data_9M3R
# 
_entry.id   9M3R 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9M3R         pdb_00009m3r 10.2210/pdb9m3r/pdb 
WWPDB D_1300057121 ?            ?                   
# 
_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       2025-06-25 
_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                        9M3R 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bruce.xu@roche.com 
_pdbx_contact_author.name_first         bruce 
_pdbx_contact_author.name_last          xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7301-015X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, Z.H.' 1 ? 
'Chen, S.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem.Lett. 
_citation.journal_id_ASTM           BMCLE8 
_citation.journal_id_CSD            1127 
_citation.journal_id_ISSN           1464-3405 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                130190 
_citation.page_last                 130190 
_citation.title                     'Discovery of ATP competitive PDHK1/2 dual inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2025.130190 
_citation.pdbx_database_id_PubMed   40107630 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, H.'         1  ? 
primary 'Ding, D.'       2  ? 
primary 'Han, X.'        3  ? 
primary 'Miao, K.'       4  ? 
primary 'Liang, C.'      5  ? 
primary 'Yun, H.'        6  ? 
primary 'Zhu, W.'        7  ? 
primary 'Dey, F.'        8  ? 
primary 'Zhao, D.'       9  ? 
primary 'Wu, Y.'         10 ? 
primary 'Reutlinger, M.' 11 ? 
primary 'Yang, J.'       12 ? 
primary 'Zhai, G.'       13 ? 
primary 'Lin, Z.'        14 ? 
primary 'Li, C.'         15 ? 
primary 'Wu, W.'         16 ? 
primary 'Xu, B.'         17 ? 
primary 'Han, L.'        18 ? 
primary 'Chen, S.'       19 ? 
primary 'Huang, X.'      20 ? 
primary 'Casagrande, F.' 21 ? 
primary 'Hilbert, M.'    22 ? 
primary 'Strebel, Q.'    23 ? 
primary 'Wichert, M.'    24 ? 
primary 'Westwood, P.'   25 ? 
primary 'Schafer, R.'    26 ? 
primary 'Roth, D.'       27 ? 
primary 'Heer, D.'       28 ? 
primary 'Tian, X.'       29 ? 
primary 'Ma, T.'         30 ? 
primary 'Zhang, T.'      31 ? 
primary 'Zhao, J.'       32 ? 
primary 'Urich, E.'      33 ? 
primary 'Xia, G.'        34 ? 
primary 'Lassen, K.'     35 ? 
primary 'Shen, H.C.'     36 ? 
primary 'Zou, G.'        37 ? 
# 
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 '[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial'                         
42978.977 1   2.7.11.2 ? ? ? 
2 non-polymer syn 'SULFATE ION'                                                                                            96.063 
2   ?        ? ? ? 
3 non-polymer syn 'N-(2-AMINOETHYL)-2-{3-CHLORO-4-[(4-ISOPROPYLBENZYL)OXY]PHENYL} ACETAMIDE'                               360.878 
1   ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                                           62.068 
1   ?        ? ? ? 
5 non-polymer nat GLYCEROL                                                                                                 92.094 
1   ?        ? ? ? 
6 non-polymer syn '3-[4-[4-(ethylamino)-6-fluoranyl-2-oxidanylidene-3H-benzimidazol-1-yl]phenoxy]benzenesulfonyl fluoride' 445.439 
1   ?        ? ? ? 
7 water       nat water                                                                                                    18.015 
126 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Pyruvate dehydrogenase kinase isoform 2,PDH kinase 2,PDKII' 
# 
_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       
;PKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIM
EFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIF
DGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNA
MRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLY
AKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIM
EFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIF
DGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNA
MRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLY
AKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVP
;
_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 'SULFATE ION'                                                                                            SO4   
3 'N-(2-AMINOETHYL)-2-{3-CHLORO-4-[(4-ISOPROPYLBENZYL)OXY]PHENYL} ACETAMIDE'                               TF3   
4 1,2-ETHANEDIOL                                                                                           EDO   
5 GLYCEROL                                                                                                 GOL   
6 '3-[4-[4-(ethylamino)-6-fluoranyl-2-oxidanylidene-3H-benzimidazol-1-yl]phenoxy]benzenesulfonyl fluoride' A1EQH 
7 water                                                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   LYS n 
1 3   TYR n 
1 4   ILE n 
1 5   GLU n 
1 6   HIS n 
1 7   PHE n 
1 8   SER n 
1 9   LYS n 
1 10  PHE n 
1 11  SER n 
1 12  PRO n 
1 13  SER n 
1 14  PRO n 
1 15  LEU n 
1 16  SER n 
1 17  MET n 
1 18  LYS n 
1 19  GLN n 
1 20  PHE n 
1 21  LEU n 
1 22  ASP n 
1 23  PHE n 
1 24  GLY n 
1 25  SER n 
1 26  SER n 
1 27  ASN n 
1 28  ALA n 
1 29  CYS n 
1 30  GLU n 
1 31  LYS n 
1 32  THR n 
1 33  SER n 
1 34  PHE n 
1 35  THR n 
1 36  PHE n 
1 37  LEU n 
1 38  ARG n 
1 39  GLN n 
1 40  GLU n 
1 41  LEU n 
1 42  PRO n 
1 43  VAL n 
1 44  ARG n 
1 45  LEU n 
1 46  ALA n 
1 47  ASN n 
1 48  ILE n 
1 49  MET n 
1 50  LYS n 
1 51  GLU n 
1 52  ILE n 
1 53  ASN n 
1 54  LEU n 
1 55  LEU n 
1 56  PRO n 
1 57  ASP n 
1 58  ARG n 
1 59  VAL n 
1 60  LEU n 
1 61  SER n 
1 62  THR n 
1 63  PRO n 
1 64  SER n 
1 65  VAL n 
1 66  GLN n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  SER n 
1 71  TRP n 
1 72  TYR n 
1 73  VAL n 
1 74  GLN n 
1 75  SER n 
1 76  LEU n 
1 77  LEU n 
1 78  ASP n 
1 79  ILE n 
1 80  MET n 
1 81  GLU n 
1 82  PHE n 
1 83  LEU n 
1 84  ASP n 
1 85  LYS n 
1 86  ASP n 
1 87  PRO n 
1 88  GLU n 
1 89  ASP n 
1 90  HIS n 
1 91  ARG n 
1 92  THR n 
1 93  LEU n 
1 94  SER n 
1 95  GLN n 
1 96  PHE n 
1 97  THR n 
1 98  ASP n 
1 99  ALA n 
1 100 LEU n 
1 101 VAL n 
1 102 THR n 
1 103 ILE n 
1 104 ARG n 
1 105 ASN n 
1 106 ARG n 
1 107 HIS n 
1 108 ASN n 
1 109 ASP n 
1 110 VAL n 
1 111 VAL n 
1 112 PRO n 
1 113 THR n 
1 114 MET n 
1 115 ALA n 
1 116 GLN n 
1 117 GLY n 
1 118 VAL n 
1 119 LEU n 
1 120 GLU n 
1 121 TYR n 
1 122 LYS n 
1 123 ASP n 
1 124 THR n 
1 125 TYR n 
1 126 GLY n 
1 127 ASP n 
1 128 ASP n 
1 129 PRO n 
1 130 VAL n 
1 131 SER n 
1 132 ASN n 
1 133 GLN n 
1 134 ASN n 
1 135 ILE n 
1 136 GLN n 
1 137 TYR n 
1 138 PHE n 
1 139 LEU n 
1 140 ASP n 
1 141 ARG n 
1 142 PHE n 
1 143 TYR n 
1 144 LEU n 
1 145 SER n 
1 146 ARG n 
1 147 ILE n 
1 148 SER n 
1 149 ILE n 
1 150 ARG n 
1 151 MET n 
1 152 LEU n 
1 153 ILE n 
1 154 ASN n 
1 155 GLN n 
1 156 HIS n 
1 157 THR n 
1 158 LEU n 
1 159 ILE n 
1 160 PHE n 
1 161 ASP n 
1 162 GLY n 
1 163 SER n 
1 164 THR n 
1 165 ASN n 
1 166 PRO n 
1 167 ALA n 
1 168 HIS n 
1 169 PRO n 
1 170 LYS n 
1 171 HIS n 
1 172 ILE n 
1 173 GLY n 
1 174 SER n 
1 175 ILE n 
1 176 ASP n 
1 177 PRO n 
1 178 ASN n 
1 179 CYS n 
1 180 ASN n 
1 181 VAL n 
1 182 SER n 
1 183 GLU n 
1 184 VAL n 
1 185 VAL n 
1 186 LYS n 
1 187 ASP n 
1 188 ALA n 
1 189 TYR n 
1 190 ASP n 
1 191 MET n 
1 192 ALA n 
1 193 LYS n 
1 194 LEU n 
1 195 LEU n 
1 196 CYS n 
1 197 ASP n 
1 198 LYS n 
1 199 TYR n 
1 200 TYR n 
1 201 MET n 
1 202 ALA n 
1 203 SER n 
1 204 PRO n 
1 205 ASP n 
1 206 LEU n 
1 207 GLU n 
1 208 ILE n 
1 209 GLN n 
1 210 GLU n 
1 211 ILE n 
1 212 ASN n 
1 213 ALA n 
1 214 ALA n 
1 215 ASN n 
1 216 SER n 
1 217 LYS n 
1 218 GLN n 
1 219 PRO n 
1 220 ILE n 
1 221 HIS n 
1 222 MET n 
1 223 VAL n 
1 224 TYR n 
1 225 VAL n 
1 226 PRO n 
1 227 SER n 
1 228 HIS n 
1 229 LEU n 
1 230 TYR n 
1 231 HIS n 
1 232 MET n 
1 233 LEU n 
1 234 PHE n 
1 235 GLU n 
1 236 LEU n 
1 237 PHE n 
1 238 LYS n 
1 239 ASN n 
1 240 ALA n 
1 241 MET n 
1 242 ARG n 
1 243 ALA n 
1 244 THR n 
1 245 VAL n 
1 246 GLU n 
1 247 SER n 
1 248 HIS n 
1 249 GLU n 
1 250 SER n 
1 251 SER n 
1 252 LEU n 
1 253 ILE n 
1 254 LEU n 
1 255 PRO n 
1 256 PRO n 
1 257 ILE n 
1 258 LYS n 
1 259 VAL n 
1 260 MET n 
1 261 VAL n 
1 262 ALA n 
1 263 LEU n 
1 264 GLY n 
1 265 GLU n 
1 266 GLU n 
1 267 ASP n 
1 268 LEU n 
1 269 SER n 
1 270 ILE n 
1 271 LYS n 
1 272 MET n 
1 273 SER n 
1 274 ASP n 
1 275 ARG n 
1 276 GLY n 
1 277 GLY n 
1 278 GLY n 
1 279 VAL n 
1 280 PRO n 
1 281 LEU n 
1 282 ARG n 
1 283 LYS n 
1 284 ILE n 
1 285 GLU n 
1 286 ARG n 
1 287 LEU n 
1 288 PHE n 
1 289 SER n 
1 290 TYR n 
1 291 MET n 
1 292 TYR n 
1 293 SER n 
1 294 THR n 
1 295 ALA n 
1 296 PRO n 
1 297 THR n 
1 298 PRO n 
1 299 GLN n 
1 300 PRO n 
1 301 GLY n 
1 302 THR n 
1 303 GLY n 
1 304 GLY n 
1 305 THR n 
1 306 PRO n 
1 307 LEU n 
1 308 ALA n 
1 309 GLY n 
1 310 PHE n 
1 311 GLY n 
1 312 TYR n 
1 313 GLY n 
1 314 LEU n 
1 315 PRO n 
1 316 ILE n 
1 317 SER n 
1 318 ARG n 
1 319 LEU n 
1 320 TYR n 
1 321 ALA n 
1 322 LYS n 
1 323 TYR n 
1 324 PHE n 
1 325 GLN n 
1 326 GLY n 
1 327 ASP n 
1 328 LEU n 
1 329 GLN n 
1 330 LEU n 
1 331 PHE n 
1 332 SER n 
1 333 MET n 
1 334 GLU n 
1 335 GLY n 
1 336 PHE n 
1 337 GLY n 
1 338 THR n 
1 339 ASP n 
1 340 ALA n 
1 341 VAL n 
1 342 ILE n 
1 343 TYR n 
1 344 LEU n 
1 345 LYS n 
1 346 ALA n 
1 347 LEU n 
1 348 SER n 
1 349 THR n 
1 350 ASP n 
1 351 SER n 
1 352 VAL n 
1 353 GLU n 
1 354 ARG n 
1 355 LEU n 
1 356 PRO n 
1 357 VAL n 
1 358 TYR n 
1 359 ASN n 
1 360 LYS n 
1 361 SER n 
1 362 ALA n 
1 363 TRP n 
1 364 ARG n 
1 365 HIS n 
1 366 TYR n 
1 367 GLN n 
1 368 THR n 
1 369 ILE n 
1 370 GLN n 
1 371 GLU n 
1 372 ALA n 
1 373 GLY n 
1 374 ASP n 
1 375 TRP n 
1 376 CYS n 
1 377 VAL n 
1 378 PRO 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                   378 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PDK2, PDHK2' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
A1EQH non-polymer         . 
'3-[4-[4-(ethylamino)-6-fluoranyl-2-oxidanylidene-3H-benzimidazol-1-yl]phenoxy]benzenesulfonyl fluoride' ? 'C21 H17 F2 N3 O4 S' 
445.439 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'               'C2 H6 O2'           62.068  
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  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'           92.094  
HIS   'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER ?                               'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'         105.093 
SO4   non-polymer         . 'SULFATE ION' ?                               'O4 S -2'            96.063  
TF3   non-polymer         . 'N-(2-AMINOETHYL)-2-{3-CHLORO-4-[(4-ISOPROPYLBENZYL)OXY]PHENYL} ACETAMIDE' ? 'C20 H25 Cl N2 O2'   
360.878 
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   PRO 1   17  17  PRO PRO A . n 
A 1 2   LYS 2   18  18  LYS LYS A . n 
A 1 3   TYR 3   19  19  TYR TYR A . n 
A 1 4   ILE 4   20  20  ILE ILE A . n 
A 1 5   GLU 5   21  21  GLU GLU A . n 
A 1 6   HIS 6   22  22  HIS HIS A . n 
A 1 7   PHE 7   23  23  PHE PHE A . n 
A 1 8   SER 8   24  24  SER SER A . n 
A 1 9   LYS 9   25  25  LYS LYS A . n 
A 1 10  PHE 10  26  26  PHE PHE A . n 
A 1 11  SER 11  27  27  SER SER A . n 
A 1 12  PRO 12  28  28  PRO PRO A . n 
A 1 13  SER 13  29  29  SER SER A . n 
A 1 14  PRO 14  30  30  PRO PRO A . n 
A 1 15  LEU 15  31  31  LEU LEU A . n 
A 1 16  SER 16  32  32  SER SER A . n 
A 1 17  MET 17  33  33  MET MET A . n 
A 1 18  LYS 18  34  34  LYS LYS A . n 
A 1 19  GLN 19  35  35  GLN GLN A . n 
A 1 20  PHE 20  36  36  PHE PHE A . n 
A 1 21  LEU 21  37  37  LEU LEU A . n 
A 1 22  ASP 22  38  38  ASP ASP A . n 
A 1 23  PHE 23  39  39  PHE PHE A . n 
A 1 24  GLY 24  40  40  GLY GLY A . n 
A 1 25  SER 25  41  41  SER SER A . n 
A 1 26  SER 26  42  42  SER SER A . n 
A 1 27  ASN 27  43  43  ASN ASN A . n 
A 1 28  ALA 28  44  44  ALA ALA A . n 
A 1 29  CYS 29  45  45  CYS CYS A . n 
A 1 30  GLU 30  46  46  GLU GLU A . n 
A 1 31  LYS 31  47  47  LYS LYS A . n 
A 1 32  THR 32  48  48  THR THR A . n 
A 1 33  SER 33  49  49  SER SER A . n 
A 1 34  PHE 34  50  50  PHE PHE A . n 
A 1 35  THR 35  51  51  THR THR A . n 
A 1 36  PHE 36  52  52  PHE PHE A . n 
A 1 37  LEU 37  53  53  LEU LEU A . n 
A 1 38  ARG 38  54  54  ARG ARG A . n 
A 1 39  GLN 39  55  55  GLN GLN A . n 
A 1 40  GLU 40  56  56  GLU GLU A . n 
A 1 41  LEU 41  57  57  LEU LEU A . n 
A 1 42  PRO 42  58  58  PRO PRO A . n 
A 1 43  VAL 43  59  59  VAL VAL A . n 
A 1 44  ARG 44  60  60  ARG ARG A . n 
A 1 45  LEU 45  61  61  LEU LEU A . n 
A 1 46  ALA 46  62  62  ALA ALA A . n 
A 1 47  ASN 47  63  63  ASN ASN A . n 
A 1 48  ILE 48  64  64  ILE ILE A . n 
A 1 49  MET 49  65  65  MET MET A . n 
A 1 50  LYS 50  66  66  LYS LYS A . n 
A 1 51  GLU 51  67  67  GLU GLU A . n 
A 1 52  ILE 52  68  68  ILE ILE A . n 
A 1 53  ASN 53  69  69  ASN ASN A . n 
A 1 54  LEU 54  70  70  LEU LEU A . n 
A 1 55  LEU 55  71  71  LEU LEU A . n 
A 1 56  PRO 56  72  72  PRO PRO A . n 
A 1 57  ASP 57  73  73  ASP ASP A . n 
A 1 58  ARG 58  74  74  ARG ARG A . n 
A 1 59  VAL 59  75  75  VAL VAL A . n 
A 1 60  LEU 60  76  76  LEU LEU A . n 
A 1 61  SER 61  77  77  SER SER A . n 
A 1 62  THR 62  78  78  THR THR A . n 
A 1 63  PRO 63  79  79  PRO PRO A . n 
A 1 64  SER 64  80  80  SER SER A . n 
A 1 65  VAL 65  81  81  VAL VAL A . n 
A 1 66  GLN 66  82  82  GLN GLN A . n 
A 1 67  LEU 67  83  83  LEU LEU A . n 
A 1 68  VAL 68  84  84  VAL VAL A . n 
A 1 69  GLN 69  85  85  GLN GLN A . n 
A 1 70  SER 70  86  86  SER SER A . n 
A 1 71  TRP 71  87  87  TRP TRP A . n 
A 1 72  TYR 72  88  88  TYR TYR A . n 
A 1 73  VAL 73  89  89  VAL VAL A . n 
A 1 74  GLN 74  90  90  GLN GLN A . n 
A 1 75  SER 75  91  91  SER SER A . n 
A 1 76  LEU 76  92  92  LEU LEU A . n 
A 1 77  LEU 77  93  93  LEU LEU A . n 
A 1 78  ASP 78  94  94  ASP ASP A . n 
A 1 79  ILE 79  95  95  ILE ILE A . n 
A 1 80  MET 80  96  96  MET MET A . n 
A 1 81  GLU 81  97  97  GLU GLU A . n 
A 1 82  PHE 82  98  98  PHE PHE A . n 
A 1 83  LEU 83  99  99  LEU LEU A . n 
A 1 84  ASP 84  100 100 ASP ASP A . n 
A 1 85  LYS 85  101 101 LYS LYS A . n 
A 1 86  ASP 86  102 102 ASP ASP A . n 
A 1 87  PRO 87  103 103 PRO PRO A . n 
A 1 88  GLU 88  104 104 GLU GLU A . n 
A 1 89  ASP 89  105 105 ASP ASP A . n 
A 1 90  HIS 90  106 106 HIS HIS A . n 
A 1 91  ARG 91  107 107 ARG ARG A . n 
A 1 92  THR 92  108 108 THR THR A . n 
A 1 93  LEU 93  109 109 LEU LEU A . n 
A 1 94  SER 94  110 110 SER SER A . n 
A 1 95  GLN 95  111 111 GLN GLN A . n 
A 1 96  PHE 96  112 112 PHE PHE A . n 
A 1 97  THR 97  113 113 THR THR A . n 
A 1 98  ASP 98  114 114 ASP ASP A . n 
A 1 99  ALA 99  115 115 ALA ALA A . n 
A 1 100 LEU 100 116 116 LEU LEU A . n 
A 1 101 VAL 101 117 117 VAL VAL A . n 
A 1 102 THR 102 118 118 THR THR A . n 
A 1 103 ILE 103 119 119 ILE ILE A . n 
A 1 104 ARG 104 120 120 ARG ARG A . n 
A 1 105 ASN 105 121 121 ASN ASN A . n 
A 1 106 ARG 106 122 122 ARG ARG A . n 
A 1 107 HIS 107 123 123 HIS HIS A . n 
A 1 108 ASN 108 124 124 ASN ASN A . n 
A 1 109 ASP 109 125 125 ASP ASP A . n 
A 1 110 VAL 110 126 126 VAL VAL A . n 
A 1 111 VAL 111 127 127 VAL VAL A . n 
A 1 112 PRO 112 128 128 PRO PRO A . n 
A 1 113 THR 113 129 129 THR THR A . n 
A 1 114 MET 114 130 130 MET MET A . n 
A 1 115 ALA 115 131 131 ALA ALA A . n 
A 1 116 GLN 116 132 132 GLN GLN A . n 
A 1 117 GLY 117 133 133 GLY GLY A . n 
A 1 118 VAL 118 134 134 VAL VAL A . n 
A 1 119 LEU 119 135 135 LEU LEU A . n 
A 1 120 GLU 120 136 136 GLU GLU A . n 
A 1 121 TYR 121 137 137 TYR TYR A . n 
A 1 122 LYS 122 138 138 LYS LYS A . n 
A 1 123 ASP 123 139 139 ASP ASP A . n 
A 1 124 THR 124 140 140 THR THR A . n 
A 1 125 TYR 125 141 141 TYR TYR A . n 
A 1 126 GLY 126 142 142 GLY GLY A . n 
A 1 127 ASP 127 143 143 ASP ASP A . n 
A 1 128 ASP 128 144 144 ASP ASP A . n 
A 1 129 PRO 129 145 145 PRO PRO A . n 
A 1 130 VAL 130 146 146 VAL VAL A . n 
A 1 131 SER 131 147 147 SER SER A . n 
A 1 132 ASN 132 148 148 ASN ASN A . n 
A 1 133 GLN 133 149 149 GLN GLN A . n 
A 1 134 ASN 134 150 150 ASN ASN A . n 
A 1 135 ILE 135 151 151 ILE ILE A . n 
A 1 136 GLN 136 152 152 GLN GLN A . n 
A 1 137 TYR 137 153 153 TYR TYR A . n 
A 1 138 PHE 138 154 154 PHE PHE A . n 
A 1 139 LEU 139 155 155 LEU LEU A . n 
A 1 140 ASP 140 156 156 ASP ASP A . n 
A 1 141 ARG 141 157 157 ARG ARG A . n 
A 1 142 PHE 142 158 158 PHE PHE A . n 
A 1 143 TYR 143 159 159 TYR TYR A . n 
A 1 144 LEU 144 160 160 LEU LEU A . n 
A 1 145 SER 145 161 161 SER SER A . n 
A 1 146 ARG 146 162 162 ARG ARG A . n 
A 1 147 ILE 147 163 163 ILE ILE A . n 
A 1 148 SER 148 164 164 SER SER A . n 
A 1 149 ILE 149 165 165 ILE ILE A . n 
A 1 150 ARG 150 166 166 ARG ARG A . n 
A 1 151 MET 151 167 167 MET MET A . n 
A 1 152 LEU 152 168 168 LEU LEU A . n 
A 1 153 ILE 153 169 169 ILE ILE A . n 
A 1 154 ASN 154 170 170 ASN ASN A . n 
A 1 155 GLN 155 171 171 GLN GLN A . n 
A 1 156 HIS 156 172 172 HIS HIS A . n 
A 1 157 THR 157 173 173 THR THR A . n 
A 1 158 LEU 158 174 174 LEU LEU A . n 
A 1 159 ILE 159 175 175 ILE ILE A . n 
A 1 160 PHE 160 176 176 PHE PHE A . n 
A 1 161 ASP 161 177 177 ASP ASP A . n 
A 1 162 GLY 162 178 178 GLY GLY A . n 
A 1 163 SER 163 179 ?   ?   ?   A . n 
A 1 164 THR 164 180 ?   ?   ?   A . n 
A 1 165 ASN 165 181 ?   ?   ?   A . n 
A 1 166 PRO 166 182 ?   ?   ?   A . n 
A 1 167 ALA 167 183 ?   ?   ?   A . n 
A 1 168 HIS 168 184 ?   ?   ?   A . n 
A 1 169 PRO 169 185 185 PRO PRO A . n 
A 1 170 LYS 170 186 186 LYS LYS A . n 
A 1 171 HIS 171 187 187 HIS HIS A . n 
A 1 172 ILE 172 188 188 ILE ILE A . n 
A 1 173 GLY 173 189 189 GLY GLY A . n 
A 1 174 SER 174 190 190 SER SER A . n 
A 1 175 ILE 175 191 191 ILE ILE A . n 
A 1 176 ASP 176 192 192 ASP ASP A . n 
A 1 177 PRO 177 193 193 PRO PRO A . n 
A 1 178 ASN 178 194 194 ASN ASN A . n 
A 1 179 CYS 179 195 195 CYS CYS A . n 
A 1 180 ASN 180 196 196 ASN ASN A . n 
A 1 181 VAL 181 197 197 VAL VAL A . n 
A 1 182 SER 182 198 198 SER SER A . n 
A 1 183 GLU 183 199 199 GLU GLU A . n 
A 1 184 VAL 184 200 200 VAL VAL A . n 
A 1 185 VAL 185 201 201 VAL VAL A . n 
A 1 186 LYS 186 202 202 LYS LYS A . n 
A 1 187 ASP 187 203 203 ASP ASP A . n 
A 1 188 ALA 188 204 204 ALA ALA A . n 
A 1 189 TYR 189 205 205 TYR TYR A . n 
A 1 190 ASP 190 206 206 ASP ASP A . n 
A 1 191 MET 191 207 207 MET MET A . n 
A 1 192 ALA 192 208 208 ALA ALA A . n 
A 1 193 LYS 193 209 209 LYS LYS A . n 
A 1 194 LEU 194 210 210 LEU LEU A . n 
A 1 195 LEU 195 211 211 LEU LEU A . n 
A 1 196 CYS 196 212 212 CYS CYS A . n 
A 1 197 ASP 197 213 213 ASP ASP A . n 
A 1 198 LYS 198 214 214 LYS LYS A . n 
A 1 199 TYR 199 215 215 TYR TYR A . n 
A 1 200 TYR 200 216 216 TYR TYR A . n 
A 1 201 MET 201 217 217 MET MET A . n 
A 1 202 ALA 202 218 218 ALA ALA A . n 
A 1 203 SER 203 219 219 SER SER A . n 
A 1 204 PRO 204 220 220 PRO PRO A . n 
A 1 205 ASP 205 221 221 ASP ASP A . n 
A 1 206 LEU 206 222 222 LEU LEU A . n 
A 1 207 GLU 207 223 223 GLU GLU A . n 
A 1 208 ILE 208 224 224 ILE ILE A . n 
A 1 209 GLN 209 225 225 GLN GLN A . n 
A 1 210 GLU 210 226 226 GLU GLU A . n 
A 1 211 ILE 211 227 227 ILE ILE A . n 
A 1 212 ASN 212 228 228 ASN ASN A . n 
A 1 213 ALA 213 229 229 ALA ALA A . n 
A 1 214 ALA 214 230 230 ALA ALA A . n 
A 1 215 ASN 215 231 231 ASN ASN A . n 
A 1 216 SER 216 232 232 SER SER A . n 
A 1 217 LYS 217 233 233 LYS LYS A . n 
A 1 218 GLN 218 234 234 GLN GLN A . n 
A 1 219 PRO 219 235 235 PRO PRO A . n 
A 1 220 ILE 220 236 236 ILE ILE A . n 
A 1 221 HIS 221 237 237 HIS HIS A . n 
A 1 222 MET 222 238 238 MET MET A . n 
A 1 223 VAL 223 239 239 VAL VAL A . n 
A 1 224 TYR 224 240 240 TYR TYR A . n 
A 1 225 VAL 225 241 241 VAL VAL A . n 
A 1 226 PRO 226 242 242 PRO PRO A . n 
A 1 227 SER 227 243 243 SER SER A . n 
A 1 228 HIS 228 244 244 HIS HIS A . n 
A 1 229 LEU 229 245 245 LEU LEU A . n 
A 1 230 TYR 230 246 246 TYR TYR A . n 
A 1 231 HIS 231 247 247 HIS HIS A . n 
A 1 232 MET 232 248 248 MET MET A . n 
A 1 233 LEU 233 249 249 LEU LEU A . n 
A 1 234 PHE 234 250 250 PHE PHE A . n 
A 1 235 GLU 235 251 251 GLU GLU A . n 
A 1 236 LEU 236 252 252 LEU LEU A . n 
A 1 237 PHE 237 253 253 PHE PHE A . n 
A 1 238 LYS 238 254 254 LYS LYS A . n 
A 1 239 ASN 239 255 255 ASN ASN A . n 
A 1 240 ALA 240 256 256 ALA ALA A . n 
A 1 241 MET 241 257 257 MET MET A . n 
A 1 242 ARG 242 258 258 ARG ARG A . n 
A 1 243 ALA 243 259 259 ALA ALA A . n 
A 1 244 THR 244 260 260 THR THR A . n 
A 1 245 VAL 245 261 261 VAL VAL A . n 
A 1 246 GLU 246 262 262 GLU GLU A . n 
A 1 247 SER 247 263 263 SER SER A . n 
A 1 248 HIS 248 264 264 HIS HIS A . n 
A 1 249 GLU 249 265 265 GLU GLU A . n 
A 1 250 SER 250 266 266 SER SER A . n 
A 1 251 SER 251 267 267 SER SER A . n 
A 1 252 LEU 252 268 268 LEU LEU A . n 
A 1 253 ILE 253 269 269 ILE ILE A . n 
A 1 254 LEU 254 270 270 LEU LEU A . n 
A 1 255 PRO 255 271 271 PRO PRO A . n 
A 1 256 PRO 256 272 272 PRO PRO A . n 
A 1 257 ILE 257 273 273 ILE ILE A . n 
A 1 258 LYS 258 274 274 LYS LYS A . n 
A 1 259 VAL 259 275 275 VAL VAL A . n 
A 1 260 MET 260 276 276 MET MET A . n 
A 1 261 VAL 261 277 277 VAL VAL A . n 
A 1 262 ALA 262 278 278 ALA ALA A . n 
A 1 263 LEU 263 279 279 LEU LEU A . n 
A 1 264 GLY 264 280 280 GLY GLY A . n 
A 1 265 GLU 265 281 281 GLU GLU A . n 
A 1 266 GLU 266 282 282 GLU GLU A . n 
A 1 267 ASP 267 283 283 ASP ASP A . n 
A 1 268 LEU 268 284 284 LEU LEU A . n 
A 1 269 SER 269 285 285 SER SER A . n 
A 1 270 ILE 270 286 286 ILE ILE A . n 
A 1 271 LYS 271 287 287 LYS LYS A . n 
A 1 272 MET 272 288 288 MET MET A . n 
A 1 273 SER 273 289 289 SER SER A . n 
A 1 274 ASP 274 290 290 ASP ASP A . n 
A 1 275 ARG 275 291 291 ARG ARG A . n 
A 1 276 GLY 276 292 292 GLY GLY A . n 
A 1 277 GLY 277 293 293 GLY GLY A . n 
A 1 278 GLY 278 294 294 GLY GLY A . n 
A 1 279 VAL 279 295 295 VAL VAL A . n 
A 1 280 PRO 280 296 296 PRO PRO A . n 
A 1 281 LEU 281 297 297 LEU LEU A . n 
A 1 282 ARG 282 298 298 ARG ARG A . n 
A 1 283 LYS 283 299 299 LYS LYS A . n 
A 1 284 ILE 284 300 300 ILE ILE A . n 
A 1 285 GLU 285 301 301 GLU GLU A . n 
A 1 286 ARG 286 302 302 ARG ARG A . n 
A 1 287 LEU 287 303 303 LEU LEU A . n 
A 1 288 PHE 288 304 304 PHE PHE A . n 
A 1 289 SER 289 305 305 SER SER A . n 
A 1 290 TYR 290 306 306 TYR TYR A . n 
A 1 291 MET 291 307 307 MET MET A . n 
A 1 292 TYR 292 308 308 TYR TYR A . n 
A 1 293 SER 293 309 309 SER SER A . n 
A 1 294 THR 294 310 310 THR THR A . n 
A 1 295 ALA 295 311 311 ALA ALA A . n 
A 1 296 PRO 296 312 ?   ?   ?   A . n 
A 1 297 THR 297 313 ?   ?   ?   A . n 
A 1 298 PRO 298 314 ?   ?   ?   A . n 
A 1 299 GLN 299 315 ?   ?   ?   A . n 
A 1 300 PRO 300 316 ?   ?   ?   A . n 
A 1 301 GLY 301 317 ?   ?   ?   A . n 
A 1 302 THR 302 318 ?   ?   ?   A . n 
A 1 303 GLY 303 319 ?   ?   ?   A . n 
A 1 304 GLY 304 320 ?   ?   ?   A . n 
A 1 305 THR 305 321 ?   ?   ?   A . n 
A 1 306 PRO 306 322 322 PRO PRO A . n 
A 1 307 LEU 307 323 323 LEU LEU A . n 
A 1 308 ALA 308 324 324 ALA ALA A . n 
A 1 309 GLY 309 325 325 GLY GLY A . n 
A 1 310 PHE 310 326 326 PHE PHE A . n 
A 1 311 GLY 311 327 327 GLY GLY A . n 
A 1 312 TYR 312 328 328 TYR TYR A . n 
A 1 313 GLY 313 329 329 GLY GLY A . n 
A 1 314 LEU 314 330 330 LEU LEU A . n 
A 1 315 PRO 315 331 331 PRO PRO A . n 
A 1 316 ILE 316 332 332 ILE ILE A . n 
A 1 317 SER 317 333 333 SER SER A . n 
A 1 318 ARG 318 334 334 ARG ARG A . n 
A 1 319 LEU 319 335 335 LEU LEU A . n 
A 1 320 TYR 320 336 336 TYR TYR A . n 
A 1 321 ALA 321 337 337 ALA ALA A . n 
A 1 322 LYS 322 338 338 LYS LYS A . n 
A 1 323 TYR 323 339 339 TYR TYR A . n 
A 1 324 PHE 324 340 340 PHE PHE A . n 
A 1 325 GLN 325 341 341 GLN GLN A . n 
A 1 326 GLY 326 342 342 GLY GLY A . n 
A 1 327 ASP 327 343 343 ASP ASP A . n 
A 1 328 LEU 328 344 344 LEU LEU A . n 
A 1 329 GLN 329 345 345 GLN GLN A . n 
A 1 330 LEU 330 346 346 LEU LEU A . n 
A 1 331 PHE 331 347 347 PHE PHE A . n 
A 1 332 SER 332 348 348 SER SER A . n 
A 1 333 MET 333 349 349 MET MET A . n 
A 1 334 GLU 334 350 350 GLU GLU A . n 
A 1 335 GLY 335 351 351 GLY GLY A . n 
A 1 336 PHE 336 352 352 PHE PHE A . n 
A 1 337 GLY 337 353 353 GLY GLY A . n 
A 1 338 THR 338 354 354 THR THR A . n 
A 1 339 ASP 339 355 355 ASP ASP A . n 
A 1 340 ALA 340 356 356 ALA ALA A . n 
A 1 341 VAL 341 357 357 VAL VAL A . n 
A 1 342 ILE 342 358 358 ILE ILE A . n 
A 1 343 TYR 343 359 359 TYR TYR A . n 
A 1 344 LEU 344 360 360 LEU LEU A . n 
A 1 345 LYS 345 361 361 LYS LYS A . n 
A 1 346 ALA 346 362 362 ALA ALA A . n 
A 1 347 LEU 347 363 363 LEU LEU A . n 
A 1 348 SER 348 364 364 SER SER A . n 
A 1 349 THR 349 365 365 THR THR A . n 
A 1 350 ASP 350 366 366 ASP ASP A . n 
A 1 351 SER 351 367 367 SER SER A . n 
A 1 352 VAL 352 368 368 VAL VAL A . n 
A 1 353 GLU 353 369 369 GLU GLU A . n 
A 1 354 ARG 354 370 370 ARG ARG A . n 
A 1 355 LEU 355 371 371 LEU LEU A . n 
A 1 356 PRO 356 372 372 PRO PRO A . n 
A 1 357 VAL 357 373 373 VAL VAL A . n 
A 1 358 TYR 358 374 374 TYR TYR A . n 
A 1 359 ASN 359 375 375 ASN ASN A . n 
A 1 360 LYS 360 376 376 LYS LYS A . n 
A 1 361 SER 361 377 377 SER SER A . n 
A 1 362 ALA 362 378 378 ALA ALA A . n 
A 1 363 TRP 363 379 379 TRP TRP A . n 
A 1 364 ARG 364 380 380 ARG ARG A . n 
A 1 365 HIS 365 381 381 HIS HIS A . n 
A 1 366 TYR 366 382 382 TYR TYR A . n 
A 1 367 GLN 367 383 383 GLN GLN A . n 
A 1 368 THR 368 384 ?   ?   ?   A . n 
A 1 369 ILE 369 385 ?   ?   ?   A . n 
A 1 370 GLN 370 386 ?   ?   ?   A . n 
A 1 371 GLU 371 387 ?   ?   ?   A . n 
A 1 372 ALA 372 388 ?   ?   ?   A . n 
A 1 373 GLY 373 389 389 GLY GLY A . n 
A 1 374 ASP 374 390 390 ASP ASP A . n 
A 1 375 TRP 375 391 391 TRP TRP A . n 
A 1 376 CYS 376 392 392 CYS CYS A . n 
A 1 377 VAL 377 393 393 VAL VAL A . n 
A 1 378 PRO 378 394 394 PRO PRO A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EQH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EQH 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4   1   401 401 SO4   SO4 A . 
C 3 TF3   1   402 501 TF3   TF3 A . 
D 4 EDO   1   403 601 EDO   EDO A . 
E 5 GOL   1   404 701 GOL   GOL A . 
F 2 SO4   1   405 801 SO4   SO4 A . 
G 6 A1EQH 1   406 901 A1EQH L0R A . 
H 7 HOH   1   501 71  HOH   HOH A . 
H 7 HOH   2   502 78  HOH   HOH A . 
H 7 HOH   3   503 28  HOH   HOH A . 
H 7 HOH   4   504 13  HOH   HOH A . 
H 7 HOH   5   505 44  HOH   HOH A . 
H 7 HOH   6   506 15  HOH   HOH A . 
H 7 HOH   7   507 79  HOH   HOH A . 
H 7 HOH   8   508 106 HOH   HOH A . 
H 7 HOH   9   509 5   HOH   HOH A . 
H 7 HOH   10  510 29  HOH   HOH A . 
H 7 HOH   11  511 81  HOH   HOH A . 
H 7 HOH   12  512 68  HOH   HOH A . 
H 7 HOH   13  513 38  HOH   HOH A . 
H 7 HOH   14  514 43  HOH   HOH A . 
H 7 HOH   15  515 118 HOH   HOH A . 
H 7 HOH   16  516 6   HOH   HOH A . 
H 7 HOH   17  517 65  HOH   HOH A . 
H 7 HOH   18  518 115 HOH   HOH A . 
H 7 HOH   19  519 100 HOH   HOH A . 
H 7 HOH   20  520 97  HOH   HOH A . 
H 7 HOH   21  521 41  HOH   HOH A . 
H 7 HOH   22  522 57  HOH   HOH A . 
H 7 HOH   23  523 92  HOH   HOH A . 
H 7 HOH   24  524 45  HOH   HOH A . 
H 7 HOH   25  525 27  HOH   HOH A . 
H 7 HOH   26  526 67  HOH   HOH A . 
H 7 HOH   27  527 14  HOH   HOH A . 
H 7 HOH   28  528 80  HOH   HOH A . 
H 7 HOH   29  529 75  HOH   HOH A . 
H 7 HOH   30  530 52  HOH   HOH A . 
H 7 HOH   31  531 40  HOH   HOH A . 
H 7 HOH   32  532 7   HOH   HOH A . 
H 7 HOH   33  533 69  HOH   HOH A . 
H 7 HOH   34  534 120 HOH   HOH A . 
H 7 HOH   35  535 17  HOH   HOH A . 
H 7 HOH   36  536 62  HOH   HOH A . 
H 7 HOH   37  537 60  HOH   HOH A . 
H 7 HOH   38  538 53  HOH   HOH A . 
H 7 HOH   39  539 90  HOH   HOH A . 
H 7 HOH   40  540 63  HOH   HOH A . 
H 7 HOH   41  541 22  HOH   HOH A . 
H 7 HOH   42  542 88  HOH   HOH A . 
H 7 HOH   43  543 125 HOH   HOH A . 
H 7 HOH   44  544 84  HOH   HOH A . 
H 7 HOH   45  545 35  HOH   HOH A . 
H 7 HOH   46  546 55  HOH   HOH A . 
H 7 HOH   47  547 109 HOH   HOH A . 
H 7 HOH   48  548 91  HOH   HOH A . 
H 7 HOH   49  549 72  HOH   HOH A . 
H 7 HOH   50  550 16  HOH   HOH A . 
H 7 HOH   51  551 50  HOH   HOH A . 
H 7 HOH   52  552 77  HOH   HOH A . 
H 7 HOH   53  553 20  HOH   HOH A . 
H 7 HOH   54  554 26  HOH   HOH A . 
H 7 HOH   55  555 23  HOH   HOH A . 
H 7 HOH   56  556 116 HOH   HOH A . 
H 7 HOH   57  557 51  HOH   HOH A . 
H 7 HOH   58  558 93  HOH   HOH A . 
H 7 HOH   59  559 21  HOH   HOH A . 
H 7 HOH   60  560 54  HOH   HOH A . 
H 7 HOH   61  561 102 HOH   HOH A . 
H 7 HOH   62  562 114 HOH   HOH A . 
H 7 HOH   63  563 83  HOH   HOH A . 
H 7 HOH   64  564 34  HOH   HOH A . 
H 7 HOH   65  565 117 HOH   HOH A . 
H 7 HOH   66  566 11  HOH   HOH A . 
H 7 HOH   67  567 64  HOH   HOH A . 
H 7 HOH   68  568 123 HOH   HOH A . 
H 7 HOH   69  569 58  HOH   HOH A . 
H 7 HOH   70  570 2   HOH   HOH A . 
H 7 HOH   71  571 18  HOH   HOH A . 
H 7 HOH   72  572 42  HOH   HOH A . 
H 7 HOH   73  573 107 HOH   HOH A . 
H 7 HOH   74  574 32  HOH   HOH A . 
H 7 HOH   75  575 108 HOH   HOH A . 
H 7 HOH   76  576 39  HOH   HOH A . 
H 7 HOH   77  577 119 HOH   HOH A . 
H 7 HOH   78  578 121 HOH   HOH A . 
H 7 HOH   79  579 86  HOH   HOH A . 
H 7 HOH   80  580 61  HOH   HOH A . 
H 7 HOH   81  581 30  HOH   HOH A . 
H 7 HOH   82  582 48  HOH   HOH A . 
H 7 HOH   83  583 112 HOH   HOH A . 
H 7 HOH   84  584 12  HOH   HOH A . 
H 7 HOH   85  585 59  HOH   HOH A . 
H 7 HOH   86  586 96  HOH   HOH A . 
H 7 HOH   87  587 76  HOH   HOH A . 
H 7 HOH   88  588 9   HOH   HOH A . 
H 7 HOH   89  589 122 HOH   HOH A . 
H 7 HOH   90  590 1   HOH   HOH A . 
H 7 HOH   91  591 94  HOH   HOH A . 
H 7 HOH   92  592 4   HOH   HOH A . 
H 7 HOH   93  593 36  HOH   HOH A . 
H 7 HOH   94  594 47  HOH   HOH A . 
H 7 HOH   95  595 8   HOH   HOH A . 
H 7 HOH   96  596 70  HOH   HOH A . 
H 7 HOH   97  597 113 HOH   HOH A . 
H 7 HOH   98  598 89  HOH   HOH A . 
H 7 HOH   99  599 37  HOH   HOH A . 
H 7 HOH   100 600 73  HOH   HOH A . 
H 7 HOH   101 601 87  HOH   HOH A . 
H 7 HOH   102 602 104 HOH   HOH A . 
H 7 HOH   103 603 98  HOH   HOH A . 
H 7 HOH   104 604 126 HOH   HOH A . 
H 7 HOH   105 605 101 HOH   HOH A . 
H 7 HOH   106 606 103 HOH   HOH A . 
H 7 HOH   107 607 111 HOH   HOH A . 
H 7 HOH   108 608 24  HOH   HOH A . 
H 7 HOH   109 609 33  HOH   HOH A . 
H 7 HOH   110 610 95  HOH   HOH A . 
H 7 HOH   111 611 110 HOH   HOH A . 
H 7 HOH   112 612 46  HOH   HOH A . 
H 7 HOH   113 613 19  HOH   HOH A . 
H 7 HOH   114 614 56  HOH   HOH A . 
H 7 HOH   115 615 124 HOH   HOH A . 
H 7 HOH   116 616 25  HOH   HOH A . 
H 7 HOH   117 617 3   HOH   HOH A . 
H 7 HOH   118 618 105 HOH   HOH A . 
H 7 HOH   119 619 74  HOH   HOH A . 
H 7 HOH   120 620 10  HOH   HOH A . 
H 7 HOH   121 621 66  HOH   HOH A . 
H 7 HOH   122 622 99  HOH   HOH A . 
H 7 HOH   123 623 31  HOH   HOH A . 
H 7 HOH   124 624 85  HOH   HOH A . 
H 7 HOH   125 625 49  HOH   HOH A . 
H 7 HOH   126 626 82  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.19rc4_4035: ???)' ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                     ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                     ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                     ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M3R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     109.800 
_cell.length_a_esd                 ? 
_cell.length_b                     109.800 
_cell.length_b_esd                 ? 
_cell.length_c                     84.420 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9M3R 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                172 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 64' 
_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                   9M3R 
_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             3.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.14 
_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              ? 
_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    '0.42 M NaK tartrate, 0.1 M Na citrate, pH 5.6' 
_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         2019-11-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9793 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M3R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.31 
_reflns.d_resolution_low                               73 
_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                                     199622 
_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                           80.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.68 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.109 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
1.31 1.39 ? ? ? ? ? ? 5851  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.86   ? ? 1 1 0.023 ? ? ? ? 1.777 ? ? ? ? ? ? ? ? ? 
1.39 1.49 ? ? ? ? ? ? 24707 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.720  ? ? 2 1 0.018 ? ? ? ? 1.688 ? ? ? ? ? ? ? ? ? 
1.49 1.61 ? ? ? ? ? ? 33743 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.543  ? ? 3 1 0.018 ? ? ? ? 1.666 ? ? ? ? ? ? ? ? ? 
1.61 1.76 ? ? ? ? ? ? 32388 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 22.169 ? ? 4 1 0.018 ? ? ? ? 1.456 ? ? ? ? ? ? ? ? ? 
1.76 1.97 ? ? ? ? ? ? 29229 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 5.818  ? ? 5 1 0.217 ? ? ? ? 5.383 ? ? ? ? ? ? ? ? ? 
1.97 2.28 ? ? ? ? ? ? 25796 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.234  ? ? 6 1 0.833 ? ? ? ? 1.142 ? ? ? ? ? ? ? ? ? 
2.28 2.79 ? ? ? ? ? ? 21816 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.297  ? ? 7 1 0.988 ? ? ? ? 0.275 ? ? ? ? ? ? ? ? ? 
2.79 3.94 ? ? ? ? ? ? 16835 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.072  ? ? 8 1 0.999 ? ? ? ? 0.066 ? ? ? ? ? ? ? ? ? 
3.94 70   ? ? ? ? ? ? 9257  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.035  ? ? 9 1 0.999 ? ? ? ? 0.032 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9M3R 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.14 
_refine.ls_d_res_low                             47.54 
_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                     31973 
_refine.ls_number_reflns_R_free                  1571 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1835 
_refine.ls_R_factor_R_free                       0.2149 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1819 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.58 
_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                            0.26 
_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                       2.14 
_refine_hist.d_res_low                        47.54 
_refine_hist.number_atoms_solvent             126 
_refine_hist.number_atoms_total               3078 
_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        2877 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         75 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 3100 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.841  ? 4195 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 12.858 ? 1180 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.051  ? 446  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 544  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.14 2.21  . . 129 2756 100.00 . . . . 0.2362 . . . . . . . . . . . . . . . 0.2528 
'X-RAY DIFFRACTION' 2.21 2.29  . . 152 2756 100.00 . . . . 0.2229 . . . . . . . . . . . . . . . 0.2737 
'X-RAY DIFFRACTION' 2.29 2.38  . . 149 2737 100.00 . . . . 0.2137 . . . . . . . . . . . . . . . 0.2743 
'X-RAY DIFFRACTION' 2.38 2.49  . . 167 2725 100.00 . . . . 0.1959 . . . . . . . . . . . . . . . 0.2441 
'X-RAY DIFFRACTION' 2.49 2.62  . . 139 2756 100.00 . . . . 0.1986 . . . . . . . . . . . . . . . 0.2385 
'X-RAY DIFFRACTION' 2.62 2.78  . . 132 2739 100.00 . . . . 0.2087 . . . . . . . . . . . . . . . 0.2508 
'X-RAY DIFFRACTION' 2.78 3.00  . . 147 2771 100.00 . . . . 0.2173 . . . . . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 3.00 3.30  . . 131 2788 100.00 . . . . 0.1960 . . . . . . . . . . . . . . . 0.2382 
'X-RAY DIFFRACTION' 3.30 3.78  . . 140 2778 100.00 . . . . 0.1792 . . . . . . . . . . . . . . . 0.2282 
'X-RAY DIFFRACTION' 3.78 4.76  . . 155 2759 100.00 . . . . 0.1497 . . . . . . . . . . . . . . . 0.1732 
'X-RAY DIFFRACTION' 4.76 47.54 . . 130 2837 100.00 . . . . 0.1752 . . . . . . . . . . . . . . . 0.1874 
# 
_struct.entry_id                     9M3R 
_struct.title                        
'Crystal structure of human pyruvate dehydrogenase kinase isoform 1 in complex with ATP competitive inhibitor 29' 
_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        9M3R 
_struct_keywords.text            'ghkl atpase/kinase family, pyruvate dehydrogenase complex, mitochondrial kinase, transferase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 2 ? 
G N N 6 ? 
H N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PDK2_HUMAN 
_struct_ref.pdbx_db_accession          Q15119 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIM
EFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIF
DGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNA
MRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLY
AKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVP
;
_struct_ref.pdbx_align_begin           17 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9M3R 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 378 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q15119 
_struct_ref_seq.db_align_beg                  17 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  394 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       17 
_struct_ref_seq.pdbx_auth_seq_align_end       394 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7180  ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  31620 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000    0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 4_455 -x-1,-y,z -1.0000000000 0.0000000000 0.0000000000 -109.8000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 PRO A 1   ? LYS A 9   ? PRO A 17  LYS A 25  1 ? 9  
HELX_P HELX_P2  AA2 SER A 16  ? GLY A 24  ? SER A 32  GLY A 40  1 ? 9  
HELX_P HELX_P3  AA3 SER A 26  ? ALA A 28  ? SER A 42  ALA A 44  5 ? 3  
HELX_P HELX_P4  AA4 CYS A 29  ? LEU A 54  ? CYS A 45  LEU A 70  1 ? 26 
HELX_P HELX_P5  AA5 PRO A 56  ? SER A 61  ? PRO A 72  SER A 77  1 ? 6  
HELX_P HELX_P6  AA6 THR A 62  ? MET A 80  ? THR A 78  MET A 96  1 ? 19 
HELX_P HELX_P7  AA7 GLU A 81  ? LYS A 85  ? GLU A 97  LYS A 101 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 89  ? HIS A 107 ? ASP A 105 HIS A 123 1 ? 19 
HELX_P HELX_P9  AA9 ASP A 109 ? TYR A 125 ? ASP A 125 TYR A 141 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 128 ? PHE A 160 ? ASP A 144 PHE A 176 1 ? 33 
HELX_P HELX_P11 AB2 VAL A 181 ? MET A 201 ? VAL A 197 MET A 217 1 ? 21 
HELX_P HELX_P12 AB3 VAL A 225 ? SER A 247 ? VAL A 241 SER A 263 1 ? 23 
HELX_P HELX_P13 AB4 PRO A 280 ? GLU A 285 ? PRO A 296 GLU A 301 1 ? 6  
HELX_P HELX_P14 AB5 ARG A 286 ? SER A 289 ? ARG A 302 SER A 305 5 ? 4  
HELX_P HELX_P15 AB6 GLY A 313 ? PHE A 324 ? GLY A 329 PHE A 340 1 ? 12 
HELX_P HELX_P16 AB7 ASN A 359 ? GLN A 367 ? ASN A 375 GLN A 383 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           TYR 
_struct_conn.ptnr1_label_seq_id            292 
_struct_conn.ptnr1_label_atom_id           OH 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           G 
_struct_conn.ptnr2_label_comp_id           A1EQH 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           S 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            TYR 
_struct_conn.ptnr1_auth_seq_id             308 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1EQH 
_struct_conn.ptnr2_auth_seq_id             406 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.482 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1EQH 
_pdbx_modification_feature.label_asym_id                      G 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     TYR 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      292 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1EQH 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        406 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      TYR 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       308 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               S 
_pdbx_modification_feature.modified_residue_id_linking_atom   OH 
_pdbx_modification_feature.modified_residue_id                TYR 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1EQH 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
# 
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 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? 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 ASP A 176 ? ASN A 180 ? ASP A 192 ASN A 196 
AA1 2 HIS A 221 ? TYR A 224 ? HIS A 237 TYR A 240 
AA2 1 LEU A 206 ? ASN A 212 ? LEU A 222 ASN A 228 
AA2 2 ILE A 257 ? LEU A 263 ? ILE A 273 LEU A 279 
AA2 3 ASP A 267 ? SER A 273 ? ASP A 283 SER A 289 
AA2 4 GLY A 337 ? LYS A 345 ? GLY A 353 LYS A 361 
AA2 5 ASP A 327 ? MET A 333 ? ASP A 343 MET A 349 
# 
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 ASP A 176 ? N ASP A 192 O TYR A 224 ? O TYR A 240 
AA2 1 2 N GLU A 207 ? N GLU A 223 O VAL A 259 ? O VAL A 275 
AA2 2 3 N ALA A 262 ? N ALA A 278 O SER A 269 ? O SER A 285 
AA2 3 4 N MET A 272 ? N MET A 288 O ALA A 340 ? O ALA A 356 
AA2 4 5 O ASP A 339 ? O ASP A 355 N PHE A 331 ? N PHE A 347 
# 
_pdbx_entry_details.entry_id                   9M3R 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 CYS A 45  ? ? -68.97  4.69    
2 1 MET A 96  ? ? -68.86  3.29    
3 1 ARG A 291 ? ? -115.88 53.23   
4 1 SER A 309 ? ? -62.59  1.89    
5 1 LEU A 323 ? B -94.23  -117.94 
6 1 PHE A 352 ? ? -130.88 -68.95  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    PHE 
_pdbx_struct_special_symmetry.auth_seq_id     347 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   A 
_pdbx_struct_special_symmetry.label_comp_id   PHE 
_pdbx_struct_special_symmetry.label_seq_id    331 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -40.9589 25.5274 -39.3612 0.4982 ? 0.0276 ? 0.0975  ? 0.6089 ? 0.2077  ? 0.6820 ? 4.8879 ? -0.5294 
? 0.2892  ? 1.2801 ? 0.2739  ? 1.9544 ? 0.2009 ? 0.8348  ? 0.9490 ? -0.2613 ? -0.1338 ? -0.2897 ? -0.2661 ? 0.4365  ? -0.0494 ? 
2 'X-RAY DIFFRACTION' ? refined -47.8327 16.2070 -16.1319 0.4520 ? 0.0306 ? -0.0480 ? 0.2984 ? -0.0328 ? 0.4118 ? 2.2838 ? 0.2009  
? -0.4582 ? 2.1574 ? -0.1989 ? 2.1756 ? 0.0635 ? -0.1780 ? 0.2621 ? 0.4360  ? -0.0367 ? -0.1223 ? -0.1860 ? 0.1366  ? -0.0471 ? 
