2   
788  N N     . GLY A 117 ? 0.10757 0.18870 0.21701 -0.02331 0.01978  -0.00806 111 GLY A N     
789  C CA    . GLY A 117 ? 0.12779 0.17843 0.23583 -0.01470 0.00953  -0.01821 111 GLY A CA    
790  C C     . GLY A 117 ? 0.11430 0.19234 0.21932 -0.01236 0.00071  0.00831  111 GLY A C     
791  O O     . GLY A 117 ? 0.14716 0.20136 0.18860 -0.00098 -0.01319 0.01707  111 GLY A O     
792  N N     . ARG A 118 ? 0.10948 0.19545 0.22154 -0.00248 -0.00793 0.01540  112 ARG A N     
793  C CA    . ARG A 118 ? 0.10782 0.18762 0.24440 -0.00989 -0.01216 0.01322  112 ARG A CA    
794  C C     . ARG A 118 ? 0.11912 0.19823 0.24301 -0.01290 0.00127  0.00614  112 ARG A C     
795  O O     . ARG A 118 ? 0.15255 0.17142 0.24249 -0.01721 0.04539  -0.02178 112 ARG A O     
796  C CB    . ARG A 118 ? 0.11205 0.16670 0.21989 0.03294  -0.01842 0.02251  112 ARG A CB    
797  C CG    . ARG A 118 ? 0.12696 0.15056 0.23604 0.04452  -0.01960 0.04230  112 ARG A CG    
798  C CD    . ARG A 118 ? 0.13125 0.17652 0.23716 0.04484  -0.03459 0.04660  112 ARG A CD    
799  N NE    . ARG A 118 ? 0.13319 0.17429 0.23026 0.03178  -0.04102 0.01796  112 ARG A NE    
800  C CZ    . ARG A 118 ? 0.15369 0.19676 0.26516 0.00361  -0.00662 0.01009  112 ARG A CZ    
801  N NH1   . ARG A 118 ? 0.15603 0.21711 0.22963 0.00170  0.01561  0.03938  112 ARG A NH1   
802  N NH2   . ARG A 118 ? 0.14703 0.20259 0.28408 -0.03335 0.04353  -0.01980 112 ARG A NH2   
803  N N     . ALA A 119 ? 0.09416 0.18788 0.21916 0.00640  0.00837  0.02043  113 ALA A N     
804  C CA    . ALA A 119 ? 0.09031 0.19253 0.23591 -0.01606 0.01209  0.02485  113 ALA A CA    
805  C C     . ALA A 119 ? 0.13205 0.18963 0.25186 -0.01327 0.00196  0.00357  113 ALA A C     
806  O O     . ALA A 119 ? 0.16018 0.19597 0.22020 -0.02099 -0.00034 0.03938  113 ALA A O     
807  C CB    . ALA A 119 ? 0.08806 0.19425 0.23675 -0.02416 0.00865  -0.00375 113 ALA A CB    
808  N N     . SER A 120 ? 0.13808 0.18420 0.22386 -0.00318 0.01685  -0.01118 114 SER A N     
809  C CA    . SER A 120 ? 0.14246 0.19571 0.24296 0.01061  -0.02484 -0.01449 114 SER A CA    
810  C C     . SER A 120 ? 0.15054 0.18531 0.24740 0.00311  -0.01206 -0.02115 114 SER A C     
811  O O     . SER A 120 ? 0.14692 0.18701 0.25488 -0.02110 0.01119  -0.03785 114 SER A O     
812  C CB    . SER A 120 ? 0.13252 0.21481 0.28111 0.00958  -0.01665 0.01415  114 SER A CB    
813  O OG    . SER A 120 ? 0.13339 0.20767 0.25446 -0.00050 0.00744  -0.00391 114 SER A OG    
814  N N     . HIS A 121 ? 0.16059 0.18281 0.29117 0.00786  -0.01944 -0.03080 115 HIS A N     
815  C CA    . HIS A 121 ? 0.18153 0.19123 0.29571 0.00610  -0.00943 -0.03848 115 HIS A CA    
816  C C     . HIS A 121 ? 0.18516 0.19919 0.25910 0.00076  0.00211  -0.04338 115 HIS A C     
817  O O     . HIS A 121 ? 0.17645 0.20102 0.25602 -0.01156 -0.01557 -0.06108 115 HIS A O     
818  C CB    . HIS A 121 ? 0.17703 0.17765 0.27956 -0.00184 -0.00276 -0.04385 115 HIS A CB    
819  C CG    . HIS A 121 ? 0.18777 0.18741 0.29872 -0.00755 0.00167  -0.05003 115 HIS A CG    
820  N ND1   . HIS A 121 ? 0.20801 0.19982 0.33009 -0.01597 0.01793  -0.03996 115 HIS A ND1   
821  C CD2   . HIS A 121 ? 0.20716 0.20197 0.33576 -0.01711 0.03733  -0.04765 115 HIS A CD2   
822  C CE1   . HIS A 121 ? 0.21166 0.19984 0.38349 -0.02730 0.01055  -0.03228 115 HIS A CE1   
823  N NE2   . HIS A 121 ? 0.21803 0.20617 0.38764 -0.03193 0.01625  -0.04587 115 HIS A NE2   
824  N N     . GLU A 122 ? 0.20379 0.21696 0.23087 0.02332  0.01865  -0.02850 116 GLU A N     
825  C CA    . GLU A 122 ? 0.23274 0.25749 0.24614 0.04794  0.07557  -0.05038 116 GLU A CA    
826  C C     . GLU A 122 ? 0.21271 0.26100 0.26746 0.04872  0.03768  -0.05422 116 GLU A C     
827  O O     . GLU A 122 ? 0.17689 0.28209 0.25829 0.05670  0.01704  -0.05363 116 GLU A O     
828  C CB    . GLU A 122 ? 0.26082 0.27979 0.26289 0.07109  0.08096  -0.02948 116 GLU A CB    
829  N N     . VAL A 123 ? 0.21610 0.25428 0.25964 0.03069  0.01909  -0.04109 117 VAL A N     
830  C CA    . VAL A 123 ? 0.21299 0.25431 0.28035 0.02736  -0.00722 -0.00371 117 VAL A CA    
831  C C     . VAL A 123 ? 0.19381 0.24216 0.25362 0.03122  0.00525  -0.02501 117 VAL A C     
832  O O     . VAL A 123 ? 0.19938 0.24398 0.25026 0.04272  0.02415  -0.02900 117 VAL A O     
833  C CB    . VAL A 123 ? 0.21663 0.25352 0.32284 0.03952  -0.01241 0.02870  117 VAL A CB    
834  C CG1   . VAL A 123 ? 0.21193 0.25620 0.28158 0.03060  -0.01010 0.03031  117 VAL A CG1   
835  C CG2   . VAL A 123 ? 0.24573 0.28015 0.39073 0.04792  -0.01784 0.00266  117 VAL A CG2   
836  N N     . TYR A 124 ? 0.18293 0.23631 0.26136 0.02367  0.01012  -0.04777 118 TYR A N     
837  C CA    . TYR A 124 ? 0.16819 0.23172 0.24498 0.02490  0.00486  -0.03470 118 TYR A CA    
838  C C     . TYR A 124 ? 0.17308 0.25647 0.26847 0.03060  -0.00165 -0.03683 118 TYR A C     
839  O O     . TYR A 124 ? 0.17962 0.25069 0.30523 0.02864  -0.00683 -0.06442 118 TYR A O     
840  C CB    . TYR A 124 ? 0.15357 0.22227 0.23864 -0.00542 0.02702  -0.01296 118 TYR A CB    
841  C CG    . TYR A 124 ? 0.13272 0.20689 0.21638 -0.03196 0.01923  -0.01868 118 TYR A CG    
842  C CD1   . TYR A 124 ? 0.14565 0.19891 0.22965 -0.03301 0.04561  -0.02546 118 TYR A CD1   
843  C CD2   . TYR A 124 ? 0.12244 0.21102 0.18580 -0.03830 0.01751  -0.00038 118 TYR A CD2   
844  C CE1   . TYR A 124 ? 0.14948 0.19338 0.26850 -0.04304 -0.00877 -0.01759 118 TYR A CE1   
845  C CE2   . TYR A 124 ? 0.13797 0.19362 0.19849 -0.05423 0.03366  -0.02110 118 TYR A CE2   
846  C CZ    . TYR A 124 ? 0.14249 0.19124 0.24732 -0.04919 0.00313  0.02209  118 TYR A CZ    
847  O OH    . TYR A 124 ? 0.15885 0.17913 0.27453 -0.04011 0.02332  -0.00379 118 TYR A OH    
848  N N     . GLN A 125 ? 0.17048 0.27023 0.28347 0.02213  -0.00194 -0.03256 119 GLN A N     
849  C CA    . GLN A 125 ? 0.17061 0.27151 0.27226 0.01339  -0.01548 -0.03138 119 GLN A CA    
850  C C     . GLN A 125 ? 0.20137 0.30328 0.29042 0.03182  -0.01758 -0.04149 119 GLN A C     
851  O O     . GLN A 125 ? 0.22671 0.30934 0.30536 0.02661  -0.00060 -0.03763 119 GLN A O     
852  C CB    . GLN A 125 ? 0.15244 0.24861 0.34342 -0.01342 0.00247  -0.00896 119 GLN A CB    
853  C CG    . GLN A 125 ? 0.13792 0.25154 0.35104 -0.01931 -0.00430 -0.03050 119 GLN A CG    
854  C CD    . GLN A 125 ? 0.13759 0.27562 0.30195 -0.02701 -0.04339 0.01068  119 GLN A CD    
855  O OE1   . GLN A 125 ? 0.14915 0.31565 0.29216 -0.03747 -0.05851 0.01777  119 GLN A OE1   
856  N NE2   . GLN A 125 ? 0.14442 0.25213 0.29141 0.00150  -0.06408 0.02874  119 GLN A NE2   
857  N N     . PRO A 126 ? 0.20613 0.34149 0.33721 0.08765  -0.03199 -0.02565 120 PRO A N     
858  C CA    . PRO A 126 ? 0.23595 0.36554 0.39413 0.08673  -0.00916 -0.04846 120 PRO A CA    
859  C C     . PRO A 126 ? 0.25883 0.36801 0.40954 0.07630  0.02177  -0.04515 120 PRO A C     
860  O O     . PRO A 126 ? 0.25620 0.36294 0.42597 0.07527  0.02656  -0.04009 120 PRO A O     
861  C CB    . PRO A 126 ? 0.23564 0.37155 0.41355 0.08994  -0.05380 -0.03838 120 PRO A CB    
862  C CG    . PRO A 126 ? 0.23098 0.37653 0.42920 0.08267  -0.05560 -0.04911 120 PRO A CG    
863  C CD    . PRO A 126 ? 0.19531 0.36048 0.35828 0.09324  -0.05071 -0.03763 120 PRO A CD    
864  N N     . ALA A 127 ? 0.27337 0.36354 0.39117 0.07929  0.03145  -0.05995 121 ALA A N     
865  C CA    . ALA A 127 ? 0.28814 0.36213 0.39682 0.07696  0.08160  -0.08700 121 ALA A CA    
866  C C     . ALA A 127 ? 0.29171 0.35333 0.36698 0.06836  0.07624  -0.07727 121 ALA A C     
867  O O     . ALA A 127 ? 0.31217 0.36392 0.36635 0.06153  0.10529  -0.04482 121 ALA A O     
868  C CB    . ALA A 127 ? 0.29428 0.37763 0.42064 0.07228  0.11012  -0.10985 121 ALA A CB    
869  N N     . GLY A 128 ? 0.28871 0.33982 0.38581 0.04752  0.05621  -0.03959 122 GLY A N     
870  C CA    . GLY A 128 ? 0.29501 0.33987 0.42260 0.04343  0.02647  0.00194  122 GLY A CA    
871  C C     . GLY A 128 ? 0.27787 0.32994 0.39940 0.04555  0.01741  0.01228  122 GLY A C     
872  O O     . GLY A 128 ? 0.28147 0.33228 0.42003 0.05255  0.01007  -0.00729 122 GLY A O     
873  N N     . ALA A 129 ? 0.24842 0.30895 0.39593 0.03328  0.03222  0.00634  123 ALA A N     
874  C CA    . ALA A 129 ? 0.22774 0.30545 0.42961 0.01493  0.02678  0.00478  123 ALA A CA    
875  C C     . ALA A 129 ? 0.22142 0.29115 0.39031 0.01987  0.04704  -0.00181 123 ALA A C     
876  O O     . ALA A 129 ? 0.20164 0.29563 0.36945 0.02641  0.06421  0.02033  123 ALA A O     
877  C CB    . ALA A 129 ? 0.21081 0.31241 0.47919 -0.00150 0.00629  0.01604  123 ALA A CB    
878  N N     . ALA A 130 ? 0.22600 0.28888 0.31180 0.03190  0.04664  -0.01331 124 ALA A N     
879  C CA    . ALA A 130 ? 0.19806 0.28652 0.28511 0.03528  0.01963  -0.01253 124 ALA A CA    
880  C C     . ALA A 130 ? 0.16436 0.27692 0.27094 0.03241  0.01512  -0.00563 124 ALA A C     
881  O O     . ALA A 130 ? 0.16457 0.26968 0.26936 0.03504  0.01399  0.01027  124 ALA A O     
882  C CB    . ALA A 130 ? 0.21931 0.28462 0.27168 0.01613  -0.00560 -0.03455 124 ALA A CB    
883  N N     . PRO A 131 ? 0.15227 0.27484 0.25759 0.00524  0.05013  -0.01465 125 PRO A N     
884  C CA    . PRO A 131 ? 0.14461 0.26138 0.23928 -0.01094 0.04012  -0.03405 125 PRO A CA    
885  C C     . PRO A 131 ? 0.15380 0.26059 0.24588 -0.02664 0.02206  -0.03020 125 PRO A C     
886  O O     . PRO A 131 ? 0.17263 0.27266 0.27928 -0.02147 0.02718  -0.02524 125 PRO A O     
887  C CB    . PRO A 131 ? 0.11978 0.25958 0.30687 -0.02446 0.02821  -0.04733 125 PRO A CB    
888  C CG    . PRO A 131 ? 0.13198 0.30567 0.29582 0.00153  -0.00700 -0.05605 125 PRO A CG    
889  C CD    . PRO A 131 ? 0.13109 0.29773 0.26937 0.00514  0.02400  -0.04036 125 PRO A CD    
890  N N     . ILE A 132 ? 0.13996 0.24405 0.26287 -0.02333 0.02624  -0.02126 126 ILE A N     
891  C CA    . ILE A 132 ? 0.11745 0.25579 0.27389 -0.01702 0.03592  -0.02202 126 ILE A CA    
892  C C     . ILE A 132 ? 0.10523 0.22918 0.26351 -0.01622 0.04025  0.00207  126 ILE A C     
893  O O     . ILE A 132 ? 0.10386 0.23058 0.27213 0.01221  0.00830  -0.00225 126 ILE A O     
894  C CB    . ILE A 132 ? 0.13209 0.29242 0.24416 -0.02322 0.03569  -0.05844 126 ILE A CB    
895  C CG1   . ILE A 132 ? 0.13680 0.31852 0.22884 -0.05719 -0.01752 -0.06293 126 ILE A CG1   
896  C CG2   . ILE A 132 ? 0.14565 0.30930 0.32206 -0.00522 0.05344  -0.07694 126 ILE A CG2   
897  C CD1   . ILE A 132 ? 0.16638 0.34191 0.28433 -0.07130 -0.02044 -0.03442 126 ILE A CD1   
898  N N     . SER A 133 ? 0.11254 0.22207 0.24019 -0.02058 0.02073  0.01386  127 SER A N     
899  C CA    . SER A 133 ? 0.09064 0.21154 0.24288 -0.02268 0.01202  0.03157  127 SER A CA    
900  C C     . SER A 133 ? 0.09914 0.22439 0.27329 -0.02656 0.00330  -0.00339 127 SER A C     
901  O O     . SER A 133 ? 0.08111 0.24868 0.29118 -0.02174 0.01677  0.00500  127 SER A O     
902  C CB    . SER A 133 ? 0.10869 0.20851 0.27351 -0.00953 -0.01737 -0.01173 127 SER A CB    
903  O OG    . SER A 133 ? 0.12991 0.21109 0.28933 -0.01447 -0.00590 0.03071  127 SER A OG    
904  N N     . SER A 134 ? 0.10101 0.19538 0.24541 -0.01303 0.00255  -0.01485 128 SER A N     
905  C CA    . SER A 134 ? 0.11944 0.22188 0.25110 -0.03039 0.00500  -0.02129 128 SER A CA    
906  C C     . SER A 134 ? 0.14665 0.23559 0.29333 -0.03730 -0.02120 -0.00400 128 SER A C     
907  O O     . SER A 134 ? 0.14107 0.22500 0.28872 -0.03964 -0.04052 0.01799  128 SER A O     
908  C CB    . SER A 134 ? 0.09271 0.22991 0.24936 -0.03402 0.01845  -0.04383 128 SER A CB    
909  O OG    . SER A 134 ? 0.10925 0.25122 0.24824 -0.04183 0.01536  -0.01885 128 SER A OG    
910  N N     . THR A 135 ? 0.15242 0.23975 0.31527 -0.02695 -0.05377 -0.02741 129 THR A N     
911  C CA    . THR A 135 ? 0.16593 0.26048 0.32353 -0.01652 -0.03883 -0.04130 129 THR A CA    
912  C C     . THR A 135 ? 0.14158 0.26110 0.25911 -0.01630 -0.01762 -0.03310 129 THR A C     
913  O O     . THR A 135 ? 0.14158 0.24354 0.23960 -0.01325 -0.00450 -0.01091 129 THR A O     
914  C CB    . THR A 135 ? 0.17658 0.26954 0.34649 -0.00574 -0.04332 -0.04198 129 THR A CB    
915  O OG1   . THR A 135 ? 0.20824 0.27566 0.33091 -0.01660 -0.03530 -0.03493 129 THR A OG1   
916  C CG2   . THR A 135 ? 0.17231 0.28656 0.34335 -0.00243 -0.05192 -0.07364 129 THR A CG2   
917  N N     . GLU A 136 ? 0.15616 0.28735 0.25368 -0.02537 0.00047  -0.07163 130 GLU A N     
918  C CA    . GLU A 136 ? 0.19752 0.32721 0.23323 -0.00921 0.01815  -0.04139 130 GLU A CA    
919  C C     . GLU A 136 ? 0.18163 0.31482 0.24102 -0.00380 0.01545  -0.01045 130 GLU A C     
920  O O     . GLU A 136 ? 0.16650 0.28501 0.30812 -0.00828 -0.01383 0.00170  130 GLU A O     
921  C CB    . GLU A 136 ? 0.26087 0.40445 0.34498 -0.00133 0.01824  -0.03670 130 GLU A CB    
922  C CG    . GLU A 136 ? 0.35244 0.48621 0.43310 0.01339  0.03283  -0.02703 130 GLU A CG    
923  C CD    . GLU A 136 ? 0.41334 0.54664 0.54026 0.02413  0.03755  -0.02114 130 GLU A CD    
924  O OE1   . GLU A 136 ? 0.44608 0.57347 0.56835 0.00838  0.06139  -0.04097 130 GLU A OE1   
925  O OE2   . GLU A 136 ? 0.44790 0.55902 0.60370 0.05194  0.03386  0.00215  130 GLU A OE2   
926  N N     . LYS A 137 ? 0.17626 0.31731 0.22641 -0.01091 0.03329  0.00286  131 LYS A N     
927  C CA    . LYS A 137 ? 0.19991 0.31101 0.23768 -0.01902 0.00171  0.01406  131 LYS A CA    
928  C C     . LYS A 137 ? 0.16805 0.28614 0.24306 -0.02832 0.00334  0.00225  131 LYS A C     
929  O O     . LYS A 137 ? 0.16300 0.26079 0.25295 -0.03643 0.02019  -0.00742 131 LYS A O     
930  C CB    . LYS A 137 ? 0.25293 0.32635 0.26797 -0.03013 0.00054  0.06524  131 LYS A CB    
931  C CG    . LYS A 137 ? 0.32989 0.35917 0.34974 -0.03230 -0.01573 0.06226  131 LYS A CG    
932  C CD    . LYS A 137 ? 0.40731 0.39300 0.39624 -0.02149 0.00660  0.07440  131 LYS A CD    
933  C CE    . LYS A 137 ? 0.47042 0.41925 0.41511 -0.01507 0.01931  0.06164  131 LYS A CE    
934  N NZ    . LYS A 137 ? 0.50314 0.43445 0.48246 -0.00330 0.01084  0.03233  131 LYS A NZ    
935  N N     . PRO A 138 ? 0.15715 0.26975 0.18810 -0.03212 0.00471  -0.02024 132 PRO A N     
936  C CA    . PRO A 138 ? 0.15516 0.26767 0.19849 -0.04528 0.02728  -0.01156 132 PRO A CA    
937  C C     . PRO A 138 ? 0.12897 0.26387 0.24027 -0.04383 0.00122  0.02172  132 PRO A C     
938  O O     . PRO A 138 ? 0.14335 0.27096 0.25810 -0.03147 -0.01795 0.02200  132 PRO A O     
939  C CB    . PRO A 138 ? 0.18242 0.27984 0.22931 -0.05262 0.03249  -0.02978 132 PRO A CB    
940  C CG    . PRO A 138 ? 0.22229 0.28481 0.20280 -0.05981 0.00864  0.00328  132 PRO A CG    
941  C CD    . PRO A 138 ? 0.19222 0.27923 0.21941 -0.05778 -0.01387 -0.02359 132 PRO A CD    
942  N N     . ILE A 139 ? 0.09797 0.25975 0.20601 -0.03687 0.00439  0.01786  133 ILE A N     
943  C CA    . ILE A 139 ? 0.08947 0.25803 0.20445 -0.03399 -0.01487 0.03382  133 ILE A CA    
944  C C     . ILE A 139 ? 0.13717 0.27787 0.22761 -0.00514 -0.00789 0.03057  133 ILE A C     
945  O O     . ILE A 139 ? 0.14035 0.29803 0.22431 0.00620  0.00157  -0.00624 133 ILE A O     
946  C CB    . ILE A 139 ? 0.08750 0.24940 0.23992 -0.04744 -0.02862 0.01147  133 ILE A CB    
947  C CG1   . ILE A 139 ? 0.11710 0.25743 0.18888 -0.03821 -0.04914 -0.01461 133 ILE A CG1   
948  C CG2   . ILE A 139 ? 0.10415 0.25816 0.29056 -0.02068 0.00249  0.02208  133 ILE A CG2   
949  C CD1   . ILE A 139 ? 0.13988 0.25567 0.25253 -0.02817 -0.01420 -0.01175 133 ILE A CD1   
950  N N     . SER A 140 ? 0.14796 0.27818 0.24583 0.00554  -0.02058 0.02268  134 SER A N     
951  C CA    . SER A 140 ? 0.14649 0.27989 0.24470 -0.02691 -0.03556 0.02148  134 SER A CA    
952  C C     . SER A 140 ? 0.16739 0.30218 0.26522 -0.04254 -0.04169 0.01351  134 SER A C     
953  O O     . SER A 140 ? 0.14168 0.27670 0.28630 -0.04098 -0.02001 0.03729  134 SER A O     
954  C CB    . SER A 140 ? 0.15645 0.27950 0.26590 -0.01915 0.01619  0.04721  134 SER A CB    
955  O OG    . SER A 140 ? 0.20172 0.28501 0.28095 -0.00224 0.03163  0.05399  134 SER A OG    
956  N N     . ASN A 141 ? 0.21828 0.34215 0.27888 -0.05880 -0.04580 -0.00976 135 ASN A N     
957  C CA    . ASN A 141 ? 0.26815 0.40138 0.33111 -0.06969 -0.03510 -0.00542 135 ASN A CA    
958  C C     . ASN A 141 ? 0.25223 0.40796 0.32004 -0.08036 -0.04620 0.01233  135 ASN A C     
959  O O     . ASN A 141 ? 0.28647 0.43274 0.35403 -0.10090 -0.05310 0.01499  135 ASN A O     
960  C CB    . ASN A 141 ? 0.32361 0.45433 0.37232 -0.06211 -0.04162 -0.01079 135 ASN A CB    
961  C CG    . ASN A 141 ? 0.36614 0.49625 0.39714 -0.06688 -0.06495 -0.03722 135 ASN A CG    
962  O OD1   . ASN A 141 ? 0.37510 0.51305 0.39217 -0.06551 -0.06224 -0.00380 135 ASN A OD1   
963  N ND2   . ASN A 141 ? 0.38999 0.51508 0.40778 -0.06822 -0.05668 -0.07297 135 ASN A ND2   
964  N N     . ARG A 142 ? 0.21530 0.39508 0.29032 -0.04400 -0.04877 0.06510  136 ARG A N     
965  C CA    . ARG A 142 ? 0.20278 0.37852 0.33506 -0.02839 -0.01837 0.07434  136 ARG A CA    
966  C C     . ARG A 142 ? 0.18547 0.36188 0.30724 -0.02296 -0.00144 0.07912  136 ARG A C     
967  O O     . ARG A 142 ? 0.20998 0.39905 0.34853 -0.00915 0.03169  0.10929  136 ARG A O     
968  C CB    . ARG A 142 ? 0.21332 0.37278 0.39658 -0.01634 -0.02181 0.05584  136 ARG A CB    
969  N N     . TRP A 143 ? 0.16834 0.31267 0.27205 -0.01632 -0.05121 0.05026  137 TRP A N     
970  C CA    . TRP A 143 ? 0.16940 0.26801 0.25912 0.01270  -0.09047 0.03518  137 TRP A CA    
971  C C     . TRP A 143 ? 0.19061 0.25494 0.29816 0.00905  -0.07042 0.03191  137 TRP A C     
972  O O     . TRP A 143 ? 0.20956 0.26778 0.32101 0.00396  -0.06968 0.05827  137 TRP A O     
973  C CB    . TRP A 143 ? 0.16040 0.26350 0.31413 0.01383  -0.06108 -0.01064 137 TRP A CB    
974  C CG    . TRP A 143 ? 0.17608 0.27432 0.36446 0.02084  -0.05637 -0.01472 137 TRP A CG    
975  C CD1   . TRP A 143 ? 0.17618 0.27720 0.34631 0.02273  -0.05643 -0.03424 137 TRP A CD1   
976  C CD2   . TRP A 143 ? 0.19552 0.29514 0.42176 0.02768  -0.05438 -0.02068 137 TRP A CD2   
977  N NE1   . TRP A 143 ? 0.18583 0.29069 0.38872 0.03404  -0.06598 -0.02407 137 TRP A NE1   
978  C CE2   . TRP A 143 ? 0.19096 0.29898 0.43496 0.03249  -0.06755 -0.03263 137 TRP A CE2   
979  C CE3   . TRP A 143 ? 0.20749 0.31077 0.49176 0.04212  -0.05982 -0.03595 137 TRP A CE3   
980  C CZ2   . TRP A 143 ? 0.19617 0.30736 0.43842 0.02747  -0.06450 -0.05350 137 TRP A CZ2   
981  C CZ3   . TRP A 143 ? 0.22212 0.31927 0.50599 0.03721  -0.04754 -0.04386 137 TRP A CZ3   
982  C CH2   . TRP A 143 ? 0.21037 0.31676 0.50822 0.03291  -0.05167 -0.04714 137 TRP A CH2   
983  N N     . ARG A 144 ? 0.18935 0.24319 0.28040 -0.00021 -0.08507 0.04896  138 ARG A N     
984  C CA    . ARG A 144 ? 0.21263 0.25504 0.33630 0.00736  -0.06045 0.06560  138 ARG A CA    
985  C C     . ARG A 144 ? 0.20523 0.24153 0.29540 0.01840  -0.01303 0.03176  138 ARG A C     
986  O O     . ARG A 144 ? 0.23534 0.26231 0.29985 0.04645  0.02149  0.06663  138 ARG A O     
987  C CB    . ARG A 144 ? 0.24656 0.28496 0.37542 -0.01453 -0.06132 0.09213  138 ARG A CB    
988  C CG    . ARG A 144 ? 0.28502 0.34363 0.40178 -0.02434 -0.05932 0.08610  138 ARG A CG    
989  C CD    . ARG A 144 ? 0.32956 0.39259 0.46049 -0.02779 -0.07214 0.11975  138 ARG A CD    
990  N NE    . ARG A 144 ? 0.35898 0.43767 0.55153 -0.04835 -0.10053 0.10441  138 ARG A NE    
991  C CZ    . ARG A 144 ? 0.38262 0.45879 0.60022 -0.05598 -0.11636 0.11396  138 ARG A CZ    
992  N NH1   . ARG A 144 ? 0.38676 0.46274 0.60454 -0.07085 -0.10928 0.12775  138 ARG A NH1   
993  N NH2   . ARG A 144 ? 0.39000 0.46952 0.65034 -0.04771 -0.12951 0.12298  138 ARG A NH2   
994  N N     . ILE A 145 ? 0.17764 0.18590 0.25711 0.00696  0.00189  0.05448  139 ILE A N     
995  C CA    . ILE A 145 ? 0.15569 0.20035 0.23668 -0.01311 -0.00302 0.03816  139 ILE A CA    
996  C C     . ILE A 145 ? 0.17909 0.22422 0.24722 -0.01973 -0.00688 0.03085  139 ILE A C     
997  O O     . ILE A 145 ? 0.19427 0.23661 0.25258 -0.03294 0.00979  0.02930  139 ILE A O     
998  C CB    . ILE A 145 ? 0.13901 0.21929 0.23436 -0.03187 0.00110  0.00599  139 ILE A CB    
999  C CG1   . ILE A 145 ? 0.10748 0.22117 0.24359 -0.03346 -0.01112 0.02449  139 ILE A CG1   
1000 C CG2   . ILE A 145 ? 0.15985 0.24081 0.25741 -0.04105 -0.00365 -0.00197 139 ILE A CG2   
1001 C CD1   . ILE A 145 ? 0.11329 0.23034 0.26519 -0.04366 0.00559  0.03137  139 ILE A CD1   
1002 N N     . LEU A 146 ? 0.17603 0.21230 0.22737 -0.00978 0.01790  0.00836  140 LEU A N     
1003 C CA    . LEU A 146 ? 0.18468 0.19683 0.20602 -0.00262 0.03661  0.03919  140 LEU A CA    
1004 C C     . LEU A 146 ? 0.18299 0.21163 0.19417 0.01657  0.00239  0.01364  140 LEU A C     
1005 O O     . LEU A 146 ? 0.15689 0.23600 0.25233 0.00204  0.03574  -0.00133 140 LEU A O     
1006 C CB    . LEU A 146 ? 0.18918 0.19996 0.24447 -0.02067 0.04189  0.07055  140 LEU A CB    
1007 C CG    . LEU A 146 ? 0.18248 0.21138 0.21563 -0.03524 0.05113  0.02022  140 LEU A CG    
1008 C CD1   . LEU A 146 ? 0.16618 0.21844 0.27848 -0.03841 0.05633  -0.03813 140 LEU A CD1   
1009 C CD2   . LEU A 146 ? 0.20894 0.22566 0.24668 -0.01838 0.06407  0.03765  140 LEU A CD2   
1010 N N     . MET A 147 ? 0.19369 0.18521 0.21131 0.01363  -0.00264 -0.00007 141 MET A N     
1011 C CA    . MET A 147 ? 0.19506 0.18246 0.19860 0.00711  -0.00690 -0.01536 141 MET A CA    
1012 C C     . MET A 147 ? 0.19532 0.18868 0.23357 -0.00568 -0.00508 -0.02606 141 MET A C     
1013 O O     . MET A 147 ? 0.17415 0.17856 0.22974 -0.00356 0.02354  -0.00783 141 MET A O     
1014 C CB    . MET A 147 ? 0.20613 0.22850 0.15737 0.00093  0.01853  -0.04233 141 MET A CB    
1015 C CG    . MET A 147 ? 0.20814 0.26466 0.22964 -0.02291 0.01602  -0.01554 141 MET A CG    
1016 S SD    . MET A 147 ? 0.23054 0.27643 0.29565 -0.02967 0.00105  -0.00056 141 MET A SD    
1017 C CE    . MET A 147 ? 0.23889 0.30163 0.32315 -0.03506 0.02649  -0.01385 141 MET A CE    
1018 N N     . PRO A 148 ? 0.18325 0.19886 0.26082 -0.00366 -0.00203 -0.00061 142 PRO A N     
1019 C CA    . PRO A 148 ? 0.17676 0.20335 0.30128 -0.01148 -0.01785 0.00284  142 PRO A CA    
1020 C C     . PRO A 148 ? 0.16159 0.22079 0.27065 -0.01060 -0.00226 0.01039  142 PRO A C     
1021 O O     . PRO A 148 ? 0.17605 0.23923 0.27759 -0.02646 -0.01330 -0.01885 142 PRO A O     
1022 C CB    . PRO A 148 ? 0.19291 0.22345 0.32795 -0.02293 0.01121  0.01371  142 PRO A CB    
1023 C CG    . PRO A 148 ? 0.19648 0.22879 0.30255 -0.01318 0.02957  0.00705  142 PRO A CG    
1024 C CD    . PRO A 148 ? 0.19424 0.21450 0.26439 -0.00051 0.01822  0.03364  142 PRO A CD    
1025 N N     . ASP A 149 ? 0.14690 0.20769 0.21434 0.00115  0.00394  -0.00287 143 ASP A N     
1026 C CA    . ASP A 149 ? 0.18652 0.21713 0.22424 -0.01746 -0.02016 0.00774  143 ASP A CA    
1027 C C     . ASP A 149 ? 0.20705 0.22201 0.23288 -0.02137 0.01252  0.01797  143 ASP A C     
1028 O O     . ASP A 149 ? 0.22906 0.22297 0.32583 -0.01125 0.01287  0.02690  143 ASP A O     
1029 C CB    . ASP A 149 ? 0.21861 0.23985 0.25917 -0.01629 -0.00676 -0.00327 143 ASP A CB    
1030 C CG    . ASP A 149 ? 0.23213 0.25222 0.29409 -0.02124 0.00776  -0.04242 143 ASP A CG    
1031 O OD1   . ASP A 149 ? 0.21343 0.24075 0.35469 -0.01146 0.00969  -0.03137 143 ASP A OD1   
1032 O OD2   . ASP A 149 ? 0.26446 0.28357 0.28966 -0.01867 0.02115  -0.04426 143 ASP A OD2   
1033 N N     . GLY A 150 ? 0.21636 0.25066 0.24082 -0.02086 0.01026  0.03690  144 GLY A N     
1034 C CA    . GLY A 150 ? 0.21099 0.26742 0.26007 -0.03094 -0.00366 0.03823  144 GLY A CA    
1035 C C     . GLY A 150 ? 0.20253 0.26426 0.27052 -0.02897 0.01491  0.04622  144 GLY A C     
1036 O O     . GLY A 150 ? 0.19725 0.30202 0.30457 -0.02968 0.02734  0.02473  144 GLY A O     
1037 N N     . THR A 151 ? 0.20683 0.24547 0.29056 -0.05135 0.00412  0.01267  145 THR A N     
1038 C CA    . THR A 151 ? 0.20647 0.24379 0.30672 -0.05784 -0.02646 0.02296  145 THR A CA    
1039 C C     . THR A 151 ? 0.21129 0.24451 0.29500 -0.04807 -0.02903 0.02574  145 THR A C     
1040 O O     . THR A 151 ? 0.18920 0.23849 0.28859 -0.03635 -0.03482 0.04120  145 THR A O     
1041 C CB    . THR A 151 ? 0.22257 0.24168 0.36692 -0.07003 -0.00914 0.01149  145 THR A CB    
1042 O OG1   . THR A 151 ? 0.22087 0.22840 0.31138 -0.06315 -0.00183 0.01421  145 THR A OG1   
1043 C CG2   . THR A 151 ? 0.24463 0.25206 0.43093 -0.09054 -0.01011 0.03298  145 THR A CG2   
1044 N N     . HIS A 152 ? 0.21116 0.25109 0.28500 -0.04793 -0.03280 0.03328  146 HIS A N     
1045 C CA    . HIS A 152 ? 0.22596 0.26262 0.28218 -0.04229 -0.01935 0.03473  146 HIS A CA    