3 'X-RAY DIFFRACTION' ? refined -54.1238 9.5756  -26.1287 0.3813 ? 0.0761 ? -0.0154 ? 0.3430 ? 0.0048  ? 0.3033 ? 3.0945 ? 0.3511  
? 0.0200  ? 2.2916 ? -0.5103 ? 0.9783 ? 0.0720 ? 0.4822  ? 0.1702 ? -0.1202 ? -0.0017 ? 0.0908  ? -0.1014 ? -0.0951 ? -0.1037 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 17 through 144 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 145 through 282 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 283 through 394 )
;
# 
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 SER 179 ? A SER 163 
2  1 Y 1 A THR 180 ? A THR 164 
3  1 Y 1 A ASN 181 ? A ASN 165 
4  1 Y 1 A PRO 182 ? A PRO 166 
5  1 Y 1 A ALA 183 ? A ALA 167 
6  1 Y 1 A HIS 184 ? A HIS 168 
7  1 Y 1 A PRO 312 ? A PRO 296 
8  1 Y 1 A THR 313 ? A THR 297 
9  1 Y 1 A PRO 314 ? A PRO 298 
10 1 Y 1 A GLN 315 ? A GLN 299 
11 1 Y 1 A PRO 316 ? A PRO 300 
12 1 Y 1 A GLY 317 ? A GLY 301 
13 1 Y 1 A THR 318 ? A THR 302 
14 1 Y 1 A GLY 319 ? A GLY 303 
15 1 Y 1 A GLY 320 ? A GLY 304 
16 1 Y 1 A THR 321 ? A THR 305 
17 1 Y 1 A THR 384 ? A THR 368 
18 1 Y 1 A ILE 385 ? A ILE 369 
19 1 Y 1 A GLN 386 ? A GLN 370 
20 1 Y 1 A GLU 387 ? A GLU 371 
21 1 Y 1 A ALA 388 ? A ALA 372 
# 
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 
A1EQH C10  C  N N 1   
A1EQH C11  C  N N 2   
A1EQH C13  C  Y N 3   
A1EQH C15  C  Y N 4   
A1EQH C16  C  Y N 5   
A1EQH C17  C  Y N 6   
A1EQH C18  C  Y N 7   
A1EQH C19  C  Y N 8   
A1EQH C20  C  Y N 9   
A1EQH N    N  N N 10  
A1EQH C    C  Y N 11  
A1EQH O    O  N N 12  
A1EQH C1   C  Y N 13  
A1EQH C12  C  Y N 14  
A1EQH C14  C  Y N 15  
A1EQH C2   C  Y N 16  
A1EQH C3   C  Y N 17  
A1EQH C4   C  Y N 18  
A1EQH C5   C  Y N 19  
A1EQH C6   C  Y N 20  
A1EQH C7   C  N N 21  
A1EQH C8   C  Y N 22  
A1EQH C9   C  Y N 23  
A1EQH F    F  N N 24  
A1EQH N1   N  N N 25  
A1EQH N2   N  N N 26  
A1EQH O1   O  N N 27  
A1EQH O2   O  N N 28  
A1EQH O3   O  N N 29  
A1EQH S    S  N N 30  
A1EQH H1   H  N N 31  
A1EQH H2   H  N N 32  
A1EQH H3   H  N N 33  
A1EQH H4   H  N N 34  
A1EQH H5   H  N N 35  
A1EQH H6   H  N N 36  
A1EQH H7   H  N N 37  
A1EQH H8   H  N N 38  
A1EQH H9   H  N N 39  
A1EQH H10  H  N N 40  
A1EQH H12  H  N N 41  
A1EQH H13  H  N N 42  
A1EQH H14  H  N N 43  
A1EQH H15  H  N N 44  
A1EQH H16  H  N N 45  
A1EQH H17  H  N N 46  
A1EQH H18  H  N N 47  
A1EQH F1   F  N N 48  
ALA   N    N  N N 49  
ALA   CA   C  N S 50  
ALA   C    C  N N 51  
ALA   O    O  N N 52  
ALA   CB   C  N N 53  
ALA   OXT  O  N N 54  
ALA   H    H  N N 55  
ALA   H2   H  N N 56  
ALA   HA   H  N N 57  
ALA   HB1  H  N N 58  
ALA   HB2  H  N N 59  
ALA   HB3  H  N N 60  
ALA   HXT  H  N N 61  
ARG   N    N  N N 62  
ARG   CA   C  N S 63  
ARG   C    C  N N 64  
ARG   O    O  N N 65  
ARG   CB   C  N N 66  
ARG   CG   C  N N 67  
ARG   CD   C  N N 68  
ARG   NE   N  N N 69  
ARG   CZ   C  N N 70  
ARG   NH1  N  N N 71  
ARG   NH2  N  N N 72  
ARG   OXT  O  N N 73  
ARG   H    H  N N 74  
ARG   H2   H  N N 75  
ARG   HA   H  N N 76  
ARG   HB2  H  N N 77  
ARG   HB3  H  N N 78  
ARG   HG2  H  N N 79  
ARG   HG3  H  N N 80  
ARG   HD2  H  N N 81  
ARG   HD3  H  N N 82  
ARG   HE   H  N N 83  
ARG   HH11 H  N N 84  
ARG   HH12 H  N N 85  
ARG   HH21 H  N N 86  
ARG   HH22 H  N N 87  
ARG   HXT  H  N N 88  
ASN   N    N  N N 89  
ASN   CA   C  N S 90  
ASN   C    C  N N 91  
ASN   O    O  N N 92  
ASN   CB   C  N N 93  
ASN   CG   C  N N 94  
ASN   OD1  O  N N 95  
ASN   ND2  N  N N 96  
ASN   OXT  O  N N 97  
ASN   H    H  N N 98  
ASN   H2   H  N N 99  
ASN   HA   H  N N 100 
ASN   HB2  H  N N 101 
ASN   HB3  H  N N 102 
ASN   HD21 H  N N 103 
ASN   HD22 H  N N 104 
ASN   HXT  H  N N 105 
ASP   N    N  N N 106 
ASP   CA   C  N S 107 
ASP   C    C  N N 108 
ASP   O    O  N N 109 
ASP   CB   C  N N 110 
ASP   CG   C  N N 111 
ASP   OD1  O  N N 112 
ASP   OD2  O  N N 113 
ASP   OXT  O  N N 114 
ASP   H    H  N N 115 
ASP   H2   H  N N 116 
ASP   HA   H  N N 117 
ASP   HB2  H  N N 118 
ASP   HB3  H  N N 119 
ASP   HD2  H  N N 120 
ASP   HXT  H  N N 121 
CYS   N    N  N N 122 
CYS   CA   C  N R 123 
CYS   C    C  N N 124 
CYS   O    O  N N 125 
CYS   CB   C  N N 126 
CYS   SG   S  N N 127 
CYS   OXT  O  N N 128 
CYS   H    H  N N 129 
CYS   H2   H  N N 130 
CYS   HA   H  N N 131 
CYS   HB2  H  N N 132 
CYS   HB3  H  N N 133 
CYS   HG   H  N N 134 
CYS   HXT  H  N N 135 
EDO   C1   C  N N 136 
EDO   O1   O  N N 137 
EDO   C2   C  N N 138 
EDO   O2   O  N N 139 
EDO   H11  H  N N 140 
EDO   H12  H  N N 141 
EDO   HO1  H  N N 142 
EDO   H21  H  N N 143 
EDO   H22  H  N N 144 
EDO   HO2  H  N N 145 
GLN   N    N  N N 146 
GLN   CA   C  N S 147 
GLN   C    C  N N 148 
GLN   O    O  N N 149 
GLN   CB   C  N N 150 
GLN   CG   C  N N 151 
GLN   CD   C  N N 152 
GLN   OE1  O  N N 153 
GLN   NE2  N  N N 154 
GLN   OXT  O  N N 155 
GLN   H    H  N N 156 
GLN   H2   H  N N 157 
GLN   HA   H  N N 158 
GLN   HB2  H  N N 159 
GLN   HB3  H  N N 160 
GLN   HG2  H  N N 161 
GLN   HG3  H  N N 162 
GLN   HE21 H  N N 163 
GLN   HE22 H  N N 164 
GLN   HXT  H  N N 165 
GLU   N    N  N N 166 
GLU   CA   C  N S 167 
GLU   C    C  N N 168 
GLU   O    O  N N 169 
GLU   CB   C  N N 170 
GLU   CG   C  N N 171 
GLU   CD   C  N N 172 
GLU   OE1  O  N N 173 
GLU   OE2  O  N N 174 
GLU   OXT  O  N N 175 
GLU   H    H  N N 176 
GLU   H2   H  N N 177 
GLU   HA   H  N N 178 
GLU   HB2  H  N N 179 
GLU   HB3  H  N N 180 
GLU   HG2  H  N N 181 
GLU   HG3  H  N N 182 
GLU   HE2  H  N N 183 
GLU   HXT  H  N N 184 
GLY   N    N  N N 185 
GLY   CA   C  N N 186 
GLY   C    C  N N 187 
GLY   O    O  N N 188 
GLY   OXT  O  N N 189 
GLY   H    H  N N 190 
GLY   H2   H  N N 191 
GLY   HA2  H  N N 192 
GLY   HA3  H  N N 193 
GLY   HXT  H  N N 194 
GOL   C1   C  N N 195 
GOL   O1   O  N N 196 
GOL   C2   C  N N 197 
GOL   O2   O  N N 198 
GOL   C3   C  N N 199 
GOL   O3   O  N N 200 
GOL   H11  H  N N 201 
GOL   H12  H  N N 202 
GOL   HO1  H  N N 203 
GOL   H2   H  N N 204 
GOL   HO2  H  N N 205 
GOL   H31  H  N N 206 
GOL   H32  H  N N 207 
GOL   HO3  H  N N 208 
HIS   N    N  N N 209 
HIS   CA   C  N S 210 
HIS   C    C  N N 211 
HIS   O    O  N N 212 
HIS   CB   C  N N 213 
HIS   CG   C  Y N 214 
HIS   ND1  N  Y N 215 
HIS   CD2  C  Y N 216 
HIS   CE1  C  Y N 217 
HIS   NE2  N  Y N 218 
HIS   OXT  O  N N 219 
HIS   H    H  N N 220 
HIS   H2   H  N N 221 
HIS   HA   H  N N 222 
HIS   HB2  H  N N 223 
HIS   HB3  H  N N 224 
HIS   HD1  H  N N 225 
HIS   HD2  H  N N 226 
HIS   HE1  H  N N 227 
HIS   HE2  H  N N 228 
HIS   HXT  H  N N 229 
HOH   O    O  N N 230 
HOH   H1   H  N N 231 
HOH   H2   H  N N 232 
ILE   N    N  N N 233 
ILE   CA   C  N S 234 
ILE   C    C  N N 235 
ILE   O    O  N N 236 
ILE   CB   C  N S 237 
ILE   CG1  C  N N 238 
ILE   CG2  C  N N 239 
ILE   CD1  C  N N 240 
ILE   OXT  O  N N 241 
ILE   H    H  N N 242 
ILE   H2   H  N N 243 
ILE   HA   H  N N 244 
ILE   HB   H  N N 245 
ILE   HG12 H  N N 246 
ILE   HG13 H  N N 247 
ILE   HG21 H  N N 248 
ILE   HG22 H  N N 249 
ILE   HG23 H  N N 250 
ILE   HD11 H  N N 251 
ILE   HD12 H  N N 252 
ILE   HD13 H  N N 253 
ILE   HXT  H  N N 254 
LEU   N    N  N N 255 
LEU   CA   C  N S 256 
LEU   C    C  N N 257 
LEU   O    O  N N 258 
LEU   CB   C  N N 259 
LEU   CG   C  N N 260 
LEU   CD1  C  N N 261 
LEU   CD2  C  N N 262 
LEU   OXT  O  N N 263 
LEU   H    H  N N 264 
LEU   H2   H  N N 265 
LEU   HA   H  N N 266 
LEU   HB2  H  N N 267 
LEU   HB3  H  N N 268 
LEU   HG   H  N N 269 
LEU   HD11 H  N N 270 
LEU   HD12 H  N N 271 
LEU   HD13 H  N N 272 
LEU   HD21 H  N N 273 
LEU   HD22 H  N N 274 
LEU   HD23 H  N N 275 
LEU   HXT  H  N N 276 
LYS   N    N  N N 277 
LYS   CA   C  N S 278 
LYS   C    C  N N 279 
LYS   O    O  N N 280 
LYS   CB   C  N N 281 
LYS   CG   C  N N 282 
LYS   CD   C  N N 283 
LYS   CE   C  N N 284 
LYS   NZ   N  N N 285 
LYS   OXT  O  N N 286 
LYS   H    H  N N 287 
LYS   H2   H  N N 288 
LYS   HA   H  N N 289 
LYS   HB2  H  N N 290 
LYS   HB3  H  N N 291 
LYS   HG2  H  N N 292 
LYS   HG3  H  N N 293 
LYS   HD2  H  N N 294 
LYS   HD3  H  N N 295 
LYS   HE2  H  N N 296 
LYS   HE3  H  N N 297 
LYS   HZ1  H  N N 298 
LYS   HZ2  H  N N 299 
LYS   HZ3  H  N N 300 
LYS   HXT  H  N N 301 
MET   N    N  N N 302 
MET   CA   C  N S 303 
MET   C    C  N N 304 
MET   O    O  N N 305 
MET   CB   C  N N 306 
MET   CG   C  N N 307 
MET   SD   S  N N 308 
MET   CE   C  N N 309 
MET   OXT  O  N N 310 
MET   H    H  N N 311 
MET   H2   H  N N 312 
MET   HA   H  N N 313 
MET   HB2  H  N N 314 
MET   HB3  H  N N 315 
MET   HG2  H  N N 316 
MET   HG3  H  N N 317 
MET   HE1  H  N N 318 
MET   HE2  H  N N 319 
MET   HE3  H  N N 320 
MET   HXT  H  N N 321 
PHE   N    N  N N 322 
PHE   CA   C  N S 323 
PHE   C    C  N N 324 
PHE   O    O  N N 325 
PHE   CB   C  N N 326 
PHE   CG   C  Y N 327 
PHE   CD1  C  Y N 328 
PHE   CD2  C  Y N 329 
PHE   CE1  C  Y N 330 
PHE   CE2  C  Y N 331 
PHE   CZ   C  Y N 332 
PHE   OXT  O  N N 333 
PHE   H    H  N N 334 
PHE   H2   H  N N 335 
PHE   HA   H  N N 336 
PHE   HB2  H  N N 337 
PHE   HB3  H  N N 338 
PHE   HD1  H  N N 339 
PHE   HD2  H  N N 340 
PHE   HE1  H  N N 341 
PHE   HE2  H  N N 342 
PHE   HZ   H  N N 343 
PHE   HXT  H  N N 344 
PRO   N    N  N N 345 
PRO   CA   C  N S 346 
PRO   C    C  N N 347 
PRO   O    O  N N 348 
PRO   CB   C  N N 349 
PRO   CG   C  N N 350 
PRO   CD   C  N N 351 
PRO   OXT  O  N N 352 
PRO   H    H  N N 353 
PRO   HA   H  N N 354 
PRO   HB2  H  N N 355 
PRO   HB3  H  N N 356 
PRO   HG2  H  N N 357 
PRO   HG3  H  N N 358 
PRO   HD2  H  N N 359 
PRO   HD3  H  N N 360 
PRO   HXT  H  N N 361 
SER   N    N  N N 362 
SER   CA   C  N S 363 
SER   C    C  N N 364 
SER   O    O  N N 365 
SER   CB   C  N N 366 
SER   OG   O  N N 367 
SER   OXT  O  N N 368 
SER   H    H  N N 369 
SER   H2   H  N N 370 
SER   HA   H  N N 371 
SER   HB2  H  N N 372 
SER   HB3  H  N N 373 
SER   HG   H  N N 374 
SER   HXT  H  N N 375 
SO4   S    S  N N 376 
SO4   O1   O  N N 377 
SO4   O2   O  N N 378 
SO4   O3   O  N N 379 
SO4   O4   O  N N 380 
TF3   C1   C  Y N 381 
TF3   C2   C  Y N 382 
TF3   C3   C  Y N 383 
TF3   O1   O  N N 384 
TF3   C4   C  Y N 385 
TF3   CL1  CL N N 386 
TF3   C5   C  Y N 387 
TF3   C6   C  N N 388 
TF3   C7   C  Y N 389 
TF3   C8   C  Y N 390 
TF3   C9   C  N N 391 
TF3   C10  C  Y N 392 
TF3   C11  C  Y N 393 
TF3   C12  C  N N 394 
TF3   C13  C  Y N 395 
TF3   C14  C  Y N 396 
TF3   N1   N  N N 397 
TF3   O2   O  N N 398 
TF3   C15  C  Y N 399 
TF3   C16  C  N N 400 
TF3   C17  C  N N 401 
TF3   C18  C  N N 402 
TF3   C19  C  N N 403 
TF3   C20  C  N N 404 
TF3   N2   N  N N 405 
TF3   H3   H  N N 406 
TF3   H4   H  N N 407 
TF3   H5   H  N N 408 
TF3   H6C1 H  N N 409 
TF3   H6C2 H  N N 410 
TF3   H9C1 H  N N 411 
TF3   H9C2 H  N N 412 
TF3   H10  H  N N 413 
TF3   H11  H  N N 414 
TF3   H13  H  N N 415 
TF3   H14  H  N N 416 
TF3   H1   H  N N 417 
TF3   H161 H  N N 418 
TF3   H162 H  N N 419 
TF3   H17  H  N N 420 
TF3   H181 H  N N 421 
TF3   H182 H  N N 422 
TF3   H191 H  N N 423 
TF3   H192 H  N N 424 
TF3   H193 H  N N 425 
TF3   H201 H  N N 426 
TF3   H202 H  N N 427 
TF3   H203 H  N N 428 
TF3   H2N1 H  N N 429 
TF3   H2N2 H  N N 430 
THR   N    N  N N 431 
THR   CA   C  N S 432 
THR   C    C  N N 433 
THR   O    O  N N 434 
THR   CB   C  N R 435 
THR   OG1  O  N N 436 
THR   CG2  C  N N 437 
THR   OXT  O  N N 438 
THR   H    H  N N 439 
THR   H2   H  N N 440 
THR   HA   H  N N 441 
THR   HB   H  N N 442 
THR   HG1  H  N N 443 
THR   HG21 H  N N 444 
THR   HG22 H  N N 445 
THR   HG23 H  N N 446 
THR   HXT  H  N N 447 
TRP   N    N  N N 448 
TRP   CA   C  N S 449 
TRP   C    C  N N 450 
TRP   O    O  N N 451 
TRP   CB   C  N N 452 
TRP   CG   C  Y N 453 
TRP   CD1  C  Y N 454 
TRP   CD2  C  Y N 455 
TRP   NE1  N  Y N 456 
TRP   CE2  C  Y N 457 
TRP   CE3  C  Y N 458 
TRP   CZ2  C  Y N 459 
TRP   CZ3  C  Y N 460 
TRP   CH2  C  Y N 461 
TRP   OXT  O  N N 462 
TRP   H    H  N N 463 
TRP   H2   H  N N 464 
TRP   HA   H  N N 465 
TRP   HB2  H  N N 466 
TRP   HB3  H  N N 467 
TRP   HD1  H  N N 468 
TRP   HE1  H  N N 469 
TRP   HE3  H  N N 470 
TRP   HZ2  H  N N 471 
TRP   HZ3  H  N N 472 
TRP   HH2  H  N N 473 
TRP   HXT  H  N N 474 
TYR   N    N  N N 475 
TYR   CA   C  N S 476 
TYR   C    C  N N 477 
TYR   O    O  N N 478 
TYR   CB   C  N N 479 
TYR   CG   C  Y N 480 
TYR   CD1  C  Y N 481 
TYR   CD2  C  Y N 482 
TYR   CE1  C  Y N 483 
TYR   CE2  C  Y N 484 
TYR   CZ   C  Y N 485 
TYR   OH   O  N N 486 
TYR   OXT  O  N N 487 
TYR   H    H  N N 488 
TYR   H2   H  N N 489 
TYR   HA   H  N N 490 
TYR   HB2  H  N N 491 
TYR   HB3  H  N N 492 
TYR   HD1  H  N N 493 
TYR   HD2  H  N N 494 
TYR   HE1  H  N N 495 
TYR   HE2  H  N N 496 
TYR   HH   H  N N 497 
TYR   HXT  H  N N 498 
VAL   N    N  N N 499 
VAL   CA   C  N S 500 
VAL   C    C  N N 501 
VAL   O    O  N N 502 
VAL   CB   C  N N 503 
VAL   CG1  C  N N 504 
VAL   CG2  C  N N 505 
VAL   OXT  O  N N 506 
VAL   H    H  N N 507 
VAL   H2   H  N N 508 
VAL   HA   H  N N 509 
VAL   HB   H  N N 510 
VAL   HG11 H  N N 511 
VAL   HG12 H  N N 512 
VAL   HG13 H  N N 513 
VAL   HG21 H  N N 514 
VAL   HG22 H  N N 515 
VAL   HG23 H  N N 516 
VAL   HXT  H  N N 517 
# 
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 
A1EQH O   S    doub N N 1   
A1EQH S   C    sing N N 2   
A1EQH S   O1   doub N N 3   
A1EQH C20 C    doub Y N 4   
A1EQH C20 C19  sing Y N 5   
A1EQH C   C1   sing Y N 6   
A1EQH C19 C18  doub Y N 7   
A1EQH C1  C2   doub Y N 8   
A1EQH C18 C2   sing Y N 9   
A1EQH C2  O2   sing N N 10  
A1EQH O2  C3   sing N N 11  
A1EQH C3  C17  doub Y N 12  
A1EQH C3  C4   sing Y N 13  
A1EQH C17 C16  sing Y N 14  
A1EQH F   C13  sing N N 15  
A1EQH C4  C5   doub Y N 16  
A1EQH C16 C6   doub Y N 17  
A1EQH C14 C13  doub Y N 18  
A1EQH C14 C15  sing Y N 19  
A1EQH C13 C12  sing Y N 20  
A1EQH C5  C6   sing Y N 21  
A1EQH C6  N    sing N N 22  
A1EQH C15 N    sing N N 23  
A1EQH C15 C8   doub Y N 24  
A1EQH C12 C9   doub Y N 25  
A1EQH N   C7   sing N N 26  
A1EQH C8  C9   sing Y N 27  
A1EQH C8  N1   sing N N 28  
A1EQH C9  N2   sing N N 29  
A1EQH C7  O3   doub N N 30  
A1EQH C7  N1   sing N N 31  
A1EQH N2  C10  sing N N 32  
A1EQH C10 C11  sing N N 33  
A1EQH C10 H1   sing N N 34  
A1EQH C10 H2   sing N N 35  
A1EQH C11 H3   sing N N 36  
A1EQH C11 H4   sing N N 37  
A1EQH C11 H5   sing N N 38  
A1EQH C16 H6   sing N N 39  
A1EQH C17 H7   sing N N 40  
A1EQH C18 H8   sing N N 41  
A1EQH C19 H9   sing N N 42  
A1EQH C20 H10  sing N N 43  
A1EQH C1  H12  sing N N 44  
A1EQH C12 H13  sing N N 45  
A1EQH C14 H14  sing N N 46  
A1EQH C4  H15  sing N N 47  
A1EQH C5  H16  sing N N 48  
A1EQH N1  H17  sing N N 49  
A1EQH N2  H18  sing N N 50  
A1EQH S   F1   sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CYS   N   CA   sing N N 121 
CYS   N   H    sing N N 122 
CYS   N   H2   sing N N 123 
CYS   CA  C    sing N N 124 
CYS   CA  CB   sing N N 125 
CYS   CA  HA   sing N N 126 
CYS   C   O    doub N N 127 
CYS   C   OXT  sing N N 128 
CYS   CB  SG   sing N N 129 
CYS   CB  HB2  sing N N 130 
CYS   CB  HB3  sing N N 131 
CYS   SG  HG   sing N N 132 
CYS   OXT HXT  sing N N 133 
EDO   C1  O1   sing N N 134 
EDO   C1  C2   sing N N 135 
EDO   C1  H11  sing N N 136 
EDO   C1  H12  sing N N 137 
EDO   O1  HO1  sing N N 138 
EDO   C2  O2   sing N N 139 
EDO   C2  H21  sing N N 140 
EDO   C2  H22  sing N N 141 
EDO   O2  HO2  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
GOL   C1  O1   sing N N 189 
GOL   C1  C2   sing N N 190 
GOL   C1  H11  sing N N 191 
GOL   C1  H12  sing N N 192 
GOL   O1  HO1  sing N N 193 
GOL   C2  O2   sing N N 194 
GOL   C2  C3   sing N N 195 
GOL   C2  H2   sing N N 196 
GOL   O2  HO2  sing N N 197 
GOL   C3  O3   sing N N 198 
GOL   C3  H31  sing N N 199 
GOL   C3  H32  sing N N 200 
GOL   O3  HO3  sing N N 201 
HIS   N   CA   sing N N 202 
HIS   N   H    sing N N 203 
HIS   N   H2   sing N N 204 
HIS   CA  C    sing N N 205 
HIS   CA  CB   sing N N 206 
HIS   CA  HA   sing N N 207 
HIS   C   O    doub N N 208 
HIS   C   OXT  sing N N 209 
HIS   CB  CG   sing N N 210 
HIS   CB  HB2  sing N N 211 
HIS   CB  HB3  sing N N 212 
HIS   CG  ND1  sing Y N 213 
HIS   CG  CD2  doub Y N 214 
HIS   ND1 CE1  doub Y N 215 
HIS   ND1 HD1  sing N N 216 
HIS   CD2 NE2  sing Y N 217 
HIS   CD2 HD2  sing N N 218 
HIS   CE1 NE2  sing Y N 219 
HIS   CE1 HE1  sing N N 220 
HIS   NE2 HE2  sing N N 221 
HIS   OXT HXT  sing N N 222 
HOH   O   H1   sing N N 223 
HOH   O   H2   sing N N 224 
ILE   N   CA   sing N N 225 
ILE   N   H    sing N N 226 
ILE   N   H2   sing N N 227 
ILE   CA  C    sing N N 228 
ILE   CA  CB   sing N N 229 
ILE   CA  HA   sing N N 230 
ILE   C   O    doub N N 231 
ILE   C   OXT  sing N N 232 
ILE   CB  CG1  sing N N 233 
ILE   CB  CG2  sing N N 234 
ILE   CB  HB   sing N N 235 
ILE   CG1 CD1  sing N N 236 
ILE   CG1 HG12 sing N N 237 
ILE   CG1 HG13 sing N N 238 
ILE   CG2 HG21 sing N N 239 
ILE   CG2 HG22 sing N N 240 
ILE   CG2 HG23 sing N N 241 
ILE   CD1 HD11 sing N N 242 
ILE   CD1 HD12 sing N N 243 
ILE   CD1 HD13 sing N N 244 
ILE   OXT HXT  sing N N 245 
LEU   N   CA   sing N N 246 
LEU   N   H    sing N N 247 
LEU   N   H2   sing N N 248 
LEU   CA  C    sing N N 249 
LEU   CA  CB   sing N N 250 
LEU   CA  HA   sing N N 251 
LEU   C   O    doub N N 252 
LEU   C   OXT  sing N N 253 
LEU   CB  CG   sing N N 254 
LEU   CB  HB2  sing N N 255 
LEU   CB  HB3  sing N N 256 
LEU   CG  CD1  sing N N 257 
LEU   CG  CD2  sing N N 258 
LEU   CG  HG   sing N N 259 
LEU   CD1 HD11 sing N N 260 
LEU   CD1 HD12 sing N N 261 
LEU   CD1 HD13 sing N N 262 
LEU   CD2 HD21 sing N N 263 
LEU   CD2 HD22 sing N N 264 
LEU   CD2 HD23 sing N N 265 
LEU   OXT HXT  sing N N 266 
LYS   N   CA   sing N N 267 
LYS   N   H    sing N N 268 
LYS   N   H2   sing N N 269 
LYS   CA  C    sing N N 270 
LYS   CA  CB   sing N N 271 
LYS   CA  HA   sing N N 272 
LYS   C   O    doub N N 273 
LYS   C   OXT  sing N N 274 
LYS   CB  CG   sing N N 275 
LYS   CB  HB2  sing N N 276 
LYS   CB  HB3  sing N N 277 
LYS   CG  CD   sing N N 278 
LYS   CG  HG2  sing N N 279 
LYS   CG  HG3  sing N N 280 
LYS   CD  CE   sing N N 281 
LYS   CD  HD2  sing N N 282 
LYS   CD  HD3  sing N N 283 
LYS   CE  NZ   sing N N 284 
LYS   CE  HE2  sing N N 285 
LYS   CE  HE3  sing N N 286 
LYS   NZ  HZ1  sing N N 287 
LYS   NZ  HZ2  sing N N 288 
LYS   NZ  HZ3  sing N N 289 
LYS   OXT HXT  sing N N 290 
MET   N   CA   sing N N 291 
MET   N   H    sing N N 292 
MET   N   H2   sing N N 293 
MET   CA  C    sing N N 294 
MET   CA  CB   sing N N 295 
MET   CA  HA   sing N N 296 
MET   C   O    doub N N 297 
MET   C   OXT  sing N N 298 
MET   CB  CG   sing N N 299 
MET   CB  HB2  sing N N 300 
MET   CB  HB3  sing N N 301 
MET   CG  SD   sing N N 302 
MET   CG  HG2  sing N N 303 
MET   CG  HG3  sing N N 304 
MET   SD  CE   sing N N 305 
MET   CE  HE1  sing N N 306 
MET   CE  HE2  sing N N 307 
MET   CE  HE3  sing N N 308 
MET   OXT HXT  sing N N 309 
PHE   N   CA   sing N N 310 
PHE   N   H    sing N N 311 
PHE   N   H2   sing N N 312 
PHE   CA  C    sing N N 313 
PHE   CA  CB   sing N N 314 
PHE   CA  HA   sing N N 315 
PHE   C   O    doub N N 316 
PHE   C   OXT  sing N N 317 
PHE   CB  CG   sing N N 318 
PHE   CB  HB2  sing N N 319 
PHE   CB  HB3  sing N N 320 
PHE   CG  CD1  doub Y N 321 
PHE   CG  CD2  sing Y N 322 
PHE   CD1 CE1  sing Y N 323 
PHE   CD1 HD1  sing N N 324 
PHE   CD2 CE2  doub Y N 325 
PHE   CD2 HD2  sing N N 326 
PHE   CE1 CZ   doub Y N 327 
PHE   CE1 HE1  sing N N 328 
PHE   CE2 CZ   sing Y N 329 
PHE   CE2 HE2  sing N N 330 
PHE   CZ  HZ   sing N N 331 
PHE   OXT HXT  sing N N 332 
PRO   N   CA   sing N N 333 
PRO   N   CD   sing N N 334 
PRO   N   H    sing N N 335 
PRO   CA  C    sing N N 336 
PRO   CA  CB   sing N N 337 
PRO   CA  HA   sing N N 338 
PRO   C   O    doub N N 339 
PRO   C   OXT  sing N N 340 
PRO   CB  CG   sing N N 341 
PRO   CB  HB2  sing N N 342 
PRO   CB  HB3  sing N N 343 
PRO   CG  CD   sing N N 344 
PRO   CG  HG2  sing N N 345 
PRO   CG  HG3  sing N N 346 
PRO   CD  HD2  sing N N 347 
PRO   CD  HD3  sing N N 348 
PRO   OXT HXT  sing N N 349 
SER   N   CA   sing N N 350 
SER   N   H    sing N N 351 
SER   N   H2   sing N N 352 
SER   CA  C    sing N N 353 
SER   CA  CB   sing N N 354 
SER   CA  HA   sing N N 355 
SER   C   O    doub N N 356 
SER   C   OXT  sing N N 357 
SER   CB  OG   sing N N 358 
SER   CB  HB2  sing N N 359 
SER   CB  HB3  sing N N 360 
SER   OG  HG   sing N N 361 
SER   OXT HXT  sing N N 362 
SO4   S   O1   doub N N 363 
SO4   S   O2   doub N N 364 
SO4   S   O3   sing N N 365 
SO4   S   O4   sing N N 366 
TF3   C1  C2   doub Y N 367 
TF3   C1  C3   sing Y N 368 
TF3   C1  O1   sing N N 369 
TF3   C2  C4   sing Y N 370 
TF3   C2  CL1  sing N N 371 
TF3   C3  C5   doub Y N 372 
TF3   C3  H3   sing N N 373 
TF3   O1  C6   sing N N 374 
TF3   C4  C7   doub Y N 375 
TF3   C4  H4   sing N N 376 
TF3   C5  C7   sing Y N 377 
TF3   C5  H5   sing N N 378 
TF3   C6  C8   sing N N 379 
TF3   C6  H6C1 sing N N 380 
TF3   C6  H6C2 sing N N 381 
TF3   C7  C9   sing N N 382 
TF3   C8  C10  doub Y N 383 
TF3   C8  C11  sing Y N 384 
TF3   C9  C12  sing N N 385 
TF3   C9  H9C1 sing N N 386 
TF3   C9  H9C2 sing N N 387 
TF3   C10 C13  sing Y N 388 
TF3   C10 H10  sing N N 389 
TF3   C11 C14  doub Y N 390 
TF3   C11 H11  sing N N 391 
TF3   C12 N1   sing N N 392 
TF3   C12 O2   doub N N 393 
TF3   C13 C15  doub Y N 394 
TF3   C13 H13  sing N N 395 
TF3   C14 C15  sing Y N 396 
TF3   C14 H14  sing N N 397 
TF3   N1  C16  sing N N 398 
TF3   N1  H1   sing N N 399 
TF3   C15 C17  sing N N 400 
TF3   C16 C18  sing N N 401 
TF3   C16 H161 sing N N 402 
TF3   C16 H162 sing N N 403 
TF3   C17 C19  sing N N 404 
TF3   C17 C20  sing N N 405 
TF3   C17 H17  sing N N 406 
TF3   C18 N2   sing N N 407 
TF3   C18 H181 sing N N 408 
TF3   C18 H182 sing N N 409 
TF3   C19 H191 sing N N 410 
TF3   C19 H192 sing N N 411 
TF3   C19 H193 sing N N 412 
TF3   C20 H201 sing N N 413 
TF3   C20 H202 sing N N 414 
TF3   C20 H203 sing N N 415 
TF3   N2  H2N1 sing N N 416 
TF3   N2  H2N2 sing N N 417 
THR   N   CA   sing N N 418 
THR   N   H    sing N N 419 
THR   N   H2   sing N N 420 
THR   CA  C    sing N N 421 
THR   CA  CB   sing N N 422 
THR   CA  HA   sing N N 423 
THR   C   O    doub N N 424 
THR   C   OXT  sing N N 425 
THR   CB  OG1  sing N N 426 
THR   CB  CG2  sing N N 427 
THR   CB  HB   sing N N 428 
THR   OG1 HG1  sing N N 429 
THR   CG2 HG21 sing N N 430 
THR   CG2 HG22 sing N N 431 
THR   CG2 HG23 sing N N 432 
THR   OXT HXT  sing N N 433 
TRP   N   CA   sing N N 434 
TRP   N   H    sing N N 435 
TRP   N   H2   sing N N 436 
TRP   CA  C    sing N N 437 
TRP   CA  CB   sing N N 438 
TRP   CA  HA   sing N N 439 
TRP   C   O    doub N N 440 
TRP   C   OXT  sing N N 441 
TRP   CB  CG   sing N N 442 
TRP   CB  HB2  sing N N 443 
TRP   CB  HB3  sing N N 444 
TRP   CG  CD1  doub Y N 445 
TRP   CG  CD2  sing Y N 446 
TRP   CD1 NE1  sing Y N 447 
TRP   CD1 HD1  sing N N 448 
TRP   CD2 CE2  doub Y N 449 
TRP   CD2 CE3  sing Y N 450 
TRP   NE1 CE2  sing Y N 451 
TRP   NE1 HE1  sing N N 452 
TRP   CE2 CZ2  sing Y N 453 
TRP   CE3 CZ3  doub Y N 454 
TRP   CE3 HE3  sing N N 455 
TRP   CZ2 CH2  doub Y N 456 
TRP   CZ2 HZ2  sing N N 457 
TRP   CZ3 CH2  sing Y N 458 
TRP   CZ3 HZ3  sing N N 459 
TRP   CH2 HH2  sing N N 460 
TRP   OXT HXT  sing N N 461 
TYR   N   CA   sing N N 462 
TYR   N   H    sing N N 463 
TYR   N   H2   sing N N 464 
TYR   CA  C    sing N N 465 
TYR   CA  CB   sing N N 466 
TYR   CA  HA   sing N N 467 
TYR   C   O    doub N N 468 
TYR   C   OXT  sing N N 469 
TYR   CB  CG   sing N N 470 
TYR   CB  HB2  sing N N 471 
TYR   CB  HB3  sing N N 472 
TYR   CG  CD1  doub Y N 473 
TYR   CG  CD2  sing Y N 474 
TYR   CD1 CE1  sing Y N 475 
TYR   CD1 HD1  sing N N 476 
TYR   CD2 CE2  doub Y N 477 
TYR   CD2 HD2  sing N N 478 
TYR   CE1 CZ   doub Y N 479 
TYR   CE1 HE1  sing N N 480 
TYR   CE2 CZ   sing Y N 481 
TYR   CE2 HE2  sing N N 482 
TYR   CZ  OH   sing N N 483 
TYR   OH  HH   sing N N 484 
TYR   OXT HXT  sing N N 485 
VAL   N   CA   sing N N 486 
VAL   N   H    sing N N 487 
VAL   N   H2   sing N N 488 
VAL   CA  C    sing N N 489 
VAL   CA  CB   sing N N 490 
VAL   CA  HA   sing N N 491 
VAL   C   O    doub N N 492 
VAL   C   OXT  sing N N 493 
VAL   CB  CG1  sing N N 494 
VAL   CB  CG2  sing N N 495 
VAL   CB  HB   sing N N 496 
VAL   CG1 HG11 sing N N 497 
VAL   CG1 HG12 sing N N 498 
VAL   CG1 HG13 sing N N 499 
VAL   CG2 HG21 sing N N 500 
VAL   CG2 HG22 sing N N 501 
VAL   CG2 HG23 sing N N 502 
VAL   OXT HXT  sing N N 503 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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   2Q8F 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9M3R 
_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]   0.009107 
_atom_sites.fract_transf_matrix[1][2]   0.005258 
_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]   0.010516 
_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]   0.011846 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . PRO   A 1 1   ? -44.237 24.817  -55.085 1.00 87.66  ? 17  PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 1   ? -43.332 25.685  -54.318 1.00 91.49  ? 17  PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 1   ? -41.949 25.052  -54.183 1.00 97.42  ? 17  PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 1   ? -41.783 24.139  -53.377 1.00 89.82  ? 17  PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 1   ? -44.022 25.805  -52.951 1.00 92.01  ? 17  PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 1   ? -45.409 25.249  -53.149 1.00 83.28  ? 17  PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 1   ? -45.284 24.235  -54.233 1.00 90.36  ? 17  PRO   A CD  1 
ATOM   8    N  N   . LYS   A 1 2   ? -40.977 25.532  -54.968 1.00 109.31 ? 18  LYS   A N   1 
ATOM   9    C  CA  . LYS   A 1 2   ? -39.710 24.812  -55.092 1.00 111.00 ? 18  LYS   A CA  1 
ATOM   10   C  C   . LYS   A 1 2   ? -38.885 24.860  -53.811 1.00 111.73 ? 18  LYS   A C   1 
ATOM   11   O  O   . LYS   A 1 2   ? -38.204 23.883  -53.474 1.00 110.50 ? 18  LYS   A O   1 
ATOM   12   C  CB  . LYS   A 1 2   ? -38.905 25.351  -56.276 1.00 109.38 ? 18  LYS   A CB  1 
ATOM   13   C  CG  . LYS   A 1 2   ? -39.300 24.718  -57.593 1.00 115.29 ? 18  LYS   A CG  1 
ATOM   14   C  CD  . LYS   A 1 2   ? -39.454 23.218  -57.425 1.00 118.43 ? 18  LYS   A CD  1 
ATOM   15   C  CE  . LYS   A 1 2   ? -40.292 22.626  -58.541 1.00 119.58 ? 18  LYS   A CE  1 
ATOM   16   N  NZ  . LYS   A 1 2   ? -40.922 21.350  -58.095 1.00 126.17 ? 18  LYS   A NZ  1 
ATOM   17   N  N   . TYR   A 1 3   ? -38.908 25.991  -53.102 1.00 95.37  ? 19  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 3   ? -38.183 26.089  -51.834 1.00 91.85  ? 19  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 3   ? -38.738 25.104  -50.800 1.00 89.03  ? 19  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 3   ? -37.976 24.461  -50.062 1.00 82.38  ? 19  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 3   ? -38.248 27.527  -51.313 1.00 89.35  ? 19  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 3   ? -39.662 28.061  -51.136 1.00 94.47  ? 19  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 3   ? -40.420 28.494  -52.226 1.00 94.14  ? 19  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 3   ? -40.234 28.136  -49.879 1.00 91.62  ? 19  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 3   ? -41.701 28.974  -52.056 1.00 90.47  ? 19  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 3   ? -41.513 28.618  -49.703 1.00 91.27  ? 19  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 3   ? -42.240 29.034  -50.791 1.00 91.98  ? 19  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 3   ? -43.517 29.510  -50.606 1.00 101.48 ? 19  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 4   ? -40.063 24.964  -50.737 1.00 87.66  ? 20  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 4   ? -40.660 23.869  -49.978 1.00 83.36  ? 20  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 4   ? -40.247 22.537  -50.578 1.00 82.88  ? 20  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 4   ? -39.908 21.590  -49.861 1.00 68.05  ? 20  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 4   ? -42.194 24.008  -49.945 1.00 81.45  ? 20  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 4   ? -42.615 25.209  -49.102 1.00 84.77  ? 20  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 4   ? -42.844 22.728  -49.418 1.00 72.93  ? 20  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 4   ? -44.065 25.585  -49.301 1.00 87.08  ? 20  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 5   ? -40.272 22.445  -51.910 1.00 81.80  ? 21  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 5   ? -39.951 21.191  -52.576 1.00 84.25  ? 21  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 5   ? -38.534 20.735  -52.253 1.00 80.34  ? 21  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 5   ? -38.293 19.538  -52.060 1.00 78.25  ? 21  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 5   ? -40.134 21.355  -54.084 1.00 95.17  ? 21  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 5   ? -40.160 20.051  -54.855 1.00 94.91  ? 21  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 5   ? -41.398 19.233  -54.551 1.00 103.64 ? 21  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 5   ? -42.386 19.810  -54.036 1.00 102.88 ? 21  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 5   ? -41.384 18.014  -54.828 1.00 109.57 ? 21  GLU   A OE2 1 
ATOM   46   N  N   . HIS   A 1 6   ? -37.587 21.676  -52.187 1.00 78.74  ? 22  HIS   A N   1 
ATOM   47   C  CA  . HIS   A 1 6   ? -36.201 21.328  -51.891 1.00 77.66  ? 22  HIS   A CA  1 
ATOM   48   C  C   . HIS   A 1 6   ? -36.071 20.670  -50.523 1.00 75.27  ? 22  HIS   A C   1 
ATOM   49   O  O   . HIS   A 1 6   ? -35.549 19.556  -50.397 1.00 77.72  ? 22  HIS   A O   1 
ATOM   50   C  CB  . HIS   A 1 6   ? -35.313 22.568  -51.950 1.00 76.71  ? 22  HIS   A CB  1 
ATOM   51   C  CG  . HIS   A 1 6   ? -33.892 22.304  -51.555 1.00 78.42  ? 22  HIS   A CG  1 
ATOM   52   N  ND1 . HIS   A 1 6   ? -33.002 21.651  -52.381 1.00 77.47  ? 22  HIS   A ND1 1 
ATOM   53   C  CD2 . HIS   A 1 6   ? -33.212 22.586  -50.417 1.00 76.54  ? 22  HIS   A CD2 1 
ATOM   54   C  CE1 . HIS   A 1 6   ? -31.834 21.549  -51.771 1.00 78.74  ? 22  HIS   A CE1 1 
ATOM   55   N  NE2 . HIS   A 1 6   ? -31.932 22.112  -50.581 1.00 73.87  ? 22  HIS   A NE2 1 
ATOM   56   N  N   . PHE   A 1 7   ? -36.516 21.361  -49.475 1.00 71.29  ? 23  PHE   A N   1 
ATOM   57   C  CA  . PHE   A 1 7   ? -36.258 20.852  -48.135 1.00 69.43  ? 23  PHE   A CA  1 
ATOM   58   C  C   . PHE   A 1 7   ? -37.138 19.654  -47.802 1.00 64.53  ? 23  PHE   A C   1 
ATOM   59   O  O   . PHE   A 1 7   ? -36.737 18.796  -47.005 1.00 64.75  ? 23  PHE   A O   1 
ATOM   60   C  CB  . PHE   A 1 7   ? -36.423 21.974  -47.116 1.00 65.38  ? 23  PHE   A CB  1 
ATOM   61   C  CG  . PHE   A 1 7   ? -35.340 23.000  -47.190 1.00 68.23  ? 23  PHE   A CG  1 
ATOM   62   C  CD1 . PHE   A 1 7   ? -34.062 22.701  -46.741 1.00 68.98  ? 23  PHE   A CD1 1 
ATOM   63   C  CD2 . PHE   A 1 7   ? -35.584 24.256  -47.733 1.00 72.22  ? 23  PHE   A CD2 1 
ATOM   64   C  CE1 . PHE   A 1 7   ? -33.038 23.645  -46.821 1.00 74.63  ? 23  PHE   A CE1 1 
ATOM   65   C  CE2 . PHE   A 1 7   ? -34.571 25.205  -47.808 1.00 75.74  ? 23  PHE   A CE2 1 
ATOM   66   C  CZ  . PHE   A 1 7   ? -33.294 24.897  -47.355 1.00 75.31  ? 23  PHE   A CZ  1 
ATOM   67   N  N   . SER   A 1 8   ? -38.313 19.554  -48.423 1.00 66.06  ? 24  SER   A N   1 
ATOM   68   C  CA  . SER   A 1 8   ? -39.190 18.420  -48.163 1.00 66.73  ? 24  SER   A CA  1 
ATOM   69   C  C   . SER   A 1 8   ? -38.591 17.105  -48.650 1.00 70.47  ? 24  SER   A C   1 
ATOM   70   O  O   . SER   A 1 8   ? -39.050 16.042  -48.223 1.00 70.96  ? 24  SER   A O   1 
ATOM   71   C  CB  . SER   A 1 8   ? -40.550 18.638  -48.820 1.00 69.22  ? 24  SER   A CB  1 
ATOM   72   O  OG  . SER   A 1 8   ? -40.458 18.452  -50.224 1.00 75.44  ? 24  SER   A OG  1 
ATOM   73   N  N   . LYS   A 1 9   ? -37.586 17.154  -49.535 1.00 69.82  ? 25  LYS   A N   1 
ATOM   74   C  CA  . LYS   A 1 9   ? -36.910 15.941  -49.981 1.00 72.39  ? 25  LYS   A CA  1 
ATOM   75   C  C   . LYS   A 1 9   ? -35.999 15.353  -48.911 1.00 73.06  ? 25  LYS   A C   1 
ATOM   76   O  O   . LYS   A 1 9   ? -35.640 14.173  -49.003 1.00 74.48  ? 25  LYS   A O   1 
ATOM   77   C  CB  . LYS   A 1 9   ? -36.090 16.208  -51.247 1.00 76.46  ? 25  LYS   A CB  1 
ATOM   78   C  CG  . LYS   A 1 9   ? -36.928 16.619  -52.448 1.00 85.22  ? 25  LYS   A CG  1 
ATOM   79   C  CD  . LYS   A 1 9   ? -36.220 16.316  -53.765 1.00 101.45 ? 25  LYS   A CD  1 
ATOM   80   C  CE  . LYS   A 1 9   ? -36.229 14.818  -54.075 1.00 107.84 ? 25  LYS   A CE  1 
ATOM   81   N  NZ  . LYS   A 1 9   ? -35.614 14.475  -55.395 1.00 108.61 ? 25  LYS   A NZ  1 
ATOM   82   N  N   . PHE   A 1 10  ? -35.596 16.145  -47.921 1.00 66.32  ? 26  PHE   A N   1 
ATOM   83   C  CA  . PHE   A 1 10  ? -34.840 15.624  -46.793 1.00 67.84  ? 26  PHE   A CA  1 
ATOM   84   C  C   . PHE   A 1 10  ? -35.812 15.075  -45.754 1.00 68.11  ? 26  PHE   A C   1 
ATOM   85   O  O   . PHE   A 1 10  ? -36.985 15.462  -45.700 1.00 64.14  ? 26  PHE   A O   1 
ATOM   86   C  CB  . PHE   A 1 10  ? -33.950 16.709  -46.168 1.00 65.87  ? 26  PHE   A CB  1 
ATOM   87   C  CG  . PHE   A 1 10  ? -32.896 17.244  -47.095 1.00 70.48  ? 26  PHE   A CG  1 
ATOM   88   C  CD1 . PHE   A 1 10  ? -33.224 18.149  -48.095 1.00 75.78  ? 26  PHE   A CD1 1 
ATOM   89   C  CD2 . PHE   A 1 10  ? -31.578 16.844  -46.971 1.00 68.79  ? 26  PHE   A CD2 1 
ATOM   90   C  CE1 . PHE   A 1 10  ? -32.252 18.640  -48.966 1.00 78.41  ? 26  PHE   A CE1 1 
ATOM   91   C  CE2 . PHE   A 1 10  ? -30.601 17.333  -47.834 1.00 77.99  ? 26  PHE   A CE2 1 
ATOM   92   C  CZ  . PHE   A 1 10  ? -30.938 18.232  -48.831 1.00 74.22  ? 26  PHE   A CZ  1 
ATOM   93   N  N   . SER   A 1 11  ? -35.324 14.145  -44.941 1.00 59.72  ? 27  SER   A N   1 
ATOM   94   C  CA  . SER   A 1 11  ? -36.226 13.837  -43.851 1.00 67.74  ? 27  SER   A CA  1 
ATOM   95   C  C   . SER   A 1 11  ? -35.686 14.431  -42.555 1.00 56.60  ? 27  SER   A C   1 
ATOM   96   O  O   . SER   A 1 11  ? -34.471 14.606  -42.418 1.00 58.55  ? 27  SER   A O   1 
ATOM   97   C  CB  . SER   A 1 11  ? -36.420 12.327  -43.689 1.00 67.44  ? 27  SER   A CB  1 
ATOM   98   O  OG  . SER   A 1 11  ? -35.202 11.726  -43.365 1.00 74.56  ? 27  SER   A OG  1 
ATOM   99   N  N   . PRO   A 1 12  ? -36.557 14.795  -41.609 1.00 59.76  ? 28  PRO   A N   1 
ATOM   100  C  CA  . PRO   A 1 12  ? -36.067 15.297  -40.322 1.00 52.72  ? 28  PRO   A CA  1 
ATOM   101  C  C   . PRO   A 1 12  ? -35.106 14.300  -39.689 1.00 53.99  ? 28  PRO   A C   1 
ATOM   102  O  O   . PRO   A 1 12  ? -35.176 13.096  -39.942 1.00 51.78  ? 28  PRO   A O   1 
ATOM   103  C  CB  . PRO   A 1 12  ? -37.348 15.454  -39.488 1.00 54.66  ? 28  PRO   A CB  1 
ATOM   104  C  CG  . PRO   A 1 12  ? -38.446 15.596  -40.476 1.00 52.37  ? 28  PRO   A CG  1 
ATOM   105  C  CD  . PRO   A 1 12  ? -38.031 14.797  -41.682 1.00 59.83  ? 28  PRO   A CD  1 
ATOM   106  N  N   . SER   A 1 13  ? -34.179 14.821  -38.883 1.00 47.73  ? 29  SER   A N   1 
ATOM   107  C  CA  . SER   A 1 13  ? -33.224 13.987  -38.158 1.00 50.74  ? 29  SER   A CA  1 
ATOM   108  C  C   . SER   A 1 13  ? -33.605 13.993  -36.685 1.00 53.98  ? 29  SER   A C   1 
ATOM   109  O  O   . SER   A 1 13  ? -33.344 14.980  -35.981 1.00 52.41  ? 29  SER   A O   1 
ATOM   110  C  CB  . SER   A 1 13  ? -31.790 14.492  -38.341 1.00 49.68  ? 29  SER   A CB  1 
ATOM   111  O  OG  . SER   A 1 13  ? -31.463 14.593  -39.708 1.00 63.59  ? 29  SER   A OG  1 
ATOM   112  N  N   . PRO   A 1 14  ? -34.228 12.941  -36.175 1.00 52.19  ? 30  PRO   A N   1 
ATOM   113  C  CA  . PRO   A 1 14  ? -34.648 12.955  -34.772 1.00 52.34  ? 30  PRO   A CA  1 
ATOM   114  C  C   . PRO   A 1 14  ? -33.451 12.811  -33.847 1.00 52.86  ? 30  PRO   A C   1 
ATOM   115  O  O   . PRO   A 1 14  ? -32.536 12.026  -34.105 1.00 53.06  ? 30  PRO   A O   1 
ATOM   116  C  CB  . PRO   A 1 14  ? -35.595 11.754  -34.672 1.00 54.20  ? 30  PRO   A CB  1 
ATOM   117  C  CG  . PRO   A 1 14  ? -35.186 10.849  -35.800 1.00 59.67  ? 30  PRO   A CG  1 
ATOM   118  C  CD  . PRO   A 1 14  ? -34.658 11.727  -36.893 1.00 57.91  ? 30  PRO   A CD  1 
ATOM   119  N  N   . LEU   A 1 15  ? -33.457 13.603  -32.777 1.00 50.89  ? 31  LEU   A N   1 
ATOM   120  C  CA  . LEU   A 1 15  ? -32.372 13.633  -31.810 1.00 50.02  ? 31  LEU   A CA  1 
ATOM   121  C  C   . LEU   A 1 15  ? -32.750 12.895  -30.536 1.00 53.98  ? 31  LEU   A C   1 
ATOM   122  O  O   . LEU   A 1 15  ? -33.912 12.879  -30.115 1.00 52.80  ? 31  LEU   A O   1 
ATOM   123  C  CB  . LEU   A 1 15  ? -31.994 15.073  -31.458 1.00 50.90  ? 31  LEU   A CB  1 
ATOM   124  C  CG  . LEU   A 1 15  ? -31.588 15.978  -32.621 1.00 55.26  ? 31  LEU   A CG  1 
ATOM   125  C  CD1 . LEU   A 1 15  ? -31.279 17.380  -32.119 1.00 54.38  ? 31  LEU   A CD1 1 
ATOM   126  C  CD2 . LEU   A 1 15  ? -30.400 15.378  -33.362 1.00 53.77  ? 31  LEU   A CD2 1 
ATOM   127  N  N   . SER   A 1 16  ? -31.743 12.319  -29.898 1.00 51.53  ? 32  SER   A N   1 
ATOM   128  C  CA  . SER   A 1 16  ? -31.941 11.713  -28.596 1.00 54.17  ? 32  SER   A CA  1 
ATOM   129  C  C   . SER   A 1 16  ? -31.810 12.761  -27.501 1.00 58.95  ? 32  SER   A C   1 
ATOM   130  O  O   . SER   A 1 16  ? -31.193 13.817  -27.679 1.00 55.81  ? 32  SER   A O   1 
ATOM   131  C  CB  . SER   A 1 16  ? -30.919 10.602  -28.346 1.00 53.18  ? 32  SER   A CB  1 
ATOM   132  O  OG  . SER   A 1 16  ? -29.635 11.164  -28.141 1.00 59.32  ? 32  SER   A OG  1 
ATOM   133  N  N   . MET   A 1 17  ? -32.392 12.441  -26.346 1.00 55.57  ? 33  MET   A N   1 
ATOM   134  C  CA  . MET   A 1 17  ? -32.207 13.279  -25.170 1.00 63.10  ? 33  MET   A CA  1 
ATOM   135  C  C   . MET   A 1 17  ? -30.727 13.440  -24.844 1.00 61.00  ? 33  MET   A C   1 
ATOM   136  O  O   . MET   A 1 17  ? -30.270 14.537  -24.506 1.00 62.61  ? 33  MET   A O   1 
ATOM   137  C  CB  . MET   A 1 17  ? -32.962 12.678  -23.990 1.00 59.57  ? 33  MET   A CB  1 
ATOM   138  C  CG  . MET   A 1 17  ? -33.094 13.602  -22.845 1.00 60.73  ? 33  MET   A CG  1 
ATOM   139  S  SD  . MET   A 1 17  ? -34.436 14.752  -23.073 1.00 67.82  ? 33  MET   A SD  1 
ATOM   140  C  CE  . MET   A 1 17  ? -35.875 13.690  -22.884 1.00 51.56  ? 33  MET   A CE  1 
ATOM   141  N  N   . LYS   A 1 18  ? -29.957 12.359  -24.967 1.00 66.43  ? 34  LYS   A N   1 
ATOM   142  C  CA  . LYS   A 1 18  ? -28.515 12.448  -24.777 1.00 62.89  ? 34  LYS   A CA  1 
ATOM   143  C  C   . LYS   A 1 18  ? -27.880 13.411  -25.776 1.00 67.01  ? 34  LYS   A C   1 
ATOM   144  O  O   . LYS   A 1 18  ? -26.968 14.172  -25.426 1.00 67.88  ? 34  LYS   A O   1 
ATOM   145  C  CB  . LYS   A 1 18  ? -27.895 11.057  -24.901 1.00 70.86  ? 34  LYS   A CB  1 
ATOM   146  C  CG  . LYS   A 1 18  ? -26.501 10.945  -24.305 1.00 76.63  ? 34  LYS   A CG  1 
ATOM   147  C  CD  . LYS   A 1 18  ? -25.932 9.552   -24.514 1.00 86.12  ? 34  LYS   A CD  1 
ATOM   148  C  CE  . LYS   A 1 18  ? -24.803 9.240   -23.532 1.00 91.63  ? 34  LYS   A CE  1 
ATOM   149  N  NZ  . LYS   A 1 18  ? -24.443 7.782   -23.543 1.00 87.12  ? 34  LYS   A NZ  1 
ATOM   150  N  N   . GLN   A 1 19  ? -28.350 13.394  -27.028 1.00 65.72  ? 35  GLN   A N   1 
ATOM   151  C  CA  . GLN   A 1 19  ? -27.824 14.307  -28.041 1.00 63.20  ? 35  GLN   A CA  1 
ATOM   152  C  C   . GLN   A 1 19  ? -28.190 15.755  -27.751 1.00 65.62  ? 35  GLN   A C   1 
ATOM   153  O  O   . GLN   A 1 19  ? -27.424 16.665  -28.090 1.00 65.95  ? 35  GLN   A O   1 
ATOM   154  C  CB  . GLN   A 1 19  ? -28.353 13.926  -29.418 1.00 57.69  ? 35  GLN   A CB  1 
ATOM   155  C  CG  . GLN   A 1 19  ? -27.390 13.124  -30.247 1.00 64.13  ? 35  GLN   A CG  1 
ATOM   156  C  CD  . GLN   A 1 19  ? -28.076 12.454  -31.406 1.00 60.28  ? 35  GLN   A CD  1 
ATOM   157  O  OE1 . GLN   A 1 19  ? -29.271 12.173  -31.355 1.00 57.26  ? 35  GLN   A OE1 1 
ATOM   158  N  NE2 . GLN   A 1 19  ? -27.327 12.203  -32.462 1.00 64.33  ? 35  GLN   A NE2 1 
ATOM   159  N  N   . PHE   A 1 20  ? -29.368 15.989  -27.170 1.00 61.20  ? 36  PHE   A N   1 
ATOM   160  C  CA  . PHE   A 1 20  ? -29.724 17.338  -26.756 1.00 63.34  ? 36  PHE   A CA  1 
ATOM   161  C  C   . PHE   A 1 20  ? -28.789 17.835  -25.666 1.00 66.09  ? 36  PHE   A C   1 
ATOM   162  O  O   . PHE   A 1 20  ? -28.385 19.004  -25.670 1.00 64.80  ? 36  PHE   A O   1 
ATOM   163  C  CB  . PHE   A 1 20  ? -31.164 17.378  -26.264 1.00 57.24  ? 36  PHE   A CB  1 
ATOM   164  C  CG  . PHE   A 1 20  ? -32.171 17.555  -27.350 1.00 54.38  ? 36  PHE   A CG  1 
ATOM   165  C  CD1 . PHE   A 1 20  ? -32.243 18.747  -28.052 1.00 50.94  ? 36  PHE   A CD1 1 
ATOM   166  C  CD2 . PHE   A 1 20  ? -33.067 16.546  -27.646 1.00 49.68  ? 36  PHE   A CD2 1 
ATOM   167  C  CE1 . PHE   A 1 20  ? -33.185 18.921  -29.052 1.00 53.23  ? 36  PHE   A CE1 1 
ATOM   168  C  CE2 . PHE   A 1 20  ? -34.011 16.718  -28.634 1.00 56.99  ? 36  PHE   A CE2 1 
ATOM   169  C  CZ  . PHE   A 1 20  ? -34.071 17.904  -29.339 1.00 51.11  ? 36  PHE   A CZ  1 
ATOM   170  N  N   . LEU   A 1 21  ? -28.441 16.965  -24.717 1.00 64.15  ? 37  LEU   A N   1 
ATOM   171  C  CA  . LEU   A 1 21  ? -27.556 17.384  -23.635 1.00 72.29  ? 37  LEU   A CA  1 
ATOM   172  C  C   . LEU   A 1 21  ? -26.188 17.796  -24.161 1.00 74.73  ? 37  LEU   A C   1 
ATOM   173  O  O   . LEU   A 1 21  ? -25.605 18.776  -23.686 1.00 81.38  ? 37  LEU   A O   1 
ATOM   174  C  CB  . LEU   A 1 21  ? -27.420 16.269  -22.609 1.00 67.73  ? 37  LEU   A CB  1 
ATOM   175  C  CG  . LEU   A 1 21  ? -28.690 16.012  -21.813 1.00 67.47  ? 37  LEU   A CG  1 
ATOM   176  C  CD1 . LEU   A 1 21  ? -28.505 14.747  -21.005 1.00 70.82  ? 37  LEU   A CD1 1 
ATOM   177  C  CD2 . LEU   A 1 21  ? -29.005 17.195  -20.899 1.00 63.30  ? 37  LEU   A CD2 1 
ATOM   178  N  N   . ASP   A 1 22  ? -25.666 17.078  -25.158 1.00 74.34  ? 38  ASP   A N   1 
ATOM   179  C  CA  . ASP   A 1 22  ? -24.354 17.426  -25.690 1.00 80.83  ? 38  ASP   A CA  1 
ATOM   180  C  C   . ASP   A 1 22  ? -24.392 18.679  -26.558 1.00 80.07  ? 38  ASP   A C   1 
ATOM   181  O  O   . ASP   A 1 22  ? -23.338 19.267  -26.822 1.00 87.93  ? 38  ASP   A O   1 
ATOM   182  C  CB  . ASP   A 1 22  ? -23.773 16.243  -26.472 1.00 81.94  ? 38  ASP   A CB  1 
ATOM   183  C  CG  . ASP   A 1 22  ? -23.729 14.960  -25.642 1.00 84.79  ? 38  ASP   A CG  1 
ATOM   184  O  OD1 . ASP   A 1 22  ? -23.644 15.047  -24.393 1.00 85.63  ? 38  ASP   A OD1 1 
ATOM   185  O  OD2 . ASP   A 1 22  ? -23.792 13.862  -26.239 1.00 87.15  ? 38  ASP   A OD2 1 
ATOM   186  N  N   . PHE   A 1 23  ? -25.575 19.110  -26.999 1.00 78.98  ? 39  PHE   A N   1 
ATOM   187  C  CA  . PHE   A 1 23  ? -25.684 20.352  -27.758 1.00 79.37  ? 39  PHE   A CA  1 
ATOM   188  C  C   . PHE   A 1 23  ? -25.673 21.576  -26.861 1.00 84.24  ? 39  PHE   A C   1 
ATOM   189  O  O   . PHE   A 1 23  ? -25.243 22.648  -27.294 1.00 89.50  ? 39  PHE   A O   1 
ATOM   190  C  CB  . PHE   A 1 23  ? -26.960 20.364  -28.592 1.00 79.44  ? 39  PHE   A CB  1 
ATOM   191  C  CG  . PHE   A 1 23  ? -26.723 20.163  -30.054 1.00 86.19  ? 39  PHE   A CG  1 
ATOM   192  C  CD1 . PHE   A 1 23  ? -26.057 21.127  -30.799 1.00 85.08  ? 39  PHE   A CD1 1 
ATOM   193  C  CD2 . PHE   A 1 23  ? -27.164 19.010  -30.688 1.00 86.60  ? 39  PHE   A CD2 1 
ATOM   194  C  CE1 . PHE   A 1 23  ? -25.830 20.944  -32.155 1.00 82.67  ? 39  PHE   A CE1 1 
ATOM   195  C  CE2 . PHE   A 1 23  ? -26.943 18.818  -32.049 1.00 87.49  ? 39  PHE   A CE2 1 
ATOM   196  C  CZ  . PHE   A 1 23  ? -26.272 19.788  -32.783 1.00 83.09  ? 39  PHE   A CZ  1 
ATOM   197  N  N   . GLY   A 1 24  ? -26.156 21.445  -25.629 1.00 85.90  ? 40  GLY   A N   1 
ATOM   198  C  CA  . GLY   A 1 24  ? -26.119 22.523  -24.665 1.00 89.05  ? 40  GLY   A CA  1 
ATOM   199  C  C   . GLY   A 1 24  ? -25.075 22.384  -23.590 1.00 92.46  ? 40  GLY   A C   1 
ATOM   200  O  O   . GLY   A 1 24  ? -25.169 23.084  -22.566 1.00 95.00  ? 40  GLY   A O   1 
ATOM   201  N  N   . SER   A 1 25  ? -24.080 21.515  -23.762 1.00 96.34  ? 41  SER   A N   1 
ATOM   202  C  CA  . SER   A 1 25  ? -23.049 21.348  -22.743 1.00 107.38 ? 41  SER   A CA  1 
ATOM   203  C  C   . SER   A 1 25  ? -22.186 22.599  -22.595 1.00 114.62 ? 41  SER   A C   1 
ATOM   204  O  O   . SER   A 1 25  ? -21.634 22.844  -21.515 1.00 117.33 ? 41  SER   A O   1 
ATOM   205  C  CB  . SER   A 1 25  ? -22.177 20.136  -23.072 1.00 104.85 ? 41  SER   A CB  1 
ATOM   206  O  OG  . SER   A 1 25  ? -21.692 20.202  -24.406 1.00 105.28 ? 41  SER   A OG  1 
ATOM   207  N  N   . SER   A 1 26  ? -22.054 23.396  -23.656 1.00 127.52 ? 42  SER   A N   1 
ATOM   208  C  CA  . SER   A 1 26  ? -21.232 24.599  -23.622 1.00 127.98 ? 42  SER   A CA  1 
ATOM   209  C  C   . SER   A 1 26  ? -21.845 25.657  -24.527 1.00 125.43 ? 42  SER   A C   1 
ATOM   210  O  O   . SER   A 1 26  ? -22.558 25.342  -25.485 1.00 120.54 ? 42  SER   A O   1 
ATOM   211  C  CB  . SER   A 1 26  ? -19.784 24.323  -24.059 1.00 123.12 ? 42  SER   A CB  1 
ATOM   212  O  OG  . SER   A 1 26  ? -19.118 23.477  -23.139 1.00 127.47 ? 42  SER   A OG  1 
ATOM   213  N  N   . ASN   A 1 27  ? -21.552 26.918  -24.211 1.00 120.79 ? 43  ASN   A N   1 
ATOM   214  C  CA  . ASN   A 1 27  ? -21.944 28.039  -25.054 1.00 115.10 ? 43  ASN   A CA  1 
ATOM   215  C  C   . ASN   A 1 27  ? -21.016 28.226  -26.248 1.00 113.18 ? 43  ASN   A C   1 
ATOM   216  O  O   . ASN   A 1 27  ? -21.271 29.105  -27.079 1.00 109.89 ? 43  ASN   A O   1 
ATOM   217  C  CB  . ASN   A 1 27  ? -22.006 29.323  -24.217 1.00 116.20 ? 43  ASN   A CB  1 
ATOM   218  C  CG  . ASN   A 1 27  ? -23.058 29.252  -23.120 1.00 117.80 ? 43  ASN   A CG  1 
ATOM   219  O  OD1 . ASN   A 1 27  ? -23.547 28.169  -22.785 1.00 113.27 ? 43  ASN   A OD1 1 
ATOM   220  N  ND2 . ASN   A 1 27  ? -23.414 30.406  -22.558 1.00 116.88 ? 43  ASN   A ND2 1 
ATOM   221  N  N   . ALA   A 1 28  ? -19.954 27.421  -26.355 1.00 113.03 ? 44  ALA   A N   1 
ATOM   222  C  CA  . ALA   A 1 28  ? -19.116 27.447  -27.550 1.00 114.81 ? 44  ALA   A CA  1 
ATOM   223  C  C   . ALA   A 1 28  ? -19.781 26.725  -28.717 1.00 111.14 ? 44  ALA   A C   1 
ATOM   224  O  O   . ALA   A 1 28  ? -19.485 27.022  -29.885 1.00 103.64 ? 44  ALA   A O   1 
ATOM   225  C  CB  . ALA   A 1 28  ? -17.752 26.829  -27.242 1.00 114.11 ? 44  ALA   A CB  1 
ATOM   226  N  N   . CYS   A 1 29  ? -20.679 25.778  -28.421 1.00 106.21 ? 45  CYS   A N   1 
ATOM   227  C  CA  . CYS   A 1 29  ? -21.440 25.005  -29.404 1.00 97.11  ? 45  CYS   A CA  1 
ATOM   228  C  C   . CYS   A 1 29  ? -22.464 25.844  -30.152 1.00 86.83  ? 45  CYS   A C   1 
ATOM   229  O  O   . CYS   A 1 29  ? -23.219 25.275  -30.943 1.00 83.16  ? 45  CYS   A O   1 
ATOM   230  C  CB  . CYS   A 1 29  ? -22.140 23.834  -28.708 1.00 100.70 ? 45  CYS   A CB  1 
ATOM   231  S  SG  . CYS   A 1 29  ? -21.096 22.885  -27.562 1.00 112.36 ? 45  CYS   A SG  1 
ATOM   232  N  N   . GLU   A 1 30  ? -22.516 27.164  -29.936 1.00 87.68  ? 46  GLU   A N   1 
ATOM   233  C  CA  . GLU   A 1 30  ? -23.535 27.974  -30.596 1.00 82.49  ? 46  GLU   A CA  1 
ATOM   234  C  C   . GLU   A 1 30  ? -23.385 27.933  -32.112 1.00 78.65  ? 46  GLU   A C   1 
ATOM   235  O  O   . GLU   A 1 30  ? -24.382 27.827  -32.836 1.00 75.29  ? 46  GLU   A O   1 
ATOM   236  C  CB  . GLU   A 1 30  ? -23.471 29.413  -30.084 1.00 81.21  ? 46  GLU   A CB  1 
ATOM   237  C  CG  . GLU   A 1 30  ? -24.502 30.315  -30.731 1.00 79.14  ? 46  GLU   A CG  1 
ATOM   238  C  CD  . GLU   A 1 30  ? -24.628 31.667  -30.061 1.00 81.08  ? 46  GLU   A CD  1 
ATOM   239  O  OE1 . GLU   A 1 30  ? -23.865 31.956  -29.113 1.00 85.48  ? 46  GLU   A OE1 1 
ATOM   240  O  OE2 . GLU   A 1 30  ? -25.504 32.445  -30.492 1.00 81.98  ? 46  GLU   A OE2 1 
ATOM   241  N  N   . LYS   A 1 31  ? -22.148 28.018  -32.611 1.00 77.13  ? 47  LYS   A N   1 
ATOM   242  C  CA  . LYS   A 1 31  ? -21.917 27.883  -34.046 1.00 79.21  ? 47  LYS   A CA  1 
ATOM   243  C  C   . LYS   A 1 31  ? -22.437 26.552  -34.560 1.00 74.69  ? 47  LYS   A C   1 
ATOM   244  O  O   . LYS   A 1 31  ? -23.043 26.483  -35.637 1.00 72.51  ? 47  LYS   A O   1 
ATOM   245  C  CB  . LYS   A 1 31  ? -20.426 28.014  -34.357 1.00 76.03  ? 47  LYS   A CB  1 
ATOM   246  C  CG  . LYS   A 1 31  ? -19.937 29.432  -34.405 1.00 86.65  ? 47  LYS   A CG  1 
ATOM   247  C  CD  . LYS   A 1 31  ? -18.453 29.489  -34.719 1.00 91.33  ? 47  LYS   A CD  1 
ATOM   248  C  CE  . LYS   A 1 31  ? -17.607 29.015  -33.545 1.00 92.00  ? 47  LYS   A CE  1 
ATOM   249  N  NZ  . LYS   A 1 31  ? -16.224 29.589  -33.613 1.00 89.26  ? 47  LYS   A NZ  1 
ATOM   250  N  N   . THR   A 1 32  ? -22.195 25.480  -33.807 1.00 74.73  ? 48  THR   A N   1 
ATOM   251  C  CA  . THR   A 1 32  ? -22.661 24.163  -34.215 1.00 73.85  ? 48  THR   A CA  1 
ATOM   252  C  C   . THR   A 1 32  ? -24.180 24.107  -34.233 1.00 70.24  ? 48  THR   A C   1 
ATOM   253  O  O   . THR   A 1 32  ? -24.782 23.549  -35.157 1.00 70.44  ? 48  THR   A O   1 
ATOM   254  C  CB  . THR   A 1 32  ? -22.093 23.104  -33.274 1.00 74.07  ? 48  THR   A CB  1 
ATOM   255  O  OG1 . THR   A 1 32  ? -20.669 23.241  -33.226 1.00 82.34  ? 48  THR   A OG1 1 
ATOM   256  C  CG2 . THR   A 1 32  ? -22.444 21.722  -33.766 1.00 76.37  ? 48  THR   A CG2 1 
ATOM   257  N  N   . SER   A 1 33  ? -24.819 24.690  -33.223 1.00 73.83  ? 49  SER   A N   1 
ATOM   258  C  CA  . SER   A 1 33  ? -26.274 24.704  -33.191 1.00 68.65  ? 49  SER   A CA  1 
ATOM   259  C  C   . SER   A 1 33  ? -26.835 25.532  -34.342 1.00 69.73  ? 49  SER   A C   1 
ATOM   260  O  O   . SER   A 1 33  ? -27.824 25.136  -34.970 1.00 66.99  ? 49  SER   A O   1 
ATOM   261  C  CB  . SER   A 1 33  ? -26.752 25.233  -31.840 1.00 68.60  ? 49  SER   A CB  1 
ATOM   262  O  OG  . SER   A 1 33  ? -28.167 25.211  -31.748 1.00 65.84  ? 49  SER   A OG  1 
ATOM   263  N  N   . PHE   A 1 34  ? -26.190 26.659  -34.664 1.00 72.62  ? 50  PHE   A N   1 