1046 C C     . HIS A 152 ? 0.23381 0.26422 0.26853 -0.08234 -0.01041 0.03749  146 HIS A C     
1047 O O     . HIS A 152 ? 0.27330 0.30844 0.30513 -0.10360 0.00829  0.02922  146 HIS A O     
1048 C CB    . HIS A 152 ? 0.24898 0.27541 0.35839 -0.01402 0.00984  0.03068  146 HIS A CB    
1049 C CG    . HIS A 152 ? 0.26542 0.30715 0.42691 0.01134  0.04468  0.00736  146 HIS A CG    
1050 N ND1   . HIS A 152 ? 0.28007 0.33993 0.45388 0.01084  0.06369  -0.00796 146 HIS A ND1   
1051 C CD2   . HIS A 152 ? 0.27206 0.33674 0.45134 0.02889  0.04083  0.00453  146 HIS A CD2   
1052 C CE1   . HIS A 152 ? 0.29374 0.34075 0.47762 0.00370  0.06039  -0.03475 146 HIS A CE1   
1053 N NE2   . HIS A 152 ? 0.28675 0.34490 0.47916 0.01718  0.05647  -0.00995 146 HIS A NE2   
1054 N N     . GLY A 153 ? 0.20581 0.23373 0.22012 -0.08235 -0.02862 0.03504  147 GLY A N     
1055 C CA    . GLY A 153 ? 0.22545 0.22651 0.19743 -0.08772 0.02718  0.03988  147 GLY A CA    
1056 C C     . GLY A 153 ? 0.23293 0.23537 0.24455 -0.07588 0.02060  0.02712  147 GLY A C     
1057 O O     . GLY A 153 ? 0.21544 0.23774 0.24372 -0.05450 0.01749  0.03424  147 GLY A O     
1058 N N     . ILE A 154 ? 0.25266 0.23609 0.22360 -0.06220 0.01261  0.01223  148 ILE A N     
1059 C CA    . ILE A 154 ? 0.27283 0.24708 0.20852 -0.08691 0.00894  0.01562  148 ILE A CA    
1060 C C     . ILE A 154 ? 0.24484 0.24386 0.19809 -0.06152 -0.01040 0.00897  148 ILE A C     
1061 O O     . ILE A 154 ? 0.25353 0.22222 0.24127 -0.04368 -0.00771 0.00547  148 ILE A O     
1062 C CB    . ILE A 154 ? 0.33343 0.27231 0.22743 -0.09157 0.00690  -0.00190 148 ILE A CB    
1063 C CG1   . ILE A 154 ? 0.36685 0.29083 0.26387 -0.09231 -0.00028 -0.05795 148 ILE A CG1   
1064 C CG2   . ILE A 154 ? 0.35415 0.25277 0.15498 -0.10078 0.00252  0.01509  148 ILE A CG2   
1065 C CD1   . ILE A 154 ? 0.39474 0.31967 0.36634 -0.07038 0.00913  -0.02040 148 ILE A CD1   
1066 N N     . TYR A 155 ? 0.21385 0.23054 0.22265 -0.04949 0.02202  0.00294  149 TYR A N     
1067 C CA    . TYR A 155 ? 0.20171 0.22899 0.23655 -0.04244 0.00762  -0.02524 149 TYR A CA    
1068 C C     . TYR A 155 ? 0.20961 0.24002 0.24878 -0.03159 0.01948  -0.01420 149 TYR A C     
1069 O O     . TYR A 155 ? 0.20985 0.22918 0.24354 -0.00746 0.02236  0.00478  149 TYR A O     
1070 C CB    . TYR A 155 ? 0.19355 0.21654 0.23143 -0.03909 0.00075  -0.01496 149 TYR A CB    
1071 C CG    . TYR A 155 ? 0.20377 0.21059 0.19074 -0.04572 0.00380  -0.00620 149 TYR A CG    
1072 C CD1   . TYR A 155 ? 0.21287 0.19094 0.19014 -0.06203 0.01502  0.00326  149 TYR A CD1   
1073 C CD2   . TYR A 155 ? 0.20239 0.22283 0.21075 -0.03718 0.00901  0.01175  149 TYR A CD2   
1074 C CE1   . TYR A 155 ? 0.21146 0.19986 0.23604 -0.04346 0.01790  -0.00849 149 TYR A CE1   
1075 C CE2   . TYR A 155 ? 0.22080 0.21147 0.18483 -0.02811 0.01827  0.01393  149 TYR A CE2   
1076 C CZ    . TYR A 155 ? 0.23819 0.20673 0.22763 -0.02711 0.03717  -0.00116 149 TYR A CZ    
1077 O OH    . TYR A 155 ? 0.26618 0.22150 0.21205 -0.01872 0.05197  0.00838  149 TYR A OH    
1078 N N     . PRO A 156 ? 0.19913 0.27479 0.26969 -0.02219 0.02419  -0.00777 150 PRO A N     
1079 C CA    . PRO A 156 ? 0.19511 0.27846 0.24508 -0.03839 0.04728  -0.00326 150 PRO A CA    
1080 C C     . PRO A 156 ? 0.18795 0.27793 0.24976 -0.03557 0.02566  -0.01992 150 PRO A C     
1081 O O     . PRO A 156 ? 0.18196 0.28970 0.27530 -0.01897 0.00655  -0.01931 150 PRO A O     
1082 C CB    . PRO A 156 ? 0.21018 0.29406 0.23722 -0.02855 0.07100  -0.00499 150 PRO A CB    
1083 C CG    . PRO A 156 ? 0.20521 0.30561 0.26444 -0.02726 0.07390  -0.00223 150 PRO A CG    
1084 C CD    . PRO A 156 ? 0.20400 0.30106 0.24847 -0.02304 0.04552  0.00611  150 PRO A CD    
1085 N N     . LYS A 157 ? 0.18652 0.28358 0.21002 -0.04326 0.03733  -0.01105 151 LYS A N     
1086 C CA    . LYS A 157 ? 0.19900 0.29474 0.19256 -0.02897 0.03008  -0.00714 151 LYS A CA    
1087 C C     . LYS A 157 ? 0.18311 0.27860 0.26575 -0.02021 -0.00175 -0.02046 151 LYS A C     
1088 O O     . LYS A 157 ? 0.17504 0.28665 0.30975 -0.03071 0.01398  -0.01717 151 LYS A O     
1089 C CB    . LYS A 157 ? 0.23634 0.31753 0.25577 -0.04225 0.08082  0.03759  151 LYS A CB    
1090 C CG    . LYS A 157 ? 0.27376 0.34865 0.32130 -0.03628 0.10241  0.05986  151 LYS A CG    
1091 C CD    . LYS A 157 ? 0.28927 0.36549 0.29859 -0.02905 0.11906  0.06829  151 LYS A CD    
1092 C CE    . LYS A 157 ? 0.32087 0.38587 0.33948 -0.02090 0.09828  0.05454  151 LYS A CE    
1093 N NZ    . LYS A 157 ? 0.33386 0.39045 0.35129 -0.01853 0.07936  0.06262  151 LYS A NZ    
1094 N N     . PRO A 158 ? 0.17483 0.24948 0.27909 -0.01513 0.00290  -0.03329 152 PRO A N     
1095 C CA    . PRO A 158 ? 0.17095 0.24637 0.23196 -0.02129 0.04187  -0.04153 152 PRO A CA    
1096 C C     . PRO A 158 ? 0.16185 0.25632 0.24802 -0.03885 0.03370  -0.03885 152 PRO A C     
1097 O O     . PRO A 158 ? 0.19329 0.26274 0.25922 -0.03880 0.00219  -0.00805 152 PRO A O     
1098 C CB    . PRO A 158 ? 0.18119 0.24303 0.26612 -0.00645 0.01288  -0.04011 152 PRO A CB    
1099 C CG    . PRO A 158 ? 0.18652 0.23561 0.27416 -0.00615 -0.02214 -0.01192 152 PRO A CG    
1100 C CD    . PRO A 158 ? 0.18926 0.23045 0.29858 -0.01065 -0.00596 -0.02171 152 PRO A CD    
1101 N N     . ARG A 159 ? 0.12573 0.27910 0.26122 -0.02720 0.05786  -0.02397 153 ARG A N     
1102 C CA    . ARG A 159 ? 0.13856 0.29317 0.29674 -0.02604 0.06357  -0.02429 153 ARG A CA    
1103 C C     . ARG A 159 ? 0.13554 0.28521 0.28295 -0.01938 0.02513  -0.01697 153 ARG A C     
1104 O O     . ARG A 159 ? 0.12342 0.28322 0.23365 -0.02495 0.03458  -0.00275 153 ARG A O     
1105 C CB    . ARG A 159 ? 0.13607 0.30691 0.34847 -0.00010 0.09124  -0.03636 153 ARG A CB    
1106 C CG    . ARG A 159 ? 0.13856 0.32349 0.41725 0.00700  0.05341  -0.06901 153 ARG A CG    
1107 C CD    . ARG A 159 ? 0.13476 0.34233 0.43158 0.01663  0.02665  -0.09426 153 ARG A CD    
1108 N NE    . ARG A 159 ? 0.14083 0.33947 0.38693 0.01261  -0.01383 -0.11513 153 ARG A NE    
1109 C CZ    . ARG A 159 ? 0.17573 0.34795 0.39756 0.00151  -0.01481 -0.12429 153 ARG A CZ    
1110 N NH1   . ARG A 159 ? 0.17609 0.35019 0.44246 -0.00575 -0.01799 -0.14173 153 ARG A NH1   
1111 N NH2   . ARG A 159 ? 0.18471 0.35498 0.38235 0.00753  0.01312  -0.12626 153 ARG A NH2   
1112 N N     . ALA A 160 ? 0.13169 0.27085 0.29252 -0.01867 0.00698  -0.03920 154 ALA A N     
1113 C CA    . ALA A 160 ? 0.12792 0.28487 0.31259 -0.00995 -0.00524 -0.02594 154 ALA A CA    
1114 C C     . ALA A 160 ? 0.11860 0.30175 0.29579 -0.01174 0.00285  -0.04245 154 ALA A C     
1115 O O     . ALA A 160 ? 0.13544 0.32529 0.30472 0.00683  0.04536  -0.04865 154 ALA A O     
1116 C CB    . ALA A 160 ? 0.12739 0.28030 0.31200 -0.00595 0.00703  -0.01887 154 ALA A CB    
1117 N N     . ILE A 161 ? 0.10889 0.29041 0.26245 -0.01942 -0.01868 -0.05178 155 ILE A N     
1118 C CA    . ILE A 161 ? 0.09936 0.27800 0.23944 -0.02552 -0.01970 -0.00547 155 ILE A CA    
1119 C C     . ILE A 161 ? 0.11400 0.28820 0.25076 -0.02510 -0.00930 0.01678  155 ILE A C     
1120 O O     . ILE A 161 ? 0.12970 0.29532 0.31989 -0.03011 -0.03627 0.03825  155 ILE A O     
1121 C CB    . ILE A 161 ? 0.12825 0.26725 0.23309 -0.03514 0.03269  -0.00187 155 ILE A CB    
1122 C CG1   . ILE A 161 ? 0.16129 0.27416 0.21791 -0.03951 0.03393  -0.00158 155 ILE A CG1   
1123 C CG2   . ILE A 161 ? 0.15392 0.25994 0.26980 -0.03050 0.01429  0.01259  155 ILE A CG2   
1124 C CD1   . ILE A 161 ? 0.17546 0.29396 0.24621 -0.04996 0.02288  0.01478  155 ILE A CD1   
1125 N N     . GLY A 162 ? 0.10712 0.28829 0.21985 -0.05787 0.01934  0.00316  156 GLY A N     
1126 C CA    . GLY A 162 ? 0.10164 0.27110 0.21725 -0.05844 0.01253  0.00212  156 GLY A CA    
1127 C C     . GLY A 162 ? 0.09219 0.26228 0.24227 -0.03841 -0.01333 0.00103  156 GLY A C     
1128 O O     . GLY A 162 ? 0.08315 0.26090 0.25029 -0.02881 0.01648  -0.00857 156 GLY A O     
1129 N N     . THR A 163 ? 0.07606 0.24821 0.26503 -0.02630 -0.02051 -0.00783 157 THR A N     
1130 C CA    . THR A 163 ? 0.09440 0.22762 0.24859 -0.02013 -0.00368 -0.01712 157 THR A CA    
1131 C C     . THR A 163 ? 0.08975 0.21285 0.27130 -0.02219 0.00101  -0.02522 157 THR A C     
1132 O O     . THR A 163 ? 0.10606 0.21559 0.28332 -0.02093 0.02241  -0.00559 157 THR A O     
1133 C CB    . THR A 163 ? 0.08813 0.21190 0.26213 -0.00939 0.01535  -0.01948 157 THR A CB    
1134 O OG1   . THR A 163 ? 0.10194 0.23269 0.28914 -0.00912 0.02620  -0.01749 157 THR A OG1   
1135 C CG2   . THR A 163 ? 0.09847 0.21301 0.24378 0.01205  -0.01409 -0.01668 157 THR A CG2   
1136 N N     . TYR A 164 ? 0.08765 0.20118 0.27624 -0.02516 0.00494  -0.01294 158 TYR A N     
1137 C CA    . TYR A 164 ? 0.08644 0.19795 0.31855 -0.01582 0.01968  -0.00496 158 TYR A CA    
1138 C C     . TYR A 164 ? 0.09301 0.20170 0.28454 -0.01491 0.01330  0.00623  158 TYR A C     
1139 O O     . TYR A 164 ? 0.08593 0.22141 0.26147 -0.01948 -0.00435 0.01388  158 TYR A O     
1140 C CB    . TYR A 164 ? 0.09396 0.20893 0.32463 0.01969  0.03694  0.01221  158 TYR A CB    
1141 C CG    . TYR A 164 ? 0.10601 0.23476 0.34601 0.03140  0.04555  0.00902  158 TYR A CG    
1142 C CD1   . TYR A 164 ? 0.11801 0.24896 0.34835 0.05598  0.03418  0.04055  158 TYR A CD1   
1143 C CD2   . TYR A 164 ? 0.11647 0.23766 0.37895 0.04505  0.02882  0.03258  158 TYR A CD2   
1144 C CE1   . TYR A 164 ? 0.12833 0.25208 0.35757 0.06470  0.02725  0.05615  158 TYR A CE1   
1145 C CE2   . TYR A 164 ? 0.12817 0.24156 0.38672 0.05380  0.02207  0.06361  158 TYR A CE2   
1146 C CZ    . TYR A 164 ? 0.14710 0.26203 0.38437 0.06936  0.02038  0.08963  158 TYR A CZ    
1147 O OH    . TYR A 164 ? 0.17187 0.31052 0.46716 0.08081  0.00659  0.09195  158 TYR A OH    
1148 N N     . GLU A 165 ? 0.07408 0.18179 0.27902 -0.00481 0.01272  -0.01530 159 GLU A N     
1149 C CA    . GLU A 165 ? 0.08943 0.20250 0.27418 -0.03802 0.01441  -0.00529 159 GLU A CA    
1150 C C     . GLU A 165 ? 0.09802 0.20518 0.24539 -0.02908 -0.01491 -0.01232 159 GLU A C     
1151 O O     . GLU A 165 ? 0.10938 0.21518 0.23617 -0.02147 0.01046  0.02072  159 GLU A O     
1152 C CB    . GLU A 165 ? 0.13457 0.23434 0.28791 -0.04824 -0.00536 -0.00427 159 GLU A CB    
1153 C CG    . GLU A 165 ? 0.18425 0.27863 0.34843 -0.05269 0.01734  -0.01598 159 GLU A CG    
1154 C CD    . GLU A 165 ? 0.23154 0.32053 0.38828 -0.05319 0.01732  -0.04536 159 GLU A CD    
1155 O OE1   . GLU A 165 ? 0.26577 0.33690 0.40056 -0.02974 0.02736  -0.05715 159 GLU A OE1   
1156 O OE2   . GLU A 165 ? 0.24371 0.35547 0.40224 -0.06648 0.02577  -0.08444 159 GLU A OE2   
1157 N N     . ILE A 166 ? 0.10624 0.21760 0.27411 0.00147  -0.03906 -0.01229 160 ILE A N     
1158 C CA    . ILE A 166 ? 0.11506 0.22832 0.25748 0.01551  -0.00619 0.00941  160 ILE A CA    
1159 C C     . ILE A 166 ? 0.11384 0.22386 0.24824 -0.01089 -0.01491 0.01391  160 ILE A C     
1160 O O     . ILE A 166 ? 0.11122 0.20703 0.30320 -0.01188 -0.02104 0.04982  160 ILE A O     
1161 C CB    . ILE A 166 ? 0.13000 0.22256 0.24670 0.02073  0.01464  0.02619  160 ILE A CB    
1162 C CG1   . ILE A 166 ? 0.11780 0.22002 0.26546 0.01554  0.00501  0.02919  160 ILE A CG1   
1163 C CG2   . ILE A 166 ? 0.15930 0.22757 0.23851 0.00610  0.00904  0.02784  160 ILE A CG2   
1164 C CD1   . ILE A 166 ? 0.11897 0.20920 0.28908 0.00722  -0.00050 0.02148  160 ILE A CD1   
1165 N N     . SER A 167 ? 0.09033 0.22388 0.23049 -0.02129 -0.01257 -0.00258 161 SER A N     
1166 C CA    . SER A 167 ? 0.08010 0.23211 0.28835 -0.02851 0.00478  0.00435  161 SER A CA    
1167 C C     . SER A 167 ? 0.09773 0.22554 0.28179 0.01106  -0.01324 -0.01984 161 SER A C     
1168 O O     . SER A 167 ? 0.08944 0.22444 0.26292 0.02938  0.00855  -0.03807 161 SER A O     
1169 C CB    . SER A 167 ? 0.08622 0.24398 0.27491 -0.01860 0.04425  -0.00969 161 SER A CB    
1170 O OG    . SER A 167 ? 0.08563 0.26353 0.25353 0.00106  0.02532  -0.01883 161 SER A OG    
1171 N N     . GLN A 168 ? 0.09519 0.20717 0.24429 0.00406  -0.01723 -0.02014 162 GLN A N     
1172 C CA    . GLN A 168 ? 0.08652 0.22955 0.29395 0.01779  0.01902  -0.00083 162 GLN A CA    
1173 C C     . GLN A 168 ? 0.08600 0.21808 0.28939 0.01779  0.01046  0.00021  162 GLN A C     
1174 O O     . GLN A 168 ? 0.09972 0.22729 0.31819 0.00872  0.03609  0.01574  162 GLN A O     
1175 C CB    . GLN A 168 ? 0.10078 0.26344 0.28716 0.01643  0.06050  0.02450  162 GLN A CB    
1176 C CG    . GLN A 168 ? 0.11579 0.30620 0.34257 0.01260  0.05281  0.07054  162 GLN A CG    
1177 C CD    . GLN A 168 ? 0.17647 0.34409 0.45077 0.02696  0.03292  0.09427  162 GLN A CD    
1178 O OE1   . GLN A 168 ? 0.21205 0.36699 0.50730 0.05102  -0.00158 0.09832  162 GLN A OE1   
1179 N NE2   . GLN A 168 ? 0.17657 0.35370 0.45685 0.01707  0.04071  0.07443  162 GLN A NE2   
1180 N N     . VAL A 169 ? 0.08124 0.22373 0.23141 0.00515  -0.00468 -0.01239 163 VAL A N     
1181 C CA    . VAL A 169 ? 0.07633 0.23568 0.23478 -0.00014 0.00229  -0.01060 163 VAL A CA    
1182 C C     . VAL A 169 ? 0.08005 0.21641 0.25065 -0.01360 0.00099  -0.03665 163 VAL A C     
1183 O O     . VAL A 169 ? 0.08439 0.20066 0.24131 -0.01498 0.01181  -0.01400 163 VAL A O     
1184 C CB    . VAL A 169 ? 0.06757 0.24781 0.21392 -0.00131 0.01759  -0.01144 163 VAL A CB    
1185 C CG1   . VAL A 169 ? 0.07214 0.26477 0.22045 0.00655  0.02072  -0.00623 163 VAL A CG1   
1186 C CG2   . VAL A 169 ? 0.07268 0.24983 0.22889 -0.02145 0.01350  -0.02209 163 VAL A CG2   
1187 N N     . VAL A 170 ? 0.07975 0.20462 0.26505 -0.00387 -0.00163 -0.04582 164 VAL A N     
1188 C CA    . VAL A 170 ? 0.09148 0.22070 0.27510 -0.00060 -0.03470 -0.03399 164 VAL A CA    
1189 C C     . VAL A 170 ? 0.09951 0.23109 0.30764 0.01051  -0.02267 -0.03593 164 VAL A C     
1190 O O     . VAL A 170 ? 0.10148 0.21841 0.32113 -0.00074 -0.01364 0.00153  164 VAL A O     
1191 C CB    . VAL A 170 ? 0.10371 0.21541 0.27737 -0.00692 -0.02411 -0.01997 164 VAL A CB    
1192 C CG1   . VAL A 170 ? 0.11414 0.21386 0.25398 -0.01621 0.00048  -0.04973 164 VAL A CG1   
1193 C CG2   . VAL A 170 ? 0.09915 0.21664 0.26354 -0.00437 -0.02159 0.03256  164 VAL A CG2   
1194 N N     . GLU A 171 ? 0.10945 0.25900 0.27733 0.02878  -0.00169 -0.06344 165 GLU A N     
1195 C CA    . GLU A 171 ? 0.12328 0.25984 0.32861 0.03234  -0.00473 -0.01537 165 GLU A CA    
1196 C C     . GLU A 171 ? 0.11030 0.25775 0.32121 0.02096  0.01079  0.01287  165 GLU A C     
1197 O O     . GLU A 171 ? 0.09213 0.25402 0.33338 0.02255  -0.00041 0.02047  165 GLU A O     
1198 C CB    . GLU A 171 ? 0.15103 0.29597 0.32003 0.05110  -0.05515 -0.00486 165 GLU A CB    
1199 C CG    . GLU A 171 ? 0.21006 0.34166 0.38878 0.02576  -0.09286 0.01614  165 GLU A CG    
1200 C CD    . GLU A 171 ? 0.27544 0.39675 0.47178 0.02619  -0.12887 0.02480  165 GLU A CD    
1201 O OE1   . GLU A 171 ? 0.27973 0.40884 0.52599 0.02219  -0.15317 -0.01148 165 GLU A OE1   
1202 O OE2   . GLU A 171 ? 0.31806 0.43143 0.49022 0.02421  -0.13143 0.03919  165 GLU A OE2   
1203 N N     . ASP A 172 ? 0.09604 0.22937 0.28480 0.00293  0.00521  0.00535  166 ASP A N     
1204 C CA    . ASP A 172 ? 0.11145 0.22516 0.23554 -0.00246 -0.00278 0.00417  166 ASP A CA    
1205 C C     . ASP A 172 ? 0.11286 0.20654 0.23826 0.00014  0.00210  -0.00733 166 ASP A C     
1206 O O     . ASP A 172 ? 0.12318 0.19418 0.22441 0.00186  0.01942  0.00493  166 ASP A O     
1207 C CB    . ASP A 172 ? 0.14516 0.23821 0.18516 -0.00187 0.01122  -0.02355 166 ASP A CB    
1208 C CG    . ASP A 172 ? 0.18548 0.27296 0.30878 -0.00376 0.01251  -0.02801 166 ASP A CG    
1209 O OD1   . ASP A 172 ? 0.21372 0.29232 0.36906 0.02667  0.01901  -0.03735 166 ASP A OD1   
1210 O OD2   . ASP A 172 ? 0.20170 0.29108 0.35891 -0.02119 0.05380  -0.02254 166 ASP A OD2   
1211 N N     . TYR A 173 ? 0.09560 0.18079 0.26777 0.00615  0.01712  -0.00563 167 TYR A N     
1212 C CA    . TYR A 173 ? 0.10096 0.20399 0.24815 0.01210  0.02043  -0.00284 167 TYR A CA    
1213 C C     . TYR A 173 ? 0.09740 0.21889 0.24858 0.00429  -0.00061 -0.02029 167 TYR A C     
1214 O O     . TYR A 173 ? 0.10703 0.23211 0.24159 -0.00146 -0.01767 -0.00283 167 TYR A O     
1215 C CB    . TYR A 173 ? 0.09854 0.19749 0.27099 0.00678  -0.00016 0.01736  167 TYR A CB    
1216 C CG    . TYR A 173 ? 0.09524 0.17835 0.25979 0.00167  -0.00809 0.03653  167 TYR A CG    
1217 C CD1   . TYR A 173 ? 0.09311 0.17944 0.26814 0.01151  0.00664  0.01367  167 TYR A CD1   
1218 C CD2   . TYR A 173 ? 0.09573 0.19877 0.19801 -0.00687 -0.02167 -0.01230 167 TYR A CD2   
1219 C CE1   . TYR A 173 ? 0.10461 0.18143 0.26687 0.00761  -0.01405 0.00191  167 TYR A CE1   
1220 C CE2   . TYR A 173 ? 0.07653 0.19204 0.22899 -0.01886 -0.01685 -0.00973 167 TYR A CE2   
1221 C CZ    . TYR A 173 ? 0.09842 0.18866 0.23596 -0.00792 -0.01434 -0.01169 167 TYR A CZ    
1222 O OH    . TYR A 173 ? 0.11700 0.19287 0.24470 -0.01360 -0.03228 -0.02532 167 TYR A OH    
1223 N N     . ARG A 174 ? 0.07015 0.23173 0.24002 0.01318  -0.00955 -0.02714 168 ARG A N     
1224 C CA    . ARG A 174 ? 0.08919 0.25617 0.26656 0.00351  -0.04171 -0.01003 168 ARG A CA    
1225 C C     . ARG A 174 ? 0.10260 0.24802 0.25695 0.00722  -0.02701 -0.00832 168 ARG A C     
1226 O O     . ARG A 174 ? 0.11969 0.23259 0.28006 0.00934  -0.01385 -0.00031 168 ARG A O     
1227 C CB    . ARG A 174 ? 0.12102 0.29644 0.29202 -0.03181 -0.05059 -0.04782 168 ARG A CB    
1228 C CG    . ARG A 174 ? 0.14043 0.34308 0.35350 -0.04753 -0.05288 -0.07772 168 ARG A CG    
1229 C CD    . ARG A 174 ? 0.15875 0.40189 0.43548 -0.02829 -0.05985 -0.06713 168 ARG A CD    
1230 N NE    . ARG A 174 ? 0.17545 0.45189 0.48593 -0.01563 -0.06205 -0.03513 168 ARG A NE    
1231 C CZ    . ARG A 174 ? 0.20628 0.49197 0.54650 -0.00757 -0.04056 -0.03032 168 ARG A CZ    
1232 N NH1   . ARG A 174 ? 0.21193 0.50126 0.57180 -0.02188 -0.02767 -0.03595 168 ARG A NH1   
1233 N NH2   . ARG A 174 ? 0.22758 0.49867 0.56335 0.02279  -0.04971 -0.01474 168 ARG A NH2   
1234 N N     . ARG A 175 ? 0.10110 0.26247 0.27302 0.00145  -0.01026 0.00602  169 ARG A N     
1235 C CA    . ARG A 175 ? 0.09276 0.26572 0.24840 0.00254  0.01083  0.00146  169 ARG A CA    
1236 C C     . ARG A 175 ? 0.09936 0.24805 0.21406 -0.01504 -0.03343 -0.00536 169 ARG A C     
1237 O O     . ARG A 175 ? 0.10558 0.25510 0.27075 -0.01765 -0.04304 -0.00524 169 ARG A O     
1238 C CB    . ARG A 175 ? 0.11716 0.28803 0.30139 -0.00996 0.00893  -0.00702 169 ARG A CB    
1239 N N     . SER A 176 ? 0.09696 0.24327 0.21471 -0.00484 -0.02711 -0.02206 170 SER A N     
1240 C CA    . SER A 176 ? 0.10692 0.24860 0.22625 0.00189  -0.02650 -0.02299 170 SER A CA    
1241 C C     . SER A 176 ? 0.12615 0.23001 0.24526 0.00031  -0.02307 -0.00141 170 SER A C     
1242 O O     . SER A 176 ? 0.13281 0.21834 0.25091 -0.00582 -0.01721 0.01262  170 SER A O     
1243 C CB    . SER A 176 ? 0.15175 0.26204 0.24436 0.00105  -0.02511 -0.02857 170 SER A CB    
1244 O OG    . SER A 176 ? 0.16790 0.24239 0.28295 0.00100  -0.02718 -0.01060 170 SER A OG    
1245 N N     . ALA A 177 ? 0.11354 0.20863 0.26144 0.01502  -0.03839 -0.02423 171 ALA A N     
1246 C CA    . ALA A 177 ? 0.12897 0.19219 0.25185 0.01926  -0.05494 -0.00072 171 ALA A CA    
1247 C C     . ALA A 177 ? 0.13697 0.20288 0.27553 0.00560  -0.03892 0.00719  171 ALA A C     
1248 O O     . ALA A 177 ? 0.15357 0.20057 0.28462 -0.02413 -0.03016 0.00638  171 ALA A O     
1249 C CB    . ALA A 177 ? 0.12091 0.20007 0.27952 0.02635  -0.03251 0.01748  171 ALA A CB    
1250 N N     . LEU A 178 ? 0.10309 0.19778 0.25704 0.00512  -0.01174 0.02516  172 LEU A N     
1251 C CA    . LEU A 178 ? 0.10448 0.20143 0.26192 0.00041  0.00658  0.01985  172 LEU A CA    
1252 C C     . LEU A 178 ? 0.13112 0.20855 0.27604 0.01800  -0.02249 0.01232  172 LEU A C     
1253 O O     . LEU A 178 ? 0.15628 0.21696 0.29429 0.02192  -0.01080 0.00943  172 LEU A O     
1254 C CB    . LEU A 178 ? 0.09457 0.21264 0.26250 -0.01601 0.00215  0.00834  172 LEU A CB    
1255 C CG    . LEU A 178 ? 0.10491 0.24557 0.26076 -0.01220 -0.00496 -0.00707 172 LEU A CG    
1256 C CD1   . LEU A 178 ? 0.11836 0.26172 0.27799 -0.00571 -0.00373 -0.01885 172 LEU A CD1   
1257 C CD2   . LEU A 178 ? 0.11167 0.25741 0.33708 0.00274  -0.02770 -0.04740 172 LEU A CD2   
1258 N N     . ASN A 179 ? 0.12687 0.18436 0.29220 0.02578  -0.00764 -0.00515 173 ASN A N     
1259 C CA    . ASN A 179 ? 0.11463 0.21638 0.27320 0.00190  -0.01756 -0.01167 173 ASN A CA    
1260 C C     . ASN A 179 ? 0.11551 0.22477 0.24133 0.01722  -0.04016 -0.01279 173 ASN A C     
1261 O O     . ASN A 179 ? 0.11767 0.23162 0.24273 0.02107  -0.01542 0.01218  173 ASN A O     
1262 C CB    . ASN A 179 ? 0.09702 0.22880 0.23683 0.02117  0.00057  -0.04566 173 ASN A CB    
1263 C CG    . ASN A 179 ? 0.11636 0.28371 0.28599 0.01306  -0.00065 -0.05328 173 ASN A CG    
1264 O OD1   . ASN A 179 ? 0.11747 0.32714 0.28571 0.02244  -0.01625 -0.07913 173 ASN A OD1   
1265 N ND2   . ASN A 179 ? 0.13414 0.27964 0.30967 0.01329  -0.00474 -0.07408 173 ASN A ND2   
1266 N N     . ALA A 180 ? 0.08367 0.21287 0.20617 0.02768  -0.04939 -0.00835 174 ALA A N     
1267 C CA    . ALA A 180 ? 0.10951 0.22028 0.22738 0.02620  -0.04390 -0.00184 174 ALA A CA    
1268 C C     . ALA A 180 ? 0.11911 0.20861 0.25826 0.01384  -0.07556 -0.01675 174 ALA A C     
1269 O O     . ALA A 180 ? 0.13289 0.20713 0.25440 0.02002  -0.09322 0.00769  174 ALA A O     
1270 C CB    . ALA A 180 ? 0.10081 0.22497 0.23194 0.00925  -0.02547 0.00159  174 ALA A CB    
1271 N N     . ILE A 181 ? 0.12172 0.19696 0.25290 -0.00581 -0.07837 -0.04853 175 ILE A N     
1272 C CA    . ILE A 181 ? 0.15016 0.21230 0.28536 -0.01174 -0.06132 -0.02494 175 ILE A CA    
1273 C C     . ILE A 181 ? 0.15603 0.23362 0.31737 0.00050  -0.05623 -0.01956 175 ILE A C     
1274 O O     . ILE A 181 ? 0.16074 0.23483 0.28328 -0.00124 -0.06358 -0.01098 175 ILE A O     
1275 C CB    . ILE A 181 ? 0.15723 0.22565 0.31736 -0.01187 -0.04161 0.00721  175 ILE A CB    
1276 C CG1   . ILE A 181 ? 0.15845 0.20539 0.35262 -0.01295 -0.00748 0.01429  175 ILE A CG1   
1277 C CG2   . ILE A 181 ? 0.17278 0.25752 0.37178 -0.00928 -0.04976 -0.01064 175 ILE A CG2   
1278 C CD1   . ILE A 181 ? 0.17419 0.20936 0.38996 -0.02218 -0.02515 0.00971  175 ILE A CD1   
1279 N N     . GLU A 182 ? 0.15442 0.23331 0.35366 0.00796  -0.04577 0.00024  176 GLU A N     
1280 C CA    . GLU A 182 ? 0.17745 0.24498 0.32464 0.01608  -0.01456 0.05712  176 GLU A CA    
1281 C C     . GLU A 182 ? 0.17642 0.23859 0.29676 0.01758  -0.03430 0.03831  176 GLU A C     
1282 O O     . GLU A 182 ? 0.18821 0.23630 0.29346 0.04208  -0.05403 0.01680  176 GLU A O     
1283 C CB    . GLU A 182 ? 0.22853 0.29048 0.40883 0.03582  -0.01001 0.07641  176 GLU A CB    
1284 C CG    . GLU A 182 ? 0.28549 0.35831 0.50737 0.03515  0.01112  0.08441  176 GLU A CG    
1285 C CD    . GLU A 182 ? 0.35165 0.41702 0.62176 0.03051  0.02581  0.09491  176 GLU A CD    
1286 O OE1   . GLU A 182 ? 0.37920 0.45479 0.66586 0.03385  0.03597  0.06707  176 GLU A OE1   
1287 O OE2   . GLU A 182 ? 0.38391 0.44354 0.67250 0.02680  0.02747  0.10235  176 GLU A OE2   
1288 N N     . ALA A 183 ? 0.15338 0.23419 0.25535 0.00715  -0.00950 0.04060  177 ALA A N     
1289 C CA    . ALA A 183 ? 0.16311 0.24438 0.29067 -0.00296 -0.01438 0.02562  177 ALA A CA    
1290 C C     . ALA A 183 ? 0.17893 0.24168 0.30152 -0.02145 0.00407  0.03445  177 ALA A C     
1291 O O     . ALA A 183 ? 0.20799 0.25568 0.31931 -0.01676 0.02349  0.04177  177 ALA A O     
1292 C CB    . ALA A 183 ? 0.15098 0.24412 0.24688 -0.00200 -0.03364 0.02762  177 ALA A CB    
1293 N N     . GLY A 184 ? 0.15014 0.21903 0.27595 -0.01878 -0.00972 0.03022  178 GLY A N     
1294 C CA    . GLY A 184 ? 0.12955 0.21411 0.26154 -0.01295 -0.01818 0.02448  178 GLY A CA    
1295 C C     . GLY A 184 ? 0.13755 0.22237 0.24218 -0.01147 -0.02561 0.03061  178 GLY A C     
1296 O O     . GLY A 184 ? 0.15821 0.24661 0.19313 -0.01329 -0.02720 0.00563  178 GLY A O     
1297 N N     . PHE A 185 ? 0.12856 0.21486 0.22212 -0.00713 -0.04390 0.06050  179 PHE A N     
1298 C CA    . PHE A 185 ? 0.12573 0.20356 0.18500 0.00548  -0.04850 0.03809  179 PHE A CA    
1299 C C     . PHE A 185 ? 0.13411 0.22442 0.19555 0.01880  -0.02471 0.01576  179 PHE A C     
1300 O O     . PHE A 185 ? 0.14298 0.23645 0.22343 0.00789  -0.00897 0.02071  179 PHE A O     
1301 C CB    . PHE A 185 ? 0.11734 0.18759 0.17151 0.00415  -0.05348 0.03016  179 PHE A CB    
1302 C CG    . PHE A 185 ? 0.11541 0.18109 0.19566 -0.00162 -0.04152 0.00827  179 PHE A CG    
1303 C CD1   . PHE A 185 ? 0.12208 0.18471 0.21078 -0.01391 -0.05920 0.00876  179 PHE A CD1   
1304 C CD2   . PHE A 185 ? 0.13667 0.19052 0.21531 -0.00661 -0.02352 0.01098  179 PHE A CD2   
1305 C CE1   . PHE A 185 ? 0.12689 0.18661 0.23228 -0.00723 -0.00767 -0.02936 179 PHE A CE1   
1306 C CE2   . PHE A 185 ? 0.13361 0.20362 0.24405 -0.00669 -0.03995 -0.00525 179 PHE A CE2   
1307 C CZ    . PHE A 185 ? 0.13106 0.20919 0.23815 0.00358  -0.01712 -0.02414 179 PHE A CZ    
1308 N N     . ASP A 186 ? 0.14209 0.22150 0.19230 0.02284  -0.00340 0.01485  180 ASP A N     
1309 C CA    . ASP A 186 ? 0.13402 0.23704 0.20859 0.01351  0.03020  0.02009  180 ASP A CA    
1310 C C     . ASP A 186 ? 0.12967 0.22619 0.16073 0.00293  -0.00899 0.01176  180 ASP A C     
1311 O O     . ASP A 186 ? 0.15946 0.21917 0.20934 -0.01199 -0.02040 -0.02827 180 ASP A O     
1312 C CB    . ASP A 186 ? 0.14266 0.26805 0.20986 0.02049  0.00579  0.03199  180 ASP A CB    
1313 C CG    . ASP A 186 ? 0.16066 0.28675 0.22860 -0.00409 -0.01189 0.03041  180 ASP A CG    
1314 O OD1   . ASP A 186 ? 0.18046 0.32962 0.26717 -0.02255 -0.03745 0.00320  180 ASP A OD1   
1315 O OD2   . ASP A 186 ? 0.15539 0.28084 0.27243 -0.00868 -0.00887 0.01851  180 ASP A OD2   
1316 N N     . GLY A 187 ? 0.13469 0.22171 0.12707 -0.00130 -0.02727 0.03419  181 GLY A N     
1317 C CA    . GLY A 187 ? 0.13768 0.21902 0.09422 -0.00668 -0.03499 0.02294  181 GLY A CA    
1318 C C     . GLY A 187 ? 0.12252 0.20771 0.20802 -0.00033 -0.02885 0.01627  181 GLY A C     
1319 O O     . GLY A 187 ? 0.09911 0.17949 0.20391 0.00488  0.00040  0.02592  181 GLY A O     
1320 N N     . ILE A 188 ? 0.11490 0.19315 0.19297 0.01002  -0.04637 0.02218  182 ILE A N     
1321 C CA    . ILE A 188 ? 0.11121 0.18457 0.16280 0.02379  -0.05379 0.01272  182 ILE A CA    
1322 C C     . ILE A 188 ? 0.09958 0.17155 0.20669 0.01648  -0.02557 -0.01626 182 ILE A C     
1323 O O     . ILE A 188 ? 0.09353 0.16921 0.24644 0.00230  -0.01557 -0.03316 182 ILE A O     
1324 C CB    . ILE A 188 ? 0.11022 0.18868 0.22519 0.01640  -0.00401 0.01922  182 ILE A CB    
1325 C CG1   . ILE A 188 ? 0.12943 0.19511 0.24424 0.00280  -0.00357 0.01700  182 ILE A CG1   
1326 C CG2   . ILE A 188 ? 0.09239 0.19756 0.21929 0.02160  -0.00770 0.00206  182 ILE A CG2   
1327 C CD1   . ILE A 188 ? 0.13396 0.20466 0.28964 0.00584  0.01733  0.02200  182 ILE A CD1   
1328 N N     . GLU A 189 ? 0.10261 0.18069 0.22230 0.00079  -0.01129 0.00380  183 GLU A N     
1329 C CA    . GLU A 189 ? 0.11316 0.19372 0.22660 -0.00663 -0.02124 0.00108  183 GLU A CA    
1330 C C     . GLU A 189 ? 0.12389 0.18856 0.19827 -0.01640 -0.03454 -0.00969 183 GLU A C     
1331 O O     . GLU A 189 ? 0.15906 0.18516 0.20609 -0.01643 -0.02045 -0.04160 183 GLU A O     
1332 C CB    . GLU A 189 ? 0.12391 0.20163 0.25051 0.02221  -0.00804 -0.00599 183 GLU A CB    
1333 C CG    . GLU A 189 ? 0.12639 0.19948 0.24324 0.02881  -0.01751 0.02261  183 GLU A CG    
1334 C CD    . GLU A 189 ? 0.13966 0.18890 0.25285 0.00357  0.00357  0.00840  183 GLU A CD    
1335 O OE1   . GLU A 189 ? 0.14915 0.18268 0.29406 -0.00977 0.02431  -0.01474 183 GLU A OE1   
1336 O OE2   . GLU A 189 ? 0.12518 0.19577 0.30467 0.01126  0.00725  -0.02398 183 GLU A OE2   
1337 N N     . ILE A 190 ? 0.11452 0.18994 0.18985 -0.01873 -0.03393 0.02429  184 ILE A N     
1338 C CA    . ILE A 190 ? 0.09852 0.18164 0.18379 -0.01060 -0.02473 0.00186  184 ILE A CA    
1339 C C     . ILE A 190 ? 0.08426 0.18263 0.22332 0.00171  -0.02423 -0.00253 184 ILE A C     
1340 O O     . ILE A 190 ? 0.08623 0.19707 0.19838 0.03914  -0.01493 -0.00510 184 ILE A O     
1341 C CB    . ILE A 190 ? 0.09522 0.19758 0.19549 -0.00983 -0.01176 0.02897  184 ILE A CB    
1342 C CG1   . ILE A 190 ? 0.07739 0.17441 0.27748 0.01007  -0.00969 0.03943  184 ILE A CG1   
1343 C CG2   . ILE A 190 ? 0.09559 0.21397 0.22344 -0.00496 -0.00424 0.03814  184 ILE A CG2   
1344 C CD1   . ILE A 190 ? 0.09211 0.15441 0.33455 0.00369  -0.00381 0.06545  184 ILE A CD1   
1345 N N     . HIS A 191 ? 0.07382 0.19353 0.23582 -0.00785 -0.03999 -0.00436 185 HIS A N     
1346 C CA    . HIS A 191 ? 0.08272 0.18903 0.19810 -0.00176 -0.02978 0.01508  185 HIS A CA    
1347 C C     . HIS A 191 ? 0.10121 0.20575 0.22947 -0.00765 -0.01082 0.01343  185 HIS A C     
1348 O O     . HIS A 191 ? 0.11523 0.20819 0.23148 -0.00802 0.01829  -0.00541 185 HIS A O     
1349 C CB    . HIS A 191 ? 0.07372 0.19146 0.26881 -0.01071 -0.01568 -0.00346 185 HIS A CB    
1350 C CG    . HIS A 191 ? 0.08882 0.20353 0.29384 -0.01153 0.01031  -0.00449 185 HIS A CG    
1351 N ND1   . HIS A 191 ? 0.08383 0.19677 0.30488 -0.02008 0.01590  0.00555  185 HIS A ND1   
1352 C CD2   . HIS A 191 ? 0.07586 0.19993 0.28903 -0.00124 0.00303  -0.01526 185 HIS A CD2   
1353 C CE1   . HIS A 191 ? 0.09277 0.19364 0.29943 -0.03608 -0.01393 0.01974  185 HIS A CE1   
1354 N NE2   . HIS A 191 ? 0.10348 0.20879 0.27041 0.00233  -0.00535 -0.00169 185 HIS A NE2   
1355 N N     . GLY A 192 ? 0.10239 0.20356 0.21978 -0.02681 -0.02454 0.03601  186 GLY A N     
1356 C CA    . GLY A 192 ? 0.09403 0.22877 0.21467 -0.01721 -0.01873 0.02542  186 GLY A CA    
1357 C C     . GLY A 192 ? 0.08939 0.22945 0.22152 -0.00070 0.00751  0.00766  186 GLY A C     
1358 O O     . GLY A 192 ? 0.11305 0.25522 0.24081 -0.03239 0.02876  0.02180  186 GLY A O     
1359 N N     . ALA A 193 ? 0.07343 0.21742 0.22856 0.01185  0.01566  -0.01139 187 ALA A N     
1360 C CA    . ALA A 193 ? 0.06734 0.22163 0.22791 0.00793  0.02801  -0.01029 187 ALA A CA    
1361 C C     . ALA A 193 ? 0.08662 0.21694 0.21663 -0.00298 0.01142  -0.02147 187 ALA A C     
1362 O O     . ALA A 193 ? 0.08846 0.23018 0.24535 0.01385  -0.02083 -0.01688 187 ALA A O     
1363 C CB    . ALA A 193 ? 0.06875 0.21703 0.20582 -0.00269 0.03506  -0.01488 187 ALA A CB    
1364 N N     . HIS A 194 ? 0.11440 0.22827 0.21282 -0.02592 -0.01465 -0.05636 188 HIS A N     
1365 C CA    . HIS A 194 ? 0.14021 0.23589 0.23989 -0.03059 -0.00013 -0.03348 188 HIS A CA    
1366 C C     . HIS A 194 ? 0.14896 0.23362 0.22005 -0.01909 -0.00031 -0.00503 188 HIS A C     
1367 O O     . HIS A 194 ? 0.16322 0.24053 0.20428 0.00351  0.01052  -0.02646 188 HIS A O     
1368 C CB    . HIS A 194 ? 0.15085 0.27165 0.19833 -0.00827 0.01412  -0.02791 188 HIS A CB    
1369 C CG    . HIS A 194 ? 0.15625 0.27114 0.22756 0.00722  -0.00494 -0.01686 188 HIS A CG    
1370 N ND1   . HIS A 194 ? 0.17700 0.28559 0.24456 0.00302  0.00952  -0.02359 188 HIS A ND1   
1371 C CD2   . HIS A 194 ? 0.15662 0.30386 0.24984 0.01949  0.02979  -0.01243 188 HIS A CD2   
1372 C CE1   . HIS A 194 ? 0.17249 0.30254 0.28401 0.02063  0.01702  -0.02621 188 HIS A CE1   
1373 N NE2   . HIS A 194 ? 0.17388 0.30578 0.26746 0.02687  0.02580  -0.03562 188 HIS A NE2   
1374 N N     . GLY A 195 ? 0.13367 0.23099 0.22963 -0.01687 0.00318  0.03505  189 GLY A N     
1375 C CA    . GLY A 195 ? 0.11096 0.22349 0.20442 0.00383  -0.02677 0.06334  189 GLY A CA    
1376 C C     . GLY A 195 ? 0.10209 0.21149 0.20549 -0.01058 0.00782  0.03948  189 GLY A C     
1377 O O     . GLY A 195 ? 0.12918 0.21872 0.19864 -0.01610 -0.02753 0.02580  189 GLY A O     
1378 N N     . TYR A 196 ? 0.08533 0.19936 0.20319 -0.00485 0.00199  0.02956  190 TYR A N     
1379 C CA    . TYR A 196 ? 0.07892 0.19358 0.18895 0.01219  -0.00781 0.02014  190 TYR A CA    
1380 C C     . TYR A 196 ? 0.08630 0.19430 0.19060 0.00596  -0.01767 -0.00733 190 TYR A C     
1381 O O     . TYR A 196 ? 0.10302 0.17836 0.19978 0.00389  -0.03091 -0.02488 190 TYR A O     
1382 C CB    . TYR A 196 ? 0.06326 0.19498 0.21471 -0.00444 0.00913  -0.01065 190 TYR A CB    
1383 C CG    . TYR A 196 ? 0.06863 0.21448 0.22915 -0.01376 0.03145  0.00320  190 TYR A CG    
1384 C CD1   . TYR A 196 ? 0.08581 0.22277 0.26050 -0.01700 0.02275  0.01623  190 TYR A CD1   
1385 C CD2   . TYR A 196 ? 0.06532 0.22455 0.23153 -0.00902 0.02415  -0.00026 190 TYR A CD2   
1386 C CE1   . TYR A 196 ? 0.08413 0.23661 0.26502 -0.02029 0.01399  0.03826  190 TYR A CE1   
1387 C CE2   . TYR A 196 ? 0.08207 0.24693 0.30714 -0.01576 0.00598  0.01308  190 TYR A CE2   
1388 C CZ    . TYR A 196 ? 0.09747 0.25779 0.31934 -0.02165 0.02030  0.03155  190 TYR A CZ    
1389 O OH    . TYR A 196 ? 0.13577 0.28150 0.36150 -0.04319 0.03924  0.04418  190 TYR A OH    
1390 N N     . LEU A 197 ? 0.07401 0.21176 0.18738 -0.00526 0.00023  -0.00482 191 LEU A N     
1391 C CA    . LEU A 197 ? 0.10326 0.19062 0.23530 -0.01159 -0.00494 0.02685  191 LEU A CA    
1392 C C     . LEU A 197 ? 0.11346 0.18709 0.23010 0.01521  -0.00685 -0.00212 191 LEU A C     
1393 O O     . LEU A 197 ? 0.12697 0.18759 0.18384 0.01290  -0.00015 -0.02625 191 LEU A O     
1394 C CB    . LEU A 197 ? 0.09449 0.20153 0.21269 -0.00007 0.00150  0.01045  191 LEU A CB    
1395 C CG    . LEU A 197 ? 0.10925 0.22191 0.22304 0.00384  -0.00445 0.02869  191 LEU A CG    
1396 C CD1   . LEU A 197 ? 0.11787 0.22418 0.19795 -0.00234 0.02365  0.01184  191 LEU A CD1   
1397 C CD2   . LEU A 197 ? 0.11592 0.22241 0.28552 0.00636  -0.01681 0.03807  191 LEU A CD2   
1398 N N     . ILE A 198 ? 0.10657 0.15928 0.23227 0.02032  -0.02436 -0.01665 192 ILE A N     
1399 C CA    . ILE A 198 ? 0.11513 0.16117 0.19633 0.01481  -0.01222 -0.02841 192 ILE A CA    
1400 C C     . ILE A 198 ? 0.10123 0.18694 0.22859 -0.00842 -0.01920 -0.04304 192 ILE A C     
1401 O O     . ILE A 198 ? 0.12617 0.19131 0.20518 -0.00202 0.00463  -0.01494 192 ILE A O     
1402 C CB    . ILE A 198 ? 0.14093 0.15731 0.18063 0.01014  -0.02102 -0.03241 192 ILE A CB    
1403 C CG1   . ILE A 198 ? 0.14125 0.17559 0.18291 0.00478  -0.01318 0.00975  192 ILE A CG1   
1404 C CG2   . ILE A 198 ? 0.15955 0.14520 0.29440 0.00077  0.00262  -0.03928 192 ILE A CG2   
1405 C CD1   . ILE A 198 ? 0.15351 0.18268 0.22399 0.00153  -0.00221 0.00392  192 ILE A CD1   
1406 N N     . ASP A 199 ? 0.09494 0.20847 0.25359 -0.02442 -0.01829 -0.06682 193 ASP A N     
1407 C CA    . ASP A 199 ? 0.11347 0.22739 0.25134 -0.01012 0.00628  -0.03038 193 ASP A CA    
1408 C C     . ASP A 199 ? 0.10770 0.22265 0.23504 0.01889  -0.00407 -0.03314 193 ASP A C     
1409 O O     . ASP A 199 ? 0.13368 0.24255 0.21411 0.02020  -0.00561 -0.01592 193 ASP A O     
1410 C CB    . ASP A 199 ? 0.11130 0.22745 0.29012 -0.00938 0.01502  -0.03540 193 ASP A CB    
1411 C CG    . ASP A 199 ? 0.17178 0.24544 0.32374 -0.01566 0.00132  -0.01280 193 ASP A CG    
1412 O OD1   . ASP A 199 ? 0.21028 0.27562 0.31313 -0.00662 -0.02456 0.01320  193 ASP A OD1   
1413 O OD2   . ASP A 199 ? 0.18199 0.24593 0.32258 0.00321  -0.02767 -0.03970 193 ASP A OD2   
1414 N N     . GLN A 200 ? 0.11010 0.20573 0.20477 0.01886  -0.00756 -0.04781 194 GLN A N     
1415 C CA    . GLN A 200 ? 0.11029 0.18666 0.19699 0.00234  -0.00351 -0.04809 194 GLN A CA    
1416 C C     . GLN A 200 ? 0.11920 0.19693 0.18075 -0.00698 -0.01000 -0.03443 194 GLN A C     
1417 O O     . GLN A 200 ? 0.11621 0.21757 0.20092 -0.01565 -0.02675 0.00128  194 GLN A O     
1418 C CB    . GLN A 200 ? 0.11708 0.16897 0.18904 -0.00620 0.02659  -0.02833 194 GLN A CB    
1419 C CG    . GLN A 200 ? 0.12670 0.18752 0.18385 -0.02580 0.01445  -0.00228 194 GLN A CG    
1420 C CD    . GLN A 200 ? 0.11756 0.20826 0.17681 -0.01249 0.00588  -0.00042 194 GLN A CD    
1421 O OE1   . GLN A 200 ? 0.11951 0.21266 0.17933 -0.00427 0.01674  0.01670  194 GLN A OE1   
1422 N NE2   . GLN A 200 ? 0.12249 0.23059 0.18314 -0.01555 -0.00066 -0.00642 194 GLN A NE2   
1423 N N     . PHE A 201 ? 0.10740 0.19484 0.19265 -0.00670 -0.01475 -0.03465 195 PHE A N     
1424 C CA    . PHE A 201 ? 0.08569 0.20584 0.19775 -0.00598 -0.02211 -0.01912 195 PHE A CA    
1425 C C     . PHE A 201 ? 0.08973 0.20810 0.21597 -0.01010 -0.00363 -0.00701 195 PHE A C     
1426 O O     . PHE A 201 ? 0.10693 0.22386 0.25372 -0.01667 0.02489  0.00304  195 PHE A O     
1427 C CB    . PHE A 201 ? 0.07006 0.20560 0.25029 -0.00091 -0.01096 0.00769  195 PHE A CB    
1428 C CG    . PHE A 201 ? 0.09315 0.20964 0.27230 -0.00552 -0.00437 0.00333  195 PHE A CG    
1429 C CD1   . PHE A 201 ? 0.10777 0.21361 0.29108 0.01014  -0.01192 -0.00177 195 PHE A CD1   
1430 C CD2   . PHE A 201 ? 0.08494 0.21403 0.24832 -0.00322 0.00735  -0.00049 195 PHE A CD2   
1431 C CE1   . PHE A 201 ? 0.09523 0.22263 0.26318 -0.00024 0.01437  0.02013  195 PHE A CE1   
1432 C CE2   . PHE A 201 ? 0.10323 0.20537 0.22121 0.00429  0.02236  -0.00437 195 PHE A CE2   
1433 C CZ    . PHE A 201 ? 0.10741 0.21898 0.25398 -0.00510 0.01446  0.00333  195 PHE A CZ    
1434 N N     . LEU A 202 ? 0.08364 0.20398 0.23381 0.00152  0.01577  -0.00742 196 LEU A N     
1435 C CA    . LEU A 202 ? 0.09588 0.21305 0.22980 0.01148  0.01047  -0.00375 196 LEU A CA    
1436 C C     . LEU A 202 ? 0.13531 0.22396 0.22790 0.00288  -0.00457 0.00892  196 LEU A C     
1437 O O     . LEU A 202 ? 0.14644 0.22378 0.24441 0.01078  0.01850  0.00405  196 LEU A O     
1438 C CB    . LEU A 202 ? 0.12143 0.21077 0.22688 -0.00864 0.02901  -0.00630 196 LEU A CB    
1439 C CG    . LEU A 202 ? 0.11611 0.19584 0.20206 -0.02495 0.02579  0.01201  196 LEU A CG    
1440 C CD1   . LEU A 202 ? 0.13701 0.21453 0.24691 -0.02223 0.03417  -0.00483 196 LEU A CD1   
1441 C CD2   . LEU A 202 ? 0.12753 0.19487 0.24506 -0.04383 0.02992  -0.02529 196 LEU A CD2   
1442 N N     . LYS A 203 ? 0.14134 0.23546 0.23513 -0.00186 -0.02259 -0.00162 197 LYS A N     
1443 C CA    . LYS A 203 ? 0.14246 0.23234 0.20803 -0.01146 -0.01002 0.04572  197 LYS A CA    
1444 C C     . LYS A 203 ? 0.16190 0.23254 0.19715 -0.01550 0.00840  0.02553  197 LYS A C     
1445 O O     . LYS A 203 ? 0.17174 0.23296 0.20125 0.00896  0.00150  0.01022  197 LYS A O     
1446 C CB    . LYS A 203 ? 0.13055 0.23768 0.16305 -0.00221 0.03291  0.04573  197 LYS A CB    
1447 C CG    . LYS A 203 ? 0.15300 0.25828 0.21321 0.02874  0.02555  0.02916  197 LYS A CG    
1448 C CD    . LYS A 203 ? 0.18409 0.27241 0.25094 0.03169  0.01975  0.00911  197 LYS A CD    
1449 C CE    . LYS A 203 ? 0.18902 0.26440 0.30806 0.01499  -0.00128 0.01646  197 LYS A CE    
1450 N NZ    . LYS A 203 ? 0.18259 0.26023 0.31550 0.01111  -0.01584 0.01580  197 LYS A NZ    
1451 N N     . ASP A 204 ? 0.17338 0.20555 0.19110 -0.02096 0.00058  0.06878  198 ASP A N     
1452 C CA    . ASP A 204 ? 0.21274 0.24081 0.23718 -0.01231 -0.01592 0.04602  198 ASP A CA    
1453 C C     . ASP A 204 ? 0.21498 0.27328 0.21815 0.00324  -0.00860 0.03762  198 ASP A C     
1454 O O     . ASP A 204 ? 0.23204 0.29060 0.26619 0.00759  0.03401  0.00991  198 ASP A O     
1455 C CB    . ASP A 204 ? 0.24115 0.24294 0.29610 -0.01725 -0.02748 0.02936  198 ASP A CB    
1456 C CG    . ASP A 204 ? 0.27630 0.26643 0.37265 -0.02443 -0.04544 0.03692  198 ASP A CG    
1457 O OD1   . ASP A 204 ? 0.26751 0.26966 0.37971 -0.02788 -0.02414 0.02988  198 ASP A OD1   
1458 O OD2   . ASP A 204 ? 0.30449 0.31642 0.41571 -0.02246 -0.08528 0.04917  198 ASP A OD2   
1459 N N     . GLY A 205 ? 0.17396 0.26813 0.24384 0.02003  -0.03573 -0.00521 199 GLY A N     
1460 C CA    . GLY A 205 ? 0.20130 0.28145 0.31078 0.04432  -0.04603 -0.02009 199 GLY A CA    
1461 C C     . GLY A 205 ? 0.20554 0.28017 0.31049 0.04099  -0.05003 -0.06485 199 GLY A C     
1462 O O     . GLY A 205 ? 0.24417 0.31163 0.37992 0.05636  -0.06596 -0.08726 199 GLY A O     
1463 N N     . ILE A 206 ? 0.18319 0.26587 0.24291 0.04837  -0.01754 -0.02025 200 ILE A N     
1464 C CA    . ILE A 206 ? 0.17999 0.27635 0.28674 0.03857  -0.02289 -0.02276 200 ILE A CA    
1465 C C     . ILE A 206 ? 0.20246 0.29094 0.25031 0.04205  -0.01499 -0.02658 200 ILE A C     
1466 O O     . ILE A 206 ? 0.24800 0.31556 0.23366 0.03760  -0.04849 -0.04002 200 ILE A O     
1467 C CB    . ILE A 206 ? 0.16628 0.26577 0.33110 0.03936  -0.03393 0.01055  200 ILE A CB    
1468 C CG1   . ILE A 206 ? 0.15474 0.27281 0.36546 0.01865  -0.05896 0.04622  200 ILE A CG1   
1469 C CG2   . ILE A 206 ? 0.17100 0.24906 0.30186 0.02421  -0.04532 -0.01317 200 ILE A CG2   
1470 C CD1   . ILE A 206 ? 0.15195 0.25808 0.36087 0.02566  -0.07027 0.06421  200 ILE A CD1   
1471 N N     . ASN A 207 ? 0.18637 0.29085 0.24918 0.01204  0.00753  -0.03731 201 ASN A N     
1472 C CA    . ASN A 207 ? 0.19889 0.28877 0.22195 -0.00076 0.03559  0.01274  201 ASN A CA    
1473 C C     . ASN A 207 ? 0.23197 0.32206 0.23878 0.02236  0.04241  -0.00259 201 ASN A C     
1474 O O     . ASN A 207 ? 0.25375 0.32623 0.29509 0.02715  0.08679  0.04156  201 ASN A O     
1475 C CB    . ASN A 207 ? 0.18389 0.26192 0.23234 -0.01066 0.01810  0.02333  201 ASN A CB    
1476 C CG    . ASN A 207 ? 0.18432 0.25464 0.20843 -0.02800 0.03863  0.02647  201 ASN A CG    
1477 O OD1   . ASN A 207 ? 0.18197 0.26581 0.21558 -0.02791 0.04969  0.01419  201 ASN A OD1   
1478 N ND2   . ASN A 207 ? 0.18698 0.23707 0.21507 -0.04216 -0.02057 0.02252  201 ASN A ND2   
1479 N N     . ASP A 208 ? 0.24979 0.35750 0.23741 0.03697  0.01502  -0.02139 202 ASP A N     
1480 C CA    . ASP A 208 ? 0.25729 0.37080 0.27624 0.02491  0.00489  0.00843  202 ASP A CA    
1481 C C     . ASP A 208 ? 0.23492 0.37542 0.27905 0.02260  0.02218  0.01639  202 ASP A C     
1482 O O     . ASP A 208 ? 0.23329 0.38835 0.22881 0.01121  -0.01002 0.01310  202 ASP A O     
1483 C CB    . ASP A 208 ? 0.29261 0.37082 0.23938 0.03197  -0.00507 -0.02370 202 ASP A CB    
1484 C CG    . ASP A 208 ? 0.31255 0.37814 0.27719 0.02627  -0.00990 0.00081  202 ASP A CG    
1485 O OD1   . ASP A 208 ? 0.30705 0.37502 0.28027 0.01910  0.00286  -0.01170 202 ASP A OD1   
1486 O OD2   . ASP A 208 ? 0.32642 0.36205 0.29677 0.03299  -0.02442 0.01243  202 ASP A OD2   
1487 N N     . ARG A 209 ? 0.21228 0.35081 0.28986 0.03633  0.02370  0.01118  203 ARG A N     
1488 C CA    . ARG A 209 ? 0.21695 0.32878 0.30236 0.01726  0.01616  0.04356  203 ARG A CA    
1489 C C     . ARG A 209 ? 0.25764 0.34156 0.30970 0.01798  0.03118  0.01795  203 ARG A C     
1490 O O     . ARG A 209 ? 0.28313 0.32548 0.33666 0.03749  0.02619  0.02115  203 ARG A O     
1491 C CB    . ARG A 209 ? 0.19296 0.30073 0.29403 0.00571  -0.00688 0.05403  203 ARG A CB    
1492 C CG    . ARG A 209 ? 0.16279 0.27068 0.29155 -0.00798 -0.00288 0.03364  203 ARG A CG    
1493 C CD    . ARG A 209 ? 0.12705 0.24560 0.26950 -0.02406 -0.01967 -0.00189 203 ARG A CD    
1494 N NE    . ARG A 209 ? 0.11645 0.22814 0.29176 -0.04577 0.00638  0.00557  203 ARG A NE    
1495 C CZ    . ARG A 209 ? 0.13501 0.22346 0.29572 -0.04848 0.01541  0.00822  203 ARG A CZ    
1496 N NH1   . ARG A 209 ? 0.14268 0.22646 0.26957 -0.05670 0.01789  -0.02371 203 ARG A NH1   
1497 N NH2   . ARG A 209 ? 0.16765 0.22795 0.29125 -0.03400 0.01790  0.02832  203 ARG A NH2   
1498 N N     . THR A 210 ? 0.27487 0.36390 0.32926 -0.01231 0.06463  0.03015  204 THR A N     
1499 C CA    . THR A 210 ? 0.29948 0.39038 0.37506 -0.02487 0.07666  0.04137  204 THR A CA    
1500 C C     . THR A 210 ? 0.29549 0.36934 0.40363 -0.05194 0.07556  0.04623  204 THR A C     
1501 O O     . THR A 210 ? 0.31994 0.36732 0.43387 -0.07463 0.07280  0.04764  204 THR A O     
1502 C CB    . THR A 210 ? 0.31978 0.42918 0.38726 -0.01390 0.10017  0.03541  204 THR A CB    
1503 O OG1   . THR A 210 ? 0.33410 0.44091 0.37931 -0.00765 0.13956  0.02710  204 THR A OG1   
1504 C CG2   . THR A 210 ? 0.32366 0.44183 0.41260 -0.00746 0.09671  0.03948  204 THR A CG2   
1505 N N     . ASP A 211 ? 0.26856 0.33452 0.38094 -0.03224 0.05475  0.03903  205 ASP A N     
1506 C CA    . ASP A 211 ? 0.24399 0.30324 0.38887 -0.03394 0.07188  0.03221  205 ASP A CA    
1507 C C     . ASP A 211 ? 0.24276 0.28522 0.37968 -0.03638 0.09177  0.02013  205 ASP A C     
1508 O O     . ASP A 211 ? 0.25499 0.27709 0.38730 -0.01497 0.10226  0.01353  205 ASP A O     
1509 C CB    . ASP A 211 ? 0.22057 0.29255 0.40743 -0.04105 0.08572  0.02876  205 ASP A CB    
1510 C CG    . ASP A 211 ? 0.19368 0.29147 0.38340 -0.04397 0.08899  0.05079  205 ASP A CG    
1511 O OD1   . ASP A 211 ? 0.17931 0.28717 0.35316 -0.03514 0.09526  0.04801  205 ASP A OD1   
1512 O OD2   . ASP A 211 ? 0.17472 0.29031 0.38807 -0.06439 0.07222  0.05127  205 ASP A OD2   
1513 N N     . GLU A 212 ? 0.24031 0.28745 0.38258 -0.04269 0.09150  0.02081  206 GLU A N     
1514 C CA    . GLU A 212 ? 0.25365 0.29823 0.41771 -0.05076 0.09738  -0.00725 206 GLU A CA    
1515 C C     . GLU A 212 ? 0.22723 0.26862 0.36010 -0.04577 0.08490  -0.01359 206 GLU A C     
1516 O O     . GLU A 212 ? 0.21097 0.24284 0.34160 -0.04178 0.13608  -0.04361 206 GLU A O     
1517 C CB    . GLU A 212 ? 0.30014 0.33582 0.53322 -0.08062 0.09355  -0.02141 206 GLU A CB    
1518 C CG    . GLU A 212 ? 0.35433 0.37924 0.66944 -0.07833 0.08266  -0.04709 206 GLU A CG    
1519 C CD    . GLU A 212 ? 0.41072 0.40964 0.78703 -0.08214 0.07848  -0.06580 206 GLU A CD    
1520 O OE1   . GLU A 212 ? 0.44778 0.44407 0.84072 -0.10700 0.04332  -0.08204 206 GLU A OE1   
1521 O OE2   . GLU A 212 ? 0.41610 0.40949 0.82110 -0.04425 0.11350  -0.05912 206 GLU A OE2   
1522 N N     . TYR A 213 ? 0.20274 0.25445 0.32194 -0.05119 0.07150  -0.00216 207 TYR A N     
1523 C CA    . TYR A 213 ? 0.18309 0.25490 0.27918 -0.02506 0.04495  -0.00580 207 TYR A CA    
1524 C C     . TYR A 213 ? 0.20430 0.25309 0.25150 -0.00748 0.01536  0.00254  207 TYR A C     
1525 O O     . TYR A 213 ? 0.18055 0.27677 0.27521 -0.01881 0.03859  0.01345  207 TYR A O     
1526 C CB    . TYR A 213 ? 0.17170 0.26664 0.29128 -0.02674 0.04397  0.01245  207 TYR A CB    
1527 C CG    . TYR A 213 ? 0.14676 0.27830 0.27281 -0.01413 0.03309  -0.00289 207 TYR A CG    
1528 C CD1   . TYR A 213 ? 0.13428 0.28784 0.27332 -0.00143 0.03129  -0.01615 207 TYR A CD1   
1529 C CD2   . TYR A 213 ? 0.14387 0.27381 0.25016 -0.01336 0.02260  0.00627  207 TYR A CD2   
1530 C CE1   . TYR A 213 ? 0.13753 0.30493 0.23904 0.01082  0.02399  -0.03432 207 TYR A CE1   
1531 C CE2   . TYR A 213 ? 0.13406 0.28412 0.27906 0.00426  0.04084  -0.01212 207 TYR A CE2   
1532 C CZ    . TYR A 213 ? 0.13514 0.31065 0.26775 0.00681  0.03354  -0.02007 207 TYR A CZ    
1533 O OH    . TYR A 213 ? 0.15943 0.33367 0.33621 0.01230  0.02693  -0.05804 207 TYR A OH    
1534 N N     . GLY A 214 ? 0.22694 0.24629 0.23636 0.01089  -0.04416 -0.01903 208 GLY A N     
1535 C CA    . GLY A 214 ? 0.25561 0.25065 0.28334 0.02375  -0.04342 0.02358  208 GLY A CA    
1536 C C     . GLY A 214 ? 0.27940 0.27475 0.30683 0.03530  -0.04931 0.00328  208 GLY A C     
1537 O O     . GLY A 214 ? 0.28803 0.26941 0.30083 0.03914  -0.05594 -0.01498 208 GLY A O     
1538 N N     . GLY A 215 ? 0.28447 0.29750 0.32676 0.04780  -0.03421 0.00918  209 GLY A N     
1539 C CA    . GLY A 215 ? 0.28724 0.32892 0.36741 0.04302  -0.02952 0.01247  209 GLY A CA    
1540 C C     . GLY A 215 ? 0.28570 0.33942 0.43473 0.02354  -0.01979 0.03438  209 GLY A C     
1541 O O     . GLY A 215 ? 0.31267 0.36151 0.49769 0.02631  -0.02856 0.04385  209 GLY A O     
1542 N N     . SER A 216 ? 0.24583 0.30807 0.32565 -0.00605 -0.00241 0.05590  210 SER A N     
1543 C CA    . SER A 216 ? 0.23627 0.28955 0.33479 -0.00729 -0.00361 0.07312  210 SER A CA    
1544 C C     . SER A 216 ? 0.21223 0.28011 0.31292 -0.01216 -0.00237 0.02614  210 SER A C     
1545 O O     . SER A 216 ? 0.18928 0.26387 0.27647 -0.01780 -0.00307 0.04211  210 SER A O     
1546 C CB    . SER A 216 ? 0.24066 0.28301 0.32860 -0.00711 -0.00976 0.06821  210 SER A CB    
1547 O OG    . SER A 216 ? 0.23843 0.26911 0.27090 0.00437  0.01422  0.07175  210 SER A OG    
1548 N N     . LEU A 217 ? 0.20856 0.27568 0.35867 0.00425  0.05800  0.01427  211 LEU A N     
1549 C CA    . LEU A 217 ? 0.22738 0.26063 0.37797 0.01248  0.08028  -0.03087 211 LEU A CA    
1550 C C     . LEU A 217 ? 0.22814 0.23273 0.35868 -0.00170 0.08331  -0.01154 211 LEU A C     
1551 O O     . LEU A 217 ? 0.21767 0.20756 0.35036 0.02645  0.08988  0.03132  211 LEU A O     
1552 C CB    . LEU A 217 ? 0.25794 0.27415 0.43280 0.01233  0.09368  -0.05078 211 LEU A CB    
1553 C CG    . LEU A 217 ? 0.27733 0.29150 0.39498 -0.00572 0.09102  -0.09768 211 LEU A CG    
1554 C CD1   . LEU A 217 ? 0.27962 0.29906 0.38314 -0.05278 0.10301  -0.08580 211 LEU A CD1   
1555 C CD2   . LEU A 217 ? 0.27975 0.30913 0.40905 0.02004  0.06180  -0.11260 211 LEU A CD2   
1556 N N     . ALA A 218 ? 0.20880 0.22386 0.36468 -0.01935 0.06718  -0.03815 212 ALA A N     
1557 C CA    . ALA A 218 ? 0.21079 0.21894 0.30825 -0.02966 0.06585  -0.02524 212 ALA A CA    
1558 C C     . ALA A 218 ? 0.20016 0.20941 0.31338 -0.02572 0.04600  -0.02625 212 ALA A C     
1559 O O     . ALA A 218 ? 0.20960 0.23184 0.32592 -0.03076 0.02973  -0.03901 212 ALA A O     
1560 C CB    . ALA A 218 ? 0.21404 0.22883 0.31541 -0.04141 0.05451  -0.03383 212 ALA A CB    
1561 N N     . ASN A 219 ? 0.19767 0.17851 0.29196 -0.01211 0.01189  -0.05494 213 ASN A N     