ATOM   264  C  CA  . PHE   A 1 34  ? -26.671 27.520  -35.743 1.00 68.35  ? 50  PHE   A CA  1 
ATOM   265  C  C   . PHE   A 1 34  ? -26.593 26.824  -37.097 1.00 68.74  ? 50  PHE   A C   1 
ATOM   266  O  O   . PHE   A 1 34  ? -27.555 26.851  -37.875 1.00 66.40  ? 50  PHE   A O   1 
ATOM   267  C  CB  . PHE   A 1 34  ? -25.872 28.822  -35.778 1.00 71.61  ? 50  PHE   A CB  1 
ATOM   268  C  CG  . PHE   A 1 34  ? -26.021 29.581  -37.067 1.00 72.27  ? 50  PHE   A CG  1 
ATOM   269  C  CD1 . PHE   A 1 34  ? -27.190 30.272  -37.347 1.00 71.76  ? 50  PHE   A CD1 1 
ATOM   270  C  CD2 . PHE   A 1 34  ? -24.999 29.595  -38.003 1.00 75.53  ? 50  PHE   A CD2 1 
ATOM   271  C  CE1 . PHE   A 1 34  ? -27.338 30.966  -38.533 1.00 74.18  ? 50  PHE   A CE1 1 
ATOM   272  C  CE2 . PHE   A 1 34  ? -25.140 30.289  -39.194 1.00 78.31  ? 50  PHE   A CE2 1 
ATOM   273  C  CZ  . PHE   A 1 34  ? -26.311 30.974  -39.460 1.00 75.50  ? 50  PHE   A CZ  1 
ATOM   274  N  N   . THR   A 1 35  ? -25.440 26.226  -37.417 1.00 70.01  ? 51  THR   A N   1 
ATOM   275  C  CA  . THR   A 1 35  ? -25.328 25.528  -38.692 1.00 69.03  ? 51  THR   A CA  1 
ATOM   276  C  C   . THR   A 1 35  ? -26.246 24.310  -38.739 1.00 65.67  ? 51  THR   A C   1 
ATOM   277  O  O   . THR   A 1 35  ? -26.780 23.980  -39.802 1.00 65.06  ? 51  THR   A O   1 
ATOM   278  C  CB  . THR   A 1 35  ? -23.869 25.127  -38.969 1.00 71.67  ? 51  THR   A CB  1 
ATOM   279  O  OG1 . THR   A 1 35  ? -23.456 24.112  -38.051 1.00 72.81  ? 51  THR   A OG1 1 
ATOM   280  C  CG2 . THR   A 1 35  ? -22.945 26.321  -38.830 1.00 72.67  ? 51  THR   A CG2 1 
ATOM   281  N  N   . PHE   A 1 36  ? -26.474 23.644  -37.603 1.00 71.84  ? 52  PHE   A N   1 
ATOM   282  C  CA  . PHE   A 1 36  ? -27.417 22.529  -37.599 1.00 60.53  ? 52  PHE   A CA  1 
ATOM   283  C  C   . PHE   A 1 36  ? -28.849 23.013  -37.833 1.00 63.66  ? 52  PHE   A C   1 
ATOM   284  O  O   . PHE   A 1 36  ? -29.546 22.519  -38.730 1.00 59.66  ? 52  PHE   A O   1 
ATOM   285  C  CB  . PHE   A 1 36  ? -27.320 21.747  -36.293 1.00 59.03  ? 52  PHE   A CB  1 
ATOM   286  C  CG  . PHE   A 1 36  ? -28.419 20.736  -36.126 1.00 60.49  ? 52  PHE   A CG  1 
ATOM   287  C  CD1 . PHE   A 1 36  ? -28.502 19.635  -36.966 1.00 60.82  ? 52  PHE   A CD1 1 
ATOM   288  C  CD2 . PHE   A 1 36  ? -29.386 20.898  -35.149 1.00 63.37  ? 52  PHE   A CD2 1 
ATOM   289  C  CE1 . PHE   A 1 36  ? -29.527 18.709  -36.831 1.00 54.23  ? 52  PHE   A CE1 1 
ATOM   290  C  CE2 . PHE   A 1 36  ? -30.406 19.972  -35.003 1.00 58.49  ? 52  PHE   A CE2 1 
ATOM   291  C  CZ  . PHE   A 1 36  ? -30.476 18.877  -35.849 1.00 56.03  ? 52  PHE   A CZ  1 
ATOM   292  N  N   . LEU   A 1 37  ? -29.294 24.005  -37.056 1.00 63.33  ? 53  LEU   A N   1 
ATOM   293  C  CA  . LEU   A 1 37  ? -30.693 24.421  -37.110 1.00 60.16  ? 53  LEU   A CA  1 
ATOM   294  C  C   . LEU   A 1 37  ? -31.040 25.147  -38.412 1.00 62.40  ? 53  LEU   A C   1 
ATOM   295  O  O   . LEU   A 1 37  ? -32.195 25.095  -38.848 1.00 60.46  ? 53  LEU   A O   1 
ATOM   296  C  CB  . LEU   A 1 37  ? -31.024 25.295  -35.890 1.00 58.03  ? 53  LEU   A CB  1 
ATOM   297  C  CG  . LEU   A 1 37  ? -31.028 24.609  -34.515 1.00 63.01  ? 53  LEU   A CG  1 
ATOM   298  C  CD1 . LEU   A 1 37  ? -31.320 25.593  -33.388 1.00 59.68  ? 53  LEU   A CD1 1 
ATOM   299  C  CD2 . LEU   A 1 37  ? -32.032 23.471  -34.478 1.00 57.60  ? 53  LEU   A CD2 1 
ATOM   300  N  N   . ARG   A 1 38  ? -30.078 25.817  -39.060 1.00 63.03  ? 54  ARG   A N   1 
ATOM   301  C  CA  . ARG   A 1 38  ? -30.436 26.546  -40.276 1.00 65.30  ? 54  ARG   A CA  1 
ATOM   302  C  C   . ARG   A 1 38  ? -30.744 25.613  -41.442 1.00 67.53  ? 54  ARG   A C   1 
ATOM   303  O  O   . ARG   A 1 38  ? -31.379 26.040  -42.409 1.00 68.24  ? 54  ARG   A O   1 
ATOM   304  C  CB  . ARG   A 1 38  ? -29.337 27.542  -40.660 1.00 69.22  ? 54  ARG   A CB  1 
ATOM   305  C  CG  . ARG   A 1 38  ? -28.015 26.942  -41.088 1.00 71.27  ? 54  ARG   A CG  1 
ATOM   306  C  CD  . ARG   A 1 38  ? -27.100 28.041  -41.629 1.00 74.85  ? 54  ARG   A CD  1 
ATOM   307  N  NE  . ARG   A 1 38  ? -25.771 27.547  -41.966 1.00 69.11  ? 54  ARG   A NE  1 
ATOM   308  C  CZ  . ARG   A 1 38  ? -24.776 28.318  -42.389 1.00 77.11  ? 54  ARG   A CZ  1 
ATOM   309  N  NH1 . ARG   A 1 38  ? -24.936 29.620  -42.565 1.00 80.44  ? 54  ARG   A NH1 1 
ATOM   310  N  NH2 . ARG   A 1 38  ? -23.589 27.769  -42.636 1.00 73.73  ? 54  ARG   A NH2 1 
ATOM   311  N  N   . GLN   A 1 39  ? -30.324 24.352  -41.358 1.00 64.68  ? 55  GLN   A N   1 
ATOM   312  C  CA  . GLN   A 1 39  ? -30.739 23.288  -42.267 1.00 60.26  ? 55  GLN   A CA  1 
ATOM   313  C  C   . GLN   A 1 39  ? -31.942 22.508  -41.719 1.00 63.10  ? 55  GLN   A C   1 
ATOM   314  O  O   . GLN   A 1 39  ? -32.931 22.282  -42.433 1.00 60.03  ? 55  GLN   A O   1 
ATOM   315  C  CB  . GLN   A 1 39  ? -29.548 22.347  -42.514 1.00 65.83  ? 55  GLN   A CB  1 
ATOM   316  C  CG  . GLN   A 1 39  ? -29.875 21.074  -43.253 1.00 65.82  ? 55  GLN   A CG  1 
ATOM   317  C  CD  . GLN   A 1 39  ? -30.172 21.336  -44.707 1.00 71.94  ? 55  GLN   A CD  1 
ATOM   318  O  OE1 . GLN   A 1 39  ? -29.866 22.410  -45.222 1.00 78.28  ? 55  GLN   A OE1 1 
ATOM   319  N  NE2 . GLN   A 1 39  ? -30.775 20.360  -45.379 1.00 71.16  ? 55  GLN   A NE2 1 
ATOM   320  N  N   . GLU   A 1 40  ? -31.899 22.142  -40.438 1.00 55.78  ? 56  GLU   A N   1 
ATOM   321  C  CA  . GLU   A 1 40  ? -32.900 21.241  -39.876 1.00 55.32  ? 56  GLU   A CA  1 
ATOM   322  C  C   . GLU   A 1 40  ? -34.277 21.894  -39.746 1.00 55.13  ? 56  GLU   A C   1 
ATOM   323  O  O   . GLU   A 1 40  ? -35.299 21.253  -40.022 1.00 53.78  ? 56  GLU   A O   1 
ATOM   324  C  CB  . GLU   A 1 40  ? -32.428 20.726  -38.514 1.00 55.87  ? 56  GLU   A CB  1 
ATOM   325  C  CG  . GLU   A 1 40  ? -33.372 19.691  -37.905 1.00 51.30  ? 56  GLU   A CG  1 
ATOM   326  C  CD  . GLU   A 1 40  ? -33.438 18.413  -38.728 1.00 54.71  ? 56  GLU   A CD  1 
ATOM   327  O  OE1 . GLU   A 1 40  ? -32.594 18.229  -39.647 1.00 56.16  ? 56  GLU   A OE1 1 
ATOM   328  O  OE2 . GLU   A 1 40  ? -34.339 17.589  -38.454 1.00 53.95  ? 56  GLU   A OE2 1 
ATOM   329  N  N   . LEU   A 1 41  ? -34.343 23.145  -39.296 1.00 54.69  ? 57  LEU   A N   1 
ATOM   330  C  CA  . LEU   A 1 41  ? -35.648 23.800  -39.198 1.00 53.73  ? 57  LEU   A CA  1 
ATOM   331  C  C   . LEU   A 1 41  ? -36.345 23.925  -40.548 1.00 56.06  ? 57  LEU   A C   1 
ATOM   332  O  O   . LEU   A 1 41  ? -37.549 23.627  -40.623 1.00 51.77  ? 57  LEU   A O   1 
ATOM   333  C  CB  . LEU   A 1 41  ? -35.499 25.160  -38.507 1.00 54.44  ? 57  LEU   A CB  1 
ATOM   334  C  CG  . LEU   A 1 41  ? -35.239 25.041  -37.011 1.00 56.46  ? 57  LEU   A CG  1 
ATOM   335  C  CD1 . LEU   A 1 41  ? -34.874 26.376  -36.413 1.00 59.19  ? 57  LEU   A CD1 1 
ATOM   336  C  CD2 . LEU   A 1 41  ? -36.465 24.451  -36.317 1.00 52.20  ? 57  LEU   A CD2 1 
ATOM   337  N  N   . PRO   A 1 42  ? -35.681 24.342  -41.637 1.00 56.94  ? 58  PRO   A N   1 
ATOM   338  C  CA  . PRO   A 1 42  ? -36.372 24.333  -42.940 1.00 56.34  ? 58  PRO   A CA  1 
ATOM   339  C  C   . PRO   A 1 42  ? -36.804 22.948  -43.373 1.00 57.77  ? 58  PRO   A C   1 
ATOM   340  O  O   . PRO   A 1 42  ? -37.859 22.801  -44.004 1.00 56.82  ? 58  PRO   A O   1 
ATOM   341  C  CB  . PRO   A 1 42  ? -35.324 24.920  -43.895 1.00 56.68  ? 58  PRO   A CB  1 
ATOM   342  C  CG  . PRO   A 1 42  ? -34.484 25.765  -43.037 1.00 60.92  ? 58  PRO   A CG  1 
ATOM   343  C  CD  . PRO   A 1 42  ? -34.378 25.023  -41.729 1.00 58.17  ? 58  PRO   A CD  1 
ATOM   344  N  N   . VAL   A 1 43  ? -36.007 21.927  -43.055 1.00 54.76  ? 59  VAL   A N   1 
ATOM   345  C  CA  . VAL   A 1 43  ? -36.397 20.552  -43.347 1.00 55.20  ? 59  VAL   A CA  1 
ATOM   346  C  C   . VAL   A 1 43  ? -37.690 20.200  -42.614 1.00 51.98  ? 59  VAL   A C   1 
ATOM   347  O  O   . VAL   A 1 43  ? -38.625 19.646  -43.203 1.00 52.46  ? 59  VAL   A O   1 
ATOM   348  C  CB  . VAL   A 1 43  ? -35.250 19.590  -42.988 1.00 53.81  ? 59  VAL   A CB  1 
ATOM   349  C  CG1 . VAL   A 1 43  ? -35.736 18.151  -42.940 1.00 53.30  ? 59  VAL   A CG1 1 
ATOM   350  C  CG2 . VAL   A 1 43  ? -34.129 19.727  -43.997 1.00 57.00  ? 59  VAL   A CG2 1 
ATOM   351  N  N   . ARG   A 1 44  ? -37.775 20.531  -41.323 1.00 51.85  ? 60  ARG   A N   1 
ATOM   352  C  CA  . ARG   A 1 44  ? -38.981 20.175  -40.570 1.00 53.56  ? 60  ARG   A CA  1 
ATOM   353  C  C   . ARG   A 1 44  ? -40.171 21.039  -40.977 1.00 49.74  ? 60  ARG   A C   1 
ATOM   354  O  O   . ARG   A 1 44  ? -41.301 20.544  -41.051 1.00 47.93  ? 60  ARG   A O   1 
ATOM   355  C  CB  . ARG   A 1 44  ? -38.727 20.264  -39.060 1.00 47.47  ? 60  ARG   A CB  1 
ATOM   356  C  CG  . ARG   A 1 44  ? -37.712 19.223  -38.570 1.00 49.56  ? 60  ARG   A CG  1 
ATOM   357  C  CD  . ARG   A 1 44  ? -37.564 19.195  -37.044 1.00 47.09  ? 60  ARG   A CD  1 
ATOM   358  N  NE  . ARG   A 1 44  ? -36.428 18.371  -36.628 1.00 47.14  ? 60  ARG   A NE  1 
ATOM   359  C  CZ  . ARG   A 1 44  ? -36.204 17.962  -35.385 1.00 46.87  ? 60  ARG   A CZ  1 
ATOM   360  N  NH1 . ARG   A 1 44  ? -37.055 18.230  -34.404 1.00 45.61  ? 60  ARG   A NH1 1 
ATOM   361  N  NH2 . ARG   A 1 44  ? -35.092 17.283  -35.117 1.00 46.55  ? 60  ARG   A NH2 1 
ATOM   362  N  N   . LEU   A 1 45  ? -39.946 22.328  -41.249 1.00 51.83  ? 61  LEU   A N   1 
ATOM   363  C  CA  . LEU   A 1 45  ? -41.041 23.168  -41.736 1.00 52.71  ? 61  LEU   A CA  1 
ATOM   364  C  C   . LEU   A 1 45  ? -41.579 22.651  -43.063 1.00 52.65  ? 61  LEU   A C   1 
ATOM   365  O  O   . LEU   A 1 45  ? -42.792 22.465  -43.224 1.00 56.39  ? 61  LEU   A O   1 
ATOM   366  C  CB  . LEU   A 1 45  ? -40.574 24.609  -41.888 1.00 56.68  ? 61  LEU   A CB  1 
ATOM   367  C  CG  . LEU   A 1 45  ? -40.280 25.304  -40.569 1.00 58.57  ? 61  LEU   A CG  1 
ATOM   368  C  CD1 . LEU   A 1 45  ? -39.547 26.591  -40.879 1.00 62.34  ? 61  LEU   A CD1 1 
ATOM   369  C  CD2 . LEU   A 1 45  ? -41.579 25.560  -39.813 1.00 52.79  ? 61  LEU   A CD2 1 
ATOM   370  N  N   . ALA   A 1 46  ? -40.683 22.383  -44.019 1.00 54.73  ? 62  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 46  ? -41.124 21.999  -45.355 1.00 57.96  ? 62  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 46  ? -41.838 20.655  -45.340 1.00 56.19  ? 62  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 46  ? -42.833 20.475  -46.047 1.00 56.47  ? 62  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 46  ? -39.933 21.957  -46.325 1.00 58.40  ? 62  ALA   A CB  1 
ATOM   375  N  N   . ASN   A 1 47  ? -41.344 19.694  -44.555 1.00 52.07  ? 63  ASN   A N   1 
ATOM   376  C  CA  . ASN   A 1 47  ? -42.003 18.393  -44.524 1.00 59.56  ? 63  ASN   A CA  1 
ATOM   377  C  C   . ASN   A 1 47  ? -43.453 18.515  -44.077 1.00 54.75  ? 63  ASN   A C   1 
ATOM   378  O  O   . ASN   A 1 47  ? -44.341 17.902  -44.674 1.00 53.60  ? 63  ASN   A O   1 
ATOM   379  C  CB  . ASN   A 1 47  ? -41.230 17.424  -43.626 1.00 57.55  ? 63  ASN   A CB  1 
ATOM   380  C  CG  . ASN   A 1 47  ? -40.164 16.658  -44.412 1.00 61.49  ? 63  ASN   A CG  1 
ATOM   381  O  OD1 . ASN   A 1 47  ? -40.390 15.531  -44.838 1.00 59.23  ? 63  ASN   A OD1 1 
ATOM   382  N  ND2 . ASN   A 1 47  ? -39.022 17.294  -44.642 1.00 59.74  ? 63  ASN   A ND2 1 
ATOM   383  N  N   . ILE   A 1 48  ? -43.727 19.328  -43.060 1.00 52.13  ? 64  ILE   A N   1 
ATOM   384  C  CA  . ILE   A 1 48  ? -45.118 19.424  -42.636 1.00 55.56  ? 64  ILE   A CA  1 
ATOM   385  C  C   . ILE   A 1 48  ? -45.923 20.316  -43.594 1.00 56.22  ? 64  ILE   A C   1 
ATOM   386  O  O   . ILE   A 1 48  ? -47.117 20.072  -43.820 1.00 49.34  ? 64  ILE   A O   1 
ATOM   387  C  CB  . ILE   A 1 48  ? -45.221 19.885  -41.164 1.00 51.87  ? 64  ILE   A CB  1 
ATOM   388  C  CG1 . ILE   A 1 48  ? -46.622 19.585  -40.634 1.00 47.25  ? 64  ILE   A CG1 1 
ATOM   389  C  CG2 . ILE   A 1 48  ? -44.869 21.350  -40.988 1.00 51.95  ? 64  ILE   A CG2 1 
ATOM   390  C  CD1 . ILE   A 1 48  ? -46.896 18.093  -40.537 1.00 52.02  ? 64  ILE   A CD1 1 
ATOM   391  N  N   . MET   A 1 49  ? -45.299 21.318  -44.220 1.00 57.37  ? 65  MET   A N   1 
ATOM   392  C  CA  . MET   A 1 49  ? -46.040 22.113  -45.202 1.00 57.57  ? 65  MET   A CA  1 
ATOM   393  C  C   . MET   A 1 49  ? -46.473 21.251  -46.382 1.00 59.18  ? 65  MET   A C   1 
ATOM   394  O  O   . MET   A 1 49  ? -47.592 21.396  -46.889 1.00 59.41  ? 65  MET   A O   1 
ATOM   395  C  CB  . MET   A 1 49  ? -45.210 23.315  -45.665 1.00 54.59  ? 65  MET   A CB  1 
ATOM   396  C  CG  . MET   A 1 49  ? -44.967 24.357  -44.556 1.00 62.03  ? 65  MET   A CG  1 
ATOM   397  S  SD  . MET   A 1 49  ? -43.443 25.339  -44.737 1.00 70.78  ? 65  MET   A SD  1 
ATOM   398  C  CE  . MET   A 1 49  ? -43.927 26.530  -45.984 1.00 66.05  ? 65  MET   A CE  1 
ATOM   399  N  N   . LYS   A 1 50  ? -45.620 20.313  -46.807 1.00 61.53  ? 66  LYS   A N   1 
ATOM   400  C  CA  . LYS   A 1 50  ? -45.999 19.414  -47.895 1.00 62.53  ? 66  LYS   A CA  1 
ATOM   401  C  C   . LYS   A 1 50  ? -47.161 18.521  -47.493 1.00 63.01  ? 66  LYS   A C   1 
ATOM   402  O  O   . LYS   A 1 50  ? -48.016 18.191  -48.320 1.00 61.67  ? 66  LYS   A O   1 
ATOM   403  C  CB  . LYS   A 1 50  ? -44.809 18.554  -48.327 1.00 64.04  ? 66  LYS   A CB  1 
ATOM   404  C  CG  . LYS   A 1 50  ? -44.014 19.135  -49.463 1.00 73.44  ? 66  LYS   A CG  1 
ATOM   405  C  CD  . LYS   A 1 50  ? -44.742 18.979  -50.781 1.00 80.66  ? 66  LYS   A CD  1 
ATOM   406  C  CE  . LYS   A 1 50  ? -44.145 17.847  -51.612 1.00 84.08  ? 66  LYS   A CE  1 
ATOM   407  N  NZ  . LYS   A 1 50  ? -44.811 17.750  -52.946 1.00 90.23  ? 66  LYS   A NZ  1 
ATOM   408  N  N   . GLU   A 1 51  ? -47.197 18.096  -46.231 1.00 60.70  ? 67  GLU   A N   1 
ATOM   409  C  CA  . GLU   A 1 51  ? -48.301 17.256  -45.786 1.00 63.97  ? 67  GLU   A CA  1 
ATOM   410  C  C   . GLU   A 1 51  ? -49.604 18.047  -45.729 1.00 62.49  ? 67  GLU   A C   1 
ATOM   411  O  O   . GLU   A 1 51  ? -50.675 17.516  -46.058 1.00 61.17  ? 67  GLU   A O   1 
ATOM   412  C  CB  . GLU   A 1 51  ? -47.975 16.630  -44.431 1.00 60.64  ? 67  GLU   A CB  1 
ATOM   413  C  CG  . GLU   A 1 51  ? -48.978 15.585  -44.022 1.00 65.79  ? 67  GLU   A CG  1 
ATOM   414  C  CD  . GLU   A 1 51  ? -48.355 14.459  -43.225 1.00 66.92  ? 67  GLU   A CD  1 
ATOM   415  O  OE1 . GLU   A 1 51  ? -47.105 14.377  -43.160 1.00 66.61  ? 67  GLU   A OE1 1 
ATOM   416  O  OE2 . GLU   A 1 51  ? -49.126 13.650  -42.673 1.00 62.34  ? 67  GLU   A OE2 1 
ATOM   417  N  N   . ILE   A 1 52  ? -49.523 19.323  -45.337 1.00 59.06  ? 68  ILE   A N   1 
ATOM   418  C  CA  . ILE   A 1 52  ? -50.697 20.189  -45.317 1.00 61.73  ? 68  ILE   A CA  1 
ATOM   419  C  C   . ILE   A 1 52  ? -51.317 20.303  -46.709 1.00 64.13  ? 68  ILE   A C   1 
ATOM   420  O  O   . ILE   A 1 52  ? -52.534 20.442  -46.836 1.00 66.97  ? 68  ILE   A O   1 
ATOM   421  C  CB  . ILE   A 1 52  ? -50.326 21.568  -44.726 1.00 58.41  ? 68  ILE   A CB  1 
ATOM   422  C  CG1 . ILE   A 1 52  ? -50.028 21.445  -43.232 1.00 57.14  ? 68  ILE   A CG1 1 
ATOM   423  C  CG2 . ILE   A 1 52  ? -51.447 22.573  -44.945 1.00 60.91  ? 68  ILE   A CG2 1 
ATOM   424  C  CD1 . ILE   A 1 52  ? -49.350 22.660  -42.610 1.00 50.06  ? 68  ILE   A CD1 1 
ATOM   425  N  N   . ASN   A 1 53  ? -50.509 20.216  -47.775 1.00 68.40  ? 69  ASN   A N   1 
ATOM   426  C  CA  . ASN   A 1 53  ? -51.071 20.284  -49.130 1.00 67.59  ? 69  ASN   A CA  1 
ATOM   427  C  C   . ASN   A 1 53  ? -51.765 18.996  -49.558 1.00 63.25  ? 69  ASN   A C   1 
ATOM   428  O  O   . ASN   A 1 53  ? -52.562 19.030  -50.492 1.00 72.72  ? 69  ASN   A O   1 
ATOM   429  C  CB  . ASN   A 1 53  ? -49.999 20.627  -50.161 1.00 68.46  ? 69  ASN   A CB  1 
ATOM   430  C  CG  . ASN   A 1 53  ? -49.298 21.942  -49.867 1.00 70.95  ? 69  ASN   A CG  1 
ATOM   431  O  OD1 . ASN   A 1 53  ? -49.812 22.777  -49.125 1.00 75.84  ? 69  ASN   A OD1 1 
ATOM   432  N  ND2 . ASN   A 1 53  ? -48.113 22.129  -50.450 1.00 80.00  ? 69  ASN   A ND2 1 
ATOM   433  N  N   . LEU   A 1 54  ? -51.492 17.868  -48.900 1.00 71.64  ? 70  LEU   A N   1 
ATOM   434  C  CA  . LEU   A 1 54  ? -52.235 16.636  -49.170 1.00 72.76  ? 70  LEU   A CA  1 
ATOM   435  C  C   . LEU   A 1 54  ? -53.684 16.711  -48.704 1.00 72.16  ? 70  LEU   A C   1 
ATOM   436  O  O   . LEU   A 1 54  ? -54.486 15.844  -49.074 1.00 73.42  ? 70  LEU   A O   1 
ATOM   437  C  CB  . LEU   A 1 54  ? -51.563 15.438  -48.485 1.00 76.86  ? 70  LEU   A CB  1 
ATOM   438  C  CG  . LEU   A 1 54  ? -50.211 14.959  -49.009 1.00 81.43  ? 70  LEU   A CG  1 
ATOM   439  C  CD1 . LEU   A 1 54  ? -49.705 13.795  -48.172 1.00 89.78  ? 70  LEU   A CD1 1 
ATOM   440  C  CD2 . LEU   A 1 54  ? -50.326 14.556  -50.460 1.00 84.24  ? 70  LEU   A CD2 1 
ATOM   441  N  N   . LEU   A 1 55  ? -54.021 17.695  -47.872 1.00 68.31  ? 71  LEU   A N   1 
ATOM   442  C  CA  . LEU   A 1 55  ? -55.397 17.880  -47.440 1.00 67.87  ? 71  LEU   A CA  1 
ATOM   443  C  C   . LEU   A 1 55  ? -56.288 18.230  -48.633 1.00 66.23  ? 71  LEU   A C   1 
ATOM   444  O  O   . LEU   A 1 55  ? -55.860 18.962  -49.535 1.00 63.11  ? 71  LEU   A O   1 
ATOM   445  C  CB  . LEU   A 1 55  ? -55.480 18.993  -46.394 1.00 61.50  ? 71  LEU   A CB  1 
ATOM   446  C  CG  . LEU   A 1 55  ? -54.755 18.726  -45.074 1.00 61.45  ? 71  LEU   A CG  1 
ATOM   447  C  CD1 . LEU   A 1 55  ? -54.884 19.927  -44.159 1.00 53.48  ? 71  LEU   A CD1 1 
ATOM   448  C  CD2 . LEU   A 1 55  ? -55.349 17.495  -44.426 1.00 58.52  ? 71  LEU   A CD2 1 
ATOM   449  N  N   . PRO   A 1 56  ? -57.534 17.758  -48.654 1.00 59.33  ? 72  PRO   A N   1 
ATOM   450  C  CA  . PRO   A 1 56  ? -58.438 18.108  -49.758 1.00 66.83  ? 72  PRO   A CA  1 
ATOM   451  C  C   . PRO   A 1 56  ? -58.668 19.610  -49.830 1.00 66.63  ? 72  PRO   A C   1 
ATOM   452  O  O   . PRO   A 1 56  ? -58.546 20.333  -48.835 1.00 60.67  ? 72  PRO   A O   1 
ATOM   453  C  CB  . PRO   A 1 56  ? -59.735 17.366  -49.414 1.00 67.20  ? 72  PRO   A CB  1 
ATOM   454  C  CG  . PRO   A 1 56  ? -59.370 16.374  -48.339 1.00 68.13  ? 72  PRO   A CG  1 
ATOM   455  C  CD  . PRO   A 1 56  ? -58.188 16.926  -47.628 1.00 63.70  ? 72  PRO   A CD  1 
ATOM   456  N  N   . ASP   A 1 57  ? -59.012 20.075  -51.033 1.00 62.57  ? 73  ASP   A N   1 
ATOM   457  C  CA  . ASP   A 1 57  ? -59.170 21.506  -51.245 1.00 63.56  ? 73  ASP   A CA  1 
ATOM   458  C  C   . ASP   A 1 57  ? -60.222 22.100  -50.323 1.00 62.87  ? 73  ASP   A C   1 
ATOM   459  O  O   . ASP   A 1 57  ? -60.093 23.254  -49.898 1.00 61.07  ? 73  ASP   A O   1 
ATOM   460  C  CB  . ASP   A 1 57  ? -59.536 21.794  -52.696 1.00 68.45  ? 73  ASP   A CB  1 
ATOM   461  C  CG  . ASP   A 1 57  ? -59.649 23.283  -52.972 1.00 80.60  ? 73  ASP   A CG  1 
ATOM   462  O  OD1 . ASP   A 1 57  ? -58.656 24.017  -52.730 1.00 83.71  ? 73  ASP   A OD1 1 
ATOM   463  O  OD2 . ASP   A 1 57  ? -60.732 23.728  -53.412 1.00 87.91  ? 73  ASP   A OD2 1 
ATOM   464  N  N   . ARG   A 1 58  ? -61.264 21.336  -49.994 1.00 60.13  ? 74  ARG   A N   1 
ATOM   465  C  CA  . ARG   A 1 58  ? -62.298 21.878  -49.120 1.00 63.25  ? 74  ARG   A CA  1 
ATOM   466  C  C   . ARG   A 1 58  ? -61.797 22.093  -47.693 1.00 57.49  ? 74  ARG   A C   1 
ATOM   467  O  O   . ARG   A 1 58  ? -62.441 22.820  -46.929 1.00 60.64  ? 74  ARG   A O   1 
ATOM   468  C  CB  . ARG   A 1 58  ? -63.527 20.971  -49.121 1.00 59.48  ? 74  ARG   A CB  1 
ATOM   469  C  CG  . ARG   A 1 58  ? -63.309 19.657  -48.392 1.00 58.61  ? 74  ARG   A CG  1 
ATOM   470  C  CD  . ARG   A 1 58  ? -64.541 18.766  -48.478 1.00 62.11  ? 74  ARG   A CD  1 
ATOM   471  N  NE  . ARG   A 1 58  ? -64.297 17.474  -47.849 1.00 61.11  ? 74  ARG   A NE  1 
ATOM   472  C  CZ  . ARG   A 1 58  ? -63.668 16.463  -48.435 1.00 68.25  ? 74  ARG   A CZ  1 
ATOM   473  N  NH1 . ARG   A 1 58  ? -63.216 16.556  -49.677 1.00 64.97  ? 74  ARG   A NH1 1 
ATOM   474  N  NH2 . ARG   A 1 58  ? -63.488 15.332  -47.758 1.00 67.64  ? 74  ARG   A NH2 1 
ATOM   475  N  N   . VAL   A 1 59  ? -60.677 21.480  -47.317 1.00 58.06  ? 75  VAL   A N   1 
ATOM   476  C  CA  . VAL   A 1 59  ? -60.011 21.799  -46.050 1.00 55.64  ? 75  VAL   A CA  1 
ATOM   477  C  C   . VAL   A 1 59  ? -58.952 22.869  -46.264 1.00 59.61  ? 75  VAL   A C   1 
ATOM   478  O  O   . VAL   A 1 59  ? -58.857 23.832  -45.496 1.00 53.49  ? 75  VAL   A O   1 
ATOM   479  C  CB  . VAL   A 1 59  ? -59.397 20.523  -45.434 1.00 53.61  ? 75  VAL   A CB  1 
ATOM   480  C  CG1 . VAL   A 1 59  ? -58.573 20.842  -44.181 1.00 54.58  ? 75  VAL   A CG1 1 
ATOM   481  C  CG2 . VAL   A 1 59  ? -60.469 19.534  -45.123 1.00 54.09  ? 75  VAL   A CG2 1 
ATOM   482  N  N   . LEU   A 1 60  ? -58.182 22.706  -47.339 1.00 59.60  ? 76  LEU   A N   1 
ATOM   483  C  CA  . LEU   A 1 60  ? -57.078 23.604  -47.644 1.00 62.47  ? 76  LEU   A CA  1 
ATOM   484  C  C   . LEU   A 1 60  ? -57.544 25.048  -47.825 1.00 60.05  ? 76  LEU   A C   1 
ATOM   485  O  O   . LEU   A 1 60  ? -56.827 25.980  -47.446 1.00 68.22  ? 76  LEU   A O   1 
ATOM   486  C  CB  . LEU   A 1 60  ? -56.373 23.081  -48.900 1.00 67.50  ? 76  LEU   A CB  1 
ATOM   487  C  CG  . LEU   A 1 60  ? -54.929 23.404  -49.246 1.00 78.73  ? 76  LEU   A CG  1 
ATOM   488  C  CD1 . LEU   A 1 60  ? -54.473 22.375  -50.270 1.00 72.20  ? 76  LEU   A CD1 1 
ATOM   489  C  CD2 . LEU   A 1 60  ? -54.813 24.812  -49.823 1.00 83.78  ? 76  LEU   A CD2 1 
ATOM   490  N  N   . SER   A 1 61  ? -58.736 25.264  -48.373 1.00 55.51  ? 77  SER   A N   1 
ATOM   491  C  CA  . SER   A 1 61  ? -59.198 26.620  -48.662 1.00 68.64  ? 77  SER   A CA  1 
ATOM   492  C  C   . SER   A 1 61  ? -59.986 27.255  -47.519 1.00 64.45  ? 77  SER   A C   1 
ATOM   493  O  O   . SER   A 1 61  ? -60.617 28.291  -47.726 1.00 73.31  ? 77  SER   A O   1 
ATOM   494  C  CB  . SER   A 1 61  ? -60.048 26.633  -49.933 1.00 68.02  ? 77  SER   A CB  1 
ATOM   495  O  OG  . SER   A 1 61  ? -61.274 25.968  -49.701 1.00 72.58  ? 77  SER   A OG  1 
ATOM   496  N  N   . THR   A 1 62  ? -59.963 26.676  -46.329 1.00 65.35  ? 78  THR   A N   1 
ATOM   497  C  CA  . THR   A 1 62  ? -60.620 27.354  -45.222 1.00 64.16  ? 78  THR   A CA  1 
ATOM   498  C  C   . THR   A 1 62  ? -59.685 28.391  -44.594 1.00 62.95  ? 78  THR   A C   1 
ATOM   499  O  O   . THR   A 1 62  ? -58.462 28.268  -44.690 1.00 61.13  ? 78  THR   A O   1 
ATOM   500  C  CB  . THR   A 1 62  ? -61.058 26.349  -44.170 1.00 61.92  ? 78  THR   A CB  1 
ATOM   501  O  OG1 . THR   A 1 62  ? -59.917 25.631  -43.707 1.00 58.71  ? 78  THR   A OG1 1 
ATOM   502  C  CG2 . THR   A 1 62  ? -62.078 25.383  -44.757 1.00 67.52  ? 78  THR   A CG2 1 
ATOM   503  N  N   . PRO   A 1 63  ? -60.235 29.434  -43.957 1.00 59.15  ? 79  PRO   A N   1 
ATOM   504  C  CA  . PRO   A 1 63  ? -59.364 30.528  -43.492 1.00 54.51  ? 79  PRO   A CA  1 
ATOM   505  C  C   . PRO   A 1 63  ? -58.331 30.096  -42.464 1.00 60.96  ? 79  PRO   A C   1 
ATOM   506  O  O   . PRO   A 1 63  ? -57.215 30.630  -42.459 1.00 57.11  ? 79  PRO   A O   1 
ATOM   507  C  CB  . PRO   A 1 63  ? -60.364 31.538  -42.908 1.00 55.57  ? 79  PRO   A CB  1 
ATOM   508  C  CG  . PRO   A 1 63  ? -61.658 31.250  -43.652 1.00 56.49  ? 79  PRO   A CG  1 
ATOM   509  C  CD  . PRO   A 1 63  ? -61.660 29.748  -43.765 1.00 57.29  ? 79  PRO   A CD  1 
ATOM   510  N  N   . SER   A 1 64  ? -58.668 29.155  -41.578 1.00 53.25  ? 80  SER   A N   1 
ATOM   511  C  CA  . SER   A 1 64  ? -57.732 28.815  -40.517 1.00 54.69  ? 80  SER   A CA  1 
ATOM   512  C  C   . SER   A 1 64  ? -56.510 28.092  -41.075 1.00 55.21  ? 80  SER   A C   1 
ATOM   513  O  O   . SER   A 1 64  ? -55.386 28.355  -40.643 1.00 54.92  ? 80  SER   A O   1 
ATOM   514  C  CB  . SER   A 1 64  ? -58.438 27.983  -39.435 1.00 50.41  ? 80  SER   A CB  1 
ATOM   515  O  OG  . SER   A 1 64  ? -58.978 26.794  -39.989 1.00 56.72  ? 80  SER   A OG  1 
ATOM   516  N  N   . VAL   A 1 65  ? -56.697 27.208  -42.061 1.00 53.94  ? 81  VAL   A N   1 
ATOM   517  C  CA  . VAL   A 1 65  ? -55.547 26.510  -42.634 1.00 56.53  ? 81  VAL   A CA  1 
ATOM   518  C  C   . VAL   A 1 65  ? -54.695 27.472  -43.454 1.00 59.53  ? 81  VAL   A C   1 
ATOM   519  O  O   . VAL   A 1 65  ? -53.462 27.435  -43.384 1.00 53.11  ? 81  VAL   A O   1 
ATOM   520  C  CB  . VAL   A 1 65  ? -56.001 25.290  -43.462 1.00 60.77  ? 81  VAL   A CB  1 
ATOM   521  C  CG1 . VAL   A 1 65  ? -54.818 24.670  -44.203 1.00 57.80  ? 81  VAL   A CG1 1 
ATOM   522  C  CG2 . VAL   A 1 65  ? -56.672 24.241  -42.546 1.00 53.59  ? 81  VAL   A CG2 1 
ATOM   523  N  N   . GLN   A 1 66  ? -55.337 28.367  -44.218 1.00 57.81  ? 82  GLN   A N   1 
ATOM   524  C  CA  . GLN   A 1 66  ? -54.597 29.387  -44.952 1.00 59.38  ? 82  GLN   A CA  1 
ATOM   525  C  C   . GLN   A 1 66  ? -53.784 30.261  -44.003 1.00 58.40  ? 82  GLN   A C   1 
ATOM   526  O  O   . GLN   A 1 66  ? -52.631 30.591  -44.291 1.00 61.57  ? 82  GLN   A O   1 
ATOM   527  C  CB  . GLN   A 1 66  ? -55.558 30.242  -45.783 1.00 57.20  ? 82  GLN   A CB  1 
ATOM   528  C  CG  . GLN   A 1 66  ? -56.235 29.489  -46.914 1.00 63.04  ? 82  GLN   A CG  1 
ATOM   529  C  CD  . GLN   A 1 66  ? -57.265 30.332  -47.678 1.00 79.17  ? 82  GLN   A CD  1 
ATOM   530  O  OE1 . GLN   A 1 66  ? -57.715 31.392  -47.213 1.00 73.83  ? 82  GLN   A OE1 1 
ATOM   531  N  NE2 . GLN   A 1 66  ? -57.636 29.860  -48.867 1.00 86.03  ? 82  GLN   A NE2 1 
ATOM   532  N  N   . LEU   A 1 67  ? -54.361 30.629  -42.857 1.00 55.33  ? 83  LEU   A N   1 
ATOM   533  C  CA  . LEU   A 1 67  ? -53.635 31.450  -41.892 1.00 60.35  ? 83  LEU   A CA  1 
ATOM   534  C  C   . LEU   A 1 67  ? -52.395 30.722  -41.377 1.00 59.16  ? 83  LEU   A C   1 
ATOM   535  O  O   . LEU   A 1 67  ? -51.287 31.274  -41.384 1.00 58.13  ? 83  LEU   A O   1 
ATOM   536  C  CB  . LEU   A 1 67  ? -54.550 31.832  -40.730 1.00 57.05  ? 83  LEU   A CB  1 
ATOM   537  C  CG  . LEU   A 1 67  ? -53.936 32.718  -39.647 1.00 62.56  ? 83  LEU   A CG  1 
ATOM   538  C  CD1 . LEU   A 1 67  ? -53.540 34.092  -40.226 1.00 60.18  ? 83  LEU   A CD1 1 
ATOM   539  C  CD2 . LEU   A 1 67  ? -54.908 32.879  -38.475 1.00 59.43  ? 83  LEU   A CD2 1 
ATOM   540  N  N   . VAL   A 1 68  ? -52.561 29.469  -40.952 1.00 58.38  ? 84  VAL   A N   1 
ATOM   541  C  CA  . VAL   A 1 68  ? -51.427 28.702  -40.443 1.00 55.80  ? 84  VAL   A CA  1 
ATOM   542  C  C   . VAL   A 1 68  ? -50.392 28.478  -41.537 1.00 57.13  ? 84  VAL   A C   1 
ATOM   543  O  O   . VAL   A 1 68  ? -49.185 28.628  -41.308 1.00 56.10  ? 84  VAL   A O   1 
ATOM   544  C  CB  . VAL   A 1 68  ? -51.913 27.372  -39.845 1.00 54.70  ? 84  VAL   A CB  1 
ATOM   545  C  CG1 . VAL   A 1 68  ? -50.734 26.440  -39.601 1.00 47.29  ? 84  VAL   A CG1 1 
ATOM   546  C  CG2 . VAL   A 1 68  ? -52.677 27.630  -38.560 1.00 48.46  ? 84  VAL   A CG2 1 
ATOM   547  N  N   . GLN   A 1 69  ? -50.848 28.114  -42.741 1.00 54.06  ? 85  GLN   A N   1 
ATOM   548  C  CA  . GLN   A 1 69  ? -49.943 27.976  -43.877 1.00 57.99  ? 85  GLN   A CA  1 
ATOM   549  C  C   . GLN   A 1 69  ? -49.144 29.249  -44.108 1.00 61.36  ? 85  GLN   A C   1 
ATOM   550  O  O   . GLN   A 1 69  ? -47.957 29.185  -44.446 1.00 63.81  ? 85  GLN   A O   1 
ATOM   551  C  CB  . GLN   A 1 69  ? -50.728 27.620  -45.140 1.00 66.23  ? 85  GLN   A CB  1 
ATOM   552  C  CG  . GLN   A 1 69  ? -50.550 26.190  -45.631 1.00 71.28  ? 85  GLN   A CG  1 
ATOM   553  C  CD  . GLN   A 1 69  ? -51.490 25.844  -46.788 1.00 79.05  ? 85  GLN   A CD  1 
ATOM   554  O  OE1 . GLN   A 1 69  ? -52.427 26.588  -47.088 1.00 80.13  ? 85  GLN   A OE1 1 
ATOM   555  N  NE2 . GLN   A 1 69  ? -51.239 24.710  -47.441 1.00 79.32  ? 85  GLN   A NE2 1 
ATOM   556  N  N   . SER   A 1 70  ? -49.775 30.421  -43.938 1.00 57.40  ? 86  SER   A N   1 
ATOM   557  C  CA  . SER   A 1 70  ? -49.046 31.667  -44.177 1.00 64.97  ? 86  SER   A CA  1 
ATOM   558  C  C   . SER   A 1 70  ? -47.956 31.879  -43.136 1.00 63.51  ? 86  SER   A C   1 
ATOM   559  O  O   . SER   A 1 70  ? -46.918 32.476  -43.439 1.00 69.46  ? 86  SER   A O   1 
ATOM   560  C  CB  . SER   A 1 70  ? -50.000 32.869  -44.206 1.00 66.99  ? 86  SER   A CB  1 
ATOM   561  O  OG  . SER   A 1 70  ? -50.558 33.128  -42.928 1.00 62.11  ? 86  SER   A OG  1 
ATOM   562  N  N   . TRP   A 1 71  ? -48.162 31.385  -41.919 1.00 61.85  ? 87  TRP   A N   1 
ATOM   563  C  CA  . TRP   A 1 71  ? -47.126 31.481  -40.892 1.00 66.94  ? 87  TRP   A CA  1 
ATOM   564  C  C   . TRP   A 1 71  ? -45.928 30.593  -41.221 1.00 63.81  ? 87  TRP   A C   1 
ATOM   565  O  O   . TRP   A 1 71  ? -44.776 31.035  -41.142 1.00 68.26  ? 87  TRP   A O   1 
ATOM   566  C  CB  . TRP   A 1 71  ? -47.709 31.116  -39.530 1.00 60.17  ? 87  TRP   A CB  1 
ATOM   567  C  CG  . TRP   A 1 71  ? -48.706 32.113  -39.037 1.00 64.35  ? 87  TRP   A CG  1 
ATOM   568  C  CD1 . TRP   A 1 71  ? -48.850 33.407  -39.459 1.00 64.93  ? 87  TRP   A CD1 1 
ATOM   569  C  CD2 . TRP   A 1 71  ? -49.700 31.909  -38.026 1.00 61.86  ? 87  TRP   A CD2 1 
ATOM   570  N  NE1 . TRP   A 1 71  ? -49.870 34.016  -38.770 1.00 65.89  ? 87  TRP   A NE1 1 
ATOM   571  C  CE2 . TRP   A 1 71  ? -50.407 33.119  -37.884 1.00 64.84  ? 87  TRP   A CE2 1 
ATOM   572  C  CE3 . TRP   A 1 71  ? -50.061 30.820  -37.229 1.00 65.48  ? 87  TRP   A CE3 1 
ATOM   573  C  CZ2 . TRP   A 1 71  ? -51.453 33.269  -36.975 1.00 67.85  ? 87  TRP   A CZ2 1 
ATOM   574  C  CZ3 . TRP   A 1 71  ? -51.095 30.971  -36.327 1.00 64.19  ? 87  TRP   A CZ3 1 
ATOM   575  C  CH2 . TRP   A 1 71  ? -51.782 32.182  -36.208 1.00 65.29  ? 87  TRP   A CH2 1 
ATOM   576  N  N   . TYR   A 1 72  ? -46.179 29.332  -41.583 1.00 64.08  ? 88  TYR   A N   1 
ATOM   577  C  CA  . TYR   A 1 72  ? -45.082 28.430  -41.919 1.00 59.21  ? 88  TYR   A CA  1 
ATOM   578  C  C   . TYR   A 1 72  ? -44.285 28.941  -43.109 1.00 71.30  ? 88  TYR   A C   1 
ATOM   579  O  O   . TYR   A 1 72  ? -43.052 28.843  -43.124 1.00 65.51  ? 88  TYR   A O   1 
ATOM   580  C  CB  . TYR   A 1 72  ? -45.616 27.030  -42.196 1.00 58.48  ? 88  TYR   A CB  1 
ATOM   581  C  CG  . TYR   A 1 72  ? -45.834 26.267  -40.919 1.00 56.87  ? 88  TYR   A CG  1 
ATOM   582  C  CD1 . TYR   A 1 72  ? -46.823 26.647  -40.033 1.00 56.01  ? 88  TYR   A CD1 1 
ATOM   583  C  CD2 . TYR   A 1 72  ? -45.034 25.189  -40.584 1.00 58.32  ? 88  TYR   A CD2 1 
ATOM   584  C  CE1 . TYR   A 1 72  ? -47.022 25.972  -38.853 1.00 59.67  ? 88  TYR   A CE1 1 
ATOM   585  C  CE2 . TYR   A 1 72  ? -45.227 24.495  -39.395 1.00 60.37  ? 88  TYR   A CE2 1 
ATOM   586  C  CZ  . TYR   A 1 72  ? -46.224 24.894  -38.531 1.00 56.95  ? 88  TYR   A CZ  1 
ATOM   587  O  OH  . TYR   A 1 72  ? -46.428 24.232  -37.340 1.00 55.73  ? 88  TYR   A OH  1 
ATOM   588  N  N   . VAL   A 1 73  ? -44.971 29.480  -44.122 1.00 65.71  ? 89  VAL   A N   1 
ATOM   589  C  CA  . VAL   A 1 73  ? -44.267 30.013  -45.279 1.00 69.86  ? 89  VAL   A CA  1 
ATOM   590  C  C   . VAL   A 1 73  ? -43.334 31.135  -44.847 1.00 73.60  ? 89  VAL   A C   1 
ATOM   591  O  O   . VAL   A 1 73  ? -42.152 31.152  -45.208 1.00 70.62  ? 89  VAL   A O   1 
ATOM   592  C  CB  . VAL   A 1 73  ? -45.263 30.476  -46.357 1.00 72.57  ? 89  VAL   A CB  1 
ATOM   593  C  CG1 . VAL   A 1 73  ? -44.566 31.363  -47.392 1.00 71.69  ? 89  VAL   A CG1 1 
ATOM   594  C  CG2 . VAL   A 1 73  ? -45.901 29.271  -47.037 1.00 67.58  ? 89  VAL   A CG2 1 
ATOM   595  N  N   . GLN   A 1 74  ? -43.840 32.063  -44.026 1.00 73.30  ? 90  GLN   A N   1 
ATOM   596  C  CA  . GLN   A 1 74  ? -43.014 33.183  -43.583 1.00 75.32  ? 90  GLN   A CA  1 
ATOM   597  C  C   . GLN   A 1 74  ? -41.866 32.701  -42.707 1.00 69.72  ? 90  GLN   A C   1 
ATOM   598  O  O   . GLN   A 1 74  ? -40.717 33.121  -42.884 1.00 70.97  ? 90  GLN   A O   1 
ATOM   599  C  CB  . GLN   A 1 74  ? -43.867 34.210  -42.836 1.00 77.22  ? 90  GLN   A CB  1 
ATOM   600  C  CG  . GLN   A 1 74  ? -43.136 35.509  -42.503 1.00 76.07  ? 90  GLN   A CG  1 
ATOM   601  C  CD  . GLN   A 1 74  ? -42.716 36.302  -43.736 1.00 84.18  ? 90  GLN   A CD  1 
ATOM   602  O  OE1 . GLN   A 1 74  ? -43.550 36.887  -44.426 1.00 86.64  ? 90  GLN   A OE1 1 
ATOM   603  N  NE2 . GLN   A 1 74  ? -41.414 36.327  -44.008 1.00 81.61  ? 90  GLN   A NE2 1 
ATOM   604  N  N   . SER   A 1 75  ? -42.161 31.814  -41.757 1.00 73.08  ? 91  SER   A N   1 
ATOM   605  C  CA  . SER   A 1 75  ? -41.115 31.277  -40.892 1.00 67.98  ? 91  SER   A CA  1 
ATOM   606  C  C   . SER   A 1 75  ? -40.015 30.607  -41.705 1.00 67.79  ? 91  SER   A C   1 
ATOM   607  O  O   . SER   A 1 75  ? -38.828 30.749  -41.394 1.00 68.92  ? 91  SER   A O   1 
ATOM   608  C  CB  . SER   A 1 75  ? -41.728 30.295  -39.901 1.00 65.02  ? 91  SER   A CB  1 
ATOM   609  O  OG  . SER   A 1 75  ? -42.566 30.979  -38.987 1.00 68.72  ? 91  SER   A OG  1 
ATOM   610  N  N   . LEU   A 1 76  ? -40.393 29.876  -42.754 1.00 67.11  ? 92  LEU   A N   1 
ATOM   611  C  CA  . LEU   A 1 76  ? -39.401 29.222  -43.593 1.00 68.14  ? 92  LEU   A CA  1 
ATOM   612  C  C   . LEU   A 1 76  ? -38.548 30.252  -44.319 1.00 74.74  ? 92  LEU   A C   1 
ATOM   613  O  O   . LEU   A 1 76  ? -37.321 30.113  -44.391 1.00 75.58  ? 92  LEU   A O   1 
ATOM   614  C  CB  . LEU   A 1 76  ? -40.100 28.292  -44.583 1.00 63.74  ? 92  LEU   A CB  1 
ATOM   615  C  CG  . LEU   A 1 76  ? -39.226 27.584  -45.610 1.00 72.82  ? 92  LEU   A CG  1 
ATOM   616  C  CD1 . LEU   A 1 76  ? -38.146 26.796  -44.908 1.00 70.39  ? 92  LEU   A CD1 1 
ATOM   617  C  CD2 . LEU   A 1 76  ? -40.071 26.672  -46.474 1.00 74.38  ? 92  LEU   A CD2 1 
ATOM   618  N  N   . LEU   A 1 77  ? -39.180 31.307  -44.841 1.00 67.64  ? 93  LEU   A N   1 
ATOM   619  C  CA  . LEU   A 1 77  ? -38.441 32.351  -45.542 1.00 75.75  ? 93  LEU   A CA  1 
ATOM   620  C  C   . LEU   A 1 77  ? -37.486 33.080  -44.606 1.00 74.63  ? 93  LEU   A C   1 
ATOM   621  O  O   . LEU   A 1 77  ? -36.360 33.419  -44.998 1.00 79.26  ? 93  LEU   A O   1 
ATOM   622  C  CB  . LEU   A 1 77  ? -39.417 33.334  -46.189 1.00 75.93  ? 93  LEU   A CB  1 
ATOM   623  C  CG  . LEU   A 1 77  ? -40.324 32.717  -47.259 1.00 80.98  ? 93  LEU   A CG  1 
ATOM   624  C  CD1 . LEU   A 1 77  ? -41.293 33.748  -47.829 1.00 84.47  ? 93  LEU   A CD1 1 
ATOM   625  C  CD2 . LEU   A 1 77  ? -39.486 32.091  -48.380 1.00 86.53  ? 93  LEU   A CD2 1 
ATOM   626  N  N   . ASP   A 1 78  ? -37.921 33.340  -43.369 1.00 72.99  ? 94  ASP   A N   1 
ATOM   627  C  CA  . ASP   A 1 78  ? -37.043 33.976  -42.393 1.00 72.48  ? 94  ASP   A CA  1 
ATOM   628  C  C   . ASP   A 1 78  ? -35.767 33.169  -42.209 1.00 76.27  ? 94  ASP   A C   1 
ATOM   629  O  O   . ASP   A 1 78  ? -34.662 33.723  -42.217 1.00 78.43  ? 94  ASP   A O   1 
ATOM   630  C  CB  . ASP   A 1 78  ? -37.750 34.134  -41.046 1.00 72.85  ? 94  ASP   A CB  1 
ATOM   631  C  CG  . ASP   A 1 78  ? -38.866 35.161  -41.069 1.00 71.23  ? 94  ASP   A CG  1 
ATOM   632  O  OD1 . ASP   A 1 78  ? -38.936 35.981  -42.011 1.00 75.27  ? 94  ASP   A OD1 1 
ATOM   633  O  OD2 . ASP   A 1 78  ? -39.679 35.148  -40.117 1.00 72.34  ? 94  ASP   A OD2 1 
ATOM   634  N  N   . ILE   A 1 79  ? -35.899 31.850  -42.057 1.00 72.25  ? 95  ILE   A N   1 
ATOM   635  C  CA  . ILE   A 1 79  ? -34.728 31.036  -41.747 1.00 74.23  ? 95  ILE   A CA  1 
ATOM   636  C  C   . ILE   A 1 79  ? -33.802 30.938  -42.950 1.00 77.56  ? 95  ILE   A C   1 
ATOM   637  O  O   . ILE   A 1 79  ? -32.587 31.130  -42.826 1.00 78.54  ? 95  ILE   A O   1 
ATOM   638  C  CB  . ILE   A 1 79  ? -35.140 29.641  -41.253 1.00 75.47  ? 95  ILE   A CB  1 
ATOM   639  C  CG1 . ILE   A 1 79  ? -35.739 29.736  -39.861 1.00 68.93  ? 95  ILE   A CG1 1 
ATOM   640  C  CG2 . ILE   A 1 79  ? -33.920 28.726  -41.204 1.00 70.86  ? 95  ILE   A CG2 1 
ATOM   641  C  CD1 . ILE   A 1 79  ? -36.378 28.466  -39.416 1.00 69.99  ? 95  ILE   A CD1 1 
ATOM   642  N  N   . MET   A 1 80  ? -34.348 30.638  -44.129 1.00 76.65  ? 96  MET   A N   1 
ATOM   643  C  CA  . MET   A 1 80  ? -33.436 30.389  -45.234 1.00 85.16  ? 96  MET   A CA  1 
ATOM   644  C  C   . MET   A 1 80  ? -32.693 31.649  -45.693 1.00 89.08  ? 96  MET   A C   1 
ATOM   645  O  O   . MET   A 1 80  ? -31.905 31.559  -46.639 1.00 84.18  ? 96  MET   A O   1 
ATOM   646  C  CB  . MET   A 1 80  ? -34.166 29.712  -46.407 1.00 86.12  ? 96  MET   A CB  1 
ATOM   647  C  CG  . MET   A 1 80  ? -35.463 30.322  -46.895 1.00 89.08  ? 96  MET   A CG  1 
ATOM   648  S  SD  . MET   A 1 80  ? -36.370 29.170  -47.987 1.00 92.20  ? 96  MET   A SD  1 
ATOM   649  C  CE  . MET   A 1 80  ? -36.020 29.854  -49.608 1.00 89.44  ? 96  MET   A CE  1 
ATOM   650  N  N   . GLU   A 1 81  ? -32.881 32.798  -45.031 1.00 89.18  ? 97  GLU   A N   1 
ATOM   651  C  CA  . GLU   A 1 81  ? -31.984 33.934  -45.239 1.00 89.85  ? 97  GLU   A CA  1 
ATOM   652  C  C   . GLU   A 1 81  ? -30.576 33.622  -44.747 1.00 91.59  ? 97  GLU   A C   1 
ATOM   653  O  O   . GLU   A 1 81  ? -29.586 34.028  -45.370 1.00 93.44  ? 97  GLU   A O   1 
ATOM   654  C  CB  . GLU   A 1 81  ? -32.519 35.173  -44.520 1.00 91.50  ? 97  GLU   A CB  1 
ATOM   655  C  CG  . GLU   A 1 81  ? -33.767 35.787  -45.133 1.00 98.35  ? 97  GLU   A CG  1 
ATOM   656  C  CD  . GLU   A 1 81  ? -33.471 37.016  -45.970 1.00 110.12 ? 97  GLU   A CD  1 
ATOM   657  O  OE1 . GLU   A 1 81  ? -32.536 37.776  -45.625 1.00 116.93 ? 97  GLU   A OE1 1 
ATOM   658  O  OE2 . GLU   A 1 81  ? -34.176 37.226  -46.981 1.00 113.00 ? 97  GLU   A OE2 1 
ATOM   659  N  N   . PHE   A 1 82  ? -30.470 32.907  -43.630 1.00 83.39  ? 98  PHE   A N   1 
ATOM   660  C  CA  . PHE   A 1 82  ? -29.193 32.654  -42.977 1.00 86.57  ? 98  PHE   A CA  1 
ATOM   661  C  C   . PHE   A 1 82  ? -28.371 31.578  -43.667 1.00 87.22  ? 98  PHE   A C   1 
ATOM   662  O  O   . PHE   A 1 82  ? -27.271 31.274  -43.190 1.00 90.05  ? 98  PHE   A O   1 
ATOM   663  C  CB  . PHE   A 1 82  ? -29.423 32.253  -41.517 1.00 81.38  ? 98  PHE   A CB  1 
ATOM   664  C  CG  . PHE   A 1 82  ? -30.086 33.316  -40.701 1.00 81.57  ? 98  PHE   A CG  1 
ATOM   665  C  CD1 . PHE   A 1 82  ? -31.459 33.495  -40.757 1.00 76.40  ? 98  PHE   A CD1 1 
ATOM   666  C  CD2 . PHE   A 1 82  ? -29.336 34.150  -39.888 1.00 84.20  ? 98  PHE   A CD2 1 
ATOM   667  C  CE1 . PHE   A 1 82  ? -32.075 34.482  -40.013 1.00 76.04  ? 98  PHE   A CE1 1 
ATOM   668  C  CE2 . PHE   A 1 82  ? -29.949 35.138  -39.137 1.00 87.02  ? 98  PHE   A CE2 1 
ATOM   669  C  CZ  . PHE   A 1 82  ? -31.323 35.303  -39.200 1.00 79.52  ? 98  PHE   A CZ  1 
ATOM   670  N  N   . LEU   A 1 83  ? -28.865 31.009  -44.771 1.00 84.43  ? 99  LEU   A N   1 
ATOM   671  C  CA  . LEU   A 1 83  ? -28.204 29.863  -45.393 1.00 88.35  ? 99  LEU   A CA  1 
ATOM   672  C  C   . LEU   A 1 83  ? -26.822 30.208  -45.946 1.00 92.51  ? 99  LEU   A C   1 
ATOM   673  O  O   . LEU   A 1 83  ? -25.947 29.335  -46.004 1.00 90.04  ? 99  LEU   A O   1 
ATOM   674  C  CB  . LEU   A 1 83  ? -29.087 29.287  -46.500 1.00 81.33  ? 99  LEU   A CB  1 
ATOM   675  C  CG  . LEU   A 1 83  ? -30.262 28.431  -46.008 1.00 91.07  ? 99  LEU   A CG  1 
ATOM   676  C  CD1 . LEU   A 1 83  ? -31.187 28.097  -47.161 1.00 89.59  ? 99  LEU   A CD1 1 
ATOM   677  C  CD2 . LEU   A 1 83  ? -29.781 27.145  -45.308 1.00 84.48  ? 99  LEU   A CD2 1 
ATOM   678  N  N   . ASP   A 1 84  ? -26.599 31.455  -46.354 1.00 88.85  ? 100 ASP   A N   1 
ATOM   679  C  CA  . ASP   A 1 84  ? -25.301 31.861  -46.876 1.00 95.15  ? 100 ASP   A CA  1 
ATOM   680  C  C   . ASP   A 1 84  ? -24.479 32.676  -45.886 1.00 97.99  ? 100 ASP   A C   1 
ATOM   681  O  O   . ASP   A 1 84  ? -23.368 33.091  -46.229 1.00 102.76 ? 100 ASP   A O   1 
ATOM   682  C  CB  . ASP   A 1 84  ? -25.471 32.664  -48.174 1.00 92.20  ? 100 ASP   A CB  1 
ATOM   683  C  CG  . ASP   A 1 84  ? -26.344 33.902  -47.994 1.00 103.03 ? 100 ASP   A CG  1 
ATOM   684  O  OD1 . ASP   A 1 84  ? -27.030 34.022  -46.947 1.00 100.71 ? 100 ASP   A OD1 1 
ATOM   685  O  OD2 . ASP   A 1 84  ? -26.349 34.755  -48.913 1.00 103.80 ? 100 ASP   A OD2 1 
ATOM   686  N  N   . LYS   A 1 85  ? -24.984 32.919  -44.678 1.00 95.03  ? 101 LYS   A N   1 
ATOM   687  C  CA  . LYS   A 1 85  ? -24.294 33.830  -43.775 1.00 99.16  ? 101 LYS   A CA  1 
ATOM   688  C  C   . LYS   A 1 85  ? -23.189 33.109  -43.003 1.00 98.88  ? 101 LYS   A C   1 
ATOM   689  O  O   . LYS   A 1 85  ? -23.138 31.877  -42.928 1.00 94.10  ? 101 LYS   A O   1 
ATOM   690  C  CB  . LYS   A 1 85  ? -25.283 34.496  -42.818 1.00 95.60  ? 101 LYS   A CB  1 
ATOM   691  C  CG  . LYS   A 1 85  ? -25.911 35.776  -43.377 1.00 102.93 ? 101 LYS   A CG  1 
ATOM   692  C  CD  . LYS   A 1 85  ? -26.982 36.304  -42.433 1.00 108.33 ? 101 LYS   A CD  1 
ATOM   693  C  CE  . LYS   A 1 85  ? -27.732 37.496  -43.011 1.00 110.48 ? 101 LYS   A CE  1 
ATOM   694  N  NZ  . LYS   A 1 85  ? -28.916 37.800  -42.149 1.00 103.89 ? 101 LYS   A NZ  1 
ATOM   695  N  N   . ASP   A 1 86  ? -22.293 33.908  -42.423 1.00 102.50 ? 102 ASP   A N   1 
ATOM   696  C  CA  . ASP   A 1 86  ? -21.041 33.400  -41.873 1.00 102.76 ? 102 ASP   A CA  1 
ATOM   697  C  C   . ASP   A 1 86  ? -21.213 33.068  -40.398 1.00 100.31 ? 102 ASP   A C   1 
ATOM   698  O  O   . ASP   A 1 86  ? -21.547 33.962  -39.608 1.00 98.42  ? 102 ASP   A O   1 
ATOM   699  C  CB  . ASP   A 1 86  ? -19.934 34.425  -42.053 1.00 102.42 ? 102 ASP   A CB  1 
ATOM   700  C  CG  . ASP   A 1 86  ? -18.556 33.858  -41.774 1.00 105.29 ? 102 ASP   A CG  1 
ATOM   701  O  OD1 . ASP   A 1 86  ? -18.458 32.706  -41.299 1.00 105.48 ? 102 ASP   A OD1 1 
ATOM   702  O  OD2 . ASP   A 1 86  ? -17.565 34.570  -42.039 1.00 108.95 ? 102 ASP   A OD2 1 
ATOM   703  N  N   . PRO   A 1 87  ? -20.998 31.815  -39.982 1.00 101.14 ? 103 PRO   A N   1 
ATOM   704  C  CA  . PRO   A 1 87  ? -21.158 31.480  -38.558 1.00 98.39  ? 103 PRO   A CA  1 
ATOM   705  C  C   . PRO   A 1 87  ? -20.101 32.099  -37.661 1.00 102.13 ? 103 PRO   A C   1 
ATOM   706  O  O   . PRO   A 1 87  ? -20.340 32.215  -36.452 1.00 100.24 ? 103 PRO   A O   1 
ATOM   707  C  CB  . PRO   A 1 87  ? -21.071 29.946  -38.541 1.00 95.98  ? 103 PRO   A CB  1 
ATOM   708  C  CG  . PRO   A 1 87  ? -21.341 29.523  -39.956 1.00 96.87  ? 103 PRO   A CG  1 
ATOM   709  C  CD  . PRO   A 1 87  ? -20.794 30.618  -40.815 1.00 99.52  ? 103 PRO   A CD  1 
ATOM   710  N  N   . GLU   A 1 88  ? -18.946 32.498  -38.200 1.00 102.50 ? 104 GLU   A N   1 
ATOM   711  C  CA  . GLU   A 1 88  ? -17.911 33.117  -37.380 1.00 103.40 ? 104 GLU   A CA  1 
ATOM   712  C  C   . GLU   A 1 88  ? -18.238 34.556  -37.007 1.00 105.21 ? 104 GLU   A C   1 
ATOM   713  O  O   . GLU   A 1 88  ? -17.503 35.155  -36.214 1.00 109.38 ? 104 GLU   A O   1 
ATOM   714  C  CB  . GLU   A 1 88  ? -16.564 33.068  -38.107 1.00 102.66 ? 104 GLU   A CB  1 
ATOM   715  C  CG  . GLU   A 1 88  ? -16.213 31.700  -38.682 1.00 105.25 ? 104 GLU   A CG  1 
ATOM   716  C  CD  . GLU   A 1 88  ? -16.073 30.625  -37.616 1.00 112.15 ? 104 GLU   A CD  1 
ATOM   717  O  OE1 . GLU   A 1 88  ? -15.498 30.911  -36.543 1.00 113.06 ? 104 GLU   A OE1 1 
ATOM   718  O  OE2 . GLU   A 1 88  ? -16.546 29.491  -37.851 1.00 112.86 ? 104 GLU   A OE2 1 
ATOM   719  N  N   . ASP   A 1 89  ? -19.309 35.122  -37.559 1.00 106.48 ? 105 ASP   A N   1 
ATOM   720  C  CA  . ASP   A 1 89  ? -19.728 36.491  -37.265 1.00 109.22 ? 105 ASP   A CA  1 
ATOM   721  C  C   . ASP   A 1 89  ? -20.759 36.449  -36.138 1.00 109.61 ? 105 ASP   A C   1 
ATOM   722  O  O   . ASP   A 1 89  ? -21.860 35.913  -36.310 1.00 103.71 ? 105 ASP   A O   1 
ATOM   723  C  CB  . ASP   A 1 89  ? -20.292 37.152  -38.523 1.00 107.08 ? 105 ASP   A CB  1 
ATOM   724  C  CG  . ASP   A 1 89  ? -20.554 38.641  -38.349 1.00 111.46 ? 105 ASP   A CG  1 
ATOM   725  O  OD1 . ASP   A 1 89  ? -20.458 39.153  -37.214 1.00 116.40 ? 105 ASP   A OD1 1 
ATOM   726  O  OD2 . ASP   A 1 89  ? -20.853 39.304  -39.364 1.00 111.13 ? 105 ASP   A OD2 1 
ATOM   727  N  N   . HIS   A 1 90  ? -20.400 37.013  -34.983 1.00 109.74 ? 106 HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 90  ? -21.299 37.023  -33.838 1.00 111.38 ? 106 HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 90  ? -22.540 37.862  -34.082 1.00 108.32 ? 106 HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 90  ? -23.509 37.733  -33.327 1.00 107.56 ? 106 HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 90  ? -20.561 37.521  -32.596 1.00 120.27 ? 106 HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 90  ? -19.478 36.597  -32.131 1.00 132.33 ? 106 HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 90  ? -18.700 36.856  -31.022 1.00 140.29 ? 106 HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 90  ? -19.041 35.414  -32.628 1.00 129.82 ? 106 HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 90  ? -17.832 35.873  -30.856 1.00 140.32 ? 106 HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 90  ? -18.018 34.986  -31.817 1.00 137.41 ? 106 HIS   A NE2 1 
ATOM   737  N  N   . ARG   A 1 91  ? -22.537 38.708  -35.114 1.00 108.68 ? 107 ARG   A N   1 
ATOM   738  C  CA  . ARG   A 1 91  ? -23.764 39.388  -35.506 1.00 110.64 ? 107 ARG   A CA  1 
ATOM   739  C  C   . ARG   A 1 91  ? -24.734 38.432  -36.194 1.00 103.75 ? 107 ARG   A C   1 
ATOM   740  O  O   . ARG   A 1 91  ? -25.952 38.564  -36.034 1.00 101.37 ? 107 ARG   A O   1 
ATOM   741  C  CB  . ARG   A 1 91  ? -23.439 40.568  -36.418 1.00 114.70 ? 107 ARG   A CB  1 
ATOM   742  C  CG  . ARG   A 1 91  ? -24.610 41.495  -36.643 1.00 120.82 ? 107 ARG   A CG  1 
ATOM   743  C  CD  . ARG   A 1 91  ? -24.788 42.454  -35.481 1.00 128.33 ? 107 ARG   A CD  1 
ATOM   744  N  NE  . ARG   A 1 91  ? -23.776 43.504  -35.496 1.00 132.58 ? 107 ARG   A NE  1 
ATOM   745  C  CZ  . ARG   A 1 91  ? -23.808 44.587  -34.732 1.00 140.96 ? 107 ARG   A CZ  1 
ATOM   746  N  NH1 . ARG   A 1 91  ? -24.792 44.797  -33.870 1.00 142.77 ? 107 ARG   A NH1 1 
ATOM   747  N  NH2 . ARG   A 1 91  ? -22.831 45.485  -34.837 1.00 139.46 ? 107 ARG   A NH2 1 
ATOM   748  N  N   . THR   A 1 92  ? -24.218 37.468  -36.959 1.00 99.94  ? 108 THR   A N   1 
ATOM   749  C  CA  . THR   A 1 92  ? -25.086 36.458  -37.555 1.00 96.23  ? 108 THR   A CA  1 
ATOM   750  C  C   . THR   A 1 92  ? -25.724 35.581  -36.483 1.00 90.14  ? 108 THR   A C   1 
ATOM   751  O  O   . THR   A 1 92  ? -26.901 35.225  -36.589 1.00 93.07  ? 108 THR   A O   1 
ATOM   752  C  CB  . THR   A 1 92  ? -24.297 35.607  -38.556 1.00 97.72  ? 108 THR   A CB  1 
ATOM   753  O  OG1 . THR   A 1 92  ? -23.877 36.423  -39.657 1.00 101.58 ? 108 THR   A OG1 1 
ATOM   754  C  CG2 . THR   A 1 92  ? -25.147 34.456  -39.089 1.00 89.48  ? 108 THR   A CG2 1 
ATOM   755  N  N   . LEU   A 1 93  ? -24.972 35.245  -35.431 1.00 90.48  ? 109 LEU   A N   1 
ATOM   756  C  CA  . LEU   A 1 93  ? -25.493 34.345  -34.405 1.00 87.89  ? 109 LEU   A CA  1 
ATOM   757  C  C   . LEU   A 1 93  ? -26.594 35.008  -33.581 1.00 92.61  ? 109 LEU   A C   1 
ATOM   758  O  O   . LEU   A 1 93  ? -27.578 34.354  -33.208 1.00 89.00  ? 109 LEU   A O   1 
ATOM   759  C  CB  . LEU   A 1 93  ? -24.354 33.859  -33.506 1.00 85.98  ? 109 LEU   A CB  1 
ATOM   760  C  CG  . LEU   A 1 93  ? -23.274 33.021  -34.203 1.00 88.33  ? 109 LEU   A CG  1 
ATOM   761  C  CD1 . LEU   A 1 93  ? -22.294 32.416  -33.205 1.00 78.10  ? 109 LEU   A CD1 1 
ATOM   762  C  CD2 . LEU   A 1 93  ? -23.899 31.928  -35.054 1.00 84.21  ? 109 LEU   A CD2 1 
ATOM   763  N  N   . SER   A 1 94  ? -26.458 36.307  -33.295 1.00 90.34  ? 110 SER   A N   1 
ATOM   764  C  CA  . SER   A 1 94  ? -27.473 36.993  -32.499 1.00 87.63  ? 110 SER   A CA  1 
ATOM   765  C  C   . SER   A 1 94  ? -28.722 37.295  -33.320 1.00 87.98  ? 110 SER   A C   1 
ATOM   766  O  O   . SER   A 1 94  ? -29.846 37.169  -32.815 1.00 85.96  ? 110 SER   A O   1 
ATOM   767  C  CB  . SER   A 1 94  ? -26.902 38.281  -31.907 1.00 94.16  ? 110 SER   A CB  1 
ATOM   768  O  OG  . SER   A 1 94  ? -26.524 39.186  -32.927 1.00 102.70 ? 110 SER   A OG  1 
ATOM   769  N  N   . GLN   A 1 95  ? -28.549 37.702  -34.580 1.00 89.26  ? 111 GLN   A N   1 
ATOM   770  C  CA  . GLN   A 1 95  ? -29.701 37.879  -35.457 1.00 88.16  ? 111 GLN   A CA  1 
ATOM   771  C  C   . GLN   A 1 95  ? -30.437 36.568  -35.682 1.00 83.55  ? 111 GLN   A C   1 
ATOM   772  O  O   . GLN   A 1 95  ? -31.639 36.573  -35.962 1.00 82.35  ? 111 GLN   A O   1 
ATOM   773  C  CB  . GLN   A 1 95  ? -29.263 38.461  -36.794 1.00 92.27  ? 111 GLN   A CB  1 
ATOM   774  C  CG  . GLN   A 1 95  ? -28.707 39.858  -36.706 1.00 95.94  ? 111 GLN   A CG  1 
ATOM   775  C  CD  . GLN   A 1 95  ? -27.951 40.239  -37.957 1.00 102.84 ? 111 GLN   A CD  1 
ATOM   776  O  OE1 . GLN   A 1 95  ? -27.792 39.426  -38.869 1.00 100.15 ? 111 GLN   A OE1 1 
ATOM   777  N  NE2 . GLN   A 1 95  ? -27.478 41.476  -38.008 1.00 107.03 ? 111 GLN   A NE2 1 
ATOM   778  N  N   . PHE   A 1 96  ? -29.734 35.438  -35.580 1.00 83.00  ? 112 PHE   A N   1 
ATOM   779  C  CA  . PHE   A 1 96  ? -30.394 34.147  -35.724 1.00 77.59  ? 112 PHE   A CA  1 
ATOM   780  C  C   . PHE   A 1 96  ? -31.292 33.863  -34.530 1.00 78.98  ? 112 PHE   A C   1 
ATOM   781  O  O   . PHE   A 1 96  ? -32.454 33.469  -34.693 1.00 77.09  ? 112 PHE   A O   1 
ATOM   782  C  CB  . PHE   A 1 96  ? -29.361 33.041  -35.894 1.00 74.33  ? 112 PHE   A CB  1 
ATOM   783  C  CG  . PHE   A 1 96  ? -29.962 31.681  -36.073 1.00 73.43  ? 112 PHE   A CG  1 
ATOM   784  C  CD1 . PHE   A 1 96  ? -30.602 31.345  -37.251 1.00 71.59  ? 112 PHE   A CD1 1 
ATOM   785  C  CD2 . PHE   A 1 96  ? -29.892 30.737  -35.063 1.00 69.75  ? 112 PHE   A CD2 1 
ATOM   786  C  CE1 . PHE   A 1 96  ? -31.158 30.094  -37.419 1.00 67.13  ? 112 PHE   A CE1 1 
ATOM   787  C  CE2 . PHE   A 1 96  ? -30.443 29.487  -35.230 1.00 66.87  ? 112 PHE   A CE2 1 
ATOM   788  C  CZ  . PHE   A 1 96  ? -31.076 29.166  -36.410 1.00 62.18  ? 112 PHE   A CZ  1 
ATOM   789  N  N   . THR   A 1 97  ? -30.773 34.065  -33.317 1.00 78.34  ? 113 THR   A N   1 
ATOM   790  C  CA  . THR   A 1 97  ? -31.602 33.900  -32.127 1.00 75.85  ? 113 THR   A CA  1 
ATOM   791  C  C   . THR   A 1 97  ? -32.820 34.818  -32.169 1.00 75.28  ? 113 THR   A C   1 
ATOM   792  O  O   . THR   A 1 97  ? -33.940 34.388  -31.872 1.00 77.88  ? 113 THR   A O   1 
ATOM   793  C  CB  . THR   A 1 97  ? -30.768 34.159  -30.876 1.00 77.20  ? 113 THR   A CB  1 
ATOM   794  O  OG1 . THR   A 1 97  ? -29.558 33.393  -30.948 1.00 78.00  ? 113 THR   A OG1 1 