1562 C CA    . ASN A 219 ? 0.18189 0.18566 0.28012 -0.00027 0.05878  -0.03357 213 ASN A CA    
1563 C C     . ASN A 219 ? 0.15654 0.19429 0.26915 0.00685  0.02657  -0.01499 213 ASN A C     
1564 O O     . ASN A 219 ? 0.14033 0.20195 0.26753 0.01706  0.01503  -0.03014 213 ASN A O     
1565 C CB    . ASN A 219 ? 0.21761 0.18990 0.26019 -0.02849 0.06996  0.00253  213 ASN A CB    
1566 C CG    . ASN A 219 ? 0.26071 0.22244 0.33149 -0.02897 0.07979  0.00223  213 ASN A CG    
1567 O OD1   . ASN A 219 ? 0.27340 0.23992 0.38222 -0.03654 0.10168  0.00891  213 ASN A OD1   
1568 N ND2   . ASN A 219 ? 0.28008 0.22419 0.34197 -0.03664 0.09702  0.00415  213 ASN A ND2   
1569 N N     . ARG A 220 ? 0.15022 0.22818 0.23804 -0.00689 0.04402  0.00782  214 ARG A N     
1570 C CA    . ARG A 220 ? 0.14512 0.23959 0.22318 -0.00239 -0.02070 0.02285  214 ARG A CA    
1571 C C     . ARG A 220 ? 0.13230 0.23615 0.22663 -0.01418 0.00148  -0.00953 214 ARG A C     
1572 O O     . ARG A 220 ? 0.15398 0.25204 0.21599 -0.03049 -0.00340 0.02513  214 ARG A O     
1573 C CB    . ARG A 220 ? 0.16062 0.25123 0.21766 -0.00438 -0.08123 0.02892  214 ARG A CB    
1574 C CG    . ARG A 220 ? 0.19098 0.26212 0.26211 0.00508  -0.08031 0.01778  214 ARG A CG    
1575 C CD    . ARG A 220 ? 0.23613 0.29601 0.27325 0.01855  -0.08107 0.03145  214 ARG A CD    
1576 N NE    . ARG A 220 ? 0.27868 0.32531 0.33295 0.01552  -0.06151 -0.00653 214 ARG A NE    
1577 C CZ    . ARG A 220 ? 0.33780 0.34914 0.38572 0.00114  -0.09829 -0.01305 214 ARG A CZ    
1578 N NH1   . ARG A 220 ? 0.34895 0.35620 0.39151 -0.02859 -0.08368 -0.02385 214 ARG A NH1   
1579 N NH2   . ARG A 220 ? 0.35982 0.35421 0.37713 0.01590  -0.15035 -0.00035 214 ARG A NH2   
1580 N N     . CYS A 221 ? 0.13047 0.21490 0.22870 -0.00460 0.03203  -0.03019 215 CYS A N     
1581 C CA    . CYS A 221 ? 0.14266 0.20969 0.21198 0.00819  -0.00383 -0.03307 215 CYS A CA    
1582 C C     . CYS A 221 ? 0.12855 0.20205 0.20098 -0.01323 0.00996  -0.03419 215 CYS A C     
1583 O O     . CYS A 221 ? 0.14528 0.20824 0.23753 0.00589  0.01460  -0.01514 215 CYS A O     
1584 C CB    . CYS A 221 ? 0.16015 0.22245 0.25740 0.04213  -0.00682 -0.04870 215 CYS A CB    
1585 S SG    . CYS A 221 ? 0.19127 0.25515 0.31618 0.03894  0.01080  -0.01130 215 CYS A SG    
1586 N N     . LYS A 222 ? 0.12795 0.22079 0.23126 -0.00741 0.00767  -0.02495 216 LYS A N     
1587 C CA    . LYS A 222 ? 0.12508 0.23591 0.23756 -0.02425 0.01844  -0.00116 216 LYS A CA    
1588 C C     . LYS A 222 ? 0.11150 0.21959 0.28721 -0.01345 0.00044  -0.01123 216 LYS A C     
1589 O O     . LYS A 222 ? 0.11740 0.21196 0.29021 -0.01491 -0.01716 -0.03247 216 LYS A O     
1590 C CB    . LYS A 222 ? 0.18301 0.28347 0.29207 -0.04828 0.07501  0.00765  216 LYS A CB    
1591 C CG    . LYS A 222 ? 0.22869 0.34147 0.35585 -0.05834 0.07903  0.01377  216 LYS A CG    
1592 C CD    . LYS A 222 ? 0.25932 0.38175 0.45232 -0.07481 0.08033  0.01409  216 LYS A CD    
1593 C CE    . LYS A 222 ? 0.26726 0.41058 0.47928 -0.09116 0.09125  0.02210  216 LYS A CE    
1594 N NZ    . LYS A 222 ? 0.25598 0.43152 0.50011 -0.08342 0.09121  0.00980  216 LYS A NZ    
1595 N N     . PHE A 223 ? 0.10269 0.20623 0.24814 0.00125  -0.00526 -0.02137 217 PHE A N     
1596 C CA    . PHE A 223 ? 0.10848 0.20778 0.24555 -0.01473 0.01648  -0.00219 217 PHE A CA    
1597 C C     . PHE A 223 ? 0.09678 0.21109 0.22678 -0.01488 0.02209  -0.01458 217 PHE A C     
1598 O O     . PHE A 223 ? 0.10275 0.21146 0.25245 -0.00455 0.02359  -0.01745 217 PHE A O     
1599 C CB    . PHE A 223 ? 0.12294 0.21224 0.25932 -0.02880 0.04655  -0.02081 217 PHE A CB    
1600 C CG    . PHE A 223 ? 0.12396 0.20828 0.30555 -0.01880 0.05973  -0.01801 217 PHE A CG    
1601 C CD1   . PHE A 223 ? 0.15196 0.20975 0.40394 -0.01518 0.07891  0.00751  217 PHE A CD1   
1602 C CD2   . PHE A 223 ? 0.12199 0.18828 0.33343 -0.04260 0.02404  -0.00241 217 PHE A CD2   
1603 C CE1   . PHE A 223 ? 0.15149 0.21042 0.40170 -0.00943 0.03697  0.04050  217 PHE A CE1   
1604 C CE2   . PHE A 223 ? 0.12983 0.18815 0.31495 -0.00321 0.02016  -0.00400 217 PHE A CE2   
1605 C CZ    . PHE A 223 ? 0.12313 0.18653 0.32712 -0.01741 0.01571  0.03111  217 PHE A CZ    
1606 N N     . ILE A 224 ? 0.10746 0.20941 0.27967 -0.03655 0.01596  -0.03169 218 ILE A N     
1607 C CA    . ILE A 224 ? 0.08465 0.20641 0.27696 -0.02002 0.02556  -0.05144 218 ILE A CA    
1608 C C     . ILE A 224 ? 0.10959 0.19882 0.30424 -0.00822 0.01791  -0.03561 218 ILE A C     
1609 O O     . ILE A 224 ? 0.09847 0.19369 0.28075 0.00056  -0.00723 0.00062  218 ILE A O     
1610 C CB    . ILE A 224 ? 0.07996 0.20746 0.28661 0.00957  0.02291  -0.02352 218 ILE A CB    
1611 C CG1   . ILE A 224 ? 0.06785 0.21201 0.19930 0.01735  0.03695  -0.00284 218 ILE A CG1   
1612 C CG2   . ILE A 224 ? 0.08548 0.20304 0.30014 0.01822  0.02046  -0.00460 218 ILE A CG2   
1613 C CD1   . ILE A 224 ? 0.07987 0.23315 0.24338 0.00939  0.04712  -0.00460 218 ILE A CD1   
1614 N N     . THR A 225 ? 0.10951 0.17676 0.26798 -0.03224 -0.00367 0.00243  219 THR A N     
1615 C CA    . THR A 225 ? 0.12309 0.17434 0.30468 -0.00861 -0.03216 0.01083  219 THR A CA    
1616 C C     . THR A 225 ? 0.12506 0.17943 0.26868 -0.00666 -0.01023 0.02398  219 THR A C     
1617 O O     . THR A 225 ? 0.13980 0.16299 0.25157 -0.01796 0.00215  -0.00735 219 THR A O     
1618 C CB    . THR A 225 ? 0.13597 0.17406 0.32033 -0.01500 -0.05750 0.01576  219 THR A CB    
1619 O OG1   . THR A 225 ? 0.16832 0.16910 0.30483 -0.00085 -0.04533 0.02141  219 THR A OG1   
1620 C CG2   . THR A 225 ? 0.13892 0.18892 0.31486 -0.02129 -0.05316 0.01053  219 THR A CG2   
1621 N N     . GLN A 226 ? 0.09715 0.17740 0.24227 0.01519  0.03627  0.04647  220 GLN A N     
1622 C CA    . GLN A 226 ? 0.09149 0.21402 0.23370 0.01944  0.03349  0.03286  220 GLN A CA    
1623 C C     . GLN A 226 ? 0.08811 0.21750 0.22610 -0.01053 0.01977  0.01171  220 GLN A C     
1624 O O     . GLN A 226 ? 0.13885 0.21399 0.26431 -0.00742 -0.02206 0.04044  220 GLN A O     
1625 C CB    . GLN A 226 ? 0.09534 0.24343 0.21449 -0.00834 0.05611  0.03558  220 GLN A CB    
1626 C CG    . GLN A 226 ? 0.13690 0.28424 0.22792 -0.02473 0.05913  0.02950  220 GLN A CG    
1627 C CD    . GLN A 226 ? 0.19499 0.30379 0.26915 -0.03699 0.06368  0.03466  220 GLN A CD    
1628 O OE1   . GLN A 226 ? 0.19441 0.30400 0.28714 -0.01263 0.06676  -0.00020 220 GLN A OE1   
1629 N NE2   . GLN A 226 ? 0.25914 0.33158 0.31659 -0.06570 0.09365  0.01843  220 GLN A NE2   
1630 N N     . VAL A 227 ? 0.07919 0.20896 0.27841 -0.02476 0.00236  -0.02665 221 VAL A N     
1631 C CA    . VAL A 227 ? 0.07767 0.21205 0.27766 -0.01721 0.00822  -0.01204 221 VAL A CA    
1632 C C     . VAL A 227 ? 0.08112 0.20885 0.27047 -0.00042 0.01089  -0.01099 221 VAL A C     
1633 O O     . VAL A 227 ? 0.08331 0.20989 0.26766 -0.00241 0.01882  -0.00616 221 VAL A O     
1634 C CB    . VAL A 227 ? 0.08269 0.20619 0.27407 -0.01191 0.04087  -0.00832 221 VAL A CB    
1635 C CG1   . VAL A 227 ? 0.09149 0.19662 0.29490 -0.01606 0.04570  0.01135  221 VAL A CG1   
1636 C CG2   . VAL A 227 ? 0.08279 0.19986 0.26266 -0.00240 0.02914  -0.05827 221 VAL A CG2   
1637 N N     . VAL A 228 ? 0.07231 0.19271 0.25053 0.00561  0.01076  -0.02723 222 VAL A N     
1638 C CA    . VAL A 228 ? 0.09335 0.19930 0.23156 0.00712  0.00523  -0.01479 222 VAL A CA    
1639 C C     . VAL A 228 ? 0.11802 0.19860 0.19353 -0.00655 0.02434  -0.00855 222 VAL A C     
1640 O O     . VAL A 228 ? 0.13666 0.19756 0.22410 -0.00602 0.01364  -0.01880 222 VAL A O     
1641 C CB    . VAL A 228 ? 0.11579 0.21431 0.23546 0.00670  0.00696  0.01380  222 VAL A CB    
1642 C CG1   . VAL A 228 ? 0.14134 0.21518 0.27166 0.00023  0.00542  0.00430  222 VAL A CG1   
1643 C CG2   . VAL A 228 ? 0.12992 0.22983 0.25379 -0.01363 0.02100  0.01172  222 VAL A CG2   
1644 N N     . GLN A 229 ? 0.12808 0.20177 0.21508 -0.01302 0.00591  -0.01853 223 GLN A N     
1645 C CA    . GLN A 229 ? 0.13996 0.18407 0.24292 -0.00711 -0.01541 0.02120  223 GLN A CA    
1646 C C     . GLN A 229 ? 0.16032 0.17987 0.26919 -0.01455 -0.01663 0.00363  223 GLN A C     
1647 O O     . GLN A 229 ? 0.17558 0.18876 0.28721 -0.00502 -0.03024 -0.00709 223 GLN A O     
1648 C CB    . GLN A 229 ? 0.15566 0.18117 0.22914 -0.00883 -0.02046 0.03476  223 GLN A CB    
1649 C CG    . GLN A 229 ? 0.16348 0.20736 0.28709 -0.00233 -0.00343 0.03052  223 GLN A CG    
1650 C CD    . GLN A 229 ? 0.18629 0.23134 0.32646 -0.01640 -0.00831 0.00604  223 GLN A CD    
1651 O OE1   . GLN A 229 ? 0.19541 0.25593 0.32395 -0.02961 0.00945  -0.01124 223 GLN A OE1   
1652 N NE2   . GLN A 229 ? 0.19611 0.22941 0.34278 -0.01221 -0.00968 0.02405  223 GLN A NE2   
1653 N N     . ALA A 230 ? 0.15747 0.17423 0.25779 -0.01843 -0.00701 0.00511  224 ALA A N     
1654 C CA    . ALA A 230 ? 0.13562 0.18460 0.24992 -0.01365 -0.02620 0.01243  224 ALA A CA    
1655 C C     . ALA A 230 ? 0.14750 0.18823 0.28204 -0.00856 -0.01757 0.00330  224 ALA A C     
1656 O O     . ALA A 230 ? 0.13265 0.18528 0.28744 -0.00799 0.00113  -0.00874 224 ALA A O     
1657 C CB    . ALA A 230 ? 0.13104 0.20295 0.23747 -0.00513 -0.01320 0.01750  224 ALA A CB    
1658 N N     . VAL A 231 ? 0.15528 0.16851 0.26609 -0.01251 -0.01615 -0.01877 225 VAL A N     
1659 C CA    . VAL A 231 ? 0.16954 0.17533 0.26061 -0.00923 -0.02219 0.01210  225 VAL A CA    
1660 C C     . VAL A 231 ? 0.15809 0.19889 0.24789 -0.01183 -0.01830 0.02072  225 VAL A C     
1661 O O     . VAL A 231 ? 0.16278 0.22741 0.26830 -0.02214 -0.04079 0.01874  225 VAL A O     
1662 C CB    . VAL A 231 ? 0.15541 0.15813 0.28505 0.00445  -0.01516 0.00523  225 VAL A CB    
1663 C CG1   . VAL A 231 ? 0.17478 0.17058 0.28368 -0.00974 -0.00537 0.00593  225 VAL A CG1   
1664 C CG2   . VAL A 231 ? 0.14669 0.15388 0.33017 0.00592  -0.00944 -0.02050 225 VAL A CG2   
1665 N N     . VAL A 232 ? 0.13990 0.20629 0.21270 0.00044  0.00748  0.03201  226 VAL A N     
1666 C CA    . VAL A 232 ? 0.13577 0.22462 0.27911 -0.00465 -0.00735 0.00907  226 VAL A CA    
1667 C C     . VAL A 232 ? 0.14719 0.24442 0.30144 -0.00301 -0.00559 -0.00061 226 VAL A C     
1668 O O     . VAL A 232 ? 0.14988 0.24198 0.30289 -0.01018 -0.00773 0.02401  226 VAL A O     
1669 C CB    . VAL A 232 ? 0.13412 0.23486 0.23895 0.00074  -0.01317 -0.01247 226 VAL A CB    
1670 C CG1   . VAL A 232 ? 0.16156 0.23987 0.30832 -0.01098 -0.00837 -0.02232 226 VAL A CG1   
1671 C CG2   . VAL A 232 ? 0.12673 0.25202 0.24867 -0.00051 0.02112  -0.01699 226 VAL A CG2   
1672 N N     . SER A 233 ? 0.13086 0.25038 0.31262 -0.00740 -0.01486 0.02359  227 SER A N     
1673 C CA    . SER A 233 ? 0.14088 0.29215 0.30980 -0.01221 -0.03150 0.03859  227 SER A CA    
1674 C C     . SER A 233 ? 0.15134 0.29054 0.31945 -0.00478 -0.04443 0.00522  227 SER A C     
1675 O O     . SER A 233 ? 0.17756 0.31319 0.34567 -0.01715 -0.08638 -0.01274 227 SER A O     
1676 C CB    . SER A 233 ? 0.17208 0.35208 0.39113 -0.00370 -0.04074 0.04857  227 SER A CB    
1677 O OG    . SER A 233 ? 0.25624 0.38874 0.50683 0.00425  0.00650  0.05847  227 SER A OG    
1678 N N     . ALA A 234 ? 0.14166 0.26446 0.26899 0.00546  -0.00227 -0.00027 228 ALA A N     
1679 C CA    . ALA A 234 ? 0.15048 0.25855 0.26452 0.00302  -0.01396 0.01400  228 ALA A CA    
1680 C C     . ALA A 234 ? 0.14369 0.25028 0.27043 -0.00085 -0.02404 0.00023  228 ALA A C     
1681 O O     . ALA A 234 ? 0.18261 0.25620 0.29251 -0.00238 -0.02891 0.02381  228 ALA A O     
1682 C CB    . ALA A 234 ? 0.17681 0.24018 0.33466 0.01647  0.00831  0.03870  228 ALA A CB    
1683 N N     . ILE A 235 ? 0.12342 0.24432 0.29315 -0.01054 -0.00435 -0.03193 229 ILE A N     
1684 C CA    . ILE A 235 ? 0.12078 0.22498 0.23212 -0.01225 -0.00290 -0.04808 229 ILE A CA    
1685 C C     . ILE A 235 ? 0.14017 0.22515 0.26022 -0.00109 -0.03021 -0.03545 229 ILE A C     
1686 O O     . ILE A 235 ? 0.17592 0.22238 0.29765 -0.00559 -0.04088 -0.01588 229 ILE A O     
1687 C CB    . ILE A 235 ? 0.12660 0.20745 0.28428 0.00159  -0.01732 -0.05577 229 ILE A CB    
1688 C CG1   . ILE A 235 ? 0.14705 0.22079 0.29629 -0.01076 -0.04598 -0.03445 229 ILE A CG1   
1689 C CG2   . ILE A 235 ? 0.13559 0.21207 0.31615 0.01227  -0.00134 -0.03793 229 ILE A CG2   
1690 C CD1   . ILE A 235 ? 0.15275 0.23920 0.34227 -0.00591 -0.05667 -0.01607 229 ILE A CD1   
1691 N N     . GLY A 236 ? 0.12467 0.22488 0.25102 0.02634  -0.02559 -0.04272 230 GLY A N     
1692 C CA    . GLY A 236 ? 0.11359 0.21645 0.26987 0.02575  -0.02722 -0.02301 230 GLY A CA    
1693 C C     . GLY A 236 ? 0.11976 0.20426 0.24323 0.00451  -0.02120 -0.01909 230 GLY A C     
1694 O O     . GLY A 236 ? 0.14215 0.20877 0.30552 -0.00247 -0.04672 -0.03174 230 GLY A O     
1695 N N     . ALA A 237 ? 0.11595 0.19834 0.22919 0.02957  -0.01730 -0.00160 231 ALA A N     
1696 C CA    . ALA A 237 ? 0.13805 0.20606 0.25886 0.00574  0.01071  0.02237  231 ALA A CA    
1697 C C     . ALA A 237 ? 0.12294 0.19819 0.22385 0.00685  -0.02182 -0.00974 231 ALA A C     
1698 O O     . ALA A 237 ? 0.12044 0.17691 0.24824 0.01235  -0.06257 -0.00729 231 ALA A O     
1699 C CB    . ALA A 237 ? 0.15475 0.21171 0.24744 0.02108  0.03763  0.00892  231 ALA A CB    
1700 N N     . ASP A 238 ? 0.15220 0.21904 0.22319 -0.00801 0.02081  -0.00079 232 ASP A N     
1701 C CA    . ASP A 238 ? 0.18804 0.25691 0.21276 -0.02179 0.02863  -0.01518 232 ASP A CA    
1702 C C     . ASP A 238 ? 0.17464 0.22867 0.22195 -0.01113 0.03062  -0.00145 232 ASP A C     
1703 O O     . ASP A 238 ? 0.15506 0.22815 0.25215 -0.02639 0.01889  -0.00222 232 ASP A O     
1704 C CB    . ASP A 238 ? 0.24484 0.33480 0.27228 -0.01896 -0.00956 -0.03985 232 ASP A CB    
1705 C CG    . ASP A 238 ? 0.31434 0.40987 0.34133 -0.01947 -0.03646 -0.07554 232 ASP A CG    
1706 O OD1   . ASP A 238 ? 0.34610 0.43872 0.37273 -0.01471 -0.06858 -0.07557 232 ASP A OD1   
1707 O OD2   . ASP A 238 ? 0.34973 0.44231 0.45832 -0.01449 -0.03610 -0.06220 232 ASP A OD2   
1708 N N     . ARG A 239 ? 0.16811 0.21548 0.21807 -0.02241 -0.02870 0.01396  233 ARG A N     
1709 C CA    A ARG A 239 ? 0.14152 0.20140 0.17512 -0.01288 -0.05656 0.01816  233 ARG A CA    
1710 C CA    B ARG A 239 ? 0.14603 0.19708 0.16593 -0.02056 -0.05724 0.02147  233 ARG A CA    
1711 C C     . ARG A 239 ? 0.13983 0.20485 0.18301 -0.01304 -0.04426 0.01149  233 ARG A C     
1712 O O     . ARG A 239 ? 0.13144 0.18618 0.18986 -0.00916 -0.01195 -0.02459 233 ARG A O     
1713 C CB    A ARG A 239 ? 0.13225 0.22367 0.20686 0.00019  -0.06744 0.02600  233 ARG A CB    
1714 C CB    B ARG A 239 ? 0.14388 0.20829 0.17507 -0.02113 -0.07164 0.03518  233 ARG A CB    
1715 C CG    A ARG A 239 ? 0.14109 0.23553 0.23740 0.01115  -0.06934 0.03780  233 ARG A CG    
1716 C CG    B ARG A 239 ? 0.15738 0.20825 0.17859 -0.02096 -0.08078 0.05792  233 ARG A CG    
1717 C CD    A ARG A 239 ? 0.14113 0.25721 0.29156 0.01331  -0.08171 0.02638  233 ARG A CD    
1718 C CD    B ARG A 239 ? 0.16898 0.22133 0.23373 -0.02563 -0.07778 0.04971  233 ARG A CD    
1719 N NE    A ARG A 239 ? 0.13339 0.26990 0.29454 0.00826  -0.08561 0.00680  233 ARG A NE    
1720 N NE    B ARG A 239 ? 0.16790 0.21989 0.21654 -0.04425 -0.06801 0.04466  233 ARG A NE    
1721 C CZ    A ARG A 239 ? 0.14741 0.28216 0.26620 -0.00981 -0.07398 -0.00165 233 ARG A CZ    
1722 C CZ    B ARG A 239 ? 0.17158 0.21406 0.20686 -0.05517 -0.06280 0.01773  233 ARG A CZ    
1723 N NH1   A ARG A 239 ? 0.16751 0.28422 0.29035 -0.01693 -0.02224 -0.02514 233 ARG A NH1   
1724 N NH1   B ARG A 239 ? 0.14282 0.17931 0.15273 -0.06558 -0.06013 -0.00108 233 ARG A NH1   
1725 N NH2   A ARG A 239 ? 0.12244 0.28285 0.21799 -0.02097 -0.07439 -0.03049 233 ARG A NH2   
1726 N NH2   B ARG A 239 ? 0.19290 0.22507 0.25996 -0.06639 -0.05268 -0.00221 233 ARG A NH2   
1727 N N     . VAL A 240 ? 0.14143 0.20040 0.22505 0.00243  -0.03097 0.02133  234 VAL A N     
1728 C CA    . VAL A 240 ? 0.12346 0.19726 0.22611 0.01317  -0.05682 0.02703  234 VAL A CA    
1729 C C     . VAL A 240 ? 0.12647 0.20248 0.23805 0.00418  -0.05268 -0.00616 234 VAL A C     
1730 O O     . VAL A 240 ? 0.13945 0.21280 0.23739 -0.00236 -0.04021 -0.02685 234 VAL A O     
1731 C CB    . VAL A 240 ? 0.09179 0.18718 0.22676 0.02840  -0.05343 0.01893  234 VAL A CB    
1732 C CG1   . VAL A 240 ? 0.09583 0.19987 0.26344 -0.01449 -0.01258 0.00897  234 VAL A CG1   
1733 C CG2   . VAL A 240 ? 0.09159 0.17203 0.21377 0.03394  -0.05412 0.00076  234 VAL A CG2   
1734 N N     . GLY A 241 ? 0.09616 0.22166 0.18311 0.00340  -0.04969 0.01203  235 GLY A N     
1735 C CA    . GLY A 241 ? 0.10657 0.21938 0.15675 -0.00315 -0.05821 0.04427  235 GLY A CA    
1736 C C     . GLY A 241 ? 0.11431 0.21087 0.16442 -0.00773 -0.02717 0.00782  235 GLY A C     
1737 O O     . GLY A 241 ? 0.11976 0.19033 0.20944 -0.00372 -0.00082 -0.02375 235 GLY A O     
1738 N N     . VAL A 242 ? 0.09851 0.21127 0.16549 -0.01886 -0.01764 0.02321  236 VAL A N     
1739 C CA    . VAL A 242 ? 0.09878 0.20844 0.18029 -0.01312 -0.00518 0.01271  236 VAL A CA    
1740 C C     . VAL A 242 ? 0.10902 0.20554 0.16795 -0.02377 -0.01332 -0.00575 236 VAL A C     
1741 O O     . VAL A 242 ? 0.11772 0.21950 0.25995 -0.03554 0.00791  0.00533  236 VAL A O     
1742 C CB    . VAL A 242 ? 0.09944 0.20740 0.17375 -0.01614 -0.04993 0.03167  236 VAL A CB    
1743 C CG1   . VAL A 242 ? 0.12552 0.23004 0.17465 -0.02052 -0.02123 0.05118  236 VAL A CG1   
1744 C CG2   . VAL A 242 ? 0.08831 0.22345 0.21396 -0.01542 -0.06021 0.00185  236 VAL A CG2   
1745 N N     . ARG A 243 ? 0.10601 0.18546 0.19090 -0.01403 -0.01425 -0.00432 237 ARG A N     
1746 C CA    . ARG A 243 ? 0.09905 0.17910 0.23087 -0.00158 -0.02405 0.03442  237 ARG A CA    
1747 C C     . ARG A 243 ? 0.12043 0.19464 0.19821 0.00755  -0.02505 -0.00143 237 ARG A C     
1748 O O     . ARG A 243 ? 0.14007 0.20938 0.19787 -0.01033 -0.00451 -0.00252 237 ARG A O     
1749 C CB    . ARG A 243 ? 0.08983 0.17442 0.24609 -0.00466 -0.01178 0.03101  237 ARG A CB    
1750 C CG    . ARG A 243 ? 0.08635 0.18223 0.32902 0.00598  0.00295  0.02573  237 ARG A CG    
1751 C CD    . ARG A 243 ? 0.09632 0.19938 0.35568 0.00941  0.02662  0.02421  237 ARG A CD    
1752 N NE    . ARG A 243 ? 0.10891 0.22911 0.39462 0.00163  0.03959  0.02496  237 ARG A NE    
1753 C CZ    . ARG A 243 ? 0.11723 0.23105 0.37757 0.01945  0.01858  0.01214  237 ARG A CZ    
1754 N NH1   . ARG A 243 ? 0.12369 0.19119 0.31757 0.01701  0.00322  0.01576  237 ARG A NH1   
1755 N NH2   . ARG A 243 ? 0.13450 0.25682 0.37811 0.02978  0.03692  -0.01809 237 ARG A NH2   
1756 N N     . VAL A 244 ? 0.12457 0.18175 0.23529 -0.01495 -0.02797 0.02737  238 VAL A N     
1757 C CA    . VAL A 244 ? 0.10259 0.16322 0.25917 -0.01496 -0.05071 0.02856  238 VAL A CA    
1758 C C     . VAL A 244 ? 0.11592 0.18040 0.24356 0.00089  -0.04238 0.00657  238 VAL A C     
1759 O O     . VAL A 244 ? 0.12774 0.19651 0.26483 0.01316  -0.00791 -0.01526 238 VAL A O     
1760 C CB    . VAL A 244 ? 0.10006 0.13944 0.30692 0.00991  -0.00749 0.02281  238 VAL A CB    
1761 C CG1   . VAL A 244 ? 0.11168 0.14084 0.29085 0.03682  -0.01491 0.04828  238 VAL A CG1   
1762 C CG2   . VAL A 244 ? 0.12583 0.15895 0.34616 -0.00574 0.00442  0.01600  238 VAL A CG2   
1763 N N     . SER A 245 ? 0.12450 0.18870 0.20403 0.02945  -0.01575 0.00975  239 SER A N     
1764 C CA    . SER A 245 ? 0.14001 0.18682 0.19561 0.01184  -0.04784 0.00047  239 SER A CA    
1765 C C     . SER A 245 ? 0.16989 0.20852 0.23273 0.02232  -0.04134 0.00402  239 SER A C     
1766 O O     . SER A 245 ? 0.16723 0.22392 0.25086 0.02618  -0.04329 0.00940  239 SER A O     
1767 C CB    . SER A 245 ? 0.14704 0.17191 0.22482 0.01863  0.00021  -0.02376 239 SER A CB    
1768 O OG    . SER A 245 ? 0.15735 0.19372 0.26917 0.01807  -0.02796 -0.01513 239 SER A OG    
1769 N N     . PRO A 246 ? 0.19646 0.20406 0.24461 0.00471  -0.02668 0.01220  240 PRO A N     
1770 C CA    . PRO A 246 ? 0.20714 0.21175 0.23552 0.00275  -0.03587 0.01172  240 PRO A CA    
1771 C C     . PRO A 246 ? 0.20227 0.24133 0.26301 0.03764  -0.00064 0.03445  240 PRO A C     
1772 O O     . PRO A 246 ? 0.21823 0.27889 0.26324 0.03150  -0.00031 0.02596  240 PRO A O     
1773 C CB    . PRO A 246 ? 0.23237 0.21956 0.26643 -0.00481 -0.04193 0.00651  240 PRO A CB    
1774 C CG    . PRO A 246 ? 0.23616 0.22471 0.26919 -0.00199 -0.01326 0.01370  240 PRO A CG    
1775 C CD    . PRO A 246 ? 0.21941 0.20563 0.25955 -0.01440 -0.01667 0.02476  240 PRO A CD    
1776 N N     . ALA A 247 ? 0.19242 0.24508 0.30324 0.05551  0.00342  0.00994  241 ALA A N     
1777 C CA    . ALA A 247 ? 0.21318 0.28037 0.30417 0.06293  -0.00997 0.01435  241 ALA A CA    
1778 C C     . ALA A 247 ? 0.23202 0.30599 0.31199 0.04992  -0.02905 0.01176  241 ALA A C     
1779 O O     . ALA A 247 ? 0.25229 0.32369 0.33654 0.02239  -0.03769 0.00185  241 ALA A O     
1780 C CB    . ALA A 247 ? 0.21751 0.29589 0.33302 0.07440  0.01794  0.01792  241 ALA A CB    
1781 N N     . ILE A 248 ? 0.22718 0.31460 0.32122 0.04132  -0.01266 0.02361  242 ILE A N     
1782 C CA    . ILE A 248 ? 0.23707 0.31444 0.29272 0.02259  -0.00284 0.01742  242 ILE A CA    
1783 C C     . ILE A 248 ? 0.24347 0.32669 0.25588 0.01453  -0.01817 -0.00553 242 ILE A C     
1784 O O     . ILE A 248 ? 0.24568 0.34083 0.25993 0.02705  -0.01303 -0.00644 242 ILE A O     
1785 C CB    . ILE A 248 ? 0.25207 0.31874 0.27653 0.01529  0.00926  0.02837  242 ILE A CB    
1786 C CG1   . ILE A 248 ? 0.28752 0.31857 0.30015 0.01089  0.00478  0.03764  242 ILE A CG1   
1787 C CG2   . ILE A 248 ? 0.24037 0.31759 0.27688 0.02524  0.03203  0.01070  242 ILE A CG2   
1788 C CD1   . ILE A 248 ? 0.30734 0.31687 0.36887 -0.01488 -0.00086 0.01930  242 ILE A CD1   
1789 N N     . ASP A 249 ? 0.25415 0.32574 0.32549 0.01412  -0.04248 0.00914  243 ASP A N     
1790 C CA    . ASP A 249 ? 0.28020 0.32225 0.30364 0.02860  -0.02863 -0.00629 243 ASP A CA    
1791 C C     . ASP A 249 ? 0.30155 0.31897 0.32731 0.01482  -0.00554 -0.05706 243 ASP A C     
1792 O O     . ASP A 249 ? 0.32107 0.34737 0.43450 0.00426  0.02355  -0.07394 243 ASP A O     
1793 C CB    . ASP A 249 ? 0.29372 0.33192 0.31856 0.05557  -0.04107 0.02064  243 ASP A CB    
1794 N N     . HIS A 250 ? 0.27703 0.27987 0.25211 0.01736  0.03617  -0.03951 244 HIS A N     
1795 C CA    . HIS A 250 ? 0.24801 0.26821 0.26224 0.00772  0.03686  0.00292  244 HIS A CA    
1796 C C     . HIS A 250 ? 0.21017 0.24451 0.27266 0.00090  0.01736  -0.01563 244 HIS A C     
1797 O O     . HIS A 250 ? 0.19653 0.22795 0.33594 -0.01374 -0.00122 -0.01167 244 HIS A O     
1798 C CB    . HIS A 250 ? 0.26933 0.27293 0.26234 -0.00752 0.01833  0.03426  244 HIS A CB    
1799 C CG    . HIS A 250 ? 0.28683 0.27205 0.30049 -0.01715 0.02157  0.01003  244 HIS A CG    
1800 N ND1   . HIS A 250 ? 0.28981 0.28806 0.39884 -0.02119 -0.00142 0.01898  244 HIS A ND1   
1801 C CD2   . HIS A 250 ? 0.28216 0.26420 0.27713 -0.01106 0.04146  0.00538  244 HIS A CD2   
1802 C CE1   . HIS A 250 ? 0.28955 0.27308 0.37497 -0.01696 -0.00521 0.02888  244 HIS A CE1   
1803 N NE2   . HIS A 250 ? 0.30107 0.27975 0.34948 -0.00782 0.02014  0.01870  244 HIS A NE2   
1804 N N     . LEU A 251 ? 0.17803 0.23359 0.25101 0.00963  0.03351  -0.00138 245 LEU A N     
1805 C CA    . LEU A 251 ? 0.15799 0.22525 0.19997 0.01402  -0.00407 0.00555  245 LEU A CA    
1806 C C     . LEU A 251 ? 0.15980 0.26409 0.21494 0.00422  -0.02667 0.00398  245 LEU A C     
1807 O O     . LEU A 251 ? 0.16439 0.26834 0.21793 0.00595  -0.04088 0.00679  245 LEU A O     
1808 C CB    . LEU A 251 ? 0.15354 0.21418 0.23121 0.00495  0.00784  0.00480  245 LEU A CB    
1809 C CG    . LEU A 251 ? 0.16806 0.21504 0.23884 -0.01280 0.00317  0.00816  245 LEU A CG    
1810 C CD1   . LEU A 251 ? 0.17508 0.21119 0.29734 -0.00421 -0.01669 0.01658  245 LEU A CD1   
1811 C CD2   . LEU A 251 ? 0.17386 0.22637 0.25415 -0.04405 -0.02272 0.01991  245 LEU A CD2   
1812 N N     . ASP A 252 ? 0.16109 0.28610 0.18716 -0.00010 -0.05388 0.01690  246 ASP A N     
1813 C CA    . ASP A 252 ? 0.18485 0.30411 0.23902 -0.02476 -0.04009 -0.00581 246 ASP A CA    
1814 C C     . ASP A 252 ? 0.20578 0.31506 0.27919 -0.06400 -0.02142 0.00972  246 ASP A C     
1815 O O     . ASP A 252 ? 0.25058 0.35973 0.30960 -0.09278 -0.00742 -0.00121 246 ASP A O     
1816 C CB    . ASP A 252 ? 0.20399 0.31772 0.27686 -0.00432 -0.06715 -0.00110 246 ASP A CB    
1817 C CG    . ASP A 252 ? 0.24118 0.31208 0.31709 0.00700  -0.04542 -0.03670 246 ASP A CG    
1818 O OD1   . ASP A 252 ? 0.25827 0.31438 0.30493 0.00910  -0.04547 -0.04733 246 ASP A OD1   
1819 O OD2   . ASP A 252 ? 0.26306 0.31818 0.34523 0.00971  -0.03895 -0.01912 246 ASP A OD2   