ATOM   795  C  CG2 . THR   A 1 97  ? -31.542 33.753  -29.638 1.00 77.96  ? 113 THR   A CG2 1 
ATOM   796  N  N   . ASP   A 1 98  ? -32.620 36.085  -32.542 1.00 78.57  ? 114 ASP   A N   1 
ATOM   797  C  CA  . ASP   A 1 98  ? -33.741 37.006  -32.709 1.00 79.38  ? 114 ASP   A CA  1 
ATOM   798  C  C   . ASP   A 1 98  ? -34.784 36.445  -33.663 1.00 78.96  ? 114 ASP   A C   1 
ATOM   799  O  O   . ASP   A 1 98  ? -35.991 36.514  -33.394 1.00 79.72  ? 114 ASP   A O   1 
ATOM   800  C  CB  . ASP   A 1 98  ? -33.236 38.353  -33.227 1.00 85.91  ? 114 ASP   A CB  1 
ATOM   801  C  CG  . ASP   A 1 98  ? -32.641 39.208  -32.134 1.00 89.09  ? 114 ASP   A CG  1 
ATOM   802  O  OD1 . ASP   A 1 98  ? -33.039 39.024  -30.966 1.00 95.26  ? 114 ASP   A OD1 1 
ATOM   803  O  OD2 . ASP   A 1 98  ? -31.789 40.069  -32.440 1.00 99.74  ? 114 ASP   A OD2 1 
ATOM   804  N  N   . ALA   A 1 99  ? -34.334 35.888  -34.789 1.00 75.71  ? 115 ALA   A N   1 
ATOM   805  C  CA  . ALA   A 1 99  ? -35.266 35.340  -35.765 1.00 78.14  ? 115 ALA   A CA  1 
ATOM   806  C  C   . ALA   A 1 99  ? -36.011 34.130  -35.215 1.00 75.31  ? 115 ALA   A C   1 
ATOM   807  O  O   . ALA   A 1 99  ? -37.170 33.895  -35.580 1.00 75.84  ? 115 ALA   A O   1 
ATOM   808  C  CB  . ALA   A 1 99  ? -34.521 34.979  -37.049 1.00 72.77  ? 115 ALA   A CB  1 
ATOM   809  N  N   . LEU   A 1 100 ? -35.377 33.355  -34.335 1.00 73.99  ? 116 LEU   A N   1 
ATOM   810  C  CA  . LEU   A 1 100 ? -36.050 32.181  -33.795 1.00 73.02  ? 116 LEU   A CA  1 
ATOM   811  C  C   . LEU   A 1 100 ? -37.159 32.582  -32.832 1.00 74.19  ? 116 LEU   A C   1 
ATOM   812  O  O   . LEU   A 1 100 ? -38.231 31.968  -32.826 1.00 71.48  ? 116 LEU   A O   1 
ATOM   813  C  CB  . LEU   A 1 100 ? -35.041 31.255  -33.117 1.00 63.46  ? 116 LEU   A CB  1 
ATOM   814  C  CG  . LEU   A 1 100 ? -34.146 30.460  -34.063 1.00 64.82  ? 116 LEU   A CG  1 
ATOM   815  C  CD1 . LEU   A 1 100 ? -33.393 29.411  -33.287 1.00 62.74  ? 116 LEU   A CD1 1 
ATOM   816  C  CD2 . LEU   A 1 100 ? -34.956 29.815  -35.167 1.00 65.94  ? 116 LEU   A CD2 1 
ATOM   817  N  N   . VAL   A 1 101 ? -36.926 33.622  -32.028 1.00 75.92  ? 117 VAL   A N   1 
ATOM   818  C  CA  . VAL   A 1 101 ? -37.955 34.104  -31.110 1.00 78.45  ? 117 VAL   A CA  1 
ATOM   819  C  C   . VAL   A 1 101 ? -39.159 34.622  -31.887 1.00 78.30  ? 117 VAL   A C   1 
ATOM   820  O  O   . VAL   A 1 101 ? -40.316 34.369  -31.521 1.00 75.29  ? 117 VAL   A O   1 
ATOM   821  C  CB  . VAL   A 1 101 ? -37.376 35.189  -30.185 1.00 76.74  ? 117 VAL   A CB  1 
ATOM   822  C  CG1 . VAL   A 1 101 ? -38.428 35.632  -29.185 1.00 79.76  ? 117 VAL   A CG1 1 
ATOM   823  C  CG2 . VAL   A 1 101 ? -36.127 34.673  -29.477 1.00 73.64  ? 117 VAL   A CG2 1 
ATOM   824  N  N   . THR   A 1 102 ? -38.906 35.360  -32.968 1.00 79.38  ? 118 THR   A N   1 
ATOM   825  C  CA  . THR   A 1 102 ? -39.996 35.868  -33.793 1.00 77.59  ? 118 THR   A CA  1 
ATOM   826  C  C   . THR   A 1 102 ? -40.811 34.725  -34.390 1.00 76.55  ? 118 THR   A C   1 
ATOM   827  O  O   . THR   A 1 102 ? -42.049 34.748  -34.360 1.00 77.69  ? 118 THR   A O   1 
ATOM   828  C  CB  . THR   A 1 102 ? -39.430 36.770  -34.887 1.00 77.36  ? 118 THR   A CB  1 
ATOM   829  O  OG1 . THR   A 1 102 ? -38.779 37.894  -34.274 1.00 78.52  ? 118 THR   A OG1 1 
ATOM   830  C  CG2 . THR   A 1 102 ? -40.542 37.254  -35.826 1.00 75.22  ? 118 THR   A CG2 1 
ATOM   831  N  N   . ILE   A 1 103 ? -40.133 33.706  -34.926 1.00 76.10  ? 119 ILE   A N   1 
ATOM   832  C  CA  . ILE   A 1 103 ? -40.850 32.574  -35.505 1.00 71.55  ? 119 ILE   A CA  1 
ATOM   833  C  C   . ILE   A 1 103 ? -41.688 31.873  -34.446 1.00 73.49  ? 119 ILE   A C   1 
ATOM   834  O  O   . ILE   A 1 103 ? -42.863 31.560  -34.680 1.00 69.57  ? 119 ILE   A O   1 
ATOM   835  C  CB  . ILE   A 1 103 ? -39.872 31.608  -36.194 1.00 68.14  ? 119 ILE   A CB  1 
ATOM   836  C  CG1 . ILE   A 1 103 ? -39.324 32.259  -37.458 1.00 70.08  ? 119 ILE   A CG1 1 
ATOM   837  C  CG2 . ILE   A 1 103 ? -40.564 30.298  -36.515 1.00 64.05  ? 119 ILE   A CG2 1 
ATOM   838  C  CD1 . ILE   A 1 103 ? -38.095 31.596  -38.008 1.00 71.14  ? 119 ILE   A CD1 1 
ATOM   839  N  N   . ARG   A 1 104 ? -41.117 31.641  -33.258 1.00 70.22  ? 120 ARG   A N   1 
ATOM   840  C  CA  . ARG   A 1 104 ? -41.889 30.991  -32.203 1.00 70.89  ? 120 ARG   A CA  1 
ATOM   841  C  C   . ARG   A 1 104 ? -43.140 31.788  -31.864 1.00 73.69  ? 120 ARG   A C   1 
ATOM   842  O  O   . ARG   A 1 104 ? -44.236 31.224  -31.778 1.00 70.54  ? 120 ARG   A O   1 
ATOM   843  C  CB  . ARG   A 1 104 ? -41.048 30.788  -30.948 1.00 75.19  ? 120 ARG   A CB  1 
ATOM   844  C  CG  . ARG   A 1 104 ? -41.822 30.071  -29.837 1.00 73.08  ? 120 ARG   A CG  1 
ATOM   845  C  CD  . ARG   A 1 104 ? -40.962 29.882  -28.606 1.00 70.93  ? 120 ARG   A CD  1 
ATOM   846  N  NE  . ARG   A 1 104 ? -40.425 31.154  -28.147 1.00 75.02  ? 120 ARG   A NE  1 
ATOM   847  C  CZ  . ARG   A 1 104 ? -39.224 31.312  -27.608 1.00 75.13  ? 120 ARG   A CZ  1 
ATOM   848  N  NH1 . ARG   A 1 104 ? -38.398 30.290  -27.437 1.00 71.81  ? 120 ARG   A NH1 1 
ATOM   849  N  NH2 . ARG   A 1 104 ? -38.837 32.527  -27.241 1.00 79.28  ? 120 ARG   A NH2 1 
ATOM   850  N  N   . ASN   A 1 105 ? -42.998 33.108  -31.679 1.00 71.23  ? 121 ASN   A N   1 
ATOM   851  C  CA  . ASN   A 1 105 ? -44.149 33.916  -31.274 1.00 77.49  ? 121 ASN   A CA  1 
ATOM   852  C  C   . ASN   A 1 105 ? -45.198 34.007  -32.377 1.00 75.95  ? 121 ASN   A C   1 
ATOM   853  O  O   . ASN   A 1 105 ? -46.398 34.072  -32.082 1.00 66.51  ? 121 ASN   A O   1 
ATOM   854  C  CB  . ASN   A 1 105 ? -43.705 35.325  -30.867 1.00 77.06  ? 121 ASN   A CB  1 
ATOM   855  C  CG  . ASN   A 1 105 ? -42.620 35.314  -29.809 1.00 82.55  ? 121 ASN   A CG  1 
ATOM   856  O  OD1 . ASN   A 1 105 ? -41.740 36.179  -29.799 1.00 90.15  ? 121 ASN   A OD1 1 
ATOM   857  N  ND2 . ASN   A 1 105 ? -42.673 34.333  -28.912 1.00 80.19  ? 121 ASN   A ND2 1 
ATOM   858  N  N   . ARG   A 1 106 ? -44.760 34.029  -33.643 1.00 74.07  ? 122 ARG   A N   1 
ATOM   859  C  CA  . ARG   A 1 106 ? -45.685 34.079  -34.777 1.00 72.21  ? 122 ARG   A CA  1 
ATOM   860  C  C   . ARG   A 1 106 ? -46.648 32.893  -34.768 1.00 71.81  ? 122 ARG   A C   1 
ATOM   861  O  O   . ARG   A 1 106 ? -47.833 33.041  -35.099 1.00 66.09  ? 122 ARG   A O   1 
ATOM   862  C  CB  . ARG   A 1 106 ? -44.887 34.123  -36.088 1.00 73.12  ? 122 ARG   A CB  1 
ATOM   863  C  CG  . ARG   A 1 106 ? -45.729 33.993  -37.344 1.00 69.39  ? 122 ARG   A CG  1 
ATOM   864  C  CD  . ARG   A 1 106 ? -44.889 33.903  -38.615 1.00 70.65  ? 122 ARG   A CD  1 
ATOM   865  N  NE  . ARG   A 1 106 ? -44.074 35.091  -38.868 1.00 71.18  ? 122 ARG   A NE  1 
ATOM   866  C  CZ  . ARG   A 1 106 ? -42.774 35.056  -39.132 1.00 74.18  ? 122 ARG   A CZ  1 
ATOM   867  N  NH1 . ARG   A 1 106 ? -42.114 33.911  -39.196 1.00 70.37  ? 122 ARG   A NH1 1 
ATOM   868  N  NH2 . ARG   A 1 106 ? -42.121 36.198  -39.351 1.00 70.69  ? 122 ARG   A NH2 1 
ATOM   869  N  N   . HIS   A 1 107 ? -46.164 31.716  -34.368 1.00 69.43  ? 123 HIS   A N   1 
ATOM   870  C  CA  . HIS   A 1 107 ? -46.946 30.487  -34.366 1.00 65.45  ? 123 HIS   A CA  1 
ATOM   871  C  C   . HIS   A 1 107 ? -47.683 30.225  -33.049 1.00 69.20  ? 123 HIS   A C   1 
ATOM   872  O  O   . HIS   A 1 107 ? -48.170 29.107  -32.846 1.00 65.35  ? 123 HIS   A O   1 
ATOM   873  C  CB  . HIS   A 1 107 ? -46.039 29.291  -34.670 1.00 57.94  ? 123 HIS   A CB  1 
ATOM   874  C  CG  . HIS   A 1 107 ? -45.447 29.307  -36.041 1.00 63.13  ? 123 HIS   A CG  1 
ATOM   875  N  ND1 . HIS   A 1 107 ? -45.702 28.323  -36.970 1.00 60.18  ? 123 HIS   A ND1 1 
ATOM   876  C  CD2 . HIS   A 1 107 ? -44.606 30.182  -36.642 1.00 63.52  ? 123 HIS   A CD2 1 
ATOM   877  C  CE1 . HIS   A 1 107 ? -45.044 28.590  -38.084 1.00 65.33  ? 123 HIS   A CE1 1 
ATOM   878  N  NE2 . HIS   A 1 107 ? -44.372 29.714  -37.913 1.00 62.82  ? 123 HIS   A NE2 1 
ATOM   879  N  N   . ASN   A 1 108 ? -47.793 31.219  -32.157 1.00 65.96  ? 124 ASN   A N   1 
ATOM   880  C  CA  . ASN   A 1 108 ? -48.248 30.926  -30.797 1.00 67.27  ? 124 ASN   A CA  1 
ATOM   881  C  C   . ASN   A 1 108 ? -49.708 30.492  -30.743 1.00 66.38  ? 124 ASN   A C   1 
ATOM   882  O  O   . ASN   A 1 108 ? -50.091 29.754  -29.827 1.00 64.05  ? 124 ASN   A O   1 
ATOM   883  C  CB  . ASN   A 1 108 ? -48.022 32.132  -29.882 1.00 67.51  ? 124 ASN   A CB  1 
ATOM   884  C  CG  . ASN   A 1 108 ? -46.740 32.000  -29.061 1.00 78.24  ? 124 ASN   A CG  1 
ATOM   885  O  OD1 . ASN   A 1 108 ? -46.259 30.891  -28.823 1.00 76.05  ? 124 ASN   A OD1 1 
ATOM   886  N  ND2 . ASN   A 1 108 ? -46.181 33.133  -28.633 1.00 80.46  ? 124 ASN   A ND2 1 
ATOM   887  N  N   . ASP   A 1 109 ? -50.527 30.915  -31.711 1.00 68.33  ? 125 ASP   A N   1 
ATOM   888  C  CA  . ASP   A 1 109 ? -51.969 30.694  -31.687 1.00 65.36  ? 125 ASP   A CA  1 
ATOM   889  C  C   . ASP   A 1 109 ? -52.413 29.521  -32.563 1.00 61.15  ? 125 ASP   A C   1 
ATOM   890  O  O   . ASP   A 1 109 ? -53.576 29.476  -32.980 1.00 59.61  ? 125 ASP   A O   1 
ATOM   891  C  CB  . ASP   A 1 109 ? -52.694 31.974  -32.123 1.00 64.01  ? 125 ASP   A CB  1 
ATOM   892  C  CG  . ASP   A 1 109 ? -52.501 33.119  -31.146 1.00 69.37  ? 125 ASP   A CG  1 
ATOM   893  O  OD1 . ASP   A 1 109 ? -52.404 32.849  -29.932 1.00 73.11  ? 125 ASP   A OD1 1 
ATOM   894  O  OD2 . ASP   A 1 109 ? -52.447 34.289  -31.588 1.00 76.16  ? 125 ASP   A OD2 1 
ATOM   895  N  N   . VAL   A 1 110 ? -51.518 28.579  -32.859 1.00 54.23  ? 126 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 110 ? -51.839 27.558  -33.850 1.00 55.57  ? 126 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 110 ? -52.930 26.629  -33.336 1.00 55.79  ? 126 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 110 ? -53.825 26.229  -34.094 1.00 55.79  ? 126 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 110 ? -50.573 26.785  -34.261 1.00 56.71  ? 126 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 110 ? -50.940 25.546  -35.012 1.00 60.13  ? 126 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 110 ? -49.704 27.637  -35.162 1.00 60.45  ? 126 VAL   A CG2 1 
ATOM   902  N  N   . VAL   A 1 111 ? -52.900 26.295  -32.048 1.00 54.02  ? 127 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 111 ? -53.815 25.282  -31.514 1.00 49.91  ? 127 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 111 ? -55.265 25.763  -31.609 1.00 53.48  ? 127 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 111 ? -56.094 25.055  -32.203 1.00 52.35  ? 127 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 111 ? -53.428 24.870  -30.080 1.00 56.03  ? 127 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 111 ? -54.485 23.954  -29.476 1.00 49.60  ? 127 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 111 ? -52.063 24.162  -30.091 1.00 47.83  ? 127 VAL   A CG2 1 
ATOM   909  N  N   . PRO   A 1 112 ? -55.639 26.933  -31.078 1.00 55.88  ? 128 PRO   A N   1 
ATOM   910  C  CA  . PRO   A 1 112 ? -57.025 27.389  -31.276 1.00 53.73  ? 128 PRO   A CA  1 
ATOM   911  C  C   . PRO   A 1 112 ? -57.359 27.723  -32.727 1.00 52.30  ? 128 PRO   A C   1 
ATOM   912  O  O   . PRO   A 1 112 ? -58.542 27.707  -33.085 1.00 52.04  ? 128 PRO   A O   1 
ATOM   913  C  CB  . PRO   A 1 112 ? -57.115 28.639  -30.389 1.00 52.28  ? 128 PRO   A CB  1 
ATOM   914  C  CG  . PRO   A 1 112 ? -55.726 29.168  -30.367 1.00 54.59  ? 128 PRO   A CG  1 
ATOM   915  C  CD  . PRO   A 1 112 ? -54.842 27.943  -30.353 1.00 56.34  ? 128 PRO   A CD  1 
ATOM   916  N  N   . THR   A 1 113 ? -56.372 28.038  -33.567 1.00 53.55  ? 129 THR   A N   1 
ATOM   917  C  CA  . THR   A 1 113 ? -56.664 28.278  -34.978 1.00 51.78  ? 129 THR   A CA  1 
ATOM   918  C  C   . THR   A 1 113 ? -57.080 26.986  -35.667 1.00 51.29  ? 129 THR   A C   1 
ATOM   919  O  O   . THR   A 1 113 ? -58.127 26.930  -36.326 1.00 45.13  ? 129 THR   A O   1 
ATOM   920  C  CB  . THR   A 1 113 ? -55.454 28.893  -35.678 1.00 53.43  ? 129 THR   A CB  1 
ATOM   921  O  OG1 . THR   A 1 113 ? -55.169 30.166  -35.095 1.00 53.12  ? 129 THR   A OG1 1 
ATOM   922  C  CG2 . THR   A 1 113 ? -55.733 29.071  -37.168 1.00 45.24  ? 129 THR   A CG2 1 
ATOM   923  N  N   . MET   A 1 114 ? -56.286 25.925  -35.496 1.00 47.04  ? 130 MET   A N   1 
ATOM   924  C  CA  . MET   A 1 114 ? -56.661 24.625  -36.041 1.00 52.85  ? 130 MET   A CA  1 
ATOM   925  C  C   . MET   A 1 114 ? -57.941 24.088  -35.418 1.00 52.25  ? 130 MET   A C   1 
ATOM   926  O  O   . MET   A 1 114 ? -58.715 23.405  -36.101 1.00 51.72  ? 130 MET   A O   1 
ATOM   927  C  CB  . MET   A 1 114 ? -55.540 23.615  -35.835 1.00 48.82  ? 130 MET   A CB  1 
ATOM   928  C  CG  . MET   A 1 114 ? -54.269 24.012  -36.489 1.00 53.77  ? 130 MET   A CG  1 
ATOM   929  S  SD  . MET   A 1 114 ? -54.394 24.014  -38.277 1.00 59.62  ? 130 MET   A SD  1 
ATOM   930  C  CE  . MET   A 1 114 ? -54.540 22.290  -38.624 1.00 59.58  ? 130 MET   A CE  1 
ATOM   931  N  N   . ALA   A 1 115 ? -58.180 24.364  -34.130 1.00 48.90  ? 131 ALA   A N   1 
ATOM   932  C  CA  . ALA   A 1 115 ? -59.427 23.917  -33.513 1.00 49.70  ? 131 ALA   A CA  1 
ATOM   933  C  C   . ALA   A 1 115 ? -60.629 24.577  -34.178 1.00 49.83  ? 131 ALA   A C   1 
ATOM   934  O  O   . ALA   A 1 115 ? -61.677 23.947  -34.357 1.00 52.21  ? 131 ALA   A O   1 
ATOM   935  C  CB  . ALA   A 1 115 ? -59.419 24.221  -32.011 1.00 49.17  ? 131 ALA   A CB  1 
ATOM   936  N  N   . GLN   A 1 116 ? -60.502 25.858  -34.525 1.00 46.69  ? 132 GLN   A N   1 
ATOM   937  C  CA  . GLN   A 1 116 ? -61.573 26.535  -35.247 1.00 51.83  ? 132 GLN   A CA  1 
ATOM   938  C  C   . GLN   A 1 116 ? -61.824 25.879  -36.601 1.00 50.43  ? 132 GLN   A C   1 
ATOM   939  O  O   . GLN   A 1 116 ? -62.970 25.803  -37.062 1.00 50.49  ? 132 GLN   A O   1 
ATOM   940  C  CB  . GLN   A 1 116 ? -61.237 28.016  -35.405 1.00 50.57  ? 132 GLN   A CB  1 
ATOM   941  C  CG  . GLN   A 1 116 ? -62.182 28.762  -36.289 1.00 53.23  ? 132 GLN   A CG  1 
ATOM   942  C  CD  . GLN   A 1 116 ? -63.581 28.877  -35.685 1.00 58.30  ? 132 GLN   A CD  1 
ATOM   943  O  OE1 . GLN   A 1 116 ? -63.764 28.702  -34.475 1.00 57.54  ? 132 GLN   A OE1 1 
ATOM   944  N  NE2 . GLN   A 1 116 ? -64.575 29.174  -36.531 1.00 50.76  ? 132 GLN   A NE2 1 
ATOM   945  N  N   . GLY   A 1 117 ? -60.764 25.400  -37.259 1.00 49.01  ? 133 GLY   A N   1 
ATOM   946  C  CA  . GLY   A 1 117 ? -60.954 24.686  -38.518 1.00 48.55  ? 133 GLY   A CA  1 
ATOM   947  C  C   . GLY   A 1 117 ? -61.718 23.383  -38.340 1.00 52.78  ? 133 GLY   A C   1 
ATOM   948  O  O   . GLY   A 1 117 ? -62.602 23.050  -39.142 1.00 49.82  ? 133 GLY   A O   1 
ATOM   949  N  N   . VAL   A 1 118 ? -61.408 22.644  -37.273 1.00 47.35  ? 134 VAL   A N   1 
ATOM   950  C  CA  . VAL   A 1 118 ? -62.139 21.414  -36.971 1.00 46.00  ? 134 VAL   A CA  1 
ATOM   951  C  C   . VAL   A 1 118 ? -63.619 21.712  -36.736 1.00 48.92  ? 134 VAL   A C   1 
ATOM   952  O  O   . VAL   A 1 118 ? -64.504 21.021  -37.263 1.00 45.28  ? 134 VAL   A O   1 
ATOM   953  C  CB  . VAL   A 1 118 ? -61.505 20.707  -35.760 1.00 50.70  ? 134 VAL   A CB  1 
ATOM   954  C  CG1 . VAL   A 1 118 ? -62.296 19.472  -35.395 1.00 48.04  ? 134 VAL   A CG1 1 
ATOM   955  C  CG2 . VAL   A 1 118 ? -60.034 20.357  -36.050 1.00 46.91  ? 134 VAL   A CG2 1 
ATOM   956  N  N   . LEU   A 1 119 ? -63.912 22.738  -35.925 1.00 48.19  ? 135 LEU   A N   1 
ATOM   957  C  CA  . LEU   A 1 119 ? -65.298 23.145  -35.698 1.00 49.95  ? 135 LEU   A CA  1 
ATOM   958  C  C   . LEU   A 1 119 ? -66.018 23.447  -37.008 1.00 54.34  ? 135 LEU   A C   1 
ATOM   959  O  O   . LEU   A 1 119 ? -67.168 23.040  -37.205 1.00 49.19  ? 135 LEU   A O   1 
ATOM   960  C  CB  . LEU   A 1 119 ? -65.344 24.374  -34.786 1.00 56.52  ? 135 LEU   A CB  1 
ATOM   961  C  CG  . LEU   A 1 119 ? -65.481 24.096  -33.290 1.00 74.91  ? 135 LEU   A CG  1 
ATOM   962  C  CD1 . LEU   A 1 119 ? -64.703 25.114  -32.435 1.00 67.47  ? 135 LEU   A CD1 1 
ATOM   963  C  CD2 . LEU   A 1 119 ? -66.969 24.091  -32.939 1.00 76.26  ? 135 LEU   A CD2 1 
ATOM   964  N  N   . GLU   A 1 120 ? -65.354 24.163  -37.917 1.00 48.12  ? 136 GLU   A N   1 
ATOM   965  C  CA  . GLU   A 1 120 ? -65.993 24.497  -39.184 1.00 54.68  ? 136 GLU   A CA  1 
ATOM   966  C  C   . GLU   A 1 120 ? -66.289 23.254  -40.003 1.00 51.20  ? 136 GLU   A C   1 
ATOM   967  O  O   . GLU   A 1 120 ? -67.377 23.135  -40.583 1.00 52.98  ? 136 GLU   A O   1 
ATOM   968  C  CB  . GLU   A 1 120 ? -65.118 25.444  -39.980 1.00 49.18  ? 136 GLU   A CB  1 
ATOM   969  C  CG  . GLU   A 1 120 ? -65.126 26.799  -39.400 1.00 52.20  ? 136 GLU   A CG  1 
ATOM   970  C  CD  . GLU   A 1 120 ? -64.178 27.719  -40.108 1.00 57.72  ? 136 GLU   A CD  1 
ATOM   971  O  OE1 . GLU   A 1 120 ? -63.626 27.329  -41.177 1.00 56.58  ? 136 GLU   A OE1 1 
ATOM   972  O  OE2 . GLU   A 1 120 ? -63.991 28.833  -39.572 1.00 56.68  ? 136 GLU   A OE2 1 
ATOM   973  N  N   . TYR   A 1 121 ? -65.340 22.311  -40.049 1.00 50.41  ? 137 TYR   A N   1 
ATOM   974  C  CA  . TYR   A 1 121 ? -65.538 21.112  -40.856 1.00 49.56  ? 137 TYR   A CA  1 
ATOM   975  C  C   . TYR   A 1 121 ? -66.713 20.287  -40.338 1.00 52.75  ? 137 TYR   A C   1 
ATOM   976  O  O   . TYR   A 1 121 ? -67.541 19.805  -41.127 1.00 52.64  ? 137 TYR   A O   1 
ATOM   977  C  CB  . TYR   A 1 121 ? -64.255 20.274  -40.895 1.00 49.25  ? 137 TYR   A CB  1 
ATOM   978  C  CG  . TYR   A 1 121 ? -64.381 19.098  -41.843 1.00 56.35  ? 137 TYR   A CG  1 
ATOM   979  C  CD1 . TYR   A 1 121 ? -64.879 17.875  -41.407 1.00 54.09  ? 137 TYR   A CD1 1 
ATOM   980  C  CD2 . TYR   A 1 121 ? -64.029 19.218  -43.194 1.00 54.96  ? 137 TYR   A CD2 1 
ATOM   981  C  CE1 . TYR   A 1 121 ? -65.024 16.807  -42.280 1.00 55.88  ? 137 TYR   A CE1 1 
ATOM   982  C  CE2 . TYR   A 1 121 ? -64.158 18.149  -44.069 1.00 52.67  ? 137 TYR   A CE2 1 
ATOM   983  C  CZ  . TYR   A 1 121 ? -64.655 16.944  -43.603 1.00 57.80  ? 137 TYR   A CZ  1 
ATOM   984  O  OH  . TYR   A 1 121 ? -64.793 15.879  -44.466 1.00 64.16  ? 137 TYR   A OH  1 
ATOM   985  N  N   . LYS   A 1 122 ? -66.820 20.141  -39.011 1.00 52.35  ? 138 LYS   A N   1 
ATOM   986  C  CA  . LYS   A 1 122 ? -67.957 19.438  -38.417 1.00 55.12  ? 138 LYS   A CA  1 
ATOM   987  C  C   . LYS   A 1 122 ? -69.291 20.009  -38.893 1.00 56.92  ? 138 LYS   A C   1 
ATOM   988  O  O   . LYS   A 1 122 ? -70.236 19.258  -39.163 1.00 53.71  ? 138 LYS   A O   1 
ATOM   989  C  CB  . LYS   A 1 122 ? -67.867 19.495  -36.886 1.00 53.09  ? 138 LYS   A CB  1 
ATOM   990  C  CG  . LYS   A 1 122 ? -69.173 19.103  -36.160 1.00 67.35  ? 138 LYS   A CG  1 
ATOM   991  C  CD  . LYS   A 1 122 ? -69.078 19.262  -34.622 1.00 74.30  ? 138 LYS   A CD  1 
ATOM   992  C  CE  . LYS   A 1 122 ? -67.965 18.401  -34.010 1.00 68.68  ? 138 LYS   A CE  1 
ATOM   993  N  NZ  . LYS   A 1 122 ? -67.895 18.512  -32.513 1.00 74.79  ? 138 LYS   A NZ  1 
ATOM   994  N  N   . ASP   A 1 123 ? -69.391 21.334  -39.012 1.00 53.44  ? 139 ASP   A N   1 
ATOM   995  C  CA  . ASP   A 1 123 ? -70.644 21.940  -39.454 1.00 54.71  ? 139 ASP   A CA  1 
ATOM   996  C  C   . ASP   A 1 123 ? -70.745 22.116  -40.971 1.00 51.22  ? 139 ASP   A C   1 
ATOM   997  O  O   . ASP   A 1 123 ? -71.861 22.149  -41.505 1.00 51.02  ? 139 ASP   A O   1 
ATOM   998  C  CB  . ASP   A 1 123 ? -70.845 23.288  -38.753 1.00 58.01  ? 139 ASP   A CB  1 
ATOM   999  C  CG  . ASP   A 1 123 ? -70.894 23.143  -37.234 1.00 59.54  ? 139 ASP   A CG  1 
ATOM   1000 O  OD1 . ASP   A 1 123 ? -71.240 22.041  -36.767 1.00 62.49  ? 139 ASP   A OD1 1 
ATOM   1001 O  OD2 . ASP   A 1 123 ? -70.580 24.109  -36.510 1.00 61.45  ? 139 ASP   A OD2 1 
ATOM   1002 N  N   . THR   A 1 124 ? -69.632 22.221  -41.696 1.00 49.27  ? 140 THR   A N   1 
ATOM   1003 C  CA  . THR   A 1 124 ? -69.783 22.364  -43.137 1.00 53.40  ? 140 THR   A CA  1 
ATOM   1004 C  C   . THR   A 1 124 ? -69.758 21.032  -43.882 1.00 53.31  ? 140 THR   A C   1 
ATOM   1005 O  O   . THR   A 1 124 ? -70.300 20.961  -44.990 1.00 54.97  ? 140 THR   A O   1 
ATOM   1006 C  CB  . THR   A 1 124 ? -68.723 23.322  -43.701 1.00 51.58  ? 140 THR   A CB  1 
ATOM   1007 O  OG1 . THR   A 1 124 ? -67.419 22.905  -43.296 1.00 57.46  ? 140 THR   A OG1 1 
ATOM   1008 C  CG2 . THR   A 1 124 ? -68.979 24.731  -43.173 1.00 53.41  ? 140 THR   A CG2 1 
ATOM   1009 N  N   . TYR   A 1 125 ? -69.186 19.978  -43.288 1.00 52.84  ? 141 TYR   A N   1 
ATOM   1010 C  CA  . TYR   A 1 125 ? -69.144 18.651  -43.906 1.00 55.95  ? 141 TYR   A CA  1 
ATOM   1011 C  C   . TYR   A 1 125 ? -69.491 17.489  -42.977 1.00 60.04  ? 141 TYR   A C   1 
ATOM   1012 O  O   . TYR   A 1 125 ? -69.787 16.405  -43.491 1.00 62.89  ? 141 TYR   A O   1 
ATOM   1013 C  CB  . TYR   A 1 125 ? -67.761 18.406  -44.548 1.00 50.66  ? 141 TYR   A CB  1 
ATOM   1014 C  CG  . TYR   A 1 125 ? -67.576 19.342  -45.736 1.00 55.91  ? 141 TYR   A CG  1 
ATOM   1015 C  CD1 . TYR   A 1 125 ? -68.313 19.163  -46.886 1.00 56.26  ? 141 TYR   A CD1 1 
ATOM   1016 C  CD2 . TYR   A 1 125 ? -66.713 20.438  -45.673 1.00 52.83  ? 141 TYR   A CD2 1 
ATOM   1017 C  CE1 . TYR   A 1 125 ? -68.192 20.032  -47.967 1.00 59.41  ? 141 TYR   A CE1 1 
ATOM   1018 C  CE2 . TYR   A 1 125 ? -66.575 21.301  -46.738 1.00 57.52  ? 141 TYR   A CE2 1 
ATOM   1019 C  CZ  . TYR   A 1 125 ? -67.316 21.096  -47.886 1.00 57.93  ? 141 TYR   A CZ  1 
ATOM   1020 O  OH  . TYR   A 1 125 ? -67.211 21.953  -48.961 1.00 69.28  ? 141 TYR   A OH  1 
ATOM   1021 N  N   . GLY   A 1 126 ? -69.509 17.657  -41.654 1.00 58.28  ? 142 GLY   A N   1 
ATOM   1022 C  CA  . GLY   A 1 126 ? -70.035 16.650  -40.748 1.00 60.17  ? 142 GLY   A CA  1 
ATOM   1023 C  C   . GLY   A 1 126 ? -68.930 15.942  -39.981 1.00 60.83  ? 142 GLY   A C   1 
ATOM   1024 O  O   . GLY   A 1 126 ? -67.740 16.148  -40.213 1.00 65.71  ? 142 GLY   A O   1 
ATOM   1025 N  N   . ASP   A 1 127 ? -69.342 15.079  -39.059 1.00 66.25  ? 143 ASP   A N   1 
ATOM   1026 C  CA  . ASP   A 1 127 ? -68.399 14.328  -38.228 1.00 73.17  ? 143 ASP   A CA  1 
ATOM   1027 C  C   . ASP   A 1 127 ? -68.665 12.831  -38.377 1.00 75.66  ? 143 ASP   A C   1 
ATOM   1028 O  O   . ASP   A 1 127 ? -69.155 12.180  -37.454 1.00 88.28  ? 143 ASP   A O   1 
ATOM   1029 C  CB  . ASP   A 1 127 ? -68.465 14.778  -36.737 1.00 75.14  ? 143 ASP   A CB  1 
ATOM   1030 C  CG  . ASP   A 1 127 ? -69.869 14.756  -36.169 1.00 83.78  ? 143 ASP   A CG  1 
ATOM   1031 O  OD1 . ASP   A 1 127 ? -70.827 14.507  -36.938 1.00 92.28  ? 143 ASP   A OD1 1 
ATOM   1032 O  OD2 . ASP   A 1 127 ? -70.010 14.989  -34.946 1.00 89.97  ? 143 ASP   A OD2 1 
ATOM   1033 N  N   . ASP   A 1 128 ? -68.320 12.288  -39.523 1.00 70.85  ? 144 ASP   A N   1 
ATOM   1034 C  CA  . ASP   A 1 128 ? -68.395 10.851  -39.717 1.00 78.37  ? 144 ASP   A CA  1 
ATOM   1035 C  C   . ASP   A 1 128 ? -67.077 10.201  -39.319 1.00 84.07  ? 144 ASP   A C   1 
ATOM   1036 O  O   . ASP   A 1 128 ? -66.034 10.863  -39.291 1.00 77.36  ? 144 ASP   A O   1 
ATOM   1037 C  CB  . ASP   A 1 128 ? -68.707 10.533  -41.175 1.00 76.25  ? 144 ASP   A CB  1 
ATOM   1038 C  CG  . ASP   A 1 128 ? -67.631 11.029  -42.115 1.00 80.29  ? 144 ASP   A CG  1 
ATOM   1039 O  OD1 . ASP   A 1 128 ? -67.549 12.258  -42.320 1.00 80.71  ? 144 ASP   A OD1 1 
ATOM   1040 O  OD2 . ASP   A 1 128 ? -66.859 10.195  -42.640 1.00 83.33  ? 144 ASP   A OD2 1 
ATOM   1041 N  N   . PRO   A 1 129 ? -67.090 8.897   -39.005 1.00 87.28  ? 145 PRO   A N   1 
ATOM   1042 C  CA  . PRO   A 1 129 ? -65.849 8.234   -38.566 1.00 84.39  ? 145 PRO   A CA  1 
ATOM   1043 C  C   . PRO   A 1 129 ? -64.684 8.324   -39.551 1.00 84.81  ? 145 PRO   A C   1 
ATOM   1044 O  O   . PRO   A 1 129 ? -63.526 8.349   -39.103 1.00 84.13  ? 145 PRO   A O   1 
ATOM   1045 C  CB  . PRO   A 1 129 ? -66.302 6.785   -38.352 1.00 83.68  ? 145 PRO   A CB  1 
ATOM   1046 C  CG  . PRO   A 1 129 ? -67.723 6.924   -37.925 1.00 87.27  ? 145 PRO   A CG  1 
ATOM   1047 C  CD  . PRO   A 1 129 ? -68.275 8.052   -38.757 1.00 85.19  ? 145 PRO   A CD  1 
ATOM   1048 N  N   . VAL   A 1 130 ? -64.937 8.383   -40.863 1.00 72.21  ? 146 VAL   A N   1 
ATOM   1049 C  CA  . VAL   A 1 130 ? -63.834 8.483   -41.822 1.00 75.24  ? 146 VAL   A CA  1 
ATOM   1050 C  C   . VAL   A 1 130 ? -63.184 9.863   -41.760 1.00 75.90  ? 146 VAL   A C   1 
ATOM   1051 O  O   . VAL   A 1 130 ? -61.952 9.986   -41.735 1.00 73.59  ? 146 VAL   A O   1 
ATOM   1052 C  CB  . VAL   A 1 130 ? -64.318 8.149   -43.244 1.00 81.48  ? 146 VAL   A CB  1 
ATOM   1053 C  CG1 . VAL   A 1 130 ? -63.231 8.482   -44.289 1.00 73.37  ? 146 VAL   A CG1 1 
ATOM   1054 C  CG2 . VAL   A 1 130 ? -64.701 6.687   -43.324 1.00 79.18  ? 146 VAL   A CG2 1 
ATOM   1055 N  N   . SER   A 1 131 ? -63.993 10.925  -41.752 1.00 72.52  ? 147 SER   A N   1 
ATOM   1056 C  CA  . SER   A 1 131 ? -63.445 12.258  -41.507 1.00 72.43  ? 147 SER   A CA  1 
ATOM   1057 C  C   . SER   A 1 131 ? -62.658 12.311  -40.194 1.00 62.93  ? 147 SER   A C   1 
ATOM   1058 O  O   . SER   A 1 131 ? -61.568 12.893  -40.139 1.00 59.31  ? 147 SER   A O   1 
ATOM   1059 C  CB  . SER   A 1 131 ? -64.572 13.292  -41.493 1.00 69.26  ? 147 SER   A CB  1 
ATOM   1060 O  OG  . SER   A 1 131 ? -65.325 13.235  -42.693 1.00 75.99  ? 147 SER   A OG  1 
ATOM   1061 N  N   . ASN   A 1 132 ? -63.201 11.708  -39.130 1.00 62.29  ? 148 ASN   A N   1 
ATOM   1062 C  CA  . ASN   A 1 132 ? -62.530 11.723  -37.836 1.00 61.80  ? 148 ASN   A CA  1 
ATOM   1063 C  C   . ASN   A 1 132 ? -61.161 11.058  -37.908 1.00 55.69  ? 148 ASN   A C   1 
ATOM   1064 O  O   . ASN   A 1 132 ? -60.196 11.560  -37.323 1.00 49.14  ? 148 ASN   A O   1 
ATOM   1065 C  CB  . ASN   A 1 132 ? -63.407 11.042  -36.775 1.00 56.81  ? 148 ASN   A CB  1 
ATOM   1066 C  CG  . ASN   A 1 132 ? -62.659 10.799  -35.469 1.00 70.35  ? 148 ASN   A CG  1 
ATOM   1067 O  OD1 . ASN   A 1 132 ? -62.486 11.711  -34.644 1.00 69.74  ? 148 ASN   A OD1 1 
ATOM   1068 N  ND2 . ASN   A 1 132 ? -62.198 9.556   -35.273 1.00 72.80  ? 148 ASN   A ND2 1 
ATOM   1069 N  N   . GLN   A 1 133 ? -61.058 9.925   -38.614 1.00 57.01  ? 149 GLN   A N   1 
ATOM   1070 C  CA  . GLN   A 1 133 ? -59.781 9.229   -38.717 1.00 62.05  ? 149 GLN   A CA  1 
ATOM   1071 C  C   . GLN   A 1 133 ? -58.743 10.076  -39.442 1.00 56.73  ? 149 GLN   A C   1 
ATOM   1072 O  O   . GLN   A 1 133 ? -57.556 10.050  -39.098 1.00 54.78  ? 149 GLN   A O   1 
ATOM   1073 C  CB  . GLN   A 1 133 ? -59.966 7.886   -39.431 1.00 66.22  ? 149 GLN   A CB  1 
ATOM   1074 C  CG  . GLN   A 1 133 ? -60.584 6.782   -38.570 1.00 74.82  ? 149 GLN   A CG  1 
ATOM   1075 C  CD  . GLN   A 1 133 ? -60.756 5.460   -39.328 1.00 91.07  ? 149 GLN   A CD  1 
ATOM   1076 O  OE1 . GLN   A 1 133 ? -61.341 5.415   -40.420 1.00 85.90  ? 149 GLN   A OE1 1 
ATOM   1077 N  NE2 . GLN   A 1 133 ? -60.238 4.379   -38.749 1.00 91.21  ? 149 GLN   A NE2 1 
ATOM   1078 N  N   . ASN   A 1 134 ? -59.165 10.831  -40.454 1.00 55.80  ? 150 ASN   A N   1 
ATOM   1079 C  CA  . ASN   A 1 134 ? -58.208 11.679  -41.154 1.00 53.97  ? 150 ASN   A CA  1 
ATOM   1080 C  C   . ASN   A 1 134 ? -57.790 12.868  -40.302 1.00 49.69  ? 150 ASN   A C   1 
ATOM   1081 O  O   . ASN   A 1 134 ? -56.619 13.255  -40.306 1.00 51.44  ? 150 ASN   A O   1 
ATOM   1082 C  CB  . ASN   A 1 134 ? -58.792 12.135  -42.484 1.00 55.74  ? 150 ASN   A CB  1 
ATOM   1083 C  CG  . ASN   A 1 134 ? -58.681 11.061  -43.549 1.00 63.16  ? 150 ASN   A CG  1 
ATOM   1084 O  OD1 . ASN   A 1 134 ? -57.616 10.862  -44.120 1.00 63.79  ? 150 ASN   A OD1 1 
ATOM   1085 N  ND2 . ASN   A 1 134 ? -59.778 10.357  -43.806 1.00 65.36  ? 150 ASN   A ND2 1 
ATOM   1086 N  N   . ILE   A 1 135 ? -58.727 13.450  -39.550 1.00 49.60  ? 151 ILE   A N   1 
ATOM   1087 C  CA  . ILE   A 1 135 ? -58.380 14.529  -38.628 1.00 47.40  ? 151 ILE   A CA  1 
ATOM   1088 C  C   . ILE   A 1 135 ? -57.394 14.038  -37.571 1.00 46.53  ? 151 ILE   A C   1 
ATOM   1089 O  O   . ILE   A 1 135 ? -56.387 14.701  -37.295 1.00 42.08  ? 151 ILE   A O   1 
ATOM   1090 C  CB  . ILE   A 1 135 ? -59.656 15.127  -38.004 1.00 46.30  ? 151 ILE   A CB  1 
ATOM   1091 C  CG1 . ILE   A 1 135 ? -60.478 15.799  -39.110 1.00 53.51  ? 151 ILE   A CG1 1 
ATOM   1092 C  CG2 . ILE   A 1 135 ? -59.307 16.140  -36.906 1.00 43.45  ? 151 ILE   A CG2 1 
ATOM   1093 C  CD1 . ILE   A 1 135 ? -61.908 16.225  -38.744 1.00 47.30  ? 151 ILE   A CD1 1 
ATOM   1094 N  N   . GLN   A 1 136 ? -57.666 12.868  -36.962 1.00 46.53  ? 152 GLN   A N   1 
ATOM   1095 C  CA  . GLN   A 1 136 ? -56.750 12.311  -35.962 1.00 47.13  ? 152 GLN   A CA  1 
ATOM   1096 C  C   . GLN   A 1 136 ? -55.359 12.129  -36.542 1.00 47.06  ? 152 GLN   A C   1 
ATOM   1097 O  O   . GLN   A 1 136 ? -54.354 12.494  -35.915 1.00 44.46  ? 152 GLN   A O   1 
ATOM   1098 C  CB  . GLN   A 1 136 ? -57.234 10.944  -35.444 1.00 46.42  ? 152 GLN   A CB  1 
ATOM   1099 C  CG  . GLN   A 1 136 ? -58.456 10.947  -34.560 1.00 53.75  ? 152 GLN   A CG  1 
ATOM   1100 C  CD  . GLN   A 1 136 ? -58.293 11.869  -33.374 1.00 49.07  ? 152 GLN   A CD  1 
ATOM   1101 O  OE1 . GLN   A 1 136 ? -58.989 12.876  -33.274 1.00 48.27  ? 152 GLN   A OE1 1 
ATOM   1102 N  NE2 . GLN   A 1 136 ? -57.361 11.541  -32.482 1.00 46.02  ? 152 GLN   A NE2 1 
ATOM   1103 N  N   . TYR   A 1 137 ? -55.286 11.490  -37.711 1.00 45.88  ? 153 TYR   A N   1 
ATOM   1104 C  CA  . TYR   A 1 137 ? -53.992 11.201  -38.310 1.00 48.41  ? 153 TYR   A CA  1 
ATOM   1105 C  C   . TYR   A 1 137 ? -53.236 12.494  -38.587 1.00 47.20  ? 153 TYR   A C   1 
ATOM   1106 O  O   . TYR   A 1 137 ? -52.059 12.628  -38.234 1.00 43.70  ? 153 TYR   A O   1 
ATOM   1107 C  CB  . TYR   A 1 137 ? -54.188 10.367  -39.586 1.00 49.53  ? 153 TYR   A CB  1 
ATOM   1108 C  CG  . TYR   A 1 137 ? -52.899 10.034  -40.310 1.00 58.77  ? 153 TYR   A CG  1 
ATOM   1109 C  CD1 . TYR   A 1 137 ? -52.078 9.002   -39.863 1.00 58.54  ? 153 TYR   A CD1 1 
ATOM   1110 C  CD2 . TYR   A 1 137 ? -52.506 10.744  -41.439 1.00 54.83  ? 153 TYR   A CD2 1 
ATOM   1111 C  CE1 . TYR   A 1 137 ? -50.908 8.690   -40.511 1.00 64.81  ? 153 TYR   A CE1 1 
ATOM   1112 C  CE2 . TYR   A 1 137 ? -51.329 10.435  -42.096 1.00 61.59  ? 153 TYR   A CE2 1 
ATOM   1113 C  CZ  . TYR   A 1 137 ? -50.538 9.407   -41.627 1.00 66.34  ? 153 TYR   A CZ  1 
ATOM   1114 O  OH  . TYR   A 1 137 ? -49.364 9.099   -42.257 1.00 66.92  ? 153 TYR   A OH  1 
ATOM   1115 N  N   . PHE   A 1 138 ? -53.916 13.484  -39.171 1.00 47.14  ? 154 PHE   A N   1 
ATOM   1116 C  CA  . PHE   A 1 138 ? -53.230 14.709  -39.556 1.00 46.35  ? 154 PHE   A CA  1 
ATOM   1117 C  C   . PHE   A 1 138 ? -52.813 15.528  -38.341 1.00 44.52  ? 154 PHE   A C   1 
ATOM   1118 O  O   . PHE   A 1 138 ? -51.666 15.983  -38.253 1.00 44.08  ? 154 PHE   A O   1 
ATOM   1119 C  CB  . PHE   A 1 138 ? -54.105 15.563  -40.472 1.00 46.11  ? 154 PHE   A CB  1 
ATOM   1120 C  CG  . PHE   A 1 138 ? -53.563 16.950  -40.655 1.00 48.39  ? 154 PHE   A CG  1 
ATOM   1121 C  CD1 . PHE   A 1 138 ? -52.452 17.170  -41.457 1.00 50.25  ? 154 PHE   A CD1 1 
ATOM   1122 C  CD2 . PHE   A 1 138 ? -54.129 18.028  -39.990 1.00 44.85  ? 154 PHE   A CD2 1 
ATOM   1123 C  CE1 . PHE   A 1 138 ? -51.924 18.442  -41.611 1.00 46.70  ? 154 PHE   A CE1 1 
ATOM   1124 C  CE2 . PHE   A 1 138 ? -53.602 19.296  -40.131 1.00 45.62  ? 154 PHE   A CE2 1 
ATOM   1125 C  CZ  . PHE   A 1 138 ? -52.491 19.503  -40.951 1.00 47.52  ? 154 PHE   A CZ  1 
ATOM   1126 N  N   . LEU   A 1 139 ? -53.739 15.755  -37.403 1.00 44.06  ? 155 LEU   A N   1 
ATOM   1127 C  CA  . LEU   A 1 139 ? -53.435 16.635  -36.275 1.00 43.07  ? 155 LEU   A CA  1 
ATOM   1128 C  C   . LEU   A 1 139 ? -52.406 16.018  -35.331 1.00 39.26  ? 155 LEU   A C   1 
ATOM   1129 O  O   . LEU   A 1 139 ? -51.532 16.730  -34.830 1.00 38.46  ? 155 LEU   A O   1 
ATOM   1130 C  CB  . LEU   A 1 139 ? -54.717 17.020  -35.527 1.00 46.39  ? 155 LEU   A CB  1 
ATOM   1131 C  CG  . LEU   A 1 139 ? -55.507 18.179  -36.182 1.00 45.64  ? 155 LEU   A CG  1 
ATOM   1132 C  CD1 . LEU   A 1 139 ? -56.708 18.600  -35.326 1.00 43.16  ? 155 LEU   A CD1 1 
ATOM   1133 C  CD2 . LEU   A 1 139 ? -54.598 19.397  -36.435 1.00 43.54  ? 155 LEU   A CD2 1 
ATOM   1134 N  N   . ASP   A 1 140 ? -52.460 14.704  -35.098 1.00 40.25  ? 156 ASP   A N   1 
ATOM   1135 C  CA  . ASP   A 1 140 ? -51.389 14.065  -34.330 1.00 41.63  ? 156 ASP   A CA  1 
ATOM   1136 C  C   . ASP   A 1 140 ? -50.023 14.359  -34.950 1.00 43.29  ? 156 ASP   A C   1 
ATOM   1137 O  O   . ASP   A 1 140 ? -49.067 14.701  -34.248 1.00 39.15  ? 156 ASP   A O   1 
ATOM   1138 C  CB  . ASP   A 1 140 ? -51.611 12.545  -34.230 1.00 41.06  ? 156 ASP   A CB  1 
ATOM   1139 C  CG  . ASP   A 1 140 ? -52.671 12.155  -33.179 1.00 42.16  ? 156 ASP   A CG  1 
ATOM   1140 O  OD1 . ASP   A 1 140 ? -53.229 13.038  -32.502 1.00 39.98  ? 156 ASP   A OD1 1 
ATOM   1141 O  OD2 . ASP   A 1 140 ? -52.963 10.954  -33.055 1.00 43.17  ? 156 ASP   A OD2 1 
ATOM   1142 N  N   . ARG   A 1 141 ? -49.913 14.232  -36.277 1.00 43.59  ? 157 ARG   A N   1 
ATOM   1143 C  CA  . ARG   A 1 141 ? -48.625 14.467  -36.923 1.00 47.76  ? 157 ARG   A CA  1 
ATOM   1144 C  C   . ARG   A 1 141 ? -48.285 15.952  -36.935 1.00 41.69  ? 157 ARG   A C   1 
ATOM   1145 O  O   . ARG   A 1 141 ? -47.154 16.336  -36.631 1.00 42.86  ? 157 ARG   A O   1 
ATOM   1146 C  CB  . ARG   A 1 141 ? -48.630 13.887  -38.341 1.00 42.66  ? 157 ARG   A CB  1 
ATOM   1147 C  CG  . ARG   A 1 141 ? -48.681 12.353  -38.349 1.00 49.31  ? 157 ARG   A CG  1 
ATOM   1148 C  CD  . ARG   A 1 141 ? -49.164 11.797  -39.703 1.00 49.21  ? 157 ARG   A CD  1 
ATOM   1149 N  NE  . ARG   A 1 141 ? -48.226 12.100  -40.774 1.00 49.45  ? 157 ARG   A NE  1 
ATOM   1150 C  CZ  . ARG   A 1 141 ? -47.105 11.423  -40.992 1.00 58.98  ? 157 ARG   A CZ  1 
ATOM   1151 N  NH1 . ARG   A 1 141 ? -46.746 10.414  -40.212 1.00 57.27  ? 157 ARG   A NH1 1 
ATOM   1152 N  NH2 . ARG   A 1 141 ? -46.320 11.774  -42.007 1.00 55.64  ? 157 ARG   A NH2 1 
ATOM   1153 N  N   . PHE   A 1 142 ? -49.265 16.802  -37.249 1.00 44.90  ? 158 PHE   A N   1 
ATOM   1154 C  CA  . PHE   A 1 142 ? -49.013 18.235  -37.294 1.00 41.42  ? 158 PHE   A CA  1 
ATOM   1155 C  C   . PHE   A 1 142 ? -48.588 18.775  -35.932 1.00 44.26  ? 158 PHE   A C   1 
ATOM   1156 O  O   . PHE   A 1 142 ? -47.675 19.606  -35.840 1.00 42.93  ? 158 PHE   A O   1 
ATOM   1157 C  CB  . PHE   A 1 142 ? -50.267 18.974  -37.797 1.00 43.69  ? 158 PHE   A CB  1 
ATOM   1158 C  CG  . PHE   A 1 142 ? -50.146 20.461  -37.689 1.00 46.07  ? 158 PHE   A CG  1 
ATOM   1159 C  CD1 . PHE   A 1 142 ? -49.475 21.179  -38.665 1.00 44.97  ? 158 PHE   A CD1 1 
ATOM   1160 C  CD2 . PHE   A 1 142 ? -50.642 21.137  -36.574 1.00 43.76  ? 158 PHE   A CD2 1 
ATOM   1161 C  CE1 . PHE   A 1 142 ? -49.340 22.555  -38.562 1.00 49.60  ? 158 PHE   A CE1 1 
ATOM   1162 C  CE2 . PHE   A 1 142 ? -50.498 22.498  -36.452 1.00 47.29  ? 158 PHE   A CE2 1 
ATOM   1163 C  CZ  . PHE   A 1 142 ? -49.846 23.217  -37.451 1.00 49.06  ? 158 PHE   A CZ  1 
ATOM   1164 N  N   . TYR   A 1 143 ? -49.236 18.319  -34.855 1.00 43.11  ? 159 TYR   A N   1 
ATOM   1165 C  CA  . TYR   A 1 143 ? -48.891 18.827  -33.532 1.00 39.17  ? 159 TYR   A CA  1 
ATOM   1166 C  C   . TYR   A 1 143 ? -47.559 18.264  -33.044 1.00 40.09  ? 159 TYR   A C   1 
ATOM   1167 O  O   . TYR   A 1 143 ? -46.793 18.969  -32.377 1.00 43.26  ? 159 TYR   A O   1 
ATOM   1168 C  CB  . TYR   A 1 143 ? -50.008 18.507  -32.534 1.00 36.14  ? 159 TYR   A CB  1 
ATOM   1169 C  CG  . TYR   A 1 143 ? -51.194 19.440  -32.630 1.00 41.44  ? 159 TYR   A CG  1 
ATOM   1170 C  CD1 . TYR   A 1 143 ? -51.014 20.789  -32.941 1.00 45.14  ? 159 TYR   A CD1 1 
ATOM   1171 C  CD2 . TYR   A 1 143 ? -52.499 18.981  -32.415 1.00 38.16  ? 159 TYR   A CD2 1 
ATOM   1172 C  CE1 . TYR   A 1 143 ? -52.097 21.661  -33.057 1.00 43.05  ? 159 TYR   A CE1 1 
ATOM   1173 C  CE2 . TYR   A 1 143 ? -53.607 19.860  -32.507 1.00 41.42  ? 159 TYR   A CE2 1 
ATOM   1174 C  CZ  . TYR   A 1 143 ? -53.388 21.194  -32.837 1.00 43.67  ? 159 TYR   A CZ  1 
ATOM   1175 O  OH  . TYR   A 1 143 ? -54.444 22.073  -32.940 1.00 45.68  ? 159 TYR   A OH  1 
ATOM   1176 N  N   . LEU   A 1 144 ? -47.270 16.995  -33.329 1.00 40.74  ? 160 LEU   A N   1 
ATOM   1177 C  CA  . LEU   A 1 144 ? -45.965 16.457  -32.943 1.00 42.39  ? 160 LEU   A CA  1 
ATOM   1178 C  C   . LEU   A 1 144 ? -44.838 17.185  -33.669 1.00 41.31  ? 160 LEU   A C   1 
ATOM   1179 O  O   . LEU   A 1 144 ? -43.801 17.510  -33.073 1.00 41.98  ? 160 LEU   A O   1 
ATOM   1180 C  CB  . LEU   A 1 144 ? -45.893 14.959  -33.252 1.00 39.14  ? 160 LEU   A CB  1 
ATOM   1181 C  CG  . LEU   A 1 144 ? -46.152 13.999  -32.106 1.00 46.53  ? 160 LEU   A CG  1 
ATOM   1182 C  CD1 . LEU   A 1 144 ? -46.246 12.591  -32.679 1.00 44.45  ? 160 LEU   A CD1 1 
ATOM   1183 C  CD2 . LEU   A 1 144 ? -45.026 14.123  -31.050 1.00 39.22  ? 160 LEU   A CD2 1 
ATOM   1184 N  N   . SER   A 1 145 ? -45.026 17.440  -34.963 1.00 41.76  ? 161 SER   A N   1 
ATOM   1185 C  CA  . SER   A 1 145 ? -44.096 18.290  -35.702 1.00 46.03  ? 161 SER   A CA  1 
ATOM   1186 C  C   . SER   A 1 145 ? -43.904 19.628  -34.997 1.00 46.94  ? 161 SER   A C   1 
ATOM   1187 O  O   . SER   A 1 145 ? -42.770 20.076  -34.772 1.00 45.51  ? 161 SER   A O   1 
ATOM   1188 C  CB  . SER   A 1 145 ? -44.631 18.498  -37.126 1.00 42.23  ? 161 SER   A CB  1 
ATOM   1189 O  OG  . SER   A 1 145 ? -43.948 19.551  -37.790 1.00 47.70  ? 161 SER   A OG  1 
ATOM   1190 N  N   . ARG   A 1 146 ? -45.014 20.269  -34.613 1.00 43.72  ? 162 ARG   A N   1 
ATOM   1191 C  CA  . ARG   A 1 146 ? -44.926 21.577  -33.972 1.00 42.76  ? 162 ARG   A CA  1 
ATOM   1192 C  C   . ARG   A 1 146 ? -44.183 21.502  -32.641 1.00 43.46  ? 162 ARG   A C   1 
ATOM   1193 O  O   . ARG   A 1 146 ? -43.376 22.382  -32.330 1.00 41.44  ? 162 ARG   A O   1 
ATOM   1194 C  CB  . ARG   A 1 146 ? -46.323 22.165  -33.766 1.00 45.17  ? 162 ARG   A CB  1 
ATOM   1195 C  CG  . ARG   A 1 146 ? -46.302 23.435  -32.945 1.00 44.07  ? 162 ARG   A CG  1 
ATOM   1196 C  CD  . ARG   A 1 146 ? -47.673 24.004  -32.768 1.00 55.31  ? 162 ARG   A CD  1 
ATOM   1197 N  NE  . ARG   A 1 146 ? -47.847 24.543  -31.426 1.00 62.96  ? 162 ARG   A NE  1 
ATOM   1198 C  CZ  . ARG   A 1 146 ? -47.721 25.823  -31.128 1.00 61.57  ? 162 ARG   A CZ  1 
ATOM   1199 N  NH1 . ARG   A 1 146 ? -47.453 26.722  -32.063 1.00 60.45  ? 162 ARG   A NH1 1 
ATOM   1200 N  NH2 . ARG   A 1 146 ? -47.869 26.211  -29.864 1.00 66.63  ? 162 ARG   A NH2 1 
ATOM   1201 N  N   . ILE   A 1 147 ? -44.437 20.450  -31.853 1.00 41.43  ? 163 ILE   A N   1 
ATOM   1202 C  CA  . ILE   A 1 147 ? -43.728 20.249  -30.591 1.00 40.71  ? 163 ILE   A CA  1 
ATOM   1203 C  C   . ILE   A 1 147 ? -42.230 20.111  -30.832 1.00 42.20  ? 163 ILE   A C   1 
ATOM   1204 O  O   . ILE   A 1 147 ? -41.409 20.674  -30.095 1.00 41.18  ? 163 ILE   A O   1 
ATOM   1205 C  CB  . ILE   A 1 147 ? -44.292 19.013  -29.857 1.00 43.38  ? 163 ILE   A CB  1 
ATOM   1206 C  CG1 . ILE   A 1 147 ? -45.697 19.294  -29.298 1.00 41.78  ? 163 ILE   A CG1 1 
ATOM   1207 C  CG2 . ILE   A 1 147 ? -43.310 18.541  -28.744 1.00 39.07  ? 163 ILE   A CG2 1 
ATOM   1208 C  CD1 . ILE   A 1 147 ? -46.460 18.018  -28.911 1.00 44.06  ? 163 ILE   A CD1 1 
ATOM   1209 N  N   . SER   A 1 148 ? -41.850 19.351  -31.866 1.00 43.44  ? 164 SER   A N   1 
ATOM   1210 C  CA  . SER   A 1 148 ? -40.432 19.136  -32.151 1.00 42.94  ? 164 SER   A CA  1 
ATOM   1211 C  C   . SER   A 1 148 ? -39.752 20.425  -32.582 1.00 46.31  ? 164 SER   A C   1 
ATOM   1212 O  O   . SER   A 1 148 ? -38.579 20.663  -32.242 1.00 46.41  ? 164 SER   A O   1 
ATOM   1213 C  CB  . SER   A 1 148 ? -40.266 18.073  -33.245 1.00 41.70  ? 164 SER   A CB  1 
ATOM   1214 O  OG  . SER   A 1 148 ? -40.481 18.625  -34.541 1.00 45.73  ? 164 SER   A OG  1 
ATOM   1215 N  N   . ILE   A 1 149 ? -40.464 21.256  -33.356 1.00 43.92  ? 165 ILE   A N   1 
ATOM   1216 C  CA  . ILE   A 1 149 ? -39.890 22.518  -33.816 1.00 45.25  ? 165 ILE   A CA  1 
ATOM   1217 C  C   . ILE   A 1 149 ? -39.728 23.479  -32.649 1.00 46.76  ? 165 ILE   A C   1 
ATOM   1218 O  O   . ILE   A 1 149 ? -38.712 24.178  -32.536 1.00 49.87  ? 165 ILE   A O   1 
ATOM   1219 C  CB  . ILE   A 1 149 ? -40.755 23.120  -34.946 1.00 45.85  ? 165 ILE   A CB  1 
ATOM   1220 C  CG1 . ILE   A 1 149 ? -40.590 22.302  -36.237 1.00 44.79  ? 165 ILE   A CG1 1 
ATOM   1221 C  CG2 . ILE   A 1 149 ? -40.340 24.541  -35.216 1.00 43.00  ? 165 ILE   A CG2 1 
ATOM   1222 C  CD1 . ILE   A 1 149 ? -41.641 22.580  -37.324 1.00 43.47  ? 165 ILE   A CD1 1 
ATOM   1223 N  N   . ARG   A 1 150 ? -40.711 23.515  -31.745 1.00 48.86  ? 166 ARG   A N   1 
ATOM   1224 C  CA  . ARG   A 1 150 ? -40.575 24.362  -30.564 1.00 46.43  ? 166 ARG   A CA  1 
ATOM   1225 C  C   . ARG   A 1 150 ? -39.455 23.864  -29.660 1.00 44.00  ? 166 ARG   A C   1 
ATOM   1226 O  O   . ARG   A 1 150 ? -38.706 24.667  -29.100 1.00 50.71  ? 166 ARG   A O   1 
ATOM   1227 C  CB  . ARG   A 1 150 ? -41.903 24.418  -29.806 1.00 49.97  ? 166 ARG   A CB  1 
ATOM   1228 C  CG  . ARG   A 1 150 ? -43.031 24.862  -30.689 1.00 58.39  ? 166 ARG   A CG  1 
ATOM   1229 C  CD  . ARG   A 1 150 ? -44.342 24.988  -29.955 1.00 65.56  ? 166 ARG   A CD  1 
ATOM   1230 N  NE  . ARG   A 1 150 ? -44.596 26.389  -29.668 1.00 76.65  ? 166 ARG   A NE  1 
ATOM   1231 C  CZ  . ARG   A 1 150 ? -44.449 26.941  -28.476 1.00 79.05  ? 166 ARG   A CZ  1 
ATOM   1232 N  NH1 . ARG   A 1 150 ? -44.170 26.207  -27.408 1.00 74.84  ? 166 ARG   A NH1 1 
ATOM   1233 N  NH2 . ARG   A 1 150 ? -44.587 28.260  -28.356 1.00 74.45  ? 166 ARG   A NH2 1 
ATOM   1234 N  N   . MET   A 1 151 ? -39.324 22.545  -29.511 1.00 43.46  ? 167 MET   A N   1 
ATOM   1235 C  CA  . MET   A 1 151 ? -38.219 21.993  -28.726 1.00 43.45  ? 167 MET   A CA  1 
ATOM   1236 C  C   . MET   A 1 151 ? -36.872 22.499  -29.245 1.00 48.63  ? 167 MET   A C   1 
ATOM   1237 O  O   . MET   A 1 151 ? -36.044 23.003  -28.477 1.00 49.67  ? 167 MET   A O   1 
ATOM   1238 C  CB  . MET   A 1 151 ? -38.280 20.461  -28.749 1.00 41.02  ? 167 MET   A CB  1 
ATOM   1239 C  CG  . MET   A 1 151 ? -37.157 19.737  -27.970 1.00 44.48  ? 167 MET   A CG  1 
ATOM   1240 S  SD  . MET   A 1 151 ? -37.348 19.965  -26.186 1.00 51.20  ? 167 MET   A SD  1 
ATOM   1241 C  CE  . MET   A 1 151 ? -35.779 19.341  -25.559 1.00 47.19  ? 167 MET   A CE  1 
ATOM   1242 N  N   . LEU   A 1 152 ? -36.633 22.368  -30.557 1.00 48.98  ? 168 LEU   A N   1 
ATOM   1243 C  CA  . LEU   A 1 152 ? -35.365 22.831  -31.123 1.00 46.43  ? 168 LEU   A CA  1 
ATOM   1244 C  C   . LEU   A 1 152 ? -35.150 24.314  -30.864 1.00 48.73  ? 168 LEU   A C   1 
ATOM   1245 O  O   . LEU   A 1 152 ? -34.041 24.737  -30.515 1.00 52.77  ? 168 LEU   A O   1 
ATOM   1246 C  CB  . LEU   A 1 152 ? -35.318 22.566  -32.625 1.00 46.45  ? 168 LEU   A CB  1 
ATOM   1247 C  CG  . LEU   A 1 152 ? -35.205 21.133  -33.135 1.00 52.91  ? 168 LEU   A CG  1 
ATOM   1248 C  CD1 . LEU   A 1 152 ? -34.971 21.134  -34.637 1.00 49.37  ? 168 LEU   A CD1 1 
ATOM   1249 C  CD2 . LEU   A 1 152 ? -34.103 20.389  -32.432 1.00 50.42  ? 168 LEU   A CD2 1 
ATOM   1250 N  N   . ILE   A 1 153 ? -36.196 25.121  -31.045 1.00 50.54  ? 169 ILE   A N   1 
ATOM   1251 C  CA  . ILE   A 1 153 ? -36.064 26.562  -30.850 1.00 53.95  ? 169 ILE   A CA  1 
ATOM   1252 C  C   . ILE   A 1 153 ? -35.794 26.880  -29.388 1.00 54.77  ? 169 ILE   A C   1 
ATOM   1253 O  O   . ILE   A 1 153 ? -34.928 27.701  -29.070 1.00 57.54  ? 169 ILE   A O   1 
ATOM   1254 C  CB  . ILE   A 1 153 ? -37.323 27.285  -31.369 1.00 51.48  ? 169 ILE   A CB  1 
ATOM   1255 C  CG1 . ILE   A 1 153 ? -37.393 27.180  -32.891 1.00 50.92  ? 169 ILE   A CG1 1 
ATOM   1256 C  CG2 . ILE   A 1 153 ? -37.328 28.729  -30.944 1.00 54.57  ? 169 ILE   A CG2 1 
ATOM   1257 C  CD1 . ILE   A 1 153 ? -38.643 27.789  -33.491 1.00 53.98  ? 169 ILE   A CD1 1 
ATOM   1258 N  N   . ASN   A 1 154 ? -36.530 26.236  -28.477 1.00 52.66  ? 170 ASN   A N   1 
ATOM   1259 C  CA  . ASN   A 1 154 ? -36.323 26.459  -27.050 1.00 57.01  ? 170 ASN   A CA  1 
ATOM   1260 C  C   . ASN   A 1 154 ? -34.905 26.103  -26.629 1.00 55.86  ? 170 ASN   A C   1 
ATOM   1261 O  O   . ASN   A 1 154 ? -34.288 26.832  -25.851 1.00 54.89  ? 170 ASN   A O   1 
ATOM   1262 C  CB  . ASN   A 1 154 ? -37.323 25.636  -26.232 1.00 57.84  ? 170 ASN   A CB  1 
ATOM   1263 C  CG  . ASN   A 1 154 ? -38.745 26.156  -26.350 1.00 62.09  ? 170 ASN   A CG  1 
ATOM   1264 O  OD1 . ASN   A 1 154 ? -38.966 27.331  -26.655 1.00 67.17  ? 170 ASN   A OD1 1 
ATOM   1265 N  ND2 . ASN   A 1 154 ? -39.720 25.280  -26.090 1.00 55.78  ? 170 ASN   A ND2 1 
ATOM   1266 N  N   . GLN   A 1 155 ? -34.380 24.972  -27.112 1.00 52.23  ? 171 GLN   A N   1 
ATOM   1267 C  CA  . GLN   A 1 155 ? -33.037 24.568  -26.712 1.00 55.19  ? 171 GLN   A CA  1 
ATOM   1268 C  C   . GLN   A 1 155 ? -31.992 25.570  -27.178 1.00 56.46  ? 171 GLN   A C   1 
ATOM   1269 O  O   . GLN   A 1 155 ? -31.007 25.810  -26.474 1.00 61.42  ? 171 GLN   A O   1 
ATOM   1270 C  CB  . GLN   A 1 155 ? -32.712 23.177  -27.248 1.00 52.14  ? 171 GLN   A CB  1 
ATOM   1271 C  CG  . GLN   A 1 155 ? -33.402 22.064  -26.491 1.00 50.27  ? 171 GLN   A CG  1 
ATOM   1272 C  CD  . GLN   A 1 155 ? -33.282 22.235  -24.996 1.00 54.68  ? 171 GLN   A CD  1 
ATOM   1273 O  OE1 . GLN   A 1 155 ? -34.233 22.634  -24.322 1.00 52.62  ? 171 GLN   A OE1 1 
ATOM   1274 N  NE2 . GLN   A 1 155 ? -32.104 21.947  -24.469 1.00 54.42  ? 171 GLN   A NE2 1 
ATOM   1275 N  N   . HIS   A 1 156 ? -32.193 26.183  -28.340 1.00 53.72  ? 172 HIS   A N   1 
ATOM   1276 C  CA  . HIS   A 1 156 ? -31.225 27.172  -28.796 1.00 57.76  ? 172 HIS   A CA  1 
ATOM   1277 C  C   . HIS   A 1 156 ? -31.379 28.494  -28.047 1.00 64.70  ? 172 HIS   A C   1 
ATOM   1278 O  O   . HIS   A 1 156 ? -30.393 29.052  -27.541 1.00 63.85  ? 172 HIS   A O   1 
ATOM   1279 C  CB  . HIS   A 1 156 ? -31.362 27.384  -30.301 1.00 58.91  ? 172 HIS   A CB  1 
ATOM   1280 C  CG  . HIS   A 1 156 ? -30.269 28.221  -30.888 1.00 63.79  ? 172 HIS   A CG  1 
ATOM   1281 N  ND1 . HIS   A 1 156 ? -29.100 27.679  -31.377 1.00 65.13  ? 172 HIS   A ND1 1 
ATOM   1282 C  CD2 . HIS   A 1 156 ? -30.157 29.562  -31.040 1.00 64.61  ? 172 HIS   A CD2 1 
ATOM   1283 C  CE1 . HIS   A 1 156 ? -28.320 28.651  -31.819 1.00 69.97  ? 172 HIS   A CE1 1 
ATOM   1284 N  NE2 . HIS   A 1 156 ? -28.937 29.803  -31.625 1.00 67.48  ? 172 HIS   A NE2 1 
ATOM   1285 N  N   . THR   A 1 157 ? -32.607 29.020  -27.965 1.00 61.21  ? 173 THR   A N   1 
ATOM   1286 C  CA  . THR   A 1 157 ? -32.774 30.371  -27.428 1.00 62.19  ? 173 THR   A CA  1 
ATOM   1287 C  C   . THR   A 1 157 ? -32.562 30.418  -25.921 1.00 66.01  ? 173 THR   A C   1 
ATOM   1288 O  O   . THR   A 1 157 ? -32.119 31.444  -25.395 1.00 68.57  ? 173 THR   A O   1 
ATOM   1289 C  CB  . THR   A 1 157 ? -34.156 30.915  -27.775 1.00 63.92  ? 173 THR   A CB  1 
ATOM   1290 O  OG1 . THR   A 1 157 ? -35.148 30.048  -27.221 1.00 63.77  ? 173 THR   A OG1 1 
ATOM   1291 C  CG2 . THR   A 1 157 ? -34.336 31.003  -29.291 1.00 59.90  ? 173 THR   A CG2 1 
ATOM   1292 N  N   . LEU   A 1 158 ? -32.872 29.324  -25.215 1.00 63.08  ? 174 LEU   A N   1 
ATOM   1293 C  CA  . LEU   A 1 158 ? -32.687 29.293  -23.768 1.00 65.53  ? 174 LEU   A CA  1 
ATOM   1294 C  C   . LEU   A 1 158 ? -31.217 29.172  -23.384 1.00 68.91  ? 174 LEU   A C   1 
ATOM   1295 O  O   . LEU   A 1 158 ? -30.784 29.773  -22.392 1.00 72.02  ? 174 LEU   A O   1 
ATOM   1296 C  CB  . LEU   A 1 158 ? -33.487 28.140  -23.163 1.00 61.31  ? 174 LEU   A CB  1 
ATOM   1297 C  CG  . LEU   A 1 158 ? -35.002 28.317  -23.161 1.00 59.64  ? 174 LEU   A CG  1 
ATOM   1298 C  CD1 . LEU   A 1 158 ? -35.678 27.016  -22.775 1.00 58.13  ? 174 LEU   A CD1 1 
ATOM   1299 C  CD2 . LEU   A 1 158 ? -35.397 29.431  -22.208 1.00 62.20  ? 174 LEU   A CD2 1 
ATOM   1300 N  N   . ILE   A 1 159 ? -30.436 28.422  -24.154 1.00 68.91  ? 175 ILE   A N   1 
ATOM   1301 C  CA  . ILE   A 1 159 ? -29.050 28.133  -23.787 1.00 71.75  ? 175 ILE   A CA  1 
ATOM   1302 C  C   . ILE   A 1 159 ? -28.100 29.244  -24.226 1.00 77.91  ? 175 ILE   A C   1 
ATOM   1303 O  O   . ILE   A 1 159 ? -27.255 29.695  -23.445 1.00 77.81  ? 175 ILE   A O   1 
ATOM   1304 C  CB  . ILE   A 1 159 ? -28.642 26.769  -24.379 1.00 70.42  ? 175 ILE   A CB  1 
ATOM   1305 C  CG1 . ILE   A 1 159 ? -29.325 25.645  -23.594 1.00 62.52  ? 175 ILE   A CG1 1 
ATOM   1306 C  CG2 . ILE   A 1 159 ? -27.134 26.605  -24.358 1.00 71.56  ? 175 ILE   A CG2 1 
ATOM   1307 C  CD1 . ILE   A 1 159 ? -29.245 24.311  -24.237 1.00 60.53  ? 175 ILE   A CD1 1 
ATOM   1308 N  N   . PHE   A 1 160 ? -28.243 29.724  -25.454 1.00 75.70  ? 176 PHE   A N   1 
ATOM   1309 C  CA  . PHE   A 1 160 ? -27.348 30.745  -25.994 1.00 79.49  ? 176 PHE   A CA  1 
ATOM   1310 C  C   . PHE   A 1 160 ? -27.981 32.133  -25.878 1.00 85.93  ? 176 PHE   A C   1 
ATOM   1311 O  O   . PHE   A 1 160 ? -28.252 32.826  -26.863 1.00 84.58  ? 176 PHE   A O   1 
ATOM   1312 C  CB  . PHE   A 1 160 ? -26.979 30.389  -27.427 1.00 76.35  ? 176 PHE   A CB  1 
ATOM   1313 C  CG  . PHE   A 1 160 ? -26.481 28.977  -27.568 1.00 74.86  ? 176 PHE   A CG  1 
ATOM   1314 C  CD1 . PHE   A 1 160 ? -25.269 28.603  -27.015 1.00 82.14  ? 176 PHE   A CD1 1 
ATOM   1315 C  CD2 . PHE   A 1 160 ? -27.231 28.024  -28.228 1.00 69.94  ? 176 PHE   A CD2 1 
ATOM   1316 C  CE1 . PHE   A 1 160 ? -24.813 27.308  -27.132 1.00 85.09  ? 176 PHE   A CE1 1 
ATOM   1317 C  CE2 . PHE   A 1 160 ? -26.783 26.722  -28.347 1.00 71.01  ? 176 PHE   A CE2 1 
ATOM   1318 C  CZ  . PHE   A 1 160 ? -25.574 26.364  -27.801 1.00 78.63  ? 176 PHE   A CZ  1 
ATOM   1319 N  N   . ASP   A 1 161 ? -28.188 32.540  -24.622 1.00 96.29  ? 177 ASP   A N   1 
ATOM   1320 C  CA  . ASP   A 1 161 ? -28.804 33.819  -24.281 1.00 95.03  ? 177 ASP   A CA  1 
ATOM   1321 C  C   . ASP   A 1 161 ? -27.777 34.942  -24.182 1.00 99.05  ? 177 ASP   A C   1 
ATOM   1322 O  O   . ASP   A 1 161 ? -27.991 36.028  -24.728 1.00 105.26 ? 177 ASP   A O   1 
ATOM   1323 C  CB  . ASP   A 1 161 ? -29.581 33.693  -22.964 1.00 95.91  ? 177 ASP   A CB  1 
ATOM   1324 C  CG  . ASP   A 1 161 ? -28.787 32.981  -21.875 1.00 98.26  ? 177 ASP   A CG  1 