1820 N N     . ALA A 253 ? 0.20750 0.28767 0.29113 -0.06139 -0.03915 0.00571  247 ALA A N     
1821 C CA    . ALA A 253 ? 0.23705 0.29361 0.28059 -0.04283 -0.04910 -0.00605 247 ALA A CA    
1822 C C     . ALA A 253 ? 0.24664 0.28693 0.30742 -0.02049 -0.04425 -0.00082 247 ALA A C     
1823 O O     . ALA A 253 ? 0.27701 0.31234 0.33050 -0.01917 -0.01042 -0.01120 247 ALA A O     
1824 C CB    . ALA A 253 ? 0.25337 0.30636 0.28623 -0.05747 -0.03916 0.00846  247 ALA A CB    
1825 N N     . MET A 254 ? 0.23232 0.25949 0.31001 -0.00021 -0.07110 0.00693  248 MET A N     
1826 C CA    . MET A 254 ? 0.24486 0.26307 0.33688 0.01535  -0.08618 0.03238  248 MET A CA    
1827 C C     . MET A 254 ? 0.21707 0.26565 0.31439 0.01665  -0.04558 0.02085  248 MET A C     
1828 O O     . MET A 254 ? 0.20925 0.28239 0.26402 0.02678  0.00166  0.02565  248 MET A O     
1829 C CB    . MET A 254 ? 0.29423 0.29854 0.44284 0.02316  -0.11948 0.03314  248 MET A CB    
1830 N N     . ASP A 255 ? 0.21553 0.24780 0.35546 0.00115  -0.03288 0.02227  249 ASP A N     
1831 C CA    . ASP A 255 ? 0.23447 0.25895 0.38656 -0.00535 -0.06451 0.00557  249 ASP A CA    
1832 C C     . ASP A 255 ? 0.23222 0.25664 0.38037 -0.00284 -0.07265 0.00613  249 ASP A C     
1833 O O     . ASP A 255 ? 0.21379 0.25652 0.42115 -0.00633 -0.08598 -0.00658 249 ASP A O     
1834 C CB    . ASP A 255 ? 0.26155 0.27679 0.38273 0.00118  -0.06458 -0.00959 249 ASP A CB    
1835 C CG    . ASP A 255 ? 0.29829 0.30081 0.41920 0.02727  -0.06342 -0.00462 249 ASP A CG    
1836 O OD1   . ASP A 255 ? 0.31302 0.30964 0.46146 0.05305  -0.02967 -0.02361 249 ASP A OD1   
1837 O OD2   . ASP A 255 ? 0.29421 0.30182 0.38955 0.02671  -0.02783 -0.00306 249 ASP A OD2   
1838 N N     . SER A 256 ? 0.25660 0.26031 0.32440 0.00813  -0.05976 -0.00058 250 SER A N     
1839 C CA    . SER A 256 ? 0.27933 0.25665 0.31463 0.00933  -0.05917 0.02600  250 SER A CA    
1840 C C     . SER A 256 ? 0.28484 0.26192 0.30185 0.01493  -0.08923 0.02377  250 SER A C     
1841 O O     . SER A 256 ? 0.30170 0.29170 0.36057 0.03505  -0.11011 0.02276  250 SER A O     
1842 C CB    . SER A 256 ? 0.29043 0.27051 0.34109 -0.00850 -0.03726 0.03160  250 SER A CB    
1843 O OG    . SER A 256 ? 0.31230 0.27531 0.37038 -0.02398 -0.03172 -0.00017 250 SER A OG    
1844 N N     . ASN A 257 ? 0.29171 0.25101 0.27761 -0.00031 -0.05887 -0.01525 251 ASN A N     
1845 C CA    . ASN A 257 ? 0.26691 0.24488 0.24646 0.00925  -0.07081 -0.01443 251 ASN A CA    
1846 C C     . ASN A 257 ? 0.21789 0.23646 0.24958 0.02523  -0.06923 -0.01723 251 ASN A C     
1847 O O     . ASN A 257 ? 0.19170 0.23611 0.26510 0.01789  -0.04875 -0.00562 251 ASN A O     
1848 C CB    . ASN A 257 ? 0.30344 0.24272 0.28731 0.00576  -0.06408 -0.01618 251 ASN A CB    
1849 C CG    . ASN A 257 ? 0.34469 0.26624 0.35553 -0.01554 -0.05455 0.00665  251 ASN A CG    
1850 O OD1   . ASN A 257 ? 0.33919 0.26498 0.34612 -0.03772 -0.05720 0.03087  251 ASN A OD1   
1851 N ND2   . ASN A 257 ? 0.38478 0.28066 0.42836 -0.01583 -0.03685 0.00288  251 ASN A ND2   
1852 N N     . PRO A 258 ? 0.18102 0.25106 0.29016 0.01911  -0.06274 0.00017  252 PRO A N     
1853 C CA    . PRO A 258 ? 0.16499 0.23858 0.31422 0.01138  -0.06156 0.01204  252 PRO A CA    
1854 C C     . PRO A 258 ? 0.15767 0.19563 0.29932 0.01885  -0.04609 -0.00094 252 PRO A C     
1855 O O     . PRO A 258 ? 0.15086 0.18312 0.33168 0.01042  -0.02768 -0.00738 252 PRO A O     
1856 C CB    . PRO A 258 ? 0.18036 0.25306 0.32675 -0.00454 -0.07095 -0.00752 252 PRO A CB    
1857 C CG    . PRO A 258 ? 0.20666 0.26713 0.34488 -0.00317 -0.05467 -0.02043 252 PRO A CG    
1858 C CD    . PRO A 258 ? 0.21404 0.27796 0.33810 0.00922  -0.06019 -0.00773 252 PRO A CD    
1859 N N     . LEU A 259 ? 0.16561 0.17376 0.27719 0.01586  -0.02849 -0.01705 253 LEU A N     
1860 C CA    . LEU A 259 ? 0.13822 0.17279 0.27540 0.00995  0.00506  -0.01665 253 LEU A CA    
1861 C C     . LEU A 259 ? 0.13975 0.19724 0.26038 0.00602  0.00570  -0.02020 253 LEU A C     
1862 O O     . LEU A 259 ? 0.12914 0.24299 0.25548 0.01637  -0.03046 -0.02310 253 LEU A O     
1863 C CB    . LEU A 259 ? 0.14931 0.18807 0.36772 0.02056  0.02044  0.01061  253 LEU A CB    
1864 C CG    . LEU A 259 ? 0.16070 0.17046 0.42948 0.03614  0.04768  0.03227  253 LEU A CG    
1865 C CD1   . LEU A 259 ? 0.15142 0.17448 0.46310 0.02195  0.07011  0.05239  253 LEU A CD1   
1866 C CD2   . LEU A 259 ? 0.17928 0.16291 0.47260 0.04580  0.03900  0.04691  253 LEU A CD2   
1867 N N     . SER A 260 ? 0.15866 0.18797 0.29283 0.00248  0.02771  0.01272  254 SER A N     
1868 C CA    . SER A 260 ? 0.17680 0.18613 0.29845 0.02468  0.04986  0.05393  254 SER A CA    
1869 C C     . SER A 260 ? 0.15870 0.19096 0.31125 0.01832  0.01292  0.03580  254 SER A C     
1870 O O     . SER A 260 ? 0.15378 0.20133 0.33171 0.01817  0.00872  0.02099  254 SER A O     
1871 C CB    . SER A 260 ? 0.25041 0.19727 0.34922 0.05514  0.01852  0.08194  254 SER A CB    
1872 O OG    . SER A 260 ? 0.28958 0.23808 0.42053 0.02223  0.03477  0.04981  254 SER A OG    
1873 N N     . LEU A 261 ? 0.13778 0.18082 0.27301 0.01830  0.00673  0.04405  255 LEU A N     
1874 C CA    . LEU A 261 ? 0.14109 0.17563 0.25038 0.02847  0.00817  0.04240  255 LEU A CA    
1875 C C     . LEU A 261 ? 0.13719 0.18732 0.26053 0.00797  0.02201  0.01460  255 LEU A C     
1876 O O     . LEU A 261 ? 0.13519 0.19434 0.27215 0.00649  0.02203  0.01500  255 LEU A O     
1877 C CB    . LEU A 261 ? 0.14153 0.17389 0.25046 0.03899  -0.00443 0.01487  255 LEU A CB    
1878 C CG    . LEU A 261 ? 0.13088 0.18982 0.32342 0.03529  -0.03054 0.00393  255 LEU A CG    
1879 C CD1   . LEU A 261 ? 0.14067 0.20838 0.36226 0.04168  -0.01060 0.01247  255 LEU A CD1   
1880 C CD2   . LEU A 261 ? 0.14270 0.19648 0.29807 0.01700  -0.07091 -0.04171 255 LEU A CD2   
1881 N N     . GLY A 262 ? 0.13813 0.17666 0.25604 0.00660  0.03031  -0.01947 256 GLY A N     
1882 C CA    . GLY A 262 ? 0.13733 0.18014 0.27714 -0.00591 -0.00979 0.00423  256 GLY A CA    
1883 C C     . GLY A 262 ? 0.11736 0.18828 0.27090 0.00163  0.00580  -0.00423 256 GLY A C     
1884 O O     . GLY A 262 ? 0.10401 0.18982 0.31735 0.00500  0.01467  0.02158  256 GLY A O     
1885 N N     . LEU A 263 ? 0.11325 0.18501 0.26488 -0.01022 -0.00182 -0.00647 257 LEU A N     
1886 C CA    . LEU A 263 ? 0.12845 0.19666 0.27869 -0.00210 -0.00073 0.00122  257 LEU A CA    
1887 C C     . LEU A 263 ? 0.13180 0.20155 0.26737 0.01195  0.01921  -0.00375 257 LEU A C     
1888 O O     . LEU A 263 ? 0.14036 0.21227 0.25959 0.01152  0.04878  -0.02454 257 LEU A O     
1889 C CB    . LEU A 263 ? 0.12454 0.18601 0.24267 0.00745  0.02429  -0.00592 257 LEU A CB    
1890 C CG    . LEU A 263 ? 0.14222 0.19850 0.20816 0.01807  0.01386  -0.01322 257 LEU A CG    
1891 C CD1   . LEU A 263 ? 0.15181 0.21277 0.20592 0.02423  0.02059  0.03745  257 LEU A CD1   
1892 C CD2   . LEU A 263 ? 0.15935 0.22268 0.23782 0.01797  -0.00050 -0.00026 257 LEU A CD2   
1893 N N     . ALA A 264 ? 0.13019 0.20070 0.25491 0.00743  0.02913  0.00344  258 ALA A N     
1894 C CA    . ALA A 264 ? 0.13773 0.21338 0.25136 0.00401  0.02058  0.01362  258 ALA A CA    
1895 C C     . ALA A 264 ? 0.12468 0.22109 0.23549 -0.00216 0.01334  0.01827  258 ALA A C     
1896 O O     . ALA A 264 ? 0.10132 0.24139 0.25402 0.00077  -0.00425 0.03123  258 ALA A O     
1897 C CB    . ALA A 264 ? 0.15312 0.22133 0.21436 -0.00091 0.00913  0.02032  258 ALA A CB    
1898 N N     . VAL A 265 ? 0.12420 0.19683 0.20487 -0.00772 0.03342  0.00439  259 VAL A N     
1899 C CA    . VAL A 265 ? 0.14380 0.19618 0.21151 -0.00073 0.00283  -0.00014 259 VAL A CA    
1900 C C     . VAL A 265 ? 0.13407 0.20391 0.19786 0.00370  0.01821  0.00047  259 VAL A C     
1901 O O     . VAL A 265 ? 0.11233 0.19537 0.25758 0.01004  -0.00170 -0.00492 259 VAL A O     
1902 C CB    . VAL A 265 ? 0.18090 0.18766 0.21350 0.00897  -0.01096 -0.00632 259 VAL A CB    
1903 C CG1   . VAL A 265 ? 0.19049 0.16692 0.20821 0.00953  0.00376  -0.00243 259 VAL A CG1   
1904 C CG2   . VAL A 265 ? 0.19752 0.19243 0.17023 0.01792  -0.00459 0.01055  259 VAL A CG2   
1905 N N     . VAL A 266 ? 0.14006 0.21286 0.19350 -0.00805 0.03984  0.00125  260 VAL A N     
1906 C CA    . VAL A 266 ? 0.14371 0.19926 0.28264 -0.01616 0.03832  -0.03786 260 VAL A CA    
1907 C C     . VAL A 266 ? 0.16168 0.18344 0.29053 -0.00645 0.03186  -0.02549 260 VAL A C     
1908 O O     . VAL A 266 ? 0.16034 0.17363 0.27217 0.02045  0.05184  0.02415  260 VAL A O     
1909 C CB    . VAL A 266 ? 0.15461 0.21815 0.30832 -0.01951 0.00303  -0.03495 260 VAL A CB    
1910 C CG1   . VAL A 266 ? 0.14964 0.20643 0.32431 0.00381  0.00594  -0.04315 260 VAL A CG1   
1911 C CG2   . VAL A 266 ? 0.16422 0.23354 0.26650 -0.02865 -0.01804 -0.01230 260 VAL A CG2   
1912 N N     . GLU A 267 ? 0.15720 0.18124 0.25890 -0.02929 0.02211  -0.00392 261 GLU A N     
1913 C CA    . GLU A 267 ? 0.16436 0.21172 0.31784 -0.01743 -0.00326 0.05907  261 GLU A CA    
1914 C C     . GLU A 267 ? 0.14568 0.22933 0.32118 -0.02551 -0.00209 0.04004  261 GLU A C     
1915 O O     . GLU A 267 ? 0.13041 0.24853 0.33676 -0.03233 -0.01397 0.03488  261 GLU A O     
1916 C CB    . GLU A 267 ? 0.22508 0.25816 0.43796 -0.03244 -0.02148 0.06088  261 GLU A CB    
1917 C CG    . GLU A 267 ? 0.29307 0.31588 0.57387 -0.00958 -0.01701 0.07686  261 GLU A CG    
1918 C CD    . GLU A 267 ? 0.36588 0.37418 0.72550 0.02137  -0.03172 0.06408  261 GLU A CD    
1919 O OE1   . GLU A 267 ? 0.39729 0.39895 0.80674 0.03648  -0.04035 0.04465  261 GLU A OE1   
1920 O OE2   . GLU A 267 ? 0.39378 0.39713 0.74587 0.01771  -0.05896 0.09035  261 GLU A OE2   
1921 N N     . ARG A 268 ? 0.13988 0.24065 0.28886 -0.00419 0.00452  0.04943  262 ARG A N     
1922 C CA    . ARG A 268 ? 0.14157 0.24066 0.26503 -0.00610 0.00327  0.01737  262 ARG A CA    
1923 C C     . ARG A 268 ? 0.14332 0.21415 0.20337 -0.02239 0.00524  -0.00836 262 ARG A C     
1924 O O     . ARG A 268 ? 0.19277 0.21713 0.24085 0.00487  -0.00117 0.00060  262 ARG A O     
1925 C CB    . ARG A 268 ? 0.17840 0.28005 0.29625 0.00370  0.02746  0.04359  262 ARG A CB    
1926 C CG    . ARG A 268 ? 0.24799 0.32728 0.30348 0.01812  0.02371  0.03791  262 ARG A CG    
1927 C CD    . ARG A 268 ? 0.28751 0.36203 0.44364 0.02582  0.03549  0.06198  262 ARG A CD    
1928 N NE    . ARG A 268 ? 0.30122 0.36565 0.47235 0.00455  0.07097  0.09368  262 ARG A NE    
1929 C CZ    . ARG A 268 ? 0.31609 0.37385 0.46933 -0.01645 0.08839  0.11992  262 ARG A CZ    
1930 N NH1   . ARG A 268 ? 0.29188 0.35920 0.45143 -0.02248 0.08077  0.14720  262 ARG A NH1   
1931 N NH2   . ARG A 268 ? 0.35217 0.39337 0.46282 -0.00733 0.09161  0.08864  262 ARG A NH2   
1932 N N     . LEU A 269 ? 0.14540 0.20182 0.21181 -0.04854 0.02024  0.01639  263 LEU A N     
1933 C CA    . LEU A 269 ? 0.11617 0.19739 0.23501 -0.03875 0.00790  -0.00437 263 LEU A CA    
1934 C C     . LEU A 269 ? 0.10909 0.19573 0.24309 -0.02019 0.00777  -0.01304 263 LEU A C     
1935 O O     . LEU A 269 ? 0.09742 0.21304 0.30087 -0.03131 -0.01642 -0.04242 263 LEU A O     
1936 C CB    . LEU A 269 ? 0.10920 0.18886 0.27535 -0.03228 0.01675  0.00181  263 LEU A CB    
1937 C CG    . LEU A 269 ? 0.08982 0.19888 0.28710 -0.01726 0.00208  0.01981  263 LEU A CG    
1938 C CD1   . LEU A 269 ? 0.08845 0.21855 0.28821 -0.00441 0.01252  0.03224  263 LEU A CD1   
1939 C CD2   . LEU A 269 ? 0.08338 0.21348 0.28628 -0.01865 0.00173  -0.02328 263 LEU A CD2   
1940 N N     . ASN A 270 ? 0.11248 0.17310 0.23938 -0.01667 -0.00765 -0.01645 264 ASN A N     
1941 C CA    . ASN A 270 ? 0.10487 0.17784 0.24929 -0.00128 -0.00803 -0.01269 264 ASN A CA    
1942 C C     . ASN A 270 ? 0.12136 0.21678 0.27505 -0.01198 0.00355  -0.00356 264 ASN A C     
1943 O O     . ASN A 270 ? 0.11889 0.25310 0.24054 -0.02119 0.01936  0.00042  264 ASN A O     
1944 C CB    . ASN A 270 ? 0.09741 0.16967 0.29376 0.03240  0.01877  -0.03816 264 ASN A CB    
1945 C CG    . ASN A 270 ? 0.12988 0.17484 0.30234 0.03324  -0.00046 -0.02024 264 ASN A CG    
1946 O OD1   . ASN A 270 ? 0.15475 0.18607 0.31491 0.02681  -0.01041 -0.00812 264 ASN A OD1   
1947 N ND2   . ASN A 270 ? 0.14533 0.17168 0.28772 0.02422  -0.04013 -0.01924 264 ASN A ND2   
1948 N N     . LYS A 271 ? 0.13764 0.21776 0.27970 -0.01151 0.01599  0.00995  265 LYS A N     
1949 C CA    . LYS A 271 ? 0.18152 0.23109 0.28530 -0.00916 -0.00322 0.04119  265 LYS A CA    
1950 C C     . LYS A 271 ? 0.15789 0.23486 0.26262 -0.02010 0.00711  0.00266  265 LYS A C     
1951 O O     . LYS A 271 ? 0.12184 0.24661 0.28995 -0.01852 -0.00021 0.00507  265 LYS A O     
1952 C CB    . LYS A 271 ? 0.26043 0.26044 0.28968 0.01345  0.01214  0.08711  265 LYS A CB    
1953 C CG    . LYS A 271 ? 0.30894 0.30264 0.35381 0.00997  0.01667  0.11608  265 LYS A CG    
1954 C CD    . LYS A 271 ? 0.35185 0.32776 0.43058 0.02622  0.01378  0.14290  265 LYS A CD    
1955 C CE    . LYS A 271 ? 0.39680 0.35849 0.47765 0.02657  0.02071  0.14444  265 LYS A CE    
1956 N NZ    . LYS A 271 ? 0.42592 0.39069 0.52647 0.01612  0.02371  0.12654  265 LYS A NZ    
1957 N N     . ILE A 272 ? 0.16687 0.22422 0.21328 -0.02372 -0.00421 0.02938  266 ILE A N     
1958 C CA    . ILE A 272 ? 0.13920 0.21963 0.23712 -0.00649 -0.03771 -0.01397 266 ILE A CA    
1959 C C     . ILE A 272 ? 0.11961 0.22523 0.20667 -0.00832 -0.01446 -0.00649 266 ILE A C     
1960 O O     . ILE A 272 ? 0.11541 0.26589 0.26508 -0.00189 -0.01179 -0.01360 266 ILE A O     
1961 C CB    . ILE A 272 ? 0.13409 0.21128 0.24601 -0.02637 -0.02424 -0.01472 266 ILE A CB    
1962 C CG1   . ILE A 272 ? 0.13770 0.20760 0.24812 -0.03147 0.00107  -0.06568 266 ILE A CG1   
1963 C CG2   . ILE A 272 ? 0.13966 0.23450 0.24962 -0.02400 -0.02579 0.00071  266 ILE A CG2   
1964 C CD1   . ILE A 272 ? 0.14490 0.23310 0.30269 -0.03085 0.01745  -0.03723 266 ILE A CD1   
1965 N N     . GLN A 273 ? 0.11376 0.22247 0.24086 -0.03509 0.03084  -0.01344 267 GLN A N     
1966 C CA    . GLN A 273 ? 0.11499 0.23356 0.23017 -0.05102 0.02068  -0.03745 267 GLN A CA    
1967 C C     . GLN A 273 ? 0.15086 0.26302 0.28280 -0.04702 0.01737  -0.04814 267 GLN A C     
1968 O O     . GLN A 273 ? 0.16960 0.26904 0.30101 -0.04070 0.00904  -0.02836 267 GLN A O     
1969 C CB    . GLN A 273 ? 0.10064 0.22977 0.20127 -0.03733 -0.00103 -0.03627 267 GLN A CB    
1970 C CG    . GLN A 273 ? 0.10903 0.21693 0.23960 -0.03069 0.00112  -0.01739 267 GLN A CG    
1971 C CD    . GLN A 273 ? 0.12955 0.22192 0.26428 -0.01305 0.01060  -0.00933 267 GLN A CD    
1972 O OE1   . GLN A 273 ? 0.13601 0.22019 0.29016 0.00369  0.00526  0.00994  267 GLN A OE1   
1973 N NE2   . GLN A 273 ? 0.14162 0.23052 0.23157 -0.00878 0.03423  -0.01648 267 GLN A NE2   
1974 N N     . LEU A 274 ? 0.15495 0.25802 0.27845 -0.04893 0.00726  -0.04633 268 LEU A N     
1975 C CA    . LEU A 274 ? 0.18401 0.29895 0.30307 -0.04471 -0.00832 -0.04673 268 LEU A CA    
1976 C C     . LEU A 274 ? 0.17698 0.33167 0.31587 -0.03302 -0.00058 -0.03041 268 LEU A C     
1977 O O     . LEU A 274 ? 0.16591 0.32866 0.37806 -0.03009 -0.00121 -0.01951 268 LEU A O     
1978 C CB    . LEU A 274 ? 0.23015 0.30980 0.36912 -0.06159 -0.01493 -0.02781 268 LEU A CB    
1979 C CG    . LEU A 274 ? 0.28145 0.32979 0.41582 -0.04996 -0.01781 -0.02354 268 LEU A CG    
1980 C CD1   . LEU A 274 ? 0.30114 0.33790 0.47043 -0.03721 -0.01794 -0.02774 268 LEU A CD1   
1981 C CD2   . LEU A 274 ? 0.30657 0.34219 0.41258 -0.05069 0.00109  -0.03191 268 LEU A CD2   
1982 N N     . HIS A 275 ? 0.15874 0.35213 0.29358 -0.01521 0.01606  -0.03370 269 HIS A N     
1983 C CA    . HIS A 275 ? 0.16016 0.37439 0.31778 -0.01821 0.02500  -0.04300 269 HIS A CA    
1984 C C     . HIS A 275 ? 0.16907 0.39692 0.30918 -0.02308 -0.02946 -0.06245 269 HIS A C     
1985 O O     . HIS A 275 ? 0.16578 0.41487 0.35626 -0.02147 -0.01764 -0.07047 269 HIS A O     
1986 C CB    . HIS A 275 ? 0.15117 0.38470 0.31817 -0.02845 0.07179  -0.04198 269 HIS A CB    
1987 C CG    . HIS A 275 ? 0.16761 0.39928 0.38816 -0.05210 0.07325  -0.03668 269 HIS A CG    
1988 N ND1   . HIS A 275 ? 0.16600 0.40272 0.41676 -0.05741 0.05655  -0.03460 269 HIS A ND1   
1989 C CD2   . HIS A 275 ? 0.16375 0.40129 0.40457 -0.05406 0.09952  -0.03846 269 HIS A CD2   
1990 C CE1   . HIS A 275 ? 0.16588 0.40259 0.41854 -0.06463 0.07375  -0.04527 269 HIS A CE1   
1991 N NE2   . HIS A 275 ? 0.17126 0.40994 0.40813 -0.06975 0.09174  -0.04854 269 HIS A NE2   
1992 N N     . SER A 276 ? 0.18838 0.40552 0.27284 -0.02201 -0.03479 -0.03656 270 SER A N     
1993 C CA    . SER A 276 ? 0.21103 0.41216 0.24567 -0.02214 -0.07826 -0.03867 270 SER A CA    
1994 C C     . SER A 276 ? 0.23569 0.42387 0.28024 -0.02817 -0.05070 -0.02019 270 SER A C     
1995 O O     . SER A 276 ? 0.24843 0.43750 0.34181 -0.01355 -0.05290 -0.02653 270 SER A O     
1996 C CB    . SER A 276 ? 0.22079 0.42513 0.33359 -0.01133 -0.06432 0.00108  270 SER A CB    
1997 O OG    . SER A 276 ? 0.25120 0.43735 0.37361 -0.01303 -0.07703 -0.00017 270 SER A OG    
1998 N N     . GLY A 277 ? 0.24761 0.41670 0.31213 -0.05643 -0.04998 -0.01666 271 GLY A N     
1999 C CA    . GLY A 277 ? 0.25013 0.41045 0.31482 -0.07139 -0.03649 -0.01294 271 GLY A CA    
2000 C C     . GLY A 277 ? 0.25865 0.39604 0.31920 -0.07675 -0.06021 -0.01662 271 GLY A C     
2001 O O     . GLY A 277 ? 0.27005 0.40284 0.32210 -0.09125 -0.07680 -0.01270 271 GLY A O     
2002 N N     . SER A 278 ? 0.25257 0.37768 0.35112 -0.07646 -0.08389 -0.02118 272 SER A N     
2003 C CA    . SER A 278 ? 0.27104 0.37010 0.39244 -0.05371 -0.08931 0.02303  272 SER A CA    
2004 C C     . SER A 278 ? 0.24591 0.34845 0.31752 -0.04868 -0.04830 -0.00414 272 SER A C     
2005 O O     . SER A 278 ? 0.24435 0.38310 0.28908 -0.03185 -0.04631 0.01913  272 SER A O     
2006 C CB    . SER A 278 ? 0.31660 0.38686 0.53354 -0.04910 -0.10015 0.04977  272 SER A CB    
2007 O OG    . SER A 278 ? 0.36369 0.40666 0.62783 -0.04333 -0.12831 0.05106  272 SER A OG    
2008 N N     . LYS A 279 ? 0.24642 0.29544 0.29455 -0.05555 -0.00859 -0.04048 273 LYS A N     
2009 C CA    . LYS A 279 ? 0.23909 0.25240 0.32622 -0.03861 0.00200  -0.04080 273 LYS A CA    
2010 C C     . LYS A 279 ? 0.20613 0.22779 0.30606 -0.03599 0.00899  -0.00980 273 LYS A C     
2011 O O     . LYS A 279 ? 0.19517 0.23760 0.27721 -0.03910 -0.01484 -0.02994 273 LYS A O     
2012 C CB    . LYS A 279 ? 0.27738 0.25095 0.36371 -0.01725 0.04134  -0.03514 273 LYS A CB    
2013 C CG    . LYS A 279 ? 0.32096 0.28667 0.44208 0.00831  0.05065  -0.07227 273 LYS A CG    
2014 C CD    . LYS A 279 ? 0.36240 0.30263 0.48820 0.02790  0.05877  -0.08052 273 LYS A CD    
2015 C CE    . LYS A 279 ? 0.39477 0.31929 0.53798 0.02626  0.05577  -0.05918 273 LYS A CE    
2016 N NZ    . LYS A 279 ? 0.40957 0.33251 0.56147 0.02920  0.08292  -0.04677 273 LYS A NZ    
2017 N N     . LEU A 280 ? 0.18160 0.20307 0.28817 -0.04437 0.00609  0.01099  274 LEU A N     
2018 C CA    . LEU A 280 ? 0.16893 0.19498 0.22813 -0.01845 0.01447  0.00487  274 LEU A CA    
2019 C C     . LEU A 280 ? 0.13723 0.18757 0.23771 -0.01153 0.01429  0.00145  274 LEU A C     
2020 O O     . LEU A 280 ? 0.14908 0.18198 0.24949 -0.03284 0.02099  -0.01157 274 LEU A O     
2021 C CB    . LEU A 280 ? 0.18159 0.19848 0.23171 0.00849  0.01721  0.04200  274 LEU A CB    
2022 C CG    . LEU A 280 ? 0.19975 0.21905 0.20757 0.05538  0.00613  0.04085  274 LEU A CG    
2023 C CD1   . LEU A 280 ? 0.26087 0.24976 0.22134 0.05724  -0.01973 0.05715  274 LEU A CD1   
2024 C CD2   . LEU A 280 ? 0.16909 0.21975 0.26012 0.06711  0.03897  0.00959  274 LEU A CD2   
2025 N N     . ALA A 281 ? 0.11337 0.17110 0.20982 0.01638  0.01682  -0.00031 275 ALA A N     
2026 C CA    . ALA A 281 ? 0.12719 0.16360 0.25807 0.01868  0.00086  0.01649  275 ALA A CA    
2027 C C     . ALA A 281 ? 0.12582 0.16876 0.22307 0.01166  -0.01256 0.00072  275 ALA A C     
2028 O O     . ALA A 281 ? 0.13221 0.19106 0.23291 0.01825  0.01715  -0.00797 275 ALA A O     
2029 C CB    . ALA A 281 ? 0.14050 0.15420 0.26649 0.01635  -0.01142 0.02920  275 ALA A CB    
2030 N N     . TYR A 282 ? 0.11727 0.18070 0.23211 0.01817  -0.02463 0.03299  276 TYR A N     
2031 C CA    . TYR A 282 ? 0.09956 0.18669 0.18368 -0.00797 0.00131  -0.00517 276 TYR A CA    
2032 C C     . TYR A 282 ? 0.10104 0.19889 0.16900 -0.00100 -0.02119 -0.03051 276 TYR A C     
2033 O O     . TYR A 282 ? 0.12326 0.22830 0.17143 -0.00036 0.01673  -0.02890 276 TYR A O     
2034 C CB    . TYR A 282 ? 0.10418 0.15725 0.20491 -0.02974 0.02770  0.01927  276 TYR A CB    
2035 C CG    . TYR A 282 ? 0.09808 0.15771 0.26305 -0.02814 0.00744  -0.01129 276 TYR A CG    
2036 C CD1   . TYR A 282 ? 0.08637 0.16742 0.23782 -0.00024 -0.00262 -0.01303 276 TYR A CD1   
2037 C CD2   . TYR A 282 ? 0.10137 0.16793 0.25895 -0.02167 0.01875  0.01055  276 TYR A CD2   
2038 C CE1   . TYR A 282 ? 0.09130 0.17059 0.24753 0.02015  0.01282  0.02506  276 TYR A CE1   
2039 C CE2   . TYR A 282 ? 0.11259 0.16008 0.25557 -0.01038 0.02141  -0.00966 276 TYR A CE2   
2040 C CZ    . TYR A 282 ? 0.11411 0.17775 0.26376 0.01914  0.02215  0.00038  276 TYR A CZ    
2041 O OH    . TYR A 282 ? 0.11469 0.17793 0.23964 0.00510  0.00910  -0.00124 276 TYR A OH    
2042 N N     . LEU A 283 ? 0.11926 0.20178 0.16561 -0.00465 -0.01969 0.01000  277 LEU A N     
2043 C CA    . LEU A 283 ? 0.11697 0.19710 0.16147 -0.00568 -0.00785 0.03131  277 LEU A CA    
2044 C C     . LEU A 283 ? 0.11332 0.17982 0.20506 -0.02204 -0.01065 -0.01128 277 LEU A C     
2045 O O     . LEU A 283 ? 0.14343 0.18516 0.20661 -0.01964 0.03859  -0.02330 277 LEU A O     
2046 C CB    . LEU A 283 ? 0.14279 0.19649 0.16574 0.00542  0.00521  0.03524  277 LEU A CB    
2047 C CG    . LEU A 283 ? 0.13371 0.18575 0.17047 0.03607  -0.00534 0.00989  277 LEU A CG    
2048 C CD1   . LEU A 283 ? 0.14314 0.18201 0.17276 0.02446  0.01816  0.00903  277 LEU A CD1   
2049 C CD2   . LEU A 283 ? 0.14721 0.21644 0.22866 0.00614  -0.02211 0.03088  277 LEU A CD2   
2050 N N     . HIS A 284 ? 0.09416 0.17189 0.24014 -0.01644 -0.01780 -0.02139 278 HIS A N     
2051 C CA    . HIS A 284 ? 0.09660 0.15351 0.21177 -0.00626 -0.00023 -0.00870 278 HIS A CA    
2052 C C     . HIS A 284 ? 0.10186 0.16082 0.24004 0.01444  -0.03189 0.02362  278 HIS A C     
2053 O O     . HIS A 284 ? 0.13300 0.16553 0.23567 0.02745  0.00078  0.00647  278 HIS A O     
2054 C CB    . HIS A 284 ? 0.10575 0.14015 0.22263 -0.01189 0.00693  0.04473  278 HIS A CB    
2055 C CG    . HIS A 284 ? 0.10217 0.16884 0.22900 -0.03153 0.02405  -0.00760 278 HIS A CG    
2056 N ND1   . HIS A 284 ? 0.10166 0.20025 0.26195 -0.03769 -0.00363 -0.01190 278 HIS A ND1   
2057 C CD2   . HIS A 284 ? 0.12566 0.16988 0.25888 -0.04484 -0.00436 -0.01041 278 HIS A CD2   
2058 C CE1   . HIS A 284 ? 0.12191 0.19989 0.27895 -0.04633 -0.01546 -0.01522 278 HIS A CE1   
2059 N NE2   . HIS A 284 ? 0.13048 0.20315 0.25917 -0.02803 -0.00551 -0.01377 278 HIS A NE2   
2060 N N     . VAL A 285 ? 0.09620 0.18595 0.25342 0.02659  -0.04487 0.04125  279 VAL A N     
2061 C CA    . VAL A 285 ? 0.09643 0.20696 0.24781 -0.00001 -0.01361 0.01830  279 VAL A CA    
2062 C C     . VAL A 285 ? 0.10398 0.21207 0.21390 -0.00105 -0.02128 0.02405  279 VAL A C     
2063 O O     . VAL A 285 ? 0.10787 0.21686 0.24808 -0.01000 0.00048  0.01969  279 VAL A O     
2064 C CB    . VAL A 285 ? 0.09470 0.21499 0.25669 -0.00427 -0.02423 0.00307  279 VAL A CB    
2065 C CG1   . VAL A 285 ? 0.12043 0.21986 0.33396 0.00054  -0.03005 0.01630  279 VAL A CG1   
2066 C CG2   . VAL A 285 ? 0.09068 0.22407 0.32103 0.00483  -0.03805 0.00100  279 VAL A CG2   
2067 N N     . THR A 286 ? 0.13176 0.19772 0.21638 -0.01144 -0.01966 0.00718  280 THR A N     
2068 C CA    . THR A 286 ? 0.15312 0.26081 0.23638 -0.02528 -0.00263 0.00103  280 THR A CA    
2069 C C     . THR A 286 ? 0.18160 0.32465 0.26319 -0.03089 0.01402  0.02795  280 THR A C     
2070 O O     . THR A 286 ? 0.19466 0.36208 0.18677 -0.01132 -0.00740 0.03884  280 THR A O     
2071 C CB    . THR A 286 ? 0.22820 0.30345 0.34091 -0.02140 0.02137  -0.02479 280 THR A CB    
2072 O OG1   . THR A 286 ? 0.26590 0.32991 0.44934 -0.02031 0.05714  -0.06746 280 THR A OG1   
2073 C CG2   . THR A 286 ? 0.24987 0.30447 0.41069 -0.02259 0.00994  0.02885  280 THR A CG2   
2074 N N     . GLN A 287 ? 0.18318 0.34297 0.30468 -0.03462 -0.01864 0.03841  281 GLN A N     
2075 C CA    . GLN A 287 ? 0.22902 0.36660 0.33526 -0.01783 -0.01268 0.01511  281 GLN A CA    
2076 C C     . GLN A 287 ? 0.26389 0.39473 0.34193 -0.00134 -0.00928 0.01096  281 GLN A C     
2077 O O     . GLN A 287 ? 0.26381 0.37626 0.36336 -0.01009 -0.00270 -0.00149 281 GLN A O     
2078 C CB    . GLN A 287 ? 0.24779 0.36499 0.34568 -0.00383 0.02009  -0.00458 281 GLN A CB    