ATOM   1325 O  OD1 . ASP   A 1 161 ? -27.605 33.322  -21.664 1.00 102.42 ? 177 ASP   A OD1 1 
ATOM   1326 O  OD2 . ASP   A 1 161 ? -29.352 32.085  -21.218 1.00 98.14  ? 177 ASP   A OD2 1 
ATOM   1327 N  N   . GLY   A 1 162 ? -26.667 34.700  -23.489 1.00 104.56 ? 178 GLY   A N   1 
ATOM   1328 C  CA  . GLY   A 1 162 ? -25.625 35.698  -23.329 1.00 103.09 ? 178 GLY   A CA  1 
ATOM   1329 C  C   . GLY   A 1 162 ? -24.923 35.621  -21.987 1.00 105.91 ? 178 GLY   A C   1 
ATOM   1330 O  O   . GLY   A 1 162 ? -24.255 34.635  -21.679 1.00 105.99 ? 178 GLY   A O   1 
ATOM   1331 N  N   . PRO   A 1 169 ? -24.286 25.205  -15.068 1.00 122.49 ? 185 PRO   A N   1 
ATOM   1332 C  CA  . PRO   A 1 169 ? -25.724 25.138  -15.362 1.00 115.73 ? 185 PRO   A CA  1 
ATOM   1333 C  C   . PRO   A 1 169 ? -26.333 23.749  -15.118 1.00 106.10 ? 185 PRO   A C   1 
ATOM   1334 O  O   . PRO   A 1 169 ? -25.963 22.786  -15.791 1.00 106.47 ? 185 PRO   A O   1 
ATOM   1335 C  CB  . PRO   A 1 169 ? -25.784 25.513  -16.847 1.00 113.09 ? 185 PRO   A CB  1 
ATOM   1336 C  CG  . PRO   A 1 169 ? -24.512 26.367  -17.088 1.00 125.25 ? 185 PRO   A CG  1 
ATOM   1337 C  CD  . PRO   A 1 169 ? -23.619 26.249  -15.866 1.00 122.57 ? 185 PRO   A CD  1 
ATOM   1338 N  N   . LYS   A 1 170 ? -27.254 23.654  -14.153 1.00 87.96  ? 186 LYS   A N   1 
ATOM   1339 C  CA  . LYS   A 1 170 ? -27.907 22.380  -13.868 1.00 75.07  ? 186 LYS   A CA  1 
ATOM   1340 C  C   . LYS   A 1 170 ? -28.924 22.038  -14.955 1.00 71.61  ? 186 LYS   A C   1 
ATOM   1341 O  O   . LYS   A 1 170 ? -28.799 21.019  -15.643 1.00 69.51  ? 186 LYS   A O   1 
ATOM   1342 C  CB  . LYS   A 1 170 ? -28.554 22.428  -12.484 1.00 72.53  ? 186 LYS   A CB  1 
ATOM   1343 C  CG  . LYS   A 1 170 ? -27.525 22.557  -11.355 1.00 83.16  ? 186 LYS   A CG  1 
ATOM   1344 C  CD  . LYS   A 1 170 ? -28.162 22.670  -9.968  1.00 86.86  ? 186 LYS   A CD  1 
ATOM   1345 C  CE  . LYS   A 1 170 ? -28.565 24.108  -9.617  1.00 88.74  ? 186 LYS   A CE  1 
ATOM   1346 N  NZ  . LYS   A 1 170 ? -27.424 24.981  -9.184  1.00 98.79  ? 186 LYS   A NZ  1 
ATOM   1347 N  N   . HIS   A 1 171 ? -29.928 22.884  -15.144 1.00 64.02  ? 187 HIS   A N   1 
ATOM   1348 C  CA  . HIS   A 1 171 ? -30.827 22.690  -16.270 1.00 66.91  ? 187 HIS   A CA  1 
ATOM   1349 C  C   . HIS   A 1 171 ? -30.104 22.996  -17.575 1.00 63.37  ? 187 HIS   A C   1 
ATOM   1350 O  O   . HIS   A 1 171 ? -29.190 23.816  -17.622 1.00 65.38  ? 187 HIS   A O   1 
ATOM   1351 C  CB  . HIS   A 1 171 ? -32.061 23.564  -16.116 1.00 60.39  ? 187 HIS   A CB  1 
ATOM   1352 C  CG  . HIS   A 1 171 ? -32.959 23.116  -15.011 1.00 58.75  ? 187 HIS   A CG  1 
ATOM   1353 N  ND1 . HIS   A 1 171 ? -34.261 22.726  -15.222 1.00 54.18  ? 187 HIS   A ND1 1 
ATOM   1354 C  CD2 . HIS   A 1 171 ? -32.734 22.978  -13.682 1.00 59.22  ? 187 HIS   A CD2 1 
ATOM   1355 C  CE1 . HIS   A 1 171 ? -34.806 22.370  -14.072 1.00 56.42  ? 187 HIS   A CE1 1 
ATOM   1356 N  NE2 . HIS   A 1 171 ? -33.899 22.515  -13.122 1.00 62.25  ? 187 HIS   A NE2 1 
ATOM   1357 N  N   . ILE   A 1 172 ? -30.493 22.296  -18.633 1.00 60.31  ? 188 ILE   A N   1 
ATOM   1358 C  CA  . ILE   A 1 172 ? -29.892 22.461  -19.957 1.00 57.15  ? 188 ILE   A CA  1 
ATOM   1359 C  C   . ILE   A 1 172 ? -31.013 22.908  -20.886 1.00 55.97  ? 188 ILE   A C   1 
ATOM   1360 O  O   . ILE   A 1 172 ? -31.690 22.087  -21.512 1.00 50.49  ? 188 ILE   A O   1 
ATOM   1361 C  CB  . ILE   A 1 172 ? -29.219 21.182  -20.458 1.00 58.68  ? 188 ILE   A CB  1 
ATOM   1362 C  CG1 . ILE   A 1 172 ? -28.228 20.656  -19.411 1.00 61.19  ? 188 ILE   A CG1 1 
ATOM   1363 C  CG2 . ILE   A 1 172 ? -28.522 21.436  -21.803 1.00 57.63  ? 188 ILE   A CG2 1 
ATOM   1364 C  CD1 . ILE   A 1 172 ? -27.108 21.617  -19.106 1.00 65.36  ? 188 ILE   A CD1 1 
ATOM   1365 N  N   . GLY   A 1 173 ? -31.220 24.215  -20.975 1.00 51.41  ? 189 GLY   A N   1 
ATOM   1366 C  CA  . GLY   A 1 173 ? -32.380 24.707  -21.700 1.00 53.51  ? 189 GLY   A CA  1 
ATOM   1367 C  C   . GLY   A 1 173 ? -33.641 24.188  -21.030 1.00 52.63  ? 189 GLY   A C   1 
ATOM   1368 O  O   . GLY   A 1 173 ? -33.852 24.361  -19.826 1.00 55.15  ? 189 GLY   A O   1 
ATOM   1369 N  N   . SER   A 1 174 ? -34.494 23.516  -21.795 1.00 48.03  ? 190 SER   A N   1 
ATOM   1370 C  CA  . SER   A 1 174 ? -35.734 22.975  -21.245 1.00 46.56  ? 190 SER   A CA  1 
ATOM   1371 C  C   . SER   A 1 174 ? -35.574 21.571  -20.665 1.00 49.81  ? 190 SER   A C   1 
ATOM   1372 O  O   . SER   A 1 174 ? -36.560 20.990  -20.204 1.00 49.42  ? 190 SER   A O   1 
ATOM   1373 C  CB  . SER   A 1 174 ? -36.832 22.977  -22.319 1.00 49.59  ? 190 SER   A CB  1 
ATOM   1374 O  OG  . SER   A 1 174 ? -36.706 21.866  -23.191 1.00 49.13  ? 190 SER   A OG  1 
ATOM   1375 N  N   . ILE   A 1 175 ? -34.360 21.016  -20.646 1.00 50.62  ? 191 ILE   A N   1 
ATOM   1376 C  CA  . ILE   A 1 175 ? -34.124 19.670  -20.137 1.00 49.74  ? 191 ILE   A CA  1 
ATOM   1377 C  C   . ILE   A 1 175 ? -33.551 19.749  -18.728 1.00 55.35  ? 191 ILE   A C   1 
ATOM   1378 O  O   . ILE   A 1 175 ? -32.680 20.580  -18.439 1.00 53.65  ? 191 ILE   A O   1 
ATOM   1379 C  CB  . ILE   A 1 175 ? -33.180 18.889  -21.067 1.00 54.61  ? 191 ILE   A CB  1 
ATOM   1380 C  CG1 . ILE   A 1 175 ? -33.854 18.673  -22.426 1.00 50.71  ? 191 ILE   A CG1 1 
ATOM   1381 C  CG2 . ILE   A 1 175 ? -32.761 17.573  -20.425 1.00 46.20  ? 191 ILE   A CG2 1 
ATOM   1382 C  CD1 . ILE   A 1 175 ? -32.899 18.247  -23.488 1.00 50.02  ? 191 ILE   A CD1 1 
ATOM   1383 N  N   . ASP   A 1 176 ? -34.060 18.894  -17.841 1.00 53.67  ? 192 ASP   A N   1 
ATOM   1384 C  CA  . ASP   A 1 176 ? -33.491 18.720  -16.511 1.00 53.27  ? 192 ASP   A CA  1 
ATOM   1385 C  C   . ASP   A 1 176 ? -32.830 17.353  -16.478 1.00 46.83  ? 192 ASP   A C   1 
ATOM   1386 O  O   . ASP   A 1 176 ? -33.534 16.332  -16.527 1.00 49.56  ? 192 ASP   A O   1 
ATOM   1387 C  CB  . ASP   A 1 176 ? -34.577 18.826  -15.433 1.00 51.24  ? 192 ASP   A CB  1 
ATOM   1388 C  CG  . ASP   A 1 176 ? -34.012 18.826  -14.015 1.00 55.64  ? 192 ASP   A CG  1 
ATOM   1389 O  OD1 . ASP   A 1 176 ? -32.834 18.475  -13.827 1.00 51.31  ? 192 ASP   A OD1 1 
ATOM   1390 O  OD2 . ASP   A 1 176 ? -34.759 19.197  -13.085 1.00 53.03  ? 192 ASP   A OD2 1 
ATOM   1391 N  N   . PRO   A 1 177 ? -31.497 17.273  -16.398 1.00 54.24  ? 193 PRO   A N   1 
ATOM   1392 C  CA  . PRO   A 1 177 ? -30.832 15.960  -16.339 1.00 57.39  ? 193 PRO   A CA  1 
ATOM   1393 C  C   . PRO   A 1 177 ? -31.046 15.216  -15.023 1.00 56.62  ? 193 PRO   A C   1 
ATOM   1394 O  O   . PRO   A 1 177 ? -30.654 14.047  -14.921 1.00 56.64  ? 193 PRO   A O   1 
ATOM   1395 C  CB  . PRO   A 1 177 ? -29.353 16.311  -16.539 1.00 55.79  ? 193 PRO   A CB  1 
ATOM   1396 C  CG  . PRO   A 1 177 ? -29.243 17.718  -16.035 1.00 59.23  ? 193 PRO   A CG  1 
ATOM   1397 C  CD  . PRO   A 1 177 ? -30.534 18.386  -16.379 1.00 54.07  ? 193 PRO   A CD  1 
ATOM   1398 N  N   . ASN   A 1 178 ? -31.647 15.855  -14.025 1.00 54.56  ? 194 ASN   A N   1 
ATOM   1399 C  CA  . ASN   A 1 178 ? -31.901 15.278  -12.706 1.00 57.45  ? 194 ASN   A CA  1 
ATOM   1400 C  C   . ASN   A 1 178 ? -33.310 15.605  -12.260 1.00 57.64  ? 194 ASN   A C   1 
ATOM   1401 O  O   . ASN   A 1 178 ? -33.546 16.040  -11.135 1.00 53.29  ? 194 ASN   A O   1 
ATOM   1402 C  CB  . ASN   A 1 178 ? -30.909 15.793  -11.678 1.00 59.22  ? 194 ASN   A CB  1 
ATOM   1403 C  CG  . ASN   A 1 178 ? -29.551 15.209  -11.862 1.00 70.48  ? 194 ASN   A CG  1 
ATOM   1404 O  OD1 . ASN   A 1 178 ? -29.336 14.031  -11.569 1.00 86.08  ? 194 ASN   A OD1 1 
ATOM   1405 N  ND2 . ASN   A 1 178 ? -28.606 16.022  -12.335 1.00 77.71  ? 194 ASN   A ND2 1 
ATOM   1406 N  N   . CYS   A 1 179 ? -34.261 15.449  -13.176 1.00 52.52  ? 195 CYS   A N   1 
ATOM   1407 C  CA  . CYS   A 1 179 ? -35.652 15.739  -12.891 1.00 49.84  ? 195 CYS   A CA  1 
ATOM   1408 C  C   . CYS   A 1 179 ? -36.200 14.800  -11.821 1.00 52.43  ? 195 CYS   A C   1 
ATOM   1409 O  O   . CYS   A 1 179 ? -36.291 13.587  -12.030 1.00 49.44  ? 195 CYS   A O   1 
ATOM   1410 C  CB  . CYS   A 1 179 ? -36.471 15.610  -14.178 1.00 49.56  ? 195 CYS   A CB  1 
ATOM   1411 S  SG  . CYS   A 1 179 ? -38.204 15.864  -13.874 1.00 50.69  ? 195 CYS   A SG  1 
ATOM   1412 N  N   . ASN   A 1 180 ? -36.580 15.375  -10.688 1.00 48.91  ? 196 ASN   A N   1 
ATOM   1413 C  CA  . ASN   A 1 180 ? -37.231 14.668  -9.587  1.00 53.61  ? 196 ASN   A CA  1 
ATOM   1414 C  C   . ASN   A 1 180 ? -38.703 14.500  -9.932  1.00 51.70  ? 196 ASN   A C   1 
ATOM   1415 O  O   . ASN   A 1 180 ? -39.484 15.448  -9.833  1.00 47.79  ? 196 ASN   A O   1 
ATOM   1416 C  CB  . ASN   A 1 180 ? -37.061 15.462  -8.291  1.00 54.39  ? 196 ASN   A CB  1 
ATOM   1417 C  CG  . ASN   A 1 180 ? -37.559 14.709  -7.061  1.00 60.03  ? 196 ASN   A CG  1 
ATOM   1418 O  OD1 . ASN   A 1 180 ? -38.574 14.018  -7.095  1.00 57.57  ? 196 ASN   A OD1 1 
ATOM   1419 N  ND2 . ASN   A 1 180 ? -36.839 14.862  -5.957  1.00 63.55  ? 196 ASN   A ND2 1 
ATOM   1420 N  N   . VAL   A 1 181 ? -39.092 13.294  -10.320 1.00 47.86  ? 197 VAL   A N   1 
ATOM   1421 C  CA  . VAL   A 1 181 ? -40.418 13.122  -10.893 1.00 47.18  ? 197 VAL   A CA  1 
ATOM   1422 C  C   . VAL   A 1 181 ? -41.516 13.426  -9.873  1.00 47.50  ? 197 VAL   A C   1 
ATOM   1423 O  O   . VAL   A 1 181 ? -42.524 14.063  -10.211 1.00 46.19  ? 197 VAL   A O   1 
ATOM   1424 C  CB  . VAL   A 1 181 ? -40.543 11.712  -11.485 1.00 43.93  ? 197 VAL   A CB  1 
ATOM   1425 C  CG1 . VAL   A 1 181 ? -41.983 11.437  -11.857 1.00 40.86  ? 197 VAL   A CG1 1 
ATOM   1426 C  CG2 . VAL   A 1 181 ? -39.645 11.631  -12.718 1.00 49.02  ? 197 VAL   A CG2 1 
ATOM   1427 N  N   . SER   A 1 182 ? -41.337 13.007  -8.612  1.00 45.87  ? 198 SER   A N   1 
ATOM   1428 C  CA  . SER   A 1 182 ? -42.383 13.213  -7.614  1.00 48.61  ? 198 SER   A CA  1 
ATOM   1429 C  C   . SER   A 1 182 ? -42.600 14.686  -7.321  1.00 47.64  ? 198 SER   A C   1 
ATOM   1430 O  O   . SER   A 1 182 ? -43.713 15.095  -6.972  1.00 46.58  ? 198 SER   A O   1 
ATOM   1431 C  CB  . SER   A 1 182 ? -42.050 12.475  -6.317  1.00 51.67  ? 198 SER   A CB  1 
ATOM   1432 O  OG  . SER   A 1 182 ? -42.405 11.103  -6.433  1.00 61.62  ? 198 SER   A OG  1 
ATOM   1433 N  N   . GLU   A 1 183 ? -41.558 15.495  -7.449  1.00 50.76  ? 199 GLU   A N   1 
ATOM   1434 C  CA  A GLU   A 1 183 ? -41.717 16.930  -7.247  0.49 54.01  ? 199 GLU   A CA  1 
ATOM   1435 C  CA  B GLU   A 1 183 ? -41.722 16.925  -7.243  0.51 53.82  ? 199 GLU   A CA  1 
ATOM   1436 C  C   . GLU   A 1 183 ? -42.560 17.556  -8.355  1.00 52.06  ? 199 GLU   A C   1 
ATOM   1437 O  O   . GLU   A 1 183 ? -43.376 18.449  -8.094  1.00 50.12  ? 199 GLU   A O   1 
ATOM   1438 C  CB  A GLU   A 1 183 ? -40.347 17.604  -7.166  0.49 53.91  ? 199 GLU   A CB  1 
ATOM   1439 C  CB  B GLU   A 1 183 ? -40.351 17.590  -7.131  0.51 54.06  ? 199 GLU   A CB  1 
ATOM   1440 C  CG  A GLU   A 1 183 ? -40.424 19.120  -7.049  0.49 56.13  ? 199 GLU   A CG  1 
ATOM   1441 C  CG  B GLU   A 1 183 ? -39.890 17.711  -5.694  0.51 56.36  ? 199 GLU   A CG  1 
ATOM   1442 C  CD  A GLU   A 1 183 ? -41.139 19.576  -5.783  0.49 63.28  ? 199 GLU   A CD  1 
ATOM   1443 C  CD  B GLU   A 1 183 ? -40.914 18.451  -4.844  0.51 64.14  ? 199 GLU   A CD  1 
ATOM   1444 O  OE1 A GLU   A 1 183 ? -41.103 18.831  -4.772  0.49 65.55  ? 199 GLU   A OE1 1 
ATOM   1445 O  OE1 B GLU   A 1 183 ? -41.409 19.515  -5.297  0.51 64.91  ? 199 GLU   A OE1 1 
ATOM   1446 O  OE2 A GLU   A 1 183 ? -41.739 20.676  -5.800  0.49 61.79  ? 199 GLU   A OE2 1 
ATOM   1447 O  OE2 B GLU   A 1 183 ? -41.246 17.959  -3.741  0.51 59.16  ? 199 GLU   A OE2 1 
ATOM   1448 N  N   . VAL   A 1 184 ? -42.385 17.103  -9.595  1.00 47.80  ? 200 VAL   A N   1 
ATOM   1449 C  CA  . VAL   A 1 184 ? -43.211 17.648  -10.670 1.00 49.50  ? 200 VAL   A CA  1 
ATOM   1450 C  C   . VAL   A 1 184 ? -44.650 17.200  -10.493 1.00 46.41  ? 200 VAL   A C   1 
ATOM   1451 O  O   . VAL   A 1 184 ? -45.580 17.969  -10.749 1.00 46.54  ? 200 VAL   A O   1 
ATOM   1452 C  CB  . VAL   A 1 184 ? -42.651 17.250  -12.049 1.00 43.29  ? 200 VAL   A CB  1 
ATOM   1453 C  CG1 . VAL   A 1 184 ? -43.553 17.773  -13.169 1.00 42.75  ? 200 VAL   A CG1 1 
ATOM   1454 C  CG2 . VAL   A 1 184 ? -41.247 17.807  -12.209 1.00 43.48  ? 200 VAL   A CG2 1 
ATOM   1455 N  N   . VAL   A 1 185 ? -44.851 15.974  -10.004 1.00 45.93  ? 201 VAL   A N   1 
ATOM   1456 C  CA  . VAL   A 1 185 ? -46.193 15.499  -9.681  1.00 47.03  ? 201 VAL   A CA  1 
ATOM   1457 C  C   . VAL   A 1 185 ? -46.853 16.414  -8.653  1.00 45.70  ? 201 VAL   A C   1 
ATOM   1458 O  O   . VAL   A 1 185 ? -48.011 16.825  -8.811  1.00 40.81  ? 201 VAL   A O   1 
ATOM   1459 C  CB  . VAL   A 1 185 ? -46.135 14.046  -9.179  1.00 46.96  ? 201 VAL   A CB  1 
ATOM   1460 C  CG1 . VAL   A 1 185 ? -47.506 13.608  -8.682  1.00 44.25  ? 201 VAL   A CG1 1 
ATOM   1461 C  CG2 . VAL   A 1 185 ? -45.639 13.129  -10.290 1.00 40.64  ? 201 VAL   A CG2 1 
ATOM   1462 N  N   . LYS   A 1 186 ? -46.120 16.750  -7.586  1.00 45.47  ? 202 LYS   A N   1 
ATOM   1463 C  CA  . LYS   A 1 186 ? -46.692 17.599  -6.546  1.00 49.14  ? 202 LYS   A CA  1 
ATOM   1464 C  C   . LYS   A 1 186 ? -46.961 19.005  -7.062  1.00 49.07  ? 202 LYS   A C   1 
ATOM   1465 O  O   . LYS   A 1 186 ? -47.965 19.614  -6.684  1.00 49.38  ? 202 LYS   A O   1 
ATOM   1466 C  CB  . LYS   A 1 186 ? -45.774 17.667  -5.326  1.00 53.22  ? 202 LYS   A CB  1 
ATOM   1467 C  CG  . LYS   A 1 186 ? -45.630 16.368  -4.553  1.00 62.29  ? 202 LYS   A CG  1 
ATOM   1468 C  CD  . LYS   A 1 186 ? -44.599 16.536  -3.422  1.00 72.26  ? 202 LYS   A CD  1 
ATOM   1469 C  CE  . LYS   A 1 186 ? -44.264 15.212  -2.736  1.00 76.33  ? 202 LYS   A CE  1 
ATOM   1470 N  NZ  . LYS   A 1 186 ? -42.972 15.285  -1.991  1.00 79.43  ? 202 LYS   A NZ  1 
ATOM   1471 N  N   . ASP   A 1 187 ? -46.060 19.552  -7.891  1.00 50.06  ? 203 ASP   A N   1 
ATOM   1472 C  CA  . ASP   A 1 187 ? -46.279 20.887  -8.460  1.00 48.12  ? 203 ASP   A CA  1 
ATOM   1473 C  C   . ASP   A 1 187 ? -47.579 20.926  -9.247  1.00 46.34  ? 203 ASP   A C   1 
ATOM   1474 O  O   . ASP   A 1 187 ? -48.374 21.863  -9.121  1.00 47.51  ? 203 ASP   A O   1 
ATOM   1475 C  CB  . ASP   A 1 187 ? -45.141 21.273  -9.420  1.00 47.15  ? 203 ASP   A CB  1 
ATOM   1476 C  CG  . ASP   A 1 187 ? -43.844 21.615  -8.735  1.00 52.85  ? 203 ASP   A CG  1 
ATOM   1477 O  OD1 . ASP   A 1 187 ? -43.801 21.812  -7.509  1.00 51.77  ? 203 ASP   A OD1 1 
ATOM   1478 O  OD2 . ASP   A 1 187 ? -42.843 21.699  -9.479  1.00 54.09  ? 203 ASP   A OD2 1 
ATOM   1479 N  N   . ALA   A 1 188 ? -47.761 19.943  -10.129 1.00 42.76  ? 204 ALA   A N   1 
ATOM   1480 C  CA  . ALA   A 1 188 ? -48.971 19.871  -10.944 1.00 43.24  ? 204 ALA   A CA  1 
ATOM   1481 C  C   . ALA   A 1 188 ? -50.215 19.668  -10.090 1.00 46.21  ? 204 ALA   A C   1 
ATOM   1482 O  O   . ALA   A 1 188 ? -51.261 20.263  -10.369 1.00 43.74  ? 204 ALA   A O   1 
ATOM   1483 C  CB  . ALA   A 1 188 ? -48.849 18.739  -11.953 1.00 41.53  ? 204 ALA   A CB  1 
ATOM   1484 N  N   . TYR   A 1 189 ? -50.131 18.810  -9.065  1.00 42.91  ? 205 TYR   A N   1 
ATOM   1485 C  CA  . TYR   A 1 189 ? -51.265 18.607  -8.173  1.00 43.79  ? 205 TYR   A CA  1 
ATOM   1486 C  C   . TYR   A 1 189 ? -51.626 19.904  -7.469  1.00 49.15  ? 205 TYR   A C   1 
ATOM   1487 O  O   . TYR   A 1 189 ? -52.801 20.275  -7.391  1.00 45.55  ? 205 TYR   A O   1 
ATOM   1488 C  CB  . TYR   A 1 189 ? -50.952 17.512  -7.137  1.00 44.94  ? 205 TYR   A CB  1 
ATOM   1489 C  CG  . TYR   A 1 189 ? -51.925 17.533  -5.967  1.00 49.34  ? 205 TYR   A CG  1 
ATOM   1490 C  CD1 . TYR   A 1 189 ? -53.140 16.877  -6.057  1.00 47.37  ? 205 TYR   A CD1 1 
ATOM   1491 C  CD2 . TYR   A 1 189 ? -51.647 18.248  -4.793  1.00 50.04  ? 205 TYR   A CD2 1 
ATOM   1492 C  CE1 . TYR   A 1 189 ? -54.047 16.904  -5.023  1.00 45.94  ? 205 TYR   A CE1 1 
ATOM   1493 C  CE2 . TYR   A 1 189 ? -52.561 18.287  -3.739  1.00 51.15  ? 205 TYR   A CE2 1 
ATOM   1494 C  CZ  . TYR   A 1 189 ? -53.768 17.605  -3.875  1.00 50.71  ? 205 TYR   A CZ  1 
ATOM   1495 O  OH  . TYR   A 1 189 ? -54.715 17.611  -2.877  1.00 48.44  ? 205 TYR   A OH  1 
ATOM   1496 N  N   . ASP   A 1 190 ? -50.616 20.601  -6.941  1.00 47.45  ? 206 ASP   A N   1 
ATOM   1497 C  CA  . ASP   A 1 190 ? -50.858 21.832  -6.192  1.00 48.06  ? 206 ASP   A CA  1 
ATOM   1498 C  C   . ASP   A 1 190 ? -51.564 22.870  -7.055  1.00 49.04  ? 206 ASP   A C   1 
ATOM   1499 O  O   . ASP   A 1 190 ? -52.477 23.560  -6.589  1.00 47.17  ? 206 ASP   A O   1 
ATOM   1500 C  CB  . ASP   A 1 190 ? -49.537 22.393  -5.663  1.00 45.13  ? 206 ASP   A CB  1 
ATOM   1501 C  CG  . ASP   A 1 190 ? -48.983 21.599  -4.490  1.00 55.22  ? 206 ASP   A CG  1 
ATOM   1502 O  OD1 . ASP   A 1 190 ? -49.727 20.798  -3.894  1.00 55.44  ? 206 ASP   A OD1 1 
ATOM   1503 O  OD2 . ASP   A 1 190 ? -47.793 21.785  -4.150  1.00 60.16  ? 206 ASP   A OD2 1 
ATOM   1504 N  N   . MET   A 1 191 ? -51.158 22.995  -8.315  1.00 41.50  ? 207 MET   A N   1 
ATOM   1505 C  CA  . MET   A 1 191 ? -51.823 23.955  -9.185  1.00 47.98  ? 207 MET   A CA  1 
ATOM   1506 C  C   . MET   A 1 191 ? -53.270 23.563  -9.427  1.00 45.92  ? 207 MET   A C   1 
ATOM   1507 O  O   . MET   A 1 191 ? -54.169 24.408  -9.360  1.00 50.48  ? 207 MET   A O   1 
ATOM   1508 C  CB  . MET   A 1 191 ? -51.082 24.073  -10.510 1.00 42.56  ? 207 MET   A CB  1 
ATOM   1509 C  CG  . MET   A 1 191 ? -51.594 25.178  -11.390 1.00 45.66  ? 207 MET   A CG  1 
ATOM   1510 S  SD  . MET   A 1 191 ? -51.282 26.826  -10.675 1.00 53.56  ? 207 MET   A SD  1 
ATOM   1511 C  CE  . MET   A 1 191 ? -52.911 27.546  -10.846 1.00 50.42  ? 207 MET   A CE  1 
ATOM   1512 N  N   . ALA   A 1 192 ? -53.512 22.280  -9.713  1.00 45.43  ? 208 ALA   A N   1 
ATOM   1513 C  CA  . ALA   A 1 192 ? -54.872 21.821  -9.963  1.00 46.36  ? 208 ALA   A CA  1 
ATOM   1514 C  C   . ALA   A 1 192 ? -55.740 21.984  -8.725  1.00 48.49  ? 208 ALA   A C   1 
ATOM   1515 O  O   . ALA   A 1 192 ? -56.912 22.362  -8.826  1.00 47.10  ? 208 ALA   A O   1 
ATOM   1516 C  CB  . ALA   A 1 192 ? -54.856 20.365  -10.412 1.00 43.06  ? 208 ALA   A CB  1 
ATOM   1517 N  N   . LYS   A 1 193 ? -55.172 21.711  -7.544  1.00 48.08  ? 209 LYS   A N   1 
ATOM   1518 C  CA  . LYS   A 1 193 ? -55.904 21.892  -6.299  1.00 49.45  ? 209 LYS   A CA  1 
ATOM   1519 C  C   . LYS   A 1 193 ? -56.320 23.336  -6.123  1.00 52.04  ? 209 LYS   A C   1 
ATOM   1520 O  O   . LYS   A 1 193 ? -57.445 23.626  -5.698  1.00 56.85  ? 209 LYS   A O   1 
ATOM   1521 C  CB  . LYS   A 1 193 ? -55.051 21.458  -5.113  1.00 50.31  ? 209 LYS   A CB  1 
ATOM   1522 C  CG  . LYS   A 1 193 ? -55.640 21.900  -3.762  1.00 54.02  ? 209 LYS   A CG  1 
ATOM   1523 C  CD  . LYS   A 1 193 ? -54.886 21.269  -2.607  1.00 58.00  ? 209 LYS   A CD  1 
ATOM   1524 C  CE  . LYS   A 1 193 ? -55.297 21.864  -1.276  1.00 60.74  ? 209 LYS   A CE  1 
ATOM   1525 N  NZ  . LYS   A 1 193 ? -56.751 21.691  -1.045  1.00 69.87  ? 209 LYS   A NZ  1 
ATOM   1526 N  N   . LEU   A 1 194 ? -55.412 24.256  -6.433  1.00 52.24  ? 210 LEU   A N   1 
ATOM   1527 C  CA  . LEU   A 1 194 ? -55.715 25.677  -6.329  1.00 50.87  ? 210 LEU   A CA  1 
ATOM   1528 C  C   . LEU   A 1 194 ? -56.930 26.039  -7.183  1.00 56.77  ? 210 LEU   A C   1 
ATOM   1529 O  O   . LEU   A 1 194 ? -57.843 26.724  -6.721  1.00 54.44  ? 210 LEU   A O   1 
ATOM   1530 C  CB  . LEU   A 1 194 ? -54.477 26.468  -6.745  1.00 51.01  ? 210 LEU   A CB  1 
ATOM   1531 C  CG  . LEU   A 1 194 ? -54.324 27.930  -6.376  1.00 67.50  ? 210 LEU   A CG  1 
ATOM   1532 C  CD1 . LEU   A 1 194 ? -52.843 28.198  -6.202  1.00 68.28  ? 210 LEU   A CD1 1 
ATOM   1533 C  CD2 . LEU   A 1 194 ? -54.903 28.793  -7.477  1.00 69.83  ? 210 LEU   A CD2 1 
ATOM   1534 N  N   . LEU   A 1 195 ? -56.980 25.537  -8.424  1.00 55.02  ? 211 LEU   A N   1 
ATOM   1535 C  CA  . LEU   A 1 195 ? -58.138 25.792  -9.283  1.00 55.64  ? 211 LEU   A CA  1 
ATOM   1536 C  C   . LEU   A 1 195 ? -59.383 25.054  -8.783  1.00 56.77  ? 211 LEU   A C   1 
ATOM   1537 O  O   . LEU   A 1 195 ? -60.493 25.604  -8.788  1.00 55.88  ? 211 LEU   A O   1 
ATOM   1538 C  CB  . LEU   A 1 195 ? -57.815 25.378  -10.725 1.00 50.03  ? 211 LEU   A CB  1 
ATOM   1539 C  CG  . LEU   A 1 195 ? -56.671 26.136  -11.420 1.00 57.60  ? 211 LEU   A CG  1 
ATOM   1540 C  CD1 . LEU   A 1 195 ? -56.332 25.533  -12.782 1.00 49.26  ? 211 LEU   A CD1 1 
ATOM   1541 C  CD2 . LEU   A 1 195 ? -57.037 27.616  -11.567 1.00 57.66  ? 211 LEU   A CD2 1 
ATOM   1542 N  N   . CYS   A 1 196 ? -59.216 23.806  -8.352  1.00 51.20  ? 212 CYS   A N   1 
ATOM   1543 C  CA  . CYS   A 1 196 ? -60.363 22.997  -7.968  1.00 56.65  ? 212 CYS   A CA  1 
ATOM   1544 C  C   . CYS   A 1 196 ? -61.025 23.547  -6.711  1.00 55.18  ? 212 CYS   A C   1 
ATOM   1545 O  O   . CYS   A 1 196 ? -62.257 23.636  -6.648  1.00 55.48  ? 212 CYS   A O   1 
ATOM   1546 C  CB  . CYS   A 1 196 ? -59.918 21.533  -7.795  1.00 56.60  ? 212 CYS   A CB  1 
ATOM   1547 S  SG  . CYS   A 1 196 ? -61.246 20.332  -7.560  1.00 56.37  ? 212 CYS   A SG  1 
ATOM   1548 N  N   . ASP   A 1 197 ? -60.221 23.959  -5.716  1.00 53.43  ? 213 ASP   A N   1 
ATOM   1549 C  CA  . ASP   A 1 197 ? -60.759 24.638  -4.537  1.00 59.34  ? 213 ASP   A CA  1 
ATOM   1550 C  C   . ASP   A 1 197 ? -61.520 25.903  -4.913  1.00 61.02  ? 213 ASP   A C   1 
ATOM   1551 O  O   . ASP   A 1 197 ? -62.570 26.198  -4.331  1.00 62.13  ? 213 ASP   A O   1 
ATOM   1552 C  CB  . ASP   A 1 197 ? -59.633 24.992  -3.559  1.00 57.05  ? 213 ASP   A CB  1 
ATOM   1553 C  CG  . ASP   A 1 197 ? -59.127 23.792  -2.789  1.00 61.34  ? 213 ASP   A CG  1 
ATOM   1554 O  OD1 . ASP   A 1 197 ? -59.842 22.767  -2.745  1.00 60.65  ? 213 ASP   A OD1 1 
ATOM   1555 O  OD2 . ASP   A 1 197 ? -58.020 23.882  -2.213  1.00 62.12  ? 213 ASP   A OD2 1 
ATOM   1556 N  N   . LYS   A 1 198 ? -60.998 26.669  -5.876  1.00 61.33  ? 214 LYS   A N   1 
ATOM   1557 C  CA  . LYS   A 1 198 ? -61.625 27.930  -6.263  1.00 61.87  ? 214 LYS   A CA  1 
ATOM   1558 C  C   . LYS   A 1 198 ? -63.016 27.710  -6.843  1.00 61.85  ? 214 LYS   A C   1 
ATOM   1559 O  O   . LYS   A 1 198 ? -63.967 28.394  -6.468  1.00 65.55  ? 214 LYS   A O   1 
ATOM   1560 C  CB  . LYS   A 1 198 ? -60.747 28.661  -7.277  1.00 65.34  ? 214 LYS   A CB  1 
ATOM   1561 C  CG  . LYS   A 1 198 ? -59.967 29.829  -6.722  1.00 65.98  ? 214 LYS   A CG  1 
ATOM   1562 C  CD  . LYS   A 1 198 ? -60.602 31.156  -7.082  1.00 69.31  ? 214 LYS   A CD  1 
ATOM   1563 C  CE  . LYS   A 1 198 ? -60.070 32.255  -6.174  1.00 70.24  ? 214 LYS   A CE  1 
ATOM   1564 N  NZ  . LYS   A 1 198 ? -60.512 33.616  -6.588  1.00 81.37  ? 214 LYS   A NZ  1 
ATOM   1565 N  N   . TYR   A 1 199 ? -63.152 26.769  -7.771  1.00 64.10  ? 215 TYR   A N   1 
ATOM   1566 C  CA  . TYR   A 1 199 ? -64.401 26.645  -8.517  1.00 64.92  ? 215 TYR   A CA  1 
ATOM   1567 C  C   . TYR   A 1 199 ? -65.370 25.637  -7.916  1.00 59.75  ? 215 TYR   A C   1 
ATOM   1568 O  O   . TYR   A 1 199 ? -66.582 25.795  -8.081  1.00 63.26  ? 215 TYR   A O   1 
ATOM   1569 C  CB  . TYR   A 1 199 ? -64.092 26.298  -9.978  1.00 67.73  ? 215 TYR   A CB  1 
ATOM   1570 C  CG  . TYR   A 1 199 ? -63.200 27.359  -10.603 1.00 74.33  ? 215 TYR   A CG  1 
ATOM   1571 C  CD1 . TYR   A 1 199 ? -63.458 28.720  -10.396 1.00 72.62  ? 215 TYR   A CD1 1 
ATOM   1572 C  CD2 . TYR   A 1 199 ? -62.075 27.013  -11.334 1.00 73.18  ? 215 TYR   A CD2 1 
ATOM   1573 C  CE1 . TYR   A 1 199 ? -62.636 29.706  -10.939 1.00 77.32  ? 215 TYR   A CE1 1 
ATOM   1574 C  CE2 . TYR   A 1 199 ? -61.246 27.984  -11.882 1.00 76.22  ? 215 TYR   A CE2 1 
ATOM   1575 C  CZ  . TYR   A 1 199 ? -61.526 29.326  -11.685 1.00 81.26  ? 215 TYR   A CZ  1 
ATOM   1576 O  OH  . TYR   A 1 199 ? -60.692 30.283  -12.235 1.00 81.60  ? 215 TYR   A OH  1 
ATOM   1577 N  N   . TYR   A 1 200 ? -64.881 24.626  -7.203  1.00 62.12  ? 216 TYR   A N   1 
ATOM   1578 C  CA  . TYR   A 1 200 ? -65.740 23.595  -6.638  1.00 62.77  ? 216 TYR   A CA  1 
ATOM   1579 C  C   . TYR   A 1 200 ? -65.844 23.635  -5.127  1.00 62.76  ? 216 TYR   A C   1 
ATOM   1580 O  O   . TYR   A 1 200 ? -66.647 22.880  -4.568  1.00 70.14  ? 216 TYR   A O   1 
ATOM   1581 C  CB  . TYR   A 1 200 ? -65.247 22.198  -7.040  1.00 62.00  ? 216 TYR   A CB  1 
ATOM   1582 C  CG  . TYR   A 1 200 ? -65.498 21.842  -8.476  1.00 61.25  ? 216 TYR   A CG  1 
ATOM   1583 C  CD1 . TYR   A 1 200 ? -66.781 21.566  -8.925  1.00 62.50  ? 216 TYR   A CD1 1 
ATOM   1584 C  CD2 . TYR   A 1 200 ? -64.451 21.743  -9.375  1.00 63.30  ? 216 TYR   A CD2 1 
ATOM   1585 C  CE1 . TYR   A 1 200 ? -67.018 21.219  -10.235 1.00 65.12  ? 216 TYR   A CE1 1 
ATOM   1586 C  CE2 . TYR   A 1 200 ? -64.674 21.400  -10.688 1.00 66.81  ? 216 TYR   A CE2 1 
ATOM   1587 C  CZ  . TYR   A 1 200 ? -65.962 21.133  -11.115 1.00 68.68  ? 216 TYR   A CZ  1 
ATOM   1588 O  OH  . TYR   A 1 200 ? -66.198 20.788  -12.431 1.00 71.37  ? 216 TYR   A OH  1 
ATOM   1589 N  N   . MET   A 1 201 ? -65.050 24.471  -4.455  1.00 62.79  ? 217 MET   A N   1 
ATOM   1590 C  CA  . MET   A 1 201 ? -65.057 24.592  -2.997  1.00 68.31  ? 217 MET   A CA  1 
ATOM   1591 C  C   . MET   A 1 201 ? -64.654 23.288  -2.322  1.00 68.72  ? 217 MET   A C   1 
ATOM   1592 O  O   . MET   A 1 201 ? -65.084 23.001  -1.202  1.00 73.54  ? 217 MET   A O   1 
ATOM   1593 C  CB  . MET   A 1 201 ? -66.419 25.062  -2.472  1.00 75.49  ? 217 MET   A CB  1 
ATOM   1594 C  CG  . MET   A 1 201 ? -67.005 26.210  -3.266  1.00 80.85  ? 217 MET   A CG  1 
ATOM   1595 S  SD  . MET   A 1 201 ? -65.854 27.587  -3.408  1.00 95.50  ? 217 MET   A SD  1 
ATOM   1596 C  CE  . MET   A 1 201 ? -65.630 28.047  -1.684  1.00 85.35  ? 217 MET   A CE  1 
ATOM   1597 N  N   . ALA   A 1 202 ? -63.816 22.504  -2.999  1.00 62.48  ? 218 ALA   A N   1 
ATOM   1598 C  CA  . ALA   A 1 202 ? -63.391 21.201  -2.503  1.00 64.95  ? 218 ALA   A CA  1 
ATOM   1599 C  C   . ALA   A 1 202 ? -62.362 20.575  -3.434  1.00 57.05  ? 218 ALA   A C   1 
ATOM   1600 O  O   . ALA   A 1 202 ? -62.331 20.867  -4.631  1.00 60.80  ? 218 ALA   A O   1 
ATOM   1601 C  CB  . ALA   A 1 202 ? -64.584 20.251  -2.343  1.00 63.95  ? 218 ALA   A CB  1 
ATOM   1602 N  N   . SER   A 1 203 ? -61.518 19.704  -2.897  1.00 56.87  ? 219 SER   A N   1 
ATOM   1603 C  CA  . SER   A 1 203 ? -60.515 19.082  -3.737  1.00 57.45  ? 219 SER   A CA  1 
ATOM   1604 C  C   . SER   A 1 203 ? -60.080 17.807  -3.052  1.00 55.90  ? 219 SER   A C   1 
ATOM   1605 O  O   . SER   A 1 203 ? -59.946 17.798  -1.822  1.00 58.33  ? 219 SER   A O   1 
ATOM   1606 C  CB  . SER   A 1 203 ? -59.318 20.008  -3.928  1.00 58.48  ? 219 SER   A CB  1 
ATOM   1607 O  OG  . SER   A 1 203 ? -58.888 20.455  -2.641  1.00 63.82  ? 219 SER   A OG  1 
ATOM   1608 N  N   . PRO   A 1 204 ? -59.852 16.732  -3.794  1.00 55.30  ? 220 PRO   A N   1 
ATOM   1609 C  CA  . PRO   A 1 204 ? -59.264 15.535  -3.196  1.00 53.22  ? 220 PRO   A CA  1 
ATOM   1610 C  C   . PRO   A 1 204 ? -57.830 15.786  -2.759  1.00 53.59  ? 220 PRO   A C   1 
ATOM   1611 O  O   . PRO   A 1 204 ? -57.127 16.641  -3.298  1.00 49.87  ? 220 PRO   A O   1 
ATOM   1612 C  CB  . PRO   A 1 204 ? -59.312 14.506  -4.335  1.00 51.64  ? 220 PRO   A CB  1 
ATOM   1613 C  CG  . PRO   A 1 204 ? -60.152 15.133  -5.413  1.00 51.86  ? 220 PRO   A CG  1 
ATOM   1614 C  CD  . PRO   A 1 204 ? -60.076 16.591  -5.244  1.00 52.99  ? 220 PRO   A CD  1 
ATOM   1615 N  N   . ASP   A 1 205 ? -57.397 15.014  -1.769  1.00 53.32  ? 221 ASP   A N   1 
ATOM   1616 C  CA  . ASP   A 1 205 ? -55.999 15.008  -1.357  1.00 52.69  ? 221 ASP   A CA  1 
ATOM   1617 C  C   . ASP   A 1 205 ? -55.152 14.164  -2.321  1.00 51.56  ? 221 ASP   A C   1 
ATOM   1618 O  O   . ASP   A 1 205 ? -55.670 13.471  -3.198  1.00 49.52  ? 221 ASP   A O   1 
ATOM   1619 C  CB  . ASP   A 1 205 ? -55.886 14.482  0.072   1.00 53.49  ? 221 ASP   A CB  1 
ATOM   1620 C  CG  . ASP   A 1 205 ? -56.451 15.454  1.093   1.00 60.95  ? 221 ASP   A CG  1 
ATOM   1621 O  OD1 . ASP   A 1 205 ? -56.683 16.632  0.748   1.00 59.05  ? 221 ASP   A OD1 1 
ATOM   1622 O  OD2 . ASP   A 1 205 ? -56.661 15.036  2.242   1.00 65.06  ? 221 ASP   A OD2 1 
ATOM   1623 N  N   . LEU   A 1 206 ? -53.828 14.209  -2.133  1.00 52.16  ? 222 LEU   A N   1 
ATOM   1624 C  CA  . LEU   A 1 206 ? -52.872 13.483  -2.966  1.00 55.96  ? 222 LEU   A CA  1 
ATOM   1625 C  C   . LEU   A 1 206 ? -52.137 12.438  -2.141  1.00 57.20  ? 222 LEU   A C   1 
ATOM   1626 O  O   . LEU   A 1 206 ? -51.713 12.725  -1.021  1.00 54.60  ? 222 LEU   A O   1 
ATOM   1627 C  CB  . LEU   A 1 206 ? -51.842 14.433  -3.586  1.00 48.80  ? 222 LEU   A CB  1 
ATOM   1628 C  CG  . LEU   A 1 206 ? -50.700 13.793  -4.389  1.00 52.28  ? 222 LEU   A CG  1 
ATOM   1629 C  CD1 . LEU   A 1 206 ? -51.210 13.119  -5.685  1.00 48.98  ? 222 LEU   A CD1 1 
ATOM   1630 C  CD2 . LEU   A 1 206 ? -49.618 14.805  -4.717  1.00 46.71  ? 222 LEU   A CD2 1 
ATOM   1631 N  N   . GLU   A 1 207 ? -51.976 11.229  -2.694  1.00 50.10  ? 223 GLU   A N   1 
ATOM   1632 C  CA  . GLU   A 1 207 ? -51.102 10.222  -2.100  1.00 54.48  ? 223 GLU   A CA  1 
ATOM   1633 C  C   . GLU   A 1 207 ? -50.102 9.773   -3.153  1.00 51.07  ? 223 GLU   A C   1 
ATOM   1634 O  O   . GLU   A 1 207 ? -50.503 9.365   -4.246  1.00 54.48  ? 223 GLU   A O   1 
ATOM   1635 C  CB  . GLU   A 1 207 ? -51.891 9.018   -1.559  1.00 49.73  ? 223 GLU   A CB  1 
ATOM   1636 C  CG  . GLU   A 1 207 ? -52.789 9.369   -0.391  1.00 59.72  ? 223 GLU   A CG  1 
ATOM   1637 C  CD  . GLU   A 1 207 ? -53.629 8.203   0.095   1.00 57.93  ? 223 GLU   A CD  1 
ATOM   1638 O  OE1 . GLU   A 1 207 ? -53.482 7.075   -0.425  1.00 62.72  ? 223 GLU   A OE1 1 
ATOM   1639 O  OE2 . GLU   A 1 207 ? -54.451 8.428   1.003   1.00 68.42  ? 223 GLU   A OE2 1 
ATOM   1640 N  N   . ILE   A 1 208 ? -48.808 9.847   -2.834  1.00 48.19  ? 224 ILE   A N   1 
ATOM   1641 C  CA  . ILE   A 1 208 ? -47.753 9.443   -3.759  1.00 56.67  ? 224 ILE   A CA  1 
ATOM   1642 C  C   . ILE   A 1 208 ? -46.948 8.313   -3.136  1.00 54.94  ? 224 ILE   A C   1 
ATOM   1643 O  O   . ILE   A 1 208 ? -46.589 8.380   -1.961  1.00 53.71  ? 224 ILE   A O   1 
ATOM   1644 C  CB  . ILE   A 1 208 ? -46.803 10.603  -4.125  1.00 57.76  ? 224 ILE   A CB  1 
ATOM   1645 C  CG1 . ILE   A 1 208 ? -47.567 11.829  -4.582  1.00 62.63  ? 224 ILE   A CG1 1 
ATOM   1646 C  CG2 . ILE   A 1 208 ? -45.857 10.180  -5.250  1.00 53.66  ? 224 ILE   A CG2 1 
ATOM   1647 C  CD1 . ILE   A 1 208 ? -46.646 12.890  -5.203  1.00 65.39  ? 224 ILE   A CD1 1 
ATOM   1648 N  N   . GLN   A 1 209 ? -46.630 7.299   -3.940  1.00 53.63  ? 225 GLN   A N   1 
ATOM   1649 C  CA  . GLN   A 1 209 ? -45.639 6.290   -3.608  1.00 55.17  ? 225 GLN   A CA  1 
ATOM   1650 C  C   . GLN   A 1 209 ? -44.688 6.111   -4.784  1.00 52.23  ? 225 GLN   A C   1 
ATOM   1651 O  O   . GLN   A 1 209 ? -45.049 6.339   -5.939  1.00 50.23  ? 225 GLN   A O   1 
ATOM   1652 C  CB  . GLN   A 1 209 ? -46.267 4.936   -3.297  1.00 60.61  ? 225 GLN   A CB  1 
ATOM   1653 C  CG  . GLN   A 1 209 ? -47.468 4.956   -2.399  1.00 67.07  ? 225 GLN   A CG  1 
ATOM   1654 C  CD  . GLN   A 1 209 ? -48.012 3.552   -2.207  1.00 84.49  ? 225 GLN   A CD  1 
ATOM   1655 O  OE1 . GLN   A 1 209 ? -47.286 2.567   -2.379  1.00 83.53  ? 225 GLN   A OE1 1 
ATOM   1656 N  NE2 . GLN   A 1 209 ? -49.294 3.448   -1.865  1.00 89.68  ? 225 GLN   A NE2 1 
ATOM   1657 N  N   . GLU   A 1 210 ? -43.474 5.660   -4.480  1.00 52.82  ? 226 GLU   A N   1 
ATOM   1658 C  CA  . GLU   A 1 210 ? -42.467 5.367   -5.486  1.00 52.33  ? 226 GLU   A CA  1 
ATOM   1659 C  C   . GLU   A 1 210 ? -42.018 3.919   -5.353  1.00 57.52  ? 226 GLU   A C   1 
ATOM   1660 O  O   . GLU   A 1 210 ? -41.908 3.404   -4.242  1.00 51.05  ? 226 GLU   A O   1 
ATOM   1661 C  CB  . GLU   A 1 210 ? -41.248 6.283   -5.328  1.00 55.60  ? 226 GLU   A CB  1 
ATOM   1662 C  CG  . GLU   A 1 210 ? -41.530 7.738   -5.589  1.00 55.59  ? 226 GLU   A CG  1 
ATOM   1663 C  CD  . GLU   A 1 210 ? -40.279 8.532   -5.866  1.00 54.85  ? 226 GLU   A CD  1 
ATOM   1664 O  OE1 . GLU   A 1 210 ? -39.162 7.995   -5.733  1.00 49.42  ? 226 GLU   A OE1 1 
ATOM   1665 O  OE2 . GLU   A 1 210 ? -40.424 9.709   -6.227  1.00 59.82  ? 226 GLU   A OE2 1 
ATOM   1666 N  N   . ILE   A 1 211 ? -41.744 3.262   -6.479  1.00 54.99  ? 227 ILE   A N   1 
ATOM   1667 C  CA  . ILE   A 1 211 ? -41.086 1.954   -6.486  1.00 54.81  ? 227 ILE   A CA  1 
ATOM   1668 C  C   . ILE   A 1 211 ? -39.870 2.092   -7.379  1.00 54.09  ? 227 ILE   A C   1 
ATOM   1669 O  O   . ILE   A 1 211 ? -40.001 2.163   -8.609  1.00 51.74  ? 227 ILE   A O   1 
ATOM   1670 C  CB  . ILE   A 1 211 ? -41.991 0.820   -6.995  1.00 59.40  ? 227 ILE   A CB  1 
ATOM   1671 C  CG1 . ILE   A 1 211 ? -43.354 0.843   -6.303  1.00 61.33  ? 227 ILE   A CG1 1 
ATOM   1672 C  CG2 . ILE   A 1 211 ? -41.297 -0.538  -6.781  1.00 53.74  ? 227 ILE   A CG2 1 
ATOM   1673 C  CD1 . ILE   A 1 211 ? -43.338 0.302   -4.871  1.00 58.53  ? 227 ILE   A CD1 1 
ATOM   1674 N  N   . ASN   A 1 212 ? -38.696 2.149   -6.774  1.00 50.98  ? 228 ASN   A N   1 
ATOM   1675 C  CA  . ASN   A 1 212 ? -37.435 2.163   -7.511  1.00 55.40  ? 228 ASN   A CA  1 
ATOM   1676 C  C   . ASN   A 1 212 ? -36.908 0.737   -7.432  1.00 57.54  ? 228 ASN   A C   1 
ATOM   1677 O  O   . ASN   A 1 212 ? -36.220 0.368   -6.484  1.00 61.89  ? 228 ASN   A O   1 
ATOM   1678 C  CB  . ASN   A 1 212 ? -36.465 3.173   -6.917  1.00 59.83  ? 228 ASN   A CB  1 
ATOM   1679 C  CG  . ASN   A 1 212 ? -35.234 3.369   -7.766  1.00 59.45  ? 228 ASN   A CG  1 
ATOM   1680 O  OD1 . ASN   A 1 212 ? -34.850 2.494   -8.539  1.00 58.77  ? 228 ASN   A OD1 1 
ATOM   1681 N  ND2 . ASN   A 1 212 ? -34.604 4.532   -7.630  1.00 58.34  ? 228 ASN   A ND2 1 
ATOM   1682 N  N   . ALA   A 1 213 ? -37.245 -0.066  -8.445  1.00 57.62  ? 229 ALA   A N   1 
ATOM   1683 C  CA  . ALA   A 1 213 ? -37.016 -1.506  -8.372  1.00 56.23  ? 229 ALA   A CA  1 
ATOM   1684 C  C   . ALA   A 1 213 ? -35.543 -1.833  -8.146  1.00 61.89  ? 229 ALA   A C   1 
ATOM   1685 O  O   . ALA   A 1 213 ? -35.200 -2.681  -7.305  1.00 59.07  ? 229 ALA   A O   1 
ATOM   1686 C  CB  . ALA   A 1 213 ? -37.536 -2.170  -9.646  1.00 51.98  ? 229 ALA   A CB  1 
ATOM   1687 N  N   . ALA   A 1 214 ? -34.651 -1.157  -8.876  1.00 60.95  ? 230 ALA   A N   1 
ATOM   1688 C  CA  . ALA   A 1 214 ? -33.228 -1.477  -8.792  1.00 65.03  ? 230 ALA   A CA  1 
ATOM   1689 C  C   . ALA   A 1 214 ? -32.568 -0.895  -7.547  1.00 63.14  ? 230 ALA   A C   1 
ATOM   1690 O  O   . ALA   A 1 214 ? -31.609 -1.486  -7.042  1.00 68.20  ? 230 ALA   A O   1 
ATOM   1691 C  CB  . ALA   A 1 214 ? -32.505 -0.995  -10.055 1.00 62.32  ? 230 ALA   A CB  1 
ATOM   1692 N  N   . ASN   A 1 215 ? -33.050 0.257   -7.041  1.00 64.83  ? 231 ASN   A N   1 
ATOM   1693 C  CA  . ASN   A 1 215 ? -32.504 0.899   -5.827  1.00 69.41  ? 231 ASN   A CA  1 
ATOM   1694 C  C   . ASN   A 1 215 ? -33.659 1.363   -4.941  1.00 68.89  ? 231 ASN   A C   1 
ATOM   1695 O  O   . ASN   A 1 215 ? -34.095 2.511   -5.052  1.00 65.81  ? 231 ASN   A O   1 
ATOM   1696 C  CB  . ASN   A 1 215 ? -31.596 2.071   -6.179  1.00 73.19  ? 231 ASN   A CB  1 
ATOM   1697 C  CG  . ASN   A 1 215 ? -30.436 1.673   -7.054  1.00 78.27  ? 231 ASN   A CG  1 
ATOM   1698 O  OD1 . ASN   A 1 215 ? -29.349 1.351   -6.564  1.00 77.10  ? 231 ASN   A OD1 1 
ATOM   1699 N  ND2 . ASN   A 1 215 ? -30.654 1.698   -8.361  1.00 63.60  ? 231 ASN   A ND2 1 
ATOM   1700 N  N   . SER   A 1 216 ? -34.092 0.498   -4.014  1.00 70.28  ? 232 SER   A N   1 
ATOM   1701 C  CA  . SER   A 1 216 ? -35.353 0.725   -3.304  1.00 72.56  ? 232 SER   A CA  1 
ATOM   1702 C  C   . SER   A 1 216 ? -35.353 1.998   -2.457  1.00 77.92  ? 232 SER   A C   1 
ATOM   1703 O  O   . SER   A 1 216 ? -36.425 2.544   -2.175  1.00 72.19  ? 232 SER   A O   1 
ATOM   1704 C  CB  . SER   A 1 216 ? -35.694 -0.485  -2.422  1.00 67.76  ? 232 SER   A CB  1 
ATOM   1705 O  OG  . SER   A 1 216 ? -34.709 -0.705  -1.427  1.00 80.57  ? 232 SER   A OG  1 
ATOM   1706 N  N   . LYS   A 1 217 ? -34.196 2.499   -2.050  1.00 90.95  ? 233 LYS   A N   1 
ATOM   1707 C  CA  . LYS   A 1 217 ? -34.201 3.696   -1.222  1.00 89.13  ? 233 LYS   A CA  1 
ATOM   1708 C  C   . LYS   A 1 217 ? -34.068 4.991   -2.023  1.00 90.61  ? 233 LYS   A C   1 
ATOM   1709 O  O   . LYS   A 1 217 ? -34.354 6.063   -1.481  1.00 92.62  ? 233 LYS   A O   1 
ATOM   1710 C  CB  . LYS   A 1 217 ? -33.094 3.599   -0.168  1.00 93.11  ? 233 LYS   A CB  1 
ATOM   1711 C  CG  . LYS   A 1 217 ? -33.461 2.675   1.005   1.00 97.70  ? 233 LYS   A CG  1 
ATOM   1712 C  CD  . LYS   A 1 217 ? -32.261 1.911   1.573   1.00 109.69 ? 233 LYS   A CD  1 
ATOM   1713 C  CE  . LYS   A 1 217 ? -31.958 0.653   0.751   1.00 111.79 ? 233 LYS   A CE  1 
ATOM   1714 N  NZ  . LYS   A 1 217 ? -30.911 -0.218  1.371   1.00 98.11  ? 233 LYS   A NZ  1 
ATOM   1715 N  N   . GLN   A 1 218 ? -33.695 4.927   -3.310  1.00 75.68  ? 234 GLN   A N   1 
ATOM   1716 C  CA  . GLN   A 1 218 ? -33.330 6.161   -3.996  1.00 72.26  ? 234 GLN   A CA  1 
ATOM   1717 C  C   . GLN   A 1 218 ? -34.560 6.864   -4.557  1.00 67.86  ? 234 GLN   A C   1 
ATOM   1718 O  O   . GLN   A 1 218 ? -35.335 6.246   -5.303  1.00 61.04  ? 234 GLN   A O   1 
ATOM   1719 C  CB  . GLN   A 1 218 ? -32.348 5.885   -5.119  1.00 70.01  ? 234 GLN   A CB  1 
ATOM   1720 C  CG  . GLN   A 1 218 ? -30.928 5.619   -4.632  1.00 85.42  ? 234 GLN   A CG  1 
ATOM   1721 C  CD  . GLN   A 1 218 ? -29.921 5.626   -5.764  1.00 88.44  ? 234 GLN   A CD  1 
ATOM   1722 O  OE1 . GLN   A 1 218 ? -30.236 6.022   -6.895  1.00 86.86  ? 234 GLN   A OE1 1 
ATOM   1723 N  NE2 . GLN   A 1 218 ? -28.703 5.183   -5.469  1.00 86.73  ? 234 GLN   A NE2 1 
ATOM   1724 N  N   . PRO   A 1 219 ? -34.761 8.140   -4.219  1.00 65.11  ? 235 PRO   A N   1 
ATOM   1725 C  CA  . PRO   A 1 219 ? -35.759 8.944   -4.933  1.00 64.67  ? 235 PRO   A CA  1 
ATOM   1726 C  C   . PRO   A 1 219 ? -35.545 8.838   -6.435  1.00 58.56  ? 235 PRO   A C   1 
ATOM   1727 O  O   . PRO   A 1 219 ? -34.410 8.794   -6.919  1.00 61.40  ? 235 PRO   A O   1 
ATOM   1728 C  CB  . PRO   A 1 219 ? -35.513 10.369  -4.425  1.00 65.75  ? 235 PRO   A CB  1 
ATOM   1729 C  CG  . PRO   A 1 219 ? -34.246 10.305  -3.595  1.00 68.65  ? 235 PRO   A CG  1 
ATOM   1730 C  CD  . PRO   A 1 219 ? -34.080 8.898   -3.151  1.00 71.29  ? 235 PRO   A CD  1 
ATOM   1731 N  N   . ILE   A 1 220 ? -36.650 8.782   -7.170  1.00 50.63  ? 236 ILE   A N   1 
ATOM   1732 C  CA  . ILE   A 1 220 ? -36.610 8.491   -8.600  1.00 56.82  ? 236 ILE   A CA  1 
ATOM   1733 C  C   . ILE   A 1 220 ? -36.346 9.780   -9.373  1.00 52.05  ? 236 ILE   A C   1 
ATOM   1734 O  O   . ILE   A 1 220 ? -37.113 10.742  -9.281  1.00 48.73  ? 236 ILE   A O   1 
ATOM   1735 C  CB  . ILE   A 1 220 ? -37.911 7.813   -9.059  1.00 50.17  ? 236 ILE   A CB  1 
ATOM   1736 C  CG1 . ILE   A 1 220 ? -37.952 6.370   -8.525  1.00 48.41  ? 236 ILE   A CG1 1 
ATOM   1737 C  CG2 . ILE   A 1 220 ? -38.052 7.887   -10.589 1.00 45.35  ? 236 ILE   A CG2 1 
ATOM   1738 C  CD1 . ILE   A 1 220 ? -39.287 5.677   -8.698  1.00 47.48  ? 236 ILE   A CD1 1 
ATOM   1739 N  N   . HIS   A 1 221 ? -35.251 9.797   -10.129 1.00 52.10  ? 237 HIS   A N   1 
ATOM   1740 C  CA  . HIS   A 1 221 ? -34.872 10.905  -10.993 1.00 52.13  ? 237 HIS   A CA  1 
ATOM   1741 C  C   . HIS   A 1 221 ? -34.724 10.381  -12.413 1.00 50.52  ? 237 HIS   A C   1 
ATOM   1742 O  O   . HIS   A 1 221 ? -34.536 9.183   -12.626 1.00 51.41  ? 237 HIS   A O   1 
ATOM   1743 C  CB  . HIS   A 1 221 ? -33.544 11.542  -10.546 1.00 51.19  ? 237 HIS   A CB  1 
ATOM   1744 C  CG  . HIS   A 1 221 ? -33.591 12.181  -9.186  1.00 63.56  ? 237 HIS   A CG  1 
ATOM   1745 N  ND1 . HIS   A 1 221 ? -33.680 13.547  -9.007  1.00 65.34  ? 237 HIS   A ND1 1 
ATOM   1746 C  CD2 . HIS   A 1 221 ? -33.528 11.645  -7.941  1.00 65.29  ? 237 HIS   A CD2 1 
ATOM   1747 C  CE1 . HIS   A 1 221 ? -33.690 13.823  -7.713  1.00 65.35  ? 237 HIS   A CE1 1 
ATOM   1748 N  NE2 . HIS   A 1 221 ? -33.598 12.687  -7.044  1.00 61.49  ? 237 HIS   A NE2 1 
ATOM   1749 N  N   . MET   A 1 222 ? -34.789 11.285  -13.386 1.00 49.58  ? 238 MET   A N   1 
ATOM   1750 C  CA  . MET   A 1 222 ? -34.630 10.918  -14.788 1.00 50.41  ? 238 MET   A CA  1 
ATOM   1751 C  C   . MET   A 1 222 ? -34.161 12.145  -15.551 1.00 53.48  ? 238 MET   A C   1 
ATOM   1752 O  O   . MET   A 1 222 ? -34.221 13.272  -15.049 1.00 51.28  ? 238 MET   A O   1 
ATOM   1753 C  CB  . MET   A 1 222 ? -35.936 10.408  -15.396 1.00 41.95  ? 238 MET   A CB  1 
ATOM   1754 C  CG  . MET   A 1 222 ? -36.940 11.512  -15.598 1.00 45.84  ? 238 MET   A CG  1 
ATOM   1755 S  SD  . MET   A 1 222 ? -38.514 11.022  -16.348 1.00 49.83  ? 238 MET   A SD  1 
ATOM   1756 C  CE  . MET   A 1 222 ? -37.955 10.105  -17.803 1.00 42.82  ? 238 MET   A CE  1 
ATOM   1757 N  N   . VAL   A 1 223 ? -33.719 11.918  -16.786 1.00 53.91  ? 239 VAL   A N   1 
ATOM   1758 C  CA  . VAL   A 1 223 ? -33.485 13.006  -17.728 1.00 49.80  ? 239 VAL   A CA  1 
ATOM   1759 C  C   . VAL   A 1 223 ? -34.782 13.243  -18.490 1.00 48.91  ? 239 VAL   A C   1 
ATOM   1760 O  O   . VAL   A 1 223 ? -35.293 12.331  -19.150 1.00 48.50  ? 239 VAL   A O   1 
ATOM   1761 C  CB  . VAL   A 1 223 ? -32.330 12.689  -18.692 1.00 50.94  ? 239 VAL   A CB  1 
ATOM   1762 C  CG1 . VAL   A 1 223 ? -32.096 13.881  -19.589 1.00 49.92  ? 239 VAL   A CG1 1 
ATOM   1763 C  CG2 . VAL   A 1 223 ? -31.030 12.326  -17.929 1.00 47.77  ? 239 VAL   A CG2 1 
ATOM   1764 N  N   . TYR   A 1 224 ? -35.325 14.456  -18.405 1.00 46.92  ? 240 TYR   A N   1 
ATOM   1765 C  CA  . TYR   A 1 224 ? -36.559 14.737  -19.129 1.00 46.40  ? 240 TYR   A CA  1 
ATOM   1766 C  C   . TYR   A 1 224 ? -36.737 16.247  -19.296 1.00 46.34  ? 240 TYR   A C   1 
ATOM   1767 O  O   . TYR   A 1 224 ? -35.907 17.053  -18.859 1.00 47.47  ? 240 TYR   A O   1 
ATOM   1768 C  CB  . TYR   A 1 224 ? -37.772 14.092  -18.436 1.00 43.86  ? 240 TYR   A CB  1 
ATOM   1769 C  CG  . TYR   A 1 224 ? -38.902 13.826  -19.419 1.00 44.72  ? 240 TYR   A CG  1 
ATOM   1770 C  CD1 . TYR   A 1 224 ? -38.774 12.833  -20.390 1.00 44.12  ? 240 TYR   A CD1 1 
ATOM   1771 C  CD2 . TYR   A 1 224 ? -40.078 14.572  -19.397 1.00 42.12  ? 240 TYR   A CD2 1 
ATOM   1772 C  CE1 . TYR   A 1 224 ? -39.780 12.593  -21.303 1.00 42.01  ? 240 TYR   A CE1 1 
ATOM   1773 C  CE2 . TYR   A 1 224 ? -41.092 14.337  -20.319 1.00 40.38  ? 240 TYR   A CE2 1 
ATOM   1774 C  CZ  . TYR   A 1 224 ? -40.928 13.343  -21.268 1.00 42.08  ? 240 TYR   A CZ  1 
ATOM   1775 O  OH  . TYR   A 1 224 ? -41.915 13.086  -22.185 1.00 43.86  ? 240 TYR   A OH  1 
ATOM   1776 N  N   . VAL   A 1 225 ? -37.817 16.612  -19.986 1.00 40.36  ? 241 VAL   A N   1 
ATOM   1777 C  CA  . VAL   A 1 225 ? -38.266 17.989  -20.171 1.00 40.63  ? 241 VAL   A CA  1 
ATOM   1778 C  C   . VAL   A 1 225 ? -39.375 18.245  -19.154 1.00 41.50  ? 241 VAL   A C   1 
ATOM   1779 O  O   . VAL   A 1 225 ? -40.527 17.846  -19.369 1.00 41.35  ? 241 VAL   A O   1 
ATOM   1780 C  CB  . VAL   A 1 225 ? -38.760 18.240  -21.608 1.00 45.93  ? 241 VAL   A CB  1 
ATOM   1781 C  CG1 . VAL   A 1 225 ? -39.267 19.700  -21.754 1.00 41.82  ? 241 VAL   A CG1 1 
ATOM   1782 C  CG2 . VAL   A 1 225 ? -37.649 17.942  -22.638 1.00 46.50  ? 241 VAL   A CG2 1 
ATOM   1783 N  N   . PRO   A 1 226 ? -39.077 18.871  -18.019 1.00 44.08  ? 242 PRO   A N   1 
ATOM   1784 C  CA  . PRO   A 1 226 ? -40.075 18.876  -16.938 1.00 40.24  ? 242 PRO   A CA  1 
ATOM   1785 C  C   . PRO   A 1 226 ? -41.337 19.642  -17.295 1.00 39.07  ? 242 PRO   A C   1 
ATOM   1786 O  O   . PRO   A 1 226 ? -42.402 19.310  -16.770 1.00 39.36  ? 242 PRO   A O   1 
ATOM   1787 C  CB  . PRO   A 1 226 ? -39.319 19.490  -15.745 1.00 43.01  ? 242 PRO   A CB  1 
ATOM   1788 C  CG  . PRO   A 1 226 ? -38.065 20.136  -16.337 1.00 43.43  ? 242 PRO   A CG  1 
ATOM   1789 C  CD  . PRO   A 1 226 ? -37.753 19.347  -17.583 1.00 40.25  ? 242 PRO   A CD  1 
ATOM   1790 N  N   . SER   A 1 227 ? -41.272 20.624  -18.197 1.00 38.78  ? 243 SER   A N   1 
ATOM   1791 C  CA  . SER   A 1 227 ? -42.490 21.350  -18.542 1.00 39.62  ? 243 SER   A CA  1 
ATOM   1792 C  C   . SER   A 1 227 ? -43.472 20.456  -19.297 1.00 42.56  ? 243 SER   A C   1 
ATOM   1793 O  O   . SER   A 1 227 ? -44.688 20.597  -19.138 1.00 41.41  ? 243 SER   A O   1 
ATOM   1794 C  CB  . SER   A 1 227 ? -42.157 22.606  -19.361 1.00 41.52  ? 243 SER   A CB  1 
ATOM   1795 O  OG  . SER   A 1 227 ? -41.568 22.246  -20.597 1.00 52.79  ? 243 SER   A OG  1 
ATOM   1796 N  N   . HIS   A 1 228 ? -42.969 19.539  -20.130 1.00 41.05  ? 244 HIS   A N   1 
ATOM   1797 C  CA  . HIS   A 1 228 ? -43.857 18.571  -20.771 1.00 39.80  ? 244 HIS   A CA  1 
ATOM   1798 C  C   . HIS   A 1 228 ? -44.504 17.662  -19.738 1.00 43.50  ? 244 HIS   A C   1 
ATOM   1799 O  O   . HIS   A 1 228 ? -45.704 17.356  -19.824 1.00 41.10  ? 244 HIS   A O   1 
ATOM   1800 C  CB  . HIS   A 1 228 ? -43.098 17.709  -21.786 1.00 39.90  ? 244 HIS   A CB  1 
ATOM   1801 C  CG  . HIS   A 1 228 ? -42.594 18.464  -22.978 1.00 41.91  ? 244 HIS   A CG  1 
ATOM   1802 N  ND1 . HIS   A 1 228 ? -41.962 17.843  -24.039 1.00 41.37  ? 244 HIS   A ND1 1 
ATOM   1803 C  CD2 . HIS   A 1 228 ? -42.628 19.783  -23.278 1.00 46.96  ? 244 HIS   A CD2 1 
ATOM   1804 C  CE1 . HIS   A 1 228 ? -41.624 18.754  -24.940 1.00 44.32  ? 244 HIS   A CE1 1 
ATOM   1805 N  NE2 . HIS   A 1 228 ? -42.018 19.939  -24.501 1.00 45.33  ? 244 HIS   A NE2 1 
ATOM   1806 N  N   . LEU   A 1 229 ? -43.711 17.184  -18.777 1.00 39.92  ? 245 LEU   A N   1 
ATOM   1807 C  CA  . LEU   A 1 229 ? -44.254 16.278  -17.774 1.00 40.34  ? 245 LEU   A CA  1 
ATOM   1808 C  C   . LEU   A 1 229 ? -45.284 16.998  -16.913 1.00 39.06  ? 245 LEU   A C   1 
ATOM   1809 O  O   . LEU   A 1 229 ? -46.334 16.437  -16.575 1.00 39.25  ? 245 LEU   A O   1 
ATOM   1810 C  CB  . LEU   A 1 229 ? -43.104 15.705  -16.933 1.00 41.28  ? 245 LEU   A CB  1 
ATOM   1811 C  CG  . LEU   A 1 229 ? -43.411 14.769  -15.758 1.00 45.00  ? 245 LEU   A CG  1 
ATOM   1812 C  CD1 . LEU   A 1 229 ? -44.146 13.537  -16.212 1.00 38.81  ? 245 LEU   A CD1 1 
ATOM   1813 C  CD2 . LEU   A 1 229 ? -42.112 14.382  -15.018 1.00 43.48  ? 245 LEU   A CD2 1 
ATOM   1814 N  N   . TYR   A 1 230 ? -45.019 18.257  -16.587 1.00 38.94  ? 246 TYR   A N   1 
ATOM   1815 C  CA  . TYR   A 1 230 ? -46.010 19.057  -15.875 1.00 43.55  ? 246 TYR   A CA  1 
ATOM   1816 C  C   . TYR   A 1 230 ? -47.315 19.159  -16.669 1.00 43.33  ? 246 TYR   A C   1 
ATOM   1817 O  O   . TYR   A 1 230 ? -48.402 18.956  -16.112 1.00 42.88  ? 246 TYR   A O   1 
ATOM   1818 C  CB  . TYR   A 1 230 ? -45.435 20.449  -15.570 1.00 38.40  ? 246 TYR   A CB  1 
ATOM   1819 C  CG  . TYR   A 1 230 ? -46.414 21.387  -14.875 1.00 46.79  ? 246 TYR   A CG  1 
ATOM   1820 C  CD1 . TYR   A 1 230 ? -47.399 22.056  -15.605 1.00 47.72  ? 246 TYR   A CD1 1 
ATOM   1821 C  CD2 . TYR   A 1 230 ? -46.352 21.608  -13.498 1.00 47.00  ? 246 TYR   A CD2 1 
ATOM   1822 C  CE1 . TYR   A 1 230 ? -48.302 22.904  -14.987 1.00 47.44  ? 246 TYR   A CE1 1 
ATOM   1823 C  CE2 . TYR   A 1 230 ? -47.246 22.463  -12.871 1.00 48.08  ? 246 TYR   A CE2 1 
ATOM   1824 C  CZ  . TYR   A 1 230 ? -48.225 23.101  -13.630 1.00 51.97  ? 246 TYR   A CZ  1 
ATOM   1825 O  OH  . TYR   A 1 230 ? -49.124 23.945  -13.041 1.00 48.70  ? 246 TYR   A OH  1 
ATOM   1826 N  N   . HIS   A 1 231 ? -47.230 19.472  -17.973 1.00 42.22  ? 247 HIS   A N   1 
ATOM   1827 C  CA  . HIS   A 1 231 ? -48.436 19.619  -18.800 1.00 44.94  ? 247 HIS   A CA  1 
ATOM   1828 C  C   . HIS   A 1 231 ? -49.312 18.374  -18.729 1.00 43.68  ? 247 HIS   A C   1 
ATOM   1829 O  O   . HIS   A 1 231 ? -50.533 18.467  -18.551 1.00 41.55  ? 247 HIS   A O   1 
ATOM   1830 C  CB  . HIS   A 1 231 ? -48.077 19.873  -20.269 1.00 46.40  ? 247 HIS   A CB  1 
ATOM   1831 C  CG  . HIS   A 1 231 ? -47.359 21.160  -20.518 1.00 54.22  ? 247 HIS   A CG  1 
ATOM   1832 N  ND1 . HIS   A 1 231 ? -47.585 22.302  -19.775 1.00 60.47  ? 247 HIS   A ND1 1 
ATOM   1833 C  CD2 . HIS   A 1 231 ? -46.422 21.489  -21.442 1.00 49.69  ? 247 HIS   A CD2 1 
ATOM   1834 C  CE1 . HIS   A 1 231 ? -46.810 23.275  -20.226 1.00 57.86  ? 247 HIS   A CE1 1 
ATOM   1835 N  NE2 . HIS   A 1 231 ? -46.096 22.807  -21.236 1.00 55.84  ? 247 HIS   A NE2 1 
ATOM   1836 N  N   . MET   A 1 232 ? -48.706 17.195  -18.892 1.00 38.31  ? 248 MET   A N   1 
ATOM   1837 C  CA  . MET   A 1 232 ? -49.487 15.962  -18.880 1.00 41.98  ? 248 MET   A CA  1 
ATOM   1838 C  C   . MET   A 1 232 ? -50.132 15.736  -17.516 1.00 43.90  ? 248 MET   A C   1 
ATOM   1839 O  O   . MET   A 1 232 ? -51.330 15.441  -17.419 1.00 41.04  ? 248 MET   A O   1 
ATOM   1840 C  CB  . MET   A 1 232 ? -48.604 14.767  -19.249 1.00 40.01  ? 248 MET   A CB  1 
ATOM   1841 C  CG  . MET   A 1 232 ? -47.889 14.888  -20.570 1.00 42.85  ? 248 MET   A CG  1 
ATOM   1842 S  SD  . MET   A 1 232 ? -46.927 13.395  -20.884 1.00 45.30  ? 248 MET   A SD  1 
ATOM   1843 C  CE  . MET   A 1 232 ? -45.382 13.779  -20.110 1.00 40.87  ? 248 MET   A CE  1 
ATOM   1844 N  N   . LEU   A 1 233 ? -49.336 15.842  -16.453 1.00 41.91  ? 249 LEU   A N   1 
ATOM   1845 C  CA  . LEU   A 1 233 ? -49.848 15.628  -15.101 1.00 45.94  ? 249 LEU   A CA  1 
ATOM   1846 C  C   . LEU   A 1 233 ? -50.935 16.637  -14.758 1.00 38.82  ? 249 LEU   A C   1 
ATOM   1847 O  O   . LEU   A 1 233 ? -51.969 16.276  -14.185 1.00 40.84  ? 249 LEU   A O   1 
ATOM   1848 C  CB  . LEU   A 1 233 ? -48.702 15.713  -14.088 1.00 40.51  ? 249 LEU   A CB  1 
ATOM   1849 C  CG  . LEU   A 1 233 ? -47.764 14.506  -14.201 1.00 42.55  ? 249 LEU   A CG  1 
ATOM   1850 C  CD1 . LEU   A 1 233 ? -46.418 14.769  -13.507 1.00 44.12  ? 249 LEU   A CD1 1 
ATOM   1851 C  CD2 . LEU   A 1 233 ? -48.410 13.260  -13.599 1.00 40.74  ? 249 LEU   A CD2 1 
ATOM   1852 N  N   . PHE   A 1 234 ? -50.709 17.916  -15.074 1.00 38.28  ? 250 PHE   A N   1 
ATOM   1853 C  CA  . PHE   A 1 234 ? -51.712 18.939  -14.783 1.00 42.80  ? 250 PHE   A CA  1 
ATOM   1854 C  C   . PHE   A 1 234 ? -53.046 18.608  -15.442 1.00 44.13  ? 250 PHE   A C   1 
ATOM   1855 O  O   . PHE   A 1 234 ? -54.112 18.699  -14.811 1.00 39.36  ? 250 PHE   A O   1 
ATOM   1856 C  CB  . PHE   A 1 234 ? -51.226 20.310  -15.252 1.00 41.99  ? 250 PHE   A CB  1 