2079 C CG    . GLN A 287 ? 0.26402 0.38302 0.39549 0.00928  0.03779  0.00487  281 GLN A CG    
2080 C CD    . GLN A 287 ? 0.30217 0.40762 0.46529 0.00150  0.04751  0.00122  281 GLN A CD    
2081 O OE1   . GLN A 287 ? 0.32666 0.42469 0.48750 -0.00597 0.08166  -0.00128 281 GLN A OE1   
2082 N NE2   . GLN A 287 ? 0.31626 0.40189 0.52293 0.00520  0.06429  0.02686  281 GLN A NE2   
2083 N N     . PRO A 288 ? 0.28772 0.44442 0.30355 0.01141  -0.01467 0.01888  282 PRO A N     
2084 C CA    . PRO A 288 ? 0.31306 0.48009 0.35792 0.00321  -0.02589 0.00644  282 PRO A CA    
2085 C C     . PRO A 288 ? 0.34625 0.51589 0.44143 -0.00289 -0.02255 0.00736  282 PRO A C     
2086 O O     . PRO A 288 ? 0.36044 0.54028 0.47267 -0.00756 -0.00826 0.02052  282 PRO A O     
2087 C CB    . PRO A 288 ? 0.31070 0.47219 0.34139 0.00055  -0.04163 0.02223  282 PRO A CB    
2088 C CG    . PRO A 288 ? 0.30822 0.46381 0.32571 0.01183  -0.05105 0.04137  282 PRO A CG    
2089 C CD    . PRO A 288 ? 0.29757 0.45159 0.32467 0.01384  -0.02892 0.03301  282 PRO A CD    
2090 N N     . ARG A 289 ? 0.38372 0.52543 0.47917 -0.00698 -0.03133 0.01347  283 ARG A N     
2091 C CA    . ARG A 289 ? 0.41797 0.53306 0.49835 -0.01019 -0.04369 0.00459  283 ARG A CA    
2092 C C     . ARG A 289 ? 0.43994 0.55974 0.54221 -0.03695 -0.03598 -0.02845 283 ARG A C     
2093 O O     . ARG A 289 ? 0.45326 0.58147 0.56424 -0.05020 -0.02103 -0.03746 283 ARG A O     
2094 C CB    . ARG A 289 ? 0.42308 0.50697 0.46530 0.01422  -0.05835 0.01349  283 ARG A CB    
2095 C CG    . ARG A 289 ? 0.41032 0.47755 0.40972 0.04939  -0.10433 0.03476  283 ARG A CG    
2096 C CD    . ARG A 289 ? 0.39564 0.45835 0.38512 0.07426  -0.11427 0.02998  283 ARG A CD    
2097 N NE    . ARG A 289 ? 0.37948 0.44219 0.39243 0.08507  -0.11584 0.03958  283 ARG A NE    
2098 C CZ    . ARG A 289 ? 0.34805 0.43394 0.39862 0.08628  -0.09747 0.04594  283 ARG A CZ    
2099 N NH1   . ARG A 289 ? 0.33751 0.42746 0.40701 0.08884  -0.09824 0.03105  283 ARG A NH1   
2100 N NH2   . ARG A 289 ? 0.31644 0.43773 0.46318 0.08763  -0.11648 0.02105  283 ARG A NH2   
2101 N N     . SER A 303 ? 0.47620 0.63262 0.69937 -0.03268 -0.11619 0.01345  297 SER A N     
2102 C CA    . SER A 303 ? 0.48079 0.62412 0.68886 -0.03455 -0.11488 0.01778  297 SER A CA    
2103 C C     . SER A 303 ? 0.46753 0.60406 0.71107 -0.03469 -0.10438 0.00126  297 SER A C     
2104 O O     . SER A 303 ? 0.46384 0.61364 0.73710 -0.03459 -0.10494 -0.00931 297 SER A O     
2105 C CB    . SER A 303 ? 0.49327 0.63148 0.67366 -0.03369 -0.10823 0.02805  297 SER A CB    
2106 N N     . GLU A 304 ? 0.44184 0.56491 0.68892 -0.04457 -0.09750 0.00264  298 GLU A N     
2107 C CA    . GLU A 304 ? 0.42888 0.53211 0.70563 -0.03099 -0.08340 0.01970  298 GLU A CA    
2108 C C     . GLU A 304 ? 0.39839 0.49977 0.66472 -0.01071 -0.08987 0.04881  298 GLU A C     
2109 O O     . GLU A 304 ? 0.38560 0.48839 0.64542 -0.00066 -0.07651 0.06903  298 GLU A O     
2110 C CB    . GLU A 304 ? 0.45394 0.53898 0.73760 -0.03058 -0.06378 0.01103  298 GLU A CB    
2111 N N     . GLU A 305 ? 0.36668 0.47505 0.63699 0.00490  -0.09109 0.05816  299 GLU A N     
2112 C CA    . GLU A 305 ? 0.33679 0.44410 0.58660 0.01178  -0.08770 0.07411  299 GLU A CA    
2113 C C     . GLU A 305 ? 0.32279 0.42044 0.53635 0.00632  -0.05900 0.09114  299 GLU A C     
2114 O O     . GLU A 305 ? 0.29853 0.39951 0.52923 0.01495  -0.08548 0.13309  299 GLU A O     
2115 C CB    . GLU A 305 ? 0.33051 0.45035 0.58034 0.02828  -0.10821 0.08801  299 GLU A CB    
2116 N N     . GLU A 306 ? 0.31338 0.41111 0.48376 -0.00367 -0.03020 0.06614  300 GLU A N     
2117 C CA    . GLU A 306 ? 0.31011 0.39694 0.44266 0.00023  -0.03488 0.04885  300 GLU A CA    
2118 C C     . GLU A 306 ? 0.30378 0.36071 0.38826 -0.00184 -0.05322 0.02350  300 GLU A C     
2119 O O     . GLU A 306 ? 0.29865 0.34079 0.38675 -0.00466 -0.07062 0.01441  300 GLU A O     
2120 C CB    . GLU A 306 ? 0.31311 0.41452 0.46161 -0.00216 -0.02360 0.05104  300 GLU A CB    
2121 N N     . GLU A 307 ? 0.29773 0.33869 0.37317 -0.00281 -0.05446 0.02708  301 GLU A N     
2122 C CA    . GLU A 307 ? 0.29402 0.32795 0.44692 -0.01478 -0.05040 0.00849  301 GLU A CA    
2123 C C     . GLU A 307 ? 0.26294 0.31065 0.46455 -0.00501 -0.03964 -0.01130 301 GLU A C     
2124 O O     . GLU A 307 ? 0.24504 0.30695 0.46250 0.01009  -0.04636 -0.02542 301 GLU A O     
2125 C CB    . GLU A 307 ? 0.32160 0.32772 0.48670 -0.02424 -0.03340 0.00364  301 GLU A CB    
2126 N N     . ALA A 308 ? 0.23508 0.29274 0.47491 0.00041  -0.02790 -0.00723 302 ALA A N     
2127 C CA    . ALA A 308 ? 0.21535 0.28518 0.47012 0.01004  -0.00389 -0.00725 302 ALA A CA    
2128 C C     . ALA A 308 ? 0.21557 0.29296 0.43463 0.00899  0.00413  0.01658  302 ALA A C     
2129 O O     . ALA A 308 ? 0.20172 0.30127 0.43258 -0.00091 -0.00696 0.01131  302 ALA A O     
2130 C CB    . ALA A 308 ? 0.19660 0.28465 0.49013 0.02933  -0.00841 -0.00938 302 ALA A CB    
2131 N N     . ARG A 309 ? 0.20985 0.26762 0.37010 0.02561  -0.01073 0.05037  303 ARG A N     
2132 C CA    . ARG A 309 ? 0.21186 0.27190 0.34743 0.03011  0.00626  0.06105  303 ARG A CA    
2133 C C     . ARG A 309 ? 0.19722 0.27525 0.32715 0.03178  0.02237  0.05367  303 ARG A C     
2134 O O     . ARG A 309 ? 0.18822 0.26364 0.34158 0.03566  0.01309  0.03476  303 ARG A O     
2135 C CB    . ARG A 309 ? 0.25491 0.27574 0.34972 0.01071  0.00366  0.08276  303 ARG A CB    
2136 C CG    . ARG A 309 ? 0.29439 0.27924 0.37771 0.00576  -0.02570 0.10460  303 ARG A CG    
2137 C CD    . ARG A 309 ? 0.33183 0.30918 0.43354 0.00403  -0.05091 0.10388  303 ARG A CD    
2138 N NE    . ARG A 309 ? 0.37214 0.34604 0.49054 -0.00107 -0.04541 0.11559  303 ARG A NE    
2139 C CZ    . ARG A 309 ? 0.42140 0.38040 0.56075 0.00583  -0.04095 0.10527  303 ARG A CZ    
2140 N NH1   . ARG A 309 ? 0.44349 0.39315 0.62011 0.01328  -0.03413 0.09920  303 ARG A NH1   
2141 N NH2   . ARG A 309 ? 0.43661 0.39031 0.51492 -0.00269 -0.03770 0.11642  303 ARG A NH2   
2142 N N     . LEU A 310 ? 0.17992 0.27430 0.26493 0.04090  0.02165  0.03775  304 LEU A N     
2143 C CA    . LEU A 310 ? 0.19855 0.28910 0.28441 0.04843  0.01937  0.01118  304 LEU A CA    
2144 C C     . LEU A 310 ? 0.18024 0.26134 0.27693 0.03816  0.02111  0.00626  304 LEU A C     
2145 O O     . LEU A 310 ? 0.17540 0.25196 0.27429 0.04896  0.00625  -0.00850 304 LEU A O     
2146 C CB    . LEU A 310 ? 0.24110 0.31812 0.30730 0.03691  0.01372  -0.00202 304 LEU A CB    
2147 C CG    . LEU A 310 ? 0.27835 0.34730 0.34990 0.04847  0.01129  -0.05530 304 LEU A CG    
2148 C CD1   . LEU A 310 ? 0.29852 0.36607 0.39107 0.04762  0.00003  -0.07009 304 LEU A CD1   
2149 C CD2   . LEU A 310 ? 0.28664 0.37209 0.37499 0.05771  -0.00766 -0.05676 304 LEU A CD2   
2150 N N     . MET A 311 ? 0.16483 0.25196 0.31178 -0.00357 -0.00243 -0.01471 305 MET A N     
2151 C CA    . MET A 311 ? 0.15761 0.24590 0.31971 -0.00780 0.00470  0.01142  305 MET A CA    
2152 C C     . MET A 311 ? 0.16117 0.23618 0.31794 0.00084  0.00263  -0.00680 305 MET A C     
2153 O O     . MET A 311 ? 0.15503 0.24347 0.34809 0.00098  0.01113  0.00134  305 MET A O     
2154 C CB    . MET A 311 ? 0.17036 0.26431 0.34661 -0.00029 0.00522  0.01998  305 MET A CB    
2155 C CG    . MET A 311 ? 0.18548 0.28482 0.42230 0.00057  -0.00734 0.02776  305 MET A CG    
2156 S SD    . MET A 311 ? 0.20269 0.30538 0.43354 0.01140  0.02514  0.03116  305 MET A SD    
2157 C CE    . MET A 311 ? 0.21145 0.31178 0.34176 0.00189  0.03363  0.06732  305 MET A CE    
2158 N N     . ARG A 312 ? 0.16991 0.23046 0.31379 0.00105  0.04454  0.00898  306 ARG A N     
2159 C CA    . ARG A 312 ? 0.17792 0.22091 0.28936 0.01948  0.03634  0.02210  306 ARG A CA    
2160 C C     . ARG A 312 ? 0.16359 0.20088 0.30979 0.00891  0.01848  0.03755  306 ARG A C     
2161 O O     . ARG A 312 ? 0.18142 0.19335 0.36729 -0.00697 0.04010  0.02786  306 ARG A O     
2162 C CB    . ARG A 312 ? 0.22096 0.24047 0.30634 0.03583  0.04457  -0.01147 306 ARG A CB    
2163 C CG    . ARG A 312 ? 0.27113 0.26278 0.34416 0.04747  0.03196  -0.00977 306 ARG A CG    
2164 C CD    . ARG A 312 ? 0.31470 0.26877 0.37490 0.06222  0.02326  0.00527  306 ARG A CD    
2165 N NE    . ARG A 312 ? 0.34683 0.27448 0.41953 0.07701  0.02179  0.02293  306 ARG A NE    
2166 C CZ    . ARG A 312 ? 0.36802 0.27348 0.46822 0.09768  -0.00975 0.01431  306 ARG A CZ    
2167 N NH1   . ARG A 312 ? 0.36365 0.28077 0.49003 0.11718  -0.00770 0.03572  306 ARG A NH1   
2168 N NH2   . ARG A 312 ? 0.38969 0.27573 0.49437 0.09041  -0.03967 -0.01380 306 ARG A NH2   
2169 N N     . THR A 313 ? 0.15654 0.19230 0.28418 0.00594  0.01642  0.03725  307 THR A N     
2170 C CA    . THR A 313 ? 0.15797 0.19634 0.27515 0.00927  0.02705  0.05370  307 THR A CA    
2171 C C     . THR A 313 ? 0.16717 0.18611 0.28055 0.02070  0.01669  0.00924  307 THR A C     
2172 O O     . THR A 313 ? 0.15425 0.18141 0.31338 0.02104  0.01255  0.01956  307 THR A O     
2173 C CB    . THR A 313 ? 0.16864 0.21468 0.31333 0.01610  0.01017  0.04869  307 THR A CB    
2174 O OG1   . THR A 313 ? 0.18513 0.23129 0.31306 0.02334  -0.01740 0.05376  307 THR A OG1   
2175 C CG2   . THR A 313 ? 0.18052 0.20890 0.34381 0.00761  0.00501  0.02433  307 THR A CG2   
2176 N N     . LEU A 314 ? 0.16699 0.17117 0.24461 0.03305  0.01733  0.00955  308 LEU A N     
2177 C CA    . LEU A 314 ? 0.15985 0.17841 0.24992 0.03903  0.02067  -0.01801 308 LEU A CA    
2178 C C     . LEU A 314 ? 0.14480 0.15488 0.24738 0.02183  0.01600  0.01157  308 LEU A C     
2179 O O     . LEU A 314 ? 0.13612 0.13730 0.29731 0.01154  -0.01687 0.00594  308 LEU A O     
2180 C CB    . LEU A 314 ? 0.18098 0.19456 0.22029 0.04421  0.02306  -0.01456 308 LEU A CB    
2181 C CG    . LEU A 314 ? 0.18884 0.20785 0.23369 0.04502  0.04758  -0.01757 308 LEU A CG    
2182 C CD1   . LEU A 314 ? 0.22086 0.22185 0.27446 0.02947  0.02369  -0.01634 308 LEU A CD1   
2183 C CD2   . LEU A 314 ? 0.17542 0.22623 0.23974 0.04921  0.09282  0.00213  308 LEU A CD2   
2184 N N     . ARG A 315 ? 0.15286 0.16200 0.19617 0.01099  0.04882  0.04131  309 ARG A N     
2185 C CA    . ARG A 315 ? 0.16092 0.17113 0.21466 0.00173  0.04750  0.02348  309 ARG A CA    
2186 C C     . ARG A 315 ? 0.16212 0.17438 0.25904 0.00194  0.00747  0.02433  309 ARG A C     
2187 O O     . ARG A 315 ? 0.15413 0.17566 0.28953 0.00388  0.00152  0.04386  309 ARG A O     
2188 C CB    . ARG A 315 ? 0.18599 0.20155 0.25039 0.00674  0.05379  0.01058  309 ARG A CB    
2189 C CG    . ARG A 315 ? 0.19920 0.21548 0.24350 0.01222  0.04849  -0.01000 309 ARG A CG    
2190 C CD    . ARG A 315 ? 0.20748 0.23662 0.25908 0.01507  0.04824  -0.00998 309 ARG A CD    
2191 N NE    . ARG A 315 ? 0.20774 0.23926 0.27178 0.02050  0.03416  0.02760  309 ARG A NE    
2192 C CZ    . ARG A 315 ? 0.18747 0.21894 0.27714 0.03493  0.03932  -0.00414 309 ARG A CZ    
2193 N NH1   . ARG A 315 ? 0.14406 0.19198 0.28543 0.01712  0.04349  -0.05034 309 ARG A NH1   
2194 N NH2   . ARG A 315 ? 0.19655 0.22107 0.26725 0.04645  0.05235  0.04303  309 ARG A NH2   
2195 N N     . ASN A 316 ? 0.14090 0.16881 0.26149 0.00912  0.00917  0.03222  310 ASN A N     
2196 C CA    . ASN A 316 ? 0.13373 0.18075 0.25957 0.00511  0.01832  0.05201  310 ASN A CA    
2197 C C     . ASN A 316 ? 0.13470 0.21231 0.28652 0.00784  0.01794  0.01532  310 ASN A C     
2198 O O     . ASN A 316 ? 0.13187 0.21652 0.29957 0.00724  0.04137  -0.02427 310 ASN A O     
2199 C CB    . ASN A 316 ? 0.12506 0.20033 0.33520 0.02673  0.02738  0.03817  310 ASN A CB    
2200 C CG    . ASN A 316 ? 0.16230 0.22486 0.36536 0.03268  0.01656  0.02457  310 ASN A CG    
2201 O OD1   . ASN A 316 ? 0.16847 0.24154 0.41652 0.02229  0.04903  0.03068  310 ASN A OD1   
2202 N ND2   . ASN A 316 ? 0.16859 0.21258 0.34918 0.06299  0.00046  0.01712  310 ASN A ND2   
2203 N N     . ALA A 317 ? 0.12161 0.20582 0.23902 0.00064  0.03829  0.03787  311 ALA A N     
2204 C CA    . ALA A 317 ? 0.11467 0.20362 0.23804 0.00257  0.04464  0.04149  311 ALA A CA    
2205 C C     . ALA A 317 ? 0.10740 0.18789 0.27440 0.01009  0.01107  0.02552  311 ALA A C     
2206 O O     . ALA A 317 ? 0.09415 0.18213 0.28068 0.00453  0.02064  0.00182  311 ALA A O     
2207 C CB    . ALA A 317 ? 0.14373 0.22044 0.24251 -0.00925 0.04266  0.03388  311 ALA A CB    
2208 N N     . TYR A 318 ? 0.11254 0.15755 0.25423 0.01447  0.00222  0.03534  312 TYR A N     
2209 C CA    . TYR A 318 ? 0.11977 0.15164 0.24614 0.00877  -0.03853 0.00493  312 TYR A CA    
2210 C C     . TYR A 318 ? 0.12635 0.17683 0.23268 0.00512  -0.02685 -0.01857 312 TYR A C     
2211 O O     . TYR A 318 ? 0.12709 0.20077 0.19490 -0.01549 -0.00210 -0.02061 312 TYR A O     
2212 C CB    . TYR A 318 ? 0.14123 0.14683 0.28001 -0.01122 -0.00785 0.01063  312 TYR A CB    
2213 C CG    . TYR A 318 ? 0.11392 0.15924 0.27067 -0.00271 -0.00488 -0.00767 312 TYR A CG    
2214 C CD1   . TYR A 318 ? 0.11596 0.17562 0.27375 0.01456  -0.00539 -0.00636 312 TYR A CD1   
2215 C CD2   . TYR A 318 ? 0.13641 0.14283 0.28975 0.01790  -0.00223 -0.00895 312 TYR A CD2   
2216 C CE1   . TYR A 318 ? 0.12306 0.16541 0.26687 0.01487  -0.03146 0.01113  312 TYR A CE1   
2217 C CE2   . TYR A 318 ? 0.11732 0.14139 0.24365 0.00797  -0.00531 0.01783  312 TYR A CE2   
2218 C CZ    . TYR A 318 ? 0.13153 0.15458 0.26016 0.01700  -0.01019 0.02798  312 TYR A CZ    
2219 O OH    . TYR A 318 ? 0.15951 0.16765 0.27546 0.01071  0.02417  0.03440  312 TYR A OH    
2220 N N     . GLN A 319 ? 0.13891 0.18143 0.20283 -0.00722 -0.06921 -0.00799 313 GLN A N     
2221 C CA    . GLN A 319 ? 0.14119 0.18226 0.24287 -0.03278 -0.02378 -0.01242 313 GLN A CA    
2222 C C     . GLN A 319 ? 0.14207 0.20349 0.24787 -0.00426 0.01515  0.00310  313 GLN A C     
2223 O O     . GLN A 319 ? 0.13252 0.22537 0.31123 0.01227  0.04608  0.03660  313 GLN A O     
2224 C CB    . GLN A 319 ? 0.14554 0.19238 0.28323 -0.01905 -0.02841 0.00786  313 GLN A CB    
2225 C CG    . GLN A 319 ? 0.15752 0.19644 0.34037 -0.02099 -0.02755 0.01587  313 GLN A CG    
2226 C CD    . GLN A 319 ? 0.17868 0.20819 0.34947 -0.01610 -0.04565 0.00493  313 GLN A CD    
2227 O OE1   . GLN A 319 ? 0.17583 0.23174 0.35651 -0.02133 -0.07283 0.01945  313 GLN A OE1   
2228 N NE2   . GLN A 319 ? 0.18898 0.17609 0.33374 -0.02506 -0.00763 -0.01771 313 GLN A NE2   
2229 N N     . GLY A 320 ? 0.15718 0.18225 0.24155 -0.02315 0.03719  0.01137  314 GLY A N     
2230 C CA    . GLY A 320 ? 0.15171 0.19971 0.23587 -0.02451 0.01590  0.00875  314 GLY A CA    
2231 C C     . GLY A 320 ? 0.13997 0.20525 0.25499 -0.01206 0.00585  -0.01603 314 GLY A C     
2232 O O     . GLY A 320 ? 0.13240 0.20096 0.27015 0.00805  0.00845  -0.01043 314 GLY A O     
2233 N N     . THR A 321 ? 0.12237 0.20592 0.27282 -0.02785 0.01198  -0.00093 315 THR A N     
2234 C CA    . THR A 321 ? 0.11409 0.19971 0.21875 -0.03419 -0.00108 0.01654  315 THR A CA    
2235 C C     . THR A 321 ? 0.09018 0.19520 0.25016 -0.00956 -0.00396 0.00329  315 THR A C     
2236 O O     . THR A 321 ? 0.08825 0.19807 0.22654 0.01712  0.02352  -0.01046 315 THR A O     
2237 C CB    . THR A 321 ? 0.12206 0.22746 0.24106 -0.02290 -0.03420 0.03623  315 THR A CB    
2238 O OG1   . THR A 321 ? 0.13584 0.24238 0.27369 -0.03116 -0.02445 0.02146  315 THR A OG1   
2239 C CG2   . THR A 321 ? 0.11172 0.21676 0.25099 -0.02235 -0.01957 0.02435  315 THR A CG2   
2240 N N     . PHE A 322 ? 0.09416 0.21244 0.25928 -0.00827 -0.01996 0.00629  316 PHE A N     
2241 C CA    . PHE A 322 ? 0.11006 0.20317 0.23069 0.00141  0.00488  0.00206  316 PHE A CA    
2242 C C     . PHE A 322 ? 0.11508 0.18643 0.20149 0.00510  0.01289  -0.00782 316 PHE A C     
2243 O O     . PHE A 322 ? 0.12980 0.20232 0.24109 -0.01481 0.03369  -0.00800 316 PHE A O     
2244 C CB    . PHE A 322 ? 0.12682 0.21459 0.23532 0.01590  -0.00525 0.01239  316 PHE A CB    
2245 C CG    . PHE A 322 ? 0.14081 0.21937 0.21590 0.02518  0.01275  0.00393  316 PHE A CG    
2246 C CD1   . PHE A 322 ? 0.16155 0.22318 0.23812 0.02630  0.00839  -0.02775 316 PHE A CD1   
2247 C CD2   . PHE A 322 ? 0.15099 0.21940 0.23778 0.01169  0.00596  -0.00726 316 PHE A CD2   
2248 C CE1   . PHE A 322 ? 0.16895 0.22505 0.24118 0.03135  -0.01921 -0.01109 316 PHE A CE1   
2249 C CE2   . PHE A 322 ? 0.14758 0.23106 0.26651 0.01325  0.01612  -0.03626 316 PHE A CE2   
2250 C CZ    . PHE A 322 ? 0.16198 0.22484 0.25030 0.01109  -0.00891 -0.01971 316 PHE A CZ    
2251 N N     . ILE A 323 ? 0.10651 0.15557 0.23248 0.02886  0.00201  -0.00099 317 ILE A N     
2252 C CA    . ILE A 323 ? 0.11510 0.15994 0.22004 0.02064  -0.00784 0.00812  317 ILE A CA    
2253 C C     . ILE A 323 ? 0.10626 0.18285 0.21709 0.00246  -0.01109 0.00041  317 ILE A C     
2254 O O     . ILE A 323 ? 0.11376 0.20407 0.19409 0.00202  0.00293  -0.00405 317 ILE A O     
2255 C CB    . ILE A 323 ? 0.12294 0.14602 0.24768 0.01180  0.00908  0.01177  317 ILE A CB    
2256 C CG1   . ILE A 323 ? 0.14817 0.14743 0.22228 -0.00098 0.00996  0.03531  317 ILE A CG1   
2257 C CG2   . ILE A 323 ? 0.12125 0.16096 0.23838 -0.02035 0.00054  0.01284  317 ILE A CG2   
2258 C CD1   . ILE A 323 ? 0.16786 0.15447 0.23320 -0.02216 0.01972  0.03976  317 ILE A CD1   
2259 N N     . CYS A 324 ? 0.10097 0.20943 0.22245 -0.00579 -0.02415 -0.00931 318 CYS A N     
2260 C CA    . CYS A 324 ? 0.12640 0.24002 0.27612 -0.00174 -0.01953 0.01097  318 CYS A CA    
2261 C C     . CYS A 324 ? 0.14395 0.24913 0.22627 0.00979  -0.03630 -0.01285 318 CYS A C     
2262 O O     . CYS A 324 ? 0.15731 0.24855 0.20033 -0.00232 -0.00723 0.00637  318 CYS A O     
2263 C CB    . CYS A 324 ? 0.13721 0.28493 0.35270 0.00390  0.01138  0.02878  318 CYS A CB    
2264 S SG    . CYS A 324 ? 0.16667 0.30982 0.41723 0.03096  0.01152  0.02068  318 CYS A SG    
2265 N N     . SER A 325 ? 0.12755 0.25545 0.20921 0.01939  -0.04414 -0.01495 319 SER A N     
2266 C CA    . SER A 325 ? 0.10798 0.26933 0.25207 0.04229  -0.06222 -0.01451 319 SER A CA    
2267 C C     . SER A 325 ? 0.12261 0.28846 0.24099 0.03003  -0.03496 0.00538  319 SER A C     
2268 O O     . SER A 325 ? 0.14881 0.30158 0.24876 0.01729  0.00175  0.01851  319 SER A O     
2269 C CB    . SER A 325 ? 0.11607 0.30684 0.35791 0.06302  -0.03043 -0.00815 319 SER A CB    
2270 O OG    . SER A 325 ? 0.13602 0.34255 0.38690 0.06639  -0.02994 -0.07366 319 SER A OG    
2271 N N     . GLY A 326 ? 0.10626 0.28595 0.25036 0.01788  -0.06685 0.02206  320 GLY A N     
2272 C CA    . GLY A 326 ? 0.10541 0.29491 0.29934 0.01105  -0.06068 0.03027  320 GLY A CA    
2273 C C     . GLY A 326 ? 0.10829 0.29598 0.30100 0.01857  -0.03277 0.03172  320 GLY A C     
2274 O O     . GLY A 326 ? 0.12347 0.29584 0.33723 0.02369  -0.01316 0.03574  320 GLY A O     
2275 N N     . GLY A 327 ? 0.09679 0.30486 0.25917 0.00542  -0.00854 0.03842  321 GLY A N     
2276 C CA    . GLY A 327 ? 0.11941 0.33372 0.29185 -0.00365 -0.00266 0.01211  321 GLY A CA    
2277 C C     . GLY A 327 ? 0.11811 0.34336 0.31619 0.00288  -0.01289 -0.00878 321 GLY A C     
2278 O O     . GLY A 327 ? 0.10372 0.35874 0.35246 0.00952  -0.01448 -0.02353 321 GLY A O     
2279 N N     . TYR A 328 ? 0.12495 0.33854 0.32515 0.00430  -0.01590 0.03029  322 TYR A N     
2280 C CA    . TYR A 328 ? 0.13486 0.34094 0.32677 0.01501  -0.00850 0.03251  322 TYR A CA    
2281 C C     . TYR A 328 ? 0.15462 0.35602 0.35740 0.03852  0.00467  0.05922  322 TYR A C     
2282 O O     . TYR A 328 ? 0.15884 0.36566 0.36206 0.03889  0.00300  0.06632  322 TYR A O     
2283 C CB    . TYR A 328 ? 0.13473 0.33013 0.30138 0.02623  -0.03469 -0.01874 322 TYR A CB    
2284 C CG    . TYR A 328 ? 0.14947 0.31215 0.36767 0.02438  -0.03445 -0.02859 322 TYR A CG    
2285 C CD1   . TYR A 328 ? 0.15010 0.30514 0.37891 0.01688  -0.01687 -0.01700 322 TYR A CD1   
2286 C CD2   . TYR A 328 ? 0.15633 0.31842 0.41384 0.02480  -0.04568 -0.02643 322 TYR A CD2   
2287 C CE1   . TYR A 328 ? 0.17257 0.31585 0.40409 0.01214  -0.02239 -0.01187 322 TYR A CE1   
2288 C CE2   . TYR A 328 ? 0.16327 0.31870 0.43342 0.01561  -0.04799 -0.01386 322 TYR A CE2   
2289 C CZ    . TYR A 328 ? 0.19152 0.31691 0.43928 0.00398  -0.03224 -0.00687 322 TYR A CZ    
2290 O OH    . TYR A 328 ? 0.21382 0.31684 0.47743 0.01894  -0.05583 0.01635  322 TYR A OH    
2291 N N     . THR A 329 ? 0.16886 0.35972 0.31942 0.04170  0.04966  0.06137  323 THR A N     
2292 C CA    . THR A 329 ? 0.17187 0.34509 0.34410 0.02778  0.04962  0.04908  323 THR A CA    
2293 C C     . THR A 329 ? 0.17707 0.32151 0.31991 0.03842  0.08465  0.02646  323 THR A C     
2294 O O     . THR A 329 ? 0.18957 0.31196 0.35174 0.01837  0.08362  0.04595  323 THR A O     
2295 C CB    . THR A 329 ? 0.18558 0.35408 0.35434 0.03376  0.00669  0.04461  323 THR A CB    
2296 O OG1   . THR A 329 ? 0.17501 0.34926 0.37505 0.05756  0.01137  0.04246  323 THR A OG1   
2297 C CG2   . THR A 329 ? 0.19991 0.37080 0.34154 0.02396  0.04412  0.04354  323 THR A CG2   
2298 N N     . ARG A 330 ? 0.17830 0.31675 0.30474 0.06304  0.05084  0.04220  324 ARG A N     
2299 C CA    . ARG A 330 ? 0.17882 0.32285 0.24598 0.05355  0.06410  0.02937  324 ARG A CA    
2300 C C     . ARG A 330 ? 0.17468 0.32123 0.29416 0.03987  0.03303  0.01852  324 ARG A C     
2301 O O     . ARG A 330 ? 0.19013 0.34878 0.28518 0.03171  0.06263  0.01469  324 ARG A O     
2302 C CB    . ARG A 330 ? 0.19140 0.33304 0.21112 0.03780  0.06182  0.05862  324 ARG A CB    
2303 C CG    . ARG A 330 ? 0.20178 0.34073 0.22408 0.03467  0.07405  0.05095  324 ARG A CG    
2304 C CD    . ARG A 330 ? 0.21233 0.35873 0.22686 0.02195  0.09929  0.04226  324 ARG A CD    
2305 N NE    . ARG A 330 ? 0.22835 0.37897 0.34202 0.01792  0.10030  0.03705  324 ARG A NE    
2306 C CZ    . ARG A 330 ? 0.25038 0.38999 0.35288 0.02401  0.12709  0.02791  324 ARG A CZ    
2307 N NH1   . ARG A 330 ? 0.25144 0.37700 0.41654 0.04132  0.12159  0.05406  324 ARG A NH1   
2308 N NH2   . ARG A 330 ? 0.26748 0.40378 0.34622 0.00969  0.15993  -0.00656 324 ARG A NH2   
2309 N N     . GLU A 331 ? 0.14869 0.29992 0.35010 0.04801  0.01218  0.03789  325 GLU A N     
2310 C CA    . GLU A 331 ? 0.15010 0.32242 0.39726 0.05428  -0.00704 0.04579  325 GLU A CA    
2311 C C     . GLU A 331 ? 0.14367 0.31976 0.35653 0.05288  0.00939  0.03096  325 GLU A C     
2312 O O     . GLU A 331 ? 0.13920 0.31462 0.34726 0.06128  -0.00193 0.02929  325 GLU A O     
2313 C CB    . GLU A 331 ? 0.17464 0.33744 0.44424 0.04761  -0.03072 0.04556  325 GLU A CB    
2314 N N     . LEU A 332 ? 0.14989 0.32989 0.34179 0.04477  0.01320  0.02055  326 LEU A N     
2315 C CA    . LEU A 332 ? 0.14979 0.34018 0.30482 0.05389  -0.00142 0.02014  326 LEU A CA    
2316 C C     . LEU A 332 ? 0.15284 0.32022 0.31601 0.05218  0.01977  0.02048  326 LEU A C     
2317 O O     . LEU A 332 ? 0.15051 0.30491 0.33798 0.05571  0.06200  0.03742  326 LEU A O     
2318 C CB    . LEU A 332 ? 0.16061 0.36875 0.28293 0.06898  -0.04033 0.04275  326 LEU A CB    
2319 C CG    . LEU A 332 ? 0.19600 0.39001 0.33084 0.08027  -0.05851 0.04766  326 LEU A CG    
2320 C CD1   . LEU A 332 ? 0.20184 0.40432 0.32616 0.08655  -0.04837 0.03333  326 LEU A CD1   
2321 C CD2   . LEU A 332 ? 0.20264 0.39538 0.36573 0.09070  -0.07565 0.06037  326 LEU A CD2   
2322 N N     . GLY A 333 ? 0.14028 0.30441 0.28806 0.04475  0.01634  0.01136  327 GLY A N     
2323 C CA    . GLY A 333 ? 0.15474 0.29647 0.28915 0.02757  0.01237  0.01050  327 GLY A CA    
2324 C C     . GLY A 333 ? 0.16234 0.29001 0.30107 0.03480  0.02288  -0.00027 327 GLY A C     
2325 O O     . GLY A 333 ? 0.17990 0.29463 0.26813 0.02572  0.01644  -0.03532 327 GLY A O     
2326 N N     . ILE A 334 ? 0.16679 0.28019 0.29880 0.04892  0.04705  0.01265  328 ILE A N     
2327 C CA    . ILE A 334 ? 0.16012 0.28481 0.32631 0.04372  0.07258  0.02588  328 ILE A CA    
2328 C C     . ILE A 334 ? 0.17165 0.28429 0.34565 0.03844  0.07496  0.04506  328 ILE A C     
2329 O O     . ILE A 334 ? 0.18148 0.26042 0.37385 0.03642  0.08407  0.00311  328 ILE A O     
2330 C CB    . ILE A 334 ? 0.16404 0.29978 0.33069 0.03508  0.11501  0.01949  328 ILE A CB    
2331 C CG1   . ILE A 334 ? 0.16206 0.31530 0.32386 0.01676  0.10932  0.03786  328 ILE A CG1   
2332 C CG2   . ILE A 334 ? 0.18085 0.30748 0.34604 0.03600  0.12195  0.01083  328 ILE A CG2   
2333 C CD1   . ILE A 334 ? 0.17623 0.32764 0.34212 -0.01319 0.11242  0.02480  328 ILE A CD1   
2334 N N     . GLU A 335 ? 0.16026 0.29286 0.34439 0.04685  0.03542  0.04730  329 GLU A N     
2335 C CA    . GLU A 335 ? 0.16471 0.30708 0.38216 0.05301  0.02376  0.03220  329 GLU A CA    
2336 C C     . GLU A 335 ? 0.15952 0.30435 0.39803 0.05099  0.03197  0.01517  329 GLU A C     