ATOM   1857 C  CG  . PHE   A 1 234 ? -52.212 21.414  -15.011 1.00 42.78  ? 250 PHE   A CG  1 
ATOM   1858 C  CD1 . PHE   A 1 234 ? -52.533 21.802  -13.719 1.00 43.05  ? 250 PHE   A CD1 1 
ATOM   1859 C  CD2 . PHE   A 1 234 ? -52.816 22.076  -16.076 1.00 45.73  ? 250 PHE   A CD2 1 
ATOM   1860 C  CE1 . PHE   A 1 234 ? -53.436 22.844  -13.491 1.00 42.72  ? 250 PHE   A CE1 1 
ATOM   1861 C  CE2 . PHE   A 1 234 ? -53.718 23.108  -15.859 1.00 50.25  ? 250 PHE   A CE2 1 
ATOM   1862 C  CZ  . PHE   A 1 234 ? -54.026 23.496  -14.569 1.00 48.76  ? 250 PHE   A CZ  1 
ATOM   1863 N  N   . GLU   A 1 235 ? -53.000 18.221  -16.716 1.00 44.02  ? 251 GLU   A N   1 
ATOM   1864 C  CA  . GLU   A 1 235 ? -54.215 17.861  -17.449 1.00 44.65  ? 251 GLU   A CA  1 
ATOM   1865 C  C   . GLU   A 1 235 ? -54.914 16.657  -16.814 1.00 43.58  ? 251 GLU   A C   1 
ATOM   1866 O  O   . GLU   A 1 235 ? -56.145 16.647  -16.651 1.00 41.12  ? 251 GLU   A O   1 
ATOM   1867 C  CB  . GLU   A 1 235 ? -53.867 17.585  -18.917 1.00 40.41  ? 251 GLU   A CB  1 
ATOM   1868 C  CG  . GLU   A 1 235 ? -55.069 17.412  -19.803 1.00 47.70  ? 251 GLU   A CG  1 
ATOM   1869 C  CD  . GLU   A 1 235 ? -55.902 18.690  -19.937 1.00 52.99  ? 251 GLU   A CD  1 
ATOM   1870 O  OE1 . GLU   A 1 235 ? -55.337 19.825  -19.887 1.00 52.85  ? 251 GLU   A OE1 1 
ATOM   1871 O  OE2 . GLU   A 1 235 ? -57.139 18.532  -20.076 1.00 59.22  ? 251 GLU   A OE2 1 
ATOM   1872 N  N   . LEU   A 1 236 ? -54.144 15.625  -16.457 1.00 37.56  ? 252 LEU   A N   1 
ATOM   1873 C  CA  . LEU   A 1 236 ? -54.729 14.460  -15.796 1.00 39.48  ? 252 LEU   A CA  1 
ATOM   1874 C  C   . LEU   A 1 236 ? -55.337 14.829  -14.439 1.00 39.89  ? 252 LEU   A C   1 
ATOM   1875 O  O   . LEU   A 1 236 ? -56.460 14.427  -14.131 1.00 40.87  ? 252 LEU   A O   1 
ATOM   1876 C  CB  . LEU   A 1 236 ? -53.679 13.359  -15.644 1.00 37.27  ? 252 LEU   A CB  1 
ATOM   1877 C  CG  . LEU   A 1 236 ? -53.251 12.803  -17.012 1.00 42.80  ? 252 LEU   A CG  1 
ATOM   1878 C  CD1 . LEU   A 1 236 ? -52.062 11.889  -16.902 1.00 32.42  ? 252 LEU   A CD1 1 
ATOM   1879 C  CD2 . LEU   A 1 236 ? -54.425 12.089  -17.701 1.00 37.90  ? 252 LEU   A CD2 1 
ATOM   1880 N  N   . PHE   A 1 237 ? -54.602 15.591  -13.612 1.00 38.04  ? 253 PHE   A N   1 
ATOM   1881 C  CA  . PHE   A 1 237 ? -55.113 15.991  -12.300 1.00 40.75  ? 253 PHE   A CA  1 
ATOM   1882 C  C   . PHE   A 1 237 ? -56.408 16.781  -12.432 1.00 46.20  ? 253 PHE   A C   1 
ATOM   1883 O  O   . PHE   A 1 237 ? -57.340 16.599  -11.640 1.00 44.21  ? 253 PHE   A O   1 
ATOM   1884 C  CB  . PHE   A 1 237 ? -54.076 16.836  -11.544 1.00 40.71  ? 253 PHE   A CB  1 
ATOM   1885 C  CG  . PHE   A 1 237 ? -53.088 16.034  -10.751 1.00 36.84  ? 253 PHE   A CG  1 
ATOM   1886 C  CD1 . PHE   A 1 237 ? -53.517 15.081  -9.836  1.00 42.24  ? 253 PHE   A CD1 1 
ATOM   1887 C  CD2 . PHE   A 1 237 ? -51.726 16.233  -10.928 1.00 36.52  ? 253 PHE   A CD2 1 
ATOM   1888 C  CE1 . PHE   A 1 237 ? -52.589 14.337  -9.090  1.00 42.39  ? 253 PHE   A CE1 1 
ATOM   1889 C  CE2 . PHE   A 1 237 ? -50.788 15.491  -10.196 1.00 38.65  ? 253 PHE   A CE2 1 
ATOM   1890 C  CZ  . PHE   A 1 237 ? -51.220 14.534  -9.283  1.00 39.80  ? 253 PHE   A CZ  1 
ATOM   1891 N  N   . LYS   A 1 238 ? -56.480 17.670  -13.423 1.00 39.86  ? 254 LYS   A N   1 
ATOM   1892 C  CA  . LYS   A 1 238 ? -57.689 18.460  -13.612 1.00 44.85  ? 254 LYS   A CA  1 
ATOM   1893 C  C   . LYS   A 1 238 ? -58.886 17.560  -13.874 1.00 45.86  ? 254 LYS   A C   1 
ATOM   1894 O  O   . LYS   A 1 238 ? -59.945 17.719  -13.254 1.00 42.87  ? 254 LYS   A O   1 
ATOM   1895 C  CB  . LYS   A 1 238 ? -57.459 19.452  -14.759 1.00 52.70  ? 254 LYS   A CB  1 
ATOM   1896 C  CG  . LYS   A 1 238 ? -58.636 20.273  -15.181 1.00 64.92  ? 254 LYS   A CG  1 
ATOM   1897 C  CD  . LYS   A 1 238 ? -58.170 21.404  -16.092 1.00 72.80  ? 254 LYS   A CD  1 
ATOM   1898 C  CE  . LYS   A 1 238 ? -58.073 20.968  -17.542 1.00 74.14  ? 254 LYS   A CE  1 
ATOM   1899 N  NZ  . LYS   A 1 238 ? -57.453 22.055  -18.354 1.00 72.80  ? 254 LYS   A NZ  1 
ATOM   1900 N  N   . ASN   A 1 239 ? -58.724 16.579  -14.769 1.00 39.11  ? 255 ASN   A N   1 
ATOM   1901 C  CA  . ASN   A 1 239 ? -59.827 15.671  -15.050 1.00 40.58  ? 255 ASN   A CA  1 
ATOM   1902 C  C   . ASN   A 1 239 ? -60.166 14.821  -13.835 1.00 38.76  ? 255 ASN   A C   1 
ATOM   1903 O  O   . ASN   A 1 239 ? -61.340 14.650  -13.503 1.00 42.36  ? 255 ASN   A O   1 
ATOM   1904 C  CB  . ASN   A 1 239 ? -59.475 14.763  -16.232 1.00 40.45  ? 255 ASN   A CB  1 
ATOM   1905 C  CG  . ASN   A 1 239 ? -59.682 15.449  -17.558 1.00 47.38  ? 255 ASN   A CG  1 
ATOM   1906 O  OD1 . ASN   A 1 239 ? -60.796 15.504  -18.061 1.00 46.72  ? 255 ASN   A OD1 1 
ATOM   1907 N  ND2 . ASN   A 1 239 ? -58.610 15.978  -18.127 1.00 42.87  ? 255 ASN   A ND2 1 
ATOM   1908 N  N   . ALA   A 1 240 ? -59.149 14.300  -13.143 1.00 37.21  ? 256 ALA   A N   1 
ATOM   1909 C  CA  . ALA   A 1 240 ? -59.416 13.412  -12.011 1.00 42.51  ? 256 ALA   A CA  1 
ATOM   1910 C  C   . ALA   A 1 240 ? -60.068 14.143  -10.839 1.00 45.90  ? 256 ALA   A C   1 
ATOM   1911 O  O   . ALA   A 1 240 ? -60.872 13.546  -10.101 1.00 42.82  ? 256 ALA   A O   1 
ATOM   1912 C  CB  . ALA   A 1 240 ? -58.119 12.741  -11.560 1.00 39.24  ? 256 ALA   A CB  1 
ATOM   1913 N  N   . MET   A 1 241 ? -59.726 15.416  -10.627 1.00 45.42  ? 257 MET   A N   1 
ATOM   1914 C  CA  . MET   A 1 241 ? -60.311 16.139  -9.501  1.00 44.21  ? 257 MET   A CA  1 
ATOM   1915 C  C   . MET   A 1 241 ? -61.760 16.499  -9.781  1.00 44.93  ? 257 MET   A C   1 
ATOM   1916 O  O   . MET   A 1 241 ? -62.631 16.320  -8.922  1.00 47.65  ? 257 MET   A O   1 
ATOM   1917 C  CB  . MET   A 1 241 ? -59.503 17.400  -9.208  1.00 44.77  ? 257 MET   A CB  1 
ATOM   1918 C  CG  . MET   A 1 241 ? -58.146 17.110  -8.673  1.00 47.84  ? 257 MET   A CG  1 
ATOM   1919 S  SD  . MET   A 1 241 ? -57.289 18.645  -8.354  1.00 62.04  ? 257 MET   A SD  1 
ATOM   1920 C  CE  . MET   A 1 241 ? -55.805 17.959  -7.694  1.00 45.65  ? 257 MET   A CE  1 
ATOM   1921 N  N   . ARG   A 1 242 ? -62.028 17.043  -10.974 1.00 43.39  ? 258 ARG   A N   1 
ATOM   1922 C  CA  . ARG   A 1 242 ? -63.400 17.373  -11.352 1.00 49.07  ? 258 ARG   A CA  1 
ATOM   1923 C  C   . ARG   A 1 242 ? -64.291 16.138  -11.323 1.00 50.20  ? 258 ARG   A C   1 
ATOM   1924 O  O   . ARG   A 1 242 ? -65.421 16.186  -10.822 1.00 50.28  ? 258 ARG   A O   1 
ATOM   1925 C  CB  . ARG   A 1 242 ? -63.404 18.025  -12.741 1.00 49.68  ? 258 ARG   A CB  1 
ATOM   1926 C  CG  . ARG   A 1 242 ? -64.752 18.039  -13.464 1.00 56.66  ? 258 ARG   A CG  1 
ATOM   1927 C  CD  . ARG   A 1 242 ? -64.675 18.853  -14.781 1.00 61.34  ? 258 ARG   A CD  1 
ATOM   1928 N  NE  . ARG   A 1 242 ? -63.880 18.183  -15.811 1.00 71.53  ? 258 ARG   A NE  1 
ATOM   1929 C  CZ  . ARG   A 1 242 ? -62.878 18.727  -16.500 1.00 70.17  ? 258 ARG   A CZ  1 
ATOM   1930 N  NH1 . ARG   A 1 242 ? -62.510 19.987  -16.328 1.00 73.12  ? 258 ARG   A NH1 1 
ATOM   1931 N  NH2 . ARG   A 1 242 ? -62.239 17.991  -17.401 1.00 67.09  ? 258 ARG   A NH2 1 
ATOM   1932 N  N   . ALA   A 1 243 ? -63.783 15.013  -11.831 1.00 44.31  ? 259 ALA   A N   1 
ATOM   1933 C  CA  . ALA   A 1 243 ? -64.539 13.770  -11.786 1.00 46.53  ? 259 ALA   A CA  1 
ATOM   1934 C  C   . ALA   A 1 243 ? -64.791 13.321  -10.354 1.00 47.39  ? 259 ALA   A C   1 
ATOM   1935 O  O   . ALA   A 1 243 ? -65.887 12.849  -10.034 1.00 46.68  ? 259 ALA   A O   1 
ATOM   1936 C  CB  . ALA   A 1 243 ? -63.795 12.680  -12.554 1.00 42.92  ? 259 ALA   A CB  1 
ATOM   1937 N  N   . THR   A 1 244 ? -63.789 13.448  -9.476  1.00 41.39  ? 260 THR   A N   1 
ATOM   1938 C  CA  . THR   A 1 244 ? -63.990 13.011  -8.102  1.00 46.28  ? 260 THR   A CA  1 
ATOM   1939 C  C   . THR   A 1 244 ? -65.027 13.887  -7.395  1.00 51.51  ? 260 THR   A C   1 
ATOM   1940 O  O   . THR   A 1 244 ? -65.915 13.370  -6.709  1.00 47.45  ? 260 THR   A O   1 
ATOM   1941 C  CB  . THR   A 1 244 ? -62.664 13.016  -7.333  1.00 43.43  ? 260 THR   A CB  1 
ATOM   1942 O  OG1 . THR   A 1 244 ? -61.728 12.143  -7.966  1.00 44.50  ? 260 THR   A OG1 1 
ATOM   1943 C  CG2 . THR   A 1 244 ? -62.880 12.568  -5.863  1.00 46.30  ? 260 THR   A CG2 1 
ATOM   1944 N  N   . VAL   A 1 245 ? -64.947 15.209  -7.570  1.00 49.04  ? 261 VAL   A N   1 
ATOM   1945 C  CA  . VAL   A 1 245 ? -65.886 16.106  -6.890  1.00 55.64  ? 261 VAL   A CA  1 
ATOM   1946 C  C   . VAL   A 1 245 ? -67.305 15.895  -7.413  1.00 59.51  ? 261 VAL   A C   1 
ATOM   1947 O  O   . VAL   A 1 245 ? -68.251 15.719  -6.639  1.00 57.11  ? 261 VAL   A O   1 
ATOM   1948 C  CB  . VAL   A 1 245 ? -65.443 17.574  -7.052  1.00 55.73  ? 261 VAL   A CB  1 
ATOM   1949 C  CG1 . VAL   A 1 245 ? -66.480 18.509  -6.430  1.00 58.92  ? 261 VAL   A CG1 1 
ATOM   1950 C  CG2 . VAL   A 1 245 ? -64.067 17.796  -6.428  1.00 53.97  ? 261 VAL   A CG2 1 
ATOM   1951 N  N   . GLU   A 1 246 ? -67.471 15.893  -8.737  1.00 56.18  ? 262 GLU   A N   1 
ATOM   1952 C  CA  . GLU   A 1 246 ? -68.809 15.831  -9.317  1.00 61.07  ? 262 GLU   A CA  1 
ATOM   1953 C  C   . GLU   A 1 246 ? -69.497 14.498  -9.046  1.00 61.73  ? 262 GLU   A C   1 
ATOM   1954 O  O   . GLU   A 1 246 ? -70.726 14.454  -8.923  1.00 66.78  ? 262 GLU   A O   1 
ATOM   1955 C  CB  . GLU   A 1 246 ? -68.729 16.124  -10.817 1.00 58.71  ? 262 GLU   A CB  1 
ATOM   1956 C  CG  . GLU   A 1 246 ? -68.290 17.576  -11.085 1.00 58.85  ? 262 GLU   A CG  1 
ATOM   1957 C  CD  . GLU   A 1 246 ? -68.419 18.019  -12.528 1.00 63.21  ? 262 GLU   A CD  1 
ATOM   1958 O  OE1 . GLU   A 1 246 ? -68.341 17.173  -13.444 1.00 68.53  ? 262 GLU   A OE1 1 
ATOM   1959 O  OE2 . GLU   A 1 246 ? -68.586 19.236  -12.746 1.00 69.29  ? 262 GLU   A OE2 1 
ATOM   1960 N  N   . SER   A 1 247 ? -68.740 13.411  -8.926  1.00 56.13  ? 263 SER   A N   1 
ATOM   1961 C  CA  . SER   A 1 247 ? -69.364 12.129  -8.625  1.00 57.89  ? 263 SER   A CA  1 
ATOM   1962 C  C   . SER   A 1 247 ? -69.689 11.949  -7.144  1.00 62.65  ? 263 SER   A C   1 
ATOM   1963 O  O   . SER   A 1 247 ? -70.302 10.934  -6.783  1.00 64.56  ? 263 SER   A O   1 
ATOM   1964 C  CB  . SER   A 1 247 ? -68.456 10.991  -9.087  1.00 54.96  ? 263 SER   A CB  1 
ATOM   1965 O  OG  . SER   A 1 247 ? -67.345 10.891  -8.223  1.00 54.07  ? 263 SER   A OG  1 
ATOM   1966 N  N   . HIS   A 1 248 ? -69.280 12.883  -6.279  1.00 63.88  ? 264 HIS   A N   1 
ATOM   1967 C  CA  . HIS   A 1 248 ? -69.506 12.776  -4.841  1.00 67.27  ? 264 HIS   A CA  1 
ATOM   1968 C  C   . HIS   A 1 248 ? -70.268 13.981  -4.304  1.00 72.26  ? 264 HIS   A C   1 
ATOM   1969 O  O   . HIS   A 1 248 ? -70.018 14.425  -3.185  1.00 69.37  ? 264 HIS   A O   1 
ATOM   1970 C  CB  . HIS   A 1 248 ? -68.189 12.606  -4.081  1.00 62.22  ? 264 HIS   A CB  1 
ATOM   1971 C  CG  . HIS   A 1 248 ? -67.525 11.281  -4.303  1.00 63.89  ? 264 HIS   A CG  1 
ATOM   1972 N  ND1 . HIS   A 1 248 ? -66.853 10.968  -5.467  1.00 59.37  ? 264 HIS   A ND1 1 
ATOM   1973 C  CD2 . HIS   A 1 248 ? -67.413 10.192  -3.505  1.00 61.85  ? 264 HIS   A CD2 1 
ATOM   1974 C  CE1 . HIS   A 1 248 ? -66.365 9.743   -5.382  1.00 52.44  ? 264 HIS   A CE1 1 
ATOM   1975 N  NE2 . HIS   A 1 248 ? -66.696 9.247   -4.205  1.00 60.52  ? 264 HIS   A NE2 1 
ATOM   1976 N  N   . GLU   A 1 249 ? -71.199 14.519  -5.099  1.00 89.25  ? 265 GLU   A N   1 
ATOM   1977 C  CA  . GLU   A 1 249 ? -71.991 15.664  -4.665  1.00 91.49  ? 265 GLU   A CA  1 
ATOM   1978 C  C   . GLU   A 1 249 ? -72.634 15.410  -3.312  1.00 90.96  ? 265 GLU   A C   1 
ATOM   1979 O  O   . GLU   A 1 249 ? -72.711 16.312  -2.473  1.00 96.27  ? 265 GLU   A O   1 
ATOM   1980 C  CB  . GLU   A 1 249 ? -73.077 15.983  -5.698  1.00 89.81  ? 265 GLU   A CB  1 
ATOM   1981 C  CG  . GLU   A 1 249 ? -72.591 16.201  -7.122  1.00 92.96  ? 265 GLU   A CG  1 
ATOM   1982 C  CD  . GLU   A 1 249 ? -71.944 17.557  -7.345  1.00 95.69  ? 265 GLU   A CD  1 
ATOM   1983 O  OE1 . GLU   A 1 249 ? -71.583 18.221  -6.348  1.00 98.17  ? 265 GLU   A OE1 1 
ATOM   1984 O  OE2 . GLU   A 1 249 ? -71.799 17.961  -8.524  1.00 93.29  ? 265 GLU   A OE2 1 
ATOM   1985 N  N   . SER   A 1 250 ? -73.079 14.180  -3.077  1.00 82.56  ? 266 SER   A N   1 
ATOM   1986 C  CA  . SER   A 1 250 ? -73.837 13.820  -1.891  1.00 89.02  ? 266 SER   A CA  1 
ATOM   1987 C  C   . SER   A 1 250 ? -72.987 13.122  -0.840  1.00 86.13  ? 266 SER   A C   1 
ATOM   1988 O  O   . SER   A 1 250 ? -73.522 12.667  0.176   1.00 90.41  ? 266 SER   A O   1 
ATOM   1989 C  CB  . SER   A 1 250 ? -75.021 12.940  -2.289  1.00 97.25  ? 266 SER   A CB  1 
ATOM   1990 O  OG  . SER   A 1 250 ? -75.612 13.422  -3.488  1.00 102.92 ? 266 SER   A OG  1 
ATOM   1991 N  N   . SER   A 1 251 ? -71.682 13.035  -1.055  1.00 84.11  ? 267 SER   A N   1 
ATOM   1992 C  CA  . SER   A 1 251 ? -70.764 12.468  -0.079  1.00 83.70  ? 267 SER   A CA  1 
ATOM   1993 C  C   . SER   A 1 251 ? -70.035 13.579  0.663   1.00 84.72  ? 267 SER   A C   1 
ATOM   1994 O  O   . SER   A 1 251 ? -69.855 14.688  0.148   1.00 84.30  ? 267 SER   A O   1 
ATOM   1995 C  CB  . SER   A 1 251 ? -69.742 11.548  -0.753  1.00 75.46  ? 267 SER   A CB  1 
ATOM   1996 O  OG  . SER   A 1 251 ? -70.251 10.235  -0.889  1.00 78.86  ? 267 SER   A OG  1 
ATOM   1997 N  N   . LEU   A 1 252 ? -69.605 13.265  1.884   1.00 87.07  ? 268 LEU   A N   1 
ATOM   1998 C  CA  . LEU   A 1 252 ? -68.811 14.191  2.679   1.00 88.76  ? 268 LEU   A CA  1 
ATOM   1999 C  C   . LEU   A 1 252 ? -67.317 13.967  2.474   1.00 88.86  ? 268 LEU   A C   1 
ATOM   2000 O  O   . LEU   A 1 252 ? -66.564 14.930  2.286   1.00 87.54  ? 268 LEU   A O   1 
ATOM   2001 C  CB  . LEU   A 1 252 ? -69.182 14.049  4.158   1.00 90.51  ? 268 LEU   A CB  1 
ATOM   2002 C  CG  . LEU   A 1 252 ? -70.674 14.239  4.439   1.00 88.16  ? 268 LEU   A CG  1 
ATOM   2003 C  CD1 . LEU   A 1 252 ? -71.047 13.864  5.875   1.00 86.70  ? 268 LEU   A CD1 1 
ATOM   2004 C  CD2 . LEU   A 1 252 ? -71.087 15.671  4.125   1.00 84.14  ? 268 LEU   A CD2 1 
ATOM   2005 N  N   . ILE   A 1 253 ? -66.878 12.712  2.488   1.00 95.53  ? 269 ILE   A N   1 
ATOM   2006 C  CA  . ILE   A 1 253 ? -65.478 12.376  2.241   1.00 94.12  ? 269 ILE   A CA  1 
ATOM   2007 C  C   . ILE   A 1 253 ? -65.215 12.378  0.739   1.00 86.37  ? 269 ILE   A C   1 
ATOM   2008 O  O   . ILE   A 1 253 ? -65.977 11.790  -0.039  1.00 84.63  ? 269 ILE   A O   1 
ATOM   2009 C  CB  . ILE   A 1 253 ? -65.133 11.008  2.855   1.00 97.23  ? 269 ILE   A CB  1 
ATOM   2010 C  CG1 . ILE   A 1 253 ? -65.652 10.899  4.295   1.00 101.23 ? 269 ILE   A CG1 1 
ATOM   2011 C  CG2 . ILE   A 1 253 ? -63.633 10.757  2.788   1.00 97.07  ? 269 ILE   A CG2 1 
ATOM   2012 C  CD1 . ILE   A 1 253 ? -65.673 9.466   4.836   1.00 108.70 ? 269 ILE   A CD1 1 
ATOM   2013 N  N   . LEU   A 1 254 ? -64.130 13.058  0.318   1.00 73.52  ? 270 LEU   A N   1 
ATOM   2014 C  CA  . LEU   A 1 254 ? -63.643 12.890  -1.048  1.00 66.45  ? 270 LEU   A CA  1 
ATOM   2015 C  C   . LEU   A 1 254 ? -62.516 11.879  -1.052  1.00 61.89  ? 270 LEU   A C   1 
ATOM   2016 O  O   . LEU   A 1 254 ? -61.548 12.052  -0.295  1.00 61.07  ? 270 LEU   A O   1 
ATOM   2017 C  CB  . LEU   A 1 254 ? -63.133 14.206  -1.633  1.00 65.22  ? 270 LEU   A CB  1 
ATOM   2018 C  CG  . LEU   A 1 254 ? -64.112 15.285  -2.085  1.00 64.53  ? 270 LEU   A CG  1 
ATOM   2019 C  CD1 . LEU   A 1 254 ? -63.347 16.536  -2.534  1.00 58.30  ? 270 LEU   A CD1 1 
ATOM   2020 C  CD2 . LEU   A 1 254 ? -64.955 14.737  -3.207  1.00 62.19  ? 270 LEU   A CD2 1 
ATOM   2021 N  N   . PRO   A 1 255 ? -62.586 10.825  -1.863  1.00 56.16  ? 271 PRO   A N   1 
ATOM   2022 C  CA  . PRO   A 1 255 ? -61.430 9.941   -2.030  1.00 57.90  ? 271 PRO   A CA  1 
ATOM   2023 C  C   . PRO   A 1 255 ? -60.230 10.724  -2.529  1.00 53.98  ? 271 PRO   A C   1 
ATOM   2024 O  O   . PRO   A 1 255 ? -60.372 11.685  -3.304  1.00 53.15  ? 271 PRO   A O   1 
ATOM   2025 C  CB  . PRO   A 1 255 ? -61.906 8.929   -3.083  1.00 55.18  ? 271 PRO   A CB  1 
ATOM   2026 C  CG  . PRO   A 1 255 ? -63.383 9.000   -3.053  1.00 56.87  ? 271 PRO   A CG  1 
ATOM   2027 C  CD  . PRO   A 1 255 ? -63.726 10.410  -2.696  1.00 55.85  ? 271 PRO   A CD  1 
ATOM   2028 N  N   . PRO   A 1 256 ? -59.029 10.356  -2.105  1.00 55.98  ? 272 PRO   A N   1 
ATOM   2029 C  CA  . PRO   A 1 256 ? -57.831 11.005  -2.645  1.00 50.52  ? 272 PRO   A CA  1 
ATOM   2030 C  C   . PRO   A 1 256 ? -57.555 10.541  -4.064  1.00 49.73  ? 272 PRO   A C   1 
ATOM   2031 O  O   . PRO   A 1 256 ? -58.120 9.573   -4.571  1.00 49.00  ? 272 PRO   A O   1 
ATOM   2032 C  CB  . PRO   A 1 256 ? -56.719 10.567  -1.689  1.00 52.26  ? 272 PRO   A CB  1 
ATOM   2033 C  CG  . PRO   A 1 256 ? -57.213 9.246   -1.150  1.00 58.14  ? 272 PRO   A CG  1 
ATOM   2034 C  CD  . PRO   A 1 256 ? -58.713 9.378   -1.050  1.00 55.72  ? 272 PRO   A CD  1 
ATOM   2035 N  N   . ILE   A 1 257 ? -56.672 11.276  -4.714  1.00 50.81  ? 273 ILE   A N   1 
ATOM   2036 C  CA  . ILE   A 1 257 ? -56.070 10.849  -5.964  1.00 45.57  ? 273 ILE   A CA  1 
ATOM   2037 C  C   . ILE   A 1 257 ? -54.722 10.232  -5.636  1.00 51.02  ? 273 ILE   A C   1 
ATOM   2038 O  O   . ILE   A 1 257 ? -53.917 10.830  -4.906  1.00 46.26  ? 273 ILE   A O   1 
ATOM   2039 C  CB  . ILE   A 1 257 ? -55.944 12.023  -6.940  1.00 47.71  ? 273 ILE   A CB  1 
ATOM   2040 C  CG1 . ILE   A 1 257 ? -57.362 12.517  -7.272  1.00 41.94  ? 273 ILE   A CG1 1 
ATOM   2041 C  CG2 . ILE   A 1 257 ? -55.196 11.565  -8.210  1.00 45.10  ? 273 ILE   A CG2 1 
ATOM   2042 C  CD1 . ILE   A 1 257 ? -57.413 13.760  -8.019  1.00 43.44  ? 273 ILE   A CD1 1 
ATOM   2043 N  N   . LYS   A 1 258 ? -54.479 9.029   -6.146  1.00 46.44  ? 274 LYS   A N   1 
ATOM   2044 C  CA  . LYS   A 1 258 ? -53.270 8.282   -5.820  1.00 48.21  ? 274 LYS   A CA  1 
ATOM   2045 C  C   . LYS   A 1 258 ? -52.341 8.264   -7.021  1.00 50.83  ? 274 LYS   A C   1 
ATOM   2046 O  O   . LYS   A 1 258 ? -52.798 8.140   -8.164  1.00 44.41  ? 274 LYS   A O   1 
ATOM   2047 C  CB  . LYS   A 1 258 ? -53.601 6.848   -5.399  1.00 48.46  ? 274 LYS   A CB  1 
ATOM   2048 C  CG  . LYS   A 1 258 ? -54.396 6.752   -4.090  1.00 50.95  ? 274 LYS   A CG  1 
ATOM   2049 C  CD  . LYS   A 1 258 ? -54.699 5.291   -3.757  1.00 53.92  ? 274 LYS   A CD  1 
ATOM   2050 C  CE  . LYS   A 1 258 ? -55.276 5.156   -2.359  1.00 63.86  ? 274 LYS   A CE  1 
ATOM   2051 N  NZ  . LYS   A 1 258 ? -55.490 3.727   -1.967  1.00 72.26  ? 274 LYS   A NZ  1 
ATOM   2052 N  N   . VAL   A 1 259 ? -51.041 8.396   -6.763  1.00 46.51  ? 275 VAL   A N   1 
ATOM   2053 C  CA  . VAL   A 1 259 ? -50.031 8.352   -7.811  1.00 43.32  ? 275 VAL   A CA  1 
ATOM   2054 C  C   . VAL   A 1 259 ? -48.965 7.356   -7.391  1.00 47.51  ? 275 VAL   A C   1 
ATOM   2055 O  O   . VAL   A 1 259 ? -48.457 7.425   -6.267  1.00 47.12  ? 275 VAL   A O   1 
ATOM   2056 C  CB  . VAL   A 1 259 ? -49.395 9.725   -8.091  1.00 45.57  ? 275 VAL   A CB  1 
ATOM   2057 C  CG1 . VAL   A 1 259 ? -48.312 9.590   -9.129  1.00 41.95  ? 275 VAL   A CG1 1 
ATOM   2058 C  CG2 . VAL   A 1 259 ? -50.439 10.714  -8.586  1.00 45.81  ? 275 VAL   A CG2 1 
ATOM   2059 N  N   . MET   A 1 260 ? -48.624 6.435   -8.293  1.00 43.72  ? 276 MET   A N   1 
ATOM   2060 C  CA  . MET   A 1 260 ? -47.489 5.536   -8.120  1.00 47.90  ? 276 MET   A CA  1 
ATOM   2061 C  C   . MET   A 1 260 ? -46.447 5.909   -9.171  1.00 50.64  ? 276 MET   A C   1 
ATOM   2062 O  O   . MET   A 1 260 ? -46.773 6.025   -10.353 1.00 44.94  ? 276 MET   A O   1 
ATOM   2063 C  CB  . MET   A 1 260 ? -47.933 4.069   -8.257  1.00 46.81  ? 276 MET   A CB  1 
ATOM   2064 C  CG  . MET   A 1 260 ? -46.819 2.997   -8.255  1.00 51.70  ? 276 MET   A CG  1 
ATOM   2065 S  SD  . MET   A 1 260 ? -46.143 2.742   -6.602  1.00 74.22  ? 276 MET   A SD  1 
ATOM   2066 C  CE  . MET   A 1 260 ? -47.471 1.847   -5.781  1.00 61.17  ? 276 MET   A CE  1 
ATOM   2067 N  N   . VAL   A 1 261 ? -45.214 6.146   -8.740  1.00 47.66  ? 277 VAL   A N   1 
ATOM   2068 C  CA  . VAL   A 1 261 ? -44.105 6.380   -9.654  1.00 47.05  ? 277 VAL   A CA  1 
ATOM   2069 C  C   . VAL   A 1 261 ? -43.206 5.153   -9.586  1.00 48.89  ? 277 VAL   A C   1 
ATOM   2070 O  O   . VAL   A 1 261 ? -42.643 4.865   -8.531  1.00 49.39  ? 277 VAL   A O   1 
ATOM   2071 C  CB  . VAL   A 1 261 ? -43.327 7.655   -9.295  1.00 50.32  ? 277 VAL   A CB  1 
ATOM   2072 C  CG1 . VAL   A 1 261 ? -42.137 7.838   -10.243 1.00 43.48  ? 277 VAL   A CG1 1 
ATOM   2073 C  CG2 . VAL   A 1 261 ? -44.252 8.887   -9.311  1.00 45.12  ? 277 VAL   A CG2 1 
ATOM   2074 N  N   . ALA   A 1 262 ? -43.068 4.433   -10.706 1.00 45.60  ? 278 ALA   A N   1 
ATOM   2075 C  CA  . ALA   A 1 262 ? -42.267 3.211   -10.770 1.00 50.67  ? 278 ALA   A CA  1 
ATOM   2076 C  C   . ALA   A 1 262 ? -41.124 3.369   -11.766 1.00 48.15  ? 278 ALA   A C   1 
ATOM   2077 O  O   . ALA   A 1 262 ? -41.307 3.934   -12.845 1.00 44.02  ? 278 ALA   A O   1 
ATOM   2078 C  CB  . ALA   A 1 262 ? -43.122 1.997   -11.171 1.00 47.09  ? 278 ALA   A CB  1 
ATOM   2079 N  N   . LEU   A 1 263 ? -39.945 2.857   -11.411 1.00 49.14  ? 279 LEU   A N   1 
ATOM   2080 C  CA  . LEU   A 1 263 ? -38.781 2.921   -12.285 1.00 50.07  ? 279 LEU   A CA  1 
ATOM   2081 C  C   . LEU   A 1 263 ? -38.301 1.507   -12.559 1.00 48.87  ? 279 LEU   A C   1 
ATOM   2082 O  O   . LEU   A 1 263 ? -37.884 0.813   -11.632 1.00 49.75  ? 279 LEU   A O   1 
ATOM   2083 C  CB  . LEU   A 1 263 ? -37.659 3.743   -11.653 1.00 50.39  ? 279 LEU   A CB  1 
ATOM   2084 C  CG  . LEU   A 1 263 ? -36.367 3.815   -12.468 1.00 47.64  ? 279 LEU   A CG  1 
ATOM   2085 C  CD1 . LEU   A 1 263 ? -36.609 4.589   -13.746 1.00 46.86  ? 279 LEU   A CD1 1 
ATOM   2086 C  CD2 . LEU   A 1 263 ? -35.251 4.471   -11.656 1.00 50.51  ? 279 LEU   A CD2 1 
ATOM   2087 N  N   . GLY   A 1 264 ? -38.379 1.074   -13.824 1.00 45.11  ? 280 GLY   A N   1 
ATOM   2088 C  CA  . GLY   A 1 264 ? -37.855 -0.205  -14.245 1.00 49.40  ? 280 GLY   A CA  1 
ATOM   2089 C  C   . GLY   A 1 264 ? -36.596 -0.081  -15.093 1.00 50.56  ? 280 GLY   A C   1 
ATOM   2090 O  O   . GLY   A 1 264 ? -35.997 0.988   -15.220 1.00 50.51  ? 280 GLY   A O   1 
ATOM   2091 N  N   . GLU   A 1 265 ? -36.209 -1.209  -15.706 1.00 49.32  ? 281 GLU   A N   1 
ATOM   2092 C  CA  . GLU   A 1 265 ? -35.014 -1.211  -16.552 1.00 52.28  ? 281 GLU   A CA  1 
ATOM   2093 C  C   . GLU   A 1 265 ? -35.212 -0.389  -17.818 1.00 48.85  ? 281 GLU   A C   1 
ATOM   2094 O  O   . GLU   A 1 265 ? -34.250 0.188   -18.340 1.00 51.04  ? 281 GLU   A O   1 
ATOM   2095 C  CB  . GLU   A 1 265 ? -34.612 -2.639  -16.938 1.00 50.49  ? 281 GLU   A CB  1 
ATOM   2096 C  CG  . GLU   A 1 265 ? -34.091 -3.483  -15.782 1.00 67.27  ? 281 GLU   A CG  1 
ATOM   2097 C  CD  . GLU   A 1 265 ? -33.004 -2.772  -14.990 1.00 74.51  ? 281 GLU   A CD  1 
ATOM   2098 O  OE1 . GLU   A 1 265 ? -31.929 -2.483  -15.568 1.00 73.86  ? 281 GLU   A OE1 1 
ATOM   2099 O  OE2 . GLU   A 1 265 ? -33.238 -2.487  -13.793 1.00 72.08  ? 281 GLU   A OE2 1 
ATOM   2100 N  N   . GLU   A 1 266 ? -36.429 -0.350  -18.343 1.00 48.63  ? 282 GLU   A N   1 
ATOM   2101 C  CA  . GLU   A 1 266 ? -36.704 0.359   -19.576 1.00 47.97  ? 282 GLU   A CA  1 
ATOM   2102 C  C   . GLU   A 1 266 ? -37.777 1.436   -19.436 1.00 46.85  ? 282 GLU   A C   1 
ATOM   2103 O  O   . GLU   A 1 266 ? -37.667 2.496   -20.074 1.00 43.29  ? 282 GLU   A O   1 
ATOM   2104 C  CB  . GLU   A 1 266 ? -37.098 -0.661  -20.671 1.00 46.63  ? 282 GLU   A CB  1 
ATOM   2105 C  CG  . GLU   A 1 266 ? -37.710 -0.043  -21.909 1.00 54.42  ? 282 GLU   A CG  1 
ATOM   2106 C  CD  . GLU   A 1 266 ? -37.925 -1.053  -23.035 1.00 54.24  ? 282 GLU   A CD  1 
ATOM   2107 O  OE1 . GLU   A 1 266 ? -37.253 -2.096  -23.051 1.00 51.08  ? 282 GLU   A OE1 1 
ATOM   2108 O  OE2 . GLU   A 1 266 ? -38.778 -0.784  -23.903 1.00 56.88  ? 282 GLU   A OE2 1 
ATOM   2109 N  N   . ASP   A 1 267 ? -38.786 1.225   -18.596 1.00 43.92  ? 283 ASP   A N   1 
ATOM   2110 C  CA  . ASP   A 1 267 ? -39.863 2.191   -18.426 1.00 42.36  ? 283 ASP   A CA  1 
ATOM   2111 C  C   . ASP   A 1 267 ? -39.723 2.955   -17.124 1.00 45.14  ? 283 ASP   A C   1 
ATOM   2112 O  O   . ASP   A 1 267 ? -39.348 2.396   -16.089 1.00 44.52  ? 283 ASP   A O   1 
ATOM   2113 C  CB  . ASP   A 1 267 ? -41.236 1.532   -18.415 1.00 41.12  ? 283 ASP   A CB  1 
ATOM   2114 C  CG  . ASP   A 1 267 ? -41.541 0.757   -19.679 1.00 44.39  ? 283 ASP   A CG  1 
ATOM   2115 O  OD1 . ASP   A 1 267 ? -40.744 0.843   -20.635 1.00 46.20  ? 283 ASP   A OD1 1 
ATOM   2116 O  OD2 . ASP   A 1 267 ? -42.583 0.050   -19.706 1.00 41.08  ? 283 ASP   A OD2 1 
ATOM   2117 N  N   . LEU   A 1 268 ? -40.094 4.221   -17.170 1.00 42.87  ? 284 LEU   A N   1 
ATOM   2118 C  CA  . LEU   A 1 268 ? -40.483 4.960   -15.980 1.00 35.92  ? 284 LEU   A CA  1 
ATOM   2119 C  C   . LEU   A 1 268 ? -41.972 5.221   -16.116 1.00 38.60  ? 284 LEU   A C   1 
ATOM   2120 O  O   . LEU   A 1 268 ? -42.388 5.900   -17.055 1.00 39.07  ? 284 LEU   A O   1 
ATOM   2121 C  CB  . LEU   A 1 268 ? -39.705 6.270   -15.854 1.00 41.77  ? 284 LEU   A CB  1 
ATOM   2122 C  CG  . LEU   A 1 268 ? -39.761 6.975   -14.483 1.00 46.68  ? 284 LEU   A CG  1 
ATOM   2123 C  CD1 . LEU   A 1 268 ? -38.525 7.831   -14.321 1.00 46.49  ? 284 LEU   A CD1 1 
ATOM   2124 C  CD2 . LEU   A 1 268 ? -41.010 7.846   -14.369 1.00 45.63  ? 284 LEU   A CD2 1 
ATOM   2125 N  N   . SER   A 1 269 ? -42.777 4.650   -15.223 1.00 39.20  ? 285 SER   A N   1 
ATOM   2126 C  CA  . SER   A 1 269 ? -44.221 4.740   -15.341 1.00 39.48  ? 285 SER   A CA  1 
ATOM   2127 C  C   . SER   A 1 269 ? -44.797 5.543   -14.181 1.00 43.50  ? 285 SER   A C   1 
ATOM   2128 O  O   . SER   A 1 269 ? -44.367 5.393   -13.036 1.00 42.78  ? 285 SER   A O   1 
ATOM   2129 C  CB  . SER   A 1 269 ? -44.844 3.353   -15.390 1.00 36.11  ? 285 SER   A CB  1 
ATOM   2130 O  OG  . SER   A 1 269 ? -44.096 2.481   -16.225 1.00 42.08  ? 285 SER   A OG  1 
ATOM   2131 N  N   . ILE   A 1 270 ? -45.786 6.381   -14.488 1.00 40.21  ? 286 ILE   A N   1 
ATOM   2132 C  CA  . ILE   A 1 270 ? -46.504 7.194   -13.504 1.00 42.90  ? 286 ILE   A CA  1 
ATOM   2133 C  C   . ILE   A 1 270 ? -47.982 6.862   -13.649 1.00 43.36  ? 286 ILE   A C   1 
ATOM   2134 O  O   . ILE   A 1 270 ? -48.609 7.229   -14.653 1.00 40.54  ? 286 ILE   A O   1 
ATOM   2135 C  CB  . ILE   A 1 270 ? -46.265 8.700   -13.701 1.00 41.79  ? 286 ILE   A CB  1 
ATOM   2136 C  CG1 . ILE   A 1 270 ? -44.764 9.017   -13.739 1.00 40.82  ? 286 ILE   A CG1 1 
ATOM   2137 C  CG2 . ILE   A 1 270 ? -46.932 9.524   -12.583 1.00 39.71  ? 286 ILE   A CG2 1 
ATOM   2138 C  CD1 . ILE   A 1 270 ? -44.420 10.268  -14.529 1.00 46.72  ? 286 ILE   A CD1 1 
ATOM   2139 N  N   . LYS   A 1 271 ? -48.545 6.168   -12.664 1.00 37.88  ? 287 LYS   A N   1 
ATOM   2140 C  CA  . LYS   A 1 271 ? -49.962 5.844   -12.680 1.00 42.56  ? 287 LYS   A CA  1 
ATOM   2141 C  C   . LYS   A 1 271 ? -50.713 6.787   -11.751 1.00 46.53  ? 287 LYS   A C   1 
ATOM   2142 O  O   . LYS   A 1 271 ? -50.350 6.928   -10.580 1.00 43.86  ? 287 LYS   A O   1 
ATOM   2143 C  CB  . LYS   A 1 271 ? -50.217 4.405   -12.249 1.00 39.69  ? 287 LYS   A CB  1 
ATOM   2144 C  CG  . LYS   A 1 271 ? -51.715 4.039   -12.278 1.00 47.47  ? 287 LYS   A CG  1 
ATOM   2145 C  CD  . LYS   A 1 271 ? -51.962 2.548   -12.006 1.00 49.43  ? 287 LYS   A CD  1 
ATOM   2146 C  CE  . LYS   A 1 271 ? -51.746 2.229   -10.550 1.00 51.49  ? 287 LYS   A CE  1 
ATOM   2147 N  NZ  . LYS   A 1 271 ? -52.058 0.804   -10.227 1.00 62.54  ? 287 LYS   A NZ  1 
ATOM   2148 N  N   . MET   A 1 272 ? -51.764 7.410   -12.268 1.00 44.19  ? 288 MET   A N   1 
ATOM   2149 C  CA  . MET   A 1 272 ? -52.675 8.204   -11.456 1.00 43.30  ? 288 MET   A CA  1 
ATOM   2150 C  C   . MET   A 1 272 ? -54.022 7.490   -11.381 1.00 44.00  ? 288 MET   A C   1 
ATOM   2151 O  O   . MET   A 1 272 ? -54.481 6.934   -12.386 1.00 41.38  ? 288 MET   A O   1 
ATOM   2152 C  CB  . MET   A 1 272 ? -52.832 9.602   -12.057 1.00 41.42  ? 288 MET   A CB  1 
ATOM   2153 C  CG  . MET   A 1 272 ? -53.560 10.590  -11.159 1.00 36.35  ? 288 MET   A CG  1 
ATOM   2154 S  SD  . MET   A 1 272 ? -53.950 12.107  -12.043 1.00 40.60  ? 288 MET   A SD  1 
ATOM   2155 C  CE  . MET   A 1 272 ? -52.327 12.758  -12.477 1.00 34.92  ? 288 MET   A CE  1 
ATOM   2156 N  N   . SER   A 1 273 ? -54.661 7.513   -10.198 1.00 38.58  ? 289 SER   A N   1 
ATOM   2157 C  CA  . SER   A 1 273 ? -55.886 6.750   -9.958  1.00 45.36  ? 289 SER   A CA  1 
ATOM   2158 C  C   . SER   A 1 273 ? -56.928 7.616   -9.277  1.00 45.76  ? 289 SER   A C   1 
ATOM   2159 O  O   . SER   A 1 273 ? -56.628 8.267   -8.271  1.00 45.27  ? 289 SER   A O   1 
ATOM   2160 C  CB  . SER   A 1 273 ? -55.631 5.525   -9.061  1.00 44.92  ? 289 SER   A CB  1 
ATOM   2161 O  OG  . SER   A 1 273 ? -54.605 4.706   -9.607  1.00 49.77  ? 289 SER   A OG  1 
ATOM   2162 N  N   . ASP   A 1 274 ? -58.164 7.595   -9.783  1.00 41.90  ? 290 ASP   A N   1 
ATOM   2163 C  CA  . ASP   A 1 274 ? -59.234 8.322   -9.106  1.00 42.34  ? 290 ASP   A CA  1 
ATOM   2164 C  C   . ASP   A 1 274 ? -60.392 7.373   -8.831  1.00 45.03  ? 290 ASP   A C   1 
ATOM   2165 O  O   . ASP   A 1 274 ? -60.450 6.255   -9.356  1.00 43.50  ? 290 ASP   A O   1 
ATOM   2166 C  CB  . ASP   A 1 274 ? -59.686 9.575   -9.893  1.00 42.54  ? 290 ASP   A CB  1 
ATOM   2167 C  CG  . ASP   A 1 274 ? -60.519 9.272   -11.157 1.00 40.92  ? 290 ASP   A CG  1 
ATOM   2168 O  OD1 . ASP   A 1 274 ? -61.465 8.448   -11.117 1.00 42.39  ? 290 ASP   A OD1 1 
ATOM   2169 O  OD2 . ASP   A 1 274 ? -60.268 9.940   -12.191 1.00 42.97  ? 290 ASP   A OD2 1 
ATOM   2170 N  N   . ARG   A 1 275 ? -61.280 7.806   -7.937  1.00 42.98  ? 291 ARG   A N   1 
ATOM   2171 C  CA  . ARG   A 1 275 ? -62.538 7.110   -7.712  1.00 48.62  ? 291 ARG   A CA  1 
ATOM   2172 C  C   . ARG   A 1 275 ? -63.680 8.029   -8.114  1.00 48.92  ? 291 ARG   A C   1 
ATOM   2173 O  O   . ARG   A 1 275 ? -64.608 8.254   -7.329  1.00 48.14  ? 291 ARG   A O   1 
ATOM   2174 C  CB  . ARG   A 1 275 ? -62.671 6.663   -6.258  1.00 46.72  ? 291 ARG   A CB  1 
ATOM   2175 C  CG  . ARG   A 1 275 ? -61.588 5.682   -5.859  1.00 57.14  ? 291 ARG   A CG  1 
ATOM   2176 C  CD  . ARG   A 1 275 ? -61.850 5.038   -4.504  1.00 65.25  ? 291 ARG   A CD  1 
ATOM   2177 N  NE  . ARG   A 1 275 ? -60.785 4.086   -4.208  1.00 77.65  ? 291 ARG   A NE  1 
ATOM   2178 C  CZ  . ARG   A 1 275 ? -60.847 3.150   -3.270  1.00 77.30  ? 291 ARG   A CZ  1 
ATOM   2179 N  NH1 . ARG   A 1 275 ? -61.922 3.005   -2.511  1.00 84.36  ? 291 ARG   A NH1 1 
ATOM   2180 N  NH2 . ARG   A 1 275 ? -59.804 2.337   -3.093  1.00 74.79  ? 291 ARG   A NH2 1 
ATOM   2181 N  N   . GLY   A 1 276 ? -63.624 8.548   -9.342  1.00 44.78  ? 292 GLY   A N   1 
ATOM   2182 C  CA  . GLY   A 1 276 ? -64.592 9.533   -9.782  1.00 47.22  ? 292 GLY   A CA  1 
ATOM   2183 C  C   . GLY   A 1 276 ? -65.730 8.998   -10.638 1.00 49.03  ? 292 GLY   A C   1 
ATOM   2184 O  O   . GLY   A 1 276 ? -66.337 9.755   -11.396 1.00 48.03  ? 292 GLY   A O   1 
ATOM   2185 N  N   . GLY   A 1 277 ? -66.037 7.709   -10.541 1.00 45.74  ? 293 GLY   A N   1 
ATOM   2186 C  CA  . GLY   A 1 277 ? -67.190 7.146   -11.203 1.00 46.05  ? 293 GLY   A CA  1 
ATOM   2187 C  C   . GLY   A 1 277 ? -66.903 6.449   -12.524 1.00 46.53  ? 293 GLY   A C   1 
ATOM   2188 O  O   . GLY   A 1 277 ? -67.723 5.633   -12.961 1.00 47.45  ? 293 GLY   A O   1 
ATOM   2189 N  N   . GLY   A 1 278 ? -65.790 6.774   -13.193 1.00 41.44  ? 294 GLY   A N   1 
ATOM   2190 C  CA  . GLY   A 1 278 ? -65.401 6.029   -14.373 1.00 42.30  ? 294 GLY   A CA  1 
ATOM   2191 C  C   . GLY   A 1 278 ? -66.209 6.416   -15.604 1.00 46.65  ? 294 GLY   A C   1 
ATOM   2192 O  O   . GLY   A 1 278 ? -67.013 7.341   -15.594 1.00 45.73  ? 294 GLY   A O   1 
ATOM   2193 N  N   . VAL   A 1 279 ? -65.968 5.683   -16.684 1.00 41.36  ? 295 VAL   A N   1 
ATOM   2194 C  CA  . VAL   A 1 279 ? -66.576 5.949   -17.986 1.00 42.14  ? 295 VAL   A CA  1 
ATOM   2195 C  C   . VAL   A 1 279 ? -66.604 4.638   -18.774 1.00 39.48  ? 295 VAL   A C   1 
ATOM   2196 O  O   . VAL   A 1 279 ? -65.660 3.842   -18.677 1.00 38.53  ? 295 VAL   A O   1 
ATOM   2197 C  CB  . VAL   A 1 279 ? -65.806 7.061   -18.730 1.00 43.53  ? 295 VAL   A CB  1 
ATOM   2198 C  CG1 . VAL   A 1 279 ? -64.324 6.798   -18.668 1.00 40.48  ? 295 VAL   A CG1 1 
ATOM   2199 C  CG2 . VAL   A 1 279 ? -66.238 7.161   -20.201 1.00 47.74  ? 295 VAL   A CG2 1 
ATOM   2200 N  N   . PRO   A 1 280 ? -67.660 4.355   -19.534 1.00 39.97  ? 296 PRO   A N   1 
ATOM   2201 C  CA  . PRO   A 1 280 ? -67.726 3.075   -20.247 1.00 43.07  ? 296 PRO   A CA  1 
ATOM   2202 C  C   . PRO   A 1 280 ? -66.640 2.962   -21.304 1.00 44.19  ? 296 PRO   A C   1 
ATOM   2203 O  O   . PRO   A 1 280 ? -66.239 3.950   -21.928 1.00 45.19  ? 296 PRO   A O   1 
ATOM   2204 C  CB  . PRO   A 1 280 ? -69.129 3.075   -20.874 1.00 47.15  ? 296 PRO   A CB  1 
ATOM   2205 C  CG  . PRO   A 1 280 ? -69.660 4.428   -20.704 1.00 47.85  ? 296 PRO   A CG  1 
ATOM   2206 C  CD  . PRO   A 1 280 ? -68.924 5.104   -19.604 1.00 45.14  ? 296 PRO   A CD  1 
ATOM   2207 N  N   . LEU   A 1 281 ? -66.164 1.730   -21.494 1.00 40.54  ? 297 LEU   A N   1 
ATOM   2208 C  CA  . LEU   A 1 281 ? -65.071 1.481   -22.429 1.00 44.14  ? 297 LEU   A CA  1 
ATOM   2209 C  C   . LEU   A 1 281 ? -65.387 2.011   -23.827 1.00 46.05  ? 297 LEU   A C   1 
ATOM   2210 O  O   . LEU   A 1 281 ? -64.514 2.569   -24.495 1.00 42.11  ? 297 LEU   A O   1 
ATOM   2211 C  CB  . LEU   A 1 281 ? -64.767 -0.009  -22.482 1.00 39.60  ? 297 LEU   A CB  1 
ATOM   2212 C  CG  . LEU   A 1 281 ? -63.637 -0.429  -23.416 1.00 48.64  ? 297 LEU   A CG  1 
ATOM   2213 C  CD1 . LEU   A 1 281 ? -62.291 0.057   -22.870 1.00 40.57  ? 297 LEU   A CD1 1 
ATOM   2214 C  CD2 . LEU   A 1 281 ? -63.670 -1.954  -23.644 1.00 42.58  ? 297 LEU   A CD2 1 
ATOM   2215 N  N   . ARG   A 1 282 ? -66.637 1.881   -24.267 1.00 44.70  ? 298 ARG   A N   1 
ATOM   2216 C  CA  . ARG   A 1 282 ? -67.007 2.316   -25.613 1.00 48.42  ? 298 ARG   A CA  1 
ATOM   2217 C  C   . ARG   A 1 282 ? -66.774 3.818   -25.813 1.00 48.47  ? 298 ARG   A C   1 
ATOM   2218 O  O   . ARG   A 1 282 ? -66.516 4.267   -26.931 1.00 46.36  ? 298 ARG   A O   1 
ATOM   2219 C  CB  . ARG   A 1 282 ? -68.464 1.939   -25.878 1.00 48.70  ? 298 ARG   A CB  1 
ATOM   2220 C  CG  . ARG   A 1 282 ? -69.037 2.390   -27.210 1.00 56.34  ? 298 ARG   A CG  1 
ATOM   2221 C  CD  . ARG   A 1 282 ? -70.482 1.934   -27.319 1.00 55.32  ? 298 ARG   A CD  1 
ATOM   2222 N  NE  . ARG   A 1 282 ? -71.322 2.496   -26.266 1.00 57.21  ? 298 ARG   A NE  1 
ATOM   2223 C  CZ  . ARG   A 1 282 ? -72.024 3.615   -26.381 1.00 53.72  ? 298 ARG   A CZ  1 
ATOM   2224 N  NH1 . ARG   A 1 282 ? -71.981 4.351   -27.481 1.00 62.39  ? 298 ARG   A NH1 1 
ATOM   2225 N  NH2 . ARG   A 1 282 ? -72.788 4.008   -25.368 1.00 53.34  ? 298 ARG   A NH2 1 
ATOM   2226 N  N   . LYS   A 1 283 ? -66.806 4.604   -24.746 1.00 47.67  ? 299 LYS   A N   1 
ATOM   2227 C  CA  . LYS   A 1 283 ? -66.689 6.047   -24.897 1.00 47.86  ? 299 LYS   A CA  1 
ATOM   2228 C  C   . LYS   A 1 283 ? -65.294 6.595   -24.639 1.00 44.18  ? 299 LYS   A C   1 
ATOM   2229 O  O   . LYS   A 1 283 ? -65.010 7.720   -25.055 1.00 38.79  ? 299 LYS   A O   1 
ATOM   2230 C  CB  . LYS   A 1 283 ? -67.660 6.754   -23.947 1.00 40.63  ? 299 LYS   A CB  1 
ATOM   2231 C  CG  . LYS   A 1 283 ? -69.123 6.542   -24.300 1.00 47.32  ? 299 LYS   A CG  1 
ATOM   2232 C  CD  . LYS   A 1 283 ? -70.013 7.329   -23.323 1.00 54.54  ? 299 LYS   A CD  1 
ATOM   2233 C  CE  . LYS   A 1 283 ? -71.488 7.080   -23.576 1.00 62.61  ? 299 LYS   A CE  1 
ATOM   2234 N  NZ  . LYS   A 1 283 ? -72.317 7.753   -22.527 1.00 62.86  ? 299 LYS   A NZ  1 
ATOM   2235 N  N   . ILE   A 1 284 ? -64.417 5.851   -23.959 1.00 45.18  ? 300 ILE   A N   1 
ATOM   2236 C  CA  . ILE   A 1 284 ? -63.251 6.506   -23.361 1.00 41.36  ? 300 ILE   A CA  1 
ATOM   2237 C  C   . ILE   A 1 284 ? -62.320 7.093   -24.428 1.00 46.68  ? 300 ILE   A C   1 
ATOM   2238 O  O   . ILE   A 1 284 ? -61.732 8.162   -24.221 1.00 44.34  ? 300 ILE   A O   1 
ATOM   2239 C  CB  . ILE   A 1 284 ? -62.521 5.539   -22.402 1.00 42.98  ? 300 ILE   A CB  1 
ATOM   2240 C  CG1 . ILE   A 1 284 ? -61.573 6.307   -21.484 1.00 47.30  ? 300 ILE   A CG1 1 
ATOM   2241 C  CG2 . ILE   A 1 284 ? -61.764 4.453   -23.146 1.00 47.11  ? 300 ILE   A CG2 1 
ATOM   2242 C  CD1 . ILE   A 1 284 ? -61.068 5.457   -20.328 1.00 45.58  ? 300 ILE   A CD1 1 
ATOM   2243 N  N   . GLU   A 1 285 ? -62.214 6.462   -25.604 1.00 40.93  ? 301 GLU   A N   1 
ATOM   2244 C  CA  . GLU   A 1 285 ? -61.277 6.978   -26.609 1.00 48.79  ? 301 GLU   A CA  1 
ATOM   2245 C  C   . GLU   A 1 285 ? -61.707 8.320   -27.200 1.00 46.15  ? 301 GLU   A C   1 
ATOM   2246 O  O   . GLU   A 1 285 ? -60.870 9.024   -27.780 1.00 43.01  ? 301 GLU   A O   1 
ATOM   2247 C  CB  . GLU   A 1 285 ? -61.075 5.963   -27.747 1.00 50.34  ? 301 GLU   A CB  1 
ATOM   2248 C  CG  . GLU   A 1 285 ? -60.036 4.905   -27.413 1.00 66.77  ? 301 GLU   A CG  1 
ATOM   2249 C  CD  . GLU   A 1 285 ? -59.680 3.992   -28.591 1.00 80.39  ? 301 GLU   A CD  1 
ATOM   2250 O  OE1 . GLU   A 1 285 ? -59.868 4.405   -29.762 1.00 80.99  ? 301 GLU   A OE1 1 
ATOM   2251 O  OE2 . GLU   A 1 285 ? -59.206 2.857   -28.336 1.00 81.19  ? 301 GLU   A OE2 1 
ATOM   2252 N  N   . ARG   A 1 286 ? -62.987 8.689   -27.072 1.00 42.59  ? 302 ARG   A N   1 
ATOM   2253 C  CA  . ARG   A 1 286 ? -63.438 10.010  -27.508 1.00 45.38  ? 302 ARG   A CA  1 
ATOM   2254 C  C   . ARG   A 1 286 ? -62.649 11.123  -26.839 1.00 46.01  ? 302 ARG   A C   1 
ATOM   2255 O  O   . ARG   A 1 286 ? -62.522 12.221  -27.399 1.00 41.71  ? 302 ARG   A O   1 
ATOM   2256 C  CB  . ARG   A 1 286 ? -64.926 10.168  -27.208 1.00 45.96  ? 302 ARG   A CB  1 
ATOM   2257 C  CG  . ARG   A 1 286 ? -65.774 9.219   -28.006 1.00 48.85  ? 302 ARG   A CG  1 
ATOM   2258 C  CD  . ARG   A 1 286 ? -67.221 9.367   -27.604 1.00 53.65  ? 302 ARG   A CD  1 
ATOM   2259 N  NE  . ARG   A 1 286 ? -68.036 8.287   -28.133 1.00 49.22  ? 302 ARG   A NE  1 
ATOM   2260 C  CZ  . ARG   A 1 286 ? -69.340 8.175   -27.923 1.00 59.78  ? 302 ARG   A CZ  1 
ATOM   2261 N  NH1 . ARG   A 1 286 ? -69.987 9.024   -27.139 1.00 53.80  ? 302 ARG   A NH1 1 
ATOM   2262 N  NH2 . ARG   A 1 286 ? -70.010 7.189   -28.515 1.00 54.18  ? 302 ARG   A NH2 1 
ATOM   2263 N  N   . LEU   A 1 287 ? -62.112 10.861  -25.644 1.00 37.81  ? 303 LEU   A N   1 
ATOM   2264 C  CA  . LEU   A 1 287 ? -61.318 11.864  -24.939 1.00 44.54  ? 303 LEU   A CA  1 
ATOM   2265 C  C   . LEU   A 1 287 ? -60.044 12.232  -25.692 1.00 45.12  ? 303 LEU   A C   1 
ATOM   2266 O  O   . LEU   A 1 287 ? -59.475 13.289  -25.424 1.00 42.63  ? 303 LEU   A O   1 
ATOM   2267 C  CB  . LEU   A 1 287 ? -60.968 11.368  -23.523 1.00 41.62  ? 303 LEU   A CB  1 
ATOM   2268 C  CG  . LEU   A 1 287 ? -62.131 11.317  -22.519 1.00 43.24  ? 303 LEU   A CG  1 
ATOM   2269 C  CD1 . LEU   A 1 287 ? -61.739 10.578  -21.260 1.00 42.47  ? 303 LEU   A CD1 1 
ATOM   2270 C  CD2 . LEU   A 1 287 ? -62.593 12.731  -22.170 1.00 47.50  ? 303 LEU   A CD2 1 
ATOM   2271 N  N   . PHE   A 1 288 ? -59.585 11.399  -26.629 1.00 41.60  ? 304 PHE   A N   1 
ATOM   2272 C  CA  . PHE   A 1 288 ? -58.391 11.730  -27.399 1.00 45.15  ? 304 PHE   A CA  1 
ATOM   2273 C  C   . PHE   A 1 288 ? -58.716 12.177  -28.810 1.00 40.59  ? 304 PHE   A C   1 
ATOM   2274 O  O   . PHE   A 1 288 ? -57.799 12.404  -29.605 1.00 42.30  ? 304 PHE   A O   1 
ATOM   2275 C  CB  . PHE   A 1 288 ? -57.411 10.549  -27.410 1.00 39.83  ? 304 PHE   A CB  1 
ATOM   2276 C  CG  . PHE   A 1 288 ? -56.821 10.256  -26.042 1.00 43.89  ? 304 PHE   A CG  1 
ATOM   2277 C  CD1 . PHE   A 1 288 ? -55.926 11.142  -25.457 1.00 41.51  ? 304 PHE   A CD1 1 
ATOM   2278 C  CD2 . PHE   A 1 288 ? -57.193 9.123   -25.333 1.00 44.19  ? 304 PHE   A CD2 1 
ATOM   2279 C  CE1 . PHE   A 1 288 ? -55.392 10.901  -24.207 1.00 44.69  ? 304 PHE   A CE1 1 
ATOM   2280 C  CE2 . PHE   A 1 288 ? -56.659 8.863   -24.082 1.00 46.59  ? 304 PHE   A CE2 1 
ATOM   2281 C  CZ  . PHE   A 1 288 ? -55.756 9.751   -23.513 1.00 45.87  ? 304 PHE   A CZ  1 
ATOM   2282 N  N   . SER   A 1 289 ? -59.995 12.361  -29.123 1.00 42.43  ? 305 SER   A N   1 
ATOM   2283 C  CA  . SER   A 1 289 ? -60.429 12.740  -30.462 1.00 43.37  ? 305 SER   A CA  1 
ATOM   2284 C  C   . SER   A 1 289 ? -60.530 14.255  -30.561 1.00 47.83  ? 305 SER   A C   1 
ATOM   2285 O  O   . SER   A 1 289 ? -61.229 14.883  -29.758 1.00 43.30  ? 305 SER   A O   1 
ATOM   2286 C  CB  . SER   A 1 289 ? -61.774 12.087  -30.789 1.00 45.42  ? 305 SER   A CB  1 
ATOM   2287 O  OG  . SER   A 1 289 ? -62.455 12.814  -31.799 1.00 50.42  ? 305 SER   A OG  1 
ATOM   2288 N  N   . TYR   A 1 290 ? -59.857 14.834  -31.567 1.00 42.98  ? 306 TYR   A N   1 
ATOM   2289 C  CA  . TYR   A 1 290 ? -59.959 16.270  -31.809 1.00 46.07  ? 306 TYR   A CA  1 
ATOM   2290 C  C   . TYR   A 1 290 ? -61.394 16.682  -32.113 1.00 51.49  ? 306 TYR   A C   1 
ATOM   2291 O  O   . TYR   A 1 290 ? -61.845 17.747  -31.677 1.00 53.39  ? 306 TYR   A O   1 
ATOM   2292 C  CB  . TYR   A 1 290 ? -59.016 16.697  -32.945 1.00 45.03  ? 306 TYR   A CB  1 
ATOM   2293 C  CG  . TYR   A 1 290 ? -57.577 16.378  -32.619 1.00 48.78  ? 306 TYR   A CG  1 
ATOM   2294 C  CD1 . TYR   A 1 290 ? -56.870 17.153  -31.706 1.00 40.82  ? 306 TYR   A CD1 1 
ATOM   2295 C  CD2 . TYR   A 1 290 ? -56.943 15.279  -33.175 1.00 45.90  ? 306 TYR   A CD2 1 
ATOM   2296 C  CE1 . TYR   A 1 290 ? -55.564 16.861  -31.390 1.00 41.13  ? 306 TYR   A CE1 1 
ATOM   2297 C  CE2 . TYR   A 1 290 ? -55.629 14.967  -32.843 1.00 46.88  ? 306 TYR   A CE2 1 
ATOM   2298 C  CZ  . TYR   A 1 290 ? -54.944 15.769  -31.949 1.00 42.38  ? 306 TYR   A CZ  1 
ATOM   2299 O  OH  . TYR   A 1 290 ? -53.634 15.488  -31.606 1.00 43.06  ? 306 TYR   A OH  1 
ATOM   2300 N  N   . MET   A 1 291 ? -62.130 15.860  -32.859 1.00 50.49  ? 307 MET   A N   1 
ATOM   2301 C  CA  . MET   A 1 291 ? -63.487 16.262  -33.219 1.00 53.57  ? 307 MET   A CA  1 
ATOM   2302 C  C   . MET   A 1 291 ? -64.448 16.194  -32.034 1.00 56.88  ? 307 MET   A C   1 
ATOM   2303 O  O   . MET   A 1 291 ? -65.404 16.970  -31.985 1.00 55.02  ? 307 MET   A O   1 
ATOM   2304 C  CB  . MET   A 1 291 ? -64.022 15.418  -34.377 1.00 54.59  ? 307 MET   A CB  1 
ATOM   2305 C  CG  . MET   A 1 291 ? -65.161 16.122  -35.120 1.00 69.28  ? 307 MET   A CG  1 
ATOM   2306 S  SD  . MET   A 1 291 ? -65.088 15.786  -36.875 1.00 89.73  ? 307 MET   A SD  1 
ATOM   2307 C  CE  . MET   A 1 291 ? -65.033 13.998  -36.803 1.00 65.75  ? 307 MET   A CE  1 
ATOM   2308 N  N   . TYR   A 1 292 ? -64.248 15.265  -31.092 1.00 52.84  ? 308 TYR   A N   1 
ATOM   2309 C  CA  . TYR   A 1 292 ? -65.105 15.246  -29.904 1.00 56.94  ? 308 TYR   A CA  1 
ATOM   2310 C  C   . TYR   A 1 292 ? -64.856 16.479  -29.064 1.00 61.44  ? 308 TYR   A C   1 
ATOM   2311 O  O   . TYR   A 1 292 ? -65.796 17.171  -28.658 1.00 59.89  ? 308 TYR   A O   1 
ATOM   2312 C  CB  . TYR   A 1 292 ? -64.847 13.995  -29.053 1.00 56.16  ? 308 TYR   A CB  1 
ATOM   2313 C  CG  . TYR   A 1 292 ? -65.829 13.756  -27.897 1.00 58.80  ? 308 TYR   A CG  1 
ATOM   2314 C  CD1 . TYR   A 1 292 ? -67.090 13.213  -28.140 1.00 59.02  ? 308 TYR   A CD1 1 
ATOM   2315 C  CD2 . TYR   A 1 292 ? -65.491 14.046  -26.568 1.00 56.55  ? 308 TYR   A CD2 1 
ATOM   2316 C  CE1 . TYR   A 1 292 ? -68.004 12.960  -27.098 1.00 59.59  ? 308 TYR   A CE1 1 
ATOM   2317 C  CE2 . TYR   A 1 292 ? -66.420 13.800  -25.490 1.00 61.71  ? 308 TYR   A CE2 1 
ATOM   2318 C  CZ  . TYR   A 1 292 ? -67.683 13.249  -25.766 1.00 65.10  ? 308 TYR   A CZ  1 
ATOM   2319 O  OH  . TYR   A 1 292 ? -68.641 12.946  -24.749 1.00 73.37  ? 308 TYR   A OH  1 
ATOM   2320 N  N   . SER   A 1 293 ? -63.576 16.760  -28.814 1.00 67.44  ? 309 SER   A N   1 
ATOM   2321 C  CA  . SER   A 1 293 ? -62.997 17.811  -27.992 1.00 68.31  ? 309 SER   A CA  1 
ATOM   2322 C  C   . SER   A 1 293 ? -63.312 19.216  -28.477 1.00 67.21  ? 309 SER   A C   1 
ATOM   2323 O  O   . SER   A 1 293 ? -62.796 20.163  -27.879 1.00 70.26  ? 309 SER   A O   1 
ATOM   2324 C  CB  . SER   A 1 293 ? -61.474 17.632  -27.948 1.00 62.97  ? 309 SER   A CB  1 
ATOM   2325 O  OG  . SER   A 1 293 ? -61.126 16.362  -27.407 1.00 62.00  ? 309 SER   A OG  1 
ATOM   2326 N  N   . THR   A 1 294 ? -64.088 19.390  -29.542 1.00 69.99  ? 310 THR   A N   1 
ATOM   2327 C  CA  . THR   A 1 294 ? -64.462 20.711  -30.028 1.00 78.36  ? 310 THR   A CA  1 
ATOM   2328 C  C   . THR   A 1 294 ? -65.982 20.806  -30.069 1.00 79.18  ? 310 THR   A C   1 
ATOM   2329 O  O   . THR   A 1 294 ? -66.660 19.856  -30.475 1.00 76.56  ? 310 THR   A O   1 
ATOM   2330 C  CB  . THR   A 1 294 ? -63.851 21.029  -31.438 1.00 77.94  ? 310 THR   A CB  1 
ATOM   2331 O  OG1 . THR   A 1 294 ? -63.947 19.902  -32.321 1.00 69.40  ? 310 THR   A OG1 1 
ATOM   2332 C  CG2 . THR   A 1 294 ? -62.383 21.450  -31.337 1.00 69.73  ? 310 THR   A CG2 1 
ATOM   2333 N  N   . ALA   A 1 295 ? -66.510 21.948  -29.629 1.00 89.46  ? 311 ALA   A N   1 
ATOM   2334 C  CA  . ALA   A 1 295 ? -67.945 22.211  -29.664 1.00 91.42  ? 311 ALA   A CA  1 
ATOM   2335 C  C   . ALA   A 1 295 ? -68.211 23.716  -29.593 1.00 89.00  ? 311 ALA   A C   1 
ATOM   2336 O  O   . ALA   A 1 295 ? -67.272 24.516  -29.522 1.00 89.10  ? 311 ALA   A O   1 
ATOM   2337 C  CB  . ALA   A 1 295 ? -68.662 21.476  -28.519 1.00 91.00  ? 311 ALA   A CB  1 
ATOM   2338 N  N   A PRO   A 1 306 ? -64.740 27.504  -16.578 0.55 89.59  ? 322 PRO   A N   1 
ATOM   2339 N  N   B PRO   A 1 306 ? -64.377 27.851  -16.334 0.45 89.11  ? 322 PRO   A N   1 
ATOM   2340 C  CA  A PRO   A 1 306 ? -64.297 26.809  -15.371 0.55 87.70  ? 322 PRO   A CA  1 
ATOM   2341 C  CA  B PRO   A 1 306 ? -64.124 26.779  -15.374 0.45 87.67  ? 322 PRO   A CA  1 
ATOM   2342 C  C   A PRO   A 1 306 ? -62.840 26.386  -15.480 0.55 85.83  ? 322 PRO   A C   1 
ATOM   2343 C  C   B PRO   A 1 306 ? -62.717 26.227  -15.517 0.45 85.84  ? 322 PRO   A C   1 
ATOM   2344 O  O   A PRO   A 1 306 ? -61.941 27.232  -15.502 0.55 84.37  ? 322 PRO   A O   1 
ATOM   2345 O  O   B PRO   A 1 306 ? -61.740 26.981  -15.503 0.45 84.45  ? 322 PRO   A O   1 
ATOM   2346 C  CB  A PRO   A 1 306 ? -65.214 25.585  -15.330 0.55 89.28  ? 322 PRO   A CB  1 
ATOM   2347 C  CB  B PRO   A 1 306 ? -65.153 25.723  -15.772 0.45 89.11  ? 322 PRO   A CB  1 
ATOM   2348 C  CG  A PRO   A 1 306 ? -65.573 25.322  -16.809 0.55 87.96  ? 322 PRO   A CG  1 
ATOM   2349 C  CG  B PRO   A 1 306 ? -65.322 25.921  -17.285 0.45 89.09  ? 322 PRO   A CG  1 
ATOM   2350 C  CD  A PRO   A 1 306 ? -65.134 26.539  -17.618 0.55 89.87  ? 322 PRO   A CD  1 
ATOM   2351 C  CD  B PRO   A 1 306 ? -64.748 27.293  -17.646 0.45 89.91  ? 322 PRO   A CD  1 
ATOM   2352 N  N   A LEU   A 1 307 ? -62.623 25.075  -15.557 0.55 86.70  ? 323 LEU   A N   1 
ATOM   2353 N  N   B LEU   A 1 307 ? -62.631 24.905  -15.663 0.45 86.72  ? 323 LEU   A N   1 
ATOM   2354 C  CA  A LEU   A 1 307 ? -61.310 24.498  -15.809 0.55 85.41  ? 323 LEU   A CA  1 
ATOM   2355 C  CA  B LEU   A 1 307 ? -61.394 24.247  -16.058 0.45 85.06  ? 323 LEU   A CA  1 
ATOM   2356 C  C   A LEU   A 1 307 ? -61.057 24.244  -17.293 0.55 82.25  ? 323 LEU   A C   1 
ATOM   2357 C  C   B LEU   A 1 307 ? -61.406 24.062  -17.575 0.45 82.72  ? 323 LEU   A C   1 
ATOM   2358 O  O   A LEU   A 1 307 ? -60.009 23.689  -17.640 0.55 81.14  ? 323 LEU   A O   1 
ATOM   2359 O  O   B LEU   A 1 307 ? -61.463 25.050  -18.315 0.45 83.41  ? 323 LEU   A O   1 
ATOM   2360 C  CB  A LEU   A 1 307 ? -61.151 23.189  -15.023 0.55 82.30  ? 323 LEU   A CB  1 
ATOM   2361 C  CB  B LEU   A 1 307 ? -61.233 22.920  -15.308 0.45 81.93  ? 323 LEU   A CB  1 
ATOM   2362 C  CG  A LEU   A 1 307 ? -61.327 23.256  -13.501 0.55 82.86  ? 323 LEU   A CG  1 
ATOM   2363 C  CG  B LEU   A 1 307 ? -61.324 23.050  -13.778 0.45 82.73  ? 323 LEU   A CG  1 
ATOM   2364 C  CD1 A LEU   A 1 307 ? -61.095 21.894  -12.843 0.55 74.71  ? 323 LEU   A CD1 1 
ATOM   2365 C  CD1 B LEU   A 1 307 ? -61.117 21.715  -13.062 0.45 75.00  ? 323 LEU   A CD1 1 
ATOM   2366 C  CD2 A LEU   A 1 307 ? -60.399 24.302  -12.914 0.55 78.13  ? 323 LEU   A CD2 1 
ATOM   2367 C  CD2 B LEU   A 1 307 ? -60.343 24.097  -13.260 0.45 78.71  ? 323 LEU   A CD2 1 
ATOM   2368 N  N   A ALA   A 1 308 ? -61.982 24.657  -18.168 0.55 82.00  ? 324 ALA   A N   1 
ATOM   2369 N  N   B ALA   A 1 308 ? -61.371 22.807  -18.063 0.45 83.46  ? 324 ALA   A N   1 
ATOM   2370 C  CA  A ALA   A 1 308 ? -61.916 24.275  -19.578 0.55 80.14  ? 324 ALA   A CA  1 
ATOM   2371 C  CA  B ALA   A 1 308 ? -61.424 22.549  -19.511 0.45 82.02  ? 324 ALA   A CA  1 
ATOM   2372 C  C   A ALA   A 1 308 ? -60.618 24.741  -20.228 0.55 76.89  ? 324 ALA   A C   1 
ATOM   2373 C  C   B ALA   A 1 308 ? -62.163 21.234  -19.771 0.45 79.89  ? 324 ALA   A C   1 
ATOM   2374 O  O   A ALA   A 1 308 ? -59.903 23.949  -20.853 0.55 77.00  ? 324 ALA   A O   1 
ATOM   2375 O  O   B ALA   A 1 308 ? -61.562 20.198  -20.072 0.45 75.17  ? 324 ALA   A O   1 
ATOM   2376 C  CB  A ALA   A 1 308 ? -63.124 24.833  -20.331 0.55 81.46  ? 324 ALA   A CB  1 
ATOM   2377 C  CB  B ALA   A 1 308 ? -60.031 22.533  -20.129 0.45 79.37  ? 324 ALA   A CB  1 
ATOM   2378 N  N   A GLY   A 1 309 ? -60.285 26.018  -20.082 0.55 72.03  ? 325 GLY   A N   1 
ATOM   2379 N  N   B GLY   A 1 309 ? -63.492 21.291  -19.663 0.45 82.28  ? 325 GLY   A N   1 
ATOM   2380 C  CA  A GLY   A 1 309 ? -59.155 26.542  -20.817 0.55 70.53  ? 325 GLY   A CA  1 
ATOM   2381 C  CA  B GLY   A 1 309 ? -64.306 20.177  -20.116 0.45 76.86  ? 325 GLY   A CA  1 
ATOM   2382 C  C   A GLY   A 1 309 ? -57.867 26.713  -20.040 0.55 64.18  ? 325 GLY   A C   1 
ATOM   2383 C  C   B GLY   A 1 309 ? -64.197 19.966  -21.614 0.45 74.04  ? 325 GLY   A C   1 
ATOM   2384 O  O   A GLY   A 1 309 ? -57.116 27.652  -20.310 0.55 62.93  ? 325 GLY   A O   1 
ATOM   2385 O  O   B GLY   A 1 309 ? -64.170 18.829  -22.091 0.45 75.19  ? 325 GLY   A O   1 
ATOM   2386 N  N   A PHE   A 1 310 ? -57.566 25.824  -19.099 0.55 60.88  ? 326 PHE   A N   1 
ATOM   2387 N  N   B PHE   A 1 310 ? -64.132 21.056  -22.375 0.45 72.04  ? 326 PHE   A N   1 
ATOM   2388 C  CA  A PHE   A 1 310 ? -56.347 26.009  -18.323 0.55 60.46  ? 326 PHE   A CA  1 
ATOM   2389 C  CA  B PHE   A 1 310 ? -63.883 21.009  -23.811 0.45 71.42  ? 326 PHE   A CA  1 
ATOM   2390 C  C   A PHE   A 1 310 ? -55.173 25.161  -18.786 0.55 62.47  ? 326 PHE   A C   1 
ATOM   2391 C  C   B PHE   A 1 310 ? -62.515 21.618  -24.101 0.45 69.11  ? 326 PHE   A C   1 
ATOM   2392 O  O   A PHE   A 1 310 ? -54.027 25.604  -18.647 0.55 70.28  ? 326 PHE   A O   1 
ATOM   2393 O  O   B PHE   A 1 310 ? -62.244 22.757  -23.704 0.45 71.01  ? 326 PHE   A O   1 
ATOM   2394 C  CB  A PHE   A 1 310 ? -56.605 25.758  -16.836 0.55 54.29  ? 326 PHE   A CB  1 
ATOM   2395 C  CB  B PHE   A 1 310 ? -64.965 21.766  -24.590 0.45 70.46  ? 326 PHE   A CB  1 
ATOM   2396 C  CG  A PHE   A 1 310 ? -56.826 27.022  -16.072 0.55 59.13  ? 326 PHE   A CG  1 
ATOM   2397 C  CG  B PHE   A 1 310 ? -66.365 21.269  -24.341 0.45 73.21  ? 326 PHE   A CG  1 
ATOM   2398 C  CD1 A PHE   A 1 310 ? -55.759 27.851  -15.774 0.55 58.32  ? 326 PHE   A CD1 1 
ATOM   2399 C  CD1 B PHE   A 1 310 ? -66.878 20.200  -25.062 0.45 72.99  ? 326 PHE   A CD1 1 
ATOM   2400 C  CD2 A PHE   A 1 310 ? -58.102 27.420  -15.704 0.55 61.82  ? 326 PHE   A CD2 1 
ATOM   2401 C  CD2 B PHE   A 1 310 ? -67.175 21.881  -23.393 0.45 73.72  ? 326 PHE   A CD2 1 
ATOM   2402 C  CE1 A PHE   A 1 310 ? -55.957 29.043  -15.089 0.55 54.06  ? 326 PHE   A CE1 1 
ATOM   2403 C  CE1 B PHE   A 1 310 ? -68.169 19.746  -24.835 0.45 72.23  ? 326 PHE   A CE1 1 
ATOM   2404 C  CE2 A PHE   A 1 310 ? -58.302 28.600  -15.023 0.55 58.86  ? 326 PHE   A CE2 1 
ATOM   2405 C  CE2 B PHE   A 1 310 ? -68.464 21.429  -23.159 0.45 72.92  ? 326 PHE   A CE2 1 
ATOM   2406 C  CZ  A PHE   A 1 310 ? -57.225 29.414  -14.719 0.55 54.69  ? 326 PHE   A CZ  1 
ATOM   2407 C  CZ  B PHE   A 1 310 ? -68.962 20.362  -23.882 0.45 72.21  ? 326 PHE   A CZ  1 
ATOM   2408 N  N   A GLY   A 1 311 ? -55.408 23.976  -19.349 0.55 58.30  ? 327 GLY   A N   1 
ATOM   2409 N  N   B GLY   A 1 311 ? -61.660 20.861  -24.785 0.45 65.67  ? 327 GLY   A N   1 
ATOM   2410 C  CA  A GLY   A 1 311 ? -54.338 23.115  -19.799 0.55 60.34  ? 327 GLY   A CA  1 
ATOM   2411 C  CA  B GLY   A 1 311 ? -60.338 21.338  -25.149 0.45 57.58  ? 327 GLY   A CA  1 
ATOM   2412 C  C   A GLY   A 1 311 ? -54.326 22.924  -21.309 0.55 55.71  ? 327 GLY   A C   1 
ATOM   2413 C  C   B GLY   A 1 311 ? -59.426 20.216  -25.594 0.45 52.29  ? 327 GLY   A C   1 
ATOM   2414 O  O   A GLY   A 1 311 ? -55.164 23.459  -22.036 0.55 55.74  ? 327 GLY   A O   1 
ATOM   2415 O  O   B GLY   A 1 311 ? -59.710 19.051  -25.315 0.45 50.53  ? 327 GLY   A O   1 
ATOM   2416 N  N   A TYR   A 1 312 ? -53.352 22.126  -21.761 0.55 54.29  ? 328 TYR   A N   1 
ATOM   2417 N  N   B TYR   A 1 312 ? -58.328 20.550  -26.280 0.45 50.26  ? 328 TYR   A N   1 
ATOM   2418 C  CA  A TYR   A 1 312 ? -53.171 21.859  -23.185 0.55 50.92  ? 328 TYR   A CA  1 
ATOM   2419 C  CA  B TYR   A 1 312 ? -57.389 19.573  -26.816 0.45 48.04  ? 328 TYR   A CA  1 
ATOM   2420 C  C   A TYR   A 1 312 ? -54.198 20.877  -23.738 0.55 50.39  ? 328 TYR   A C   1 
ATOM   2421 C  C   B TYR   A 1 312 ? -56.338 19.143  -25.808 0.45 46.05  ? 328 TYR   A C   1 
ATOM   2422 O  O   A TYR   A 1 312 ? -54.369 20.806  -24.956 0.55 47.84  ? 328 TYR   A O   1 
ATOM   2423 O  O   B TYR   A 1 312 ? -55.308 18.577  -26.215 0.45 35.23  ? 328 TYR   A O   1 
ATOM   2424 C  CB  A TYR   A 1 312 ? -51.753 21.330  -23.444 0.55 50.87  ? 328 TYR   A CB  1 
ATOM   2425 C  CB  B TYR   A 1 312 ? -56.681 20.124  -28.057 0.45 40.40  ? 328 TYR   A CB  1 
ATOM   2426 C  CG  A TYR   A 1 312 ? -50.680 22.403  -23.402 0.55 56.99  ? 328 TYR   A CG  1 
ATOM   2427 C  CG  B TYR   A 1 312 ? -57.527 20.199  -29.281 0.45 47.34  ? 328 TYR   A CG  1 
ATOM   2428 C  CD1 A TYR   A 1 312 ? -50.266 22.945  -22.192 0.55 61.60  ? 328 TYR   A CD1 1 
ATOM   2429 C  CD1 B TYR   A 1 312 ? -58.779 19.606  -29.316 0.45 47.23  ? 328 TYR   A CD1 1 
ATOM   2430 C  CD2 A TYR   A 1 312 ? -50.082 22.872  -24.566 0.55 58.24  ? 328 TYR   A CD2 1 
ATOM   2431 C  CD2 B TYR   A 1 312 ? -57.072 20.867  -30.419 0.45 42.51  ? 328 TYR   A CD2 1 
ATOM   2432 C  CE1 A TYR   A 1 312 ? -49.297 23.933  -22.139 0.55 59.68  ? 328 TYR   A CE1 1 
ATOM   2433 C  CE1 B TYR   A 1 312 ? -59.557 19.680  -30.444 0.45 48.92  ? 328 TYR   A CE1 1 
ATOM   2434 C  CE2 A TYR   A 1 312 ? -49.104 23.861  -24.523 0.55 63.66  ? 328 TYR   A CE2 1 
ATOM   2435 C  CE2 B TYR   A 1 312 ? -57.841 20.933  -31.544 0.45 43.66  ? 328 TYR   A CE2 1 
ATOM   2436 C  CZ  A TYR   A 1 312 ? -48.719 24.389  -23.302 0.55 64.88  ? 328 TYR   A CZ  1 
ATOM   2437 C  CZ  B TYR   A 1 312 ? -59.083 20.341  -31.550 0.45 40.62  ? 328 TYR   A CZ  1 
ATOM   2438 O  OH  A TYR   A 1 312 ? -47.752 25.374  -23.236 0.55 70.58  ? 328 TYR   A OH  1 
ATOM   2439 O  OH  B TYR   A 1 312 ? -59.855 20.407  -32.678 0.45 49.71  ? 328 TYR   A OH  1 
ATOM   2440 N  N   A GLY   A 1 313 ? -54.875 20.119  -22.884 0.55 47.06  ? 329 GLY   A N   1 
ATOM   2441 N  N   B GLY   A 1 313 ? -56.580 19.409  -24.522 0.45 46.26  ? 329 GLY   A N   1 
ATOM   2442 C  CA  A GLY   A 1 313 ? -55.828 19.135  -23.347 0.55 45.82  ? 329 GLY   A CA  1 
ATOM   2443 C  CA  B GLY   A 1 313 ? -55.588 19.123  -23.500 0.45 45.90  ? 329 GLY   A CA  1 
ATOM   2444 C  C   A GLY   A 1 313 ? -55.250 17.725  -23.396 0.55 45.23  ? 329 GLY   A C   1 
ATOM   2445 C  C   B GLY   A 1 313 ? -55.181 17.662  -23.454 0.45 45.16  ? 329 GLY   A C   1 
ATOM   2446 O  O   A GLY   A 1 313 ? -54.033 17.509  -23.415 0.55 44.57  ? 329 GLY   A O   1 
ATOM   2447 O  O   B GLY   A 1 313 ? -53.988 17.339  -23.432 0.45 44.49  ? 329 GLY   A O   1 
ATOM   2448 N  N   . LEU   A 1 314 ? -56.164 16.748  -23.434 1.00 42.15  ? 330 LEU   A N   1 
ATOM   2449 C  CA  . LEU   A 1 314 ? -55.780 15.334  -23.426 1.00 41.79  ? 330 LEU   A CA  1 
ATOM   2450 C  C   . LEU   A 1 314 ? -55.127 14.881  -24.732 1.00 41.61  ? 330 LEU   A C   1 
ATOM   2451 O  O   . LEU   A 1 314 ? -54.103 14.177  -24.666 1.00 37.20  ? 330 LEU   A O   1 
ATOM   2452 C  CB  . LEU   A 1 314 ? -56.984 14.468  -23.061 1.00 43.16  ? 330 LEU   A CB  1 
ATOM   2453 C  CG  . LEU   A 1 314 ? -57.419 14.566  -21.594 1.00 45.87  ? 330 LEU   A CG  1 
ATOM   2454 C  CD1 . LEU   A 1 314 ? -58.738 13.847  -21.366 1.00 42.71  ? 330 LEU   A CD1 1 
ATOM   2455 C  CD2 . LEU   A 1 314 ? -56.310 13.963  -20.727 1.00 44.78  ? 330 LEU   A CD2 1 
ATOM   2456 N  N   . PRO   A 1 315 ? -55.651 15.198  -25.929 1.00 40.89  ? 331 PRO   A N   1 
ATOM   2457 C  CA  . PRO   A 1 315 ? -54.922 14.793  -27.160 1.00 43.95  ? 331 PRO   A CA  1 
ATOM   2458 C  C   . PRO   A 1 315 ? -53.464 15.240  -27.161 1.00 38.90  ? 331 PRO   A C   1 
ATOM   2459 O  O   . PRO   A 1 315 ? -52.565 14.429  -27.420 1.00 39.37  ? 331 PRO   A O   1 
ATOM   2460 C  CB  . PRO   A 1 315 ? -55.708 15.475  -28.295 1.00 40.88  ? 331 PRO   A CB  1 
ATOM   2461 C  CG  . PRO   A 1 315 ? -57.063 15.754  -27.755 1.00 42.05  ? 331 PRO   A CG  1 
ATOM   2462 C  CD  . PRO   A 1 315 ? -56.980 15.771  -26.227 1.00 38.07  ? 331 PRO   A CD  1 
ATOM   2463 N  N   . ILE   A 1 316 ? -53.214 16.517  -26.855 1.00 37.06  ? 332 ILE   A N   1 
ATOM   2464 C  CA  . ILE   A 1 316 ? -51.857 17.048  -26.889 1.00 36.71  ? 332 ILE   A CA  1 
ATOM   2465 C  C   . ILE   A 1 316 ? -51.013 16.459  -25.758 1.00 41.52  ? 332 ILE   A C   1 
ATOM   2466 O  O   . ILE   A 1 316 ? -49.831 16.154  -25.947 1.00 43.19  ? 332 ILE   A O   1 
ATOM   2467 C  CB  . ILE   A 1 316 ? -51.908 18.585  -26.860 1.00 41.28  ? 332 ILE   A CB  1 
ATOM   2468 C  CG1 . ILE   A 1 316 ? -52.508 19.082  -28.182 1.00 39.65  ? 332 ILE   A CG1 1 
ATOM   2469 C  CG2 . ILE   A 1 316 ? -50.520 19.185  -26.581 1.00 41.59  ? 332 ILE   A CG2 1 
ATOM   2470 C  CD1 . ILE   A 1 316 ? -52.694 20.597  -28.274 1.00 41.27  ? 332 ILE   A CD1 1 
ATOM   2471 N  N   . SER   A 1 317 ? -51.608 16.250  -24.579 1.00 40.64  ? 333 SER   A N   1 
ATOM   2472 C  CA  . SER   A 1 317 ? -50.886 15.576  -23.505 1.00 39.17  ? 333 SER   A CA  1 
ATOM   2473 C  C   . SER   A 1 317 ? -50.341 14.231  -23.960 1.00 39.58  ? 333 SER   A C   1 
ATOM   2474 O  O   . SER   A 1 317 ? -49.194 13.884  -23.658 1.00 40.51  ? 333 SER   A O   1 
ATOM   2475 C  CB  . SER   A 1 317 ? -51.788 15.400  -22.276 1.00 40.49  ? 333 SER   A CB  1 
ATOM   2476 O  OG  . SER   A 1 317 ? -51.991 16.658  -21.654 1.00 44.66  ? 333 SER   A OG  1 
ATOM   2477 N  N   . ARG   A 1 318 ? -51.139 13.454  -24.691 1.00 37.02  ? 334 ARG   A N   1 
ATOM   2478 C  CA  . ARG   A 1 318 ? -50.629 12.173  -25.146 1.00 36.17  ? 334 ARG   A CA  1 
ATOM   2479 C  C   . ARG   A 1 318 ? -49.506 12.344  -26.169 1.00 37.89  ? 334 ARG   A C   1 
ATOM   2480 O  O   . ARG   A 1 318 ? -48.571 11.534  -26.199 1.00 36.99  ? 334 ARG   A O   1 
ATOM   2481 C  CB  . ARG   A 1 318 ? -51.772 11.322  -25.714 1.00 36.65  ? 334 ARG   A CB  1 
ATOM   2482 C  CG  . ARG   A 1 318 ? -51.321 9.910   -26.152 1.00 39.01  ? 334 ARG   A CG  1 
ATOM   2483 C  CD  . ARG   A 1 318 ? -52.519 8.965   -26.395 1.00 42.29  ? 334 ARG   A CD  1 
ATOM   2484 N  NE  . ARG   A 1 318 ? -53.297 9.369   -27.562 1.00 45.33  ? 334 ARG   A NE  1 
ATOM   2485 C  CZ  . ARG   A 1 318 ? -54.294 8.660   -28.083 1.00 52.05  ? 334 ARG   A CZ  1 
ATOM   2486 N  NH1 . ARG   A 1 318 ? -54.709 7.535   -27.511 1.00 39.66  ? 334 ARG   A NH1 1 
ATOM   2487 N  NH2 . ARG   A 1 318 ? -54.899 9.101   -29.199 1.00 39.77  ? 334 ARG   A NH2 1 
ATOM   2488 N  N   . LEU   A 1 319 ? -49.563 13.396  -26.991 1.00 36.67  ? 335 LEU   A N   1 
ATOM   2489 C  CA  . LEU   A 1 319 ? -48.480 13.642  -27.938 1.00 37.68  ? 335 LEU   A CA  1 
ATOM   2490 C  C   . LEU   A 1 319 ? -47.191 14.023  -27.215 1.00 35.53  ? 335 LEU   A C   1 
ATOM   2491 O  O   . LEU   A 1 319 ? -46.109 13.589  -27.614 1.00 39.20  ? 335 LEU   A O   1 
ATOM   2492 C  CB  . LEU   A 1 319 ? -48.892 14.725  -28.934 1.00 36.37  ? 335 LEU   A CB  1 
ATOM   2493 C  CG  . LEU   A 1 319 ? -50.064 14.441  -29.905 1.00 39.94  ? 335 LEU   A CG  1 
ATOM   2494 C  CD1 . LEU   A 1 319 ? -50.367 15.657  -30.676 1.00 38.15  ? 335 LEU   A CD1 1 
ATOM   2495 C  CD2 . LEU   A 1 319 ? -49.771 13.301  -30.895 1.00 38.05  ? 335 LEU   A CD2 1 
ATOM   2496 N  N   . TYR   A 1 320 ? -47.279 14.824  -26.146 1.00 36.85  ? 336 TYR   A N   1 
ATOM   2497 C  CA  . TYR   A 1 320 ? -46.084 15.088  -25.343 1.00 38.54  ? 336 TYR   A CA  1 
ATOM   2498 C  C   . TYR   A 1 320 ? -45.445 13.786  -24.869 1.00 37.47  ? 336 TYR   A C   1 
ATOM   2499 O  O   . TYR   A 1 320 ? -44.225 13.622  -24.957 1.00 38.09  ? 336 TYR   A O   1 
ATOM   2500 C  CB  . TYR   A 1 320 ? -46.431 15.982  -24.141 1.00 37.47  ? 336 TYR   A CB  1 
ATOM   2501 C  CG  . TYR   A 1 320 ? -46.549 17.463  -24.461 1.00 42.80  ? 336 TYR   A CG  1 
ATOM   2502 C  CD1 . TYR   A 1 320 ? -45.532 18.144  -25.108 1.00 38.00  ? 336 TYR   A CD1 1 
ATOM   2503 C  CD2 . TYR   A 1 320 ? -47.669 18.184  -24.076 1.00 47.36  ? 336 TYR   A CD2 1 
ATOM   2504 C  CE1 . TYR   A 1 320 ? -45.640 19.497  -25.387 1.00 48.27  ? 336 TYR   A CE1 1 
ATOM   2505 C  CE2 . TYR   A 1 320 ? -47.790 19.527  -24.353 1.00 50.06  ? 336 TYR   A CE2 1 
ATOM   2506 C  CZ  . TYR   A 1 320 ? -46.779 20.179  -25.012 1.00 53.50  ? 336 TYR   A CZ  1 
ATOM   2507 O  OH  . TYR   A 1 320 ? -46.909 21.520  -25.278 1.00 59.07  ? 336 TYR   A OH  1 
ATOM   2508 N  N   . ALA   A 1 321 ? -46.261 12.839  -24.389 1.00 35.92  ? 337 ALA   A N   1 
ATOM   2509 C  CA  . ALA   A 1 321 ? -45.740 11.540  -23.975 1.00 38.81  ? 337 ALA   A CA  1 
ATOM   2510 C  C   . ALA   A 1 321 ? -45.106 10.787  -25.140 1.00 40.31  ? 337 ALA   A C   1 
ATOM   2511 O  O   . ALA   A 1 321 ? -44.013 10.225  -25.001 1.00 38.46  ? 337 ALA   A O   1 
ATOM   2512 C  CB  . ALA   A 1 321 ? -46.858 10.699  -23.357 1.00 35.22  ? 337 ALA   A CB  1 
ATOM   2513 N  N   . LYS   A 1 322 ? -45.753 10.798  -26.309 1.00 37.75  ? 338 LYS   A N   1 
ATOM   2514 C  CA  . LYS   A 1 322 ? -45.221 10.065  -27.454 1.00 38.66  ? 338 LYS   A CA  1 
ATOM   2515 C  C   . LYS   A 1 322 ? -43.968 10.717  -28.032 1.00 40.81  ? 338 LYS   A C   1 
ATOM   2516 O  O   . LYS   A 1 322 ? -43.178 10.019  -28.669 1.00 36.24  ? 338 LYS   A O   1 
ATOM   2517 C  CB  . LYS   A 1 322 ? -46.303 9.939   -28.547 1.00 38.29  ? 338 LYS   A CB  1 
ATOM   2518 C  CG  . LYS   A 1 322 ? -47.394 8.916   -28.228 1.00 45.69  ? 338 LYS   A CG  1 
ATOM   2519 C  CD  . LYS   A 1 322 ? -48.462 8.818   -29.343 1.00 46.19  ? 338 LYS   A CD  1 
ATOM   2520 C  CE  . LYS   A 1 322 ? -49.565 7.818   -28.957 1.00 46.15  ? 338 LYS   A CE  1 
ATOM   2521 N  NZ  . LYS   A 1 322 ? -50.670 7.764   -29.950 1.00 54.71  ? 338 LYS   A NZ  1 
ATOM   2522 N  N   . TYR   A 1 323 ? -43.751 12.020  -27.786 1.00 38.37  ? 339 TYR   A N   1 
ATOM   2523 C  CA  . TYR   A 1 323 ? -42.676 12.767  -28.463 1.00 42.81  ? 339 TYR   A CA  1 
ATOM   2524 C  C   . TYR   A 1 323 ? -41.283 12.151  -28.250 1.00 42.32  ? 339 TYR   A C   1 
ATOM   2525 O  O   . TYR   A 1 323 ? -40.444 12.172  -29.165 1.00 39.44  ? 339 TYR   A O   1 
ATOM   2526 C  CB  . TYR   A 1 323 ? -42.705 14.227  -27.990 1.00 37.42  ? 339 TYR   A CB  1 
ATOM   2527 C  CG  . TYR   A 1 323 ? -41.570 15.088  -28.484 1.00 41.59  ? 339 TYR   A CG  1 
ATOM   2528 C  CD1 . TYR   A 1 323 ? -41.176 15.058  -29.822 1.00 39.73  ? 339 TYR   A CD1 1 
ATOM   2529 C  CD2 . TYR   A 1 323 ? -40.882 15.945  -27.610 1.00 39.42  ? 339 TYR   A CD2 1 
ATOM   2530 C  CE1 . TYR   A 1 323 ? -40.130 15.845  -30.282 1.00 42.71  ? 339 TYR   A CE1 1 
ATOM   2531 C  CE2 . TYR   A 1 323 ? -39.836 16.752  -28.075 1.00 43.28  ? 339 TYR   A CE2 1 
ATOM   2532 C  CZ  . TYR   A 1 323 ? -39.464 16.688  -29.411 1.00 41.42  ? 339 TYR   A CZ  1 
ATOM   2533 O  OH  . TYR   A 1 323 ? -38.432 17.466  -29.887 1.00 44.11  ? 339 TYR   A OH  1 
ATOM   2534 N  N   . PHE   A 1 324 ? -40.999 11.635  -27.047 1.00 41.53  ? 340 PHE   A N   1 
ATOM   2535 C  CA  . PHE   A 1 324 ? -39.757 10.906  -26.766 1.00 43.39  ? 340 PHE   A CA  1 
ATOM   2536 C  C   . PHE   A 1 324 ? -39.998 9.411   -26.532 1.00 42.81  ? 340 PHE   A C   1 
ATOM   2537 O  O   . PHE   A 1 324 ? -39.390 8.800   -25.641 1.00 40.03  ? 340 PHE   A O   1 
ATOM   2538 C  CB  . PHE   A 1 324 ? -39.022 11.510  -25.570 1.00 40.68  ? 340 PHE   A CB  1 
ATOM   2539 C  CG  . PHE   A 1 324 ? -38.306 12.808  -25.882 1.00 43.69  ? 340 PHE   A CG  1 
ATOM   2540 C  CD1 . PHE   A 1 324 ? -37.187 12.817  -26.701 1.00 46.22  ? 340 PHE   A CD1 1 
ATOM   2541 C  CD2 . PHE   A 1 324 ? -38.750 14.010  -25.355 1.00 41.86  ? 340 PHE   A CD2 1 
ATOM   2542 C  CE1 . PHE   A 1 324 ? -36.516 14.001  -26.982 1.00 48.15  ? 340 PHE   A CE1 1 
ATOM   2543 C  CE2 . PHE   A 1 324 ? -38.091 15.198  -25.639 1.00 44.70  ? 340 PHE   A CE2 1 
ATOM   2544 C  CZ  . PHE   A 1 324 ? -36.975 15.192  -26.457 1.00 46.07  ? 340 PHE   A CZ  1 
ATOM   2545 N  N   . GLN   A 1 325 ? -40.874 8.807   -27.351 1.00 43.09  ? 341 GLN   A N   1 
ATOM   2546 C  CA  . GLN   A 1 325 ? -41.104 7.359   -27.429 1.00 41.72  ? 341 GLN   A CA  1 
ATOM   2547 C  C   . GLN   A 1 325 ? -41.879 6.817   -26.234 1.00 44.36  ? 341 GLN   A C   1 
ATOM   2548 O  O   . GLN   A 1 325 ? -41.797 5.621   -25.949 1.00 44.43  ? 341 GLN   A O   1 
ATOM   2549 C  CB  . GLN   A 1 325 ? -39.794 6.563   -27.582 1.00 42.14  ? 341 GLN   A CB  1 
ATOM   2550 C  CG  . GLN   A 1 325 ? -38.882 7.019   -28.715 1.00 45.35  ? 341 GLN   A CG  1 
ATOM   2551 C  CD  . GLN   A 1 325 ? -39.526 6.874   -30.087 1.00 50.52  ? 341 GLN   A CD  1 
ATOM   2552 O  OE1 . GLN   A 1 325 ? -40.213 5.890   -30.368 1.00 48.40  ? 341 GLN   A OE1 1 
ATOM   2553 N  NE2 . GLN   A 1 325 ? -39.326 7.871   -30.940 1.00 44.70  ? 341 GLN   A NE2 1 
ATOM   2554 N  N   . GLY   A 1 326 ? -42.630 7.669   -25.534 1.00 41.42  ? 342 GLY   A N   1 
ATOM   2555 C  CA  . GLY   A 1 326 ? -43.485 7.265   -24.438 1.00 36.09  ? 342 GLY   A CA  1 
ATOM   2556 C  C   . GLY   A 1 326 ? -44.932 7.096   -24.868 1.00 42.53  ? 342 GLY   A C   1 
ATOM   2557 O  O   . GLY   A 1 326 ? -45.251 7.004   -26.058 1.00 37.23  ? 342 GLY   A O   1 
ATOM   2558 N  N   . ASP   A 1 327 ? -45.830 7.072   -23.883 1.00 39.38  ? 343 ASP   A N   1 
ATOM   2559 C  CA  . ASP   A 1 327 ? -47.247 6.920   -24.188 1.00 38.60  ? 343 ASP   A CA  1 
ATOM   2560 C  C   . ASP   A 1 327 ? -48.054 7.375   -22.976 1.00 39.10  ? 343 ASP   A C   1 
ATOM   2561 O  O   . ASP   A 1 327 ? -47.520 7.580   -21.879 1.00 36.03  ? 343 ASP   A O   1 
ATOM   2562 C  CB  . ASP   A 1 327 ? -47.592 5.471   -24.596 1.00 38.24  ? 343 ASP   A CB  1 
ATOM   2563 C  CG  . ASP   A 1 327 ? -48.902 5.369   -25.423 1.00 42.13  ? 343 ASP   A CG  1 
ATOM   2564 O  OD1 . ASP   A 1 327 ? -49.562 6.401   -25.701 1.00 39.02  ? 343 ASP   A OD1 1 
ATOM   2565 O  OD2 . ASP   A 1 327 ? -49.293 4.234   -25.768 1.00 47.47  ? 343 ASP   A OD2 1 
ATOM   2566 N  N   . LEU   A 1 328 ? -49.343 7.594   -23.210 1.00 34.68  ? 344 LEU   A N   1 
ATOM   2567 C  CA  . LEU   A 1 328 ? -50.273 8.006   -22.169 1.00 34.88  ? 344 LEU   A CA  1 
ATOM   2568 C  C   . LEU   A 1 328 ? -51.547 7.220   -22.401 1.00 40.72  ? 344 LEU   A C   1 
ATOM   2569 O  O   . LEU   A 1 328 ? -52.198 7.401   -23.427 1.00 38.56  ? 344 LEU   A O   1 
ATOM   2570 C  CB  . LEU   A 1 328 ? -50.532 9.514   -22.208 1.00 35.24  ? 344 LEU   A CB  1 
ATOM   2571 C  CG  . LEU   A 1 328 ? -51.207 10.193  -21.001 1.00 41.17  ? 344 LEU   A CG  1 
ATOM   2572 C  CD1 . LEU   A 1 328 ? -51.089 11.747  -21.121 1.00 41.63  ? 344 LEU   A CD1 1 
ATOM   2573 C  CD2 . LEU   A 1 328 ? -52.684 9.806   -20.858 1.00 41.65  ? 344 LEU   A CD2 1 
ATOM   2574 N  N   . GLN   A 1 329 ? -51.909 6.358   -21.458 1.00 38.33  ? 345 GLN   A N   1 
ATOM   2575 C  CA  . GLN   A 1 329 ? -53.049 5.470   -21.624 1.00 38.48  ? 345 GLN   A CA  1 
ATOM   2576 C  C   . GLN   A 1 329 ? -54.047 5.666   -20.492 1.00 41.98  ? 345 GLN   A C   1 
ATOM   2577 O  O   . GLN   A 1 329 ? -53.656 5.885   -19.341 1.00 40.35  ? 345 GLN   A O   1 
ATOM   2578 C  CB  . GLN   A 1 329 ? -52.598 4.007   -21.668 1.00 41.03  ? 345 GLN   A CB  1 
ATOM   2579 C  CG  . GLN   A 1 329 ? -51.682 3.719   -22.840 1.00 42.98  ? 345 GLN   A CG  1 
ATOM   2580 C  CD  . GLN   A 1 329 ? -51.204 2.275   -22.913 1.00 49.96  ? 345 GLN   A CD  1 
ATOM   2581 O  OE1 . GLN   A 1 329 ? -51.516 1.443   -22.054 1.00 45.22  ? 345 GLN   A OE1 1 
ATOM   2582 N  NE2 . GLN   A 1 329 ? -50.438 1.977   -23.952 1.00 50.37  ? 345 GLN   A NE2 1 
ATOM   2583 N  N   . LEU   A 1 330 ? -55.338 5.570   -20.827 1.00 40.44  ? 346 LEU   A N   1 
ATOM   2584 C  CA  . LEU   A 1 330 ? -56.410 5.604   -19.847 1.00 42.04  ? 346 LEU   A CA  1 
ATOM   2585 C  C   . LEU   A 1 330 ? -57.056 4.235   -19.735 1.00 42.42  ? 346 LEU   A C   1 
ATOM   2586 O  O   . LEU   A 1 330 ? -57.200 3.523   -20.728 1.00 41.96  ? 346 LEU   A O   1 
ATOM   2587 C  CB  . LEU   A 1 330 ? -57.492 6.620   -20.216 1.00 37.45  ? 346 LEU   A CB  1 
ATOM   2588 C  CG  . LEU   A 1 330 ? -57.101 8.079   -20.404 1.00 46.00  ? 346 LEU   A CG  1 
ATOM   2589 C  CD1 . LEU   A 1 330 ? -58.342 8.960   -20.749 1.00 45.64  ? 346 LEU   A CD1 1 
ATOM   2590 C  CD2 . LEU   A 1 330 ? -56.365 8.621   -19.189 1.00 40.72  ? 346 LEU   A CD2 1 
ATOM   2591 N  N   A PHE   A 1 331 ? -57.463 3.887   -18.511 0.48 41.37  ? 347 PHE   A N   1 
ATOM   2592 N  N   B PHE   A 1 331 ? -57.456 3.864   -18.526 0.52 41.28  ? 347 PHE   A N   1 
ATOM   2593 C  CA  A PHE   A 1 331 ? -58.175 2.651   -18.211 0.48 40.09  ? 347 PHE   A CA  1 
ATOM   2594 C  CA  B PHE   A 1 331 ? -58.332 2.711   -18.421 0.52 39.75  ? 347 PHE   A CA  1 
ATOM   2595 C  C   A PHE   A 1 331 ? -59.213 2.975   -17.146 0.48 41.44  ? 347 PHE   A C   1 
ATOM   2596 C  C   B PHE   A 1 331 ? -59.199 2.867   -17.189 0.52 41.46  ? 347 PHE   A C   1 
ATOM   2597 O  O   A PHE   A 1 331 ? -58.861 3.494   -16.083 0.48 41.45  ? 347 PHE   A O   1 
ATOM   2598 O  O   B PHE   A 1 331 ? -58.719 3.156   -16.086 0.52 41.57  ? 347 PHE   A O   1 
ATOM   2599 C  CB  A PHE   A 1 331 ? -57.226 1.557   -17.690 0.48 39.60  ? 347 PHE   A CB  1 
ATOM   2600 C  CB  B PHE   A 1 331 ? -57.564 1.385   -18.412 0.52 41.36  ? 347 PHE   A CB  1 
ATOM   2601 C  CG  A PHE   A 1 331 ? -56.039 1.283   -18.583 0.48 39.71  ? 347 PHE   A CG  1 
ATOM   2602 C  CG  B PHE   A 1 331 ? -56.538 1.251   -17.327 0.52 38.20  ? 347 PHE   A CG  1 
ATOM   2603 C  CD1 A PHE   A 1 331 ? -56.107 0.314   -19.576 0.48 40.33  ? 347 PHE   A CD1 1 
ATOM   2604 C  CD1 B PHE   A 1 331 ? -55.311 1.881   -17.428 0.52 40.25  ? 347 PHE   A CD1 1 
ATOM   2605 C  CD2 A PHE   A 1 331 ? -54.848 1.974   -18.409 0.48 39.86  ? 347 PHE   A CD2 1 
ATOM   2606 C  CD2 B PHE   A 1 331 ? -56.769 0.420   -16.247 0.52 43.09  ? 347 PHE   A CD2 1 
ATOM   2607 C  CE1 A PHE   A 1 331 ? -55.010 0.052   -20.396 0.48 40.92  ? 347 PHE   A CE1 1 
ATOM   2608 C  CE1 B PHE   A 1 331 ? -54.347 1.723   -16.442 0.52 40.77  ? 347 PHE   A CE1 1 
ATOM   2609 C  CE2 A PHE   A 1 331 ? -53.746 1.716   -19.217 0.48 40.31  ? 347 PHE   A CE2 1 
ATOM   2610 C  CE2 B PHE   A 1 331 ? -55.801 0.253   -15.252 0.52 44.17  ? 347 PHE   A CE2 1 
ATOM   2611 C  CZ  A PHE   A 1 331 ? -53.826 0.753   -20.208 0.48 40.53  ? 347 PHE   A CZ  1 
ATOM   2612 C  CZ  B PHE   A 1 331 ? -54.595 0.908   -15.355 0.52 40.60  ? 347 PHE   A CZ  1 
ATOM   2613 N  N   . SER   A 1 332 ? -60.477 2.655   -17.404 1.00 38.98  ? 348 SER   A N   1 
ATOM   2614 C  CA  . SER   A 1 332 ? -61.521 3.025   -16.482 1.00 44.44  ? 348 SER   A CA  1 
ATOM   2615 C  C   . SER   A 1 332 ? -62.334 1.800   -16.080 1.00 45.22  ? 348 SER   A C   1 
ATOM   2616 O  O   . SER   A 1 332 ? -62.308 0.760   -16.743 1.00 40.03  ? 348 SER   A O   1 
ATOM   2617 C  CB  . SER   A 1 332 ? -62.406 4.099   -17.110 1.00 35.94  ? 348 SER   A CB  1 
ATOM   2618 O  OG  . SER   A 1 332 ? -63.288 4.607   -16.150 1.00 39.85  ? 348 SER   A OG  1 
ATOM   2619 N  N   . MET   A 1 333 ? -63.056 1.946   -14.971 1.00 41.47  ? 349 MET   A N   1 
ATOM   2620 C  CA  . MET   A 1 333 ? -64.043 0.966   -14.530 1.00 41.69  ? 349 MET   A CA  1 
ATOM   2621 C  C   . MET   A 1 333 ? -65.328 1.739   -14.291 1.00 43.65  ? 349 MET   A C   1 
ATOM   2622 O  O   . MET   A 1 333 ? -65.456 2.430   -13.274 1.00 42.63  ? 349 MET   A O   1 
ATOM   2623 C  CB  . MET   A 1 333 ? -63.587 0.235   -13.272 1.00 40.77  ? 349 MET   A CB  1 
ATOM   2624 C  CG  . MET   A 1 333 ? -62.472 -0.783  -13.552 1.00 48.27  ? 349 MET   A CG  1 
ATOM   2625 S  SD  . MET   A 1 333 ? -61.890 -1.617  -12.091 1.00 57.91  ? 349 MET   A SD  1 
ATOM   2626 C  CE  . MET   A 1 333 ? -63.079 -2.945  -11.934 1.00 43.90  ? 349 MET   A CE  1 
ATOM   2627 N  N   . GLU   A 1 334 ? -66.258 1.647   -15.233 1.00 38.57  ? 350 GLU   A N   1 
ATOM   2628 C  CA  . GLU   A 1 334 ? -67.487 2.399   -15.112 1.00 43.08  ? 350 GLU   A CA  1 
ATOM   2629 C  C   . GLU   A 1 334 ? -68.159 2.059   -13.789 1.00 46.66  ? 350 GLU   A C   1 
ATOM   2630 O  O   . GLU   A 1 334 ? -68.260 0.887   -13.421 1.00 44.15  ? 350 GLU   A O   1 
ATOM   2631 C  CB  . GLU   A 1 334 ? -68.425 2.108   -16.285 1.00 41.05  ? 350 GLU   A CB  1 
ATOM   2632 C  CG  . GLU   A 1 334 ? -69.656 3.033   -16.259 1.00 43.76  ? 350 GLU   A CG  1 
ATOM   2633 C  CD  . GLU   A 1 334 ? -70.791 2.565   -17.152 1.00 47.68  ? 350 GLU   A CD  1 
ATOM   2634 O  OE1 . GLU   A 1 334 ? -70.793 1.397   -17.608 1.00 46.96  ? 350 GLU   A OE1 1 
ATOM   2635 O  OE2 . GLU   A 1 334 ? -71.684 3.388   -17.417 1.00 50.98  ? 350 GLU   A OE2 1 
ATOM   2636 N  N   . GLY   A 1 335 ? -68.598 3.091   -13.067 1.00 46.81  ? 351 GLY   A N   1 
ATOM   2637 C  CA  . GLY   A 1 335 ? -69.163 2.931   -11.741 1.00 41.55  ? 351 GLY   A CA  1 
ATOM   2638 C  C   . GLY   A 1 335 ? -68.161 3.008   -10.603 1.00 48.32  ? 351 GLY   A C   1 
ATOM   2639 O  O   . GLY   A 1 335 ? -68.567 2.983   -9.440  1.00 47.24  ? 351 GLY   A O   1 
ATOM   2640 N  N   . PHE   A 1 336 ? -66.864 3.089   -10.889 1.00 45.52  ? 352 PHE   A N   1 
ATOM   2641 C  CA  . PHE   A 1 336 ? -65.881 3.122   -9.814  1.00 45.68  ? 352 PHE   A CA  1 
ATOM   2642 C  C   . PHE   A 1 336 ? -64.886 4.256   -10.006 1.00 47.82  ? 352 PHE   A C   1 
ATOM   2643 O  O   . PHE   A 1 336 ? -64.876 5.211   -9.222  1.00 46.33  ? 352 PHE   A O   1 
ATOM   2644 C  CB  . PHE   A 1 336 ? -65.146 1.779   -9.713  1.00 47.97  ? 352 PHE   A CB  1 
ATOM   2645 C  CG  . PHE   A 1 336 ? -64.053 1.762   -8.672  1.00 51.02  ? 352 PHE   A CG  1 
ATOM   2646 C  CD1 . PHE   A 1 336 ? -64.337 2.044   -7.343  1.00 56.19  ? 352 PHE   A CD1 1 
ATOM   2647 C  CD2 . PHE   A 1 336 ? -62.748 1.436   -9.014  1.00 54.90  ? 352 PHE   A CD2 1 
ATOM   2648 C  CE1 . PHE   A 1 336 ? -63.331 2.028   -6.377  1.00 55.36  ? 352 PHE   A CE1 1 
ATOM   2649 C  CE2 . PHE   A 1 336 ? -61.739 1.422   -8.048  1.00 52.84  ? 352 PHE   A CE2 1 
ATOM   2650 C  CZ  . PHE   A 1 336 ? -62.035 1.718   -6.738  1.00 54.59  ? 352 PHE   A CZ  1 
ATOM   2651 N  N   . GLY   A 1 337 ? -64.028 4.160   -11.015 1.00 42.28  ? 353 GLY   A N   1 
ATOM   2652 C  CA  . GLY   A 1 337 ? -63.030 5.195   -11.221 1.00 38.74  ? 353 GLY   A CA  1 
ATOM   2653 C  C   . GLY   A 1 337 ? -62.193 4.935   -12.456 1.00 41.16  ? 353 GLY   A C   1 
ATOM   2654 O  O   . GLY   A 1 337 ? -62.487 4.046   -13.262 1.00 40.85  ? 353 GLY   A O   1 
ATOM   2655 N  N   . THR   A 1 338 ? -61.118 5.718   -12.569 1.00 38.31  ? 354 THR   A N   1 
ATOM   2656 C  CA  . THR   A 1 338 ? -60.282 5.766   -13.756 1.00 38.47  ? 354 THR   A CA  1 
ATOM   2657 C  C   . THR   A 1 338 ? -58.811 5.824   -13.365 1.00 41.06  ? 354 THR   A C   1 
ATOM   2658 O  O   . THR   A 1 338 ? -58.446 6.503   -12.395 1.00 38.98  ? 354 THR   A O   1 
ATOM   2659 C  CB  . THR   A 1 338 ? -60.641 6.991   -14.607 1.00 39.74  ? 354 THR   A CB  1 
ATOM   2660 O  OG1 . THR   A 1 338 ? -62.046 6.977   -14.888 1.00 36.99  ? 354 THR   A OG1 1 
ATOM   2661 C  CG2 . THR   A 1 338 ? -59.837 7.002   -15.928 1.00 36.20  ? 354 THR   A CG2 1 
ATOM   2662 N  N   . ASP   A 1 339 ? -57.976 5.104   -14.115 1.00 38.22  ? 355 ASP   A N   1 
ATOM   2663 C  CA  . ASP   A 1 339 ? -56.525 5.203   -14.021 1.00 39.46  ? 355 ASP   A CA  1 
ATOM   2664 C  C   . ASP   A 1 339 ? -55.956 5.807   -15.298 1.00 40.82  ? 355 ASP   A C   1 
ATOM   2665 O  O   . ASP   A 1 339 ? -56.498 5.632   -16.391 1.00 38.37  ? 355 ASP   A O   1 
ATOM   2666 C  CB  . ASP   A 1 339 ? -55.856 3.845   -13.814 1.00 43.53  ? 355 ASP   A CB  1 
ATOM   2667 C  CG  . ASP   A 1 339 ? -56.270 3.167   -12.509 1.00 42.71  ? 355 ASP   A CG  1 
ATOM   2668 O  OD1 . ASP   A 1 339 ? -56.743 3.852   -11.595 1.00 47.89  ? 355 ASP   A OD1 1 
ATOM   2669 O  OD2 . ASP   A 1 339 ? -56.117 1.939   -12.403 1.00 52.81  ? 355 ASP   A OD2 1 
ATOM   2670 N  N   . ALA   A 1 340 ? -54.858 6.524   -15.146 1.00 39.02  ? 356 ALA   A N   1 
ATOM   2671 C  CA  . ALA   A 1 340 ? -54.069 7.002   -16.262 1.00 40.19  ? 356 ALA   A CA  1 
ATOM   2672 C  C   . ALA   A 1 340 ? -52.637 6.593   -16.001 1.00 41.45  ? 356 ALA   A C   1 
ATOM   2673 O  O   . ALA   A 1 340 ? -52.189 6.646   -14.859 1.00 40.79  ? 356 ALA   A O   1 
ATOM   2674 C  CB  . ALA   A 1 340 ? -54.147 8.520   -16.418 1.00 38.63  ? 356 ALA   A CB  1 
ATOM   2675 N  N   . VAL   A 1 341 ? -51.928 6.155   -17.042 1.00 40.23  ? 357 VAL   A N   1 
ATOM   2676 C  CA  . VAL   A 1 341 ? -50.519 5.813   -16.908 1.00 38.49  ? 357 VAL   A CA  1 
ATOM   2677 C  C   . VAL   A 1 341 ? -49.737 6.608   -17.949 1.00 39.06  ? 357 VAL   A C   1 
ATOM   2678 O  O   . VAL   A 1 341 ? -50.008 6.502   -19.149 1.00 37.39  ? 357 VAL   A O   1 
ATOM   2679 C  CB  . VAL   A 1 341 ? -50.271 4.304   -17.068 1.00 41.54  ? 357 VAL   A CB  1 
ATOM   2680 C  CG1 . VAL   A 1 341 ? -48.798 3.975   -16.782 1.00 40.84  ? 357 VAL   A CG1 1 
ATOM   2681 C  CG2 . VAL   A 1 341 ? -51.184 3.492   -16.118 1.00 41.69  ? 357 VAL   A CG2 1 
ATOM   2682 N  N   . ILE   A 1 342 ? -48.767 7.384   -17.491 1.00 39.29  ? 358 ILE   A N   1 
ATOM   2683 C  CA  . ILE   A 1 342 ? -47.759 7.981   -18.356 1.00 37.56  ? 358 ILE   A CA  1 
ATOM   2684 C  C   . ILE   A 1 342 ? -46.577 7.025   -18.422 1.00 40.69  ? 358 ILE   A C   1 
ATOM   2685 O  O   . ILE   A 1 342 ? -46.025 6.642   -17.386 1.00 40.11  ? 358 ILE   A O   1 
ATOM   2686 C  CB  . ILE   A 1 342 ? -47.314 9.352   -17.830 1.00 38.74  ? 358 ILE   A CB  1 
ATOM   2687 C  CG1 . ILE   A 1 342 ? -48.470 10.342  -17.835 1.00 39.72  ? 358 ILE   A CG1 1 
ATOM   2688 C  CG2 . ILE   A 1 342 ? -46.189 9.909   -18.701 1.00 42.69  ? 358 ILE   A CG2 1 
ATOM   2689 C  CD1 . ILE   A 1 342 ? -48.175 11.625  -17.010 1.00 42.44  ? 358 ILE   A CD1 1 
ATOM   2690 N  N   . TYR   A 1 343 ? -46.192 6.619   -19.630 1.00 39.55  ? 359 TYR   A N   1 
ATOM   2691 C  CA  . TYR   A 1 343 ? -45.040 5.750   -19.828 1.00 37.76  ? 359 TYR   A CA  1 
ATOM   2692 C  C   . TYR   A 1 343 ? -43.930 6.562   -20.470 1.00 38.90  ? 359 TYR   A C   1 
ATOM   2693 O  O   . TYR   A 1 343 ? -44.154 7.203   -21.499 1.00 40.54  ? 359 TYR   A O   1 
ATOM   2694 C  CB  . TYR   A 1 343 ? -45.375 4.553   -20.714 1.00 37.18  ? 359 TYR   A CB  1 
ATOM   2695 C  CG  . TYR   A 1 343 ? -46.404 3.570   -20.167 1.00 39.39  ? 359 TYR   A CG  1 
ATOM   2696 C  CD1 . TYR   A 1 343 ? -46.029 2.562   -19.266 1.00 34.96  ? 359 TYR   A CD1 1 
ATOM   2697 C  CD2 . TYR   A 1 343 ? -47.742 3.629   -20.569 1.00 36.50  ? 359 TYR   A CD2 1 
ATOM   2698 C  CE1 . TYR   A 1 343 ? -46.962 1.656   -18.779 1.00 39.52  ? 359 TYR   A CE1 1 
ATOM   2699 C  CE2 . TYR   A 1 343 ? -48.687 2.719   -20.074 1.00 40.62  ? 359 TYR   A CE2 1 
ATOM   2700 C  CZ  . TYR   A 1 343 ? -48.296 1.743   -19.194 1.00 41.61  ? 359 TYR   A CZ  1 
ATOM   2701 O  OH  . TYR   A 1 343 ? -49.228 0.856   -18.705 1.00 45.72  ? 359 TYR   A OH  1 
ATOM   2702 N  N   . LEU   A 1 344 ? -42.749 6.558   -19.850 1.00 37.50  ? 360 LEU   A N   1 
ATOM   2703 C  CA  . LEU   A 1 344 ? -41.587 7.285   -20.341 1.00 37.73  ? 360 LEU   A CA  1 
ATOM   2704 C  C   . LEU   A 1 344 ? -40.399 6.341   -20.453 1.00 40.45  ? 360 LEU   A C   1 
ATOM   2705 O  O   . LEU   A 1 344 ? -40.295 5.352   -19.717 1.00 37.53  ? 360 LEU   A O   1 
ATOM   2706 C  CB  . LEU   A 1 344 ? -41.225 8.458   -19.413 1.00 37.87  ? 360 LEU   A CB  1 
ATOM   2707 C  CG  . LEU   A 1 344 ? -42.353 9.434   -19.058 1.00 40.53  ? 360 LEU   A CG  1 
ATOM   2708 C  CD1 . LEU   A 1 344 ? -41.889 10.433  -17.975 1.00 39.39  ? 360 LEU   A CD1 1 
ATOM   2709 C  CD2 . LEU   A 1 344 ? -42.819 10.185  -20.279 1.00 37.63  ? 360 LEU   A CD2 1 
ATOM   2710 N  N   . LYS   A 1 345 ? -39.500 6.639   -21.386 1.00 37.10  ? 361 LYS   A N   1 
ATOM   2711 C  CA  . LYS   A 1 345 ? -38.272 5.864   -21.470 1.00 41.16  ? 361 LYS   A CA  1 
ATOM   2712 C  C   . LYS   A 1 345 ? -37.396 6.171   -20.261 1.00 42.86  ? 361 LYS   A C   1 
ATOM   2713 O  O   . LYS   A 1 345 ? -37.161 7.336   -19.940 1.00 41.83  ? 361 LYS   A O   1 
ATOM   2714 C  CB  . LYS   A 1 345 ? -37.526 6.173   -22.768 1.00 43.07  ? 361 LYS   A CB  1 
ATOM   2715 C  CG  . LYS   A 1 345 ? -38.240 5.688   -24.027 1.00 41.91  ? 361 LYS   A CG  1 
ATOM   2716 C  CD  . LYS   A 1 345 ? -38.276 4.165   -24.061 1.00 48.78  ? 361 LYS   A CD  1 
ATOM   2717 C  CE  . LYS   A 1 345 ? -38.883 3.641   -25.365 1.00 43.09  ? 361 LYS   A CE  1 
ATOM   2718 N  NZ  . LYS   A 1 345 ? -39.262 2.216   -25.205 1.00 45.27  ? 361 LYS   A NZ  1 
ATOM   2719 N  N   . ALA   A 1 346 ? -36.921 5.123   -19.588 1.00 45.35  ? 362 ALA   A N   1 
ATOM   2720 C  CA  . ALA   A 1 346 ? -36.055 5.301   -18.426 1.00 46.53  ? 362 ALA   A CA  1 
ATOM   2721 C  C   . ALA   A 1 346 ? -34.644 5.756   -18.808 1.00 50.31  ? 362 ALA   A C   1 
ATOM   2722 O  O   . ALA   A 1 346 ? -33.994 6.449   -18.021 1.00 53.70  ? 362 ALA   A O   1 
ATOM   2723 C  CB  . ALA   A 1 346 ? -35.983 3.992   -17.625 1.00 45.83  ? 362 ALA   A CB  1 
ATOM   2724 N  N   . LEU   A 1 347 ? -34.157 5.387   -19.993 1.00 47.48  ? 363 LEU   A N   1 
ATOM   2725 C  CA  . LEU   A 1 347 ? -32.789 5.670   -20.431 1.00 52.42  ? 363 LEU   A CA  1 
ATOM   2726 C  C   . LEU   A 1 347 ? -32.754 6.831   -21.422 1.00 54.53  ? 363 LEU   A C   1 
ATOM   2727 O  O   . LEU   A 1 347 ? -33.505 6.843   -22.404 1.00 53.34  ? 363 LEU   A O   1 
ATOM   2728 C  CB  . LEU   A 1 347 ? -32.164 4.431   -21.074 1.00 53.58  ? 363 LEU   A CB  1 
ATOM   2729 C  CG  . LEU   A 1 347 ? -32.216 3.125   -20.275 1.00 57.87  ? 363 LEU   A CG  1 
ATOM   2730 C  CD1 . LEU   A 1 347 ? -31.344 2.051   -20.913 1.00 56.45  ? 363 LEU   A CD1 1 
ATOM   2731 C  CD2 . LEU   A 1 347 ? -31.801 3.350   -18.822 1.00 61.28  ? 363 LEU   A CD2 1 
ATOM   2732 N  N   . SER   A 1 348 ? -31.854 7.789   -21.183 1.00 50.58  ? 364 SER   A N   1 
ATOM   2733 C  CA  . SER   A 1 348 ? -31.743 8.945   -22.061 1.00 55.27  ? 364 SER   A CA  1 
ATOM   2734 C  C   . SER   A 1 348 ? -31.328 8.568   -23.479 1.00 54.73  ? 364 SER   A C   1 
ATOM   2735 O  O   . SER   A 1 348 ? -31.558 9.348   -24.407 1.00 55.83  ? 364 SER   A O   1 
ATOM   2736 C  CB  . SER   A 1 348 ? -30.738 9.943   -21.490 1.00 57.20  ? 364 SER   A CB  1 
ATOM   2737 O  OG  . SER   A 1 348 ? -29.483 9.310   -21.313 1.00 68.12  ? 364 SER   A OG  1 
ATOM   2738 N  N   . THR   A 1 349 ? -30.713 7.407   -23.671 1.00 54.30  ? 365 THR   A N   1 
ATOM   2739 C  CA  . THR   A 1 349 ? -30.370 6.993   -25.024 1.00 59.01  ? 365 THR   A CA  1 
ATOM   2740 C  C   . THR   A 1 349 ? -31.577 6.455   -25.777 1.00 57.43  ? 365 THR   A C   1 
ATOM   2741 O  O   . THR   A 1 349 ? -31.594 6.515   -27.008 1.00 56.03  ? 365 THR   A O   1 
ATOM   2742 C  CB  . THR   A 1 349 ? -29.260 5.946   -24.986 1.00 57.81  ? 365 THR   A CB  1 
ATOM   2743 O  OG1 . THR   A 1 349 ? -29.569 4.962   -23.994 1.00 61.64  ? 365 THR   A OG1 1 
ATOM   2744 C  CG2 . THR   A 1 349 ? -27.943 6.598   -24.638 1.00 62.35  ? 365 THR   A CG2 1 
ATOM   2745 N  N   . ASP   A 1 350 ? -32.590 5.944   -25.064 1.00 52.40  ? 366 ASP   A N   1 
ATOM   2746 C  CA  . ASP   A 1 350 ? -33.837 5.514   -25.689 1.00 51.81  ? 366 ASP   A CA  1 
ATOM   2747 C  C   . ASP   A 1 350 ? -34.831 6.654   -25.901 1.00 48.15  ? 366 ASP   A C   1 
ATOM   2748 O  O   . ASP   A 1 350 ? -35.832 6.452   -26.599 1.00 48.23  ? 366 ASP   A O   1 
ATOM   2749 C  CB  . ASP   A 1 350 ? -34.536 4.437   -24.849 1.00 48.20  ? 366 ASP   A CB  1 
ATOM   2750 C  CG  . ASP   A 1 350 ? -33.791 3.113   -24.822 1.00 54.91  ? 366 ASP   A CG  1 
ATOM   2751 O  OD1 . ASP   A 1 350 ? -32.850 2.927   -25.612 1.00 56.15  ? 366 ASP   A OD1 1 
ATOM   2752 O  OD2 . ASP   A 1 350 ? -34.154 2.251   -23.992 1.00 56.12  ? 366 ASP   A OD2 1 
ATOM   2753 N  N   . SER   A 1 351 ? -34.610 7.821   -25.292 1.00 45.30  ? 367 SER   A N   1 
ATOM   2754 C  CA  . SER   A 1 351 ? -35.540 8.951   -25.395 1.00 50.94  ? 367 SER   A CA  1 
ATOM   2755 C  C   . SER   A 1 351 ? -35.211 9.729   -26.656 1.00 49.69  ? 367 SER   A C   1 
ATOM   2756 O  O   . SER   A 1 351 ? -34.406 10.658  -26.641 1.00 55.23  ? 367 SER   A O   1 
ATOM   2757 C  CB  . SER   A 1 351 ? -35.448 9.854   -24.174 1.00 47.39  ? 367 SER   A CB  1 
ATOM   2758 O  OG  . SER   A 1 351 ? -35.894 9.180   -23.018 1.00 56.49  ? 367 SER   A OG  1 
ATOM   2759 N  N   . VAL   A 1 352 ? -35.852 9.364   -27.760 1.00 49.29  ? 368 VAL   A N   1 
ATOM   2760 C  CA  . VAL   A 1 352 ? -35.549 9.936   -29.068 1.00 42.99  ? 368 VAL   A CA  1 
ATOM   2761 C  C   . VAL   A 1 352 ? -36.813 10.573  -29.631 1.00 43.52  ? 368 VAL   A C   1 
ATOM   2762 O  O   . VAL   A 1 352 ? -37.916 10.043  -29.461 1.00 46.11  ? 368 VAL   A O   1 
ATOM   2763 C  CB  . VAL   A 1 352 ? -35.008 8.848   -30.019 1.00 50.47  ? 368 VAL   A CB  1 
ATOM   2764 C  CG1 . VAL   A 1 352 ? -34.578 9.455   -31.337 1.00 52.23  ? 368 VAL   A CG1 1 
ATOM   2765 C  CG2 . VAL   A 1 352 ? -33.853 8.080   -29.346 1.00 51.65  ? 368 VAL   A CG2 1 
ATOM   2766 N  N   . GLU   A 1 353 ? -36.649 11.708  -30.307 1.00 47.39  ? 369 GLU   A N   1 
ATOM   2767 C  CA  . GLU   A 1 353 ? -37.773 12.390  -30.937 1.00 42.61  ? 369 GLU   A CA  1 
ATOM   2768 C  C   . GLU   A 1 353 ? -38.576 11.447  -31.836 1.00 47.93  ? 369 GLU   A C   1 
ATOM   2769 O  O   . GLU   A 1 353 ? -38.009 10.704  -32.645 1.00 49.03  ? 369 GLU   A O   1 
ATOM   2770 C  CB  . GLU   A 1 353 ? -37.254 13.560  -31.764 1.00 45.25  ? 369 GLU   A CB  1 
ATOM   2771 C  CG  . GLU   A 1 353 ? -36.602 14.691  -30.992 1.00 45.77  ? 369 GLU   A CG  1 
ATOM   2772 C  CD  . GLU   A 1 353 ? -36.329 15.861  -31.899 1.00 50.68  ? 369 GLU   A CD  1 
ATOM   2773 O  OE1 . GLU   A 1 353 ? -35.338 15.790  -32.677 1.00 52.22  ? 369 GLU   A OE1 1 
ATOM   2774 O  OE2 . GLU   A 1 353 ? -37.139 16.824  -31.886 1.00 46.79  ? 369 GLU   A OE2 1 
ATOM   2775 N  N   . ARG   A 1 354 ? -39.902 11.493  -31.706 1.00 46.12  ? 370 ARG   A N   1 
ATOM   2776 C  CA  . ARG   A 1 354 ? -40.805 10.818  -32.633 1.00 51.31  ? 370 ARG   A CA  1 
ATOM   2777 C  C   . ARG   A 1 354 ? -41.324 11.863  -33.618 1.00 49.08  ? 370 ARG   A C   1 
ATOM   2778 O  O   . ARG   A 1 354 ? -42.178 12.687  -33.261 1.00 47.61  ? 370 ARG   A O   1 
ATOM   2779 C  CB  . ARG   A 1 354 ? -41.982 10.144  -31.918 1.00 46.58  ? 370 ARG   A CB  1 
ATOM   2780 C  CG  . ARG   A 1 354 ? -42.957 9.577   -32.965 1.00 52.55  ? 370 ARG   A CG  1 
ATOM   2781 C  CD  . ARG   A 1 354 ? -43.980 8.630   -32.427 1.00 51.80  ? 370 ARG   A CD  1 
ATOM   2782 N  NE  . ARG   A 1 354 ? -43.348 7.615   -31.596 1.00 63.63  ? 370 ARG   A NE  1 
ATOM   2783 C  CZ  . ARG   A 1 354 ? -44.007 6.733   -30.856 1.00 66.99  ? 370 ARG   A CZ  1 
ATOM   2784 N  NH1 . ARG   A 1 354 ? -45.334 6.671   -30.870 1.00 60.87  ? 370 ARG   A NH1 1 
ATOM   2785 N  NH2 . ARG   A 1 354 ? -43.319 5.895   -30.080 1.00 69.34  ? 370 ARG   A NH2 1 
ATOM   2786 N  N   . LEU   A 1 355 ? -40.813 11.829  -34.845 1.00 43.66  ? 371 LEU   A N   1 
ATOM   2787 C  CA  . LEU   A 1 355 ? -41.111 12.847  -35.850 1.00 50.56  ? 371 LEU   A CA  1 
ATOM   2788 C  C   . LEU   A 1 355 ? -41.886 12.273  -37.031 1.00 55.16  ? 371 LEU   A C   1 
ATOM   2789 O  O   . LEU   A 1 355 ? -41.492 11.248  -37.590 1.00 56.19  ? 371 LEU   A O   1 
ATOM   2790 C  CB  . LEU   A 1 355 ? -39.817 13.483  -36.390 1.00 46.72  ? 371 LEU   A CB  1 
ATOM   2791 C  CG  . LEU   A 1 355 ? -38.860 14.012  -35.322 1.00 53.95  ? 371 LEU   A CG  1 
ATOM   2792 C  CD1 . LEU   A 1 355 ? -37.641 14.703  -35.925 1.00 49.41  ? 371 LEU   A CD1 1 
ATOM   2793 C  CD2 . LEU   A 1 355 ? -39.617 14.950  -34.416 1.00 47.69  ? 371 LEU   A CD2 1 
ATOM   2794 N  N   . PRO   A 1 356 ? -42.934 12.950  -37.489 1.00 54.38  ? 372 PRO   A N   1 
ATOM   2795 C  CA  . PRO   A 1 356 ? -43.540 12.578  -38.773 1.00 49.48  ? 372 PRO   A CA  1 
ATOM   2796 C  C   . PRO   A 1 356 ? -42.618 12.916  -39.934 1.00 55.73  ? 372 PRO   A C   1 
ATOM   2797 O  O   . PRO   A 1 356 ? -41.806 13.839  -39.853 1.00 55.88  ? 372 PRO   A O   1 
ATOM   2798 C  CB  . PRO   A 1 356 ? -44.811 13.431  -38.817 1.00 54.27  ? 372 PRO   A CB  1 
ATOM   2799 C  CG  . PRO   A 1 356 ? -44.437 14.686  -37.997 1.00 53.84  ? 372 PRO   A CG  1 
ATOM   2800 C  CD  . PRO   A 1 356 ? -43.563 14.140  -36.878 1.00 51.43  ? 372 PRO   A CD  1 
ATOM   2801 N  N   . VAL   A 1 357 ? -42.753 12.165  -41.035 1.00 56.82  ? 373 VAL   A N   1 
ATOM   2802 C  CA  . VAL   A 1 357 ? -42.047 12.460  -42.279 1.00 62.62  ? 373 VAL   A CA  1 
ATOM   2803 C  C   . VAL   A 1 357 ? -43.036 12.374  -43.433 1.00 66.17  ? 373 VAL   A C   1 
ATOM   2804 O  O   . VAL   A 1 357 ? -43.954 11.547  -43.418 1.00 73.56  ? 373 VAL   A O   1 
ATOM   2805 C  CB  . VAL   A 1 357 ? -40.844 11.514  -42.514 1.00 65.28  ? 373 VAL   A CB  1 
ATOM   2806 C  CG1 . VAL   A 1 357 ? -41.291 10.079  -42.671 1.00 72.92  ? 373 VAL   A CG1 1 
ATOM   2807 C  CG2 . VAL   A 1 357 ? -40.030 11.948  -43.758 1.00 65.44  ? 373 VAL   A CG2 1 
ATOM   2808 N  N   . TYR   A 1 358 ? -42.863 13.246  -44.422 1.00 67.33  ? 374 TYR   A N   1 
ATOM   2809 C  CA  . TYR   A 1 358 ? -43.683 13.235  -45.630 1.00 78.09  ? 374 TYR   A CA  1 
ATOM   2810 C  C   . TYR   A 1 358 ? -43.022 12.378  -46.709 1.00 82.33  ? 374 TYR   A C   1 
ATOM   2811 O  O   . TYR   A 1 358 ? -41.877 12.639  -47.100 1.00 87.37  ? 374 TYR   A O   1 
ATOM   2812 C  CB  . TYR   A 1 358 ? -43.910 14.655  -46.149 1.00 73.04  ? 374 TYR   A CB  1 
ATOM   2813 C  CG  . TYR   A 1 358 ? -44.475 14.689  -47.560 1.00 78.41  ? 374 TYR   A CG  1 
ATOM   2814 C  CD1 . TYR   A 1 358 ? -45.843 14.538  -47.788 1.00 78.83  ? 374 TYR   A CD1 1 
ATOM   2815 C  CD2 . TYR   A 1 358 ? -43.636 14.855  -48.668 1.00 80.66  ? 374 TYR   A CD2 1 
ATOM   2816 C  CE1 . TYR   A 1 358 ? -46.366 14.559  -49.087 1.00 84.87  ? 374 TYR   A CE1 1 
ATOM   2817 C  CE2 . TYR   A 1 358 ? -44.146 14.875  -49.971 1.00 84.51  ? 374 TYR   A CE2 1 
ATOM   2818 C  CZ  . TYR   A 1 358 ? -45.512 14.728  -50.173 1.00 87.63  ? 374 TYR   A CZ  1 
ATOM   2819 O  OH  . TYR   A 1 358 ? -46.018 14.749  -51.459 1.00 94.09  ? 374 TYR   A OH  1 
ATOM   2820 N  N   . ASN   A 1 359 ? -43.750 11.378  -47.199 1.00 97.68  ? 375 ASN   A N   1 
ATOM   2821 C  CA  . ASN   A 1 359 ? -43.350 10.563  -48.348 1.00 100.21 ? 375 ASN   A CA  1 
ATOM   2822 C  C   . ASN   A 1 359 ? -44.615 9.943   -48.944 1.00 112.42 ? 375 ASN   A C   1 
ATOM   2823 O  O   . ASN   A 1 359 ? -45.729 10.413  -48.681 1.00 113.09 ? 375 ASN   A O   1 
ATOM   2824 C  CB  . ASN   A 1 359 ? -42.302 9.510   -47.941 1.00 102.90 ? 375 ASN   A CB  1 
ATOM   2825 C  CG  . ASN   A 1 359 ? -42.665 8.772   -46.655 1.00 102.90 ? 375 ASN   A CG  1 
ATOM   2826 O  OD1 . ASN   A 1 359 ? -43.810 8.800   -46.200 1.00 103.30 ? 375 ASN   A OD1 1 
ATOM   2827 N  ND2 . ASN   A 1 359 ? -41.678 8.103   -46.064 1.00 99.32  ? 375 ASN   A ND2 1 
ATOM   2828 N  N   . LYS   A 1 360 ? -44.447 8.887   -49.749 1.00 117.96 ? 376 LYS   A N   1 
ATOM   2829 C  CA  . LYS   A 1 360 ? -45.600 8.174   -50.287 1.00 117.11 ? 376 LYS   A CA  1 
ATOM   2830 C  C   . LYS   A 1 360 ? -46.236 7.233   -49.272 1.00 118.11 ? 376 LYS   A C   1 
ATOM   2831 O  O   . LYS   A 1 360 ? -47.404 6.861   -49.439 1.00 120.57 ? 376 LYS   A O   1 
ATOM   2832 C  CB  . LYS   A 1 360 ? -45.207 7.397   -51.538 1.00 112.55 ? 376 LYS   A CB  1 
ATOM   2833 C  CG  . LYS   A 1 360 ? -44.927 8.298   -52.716 1.00 123.49 ? 376 LYS   A CG  1 
ATOM   2834 C  CD  . LYS   A 1 360 ? -46.052 9.302   -52.893 1.00 124.03 ? 376 LYS   A CD  1 
ATOM   2835 C  CE  . LYS   A 1 360 ? -45.804 10.196  -54.097 1.00 129.28 ? 376 LYS   A CE  1 
ATOM   2836 N  NZ  . LYS   A 1 360 ? -45.633 9.412   -55.351 1.00 129.00 ? 376 LYS   A NZ  1 
ATOM   2837 N  N   . SER   A 1 361 ? -45.496 6.843   -48.230 1.00 113.22 ? 377 SER   A N   1 
ATOM   2838 C  CA  . SER   A 1 361 ? -46.089 6.058   -47.150 1.00 115.62 ? 377 SER   A CA  1 
ATOM   2839 C  C   . SER   A 1 361 ? -47.155 6.862   -46.406 1.00 116.68 ? 377 SER   A C   1 
ATOM   2840 O  O   . SER   A 1 361 ? -48.202 6.319   -46.032 1.00 114.14 ? 377 SER   A O   1 
ATOM   2841 C  CB  . SER   A 1 361 ? -44.995 5.580   -46.191 1.00 106.13 ? 377 SER   A CB  1 
ATOM   2842 O  OG  . SER   A 1 361 ? -45.512 4.710   -45.199 1.00 103.40 ? 377 SER   A OG  1 
ATOM   2843 N  N   . ALA   A 1 362 ? -46.908 8.162   -46.187 1.00 124.66 ? 378 ALA   A N   1 
ATOM   2844 C  CA  . ALA   A 1 362 ? -47.927 9.059   -45.653 1.00 122.50 ? 378 ALA   A CA  1 
ATOM   2845 C  C   . ALA   A 1 362 ? -48.944 9.484   -46.711 1.00 127.35 ? 378 ALA   A C   1 
ATOM   2846 O  O   . ALA   A 1 362 ? -50.078 9.822   -46.354 1.00 126.53 ? 378 ALA   A O   1 
ATOM   2847 C  CB  . ALA   A 1 362 ? -47.270 10.301  -45.043 1.00 114.59 ? 378 ALA   A CB  1 
ATOM   2848 N  N   . TRP   A 1 363 ? -48.570 9.455   -47.996 1.00 122.00 ? 379 TRP   A N   1 
ATOM   2849 C  CA  . TRP   A 1 363 ? -49.448 9.927   -49.062 1.00 124.85 ? 379 TRP   A CA  1 
ATOM   2850 C  C   . TRP   A 1 363 ? -50.718 9.090   -49.189 1.00 123.95 ? 379 TRP   A C   1 
ATOM   2851 O  O   . TRP   A 1 363 ? -51.775 9.627   -49.541 1.00 121.16 ? 379 TRP   A O   1 
ATOM   2852 C  CB  . TRP   A 1 363 ? -48.684 9.920   -50.388 1.00 127.49 ? 379 TRP   A CB  1 
ATOM   2853 C  CG  . TRP   A 1 363 ? -49.482 10.364  -51.582 1.00 130.00 ? 379 TRP   A CG  1 
ATOM   2854 C  CD1 . TRP   A 1 363 ? -49.457 11.596  -52.164 1.00 130.39 ? 379 TRP   A CD1 1 
ATOM   2855 C  CD2 . TRP   A 1 363 ? -50.412 9.577   -52.346 1.00 134.97 ? 379 TRP   A CD2 1 
ATOM   2856 N  NE1 . TRP   A 1 363 ? -50.317 11.630  -53.236 1.00 138.54 ? 379 TRP   A NE1 1 
ATOM   2857 C  CE2 . TRP   A 1 363 ? -50.915 10.404  -53.368 1.00 140.20 ? 379 TRP   A CE2 1 
ATOM   2858 C  CE3 . TRP   A 1 363 ? -50.866 8.256   -52.265 1.00 134.35 ? 379 TRP   A CE3 1 
ATOM   2859 C  CZ2 . TRP   A 1 363 ? -51.853 9.955   -54.299 1.00 140.33 ? 379 TRP   A CZ2 1 
ATOM   2860 C  CZ3 . TRP   A 1 363 ? -51.800 7.814   -53.187 1.00 132.67 ? 379 TRP   A CZ3 1 
ATOM   2861 C  CH2 . TRP   A 1 363 ? -52.282 8.660   -54.189 1.00 137.04 ? 379 TRP   A CH2 1 
ATOM   2862 N  N   . ARG   A 1 364 ? -50.635 7.775   -48.951 1.00 124.09 ? 380 ARG   A N   1 
ATOM   2863 C  CA  . ARG   A 1 364 ? -51.775 6.895   -49.180 1.00 127.87 ? 380 ARG   A CA  1 
ATOM   2864 C  C   . ARG   A 1 364 ? -52.713 6.812   -47.983 1.00 122.14 ? 380 ARG   A C   1 
ATOM   2865 O  O   . ARG   A 1 364 ? -53.855 6.362   -48.139 1.00 119.43 ? 380 ARG   A O   1 
ATOM   2866 C  CB  . ARG   A 1 364 ? -51.293 5.490   -49.564 1.00 131.15 ? 380 ARG   A CB  1 
ATOM   2867 C  CG  . ARG   A 1 364 ? -52.266 4.745   -50.479 1.00 130.84 ? 380 ARG   A CG  1 
ATOM   2868 C  CD  . ARG   A 1 364 ? -51.681 3.458   -51.051 1.00 134.42 ? 380 ARG   A CD  1 
ATOM   2869 N  NE  . ARG   A 1 364 ? -50.871 3.682   -52.244 1.00 135.35 ? 380 ARG   A NE  1 
ATOM   2870 C  CZ  . ARG   A 1 364 ? -49.617 3.275   -52.392 1.00 136.75 ? 380 ARG   A CZ  1 
ATOM   2871 N  NH1 . ARG   A 1 364 ? -48.987 2.609   -51.436 1.00 135.16 ? 380 ARG   A NH1 1 
ATOM   2872 N  NH2 . ARG   A 1 364 ? -48.981 3.532   -53.533 1.00 133.13 ? 380 ARG   A NH2 1 
ATOM   2873 N  N   . HIS   A 1 365 ? -52.259 7.235   -46.799 1.00 119.38 ? 381 HIS   A N   1 
ATOM   2874 C  CA  . HIS   A 1 365 ? -53.150 7.338   -45.648 1.00 111.65 ? 381 HIS   A CA  1 
ATOM   2875 C  C   . HIS   A 1 365 ? -54.315 8.274   -45.933 1.00 113.77 ? 381 HIS   A C   1 
ATOM   2876 O  O   . HIS   A 1 365 ? -55.456 7.996   -45.544 1.00 113.12 ? 381 HIS   A O   1 
ATOM   2877 C  CB  . HIS   A 1 365 ? -52.375 7.830   -44.434 1.00 104.46 ? 381 HIS   A CB  1 
ATOM   2878 C  CG  . HIS   A 1 365 ? -51.602 6.757   -43.735 1.00 107.70 ? 381 HIS   A CG  1 
ATOM   2879 N  ND1 . HIS   A 1 365 ? -50.413 6.257   -44.224 1.00 107.67 ? 381 HIS   A ND1 1 
ATOM   2880 C  CD2 . HIS   A 1 365 ? -51.844 6.094   -42.578 1.00 98.81  ? 381 HIS   A CD2 1 
ATOM   2881 C  CE1 . HIS   A 1 365 ? -49.958 5.331   -43.398 1.00 108.38 ? 381 HIS   A CE1 1 
ATOM   2882 N  NE2 . HIS   A 1 365 ? -50.807 5.214   -42.391 1.00 104.81 ? 381 HIS   A NE2 1 
ATOM   2883 N  N   . TYR   A 1 366 ? -54.043 9.395   -46.608 1.00 115.31 ? 382 TYR   A N   1 
ATOM   2884 C  CA  . TYR   A 1 366 ? -55.090 10.362  -46.923 1.00 105.05 ? 382 TYR   A CA  1 
ATOM   2885 C  C   . TYR   A 1 366 ? -56.065 9.815   -47.957 1.00 114.92 ? 382 TYR   A C   1 
ATOM   2886 O  O   . TYR   A 1 366 ? -57.250 10.174  -47.947 1.00 110.67 ? 382 TYR   A O   1 
ATOM   2887 C  CB  . TYR   A 1 366 ? -54.447 11.676  -47.387 1.00 94.63  ? 382 TYR   A CB  1 
ATOM   2888 C  CG  . TYR   A 1 366 ? -53.664 12.352  -46.270 1.00 96.05  ? 382 TYR   A CG  1 
ATOM   2889 C  CD1 . TYR   A 1 366 ? -52.340 12.002  -45.999 1.00 90.52  ? 382 TYR   A CD1 1 
ATOM   2890 C  CD2 . TYR   A 1 366 ? -54.266 13.308  -45.454 1.00 90.81  ? 382 TYR   A CD2 1 
ATOM   2891 C  CE1 . TYR   A 1 366 ? -51.634 12.604  -44.963 1.00 79.42  ? 382 TYR   A CE1 1 
ATOM   2892 C  CE2 . TYR   A 1 366 ? -53.572 13.909  -44.415 1.00 76.13  ? 382 TYR   A CE2 1 
ATOM   2893 C  CZ  . TYR   A 1 366 ? -52.259 13.555  -44.176 1.00 75.01  ? 382 TYR   A CZ  1 
ATOM   2894 O  OH  . TYR   A 1 366 ? -51.590 14.163  -43.142 1.00 67.04  ? 382 TYR   A OH  1 
ATOM   2895 N  N   . GLN   A 1 367 ? -55.601 8.925   -48.827 1.00 123.04 ? 383 GLN   A N   1 
ATOM   2896 C  CA  . GLN   A 1 367 ? -56.455 8.331   -49.843 1.00 124.22 ? 383 GLN   A CA  1 
ATOM   2897 C  C   . GLN   A 1 367 ? -57.481 7.368   -49.244 1.00 125.33 ? 383 GLN   A C   1 
ATOM   2898 O  O   . GLN   A 1 367 ? -58.677 7.669   -49.193 1.00 122.24 ? 383 GLN   A O   1 
ATOM   2899 C  CB  . GLN   A 1 367 ? -55.602 7.614   -50.889 1.00 123.40 ? 383 GLN   A CB  1 
ATOM   2900 C  CG  . GLN   A 1 367 ? -56.404 6.784   -51.881 1.00 134.75 ? 383 GLN   A CG  1 
ATOM   2901 C  CD  . GLN   A 1 367 ? -57.443 7.591   -52.659 1.00 138.48 ? 383 GLN   A CD  1 
ATOM   2902 O  OE1 . GLN   A 1 367 ? -57.478 8.824   -52.604 1.00 134.15 ? 383 GLN   A OE1 1 
ATOM   2903 N  NE2 . GLN   A 1 367 ? -58.295 6.888   -53.397 1.00 139.34 ? 383 GLN   A NE2 1 
ATOM   2904 N  N   . GLY   A 1 373 ? -65.993 -3.097  -43.182 1.00 98.86  ? 389 GLY   A N   1 
ATOM   2905 C  CA  . GLY   A 1 373 ? -67.170 -3.948  -43.202 1.00 92.10  ? 389 GLY   A CA  1 
ATOM   2906 C  C   . GLY   A 1 373 ? -66.892 -5.442  -43.317 1.00 92.02  ? 389 GLY   A C   1 
ATOM   2907 O  O   . GLY   A 1 373 ? -67.507 -6.132  -44.131 1.00 88.84  ? 389 GLY   A O   1 
ATOM   2908 N  N   . ASP   A 1 374 ? -65.971 -5.952  -42.492 1.00 88.94  ? 390 ASP   A N   1 
ATOM   2909 C  CA  . ASP   A 1 374 ? -65.602 -7.366  -42.506 1.00 85.61  ? 390 ASP   A CA  1 
ATOM   2910 C  C   . ASP   A 1 374 ? -66.100 -8.124  -41.275 1.00 78.49  ? 390 ASP   A C   1 
ATOM   2911 O  O   . ASP   A 1 374 ? -65.779 -9.309  -41.116 1.00 73.33  ? 390 ASP   A O   1 
ATOM   2912 C  CB  . ASP   A 1 374 ? -64.080 -7.522  -42.644 1.00 85.18  ? 390 ASP   A CB  1 
ATOM   2913 C  CG  . ASP   A 1 374 ? -63.313 -6.727  -41.602 1.00 84.76  ? 390 ASP   A CG  1 
ATOM   2914 O  OD1 . ASP   A 1 374 ? -63.879 -5.738  -41.094 1.00 89.30  ? 390 ASP   A OD1 1 
ATOM   2915 O  OD2 . ASP   A 1 374 ? -62.149 -7.073  -41.290 1.00 81.12  ? 390 ASP   A OD2 1 
ATOM   2916 N  N   . TRP   A 1 375 ? -66.884 -7.480  -40.409 1.00 75.01  ? 391 TRP   A N   1 
ATOM   2917 C  CA  . TRP   A 1 375 ? -67.551 -8.152  -39.302 1.00 66.49  ? 391 TRP   A CA  1 
ATOM   2918 C  C   . TRP   A 1 375 ? -69.064 -8.075  -39.481 1.00 73.25  ? 391 TRP   A C   1 
ATOM   2919 O  O   . TRP   A 1 375 ? -69.580 -7.265  -40.259 1.00 77.74  ? 391 TRP   A O   1 