2337 O O     . GLU A 335 ? 0.15315 0.29751 0.42187 0.06937  0.02346  0.00246  329 GLU A O     
2338 C CB    . GLU A 335 ? 0.19704 0.31092 0.37026 0.05443  0.02601  0.04674  329 GLU A CB    
2339 N N     . ALA A 336 ? 0.13922 0.31350 0.39962 0.04947  0.03411  0.02775  330 ALA A N     
2340 C CA    . ALA A 336 ? 0.15412 0.30040 0.34935 0.04861  0.03991  0.01150  330 ALA A CA    
2341 C C     . ALA A 336 ? 0.17347 0.28124 0.34090 0.05424  0.04649  0.00263  330 ALA A C     
2342 O O     . ALA A 336 ? 0.17587 0.27078 0.34308 0.04947  0.07529  0.01934  330 ALA A O     
2343 C CB    . ALA A 336 ? 0.15762 0.30631 0.32756 0.04490  0.07698  0.03304  330 ALA A CB    
2344 N N     . VAL A 337 ? 0.18746 0.27191 0.31869 0.06392  0.05568  -0.00639 331 VAL A N     
2345 C CA    . VAL A 337 ? 0.20918 0.25680 0.32287 0.03558  0.07212  -0.02746 331 VAL A CA    
2346 C C     . VAL A 337 ? 0.22872 0.26016 0.36305 0.01416  0.08836  -0.03628 331 VAL A C     
2347 O O     . VAL A 337 ? 0.24892 0.23664 0.37550 -0.02495 0.08577  -0.05198 331 VAL A O     
2348 C CB    . VAL A 337 ? 0.22366 0.25716 0.30780 0.03403  0.07248  -0.04473 331 VAL A CB    
2349 C CG1   . VAL A 337 ? 0.21811 0.24180 0.28933 0.02435  0.06978  -0.07466 331 VAL A CG1   
2350 C CG2   . VAL A 337 ? 0.22902 0.27204 0.34656 0.04094  0.07557  -0.04216 331 VAL A CG2   
2351 N N     . ALA A 338 ? 0.21042 0.25874 0.35381 0.04130  0.12032  -0.01314 332 ALA A N     
2352 C CA    . ALA A 338 ? 0.22538 0.26192 0.37123 0.03837  0.13919  0.01587  332 ALA A CA    
2353 C C     . ALA A 338 ? 0.24817 0.26221 0.40235 0.05060  0.12507  0.02339  332 ALA A C     
2354 O O     . ALA A 338 ? 0.27465 0.26999 0.45129 0.03678  0.10163  0.01859  332 ALA A O     
2355 C CB    . ALA A 338 ? 0.22773 0.27238 0.40087 0.03617  0.13583  0.02120  332 ALA A CB    
2356 N N     . GLN A 339 ? 0.23312 0.26379 0.37610 0.06806  0.14429  0.04060  333 GLN A N     
2357 C CA    . GLN A 339 ? 0.24941 0.29424 0.40784 0.05727  0.12900  0.06507  333 GLN A CA    
2358 C C     . GLN A 339 ? 0.25612 0.27016 0.41406 0.04660  0.12565  0.06876  333 GLN A C     
2359 O O     . GLN A 339 ? 0.28075 0.28260 0.49049 0.05049  0.14048  0.05495  333 GLN A O     
2360 C CB    . GLN A 339 ? 0.26716 0.35747 0.47217 0.04303  0.12567  0.08482  333 GLN A CB    
2361 C CG    . GLN A 339 ? 0.30161 0.41880 0.56965 0.05544  0.11109  0.08312  333 GLN A CG    
2362 C CD    . GLN A 339 ? 0.33734 0.47959 0.68403 0.05791  0.10675  0.10005  333 GLN A CD    
2363 O OE1   . GLN A 339 ? 0.36235 0.49954 0.72639 0.05902  0.07844  0.10076  333 GLN A OE1   
2364 N NE2   . GLN A 339 ? 0.35512 0.50310 0.70888 0.06667  0.11210  0.10658  333 GLN A NE2   
2365 N N     . GLY A 340 ? 0.20471 0.25375 0.39538 0.04857  0.13329  0.04491  334 GLY A N     
2366 C CA    . GLY A 340 ? 0.19560 0.26337 0.39356 0.04137  0.12742  0.05206  334 GLY A CA    
2367 C C     . GLY A 340 ? 0.16893 0.26293 0.40665 0.05705  0.10232  0.06739  334 GLY A C     
2368 O O     . GLY A 340 ? 0.16914 0.28517 0.44739 0.05713  0.08836  0.06895  334 GLY A O     
2369 N N     . ASP A 341 ? 0.15888 0.26406 0.39994 0.05284  0.06985  0.04988  335 ASP A N     
2370 C CA    . ASP A 341 ? 0.15681 0.27922 0.37371 0.03713  0.05619  0.05642  335 ASP A CA    
2371 C C     . ASP A 341 ? 0.14004 0.26415 0.33191 0.02301  0.05071  0.04982  335 ASP A C     
2372 O O     . ASP A 341 ? 0.14481 0.26154 0.33344 -0.00271 0.05793  0.04890  335 ASP A O     
2373 C CB    . ASP A 341 ? 0.18091 0.31447 0.42091 0.02467  0.03607  0.05051  335 ASP A CB    
2374 C CG    . ASP A 341 ? 0.23222 0.36274 0.49898 0.00150  0.04685  0.07917  335 ASP A CG    
2375 O OD1   . ASP A 341 ? 0.25725 0.36801 0.49056 0.00523  0.06145  0.10944  335 ASP A OD1   
2376 O OD2   . ASP A 341 ? 0.24804 0.39987 0.51815 0.01397  0.04519  0.08047  335 ASP A OD2   
2377 N N     . ALA A 342 ? 0.13317 0.24648 0.31430 0.03943  0.02897  0.01576  336 ALA A N     
2378 C CA    . ALA A 342 ? 0.12646 0.21127 0.30330 0.04914  0.00909  -0.01336 336 ALA A CA    
2379 C C     . ALA A 342 ? 0.12830 0.19133 0.30230 0.04298  0.02366  0.00034  336 ALA A C     
2380 O O     . ALA A 342 ? 0.15911 0.21222 0.33569 0.04609  0.02316  0.00222  336 ALA A O     
2381 C CB    . ALA A 342 ? 0.14840 0.23321 0.33082 0.03573  -0.01075 -0.00811 336 ALA A CB    
2382 N N     . ASP A 343 ? 0.12561 0.17916 0.30617 0.00773  0.03004  0.00485  337 ASP A N     
2383 C CA    . ASP A 343 ? 0.14124 0.17295 0.30650 -0.00810 0.01020  0.00650  337 ASP A CA    
2384 C C     . ASP A 343 ? 0.14773 0.18082 0.29700 0.00877  -0.00715 -0.00633 337 ASP A C     
2385 O O     . ASP A 343 ? 0.18388 0.17708 0.28786 0.01209  0.02145  -0.00034 337 ASP A O     
2386 C CB    . ASP A 343 ? 0.15665 0.19117 0.29524 0.00427  0.01279  -0.00470 337 ASP A CB    
2387 C CG    . ASP A 343 ? 0.17204 0.20570 0.28068 0.00652  0.02840  -0.01216 337 ASP A CG    
2388 O OD1   . ASP A 343 ? 0.17437 0.20312 0.26355 0.01133  0.04805  -0.04133 337 ASP A OD1   
2389 O OD2   . ASP A 343 ? 0.17472 0.20916 0.21300 -0.00044 0.03957  -0.00322 337 ASP A OD2   
2390 N N     . LEU A 344 ? 0.13169 0.19742 0.25246 0.00008  -0.02764 -0.02718 338 LEU A N     
2391 C CA    . LEU A 344 ? 0.10381 0.20405 0.25489 0.01091  -0.02357 -0.00809 338 LEU A CA    
2392 C C     . LEU A 344 ? 0.10482 0.20285 0.22883 0.00460  0.00854  -0.01803 338 LEU A C     
2393 O O     . LEU A 344 ? 0.10062 0.23330 0.27267 0.00437  -0.02538 -0.00310 338 LEU A O     
2394 C CB    . LEU A 344 ? 0.09869 0.24055 0.23357 0.01789  -0.02174 -0.00467 338 LEU A CB    
2395 C CG    . LEU A 344 ? 0.12766 0.25698 0.22396 0.03572  0.02219  0.00561  338 LEU A CG    
2396 C CD1   . LEU A 344 ? 0.10800 0.24887 0.22162 0.03827  -0.00430 0.00667  338 LEU A CD1   
2397 C CD2   . LEU A 344 ? 0.15282 0.25158 0.24181 0.04176  0.04101  0.04023  338 LEU A CD2   
2398 N N     . VAL A 345 ? 0.09915 0.20961 0.24835 -0.01639 0.00507  -0.02510 339 VAL A N     
2399 C CA    . VAL A 345 ? 0.10051 0.19302 0.28730 -0.02242 0.00248  -0.01771 339 VAL A CA    
2400 C C     . VAL A 345 ? 0.10378 0.20240 0.26877 -0.00944 -0.01988 0.00104  339 VAL A C     
2401 O O     . VAL A 345 ? 0.10135 0.19853 0.24387 -0.02392 0.01828  0.02942  339 VAL A O     
2402 C CB    . VAL A 345 ? 0.10442 0.19421 0.31252 -0.01735 0.01991  -0.01171 339 VAL A CB    
2403 C CG1   . VAL A 345 ? 0.12132 0.21510 0.27718 -0.01442 0.00796  -0.02425 339 VAL A CG1   
2404 C CG2   . VAL A 345 ? 0.10358 0.20368 0.34596 -0.00568 0.03700  -0.04973 339 VAL A CG2   
2405 N N     . SER A 346 ? 0.10122 0.19898 0.22502 0.00152  -0.01462 0.00465  340 SER A N     
2406 C CA    . SER A 346 ? 0.10166 0.21154 0.22133 -0.00247 -0.02378 -0.01166 340 SER A CA    
2407 C C     . SER A 346 ? 0.09795 0.21401 0.22096 -0.00280 -0.00621 0.00803  340 SER A C     
2408 O O     . SER A 346 ? 0.14267 0.20563 0.23727 -0.01739 -0.01057 0.00075  340 SER A O     
2409 C CB    . SER A 346 ? 0.11704 0.23545 0.23119 -0.01980 0.00994  0.00519  340 SER A CB    
2410 O OG    . SER A 346 ? 0.10026 0.25942 0.24956 -0.01661 0.02818  -0.00980 340 SER A OG    
2411 N N     . TYR A 347 ? 0.07938 0.20790 0.25591 -0.01507 0.00952  -0.02371 341 TYR A N     
2412 C CA    . TYR A 347 ? 0.08058 0.20519 0.25718 -0.01269 0.01571  -0.05010 341 TYR A CA    
2413 C C     . TYR A 347 ? 0.07908 0.21542 0.27238 -0.01381 0.02217  -0.03175 341 TYR A C     
2414 O O     . TYR A 347 ? 0.07347 0.22036 0.27236 -0.00953 0.01196  -0.01752 341 TYR A O     
2415 C CB    . TYR A 347 ? 0.08829 0.19526 0.27363 -0.00141 0.03396  -0.04879 341 TYR A CB    
2416 C CG    . TYR A 347 ? 0.10973 0.20334 0.26058 0.02745  0.01981  -0.01269 341 TYR A CG    
2417 C CD1   . TYR A 347 ? 0.13407 0.20655 0.21334 0.03443  0.02729  -0.00875 341 TYR A CD1   
2418 C CD2   . TYR A 347 ? 0.12133 0.21362 0.25456 0.05006  0.00797  0.02192  341 TYR A CD2   
2419 C CE1   . TYR A 347 ? 0.13855 0.21936 0.21404 0.03662  0.03335  -0.00415 341 TYR A CE1   
2420 C CE2   . TYR A 347 ? 0.12361 0.21230 0.26612 0.06356  -0.00236 0.01059  341 TYR A CE2   
2421 C CZ    . TYR A 347 ? 0.13208 0.21712 0.26288 0.04983  0.00873  -0.00053 341 TYR A CZ    
2422 O OH    . TYR A 347 ? 0.14167 0.20454 0.26589 0.02606  0.04000  0.01764  341 TYR A OH    
2423 N N     . GLY A 348 ? 0.08616 0.20022 0.27217 -0.02100 0.02113  -0.05960 342 GLY A N     
2424 C CA    . GLY A 348 ? 0.10102 0.20196 0.28439 -0.02502 0.02472  -0.06019 342 GLY A CA    
2425 C C     . GLY A 348 ? 0.08630 0.21067 0.28523 -0.03071 0.02030  -0.03311 342 GLY A C     
2426 O O     . GLY A 348 ? 0.10523 0.20939 0.31465 -0.03866 0.03751  -0.04352 342 GLY A O     
2427 N N     . ARG A 349 ? 0.07411 0.21411 0.21259 -0.03087 -0.01600 -0.03207 343 ARG A N     
2428 C CA    . ARG A 349 ? 0.09216 0.23655 0.20140 -0.03028 -0.02288 -0.04123 343 ARG A CA    
2429 C C     . ARG A 349 ? 0.09860 0.22840 0.22282 0.00845  -0.01256 -0.04031 343 ARG A C     
2430 O O     . ARG A 349 ? 0.10658 0.21055 0.25640 0.01700  -0.00061 -0.03265 343 ARG A O     
2431 C CB    . ARG A 349 ? 0.10312 0.26144 0.23422 -0.01396 -0.02401 -0.02192 343 ARG A CB    
2432 C CG    . ARG A 349 ? 0.12384 0.28417 0.20845 -0.01966 -0.01672 -0.02890 343 ARG A CG    
2433 C CD    . ARG A 349 ? 0.15536 0.31158 0.25306 -0.01696 -0.02093 -0.01341 343 ARG A CD    
2434 N NE    . ARG A 349 ? 0.17487 0.32367 0.26388 0.01594  -0.01290 0.01498  343 ARG A NE    
2435 C CZ    . ARG A 349 ? 0.19295 0.34827 0.31664 0.00031  -0.04708 -0.02631 343 ARG A CZ    
2436 N NH1   . ARG A 349 ? 0.21323 0.35965 0.34549 -0.01145 -0.10551 -0.04489 343 ARG A NH1   
2437 N NH2   . ARG A 349 ? 0.20237 0.35771 0.36441 0.00349  -0.02966 -0.03775 343 ARG A NH2   
2438 N N     . LEU A 350 ? 0.09246 0.23413 0.23249 0.02248  -0.00263 -0.04188 344 LEU A N     
2439 C CA    . LEU A 350 ? 0.09688 0.24847 0.26256 0.03435  0.01193  -0.03843 344 LEU A CA    
2440 C C     . LEU A 350 ? 0.08529 0.24429 0.24946 0.02308  0.01889  -0.01582 344 LEU A C     
2441 O O     . LEU A 350 ? 0.11416 0.25185 0.23380 0.01169  -0.01242 -0.01545 344 LEU A O     
2442 C CB    . LEU A 350 ? 0.09898 0.24222 0.26445 0.05495  0.03400  -0.02253 344 LEU A CB    
2443 C CG    . LEU A 350 ? 0.10575 0.23451 0.28406 0.02349  0.01568  -0.01281 344 LEU A CG    
2444 C CD1   . LEU A 350 ? 0.14145 0.23000 0.34037 0.04371  0.00341  0.02214  344 LEU A CD1   
2445 C CD2   . LEU A 350 ? 0.07740 0.22804 0.27708 0.00041  0.02757  -0.01373 344 LEU A CD2   
2446 N N     . PHE A 351 ? 0.07369 0.22815 0.24351 0.01582  0.02456  -0.02361 345 PHE A N     
2447 C CA    . PHE A 351 ? 0.09606 0.20813 0.27378 -0.00731 0.00558  -0.02434 345 PHE A CA    
2448 C C     . PHE A 351 ? 0.13435 0.20637 0.25058 -0.01178 0.01151  -0.02773 345 PHE A C     
2449 O O     . PHE A 351 ? 0.14792 0.19133 0.26566 -0.00836 -0.00368 -0.03785 345 PHE A O     
2450 C CB    . PHE A 351 ? 0.10316 0.20685 0.24819 -0.02329 -0.02172 -0.02586 345 PHE A CB    
2451 C CG    . PHE A 351 ? 0.12663 0.18844 0.23220 -0.01269 -0.01639 -0.01051 345 PHE A CG    
2452 C CD1   . PHE A 351 ? 0.13128 0.20463 0.21730 0.01141  0.00540  -0.01493 345 PHE A CD1   
2453 C CD2   . PHE A 351 ? 0.13421 0.19698 0.25492 -0.01328 0.01739  -0.03304 345 PHE A CD2   
2454 C CE1   . PHE A 351 ? 0.14314 0.20509 0.26109 0.01155  -0.00891 -0.04189 345 PHE A CE1   
2455 C CE2   . PHE A 351 ? 0.14090 0.18634 0.21750 -0.01046 0.00723  -0.05705 345 PHE A CE2   
2456 C CZ    . PHE A 351 ? 0.15328 0.19297 0.24504 0.01493  -0.00351 -0.08407 345 PHE A CZ    
2457 N N     . ILE A 352 ? 0.15057 0.19563 0.22579 -0.02431 0.00873  -0.04316 346 ILE A N     
2458 C CA    . ILE A 352 ? 0.13992 0.22874 0.19289 -0.03200 0.00112  -0.02331 346 ILE A CA    
2459 C C     . ILE A 352 ? 0.10733 0.21679 0.23682 -0.01933 -0.00226 0.00744  346 ILE A C     
2460 O O     . ILE A 352 ? 0.09703 0.20566 0.25937 -0.01764 -0.01543 0.01818  346 ILE A O     
2461 C CB    . ILE A 352 ? 0.14023 0.24670 0.18891 -0.03173 0.00600  -0.03200 346 ILE A CB    
2462 C CG1   . ILE A 352 ? 0.15632 0.25070 0.18589 -0.05738 0.01804  -0.03700 346 ILE A CG1   
2463 C CG2   . ILE A 352 ? 0.12119 0.23928 0.19529 -0.02693 -0.03764 -0.00922 346 ILE A CG2   
2464 C CD1   . ILE A 352 ? 0.18743 0.25539 0.23660 -0.07115 0.00790  -0.03757 346 ILE A CD1   
2465 N N     . SER A 353 ? 0.10182 0.21926 0.22892 -0.00546 -0.01293 -0.00491 347 SER A N     
2466 C CA    . SER A 353 ? 0.09381 0.22532 0.23228 -0.00108 -0.01042 -0.00300 347 SER A CA    
2467 C C     . SER A 353 ? 0.10298 0.22382 0.23193 -0.02005 -0.03648 -0.00793 347 SER A C     
2468 O O     . SER A 353 ? 0.11503 0.21260 0.26779 -0.04429 -0.02198 0.02542  347 SER A O     
2469 C CB    . SER A 353 ? 0.09787 0.20891 0.25438 0.00814  -0.01103 0.02598  347 SER A CB    
2470 O OG    . SER A 353 ? 0.12135 0.19674 0.27172 0.01633  0.01832  0.01826  347 SER A OG    
2471 N N     . ASN A 354 ? 0.11680 0.20933 0.21446 -0.00129 -0.02025 -0.05260 348 ASN A N     
2472 C CA    . ASN A 354 ? 0.10773 0.21339 0.21660 -0.00405 -0.04540 -0.02391 348 ASN A CA    
2473 C C     . ASN A 354 ? 0.10427 0.21634 0.25659 -0.00947 -0.01629 -0.00039 348 ASN A C     
2474 O O     . ASN A 354 ? 0.08962 0.21494 0.26600 -0.00809 -0.01308 0.00274  348 ASN A O     
2475 C CB    . ASN A 354 ? 0.11087 0.22463 0.24022 -0.00552 -0.00778 -0.05230 348 ASN A CB    
2476 C CG    . ASN A 354 ? 0.12421 0.22959 0.26235 -0.00877 -0.04151 -0.02247 348 ASN A CG    
2477 O OD1   . ASN A 354 ? 0.11671 0.24974 0.23499 -0.01580 -0.06479 -0.00212 348 ASN A OD1   
2478 N ND2   . ASN A 354 ? 0.12667 0.19872 0.23432 -0.00739 -0.02774 -0.01926 348 ASN A ND2   
2479 N N     . PRO A 355 ? 0.10774 0.21611 0.27188 -0.01574 0.00274  -0.01752 349 PRO A N     
2480 C CA    . PRO A 355 ? 0.12539 0.21711 0.22981 -0.02868 -0.02964 0.00241  349 PRO A CA    
2481 C C     . PRO A 355 ? 0.14415 0.21228 0.22255 -0.01752 -0.01556 -0.01513 349 PRO A C     
2482 O O     . PRO A 355 ? 0.13665 0.19509 0.22573 -0.03488 -0.02617 -0.02720 349 PRO A O     
2483 C CB    . PRO A 355 ? 0.13511 0.21546 0.33108 -0.02966 -0.03918 0.00633  349 PRO A CB    
2484 C CG    . PRO A 355 ? 0.13329 0.22874 0.40404 -0.02510 -0.02436 0.01484  349 PRO A CG    
2485 C CD    . PRO A 355 ? 0.09947 0.21473 0.33444 -0.00398 0.02282  0.01622  349 PRO A CD    
2486 N N     . ASP A 356 ? 0.14805 0.22514 0.20966 -0.01322 0.02183  -0.01202 350 ASP A N     
2487 C CA    . ASP A 356 ? 0.14746 0.22768 0.22680 -0.00941 0.04034  0.00447  350 ASP A CA    
2488 C C     . ASP A 356 ? 0.14414 0.21050 0.24220 0.00089  0.03953  0.00451  350 ASP A C     
2489 O O     . ASP A 356 ? 0.14611 0.21336 0.26393 -0.00473 0.02018  -0.01439 350 ASP A O     
2490 C CB    . ASP A 356 ? 0.13379 0.26515 0.27461 -0.02468 0.03338  -0.00870 350 ASP A CB    
2491 C CG    . ASP A 356 ? 0.15282 0.28481 0.30704 -0.02818 0.05973  -0.01164 350 ASP A CG    
2492 O OD1   . ASP A 356 ? 0.14393 0.30286 0.33239 -0.03272 0.04081  0.00519  350 ASP A OD1   
2493 O OD2   . ASP A 356 ? 0.17467 0.28771 0.34790 -0.03290 0.05289  -0.00821 350 ASP A OD2   
2494 N N     . LEU A 357 ? 0.12831 0.19013 0.24987 -0.00628 0.01044  0.03309  351 LEU A N     
2495 C CA    . LEU A 357 ? 0.12538 0.20945 0.24741 -0.01926 0.00652  0.02528  351 LEU A CA    
2496 C C     . LEU A 357 ? 0.12893 0.21456 0.21509 -0.01071 0.00967  -0.00407 351 LEU A C     
2497 O O     . LEU A 357 ? 0.14101 0.20902 0.25129 0.00936  0.00003  0.00762  351 LEU A O     
2498 C CB    . LEU A 357 ? 0.13045 0.22643 0.20029 -0.01629 -0.00184 0.01718  351 LEU A CB    
2499 C CG    . LEU A 357 ? 0.09575 0.24693 0.24466 -0.01118 -0.01695 0.04437  351 LEU A CG    
2500 C CD1   . LEU A 357 ? 0.08642 0.25032 0.27124 -0.01097 -0.03049 0.02741  351 LEU A CD1   
2501 C CD2   . LEU A 357 ? 0.09663 0.25616 0.22518 -0.00597 0.00764  0.05253  351 LEU A CD2   
2502 N N     . VAL A 358 ? 0.11946 0.23204 0.19376 -0.02757 -0.02387 -0.02402 352 VAL A N     
2503 C CA    . VAL A 358 ? 0.13287 0.24276 0.16902 -0.03322 0.00134  -0.03277 352 VAL A CA    
2504 C C     . VAL A 358 ? 0.12568 0.26076 0.24648 -0.03158 -0.00228 -0.01056 352 VAL A C     
2505 O O     . VAL A 358 ? 0.12489 0.25626 0.27687 -0.01036 -0.00927 0.00507  352 VAL A O     
2506 C CB    . VAL A 358 ? 0.14409 0.24933 0.19857 -0.01400 0.01800  -0.02580 352 VAL A CB    
2507 C CG1   . VAL A 358 ? 0.15887 0.26812 0.24978 -0.01112 0.00780  -0.05207 352 VAL A CG1   
2508 C CG2   . VAL A 358 ? 0.13811 0.24922 0.19548 -0.00120 0.02953  -0.02077 352 VAL A CG2   
2509 N N     . MET A 359 ? 0.12311 0.28236 0.25074 -0.05600 0.00959  0.00041  353 MET A N     
2510 C CA    . MET A 359 ? 0.12021 0.31370 0.26413 -0.03449 0.00540  -0.01032 353 MET A CA    
2511 C C     . MET A 359 ? 0.11202 0.29671 0.25572 -0.01658 -0.01185 -0.02977 353 MET A C     
2512 O O     . MET A 359 ? 0.10350 0.29946 0.27549 -0.00366 -0.02102 -0.02764 353 MET A O     
2513 C CB    . MET A 359 ? 0.17909 0.37590 0.35018 -0.05301 0.03884  -0.02770 353 MET A CB    
2514 C CG    . MET A 359 ? 0.26144 0.45460 0.42085 -0.04626 0.05877  -0.07349 353 MET A CG    
2515 S SD    . MET A 359 ? 0.33585 0.53552 0.48016 -0.03742 0.09525  -0.07028 353 MET A SD    
2516 C CE    . MET A 359 ? 0.33145 0.53804 0.49886 -0.03885 0.05509  -0.07733 353 MET A CE    
2517 N N     . ARG A 360 ? 0.11459 0.27957 0.25875 -0.01347 0.00046  -0.04553 354 ARG A N     
2518 C CA    . ARG A 360 ? 0.13423 0.27069 0.28258 -0.00605 0.01370  -0.05022 354 ARG A CA    
2519 C C     . ARG A 360 ? 0.13752 0.27635 0.30233 -0.01456 0.02133  -0.05189 354 ARG A C     
2520 O O     . ARG A 360 ? 0.11338 0.28780 0.32433 -0.01832 -0.00424 -0.05763 354 ARG A O     
2521 C CB    . ARG A 360 ? 0.14312 0.25103 0.24741 0.00613  0.02823  -0.04730 354 ARG A CB    
2522 C CG    . ARG A 360 ? 0.15610 0.24130 0.28100 0.01579  0.00668  -0.04025 354 ARG A CG    
2523 C CD    . ARG A 360 ? 0.18402 0.24394 0.30511 0.02378  0.02243  -0.02863 354 ARG A CD    
2524 N NE    . ARG A 360 ? 0.20512 0.24638 0.27202 0.02058  0.00585  -0.00012 354 ARG A NE    
2525 C CZ    . ARG A 360 ? 0.20402 0.27016 0.32096 0.01993  -0.01447 -0.00433 354 ARG A CZ    
2526 N NH1   . ARG A 360 ? 0.18097 0.27381 0.34327 0.00726  -0.00999 -0.01423 354 ARG A NH1   
2527 N NH2   . ARG A 360 ? 0.22757 0.27257 0.35545 0.02239  -0.00756 -0.03671 354 ARG A NH2   
2528 N N     . ILE A 361 ? 0.15951 0.26236 0.29147 -0.03989 0.01869  -0.04804 355 ILE A N     
2529 C CA    . ILE A 361 ? 0.16253 0.27050 0.28282 -0.01132 0.03515  -0.04132 355 ILE A CA    
2530 C C     . ILE A 361 ? 0.16110 0.29701 0.27848 -0.01065 0.02007  -0.03052 355 ILE A C     
2531 O O     . ILE A 361 ? 0.16672 0.30239 0.31414 -0.00558 -0.00301 -0.01115 355 ILE A O     
2532 C CB    . ILE A 361 ? 0.18622 0.25027 0.27884 -0.01460 0.05298  -0.00524 355 ILE A CB    
2533 C CG1   . ILE A 361 ? 0.20083 0.25134 0.31542 0.00210  0.04895  0.00792  355 ILE A CG1   
2534 C CG2   . ILE A 361 ? 0.19712 0.24542 0.33224 -0.00646 0.02814  -0.00256 355 ILE A CG2   
2535 C CD1   . ILE A 361 ? 0.19136 0.25783 0.28176 0.01079  0.06500  0.01830  355 ILE A CD1   
2536 N N     . LYS A 362 ? 0.15037 0.31090 0.23119 -0.02591 0.02810  -0.01083 356 LYS A N     
2537 C CA    . LYS A 362 ? 0.18638 0.34664 0.25295 -0.00581 0.02656  -0.02320 356 LYS A CA    
2538 C C     . LYS A 362 ? 0.19113 0.33403 0.29370 0.00702  0.04802  -0.02531 356 LYS A C     
2539 O O     . LYS A 362 ? 0.20699 0.31693 0.35977 0.00528  0.07207  -0.05699 356 LYS A O     
2540 C CB    . LYS A 362 ? 0.21597 0.39606 0.24806 0.02064  -0.03245 -0.03091 356 LYS A CB    
2541 C CG    . LYS A 362 ? 0.26059 0.44667 0.36704 0.02630  -0.09035 -0.04016 356 LYS A CG    
2542 C CD    . LYS A 362 ? 0.30842 0.48775 0.41372 0.03521  -0.09199 -0.06358 356 LYS A CD    
2543 C CE    . LYS A 362 ? 0.33808 0.51572 0.47706 0.05114  -0.04977 -0.07343 356 LYS A CE    
2544 N NZ    . LYS A 362 ? 0.36306 0.53590 0.50186 0.05669  -0.03476 -0.07789 356 LYS A NZ    
2545 N N     . LEU A 363 ? 0.20369 0.34613 0.32047 0.02227  0.03885  0.01112  357 LEU A N     
2546 C CA    . LEU A 363 ? 0.18441 0.34880 0.30490 0.01737  0.05966  0.00307  357 LEU A CA    
2547 C C     . LEU A 363 ? 0.17648 0.34754 0.29258 0.01204  0.06302  -0.01485 357 LEU A C     
2548 O O     . LEU A 363 ? 0.18585 0.36387 0.28014 0.01296  0.06396  -0.02734 357 LEU A O     
2549 C CB    . LEU A 363 ? 0.19120 0.34481 0.27704 0.01295  0.06057  0.03099  357 LEU A CB    
2550 C CG    . LEU A 363 ? 0.23496 0.36449 0.30165 0.02105  0.05314  0.01429  357 LEU A CG    
2551 C CD1   . LEU A 363 ? 0.23303 0.37244 0.30798 0.01616  0.06663  0.03852  357 LEU A CD1   
2552 C CD2   . LEU A 363 ? 0.25734 0.38218 0.28630 0.02661  0.05350  0.00243  357 LEU A CD2   
2553 N N     . ASN A 364 ? 0.16978 0.34319 0.27708 0.00171  0.06741  -0.03773 358 ASN A N     
2554 C CA    . ASN A 364 ? 0.15779 0.33323 0.30909 -0.00693 0.04769  -0.03275 358 ASN A CA    
2555 C C     . ASN A 364 ? 0.13617 0.32827 0.32640 -0.03310 0.04040  -0.04647 358 ASN A C     
2556 O O     . ASN A 364 ? 0.13011 0.32957 0.38763 -0.03906 0.04977  -0.03721 358 ASN A O     
2557 C CB    . ASN A 364 ? 0.17444 0.35017 0.34036 0.01375  0.05490  -0.01605 358 ASN A CB    
2558 C CG    . ASN A 364 ? 0.19428 0.37679 0.40991 0.02273  0.03510  0.00833  358 ASN A CG    
2559 O OD1   . ASN A 364 ? 0.19135 0.39069 0.38174 0.03022  0.00305  0.02583  358 ASN A OD1   
2560 N ND2   . ASN A 364 ? 0.22011 0.38752 0.48853 0.02656  0.02860  0.02415  358 ASN A ND2   
2561 N N     . ALA A 365 ? 0.14350 0.31411 0.25886 -0.04010 0.00769  -0.07585 359 ALA A N     
2562 C CA    . ALA A 365 ? 0.13220 0.32411 0.28439 -0.03054 0.00397  -0.06402 359 ALA A CA    
2563 C C     . ALA A 365 ? 0.13931 0.33138 0.33327 -0.02686 0.01144  -0.06446 359 ALA A C     
2564 O O     . ALA A 365 ? 0.14138 0.32214 0.37955 -0.03644 0.02214  -0.02082 359 ALA A O     
2565 C CB    . ALA A 365 ? 0.13779 0.33738 0.31291 -0.03509 -0.02951 -0.02574 359 ALA A CB    
2566 N N     . PRO A 366 ? 0.14409 0.35687 0.33554 -0.02707 0.03469  -0.08632 360 PRO A N     
2567 C CA    . PRO A 366 ? 0.15065 0.34917 0.32057 -0.02797 0.04573  -0.08955 360 PRO A CA    
2568 C C     . PRO A 366 ? 0.15581 0.32261 0.29899 -0.00514 0.05887  -0.05898 360 PRO A C     
2569 O O     . PRO A 366 ? 0.20697 0.31826 0.31269 -0.00158 0.08100  -0.02776 360 PRO A O     
2570 C CB    . PRO A 366 ? 0.16942 0.38503 0.33697 -0.06262 0.02139  -0.08763 360 PRO A CB    
2571 C CG    . PRO A 366 ? 0.20479 0.40690 0.39378 -0.06653 0.03911  -0.10438 360 PRO A CG    
2572 C CD    . PRO A 366 ? 0.18212 0.39015 0.35388 -0.05735 0.02534  -0.10174 360 PRO A CD    
2573 N N     . LEU A 367 ? 0.13551 0.29088 0.27786 -0.00052 0.04059  -0.05270 361 LEU A N     
2574 C CA    . LEU A 367 ? 0.09344 0.26469 0.24360 -0.01430 0.01351  -0.01599 361 LEU A CA    
2575 C C     . LEU A 367 ? 0.10579 0.25786 0.25245 -0.02586 0.01673  0.00349  361 LEU A C     
2576 O O     . LEU A 367 ? 0.09121 0.26237 0.24640 -0.04931 0.00239  0.02497  361 LEU A O     
2577 C CB    . LEU A 367 ? 0.08369 0.26257 0.24534 -0.02855 -0.00788 -0.00288 361 LEU A CB    
2578 C CG    . LEU A 367 ? 0.12451 0.25637 0.24483 -0.04564 -0.00955 -0.01366 361 LEU A CG    
2579 C CD1   . LEU A 367 ? 0.14763 0.26269 0.30247 -0.06268 0.03958  -0.00493 361 LEU A CD1   
2580 C CD2   . LEU A 367 ? 0.12334 0.26476 0.22625 -0.02694 -0.02010 -0.01678 361 LEU A CD2   
2581 N N     . ASN A 368 ? 0.10585 0.24977 0.23192 -0.02115 0.02379  -0.02170 362 ASN A N     
2582 C CA    . ASN A 368 ? 0.13243 0.27061 0.24529 -0.02384 -0.02281 0.00607  362 ASN A CA    
2583 C C     . ASN A 368 ? 0.11414 0.26072 0.23298 -0.00480 -0.00023 -0.01112 362 ASN A C     
2584 O O     . ASN A 368 ? 0.10593 0.24880 0.22686 -0.01837 -0.03860 0.02424  362 ASN A O     
2585 C CB    . ASN A 368 ? 0.13155 0.28374 0.25539 -0.00290 -0.02560 0.07744  362 ASN A CB    
2586 C CG    . ASN A 368 ? 0.14013 0.33930 0.32309 0.00108  -0.02227 0.07245  362 ASN A CG    
2587 O OD1   . ASN A 368 ? 0.15930 0.38202 0.36072 -0.01449 0.00075  0.05982  362 ASN A OD1   
2588 N ND2   . ASN A 368 ? 0.16066 0.34065 0.36071 -0.00364 -0.02716 0.09499  362 ASN A ND2   
2589 N N     . LYS A 369 ? 0.11906 0.26027 0.20461 0.00338  -0.02413 -0.03116 363 LYS A N     
2590 C CA    . LYS A 369 ? 0.12039 0.26394 0.23914 0.02306  -0.02249 -0.04421 363 LYS A CA    
2591 C C     . LYS A 369 ? 0.09977 0.26581 0.27457 0.02693  -0.00507 -0.04280 363 LYS A C     
2592 O O     . LYS A 369 ? 0.09722 0.24896 0.30880 0.01126  -0.02826 -0.01251 363 LYS A O     
2593 C CB    . LYS A 369 ? 0.12582 0.26584 0.28304 0.02670  -0.01602 -0.04989 363 LYS A CB    
2594 C CG    . LYS A 369 ? 0.15808 0.29341 0.34080 0.00138  -0.02916 -0.04606 363 LYS A CG    
2595 C CD    . LYS A 369 ? 0.21572 0.31846 0.47759 -0.00886 -0.03992 -0.07676 363 LYS A CD    
2596 C CE    . LYS A 369 ? 0.26289 0.36597 0.61280 -0.00312 0.00421  -0.05731 363 LYS A CE    
2597 N NZ    . LYS A 369 ? 0.29625 0.39403 0.70645 0.02382  0.02515  -0.04932 363 LYS A NZ    
2598 N N     . TYR A 370 ? 0.09973 0.26881 0.27624 0.03701  0.01615  -0.06435 364 TYR A N     
2599 C CA    . TYR A 370 ? 0.09493 0.28685 0.28259 0.04406  -0.00153 -0.04013 364 TYR A CA    
2600 C C     . TYR A 370 ? 0.11312 0.30902 0.28357 0.03734  -0.01638 -0.04096 364 TYR A C     
2601 O O     . TYR A 370 ? 0.13001 0.34788 0.28930 0.03677  -0.04498 -0.06351 364 TYR A O     
2602 C CB    . TYR A 370 ? 0.10247 0.31515 0.29723 0.04800  -0.00409 -0.01225 364 TYR A CB    
2603 C CG    . TYR A 370 ? 0.10929 0.34944 0.31358 0.02086  0.01633  0.01931  364 TYR A CG    
2604 C CD1   . TYR A 370 ? 0.10664 0.36424 0.34963 0.01244  0.03458  0.03483  364 TYR A CD1   
2605 C CD2   . TYR A 370 ? 0.10776 0.34944 0.35458 0.02266  0.00614  0.03867  364 TYR A CD2   
2606 C CE1   . TYR A 370 ? 0.11819 0.37384 0.37933 0.01514  0.04975  0.04093  364 TYR A CE1   
2607 C CE2   . TYR A 370 ? 0.12276 0.36086 0.37628 0.00363  0.00241  0.05025  364 TYR A CE2   
2608 C CZ    . TYR A 370 ? 0.14586 0.37634 0.40396 0.01011  0.02287  0.06316  364 TYR A CZ    
2609 O OH    . TYR A 370 ? 0.16937 0.39137 0.44291 0.00656  0.04046  0.06498  364 TYR A OH    
2610 N N     . ASN A 371 ? 0.14698 0.28216 0.28441 0.00984  -0.01096 -0.03178 365 ASN A N     
2611 C CA    A ASN A 371 ? 0.14684 0.27751 0.28962 -0.01258 0.01077  -0.02458 365 ASN A CA    
2612 C CA    B ASN A 371 ? 0.16475 0.28659 0.29291 -0.00396 0.00533  -0.02411 365 ASN A CA    
2613 C C     . ASN A 371 ? 0.14358 0.26330 0.27398 -0.00899 0.02274  -0.03888 365 ASN A C     
2614 O O     . ASN A 371 ? 0.14943 0.26134 0.31162 0.00734  -0.03784 -0.01708 365 ASN A O     
2615 C CB    A ASN A 371 ? 0.14672 0.28083 0.32575 -0.05167 0.00582  -0.00174 365 ASN A CB    
2616 C CB    B ASN A 371 ? 0.18925 0.30569 0.33393 -0.02299 -0.01045 -0.00475 365 ASN A CB    
2617 C CG    A ASN A 371 ? 0.17894 0.30526 0.39905 -0.07276 -0.00843 0.00363  365 ASN A CG    
2618 C CG    B ASN A 371 ? 0.21552 0.32641 0.40890 -0.02657 -0.02405 -0.00457 365 ASN A CG    
2619 O OD1   A ASN A 371 ? 0.16814 0.32764 0.43914 -0.10708 -0.01063 -0.00932 365 ASN A OD1   
2620 O OD1   B ASN A 371 ? 0.23666 0.32765 0.43914 -0.03895 -0.02549 -0.00958 365 ASN A OD1   
2621 N ND2   A ASN A 371 ? 0.21374 0.32974 0.42324 -0.07076 -0.01892 0.01788  365 ASN A ND2   
2622 N ND2   B ASN A 371 ? 0.22770 0.34368 0.45739 -0.03466 -0.01934 -0.00233 365 ASN A ND2   
2623 N N     . ALA A 372 ? 0.14334 0.24618 0.29438 -0.01565 0.02132  -0.02346 366 ALA A N     
2624 C CA    . ALA A 372 ? 0.15761 0.23644 0.27542 -0.00779 0.02466  -0.01588 366 ALA A CA    
2625 C C     . ALA A 372 ? 0.17264 0.22679 0.26251 -0.02235 -0.00347 -0.01216 366 ALA A C     
2626 O O     . ALA A 372 ? 0.17465 0.22422 0.23924 -0.03453 0.00111  -0.03110 366 ALA A O     
2627 C CB    . ALA A 372 ? 0.16511 0.24913 0.33466 -0.01482 0.01036  -0.00430 366 ALA A CB    
2628 N N     . LYS A 373 ? 0.17403 0.21535 0.24884 -0.00505 -0.02118 0.00587  367 LYS A N     
2629 C CA    . LYS A 373 ? 0.15322 0.22000 0.25350 -0.03040 -0.03273 -0.01316 367 LYS A CA    
2630 C C     . LYS A 373 ? 0.14563 0.21423 0.24963 -0.00876 0.00147  -0.01934 367 LYS A C     
2631 O O     . LYS A 373 ? 0.14690 0.21631 0.30347 0.03034  -0.00039 -0.05131 367 LYS A O     
2632 C CB    . LYS A 373 ? 0.14459 0.24928 0.30118 -0.05147 -0.07246 -0.01461 367 LYS A CB    
2633 C CG    . LYS A 373 ? 0.16551 0.29426 0.38239 -0.08253 -0.06712 0.01573  367 LYS A CG    
2634 C CD    . LYS A 373 ? 0.19803 0.33725 0.45998 -0.08796 -0.09700 0.01688  367 LYS A CD    
2635 C CE    . LYS A 373 ? 0.22164 0.36045 0.54384 -0.08506 -0.11224 0.00719  367 LYS A CE    
2636 N NZ    . LYS A 373 ? 0.24827 0.37839 0.58632 -0.08503 -0.12601 0.00485  367 LYS A NZ    
2637 N N     . THR A 374 ? 0.13414 0.20504 0.24623 -0.03093 -0.01652 0.01880  368 THR A N     
2638 C CA    . THR A 374 ? 0.12204 0.20260 0.27958 -0.02587 -0.02056 -0.00974 368 THR A CA    
2639 C C     . THR A 374 ? 0.12457 0.19091 0.31243 -0.01816 -0.02347 -0.01947 368 THR A C     
2640 O O     . THR A 374 ? 0.11420 0.18408 0.37825 -0.00810 -0.02586 0.00865  368 THR A O     
2641 C CB    . THR A 374 ? 0.13426 0.22896 0.27673 -0.01718 0.02199  0.00537  368 THR A CB    
2642 O OG1   . THR A 374 ? 0.11910 0.25344 0.28340 0.00419  0.02395  0.02071  368 THR A OG1   
2643 C CG2   . THR A 374 ? 0.14648 0.24144 0.31067 -0.02538 0.00369  -0.01694 368 THR A CG2   
2644 N N     . PHE A 375 ? 0.11698 0.18975 0.29165 -0.00986 0.00462  -0.03523 369 PHE A N     
2645 C CA    . PHE A 375 ? 0.10971 0.18453 0.23693 -0.00106 0.01786  -0.03868 369 PHE A CA    
2646 C C     . PHE A 375 ? 0.11168 0.18518 0.23143 0.00456  -0.00335 -0.03448 369 PHE A C     
2647 O O     . PHE A 375 ? 0.10173 0.18748 0.20294 0.00210  -0.02545 -0.01571 369 PHE A O     
2648 C CB    . PHE A 375 ? 0.10993 0.18859 0.26771 0.01771  0.01348  -0.01772 369 PHE A CB    
2649 C CG    . PHE A 375 ? 0.09645 0.21413 0.31353 0.00981  -0.01087 -0.01939 369 PHE A CG    
2650 C CD1   . PHE A 375 ? 0.09380 0.22134 0.33154 0.01061  -0.01401 -0.04134 369 PHE A CD1   
2651 C CD2   . PHE A 375 ? 0.09205 0.20459 0.34508 0.01684  0.00486  -0.01674 369 PHE A CD2   
2652 C CE1   . PHE A 375 ? 0.09621 0.22029 0.32458 0.00375  -0.02699 -0.06867 369 PHE A CE1   
2653 C CE2   . PHE A 375 ? 0.09297 0.21610 0.34122 0.01848  0.00278  -0.03360 369 PHE A CE2   
2654 C CZ    . PHE A 375 ? 0.10334 0.23184 0.37506 0.01276  -0.01485 -0.05781 369 PHE A CZ    
2655 N N     . TYR A 376 ? 0.12511 0.17120 0.24479 0.01304  0.02924  -0.02785 370 TYR A N     
2656 C CA    . TYR A 376 ? 0.12237 0.17770 0.21751 0.01802  -0.00088 -0.01119 370 TYR A CA    
2657 C C     . TYR A 376 ? 0.14436 0.18892 0.28672 0.02658  -0.00270 -0.01837 370 TYR A C     
2658 O O     . TYR A 376 ? 0.17116 0.17925 0.29756 0.02754  0.01609  -0.01635 370 TYR A O     
2659 C CB    . TYR A 376 ? 0.15786 0.20925 0.23701 0.00833  0.01135  0.00682  370 TYR A CB    
2660 C CG    . TYR A 376 ? 0.23004 0.21237 0.25837 0.02931  -0.01054 0.01146  370 TYR A CG    
2661 C CD1   . TYR A 376 ? 0.27365 0.22540 0.22666 0.04789  -0.00961 0.01559  370 TYR A CD1   
2662 C CD2   . TYR A 376 ? 0.27173 0.20499 0.29761 0.04197  -0.04225 0.03314  370 TYR A CD2   
2663 C CE1   . TYR A 376 ? 0.30071 0.21488 0.24811 0.05708  -0.03438 0.03396  370 TYR A CE1   
2664 C CE2   . TYR A 376 ? 0.31203 0.22292 0.33327 0.06543  -0.06439 0.03826  370 TYR A CE2   
2665 C CZ    . TYR A 376 ? 0.34332 0.21092 0.33346 0.06752  -0.04083 0.02834  370 TYR A CZ    
2666 O OH    . TYR A 376 ? 0.40488 0.20380 0.36763 0.06468  -0.04289 0.03846  370 TYR A OH    
2667 N N     . THR A 377 ? 0.14481 0.18738 0.27661 0.00693  -0.00504 0.00273  371 THR A N     
2668 C CA    . THR A 377 ? 0.14667 0.22363 0.30727 0.00216  0.00157  -0.02093 371 THR A CA    
2669 C C     . THR A 377 ? 0.17763 0.21370 0.28102 0.00724  0.00090  -0.00542 371 THR A C     
2670 O O     . THR A 377 ? 0.19000 0.21662 0.26582 -0.00027 -0.01229 0.01742  371 THR A O     
2671 C CB    . THR A 377 ? 0.17010 0.24606 0.32077 -0.02831 -0.00222 -0.05820 371 THR A CB    
2672 O OG1   . THR A 377 ? 0.19296 0.25014 0.34477 0.00590  -0.02383 -0.05626 371 THR A OG1   
2673 C CG2   . THR A 377 ? 0.17144 0.25608 0.33537 -0.03071 -0.01457 -0.04944 371 THR A CG2   
2674 N N     . GLN A 378 ? 0.17854 0.20190 0.27525 0.01508  0.02234  0.01159  372 GLN A N     
2675 C CA    . GLN A 378 ? 0.16624 0.19530 0.27517 0.00217  0.03100  -0.00644 372 GLN A CA    
2676 C C     . GLN A 378 ? 0.17740 0.20420 0.27271 -0.00924 -0.02340 0.02097  372 GLN A C     
2677 O O     . GLN A 378 ? 0.17195 0.21521 0.27538 -0.01010 -0.04410 0.05079  372 GLN A O     
2678 C CB    . GLN A 378 ? 0.15545 0.19728 0.29025 -0.00715 0.02355  -0.00477 372 GLN A CB    
2679 C CG    . GLN A 378 ? 0.17949 0.22015 0.25068 0.00457  -0.01524 -0.00274 372 GLN A CG    
2680 C CD    . GLN A 378 ? 0.18592 0.23212 0.24502 -0.00752 -0.02093 -0.00181 372 GLN A CD    
2681 O OE1   . GLN A 378 ? 0.22790 0.24386 0.31108 -0.02685 -0.00565 0.00896  372 GLN A OE1   
2682 N NE2   . GLN A 378 ? 0.15586 0.24184 0.21900 -0.00160 -0.00383 -0.00857 372 GLN A NE2   
2683 N N     . ASP A 379 ? 0.17638 0.21348 0.24548 -0.02276 0.02612  0.03033  373 ASP A N     
2684 C CA    . ASP A 379 ? 0.18277 0.21951 0.27908 -0.02666 0.00131  0.00781  373 ASP A CA    
2685 C C     . ASP A 379 ? 0.17530 0.20219 0.27199 -0.01176 -0.01158 0.01025  373 ASP A C     
2686 O O     . ASP A 379 ? 0.19201 0.20367 0.24941 -0.01136 0.00457  0.02573  373 ASP A O     
2687 C CB    . ASP A 379 ? 0.20798 0.23336 0.36043 -0.03819 -0.01633 0.02019  373 ASP A CB    
2688 C CG    . ASP A 379 ? 0.23562 0.26408 0.41536 -0.05942 0.00035  -0.02752 373 ASP A CG    
2689 O OD1   . ASP A 379 ? 0.23158 0.26082 0.37676 -0.05792 0.01435  -0.05618 373 ASP A OD1   
2690 O OD2   . ASP A 379 ? 0.26673 0.28603 0.48599 -0.06508 -0.01866 -0.04392 373 ASP A OD2   
2691 N N     . PRO A 380 ? 0.17498 0.19398 0.31984 0.00916  -0.01900 0.01585  374 PRO A N     
2692 C CA    . PRO A 380 ? 0.17103 0.20641 0.28710 0.02182  -0.02434 0.00933  374 PRO A CA    
2693 C C     . PRO A 380 ? 0.16723 0.21824 0.29556 0.01006  -0.01799 0.00692  374 PRO A C     
2694 O O     . PRO A 380 ? 0.16084 0.23602 0.35714 -0.02182 -0.04023 -0.01147 374 PRO A O     
2695 C CB    . PRO A 380 ? 0.18063 0.20479 0.28837 0.03513  -0.02455 0.01723  374 PRO A CB    
2696 C CG    . PRO A 380 ? 0.19164 0.20868 0.29563 0.02507  -0.02199 0.02395  374 PRO A CG    
2697 C CD    . PRO A 380 ? 0.18027 0.18990 0.32278 0.03975  -0.02041 0.05003  374 PRO A CD    
2698 N N     . VAL A 381 ? 0.14877 0.20536 0.29275 0.01412  -0.02202 0.02452  375 VAL A N     
2699 C CA    . VAL A 381 ? 0.17339 0.23383 0.32592 0.01299  -0.00320 0.01601  375 VAL A CA    
2700 C C     . VAL A 381 ? 0.18087 0.21091 0.30791 0.00162  0.01079  0.01466  375 VAL A C     
2701 O O     . VAL A 381 ? 0.17751 0.17461 0.31530 -0.02723 0.02386  0.01743  375 VAL A O     
2702 C CB    . VAL A 381 ? 0.17248 0.25241 0.33785 -0.00185 0.01114  0.03708  375 VAL A CB    
2703 C CG1   . VAL A 381 ? 0.17233 0.27994 0.35154 -0.00696 0.02884  0.03763  375 VAL A CG1   
2704 C CG2   . VAL A 381 ? 0.18624 0.25121 0.31003 0.01680  -0.00723 0.03613  375 VAL A CG2   
2705 N N     . VAL A 382 ? 0.18946 0.21277 0.31683 -0.01259 -0.00209 -0.00136 376 VAL A N     
2706 C CA    . VAL A 382 ? 0.18159 0.21264 0.32939 -0.02749 -0.02808 0.00318  376 VAL A CA    
2707 C C     . VAL A 382 ? 0.16094 0.22230 0.30427 -0.01671 -0.02261 0.00790  376 VAL A C     
2708 O O     . VAL A 382 ? 0.15305 0.23223 0.32177 -0.01558 -0.00759 -0.00183 376 VAL A O     
2709 C CB    . VAL A 382 ? 0.19958 0.20171 0.34936 -0.02953 -0.04101 0.01056  376 VAL A CB    
2710 C CG1   . VAL A 382 ? 0.19448 0.20246 0.33783 -0.02491 -0.07010 0.01237  376 VAL A CG1   
2711 C CG2   . VAL A 382 ? 0.22548 0.20857 0.40140 -0.02284 -0.02490 0.00569  376 VAL A CG2   
2712 N N     . GLY A 383 ? 0.13445 0.21961 0.30990 -0.00195 -0.02493 0.02535  377 GLY A N     
2713 C CA    . GLY A 383 ? 0.12885 0.22600 0.25527 -0.01743 -0.01263 0.03769  377 GLY A CA    
2714 C C     . GLY A 383 ? 0.11397 0.23246 0.26157 -0.01874 0.00381  0.02636  377 GLY A C     
2715 O O     . GLY A 383 ? 0.09112 0.24001 0.25827 -0.02719 -0.00508 0.01336  377 GLY A O     
2716 N N     . TYR A 384 ? 0.10608 0.22769 0.22059 -0.02208 -0.01211 -0.00233 378 TYR A N     
2717 C CA    . TYR A 384 ? 0.11349 0.21393 0.21256 -0.01643 -0.02873 -0.00989 378 TYR A CA    
2718 C C     . TYR A 384 ? 0.14760 0.20019 0.21025 -0.03143 -0.04106 0.02215  378 TYR A C     
2719 O O     . TYR A 384 ? 0.18114 0.18106 0.22772 -0.04598 -0.02848 0.03072  378 TYR A O     
2720 C CB    . TYR A 384 ? 0.09444 0.22694 0.23570 -0.00067 -0.01282 -0.00320 378 TYR A CB    
2721 C CG    . TYR A 384 ? 0.11487 0.22911 0.26007 -0.00628 -0.00413 -0.03217 378 TYR A CG    
2722 C CD1   . TYR A 384 ? 0.10691 0.24240 0.23833 -0.01180 0.03580  -0.00088 378 TYR A CD1   
2723 C CD2   . TYR A 384 ? 0.10913 0.23173 0.28116 -0.01313 -0.02892 -0.04095 378 TYR A CD2   
2724 C CE1   . TYR A 384 ? 0.10612 0.24704 0.22705 -0.01453 0.02415  -0.02085 378 TYR A CE1   
2725 C CE2   . TYR A 384 ? 0.11744 0.25507 0.27898 -0.01191 -0.00576 -0.05687 378 TYR A CE2   
2726 C CZ    . TYR A 384 ? 0.11236 0.25757 0.23768 -0.02294 0.00420  -0.03452 378 TYR A CZ    
2727 O OH    . TYR A 384 ? 0.14283 0.28492 0.29945 -0.02534 0.00267  -0.01214 378 TYR A OH    
2728 N N     . THR A 385 ? 0.14492 0.22202 0.22672 -0.03079 -0.00206 0.03800  379 THR A N     
2729 C CA    . THR A 385 ? 0.15315 0.23339 0.22214 -0.02731 -0.00307 0.03615  379 THR A CA    
2730 C C     . THR A 385 ? 0.15849 0.22284 0.22298 -0.04078 0.01784  0.02047  379 THR A C     
2731 O O     . THR A 385 ? 0.17888 0.22008 0.26224 -0.02465 0.01167  -0.00103 379 THR A O     
2732 C CB    . THR A 385 ? 0.15547 0.25049 0.25489 -0.04013 -0.01625 0.02118  379 THR A CB    
2733 O OG1   . THR A 385 ? 0.16678 0.26073 0.26793 -0.01087 -0.03102 0.02077  379 THR A OG1   
2734 C CG2   . THR A 385 ? 0.15434 0.25968 0.28500 -0.05348 0.02338  0.06788  379 THR A CG2   
2735 N N     . ASP A 386 ? 0.13365 0.22319 0.24755 -0.03593 0.00269  -0.00789 380 ASP A N     
2736 C CA    . ASP A 386 ? 0.13776 0.21123 0.27220 -0.04419 0.01797  -0.01407 380 ASP A CA    
2737 C C     . ASP A 386 ? 0.13567 0.20059 0.30680 -0.03642 -0.00097 0.01224  380 ASP A C     
2738 O O     . ASP A 386 ? 0.14388 0.22527 0.35929 -0.02304 0.02158  0.01785  380 ASP A O     
2739 C CB    . ASP A 386 ? 0.18223 0.22600 0.33290 -0.04037 0.03112  -0.02483 380 ASP A CB    
2740 C CG    . ASP A 386 ? 0.21058 0.25400 0.37190 -0.03365 0.04221  -0.04458 380 ASP A CG    
2741 O OD1   . ASP A 386 ? 0.20375 0.26088 0.35544 -0.02455 0.03537  0.00835  380 ASP A OD1   
2742 O OD2   . ASP A 386 ? 0.22056 0.29492 0.37477 -0.04299 0.05478  -0.05216 380 ASP A OD2   
2743 N N     . TYR A 387 ? 0.14220 0.19970 0.26759 -0.01875 -0.02032 0.00804  381 TYR A N     
2744 C CA    . TYR A 387 ? 0.14782 0.20456 0.27099 -0.02547 -0.01149 0.01467  381 TYR A CA    
2745 C C     . TYR A 387 ? 0.15561 0.23542 0.28947 -0.03993 -0.00159 0.00863  381 TYR A C     
2746 O O     . TYR A 387 ? 0.16453 0.25617 0.29705 -0.02458 -0.02706 0.01044  381 TYR A O     
2747 C CB    . TYR A 387 ? 0.13328 0.18988 0.25254 -0.01102 0.00152  0.01000  381 TYR A CB    
2748 C CG    . TYR A 387 ? 0.12572 0.19050 0.26269 -0.02192 -0.00556 0.00917  381 TYR A CG    
2749 C CD1   . TYR A 387 ? 0.12442 0.19200 0.26626 -0.00884 -0.02873 -0.02649 381 TYR A CD1   
2750 C CD2   . TYR A 387 ? 0.12778 0.20061 0.27543 -0.03307 0.02018  0.00291  381 TYR A CD2   
2751 C CE1   . TYR A 387 ? 0.12504 0.21195 0.25021 -0.01012 0.02066  -0.01081 381 TYR A CE1   
2752 C CE2   . TYR A 387 ? 0.12794 0.21143 0.25557 -0.02857 -0.02849 0.02244  381 TYR A CE2   
2753 C CZ    . TYR A 387 ? 0.14415 0.23982 0.25851 -0.00373 -0.01877 -0.02110 381 TYR A CZ    
2754 O OH    . TYR A 387 ? 0.15412 0.27348 0.29516 0.02309  -0.05786 -0.03899 381 TYR A OH    
2755 N N     . PRO A 388 ? 0.17862 0.27132 0.28325 -0.04607 0.02992  -0.00175 382 PRO A N     
2756 C CA    . PRO A 388 ? 0.20342 0.28963 0.30931 -0.05218 0.02391  -0.02683 382 PRO A CA    
2757 C C     . PRO A 388 ? 0.21251 0.29781 0.29891 -0.04554 0.02246  0.00046  382 PRO A C     
2758 O O     . PRO A 388 ? 0.19029 0.30597 0.27436 -0.03005 0.02451  0.03344  382 PRO A O     
2759 C CB    . PRO A 388 ? 0.20081 0.29927 0.32632 -0.06266 0.01835  0.00778  382 PRO A CB    
2760 C CG    . PRO A 388 ? 0.18949 0.32631 0.34737 -0.04377 0.03134  -0.01700 382 PRO A CG    
2761 C CD    . PRO A 388 ? 0.17784 0.31020 0.29789 -0.04429 0.03106  -0.02010 382 PRO A CD    
2762 N N     . PHE A 389 ? 0.22859 0.29669 0.28039 -0.04452 -0.00308 -0.01166 383 PHE A N     
2763 C CA    . PHE A 389 ? 0.21817 0.29442 0.31992 -0.03826 0.03263  -0.00921 383 PHE A CA    
2764 C C     . PHE A 389 ? 0.21857 0.29123 0.36996 -0.04790 0.05540  -0.00022 383 PHE A C     
2765 O O     . PHE A 389 ? 0.23313 0.27262 0.39170 -0.06333 0.05865  -0.00133 383 PHE A O     
2766 C CB    . PHE A 389 ? 0.20348 0.30073 0.26058 -0.01419 0.03191  0.01569  383 PHE A CB    
2767 C CG    . PHE A 389 ? 0.20778 0.31549 0.27476 0.00966  0.05612  0.04046  383 PHE A CG    
2768 C CD1   . PHE A 389 ? 0.20660 0.33162 0.32922 0.01541  0.06414  0.04684  383 PHE A CD1   
2769 C CD2   . PHE A 389 ? 0.21338 0.31732 0.27642 0.02065  0.06264  0.08969  383 PHE A CD2   
2770 C CE1   . PHE A 389 ? 0.21320 0.33697 0.35466 0.00866  0.07100  0.04696  383 PHE A CE1   
2771 C CE2   . PHE A 389 ? 0.20801 0.31626 0.29618 0.02888  0.06275  0.09356  383 PHE A CE2   
2772 C CZ    . PHE A 389 ? 0.21952 0.32448 0.32132 0.02219  0.06695  0.05998  383 PHE A CZ    
2773 N N     . LEU A 390 ? 0.23558 0.29545 0.31961 -0.04575 0.08449  0.00190  384 LEU A N     
2774 C CA    . LEU A 390 ? 0.27775 0.33706 0.38480 -0.03501 0.11104  0.02268  384 LEU A CA    
2775 C C     . LEU A 390 ? 0.31003 0.39183 0.41368 -0.02906 0.12993  0.03402  384 LEU A C     
2776 O O     . LEU A 390 ? 0.31026 0.41027 0.38838 -0.02421 0.12495  0.03240  384 LEU A O     
2777 C CB    . LEU A 390 ? 0.29892 0.35182 0.45808 -0.03253 0.11255  0.00520  384 LEU A CB    
2778 C CG    . LEU A 390 ? 0.31748 0.37268 0.49496 -0.05009 0.08620  0.01953  384 LEU A CG    
2779 C CD1   . LEU A 390 ? 0.33052 0.36616 0.50479 -0.04787 0.09874  0.01709  384 LEU A CD1   
2780 C CD2   . LEU A 390 ? 0.31688 0.39123 0.52821 -0.05131 0.06654  0.01886  384 LEU A CD2   
2781 N N     . GLN A 391 ? 0.33662 0.42342 0.47797 -0.02570 0.12844  0.02839  385 GLN A N     
2782 C CA    . GLN A 391 ? 0.39621 0.46896 0.54738 -0.01867 0.10041  0.02145  385 GLN A CA    
2783 C C     . GLN A 391 ? 0.43472 0.48337 0.54861 -0.01185 0.08531  0.02193  385 GLN A C     
2784 O O     . GLN A 391 ? 0.45481 0.49597 0.55533 -0.00720 0.09049  0.03113  385 GLN A O     
2785 C CB    . GLN A 391 ? 0.40249 0.48051 0.60549 -0.01561 0.09940  0.02503  385 GLN A CB    
2786 N N1    . FMN B .   ? 0.09112 0.17557 0.22236 -0.01857 0.02098  0.02397  401 FMN A N1    
2787 C C2    . FMN B .   ? 0.09058 0.17656 0.24680 -0.01798 0.05473  0.01547  401 FMN A C2    
2788 O O2    . FMN B .   ? 0.10097 0.17621 0.22484 -0.02155 0.00203  0.03160  401 FMN A O2    
2789 N N3    . FMN B .   ? 0.09099 0.17630 0.31026 -0.02439 0.02734  0.00691  401 FMN A N3    
2790 C C4    . FMN B .   ? 0.10787 0.19241 0.28881 -0.00394 0.07389  0.00079  401 FMN A C4    
2791 O O4    . FMN B .   ? 0.10291 0.21077 0.36549 -0.01561 0.03860  -0.00334 401 FMN A O4    
2792 C C4A   . FMN B .   ? 0.09396 0.19117 0.29213 -0.01053 0.04793  0.03199  401 FMN A C4A   
2793 N N5    . FMN B .   ? 0.09604 0.20605 0.33083 -0.02197 -0.01170 0.03270  401 FMN A N5    
2794 C C5A   . FMN B .   ? 0.09932 0.20776 0.24318 -0.01113 -0.04189 0.02941  401 FMN A C5A   
2795 C C6    . FMN B .   ? 0.11143 0.21978 0.21845 -0.01863 -0.04622 -0.01150 401 FMN A C6    
2796 C C7    . FMN B .   ? 0.10076 0.21255 0.26143 -0.03559 -0.00154 -0.01055 401 FMN A C7    
2797 C C7M   . FMN B .   ? 0.10969 0.18991 0.33543 -0.02990 0.03876  -0.01397 401 FMN A C7M   
2798 C C8    . FMN B .   ? 0.10221 0.21500 0.29730 -0.01901 0.04982  0.01392  401 FMN A C8    
2799 C C8M   . FMN B .   ? 0.12681 0.23510 0.40472 -0.00031 0.04455  0.01541  401 FMN A C8M   
2800 C C9    . FMN B .   ? 0.08911 0.22007 0.25839 -0.01453 -0.00954 0.01276  401 FMN A C9    
2801 C C9A   . FMN B .   ? 0.08850 0.20771 0.21965 -0.00464 -0.02649 0.01852  401 FMN A C9A   
2802 N N10   . FMN B .   ? 0.06563 0.20285 0.18301 0.01528  0.01205  0.01969  401 FMN A N10   
2803 C C10   . FMN B .   ? 0.09329 0.19191 0.24411 -0.00426 0.01064  0.03807  401 FMN A C10   
2804 C "C1'" . FMN B .   ? 0.09825 0.19443 0.20838 0.02192  -0.02284 0.02759  401 FMN A "C1'" 
2805 C "C2'" . FMN B .   ? 0.09868 0.20193 0.24106 0.00903  0.01296  0.00146  401 FMN A "C2'" 
2806 O "O2'" . FMN B .   ? 0.12373 0.21776 0.20815 -0.01371 -0.02451 -0.00380 401 FMN A "O2'" 
2807 C "C3'" . FMN B .   ? 0.09848 0.20271 0.32407 0.00746  0.02848  0.01751  401 FMN A "C3'" 
2808 O "O3'" . FMN B .   ? 0.11251 0.20424 0.32832 0.00996  0.02678  0.02509  401 FMN A "O3'" 
2809 C "C4'" . FMN B .   ? 0.12692 0.20473 0.41245 -0.00273 0.04450  -0.02710 401 FMN A "C4'" 
2810 O "O4'" . FMN B .   ? 0.13844 0.19578 0.45518 0.00311  0.06642  -0.05430 401 FMN A "O4'" 
2811 C "C5'" . FMN B .   ? 0.12234 0.22497 0.34237 0.00049  0.01659  -0.03812 401 FMN A "C5'" 
2812 O "O5'" . FMN B .   ? 0.14766 0.24486 0.33314 0.01542  0.02349  -0.01412 401 FMN A "O5'" 
2813 P P     . FMN B .   ? 0.13712 0.27063 0.25366 0.01302  0.02246  -0.01852 401 FMN A P     
2814 O O1P   . FMN B .   ? 0.12970 0.27833 0.21829 -0.00333 0.00237  -0.04368 401 FMN A O1P   
2815 O O2P   . FMN B .   ? 0.10168 0.25875 0.28801 0.01546  0.01720  -0.02101 401 FMN A O2P   
2816 O O3P   . FMN B .   ? 0.14712 0.29180 0.27640 0.05691  0.00249  0.00420  401 FMN A O3P   
2817 P PA    . NAP C .   ? 0.42477 0.59514 0.70416 -0.06047 0.06900  0.03161  402 NAP A PA    
2818 O O1A   . NAP C .   ? 0.44549 0.59786 0.75016 -0.04709 0.07643  0.02880  402 NAP A O1A   
2819 O O2A   . NAP C .   ? 0.43344 0.58942 0.72455 -0.08279 0.05009  0.02165  402 NAP A O2A   
2820 O O5B   . NAP C .   ? 0.36289 0.54005 0.57940 -0.05938 0.09726  0.01104  402 NAP A O5B   
2821 C C5B   . NAP C .   ? 0.30915 0.47894 0.48289 -0.05987 0.06958  -0.00234 402 NAP A C5B   
2822 C C4B   . NAP C .   ? 0.26752 0.41869 0.44647 -0.04439 0.03520  -0.01122 402 NAP A C4B   
2823 O O4B   . NAP C .   ? 0.25416 0.37778 0.40696 -0.05697 0.01282  -0.01704 402 NAP A O4B   
2824 C C3B   . NAP C .   ? 0.25403 0.39985 0.46333 -0.02883 0.03771  -0.01292 402 NAP A C3B   
2825 O O3B   . NAP C .   ? 0.25671 0.38942 0.51210 -0.01182 0.01605  -0.03071 402 NAP A O3B   
2826 C C2B   . NAP C .   ? 0.24178 0.39301 0.41532 -0.02438 0.01556  -0.02741 402 NAP A C2B   
2827 O O2B   . NAP C .   ? 0.22753 0.42450 0.42457 -0.02052 -0.01793 -0.00772 402 NAP A O2B   
2828 C C1B   . NAP C .   ? 0.25270 0.35817 0.39677 -0.03469 0.01443  -0.01770 402 NAP A C1B   
2829 N N9A   . NAP C .   ? 0.24150 0.31496 0.39005 -0.03053 0.02513  -0.01922 402 NAP A N9A   
2830 C C8A   . NAP C .   ? 0.23395 0.30696 0.41456 -0.03459 0.04856  -0.02126 402 NAP A C8A   
2831 N N7A   . NAP C .   ? 0.22857 0.30211 0.43063 -0.05474 0.05022  -0.02392 402 NAP A N7A   
2832 C C5A   . NAP C .   ? 0.23655 0.30524 0.42451 -0.03293 0.01405  -0.00365 402 NAP A C5A   
2833 C C6A   . NAP C .   ? 0.26435 0.30745 0.44624 -0.04537 -0.00549 0.00685  402 NAP A C6A   
2834 N N6A   . NAP C .   ? 0.29283 0.31616 0.46233 -0.05954 -0.03627 0.00797  402 NAP A N6A   
2835 N N1A   . NAP C .   ? 0.24740 0.29991 0.42844 -0.03992 -0.00362 0.00773  402 NAP A N1A   
2836 C C2A   . NAP C .   ? 0.24401 0.29366 0.39397 -0.02244 -0.01246 -0.01930 402 NAP A C2A   
2837 N N3A   . NAP C .   ? 0.22983 0.28953 0.38913 -0.01554 -0.01977 -0.00141 402 NAP A N3A   
2838 C C4A   . NAP C .   ? 0.23013 0.30124 0.38811 -0.02630 0.01301  -0.00707 402 NAP A C4A   
2839 O O3    . NAP C .   ? 0.45150 0.62470 0.76312 -0.06037 0.05658  0.03540  402 NAP A O3    
2840 P PN    . NAP C .   ? 0.46536 0.65091 0.82182 -0.07044 0.06676  0.01281  402 NAP A PN    
2841 O O1N   . NAP C .   ? 0.46697 0.65334 0.83123 -0.06425 0.03493  -0.00146 402 NAP A O1N   
2842 O O2N   . NAP C .   ? 0.44654 0.64947 0.79983 -0.06333 0.11828  -0.02745 402 NAP A O2N   
2843 O O5D   . NAP C .   ? 0.47429 0.66061 0.83085 -0.08497 0.07205  0.04780  402 NAP A O5D   
2844 P P2B   . NAP C .   ? 0.25081 0.46330 0.44570 -0.01501 0.03334  -0.02521 402 NAP A P2B   
2845 O O1X   . NAP C .   ? 0.23878 0.46235 0.41838 0.00953  0.06977  -0.02824 402 NAP A O1X   
2846 O O2X   . NAP C .   ? 0.27065 0.49443 0.45076 -0.00870 0.03323  -0.01315 402 NAP A O2X   
2847 O O3X   . NAP C .   ? 0.24531 0.46350 0.48425 -0.04962 0.00990  -0.06905 402 NAP A O3X   
2848 S S     . SO4 D .   ? 0.67655 0.77455 0.89134 -0.04878 -0.04065 -0.01076 403 SO4 A S     
2849 O O1    . SO4 D .   ? 0.67228 0.76377 0.74109 -0.03977 -0.01085 -0.06140 403 SO4 A O1    
2850 O O2    . SO4 D .   ? 0.67383 0.76815 0.93755 -0.06332 -0.06332 -0.03950 403 SO4 A O2    
2851 O O3    . SO4 D .   ? 0.66342 0.77359 0.95547 -0.03946 -0.04929 -0.00375 403 SO4 A O3    
2852 O O4    . SO4 D .   ? 0.67146 0.76442 0.86081 -0.04913 -0.02444 0.05233  403 SO4 A O4    
# 