ATOM   2920 C  CB  . TRP   A 1 375 ? -67.119 -7.557  -37.965 1.00 68.66  ? 391 TRP   A CB  1 
ATOM   2921 C  CG  . TRP   A 1 375 ? -65.648 -7.701  -37.761 1.00 73.87  ? 391 TRP   A CG  1 
ATOM   2922 C  CD1 . TRP   A 1 375 ? -64.671 -6.846  -38.195 1.00 77.10  ? 391 TRP   A CD1 1 
ATOM   2923 C  CD2 . TRP   A 1 375 ? -64.969 -8.778  -37.099 1.00 70.55  ? 391 TRP   A CD2 1 
ATOM   2924 N  NE1 . TRP   A 1 375 ? -63.427 -7.316  -37.835 1.00 69.66  ? 391 TRP   A NE1 1 
ATOM   2925 C  CE2 . TRP   A 1 375 ? -63.580 -8.498  -37.159 1.00 71.85  ? 391 TRP   A CE2 1 
ATOM   2926 C  CE3 . TRP   A 1 375 ? -65.398 -9.946  -36.452 1.00 63.07  ? 391 TRP   A CE3 1 
ATOM   2927 C  CZ2 . TRP   A 1 375 ? -62.619 -9.343  -36.594 1.00 68.82  ? 391 TRP   A CZ2 1 
ATOM   2928 C  CZ3 . TRP   A 1 375 ? -64.428 -10.797 -35.895 1.00 61.73  ? 391 TRP   A CZ3 1 
ATOM   2929 C  CH2 . TRP   A 1 375 ? -63.059 -10.483 -35.972 1.00 61.97  ? 391 TRP   A CH2 1 
ATOM   2930 N  N   . CYS   A 1 376 ? -69.774 -8.966  -38.789 1.00 69.34  ? 392 CYS   A N   1 
ATOM   2931 C  CA  . CYS   A 1 376 ? -71.210 -9.114  -38.995 1.00 72.62  ? 392 CYS   A CA  1 
ATOM   2932 C  C   . CYS   A 1 376 ? -71.991 -8.101  -38.165 1.00 80.65  ? 392 CYS   A C   1 
ATOM   2933 O  O   . CYS   A 1 376 ? -71.539 -7.640  -37.113 1.00 70.60  ? 392 CYS   A O   1 
ATOM   2934 C  CB  . CYS   A 1 376 ? -71.683 -10.516 -38.617 1.00 60.15  ? 392 CYS   A CB  1 
ATOM   2935 S  SG  . CYS   A 1 376 ? -71.279 -11.871 -39.734 1.00 69.98  ? 392 CYS   A SG  1 
ATOM   2936 N  N   . VAL   A 1 377 ? -73.183 -7.763  -38.651 1.00 93.43  ? 393 VAL   A N   1 
ATOM   2937 C  CA  . VAL   A 1 377 ? -74.134 -6.949  -37.897 1.00 92.49  ? 393 VAL   A CA  1 
ATOM   2938 C  C   . VAL   A 1 377 ? -75.461 -7.701  -37.884 1.00 89.21  ? 393 VAL   A C   1 
ATOM   2939 O  O   . VAL   A 1 377 ? -75.758 -8.434  -38.840 1.00 87.56  ? 393 VAL   A O   1 
ATOM   2940 C  CB  . VAL   A 1 377 ? -74.260 -5.537  -38.491 1.00 91.70  ? 393 VAL   A CB  1 
ATOM   2941 C  CG1 . VAL   A 1 377 ? -72.987 -4.753  -38.223 1.00 90.64  ? 393 VAL   A CG1 1 
ATOM   2942 C  CG2 . VAL   A 1 377 ? -74.539 -5.606  -39.989 1.00 91.19  ? 393 VAL   A CG2 1 
ATOM   2943 N  N   . PRO   A 1 378 ? -76.269 -7.595  -36.811 1.00 88.40  ? 394 PRO   A N   1 
ATOM   2944 C  CA  . PRO   A 1 378 ? -77.535 -8.341  -36.693 1.00 88.88  ? 394 PRO   A CA  1 
ATOM   2945 C  C   . PRO   A 1 378 ? -78.545 -8.101  -37.833 1.00 89.88  ? 394 PRO   A C   1 
ATOM   2946 O  O   . PRO   A 1 378 ? -78.720 -6.978  -38.310 1.00 92.07  ? 394 PRO   A O   1 
ATOM   2947 C  CB  . PRO   A 1 378 ? -78.094 -7.848  -35.353 1.00 87.86  ? 394 PRO   A CB  1 
ATOM   2948 C  CG  . PRO   A 1 378 ? -76.874 -7.505  -34.551 1.00 84.51  ? 394 PRO   A CG  1 
ATOM   2949 C  CD  . PRO   A 1 378 ? -75.902 -6.924  -35.547 1.00 88.07  ? 394 PRO   A CD  1 
HETATM 2950 S  S   . SO4   B 2 .   ? -73.803 7.704   -27.050 1.00 90.25  ? 401 SO4   A S   1 
HETATM 2951 O  O1  . SO4   B 2 .   ? -73.020 8.763   -26.404 1.00 77.37  ? 401 SO4   A O1  1 
HETATM 2952 O  O2  . SO4   B 2 .   ? -74.077 6.650   -26.068 1.00 79.93  ? 401 SO4   A O2  1 
HETATM 2953 O  O3  . SO4   B 2 .   ? -75.074 8.255   -27.518 1.00 91.11  ? 401 SO4   A O3  1 
HETATM 2954 O  O4  . SO4   B 2 .   ? -73.097 7.148   -28.202 1.00 74.02  ? 401 SO4   A O4  1 
HETATM 2955 C  C1  . TF3   C 3 .   ? -60.256 14.927  -44.402 1.00 62.55  ? 402 TF3   A C1  1 
HETATM 2956 C  C2  . TF3   C 3 .   ? -59.278 14.262  -45.134 1.00 59.72  ? 402 TF3   A C2  1 
HETATM 2957 C  C3  . TF3   C 3 .   ? -61.577 14.526  -44.538 1.00 66.12  ? 402 TF3   A C3  1 
HETATM 2958 O  O1  . TF3   C 3 .   ? -59.819 15.924  -43.566 1.00 60.78  ? 402 TF3   A O1  1 
HETATM 2959 C  C4  . TF3   C 3 .   ? -59.603 13.227  -45.986 1.00 62.47  ? 402 TF3   A C4  1 
HETATM 2960 CL CL1 . TF3   C 3 .   ? -57.612 14.697  -44.931 1.00 76.98  ? 402 TF3   A CL1 1 
HETATM 2961 C  C5  . TF3   C 3 .   ? -61.902 13.486  -45.396 1.00 64.23  ? 402 TF3   A C5  1 
HETATM 2962 C  C6  . TF3   C 3 .   ? -60.787 16.684  -42.839 1.00 59.83  ? 402 TF3   A C6  1 
HETATM 2963 C  C7  . TF3   C 3 .   ? -60.926 12.827  -46.134 1.00 71.47  ? 402 TF3   A C7  1 
HETATM 2964 C  C8  . TF3   C 3 .   ? -60.066 17.743  -42.053 1.00 54.32  ? 402 TF3   A C8  1 
HETATM 2965 C  C9  . TF3   C 3 .   ? -61.287 11.730  -47.110 1.00 76.03  ? 402 TF3   A C9  1 
HETATM 2966 C  C10 . TF3   C 3 .   ? -60.752 18.812  -41.495 1.00 50.88  ? 402 TF3   A C10 1 
HETATM 2967 C  C11 . TF3   C 3 .   ? -58.694 17.675  -41.861 1.00 49.80  ? 402 TF3   A C11 1 
HETATM 2968 C  C12 . TF3   C 3 .   ? -61.138 12.211  -48.540 1.00 83.20  ? 402 TF3   A C12 1 
HETATM 2969 C  C13 . TF3   C 3 .   ? -60.084 19.788  -40.775 1.00 53.90  ? 402 TF3   A C13 1 
HETATM 2970 C  C14 . TF3   C 3 .   ? -58.026 18.653  -41.143 1.00 44.97  ? 402 TF3   A C14 1 
HETATM 2971 N  N1  . TF3   C 3 .   ? -60.136 11.678  -49.239 1.00 88.46  ? 402 TF3   A N1  1 
HETATM 2972 O  O2  . TF3   C 3 .   ? -61.898 13.054  -49.010 1.00 78.93  ? 402 TF3   A O2  1 
HETATM 2973 C  C15 . TF3   C 3 .   ? -58.709 19.731  -40.598 1.00 52.95  ? 402 TF3   A C15 1 
HETATM 2974 C  C16 . TF3   C 3 .   ? -59.868 12.029  -50.628 1.00 94.93  ? 402 TF3   A C16 1 
HETATM 2975 C  C17 . TF3   C 3 .   ? -57.965 20.844  -39.878 1.00 55.39  ? 402 TF3   A C17 1 
HETATM 2976 C  C18 . TF3   C 3 .   ? -60.960 11.416  -51.561 1.00 94.61  ? 402 TF3   A C18 1 
HETATM 2977 C  C19 . TF3   C 3 .   ? -57.353 20.359  -38.567 1.00 52.27  ? 402 TF3   A C19 1 
HETATM 2978 C  C20 . TF3   C 3 .   ? -58.881 22.028  -39.610 1.00 58.83  ? 402 TF3   A C20 1 
HETATM 2979 N  N2  . TF3   C 3 .   ? -60.673 11.830  -52.935 1.00 106.04 ? 402 TF3   A N2  1 
HETATM 2980 C  C1  . EDO   D 4 .   ? -42.524 3.546   -23.800 1.00 45.51  ? 403 EDO   A C1  1 
HETATM 2981 O  O1  . EDO   D 4 .   ? -42.208 2.292   -24.452 1.00 55.60  ? 403 EDO   A O1  1 
HETATM 2982 C  C2  . EDO   D 4 .   ? -41.818 3.689   -22.443 1.00 47.66  ? 403 EDO   A C2  1 
HETATM 2983 O  O2  . EDO   D 4 .   ? -40.631 2.862   -22.347 1.00 47.46  ? 403 EDO   A O2  1 
HETATM 2984 C  C1  . GOL   E 5 .   ? -39.356 35.153  -25.490 1.00 84.49  ? 404 GOL   A C1  1 
HETATM 2985 O  O1  . GOL   E 5 .   ? -40.637 34.731  -25.087 1.00 76.66  ? 404 GOL   A O1  1 
HETATM 2986 C  C2  . GOL   E 5 .   ? -38.326 34.605  -24.454 1.00 85.20  ? 404 GOL   A C2  1 
HETATM 2987 O  O2  . GOL   E 5 .   ? -38.030 35.547  -23.490 1.00 98.78  ? 404 GOL   A O2  1 
HETATM 2988 C  C3  . GOL   E 5 .   ? -37.057 34.203  -25.266 1.00 90.09  ? 404 GOL   A C3  1 
HETATM 2989 O  O3  . GOL   E 5 .   ? -36.701 32.909  -24.862 1.00 90.67  ? 404 GOL   A O3  1 
HETATM 2990 S  S   . SO4   F 2 .   ? -43.707 23.636  -24.983 1.00 102.17 ? 405 SO4   A S   1 
HETATM 2991 O  O1  . SO4   F 2 .   ? -42.432 22.901  -24.989 1.00 77.73  ? 405 SO4   A O1  1 
HETATM 2992 O  O2  . SO4   F 2 .   ? -44.549 23.101  -26.078 1.00 78.65  ? 405 SO4   A O2  1 
HETATM 2993 O  O3  . SO4   F 2 .   ? -44.319 23.501  -23.643 1.00 74.54  ? 405 SO4   A O3  1 
HETATM 2994 O  O4  . SO4   F 2 .   ? -43.466 25.063  -25.236 1.00 85.38  ? 405 SO4   A O4  1 
HETATM 2995 C  C10 . A1EQH G 6 .   ? -56.926 10.380  -14.108 1.00 41.50  ? 406 A1EQH A C10 1 
HETATM 2996 C  C11 . A1EQH G 6 .   ? -56.644 9.471   -12.903 1.00 38.98  ? 406 A1EQH A C11 1 
HETATM 2997 C  C13 . A1EQH G 6 .   ? -58.850 11.659  -17.704 1.00 42.01  ? 406 A1EQH A C13 1 
HETATM 2998 C  C15 . A1EQH G 6 .   ? -60.967 11.260  -16.728 1.00 39.81  ? 406 A1EQH A C15 1 
HETATM 2999 C  C16 . A1EQH G 6 .   ? -63.381 12.702  -18.055 1.00 41.09  ? 406 A1EQH A C16 1 
HETATM 3000 C  C17 . A1EQH G 6 .   ? -64.390 13.026  -18.941 1.00 42.75  ? 406 A1EQH A C17 1 
HETATM 3001 C  C18 . A1EQH G 6 .   ? -65.639 10.911  -21.778 1.00 43.10  ? 406 A1EQH A C18 1 
HETATM 3002 C  C19 . A1EQH G 6 .   ? -65.858 10.276  -22.992 1.00 47.31  ? 406 A1EQH A C19 1 
HETATM 3003 C  C20 . A1EQH G 6 .   ? -66.996 10.541  -23.737 1.00 50.09  ? 406 A1EQH A C20 1 
HETATM 3004 N  N   . A1EQH G 6 .   ? -62.336 11.134  -16.503 1.00 40.08  ? 406 A1EQH A N   1 
HETATM 3005 C  C   . A1EQH G 6 .   ? -67.930 11.438  -23.237 1.00 56.88  ? 406 A1EQH A C   1 
HETATM 3006 O  O   . A1EQH G 6 .   ? -69.569 10.929  -25.163 1.00 61.60  ? 406 A1EQH A O   1 
HETATM 3007 C  C1  . A1EQH G 6 .   ? -67.737 12.059  -22.014 1.00 49.65  ? 406 A1EQH A C1  1 
HETATM 3008 C  C12 . A1EQH G 6 .   ? -58.188 11.263  -16.562 1.00 42.88  ? 406 A1EQH A C12 1 
HETATM 3009 C  C14 . A1EQH G 6 .   ? -60.225 11.674  -17.835 1.00 39.06  ? 406 A1EQH A C14 1 
HETATM 3010 C  C2  . A1EQH G 6 .   ? -66.588 11.792  -21.292 1.00 51.37  ? 406 A1EQH A C2  1 
HETATM 3011 C  C3  . A1EQH G 6 .   ? -65.399 12.113  -19.198 1.00 45.07  ? 406 A1EQH A C3  1 
HETATM 3012 C  C4  . A1EQH G 6 .   ? -65.409 10.883  -18.562 1.00 43.13  ? 406 A1EQH A C4  1 
HETATM 3013 C  C5  . A1EQH G 6 .   ? -64.401 10.564  -17.674 1.00 44.28  ? 406 A1EQH A C5  1 
HETATM 3014 C  C6  . A1EQH G 6 .   ? -63.382 11.466  -17.430 1.00 43.05  ? 406 A1EQH A C6  1 
HETATM 3015 C  C7  . A1EQH G 6 .   ? -62.562 10.663  -15.202 1.00 37.55  ? 406 A1EQH A C7  1 
HETATM 3016 C  C8  . A1EQH G 6 .   ? -60.347 10.849  -15.577 1.00 37.98  ? 406 A1EQH A C8  1 
HETATM 3017 C  C9  . A1EQH G 6 .   ? -58.956 10.857  -15.477 1.00 38.98  ? 406 A1EQH A C9  1 
HETATM 3018 F  F   . A1EQH G 6 .   ? -58.103 12.070  -18.758 1.00 41.88  ? 406 A1EQH A F   1 
HETATM 3019 N  N1  . A1EQH G 6 .   ? -61.322 10.494  -14.652 1.00 35.57  ? 406 A1EQH A N1  1 
HETATM 3020 N  N2  . A1EQH G 6 .   ? -58.381 10.446  -14.309 1.00 41.49  ? 406 A1EQH A N2  1 
HETATM 3021 O  O1  . A1EQH G 6 .   ? -70.392 11.934  -23.145 1.00 62.49  ? 406 A1EQH A O1  1 
HETATM 3022 O  O2  . A1EQH G 6 .   ? -66.432 12.449  -20.073 1.00 44.71  ? 406 A1EQH A O2  1 
HETATM 3023 O  O3  . A1EQH G 6 .   ? -63.639 10.426  -14.690 1.00 43.43  ? 406 A1EQH A O3  1 
HETATM 3024 S  S   . A1EQH G 6 .   ? -69.340 11.824  -24.080 1.00 69.41  ? 406 A1EQH A S   1 
HETATM 3025 O  O   . HOH   H 7 .   ? -36.565 -3.913  -21.873 1.00 58.54  ? 501 HOH   A O   1 
HETATM 3026 O  O   . HOH   H 7 .   ? -31.008 11.832  -35.937 1.00 59.59  ? 502 HOH   A O   1 
HETATM 3027 O  O   . HOH   H 7 .   ? -41.061 -0.341  -23.087 1.00 48.22  ? 503 HOH   A O   1 
HETATM 3028 O  O   . HOH   H 7 .   ? -41.873 11.107  -23.660 1.00 39.12  ? 504 HOH   A O   1 
HETATM 3029 O  O   . HOH   H 7 .   ? -47.022 25.824  -35.549 1.00 48.87  ? 505 HOH   A O   1 
HETATM 3030 O  O   . HOH   H 7 .   ? -49.429 23.251  -18.429 1.00 53.25  ? 506 HOH   A O   1 
HETATM 3031 O  O   . HOH   H 7 .   ? -61.282 28.052  -40.791 1.00 53.98  ? 507 HOH   A O   1 
HETATM 3032 O  O   . HOH   H 7 .   ? -64.860 26.789  -43.273 1.00 55.83  ? 508 HOH   A O   1 
HETATM 3033 O  O   . HOH   H 7 .   ? -60.979 13.736  -34.522 1.00 54.10  ? 509 HOH   A O   1 
HETATM 3034 O  O   . HOH   H 7 .   ? -58.965 17.413  -23.567 1.00 46.31  ? 510 HOH   A O   1 
HETATM 3035 O  O   . HOH   H 7 .   ? -39.235 11.268  -7.798  1.00 55.11  ? 511 HOH   A O   1 
HETATM 3036 O  O   . HOH   H 7 .   ? -33.451 -0.065  -23.307 1.00 63.61  ? 512 HOH   A O   1 
HETATM 3037 O  O   . HOH   H 7 .   ? -32.663 16.381  -41.365 1.00 57.76  ? 513 HOH   A O   1 
HETATM 3038 O  O   . HOH   H 7 .   ? -42.159 18.579  -39.285 1.00 46.94  ? 514 HOH   A O   1 
HETATM 3039 O  O   . HOH   H 7 .   ? -49.627 32.957  -33.308 1.00 69.27  ? 515 HOH   A O   1 
HETATM 3040 O  O   . HOH   H 7 .   ? -52.184 9.363   -34.883 1.00 63.63  ? 516 HOH   A O   1 
HETATM 3041 O  O   . HOH   H 7 .   ? -33.816 2.287   -14.923 1.00 53.26  ? 517 HOH   A O   1 
HETATM 3042 O  O   . HOH   H 7 .   ? -71.858 7.188   -20.073 1.00 64.83  ? 518 HOH   A O   1 
HETATM 3043 O  O   . HOH   H 7 .   ? -44.563 28.046  -31.621 1.00 68.95  ? 519 HOH   A O   1 
HETATM 3044 O  O   . HOH   H 7 .   ? -58.930 3.601   -10.266 1.00 49.88  ? 520 HOH   A O   1 
HETATM 3045 O  O   . HOH   H 7 .   ? -37.879 9.674   -21.452 1.00 45.22  ? 521 HOH   A O   1 
HETATM 3046 O  O   . HOH   H 7 .   ? -42.295 15.109  -24.065 1.00 38.62  ? 522 HOH   A O   1 
HETATM 3047 O  O   . HOH   H 7 .   ? -31.951 9.284   -6.243  1.00 72.31  ? 523 HOH   A O   1 
HETATM 3048 O  O   . HOH   H 7 .   ? -51.100 27.344  -29.749 1.00 57.08  ? 524 HOH   A O   1 
HETATM 3049 O  O   . HOH   H 7 .   ? -63.340 8.317   -13.046 1.00 37.30  ? 525 HOH   A O   1 
HETATM 3050 O  O   . HOH   H 7 .   ? -33.223 -0.852  -20.545 1.00 62.26  ? 526 HOH   A O   1 
HETATM 3051 O  O   . HOH   H 7 .   ? -39.934 9.130   -23.070 1.00 41.95  ? 527 HOH   A O   1 
HETATM 3052 O  O   . HOH   H 7 .   ? -35.168 22.818  -17.713 1.00 54.26  ? 528 HOH   A O   1 
HETATM 3053 O  O   . HOH   H 7 .   ? -52.081 5.013   -8.786  1.00 47.16  ? 529 HOH   A O   1 
HETATM 3054 O  O   . HOH   H 7 .   ? -42.077 1.325   -14.910 1.00 40.24  ? 530 HOH   A O   1 
HETATM 3055 O  O   . HOH   H 7 .   ? -34.771 10.220  -20.827 1.00 56.57  ? 531 HOH   A O   1 
HETATM 3056 O  O   . HOH   H 7 .   ? -53.791 6.153   -25.187 1.00 47.08  ? 532 HOH   A O   1 
HETATM 3057 O  O   . HOH   H 7 .   ? -40.605 2.023   -27.530 1.00 57.34  ? 533 HOH   A O   1 
HETATM 3058 O  O   . HOH   H 7 .   ? -41.654 21.500  -27.153 1.00 53.60  ? 534 HOH   A O   1 
HETATM 3059 O  O   . HOH   H 7 .   ? -44.165 -0.053  -17.506 1.00 37.68  ? 535 HOH   A O   1 
HETATM 3060 O  O   . HOH   H 7 .   ? -59.248 13.496  -0.280  1.00 55.93  ? 536 HOH   A O   1 
HETATM 3061 O  O   . HOH   H 7 .   ? -57.518 18.802  -0.670  1.00 63.71  ? 537 HOH   A O   1 
HETATM 3062 O  O   . HOH   H 7 .   ? -37.471 19.078  -12.724 1.00 50.80  ? 538 HOH   A O   1 
HETATM 3063 O  O   . HOH   H 7 .   ? -32.503 2.698   -10.117 1.00 58.35  ? 539 HOH   A O   1 
HETATM 3064 O  O   . HOH   H 7 .   ? -56.343 26.023  -2.546  1.00 57.48  ? 540 HOH   A O   1 
HETATM 3065 O  O   . HOH   H 7 .   ? -51.839 10.198  -30.417 1.00 43.34  ? 541 HOH   A O   1 
HETATM 3066 O  O   . HOH   H 7 .   ? -63.131 3.927   -26.438 1.00 52.64  ? 542 HOH   A O   1 
HETATM 3067 O  O   . HOH   H 7 .   ? -60.906 -5.767  -39.217 1.00 79.44  ? 543 HOH   A O   1 
HETATM 3068 O  O   . HOH   H 7 .   ? -68.739 16.912  -1.031  1.00 72.73  ? 544 HOH   A O   1 
HETATM 3069 O  O   . HOH   H 7 .   ? -54.210 18.500  -0.315  1.00 60.81  ? 545 HOH   A O   1 
HETATM 3070 O  O   . HOH   H 7 .   ? -31.095 19.391  -11.885 1.00 63.84  ? 546 HOH   A O   1 
HETATM 3071 O  O   . HOH   H 7 .   ? -37.954 5.791   -4.524  1.00 53.10  ? 547 HOH   A O   1 
HETATM 3072 O  O   . HOH   H 7 .   ? -32.257 5.131   -8.989  1.00 63.20  ? 548 HOH   A O   1 
HETATM 3073 O  O   . HOH   H 7 .   ? -68.148 9.423   -13.479 1.00 57.28  ? 549 HOH   A O   1 
HETATM 3074 O  O   . HOH   H 7 .   ? -60.578 10.085  -6.491  1.00 43.31  ? 550 HOH   A O   1 
HETATM 3075 O  O   . HOH   H 7 .   ? -60.543 15.737  -24.631 1.00 51.94  ? 551 HOH   A O   1 
HETATM 3076 O  O   . HOH   H 7 .   ? -30.081 21.370  -26.299 1.00 57.88  ? 552 HOH   A O   1 
HETATM 3077 O  O   . HOH   H 7 .   ? -59.584 9.119   -30.257 1.00 51.12  ? 553 HOH   A O   1 
HETATM 3078 O  O   . HOH   H 7 .   ? -35.174 0.180   -11.384 1.00 57.26  ? 554 HOH   A O   1 
HETATM 3079 O  O   . HOH   H 7 .   ? -70.800 -9.659  -35.316 1.00 55.55  ? 555 HOH   A O   1 
HETATM 3080 O  O   . HOH   H 7 .   ? -73.060 4.553   -19.575 1.00 57.99  ? 556 HOH   A O   1 
HETATM 3081 O  O   . HOH   H 7 .   ? -64.029 1.610   -19.212 1.00 39.03  ? 557 HOH   A O   1 
HETATM 3082 O  O   . HOH   H 7 .   ? -51.311 5.381   -1.507  1.00 66.08  ? 558 HOH   A O   1 
HETATM 3083 O  O   . HOH   H 7 .   ? -52.981 12.167  -29.046 1.00 43.50  ? 559 HOH   A O   1 
HETATM 3084 O  O   . HOH   H 7 .   ? -37.272 18.106  -10.496 1.00 54.31  ? 560 HOH   A O   1 
HETATM 3085 O  O   . HOH   H 7 .   ? -54.838 11.061  1.948   1.00 63.14  ? 561 HOH   A O   1 
HETATM 3086 O  O   . HOH   H 7 .   ? -66.263 11.408  -15.085 1.00 54.27  ? 562 HOH   A O   1 
HETATM 3087 O  O   . HOH   H 7 .   ? -63.369 15.076  -15.431 1.00 47.85  ? 563 HOH   A O   1 
HETATM 3088 O  O   . HOH   H 7 .   ? -38.928 22.157  -19.178 1.00 44.52  ? 564 HOH   A O   1 
HETATM 3089 O  O   . HOH   H 7 .   ? -43.953 36.834  -34.600 1.00 74.15  ? 565 HOH   A O   1 
HETATM 3090 O  O   . HOH   H 7 .   ? -31.365 11.565  -13.748 1.00 56.16  ? 566 HOH   A O   1 
HETATM 3091 O  O   . HOH   H 7 .   ? -57.700 27.863  -4.127  1.00 61.31  ? 567 HOH   A O   1 
HETATM 3092 O  O   . HOH   H 7 .   ? -72.065 19.056  -2.910  1.00 86.49  ? 568 HOH   A O   1 
HETATM 3093 O  O   . HOH   H 7 .   ? -51.858 20.813  -19.499 1.00 51.43  ? 569 HOH   A O   1 
HETATM 3094 O  O   . HOH   H 7 .   ? -32.606 13.333  -45.282 1.00 69.49  ? 570 HOH   A O   1 
HETATM 3095 O  O   . HOH   H 7 .   ? -61.203 1.687   -19.994 1.00 43.96  ? 571 HOH   A O   1 
HETATM 3096 O  O   . HOH   H 7 .   ? -35.423 3.385   -21.691 1.00 46.86  ? 572 HOH   A O   1 
HETATM 3097 O  O   . HOH   H 7 .   ? -34.617 18.888  -10.243 1.00 64.61  ? 573 HOH   A O   1 
HETATM 3098 O  O   . HOH   H 7 .   ? -36.360 1.101   -25.425 1.00 60.39  ? 574 HOH   A O   1 
HETATM 3099 O  O   . HOH   H 7 .   ? -28.285 12.555  -15.564 1.00 69.76  ? 575 HOH   A O   1 
HETATM 3100 O  O   . HOH   H 7 .   ? -33.217 9.338   -17.951 1.00 56.55  ? 576 HOH   A O   1 
HETATM 3101 O  O   . HOH   H 7 .   ? -54.993 12.073  -30.446 1.00 50.82  ? 577 HOH   A O   1 
HETATM 3102 O  O   . HOH   H 7 .   ? -39.138 22.704  -24.938 1.00 60.91  ? 578 HOH   A O   1 
HETATM 3103 O  O   . HOH   H 7 .   ? -57.501 21.812  -21.642 1.00 62.73  ? 579 HOH   A O   1 
HETATM 3104 O  O   . HOH   H 7 .   ? -60.258 16.374  0.677   1.00 66.35  ? 580 HOH   A O   1 
HETATM 3105 O  O   . HOH   H 7 .   ? -36.280 4.176   -28.362 1.00 53.67  ? 581 HOH   A O   1 
HETATM 3106 O  O   . HOH   H 7 .   ? -55.894 5.031   -23.638 1.00 39.13  ? 582 HOH   A O   1 
HETATM 3107 O  O   . HOH   H 7 .   ? -66.459 5.479   -6.766  1.00 55.23  ? 583 HOH   A O   1 
HETATM 3108 O  O   . HOH   H 7 .   ? -33.324 7.585   -9.973  1.00 55.60  ? 584 HOH   A O   1 
HETATM 3109 O  O   . HOH   H 7 .   ? -52.693 16.093  -0.151  1.00 53.86  ? 585 HOH   A O   1 
HETATM 3110 O  O   . HOH   H 7 .   ? -59.384 0.851   -0.538  1.00 78.04  ? 586 HOH   A O   1 
HETATM 3111 O  O   . HOH   H 7 .   ? -70.358 5.932   -14.333 1.00 60.78  ? 587 HOH   A O   1 
HETATM 3112 O  O   . HOH   H 7 .   ? -59.163 1.508   -21.778 1.00 42.90  ? 588 HOH   A O   1 
HETATM 3113 O  O   . HOH   H 7 .   ? -42.999 5.799   -1.517  1.00 58.35  ? 589 HOH   A O   1 
HETATM 3114 O  O   . HOH   H 7 .   ? -38.899 13.390  -46.805 1.00 66.96  ? 590 HOH   A O   1 
HETATM 3115 O  O   . HOH   H 7 .   ? -50.034 5.739   -4.297  1.00 59.55  ? 591 HOH   A O   1 
HETATM 3116 O  O   . HOH   H 7 .   ? -42.843 16.573  -40.681 1.00 50.96  ? 592 HOH   A O   1 
HETATM 3117 O  O   . HOH   H 7 .   ? -52.611 2.746   -1.941  1.00 70.08  ? 593 HOH   A O   1 
HETATM 3118 O  O   . HOH   H 7 .   ? -57.312 7.552   -30.236 1.00 55.04  ? 594 HOH   A O   1 
HETATM 3119 O  O   . HOH   H 7 .   ? -52.149 4.964   -26.574 1.00 49.75  ? 595 HOH   A O   1 
HETATM 3120 O  O   . HOH   H 7 .   ? -43.149 3.564   -28.084 1.00 64.00  ? 596 HOH   A O   1 
HETATM 3121 O  O   . HOH   H 7 .   ? -72.795 12.871  -7.260  1.00 68.18  ? 597 HOH   A O   1 
HETATM 3122 O  O   . HOH   H 7 .   ? -60.947 9.313   -32.456 1.00 59.32  ? 598 HOH   A O   1 
HETATM 3123 O  O   . HOH   H 7 .   ? -55.479 1.312   -9.435  1.00 63.92  ? 599 HOH   A O   1 
HETATM 3124 O  O   . HOH   H 7 .   ? -58.916 1.073   -13.461 1.00 55.11  ? 600 HOH   A O   1 
HETATM 3125 O  O   . HOH   H 7 .   ? -55.694 2.404   -23.244 1.00 53.82  ? 601 HOH   A O   1 
HETATM 3126 O  O   . HOH   H 7 .   ? -40.546 7.100   -33.755 1.00 57.14  ? 602 HOH   A O   1 
HETATM 3127 O  O   . HOH   H 7 .   ? -50.980 0.333   -7.279  1.00 65.07  ? 603 HOH   A O   1 
HETATM 3128 O  O   . HOH   H 7 .   ? -70.966 -7.090  -43.126 1.00 79.62  ? 604 HOH   A O   1 
HETATM 3129 O  O   . HOH   H 7 .   ? -48.213 10.692  0.209   1.00 65.40  ? 605 HOH   A O   1 
HETATM 3130 O  O   . HOH   H 7 .   ? -47.207 33.850  -46.332 1.00 77.08  ? 606 HOH   A O   1 
HETATM 3131 O  O   . HOH   H 7 .   ? -65.468 16.541  -18.084 1.00 70.31  ? 607 HOH   A O   1 
HETATM 3132 O  O   . HOH   H 7 .   ? -47.686 18.571  -2.758  1.00 67.41  ? 608 HOH   A O   1 
HETATM 3133 O  O   . HOH   H 7 .   ? -30.153 23.015  -30.411 1.00 69.19  ? 609 HOH   A O   1 
HETATM 3134 O  O   . HOH   H 7 .   ? -57.018 6.385   1.215   1.00 67.56  ? 610 HOH   A O   1 
HETATM 3135 O  O   . HOH   H 7 .   ? -70.827 9.945   -20.543 1.00 69.32  ? 611 HOH   A O   1 
HETATM 3136 O  O   . HOH   H 7 .   ? -65.546 11.416  -32.101 1.00 69.95  ? 612 HOH   A O   1 
HETATM 3137 O  O   . HOH   H 7 .   ? -48.236 22.335  -28.861 1.00 62.96  ? 613 HOH   A O   1 
HETATM 3138 O  O   . HOH   H 7 .   ? -33.838 17.368  -8.010  1.00 72.74  ? 614 HOH   A O   1 
HETATM 3139 O  O   . HOH   H 7 .   ? -69.810 19.603  -3.780  1.00 86.20  ? 615 HOH   A O   1 
HETATM 3140 O  O   . HOH   H 7 .   ? -37.645 -3.636  -13.779 1.00 59.89  ? 616 HOH   A O   1 
HETATM 3141 O  O   . HOH   H 7 .   ? -30.629 8.650   -18.086 1.00 71.92  ? 617 HOH   A O   1 
HETATM 3142 O  O   . HOH   H 7 .   ? -28.883 23.305  -27.709 1.00 67.71  ? 618 HOH   A O   1 
HETATM 3143 O  O   . HOH   H 7 .   ? -60.059 1.831   -11.575 1.00 52.27  ? 619 HOH   A O   1 
HETATM 3144 O  O   . HOH   H 7 .   ? -50.596 -1.851  -24.442 1.00 57.15  ? 620 HOH   A O   1 
HETATM 3145 O  O   . HOH   H 7 .   ? -33.181 1.280   -12.535 1.00 50.17  ? 621 HOH   A O   1 
HETATM 3146 O  O   . HOH   H 7 .   ? -49.378 9.386   -33.450 1.00 61.56  ? 622 HOH   A O   1 
HETATM 3147 O  O   . HOH   H 7 .   ? -43.593 26.852  -33.994 1.00 66.15  ? 623 HOH   A O   1 
HETATM 3148 O  O   . HOH   H 7 .   ? -51.140 3.626   -6.546  1.00 62.55  ? 624 HOH   A O   1 
HETATM 3149 O  O   . HOH   H 7 .   ? -57.865 5.356   -25.222 1.00 60.30  ? 625 HOH   A O   1 
HETATM 3150 O  O   . HOH   H 7 .   ? -65.969 14.182  -15.439 1.00 54.02  ? 626 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   . PRO A 1   ? 0.9256 1.5783 0.8267 0.1839  0.1370  0.4284  17  PRO A N   
2    C CA  . PRO A 1   ? 0.9732 1.5882 0.9148 0.1639  0.1496  0.4523  17  PRO A CA  
3    C C   . PRO A 1   ? 1.0403 1.6775 0.9838 0.1594  0.1589  0.4322  17  PRO A C   
4    O O   . PRO A 1   ? 0.9537 1.5617 0.8972 0.1576  0.1504  0.3879  17  PRO A O   
5    C CB  . PRO A 1   ? 0.9986 1.5326 0.9648 0.1526  0.1379  0.4314  17  PRO A CB  
6    C CG  . PRO A 1   ? 0.8971 1.4291 0.8382 0.1663  0.1212  0.4097  17  PRO A CG  
7    C CD  . PRO A 1   ? 0.9776 1.5772 0.8787 0.1838  0.1191  0.3901  17  PRO A CD  
8    N N   . LYS A 2   ? 1.1721 1.8625 1.1185 0.1581  0.1763  0.4663  18  LYS A N   
9    C CA  . LYS A 2   ? 1.1821 1.9113 1.1241 0.1590  0.1851  0.4455  18  LYS A CA  
10   C C   . LYS A 2   ? 1.1967 1.8731 1.1756 0.1403  0.1869  0.4297  18  LYS A C   
11   O O   . LYS A 2   ? 1.1806 1.8636 1.1544 0.1434  0.1845  0.3914  18  LYS A O   
12   C CB  . LYS A 2   ? 1.1403 1.9277 1.0882 0.1604  0.1947  0.4732  18  LYS A CB  
13   C CG  . LYS A 2   ? 1.2059 2.0588 1.1158 0.1824  0.1878  0.4598  18  LYS A CG  
14   C CD  . LYS A 2   ? 1.2522 2.1188 1.1288 0.1973  0.1792  0.4051  18  LYS A CD  
15   C CE  . LYS A 2   ? 1.2621 2.1775 1.1037 0.2186  0.1670  0.3867  18  LYS A CE  
16   N NZ  . LYS A 2   ? 1.3588 2.2607 1.1742 0.2301  0.1541  0.3348  18  LYS A NZ  
17   N N   . TYR A 3   ? 0.9932 1.6196 1.0108 0.1218  0.1906  0.4582  19  TYR A N   
18   C CA  . TYR A 3   ? 0.9529 1.5307 1.0063 0.1040  0.1906  0.4412  19  TYR A CA  
19   C C   . TYR A 3   ? 0.9367 1.4660 0.9800 0.1073  0.1725  0.3900  19  TYR A C   
20   O O   . TYR A 3   ? 0.8534 1.3717 0.9050 0.1031  0.1705  0.3600  19  TYR A O   
21   C CB  . TYR A 3   ? 0.9210 1.4544 1.0193 0.0846  0.1963  0.4786  19  TYR A CB  
22   C CG  . TYR A 3   ? 1.0004 1.4903 1.0987 0.0876  0.1853  0.4882  19  TYR A CG  
23   C CD1 . TYR A 3   ? 0.9920 1.5126 1.0722 0.0995  0.1871  0.5227  19  TYR A CD1 
24   C CD2 . TYR A 3   ? 0.9806 1.4033 1.0972 0.0795  0.1732  0.4630  19  TYR A CD2 
25   C CE1 . TYR A 3   ? 0.9573 1.4403 1.0398 0.1034  0.1766  0.5307  19  TYR A CE1 
26   C CE2 . TYR A 3   ? 0.9876 1.3739 1.1062 0.0830  0.1637  0.4699  19  TYR A CE2 
27   C CZ  . TYR A 3   ? 0.9923 1.4076 1.0949 0.0951  0.1652  0.5034  19  TYR A CZ  
28   O OH  . TYR A 3   ? 1.1227 1.5034 1.2296 0.0998  0.1551  0.5096  19  TYR A OH  
29   N N   . ILE A 4   ? 0.9337 1.4364 0.9604 0.1151  0.1594  0.3810  20  ILE A N   
30   C CA  . ILE A 4   ? 0.8955 1.3645 0.9073 0.1207  0.1429  0.3340  20  ILE A CA  
31   C C   . ILE A 4   ? 0.8846 1.3987 0.8660 0.1365  0.1402  0.3019  20  ILE A C   
32   O O   . ILE A 4   ? 0.7030 1.1979 0.6846 0.1371  0.1329  0.2652  20  ILE A O   
33   C CB  . ILE A 4   ? 0.8844 1.3253 0.8852 0.1262  0.1305  0.3334  20  ILE A CB  
34   C CG1 . ILE A 4   ? 0.9328 1.3197 0.9682 0.1113  0.1310  0.3551  20  ILE A CG1 
35   C CG2 . ILE A 4   ? 0.7900 1.2093 0.7716 0.1337  0.1145  0.2865  20  ILE A CG2 
36   C CD1 . ILE A 4   ? 0.9700 1.3406 0.9981 0.1183  0.1219  0.3646  20  ILE A CD1 
37   N N   . GLU A 5   ? 0.8586 1.4352 0.8144 0.1506  0.1458  0.3150  21  GLU A N   
38   C CA  . GLU A 5   ? 0.8833 1.5074 0.8106 0.1679  0.1426  0.2809  21  GLU A CA  
39   C C   . GLU A 5   ? 0.8244 1.4629 0.7654 0.1647  0.1506  0.2658  21  GLU A C   
40   O O   . GLU A 5   ? 0.8005 1.4404 0.7321 0.1744  0.1423  0.2241  21  GLU A O   
41   C CB  . GLU A 5   ? 1.0066 1.7040 0.9053 0.1830  0.1492  0.3019  21  GLU A CB  
42   C CG  . GLU A 5   ? 0.9978 1.7444 0.8639 0.2039  0.1420  0.2607  21  GLU A CG  
43   C CD  . GLU A 5   ? 1.1245 1.8359 0.9775 0.2109  0.1216  0.2239  21  GLU A CD  
44   O OE1 . GLU A 5   ? 1.1276 1.7921 0.9894 0.2025  0.1146  0.2381  21  GLU A OE1 
45   O OE2 . GLU A 5   ? 1.1983 1.9296 1.0352 0.2247  0.1126  0.1801  21  GLU A OE2 
46   N N   . HIS A 6   ? 0.7920 1.4412 0.7586 0.1512  0.1662  0.2993  22  HIS A N   
47   C CA  . HIS A 6   ? 0.7666 1.4344 0.7498 0.1476  0.1745  0.2872  22  HIS A CA  
48   C C   . HIS A 6   ? 0.7505 1.3600 0.7493 0.1416  0.1620  0.2515  22  HIS A C   
49   O O   . HIS A 6   ? 0.7800 1.4011 0.7718 0.1522  0.1569  0.2160  22  HIS A O   
50   C CB  . HIS A 6   ? 0.7390 1.4218 0.7537 0.1304  0.1926  0.3315  22  HIS A CB  
51   C CG  . HIS A 6   ? 0.7472 1.4482 0.7843 0.1244  0.2008  0.3201  22  HIS A CG  
52   N ND1 . HIS A 6   ? 0.7165 1.4868 0.7401 0.1378  0.2099  0.3097  22  HIS A ND1 
53   C CD2 . HIS A 6   ? 0.7243 1.3870 0.7970 0.1076  0.2005  0.3154  22  HIS A CD2 
54   C CE1 . HIS A 6   ? 0.7227 1.4953 0.7737 0.1294  0.2150  0.3005  22  HIS A CE1 
55   N NE2 . HIS A 6   ? 0.6724 1.3811 0.7532 0.1108  0.2091  0.3040  22  HIS A NE2 
56   N N   . PHE A 7   ? 0.7129 1.2613 0.7344 0.1253  0.1571  0.2609  23  PHE A N   
57   C CA  . PHE A 7   ? 0.7001 1.2003 0.7378 0.1183  0.1471  0.2322  23  PHE A CA  
58   C C   . PHE A 7   ? 0.6545 1.1274 0.6697 0.1305  0.1298  0.1946  23  PHE A C   
59   O O   . PHE A 7   ? 0.6624 1.1151 0.6828 0.1321  0.1218  0.1658  23  PHE A O   
60   C CB  . PHE A 7   ? 0.6550 1.1047 0.7244 0.0977  0.1476  0.2512  23  PHE A CB  
61   C CG  . PHE A 7   ? 0.6736 1.1435 0.7753 0.0829  0.1631  0.2809  23  PHE A CG  
62   C CD1 . PHE A 7   ? 0.6716 1.1573 0.7921 0.0782  0.1672  0.2683  23  PHE A CD1 
63   C CD2 . PHE A 7   ? 0.7176 1.1925 0.8340 0.0738  0.1735  0.3225  23  PHE A CD2 
64   C CE1 . PHE A 7   ? 0.7246 1.2320 0.8790 0.0629  0.1818  0.2951  23  PHE A CE1 
65   C CE2 . PHE A 7   ? 0.7445 1.2372 0.8961 0.0582  0.1883  0.3514  23  PHE A CE2 
66   C CZ  . PHE A 7   ? 0.7268 1.2367 0.8978 0.0520  0.1926  0.3369  23  PHE A CZ  
67   N N   . SER A 8   ? 0.6812 1.1556 0.6732 0.1392  0.1236  0.1952  24  SER A N   
68   C CA  . SER A 8   ? 0.7037 1.1536 0.6782 0.1492  0.1073  0.1600  24  SER A CA  
69   C C   . SER A 8   ? 0.7443 1.2281 0.7050 0.1659  0.1039  0.1265  24  SER A C   
70   O O   . SER A 8   ? 0.7611 1.2183 0.7166 0.1722  0.0902  0.0942  24  SER A O   
71   C CB  . SER A 8   ? 0.7410 1.1930 0.6959 0.1550  0.1015  0.1678  24  SER A CB  
72   O OG  . SER A 8   ? 0.8065 1.3218 0.7381 0.1701  0.1066  0.1712  24  SER A OG  
73   N N   . LYS A 9   ? 0.7177 1.2602 0.6750 0.1733  0.1163  0.1334  25  LYS A N   
74   C CA  . LYS A 9   ? 0.7415 1.3191 0.6899 0.1906  0.1138  0.0992  25  LYS A CA  
75   C C   . LYS A 9   ? 0.7518 1.3016 0.7226 0.1872  0.1103  0.0799  25  LYS A C   
76   O O   . LYS A 9   ? 0.7674 1.3272 0.7352 0.2021  0.1033  0.0457  25  LYS A O   
77   C CB  . LYS A 9   ? 0.7704 1.4261 0.7085 0.2002  0.1295  0.1129  25  LYS A CB  
78   C CG  . LYS A 9   ? 0.8768 1.5731 0.7880 0.2081  0.1322  0.1298  25  LYS A CG  
79   C CD  . LYS A 9   ? 1.0601 1.8419 0.9526 0.2254  0.1430  0.1253  25  LYS A CD  
80   C CE  . LYS A 9   ? 1.1401 1.9384 1.0190 0.2463  0.1308  0.0712  25  LYS A CE  
81   N NZ  . LYS A 9   ? 1.1269 2.0141 0.9856 0.2658  0.1404  0.0608  25  LYS A NZ  
82   N N   . PHE A 10  ? 0.6692 1.1868 0.6640 0.1692  0.1143  0.1000  26  PHE A N   
83   C CA  . PHE A 10  ? 0.6910 1.1806 0.7062 0.1657  0.1088  0.0829  26  PHE A CA  
84   C C   . PHE A 10  ? 0.7156 1.1424 0.7298 0.1625  0.0923  0.0662  26  PHE A C   
85   O O   . PHE A 10  ? 0.6774 1.0773 0.6823 0.1567  0.0879  0.0749  26  PHE A O   
86   C CB  . PHE A 10  ? 0.6573 1.1452 0.7003 0.1476  0.1195  0.1089  26  PHE A CB  
87   C CG  . PHE A 10  ? 0.6925 1.2431 0.7423 0.1483  0.1370  0.1279  26  PHE A CG  
88   C CD1 . PHE A 10  ? 0.7523 1.3339 0.7933 0.1453  0.1488  0.1588  26  PHE A CD1 
89   C CD2 . PHE A 10  ? 0.6555 1.2368 0.7216 0.1524  0.1419  0.1167  26  PHE A CD2 
90   C CE1 . PHE A 10  ? 0.7626 1.4062 0.8103 0.1452  0.1663  0.1799  26  PHE A CE1 
91   C CE2 . PHE A 10  ? 0.7484 1.3925 0.8224 0.1524  0.1593  0.1351  26  PHE A CE2 
92   C CZ  . PHE A 10  ? 0.6933 1.3689 0.7578 0.1481  0.1720  0.1675  26  PHE A CZ  
93   N N   . SER A 11  ? 0.6129 1.0190 0.6374 0.1670  0.0834  0.0430  27  SER A N   
94   C CA  . SER A 11  ? 0.7333 1.0812 0.7592 0.1600  0.0703  0.0358  27  SER A CA  
95   C C   . SER A 11  ? 0.5939 0.9153 0.6413 0.1445  0.0709  0.0475  27  SER A C   
96   O O   . SER A 11  ? 0.6053 0.9509 0.6685 0.1435  0.0774  0.0505  27  SER A O   
97   C CB  . SER A 11  ? 0.7364 1.0676 0.7585 0.1745  0.0564  0.0035  27  SER A CB  
98   O OG  . SER A 11  ? 0.8174 1.1613 0.8543 0.1823  0.0561  -0.0087 27  SER A OG  
99   N N   . PRO A 12  ? 0.6482 0.9249 0.6975 0.1323  0.0646  0.0536  28  PRO A N   
100  C CA  . PRO A 12  ? 0.5598 0.8147 0.6284 0.1189  0.0636  0.0600  28  PRO A CA  
101  C C   . PRO A 12  ? 0.5721 0.8293 0.6498 0.1272  0.0569  0.0426  28  PRO A C   
102  O O   . PRO A 12  ? 0.5473 0.8033 0.6169 0.1421  0.0492  0.0236  28  PRO A O   
103  C CB  . PRO A 12  ? 0.6013 0.8108 0.6646 0.1101  0.0555  0.0611  28  PRO A CB  
104  C CG  . PRO A 12  ? 0.5771 0.7894 0.6233 0.1139  0.0567  0.0657  28  PRO A CG  
105  C CD  . PRO A 12  ? 0.6632 0.9124 0.6977 0.1305  0.0583  0.0538  28  PRO A CD  
106  N N   . SER A 13  ? 0.4848 0.7466 0.5823 0.1180  0.0593  0.0486  29  SER A N   
107  C CA  . SER A 13  ? 0.5179 0.7835 0.6265 0.1255  0.0521  0.0350  29  SER A CA  
108  C C   . SER A 13  ? 0.5700 0.7986 0.6823 0.1163  0.0420  0.0347  29  SER A C   
109  O O   . SER A 13  ? 0.5461 0.7735 0.6720 0.1015  0.0450  0.0439  29  SER A O   
110  C CB  . SER A 13  ? 0.4835 0.7912 0.6130 0.1234  0.0615  0.0400  29  SER A CB  
111  O OG  . SER A 13  ? 0.6478 0.9955 0.7729 0.1308  0.0729  0.0434  29  SER A OG  
112  N N   . PRO A 14  ? 0.5604 0.7601 0.6625 0.1240  0.0303  0.0244  30  PRO A N   
113  C CA  . PRO A 14  ? 0.5720 0.7417 0.6751 0.1153  0.0217  0.0268  30  PRO A CA  
114  C C   . PRO A 14  ? 0.5683 0.7528 0.6873 0.1165  0.0173  0.0245  30  PRO A C   
115  O O   . PRO A 14  ? 0.5620 0.7657 0.6884 0.1303  0.0148  0.0163  30  PRO A O   
116  C CB  . PRO A 14  ? 0.6099 0.7495 0.6999 0.1242  0.0115  0.0188  30  PRO A CB  
117  C CG  . PRO A 14  ? 0.6737 0.8305 0.7630 0.1415  0.0115  0.0059  30  PRO A CG  
118  C CD  . PRO A 14  ? 0.6386 0.8326 0.7292 0.1401  0.0246  0.0103  30  PRO A CD  
119  N N   . LEU A 15  ? 0.5431 0.7217 0.6687 0.1026  0.0160  0.0300  31  LEU A N   
120  C CA  . LEU A 15  ? 0.5209 0.7177 0.6619 0.1018  0.0110  0.0275  31  LEU A CA  
121  C C   . LEU A 15  ? 0.5809 0.7567 0.7135 0.1047  -0.0018 0.0266  31  LEU A C   
122  O O   . LEU A 15  ? 0.5799 0.7277 0.6985 0.0992  -0.0044 0.0301  31  LEU A O   
123  C CB  . LEU A 15  ? 0.5216 0.7329 0.6796 0.0840  0.0177  0.0316  31  LEU A CB  
124  C CG  . LEU A 15  ? 0.5652 0.7984 0.7360 0.0777  0.0317  0.0383  31  LEU A CG  
125  C CD1 . LEU A 15  ? 0.5440 0.7846 0.7376 0.0585  0.0367  0.0421  31  LEU A CD1 
126  C CD2 . LEU A 15  ? 0.5313 0.8003 0.7114 0.0904  0.0349  0.0345  31  LEU A CD2 
127  N N   . SER A 16  ? 0.5408 0.7340 0.6832 0.1134  -0.0095 0.0235  32  SER A N   
128  C CA  . SER A 16  ? 0.5804 0.7615 0.7163 0.1160  -0.0215 0.0266  32  SER A CA  
129  C C   . SER A 16  ? 0.6350 0.8293 0.7757 0.1011  -0.0225 0.0266  32  SER A C   
130  O O   . SER A 16  ? 0.5824 0.7990 0.7392 0.0908  -0.0159 0.0222  32  SER A O   
131  C CB  . SER A 16  ? 0.5599 0.7555 0.7052 0.1339  -0.0310 0.0248  32  SER A CB  
132  O OG  . SER A 16  ? 0.6184 0.8530 0.7826 0.1325  -0.0301 0.0202  32  SER A OG  
133  N N   . MET A 17  ? 0.6004 0.7825 0.7286 0.0999  -0.0309 0.0311  33  MET A N   
134  C CA  . MET A 17  ? 0.6886 0.8890 0.8201 0.0887  -0.0342 0.0273  33  MET A CA  
135  C C   . MET A 17  ? 0.6421 0.8818 0.7936 0.0920  -0.0386 0.0207  33  MET A C   
136  O O   . MET A 17  ? 0.6502 0.9118 0.8168 0.0793  -0.0363 0.0116  33  MET A O   
137  C CB  . MET A 17  ? 0.6539 0.8429 0.7667 0.0907  -0.0431 0.0351  33  MET A CB  
138  C CG  . MET A 17  ? 0.6630 0.8699 0.7744 0.0788  -0.0452 0.0285  33  MET A CG  
139  S SD  . MET A 17  ? 0.7622 0.9460 0.8686 0.0623  -0.0348 0.0230  33  MET A SD  
140  C CE  . MET A 17  ? 0.5757 0.7270 0.6565 0.0674  -0.0366 0.0377  33  MET A CE  
141  N N   . LYS A 18  ? 0.7064 0.9559 0.8618 0.1090  -0.0453 0.0241  34  LYS A N   
142  C CA  . LYS A 18  ? 0.6409 0.9310 0.8177 0.1138  -0.0494 0.0176  34  LYS A CA  
143  C C   . LYS A 18  ? 0.6795 0.9886 0.8780 0.1043  -0.0371 0.0096  34  LYS A C   
144  O O   . LYS A 18  ? 0.6722 1.0149 0.8920 0.0960  -0.0374 0.0016  34  LYS A O   
145  C CB  . LYS A 18  ? 0.7400 1.0332 0.9191 0.1363  -0.0579 0.0228  34  LYS A CB  
146  C CG  . LYS A 18  ? 0.7921 1.1291 0.9904 0.1445  -0.0667 0.0185  34  LYS A CG  
147  C CD  . LYS A 18  ? 0.9107 1.2473 1.1142 0.1690  -0.0751 0.0237  34  LYS A CD  
148  C CE  . LYS A 18  ? 0.9630 1.3390 1.1796 0.1799  -0.0886 0.0247  34  LYS A CE  
149  N NZ  . LYS A 18  ? 0.9073 1.2748 1.1282 0.2056  -0.0990 0.0336  34  LYS A NZ  
150  N N   . GLN A 19  ? 0.6707 0.9611 0.8652 0.1049  -0.0264 0.0123  35  GLN A N   
151  C CA  . GLN A 19  ? 0.6261 0.9357 0.8395 0.0956  -0.0132 0.0098  35  GLN A CA  
152  C C   . GLN A 19  ? 0.6545 0.9614 0.8775 0.0734  -0.0070 0.0083  35  GLN A C   
153  O O   . GLN A 19  ? 0.6416 0.9736 0.8905 0.0623  0.0005  0.0059  35  GLN A O   
154  C CB  . GLN A 19  ? 0.5654 0.8586 0.7680 0.1027  -0.0039 0.0141  35  GLN A CB  
155  C CG  . GLN A 19  ? 0.6352 0.9540 0.8474 0.1198  -0.0023 0.0100  35  GLN A CG  
156  C CD  . GLN A 19  ? 0.5980 0.8984 0.7941 0.1308  0.0026  0.0101  35  GLN A CD  
157  O OE1 . GLN A 19  ? 0.5786 0.8424 0.7547 0.1300  -0.0002 0.0131  35  GLN A OE1 
158  N NE2 . GLN A 19  ? 0.6365 0.9659 0.8421 0.1411  0.0098  0.0054  35  GLN A NE2 
159  N N   . PHE A 20  ? 0.6144 0.8911 0.8199 0.0666  -0.0095 0.0097  36  PHE A N   
160  C CA  . PHE A 20  ? 0.6387 0.9120 0.8561 0.0473  -0.0055 0.0049  36  PHE A CA  
161  C C   . PHE A 20  ? 0.6558 0.9613 0.8939 0.0403  -0.0133 -0.0077 36  PHE A C   
162  O O   . PHE A 20  ? 0.6261 0.9444 0.8916 0.0245  -0.0082 -0.0147 36  PHE A O   
163  C CB  . PHE A 20  ? 0.5805 0.8196 0.7748 0.0442  -0.0075 0.0066  36  PHE A CB  
164  C CG  . PHE A 20  ? 0.5573 0.7676 0.7415 0.0427  0.0024  0.0158  36  PHE A CG  
165  C CD1 . PHE A 20  ? 0.5083 0.7166 0.7107 0.0300  0.0133  0.0185  36  PHE A CD1 
166  C CD2 . PHE A 20  ? 0.5144 0.7002 0.6731 0.0537  0.0001  0.0223  36  PHE A CD2 
167  C CE1 . PHE A 20  ? 0.5483 0.7337 0.7404 0.0300  0.0215  0.0287  36  PHE A CE1 
168  C CE2 . PHE A 20  ? 0.6174 0.7811 0.7671 0.0527  0.0080  0.0290  36  PHE A CE2 
169  C CZ  . PHE A 20  ? 0.5375 0.7024 0.7022 0.0417  0.0185  0.0327  36  PHE A CZ  
170  N N   . LEU A 21  ? 0.6301 0.9500 0.8574 0.0518  -0.0262 -0.0104 37  LEU A N   
171  C CA  . LEU A 21  ? 0.7151 1.0715 0.9600 0.0467  -0.0355 -0.0237 37  LEU A CA  
172  C C   . LEU A 21  ? 0.7225 1.1148 1.0020 0.0428  -0.0316 -0.0290 37  LEU A C   
173  O O   . LEU A 21  ? 0.7895 1.2062 1.0963 0.0283  -0.0328 -0.0425 37  LEU A O   
174  C CB  . LEU A 21  ? 0.6600 1.0283 0.8851 0.0626  -0.0502 -0.0209 37  LEU A CB  
175  C CG  . LEU A 21  ? 0.6751 1.0181 0.8702 0.0631  -0.0546 -0.0162 37  LEU A CG  
176  C CD1 . LEU A 21  ? 0.7202 1.0735 0.8970 0.0806  -0.0676 -0.0059 37  LEU A CD1 
177  C CD2 . LEU A 21  ? 0.6164 0.9708 0.8179 0.0469  -0.0560 -0.0328 37  LEU A CD2 
178  N N   . ASP A 22  ? 0.7151 1.1131 0.9963 0.0550  -0.0265 -0.0201 38  ASP A N   
179  C CA  . ASP A 22  ? 0.7731 1.2103 1.0878 0.0518  -0.0215 -0.0240 38  ASP A CA  
180  C C   . ASP A 22  ? 0.7566 1.1906 1.0952 0.0320  -0.0059 -0.0214 38  ASP A C   
181  O O   . ASP A 22  ? 0.8331 1.3017 1.2063 0.0228  -0.0010 -0.0251 38  ASP A O   
182  C CB  . ASP A 22  ? 0.7848 1.2337 1.0947 0.0730  -0.0207 -0.0173 38  ASP A CB  
183  C CG  . ASP A 22  ? 0.8278 1.2758 1.1183 0.0937  -0.0366 -0.0165 38  ASP A CG  
184  O OD1 . ASP A 22  ? 0.8351 1.2947 1.1236 0.0916  -0.0488 -0.0220 38  ASP A OD1 
185  O OD2 . ASP A 22  ? 0.8655 1.3019 1.1438 0.1124  -0.0370 -0.0103 38  ASP A OD2 
186  N N   . PHE A 23  ? 0.7608 1.1556 1.0844 0.0252  0.0019  -0.0136 39  PHE A N   
187  C CA  . PHE A 23  ? 0.7597 1.1486 1.1073 0.0066  0.0159  -0.0077 39  PHE A CA  
188  C C   . PHE A 23  ? 0.8122 1.2019 1.1868 -0.0135 0.0126  -0.0212 39  PHE A C   
189  O O   . PHE A 23  ? 0.8638 1.2621 1.2745 -0.0307 0.0218  -0.0193 39  PHE A O   
190  C CB  . PHE A 23  ? 0.7823 1.1310 1.1052 0.0085  0.0245  0.0062  39  PHE A CB  
191  C CG  . PHE A 23  ? 0.8647 1.2228 1.1874 0.0141  0.0377  0.0213  39  PHE A CG  
192  C CD1 . PHE A 23  ? 0.8325 1.2122 1.1880 0.0001  0.0507  0.0303  39  PHE A CD1 
193  C CD2 . PHE A 23  ? 0.8837 1.2316 1.1751 0.0332  0.0373  0.0262  39  PHE A CD2 
194  C CE1 . PHE A 23  ? 0.7974 1.1930 1.1506 0.0060  0.0638  0.0456  39  PHE A CE1 
195  C CE2 . PHE A 23  ? 0.8906 1.2535 1.1803 0.0398  0.0492  0.0370  39  PHE A CE2 
196  C CZ  . PHE A 23  ? 0.8165 1.2056 1.1351 0.0266  0.0628  0.0474  39  PHE A CZ  
197  N N   . GLY A 24  ? 0.8408 1.2227 1.2002 -0.0118 -0.0003 -0.0349 40  GLY A N   
198  C CA  . GLY A 24  ? 0.8704 1.2582 1.2547 -0.0286 -0.0056 -0.0539 40  GLY A CA  
199  C C   . GLY A 24  ? 0.8941 1.3255 1.2933 -0.0279 -0.0192 -0.0729 40  GLY A C   
200  O O   . GLY A 24  ? 0.9196 1.3586 1.3312 -0.0382 -0.0274 -0.0936 40  GLY A O   
201  N N   . SER A 25  ? 0.9325 1.3960 1.3319 -0.0153 -0.0228 -0.0685 41  SER A N   
202  C CA  . SER A 25  ? 1.0521 1.5618 1.4662 -0.0130 -0.0370 -0.0855 41  SER A CA  
203  C C   . SER A 25  ? 1.1168 1.6551 1.5831 -0.0352 -0.0355 -0.1027 41  SER A C   
204  O O   . SER A 25  ? 1.1349 1.7070 1.6160 -0.0391 -0.0489 -0.1245 41  SER A O   
205  C CB  . SER A 25  ? 1.0135 1.5501 1.4200 0.0072  -0.0406 -0.0757 41  SER A CB  
206  O OG  . SER A 25  ? 1.0118 1.5520 1.4364 0.0055  -0.0257 -0.0631 41  SER A OG  
207  N N   . SER A 26  ? 1.2739 1.8013 1.7700 -0.0501 -0.0198 -0.0929 42  SER A N   
208  C CA  . SER A 26  ? 1.2531 1.8042 1.8054 -0.0734 -0.0168 -0.1060 42  SER A CA  
209  C C   . SER A 26  ? 1.2264 1.7398 1.7996 -0.0909 -0.0004 -0.0927 42  SER A C   
210  O O   . SER A 26  ? 1.1833 1.6660 1.7308 -0.0833 0.0110  -0.0693 42  SER A O   
211  C CB  . SER A 26  ? 1.1648 1.7662 1.7471 -0.0726 -0.0146 -0.1031 42  SER A CB  
212  O OG  . SER A 26  ? 1.2106 1.8511 1.7815 -0.0572 -0.0314 -0.1168 42  SER A OG  
213  N N   . ASN A 27  ? 1.1498 1.6671 1.7725 -0.1143 0.0000  -0.1082 43  ASN A N   
214  C CA  . ASN A 27  ? 1.0778 1.5630 1.7325 -0.1329 0.0152  -0.0939 43  ASN A CA  
215  C C   . ASN A 27  ? 1.0350 1.5432 1.7222 -0.1415 0.0309  -0.0703 43  ASN A C   
216  O O   . ASN A 27  ? 0.9921 1.4773 1.7061 -0.1564 0.0453  -0.0513 43  ASN A O   
217  C CB  . ASN A 27  ? 1.0791 1.5565 1.7795 -0.1546 0.0087  -0.1213 43  ASN A CB  
218  C CG  . ASN A 27  ? 1.1177 1.5726 1.7855 -0.1463 -0.0043 -0.1440 43  ASN A CG  
219  O OD1 . ASN A 27  ? 1.0786 1.5330 1.6921 -0.1253 -0.0109 -0.1411 43  ASN A OD1 
220  N ND2 . ASN A 27  ? 1.1001 1.5376 1.8034 -0.1628 -0.0077 -0.1669 43  ASN A ND2 
221  N N   . ALA A 28  ? 1.0177 1.5729 1.7039 -0.1317 0.0289  -0.0697 44  ALA A N   
222  C CA  . ALA A 28  ? 1.0231 1.6058 1.7335 -0.1364 0.0453  -0.0460 44  ALA A CA  
223  C C   . ALA A 28  ? 0.9982 1.5605 1.6641 -0.1189 0.0579  -0.0170 44  ALA A C   
224  O O   . ALA A 28  ? 0.8942 1.4669 1.5767 -0.1252 0.0754  0.0079  44  ALA A O   
225  C CB  . ALA A 28  ? 0.9884 1.6321 1.7151 -0.1303 0.0383  -0.0582 44  ALA A CB  
226  N N   . CYS A 29  ? 0.9629 1.4990 1.5734 -0.0973 0.0493  -0.0200 45  CYS A N   
227  C CA  . CYS A 29  ? 0.8701 1.3842 1.4356 -0.0794 0.0579  0.0016  45  CYS A CA  
228  C C   . CYS A 29  ? 0.7538 1.2263 1.3190 -0.0898 0.0704  0.0215  45  CYS A C   
229  O O   . CYS A 29  ? 0.7263 1.1797 1.2536 -0.0756 0.0764  0.0377  45  CYS A O   
230  C CB  . CYS A 29  ? 0.9389 1.4343 1.4529 -0.0567 0.0434  -0.0093 45  CYS A CB  
231  S SG  . CYS A 29  ? 1.0724 1.6114 1.5854 -0.0429 0.0247  -0.0320 45  CYS A SG  
232  N N   . GLU A 30  ? 0.7551 1.2134 1.3631 -0.1133 0.0736  0.0202  46  GLU A N   
233  C CA  . GLU A 30  ? 0.7029 1.1191 1.3122 -0.1215 0.0841  0.0403  46  GLU A CA  
234  C C   . GLU A 30  ? 0.6506 1.0803 1.2572 -0.1192 0.1028  0.0746  46  GLU A C   
235  O O   . GLU A 30  ? 0.6276 1.0296 1.2034 -0.1105 0.1090  0.0931  46  GLU A O   
236  C CB  . GLU A 30  ? 0.6734 1.0739 1.3384 -0.1472 0.0838  0.0316  46  GLU A CB  
237  C CG  . GLU A 30  ? 0.6597 1.0152 1.3321 -0.1551 0.0938  0.0536  46  GLU A CG  
238  C CD  . GLU A 30  ? 0.6748 1.0053 1.4008 -0.1774 0.0903  0.0392  46  GLU A CD  
239  O OE1 . GLU A 30  ? 0.7123 1.0635 1.4720 -0.1887 0.0803  0.0105  46  GLU A OE1 
240  O OE2 . GLU A 30  ? 0.6962 0.9868 1.4320 -0.1828 0.0969  0.0556  46  GLU A OE2 
241  N N   . LYS A 31  ? 0.6052 1.0817 1.2438 -0.1266 0.1120  0.0832  47  LYS A N   
242  C CA  . LYS A 31  ? 0.6254 1.1258 1.2583 -0.1224 0.1303  0.1149  47  LYS A CA  
243  C C   . LYS A 31  ? 0.5882 1.0895 1.1601 -0.0939 0.1285  0.1160  47  LYS A C   
244  O O   . LYS A 31  ? 0.5706 1.0655 1.1190 -0.0867 0.1396  0.1395  47  LYS A O   
245  C CB  . LYS A 31  ? 0.5515 1.1106 1.2266 -0.1326 0.1391  0.1192  47  LYS A CB  
246  C CG  . LYS A 31  ? 0.6634 1.2248 1.4041 -0.1632 0.1484  0.1317  47  LYS A CG  
247  C CD  . LYS A 31  ? 0.6875 1.3119 1.4706 -0.1734 0.1576  0.1361  47  LYS A CD  
248  C CE  . LYS A 31  ? 0.6826 1.3343 1.4787 -0.1713 0.1404  0.0989  47  LYS A CE  
249  N NZ  . LYS A 31  ? 0.6091 1.3135 1.4690 -0.1923 0.1480  0.1005  47  LYS A NZ  
250  N N   . THR A 32  ? 0.5935 1.1045 1.1415 -0.0774 0.1141  0.0910  48  THR A N   
251  C CA  . THR A 32  ? 0.6005 1.1092 1.0964 -0.0506 0.1107  0.0890  48  THR A CA  
252  C C   . THR A 32  ? 0.5848 1.0406 1.0436 -0.0445 0.1069  0.0930  48  THR A C   
253  O O   . THR A 32  ? 0.6000 1.0509 1.0255 -0.0301 0.1126  0.1048  48  THR A O   
254  C CB  . THR A 32  ? 0.6014 1.1266 1.0861 -0.0356 0.0947  0.0632  48  THR A CB  
255  O OG1 . THR A 32  ? 0.6759 1.2532 1.1995 -0.0422 0.0977  0.0587  48  THR A OG1 
256  C CG2 . THR A 32  ? 0.6460 1.1702 1.0854 -0.0083 0.0917  0.0613  48  THR A CG2 
257  N N   . SER A 33  ? 0.6402 1.0594 1.1055 -0.0549 0.0972  0.0814  49  SER A N   
258  C CA  . SER A 33  ? 0.6009 0.9725 1.0349 -0.0499 0.0939  0.0845  49  SER A CA  
259  C C   . SER A 33  ? 0.6165 0.9759 1.0570 -0.0574 0.1089  0.1130  49  SER A C   
260  O O   . SER A 33  ? 0.6001 0.9400 1.0054 -0.0452 0.1107  0.1230  49  SER A O   
261  C CB  . SER A 33  ? 0.6067 0.9491 1.0507 -0.0597 0.0812  0.0642  49  SER A CB  
262  O OG  . SER A 33  ? 0.5958 0.8955 1.0105 -0.0542 0.0779  0.0658  49  SER A OG  
263  N N   . PHE A 34  ? 0.6330 1.0062 1.1199 -0.0771 0.1198  0.1278  50  PHE A N   
264  C CA  . PHE A 34  ? 0.5789 0.9420 1.0761 -0.0849 0.1344  0.1598  50  PHE A CA  
265  C C   . PHE A 34  ? 0.5834 0.9779 1.0505 -0.0695 0.1459  0.1806  50  PHE A C   
266  O O   . PHE A 34  ? 0.5678 0.9459 1.0091 -0.0618 0.1506  0.1984  50  PHE A O   
267  C CB  . PHE A 34  ? 0.5961 0.9699 1.1551 -0.1104 0.1438  0.1730  50  PHE A CB  
268  C CG  . PHE A 34  ? 0.5979 0.9770 1.1710 -0.1175 0.1617  0.2135  50  PHE A CG  
269  C CD1 . PHE A 34  ? 0.6067 0.9434 1.1763 -0.1193 0.1634  0.2307  50  PHE A CD1 
270  C CD2 . PHE A 34  ? 0.6167 1.0465 1.2065 -0.1215 0.1771  0.2358  50  PHE A CD2 
271  C CE1 . PHE A 34  ? 0.6310 0.9745 1.2129 -0.1245 0.1793  0.2716  50  PHE A CE1 
272  C CE2 . PHE A 34  ? 0.6450 1.0843 1.2460 -0.1276 0.1942  0.2768  50  PHE A CE2 
273  C CZ  . PHE A 34  ? 0.6255 1.0210 1.2222 -0.1290 0.1950  0.2959  50  PHE A CZ  
274  N N   . THR A 35  ? 0.5814 1.0253 1.0531 -0.0643 0.1506  0.1777  51  THR A N   
275  C CA  . THR A 35  ? 0.5667 1.0462 1.0098 -0.0479 0.1613  0.1927  51  THR A CA  
276  C C   . THR A 35  ? 0.5487 1.0091 0.9376 -0.0236 0.1507  0.1768  51  THR A C   
277  O O   . THR A 35  ? 0.5476 1.0172 0.9073 -0.0112 0.1575  0.1902  51  THR A O   
278  C CB  . THR A 35  ? 0.5737 1.1134 1.0361 -0.0463 0.1684  0.1894  51  THR A CB  
279  O OG1 . THR A 35  ? 0.5908 1.1338 1.0420 -0.0337 0.1532  0.1571  51  THR A OG1 
280  C CG2 . THR A 35  ? 0.5603 1.1190 1.0817 -0.0728 0.1780  0.2034  51  THR A CG2 
281  N N   . PHE A 36  ? 0.6396 1.0745 1.0155 -0.0170 0.1339  0.1489  52  PHE A N   
282  C CA  . PHE A 36  ? 0.5195 0.9313 0.8492 0.0035  0.1237  0.1357  52  PHE A CA  
283  C C   . PHE A 36  ? 0.5790 0.9492 0.8907 0.0013  0.1235  0.1477  52  PHE A C   
284  O O   . PHE A 36  ? 0.5385 0.9094 0.8190 0.0148  0.1261  0.1545  52  PHE A O   
285  C CB  . PHE A 36  ? 0.5083 0.9037 0.8309 0.0099  0.1065  0.1081  52  PHE A CB  
286  C CG  . PHE A 36  ? 0.5512 0.9144 0.8329 0.0265  0.0956  0.0970  52  PHE A CG  
287  C CD1 . PHE A 36  ? 0.5596 0.9373 0.8140 0.0466  0.0961  0.0935  52  PHE A CD1 
288  C CD2 . PHE A 36  ? 0.6048 0.9252 0.8776 0.0217  0.0851  0.0892  52  PHE A CD2 
289  C CE1 . PHE A 36  ? 0.4973 0.8441 0.7192 0.0600  0.0858  0.0830  52  PHE A CE1 
290  C CE2 . PHE A 36  ? 0.5638 0.8563 0.8022 0.0352  0.0760  0.0810  52  PHE A CE2 
291  C CZ  . PHE A 36  ? 0.5368 0.8410 0.7513 0.0536  0.0761  0.0784  52  PHE A CZ  
292  N N   . LEU A 37  ? 0.5788 0.9153 0.9120 -0.0150 0.1203  0.1489  53  LEU A N   
293  C CA  . LEU A 37  ? 0.5574 0.8528 0.8753 -0.0155 0.1181  0.1564  53  LEU A CA  
294  C C   . LEU A 37  ? 0.5821 0.8862 0.9026 -0.0179 0.1322  0.1885  53  LEU A C   
295  O O   . LEU A 37  ? 0.5728 0.8559 0.8684 -0.0101 0.1308  0.1960  53  LEU A O   
296  C CB  . LEU A 37  ? 0.5337 0.7942 0.8770 -0.0309 0.1107  0.1456  53  LEU A CB  
297  C CG  . LEU A 37  ? 0.6042 0.8526 0.9371 -0.0270 0.0951  0.1155  53  LEU A CG  
298  C CD1 . LEU A 37  ? 0.5620 0.7838 0.9219 -0.0423 0.0891  0.1034  53  LEU A CD1 
299  C CD2 . LEU A 37  ? 0.5570 0.7869 0.8445 -0.0091 0.0866  0.1069  53  LEU A CD2 
300  N N   . ARG A 38  ? 0.5689 0.9066 0.9196 -0.0284 0.1459  0.2093  54  ARG A N   
301  C CA  . ARG A 38  ? 0.5934 0.9410 0.9466 -0.0308 0.1596  0.2446  54  ARG A CA  
302  C C   . ARG A 38  ? 0.6263 1.0040 0.9356 -0.0099 0.1634  0.2504  54  ARG A C   
303  O O   . ARG A 38  ? 0.6372 1.0197 0.9360 -0.0070 0.1710  0.2766  54  ARG A O   
304  C CB  . ARG A 38  ? 0.6175 0.9947 1.0178 -0.0493 0.1744  0.2692  54  ARG A CB  
305  C CG  . ARG A 38  ? 0.6230 1.0577 1.0271 -0.0457 0.1824  0.2669  54  ARG A CG  
306  C CD  . ARG A 38  ? 0.6424 1.1072 1.0944 -0.0657 0.1995  0.2986  54  ARG A CD  
307  N NE  . ARG A 38  ? 0.5467 1.0706 1.0084 -0.0640 0.2079  0.2956  54  ARG A NE  
308  C CZ  . ARG A 38  ? 0.6215 1.1820 1.1264 -0.0813 0.2232  0.3199  54  ARG A CZ  
309  N NH1 . ARG A 38  ? 0.6567 1.1987 1.2009 -0.1021 0.2321  0.3512  54  ARG A NH1 
310  N NH2 . ARG A 38  ? 0.5573 1.1746 1.0696 -0.0778 0.2299  0.3132  54  ARG A NH2 
311  N N   . GLN A 39  ? 0.5913 0.9899 0.8765 0.0054  0.1573  0.2254  55  GLN A N   
312  C CA  . GLN A 39  ? 0.5422 0.9624 0.7851 0.0273  0.1565  0.2195  55  GLN A CA  
313  C C   . GLN A 39  ? 0.6029 0.9802 0.8144 0.0385  0.1405  0.1969  55  GLN A C   
314  O O   . GLN A 39  ? 0.5747 0.9478 0.7584 0.0489  0.1394  0.2021  55  GLN A O   
315  C CB  . GLN A 39  ? 0.5977 1.0654 0.8382 0.0384  0.1591  0.2037  55  GLN A CB  
316  C CG  . GLN A 39  ? 0.6042 1.0915 0.8051 0.0626  0.1551  0.1867  55  GLN A CG  
317  C CD  . GLN A 39  ? 0.6751 1.2002 0.8583 0.0694  0.1677  0.2100  55  GLN A CD  
318  O OE1 . GLN A 39  ? 0.7418 1.2875 0.9451 0.0564  0.1818  0.2422  55  GLN A OE1 
319  N NE2 . GLN A 39  ? 0.6736 1.2096 0.8207 0.0897  0.1623  0.1942  55  GLN A NE2 
320  N N   . GLU A 40  ? 0.5182 0.8656 0.7356 0.0356  0.1281  0.1734  56  GLU A N   
321  C CA  . GLU A 40  ? 0.5333 0.8461 0.7226 0.0463  0.1136  0.1521  56  GLU A CA  
322  C C   . GLU A 40  ? 0.5461 0.8196 0.7288 0.0409  0.1105  0.1614  56  GLU A C   
323  O O   . GLU A 40  ? 0.5431 0.8027 0.6975 0.0522  0.1040  0.1546  56  GLU A O   
324  C CB  . GLU A 40  ? 0.5427 0.8394 0.7408 0.0444  0.1020  0.1289  56  GLU A CB  
325  C CG  . GLU A 40  ? 0.5046 0.7689 0.6756 0.0552  0.0878  0.1096  56  GLU A CG  
326  C CD  . GLU A 40  ? 0.5508 0.8319 0.6960 0.0751  0.0853  0.0988  56  GLU A CD  
327  O OE1 . GLU A 40  ? 0.5547 0.8772 0.7020 0.0824  0.0938  0.1019  56  GLU A OE1 
328  O OE2 . GLU A 40  ? 0.5570 0.8113 0.6817 0.0834  0.0748  0.0862  56  GLU A OE2 
329  N N   . LEU A 41  ? 0.5372 0.7921 0.7487 0.0241  0.1142  0.1747  57  LEU A N   
330  C CA  . LEU A 41  ? 0.5380 0.7572 0.7464 0.0207  0.1115  0.1831  57  LEU A CA  
331  C C   . LEU A 41  ? 0.5691 0.8027 0.7584 0.0297  0.1180  0.2050  57  LEU A C   
332  O O   . LEU A 41  ? 0.5289 0.7422 0.6958 0.0376  0.1110  0.2005  57  LEU A O   
333  C CB  . LEU A 41  ? 0.5407 0.7385 0.7895 0.0018  0.1144  0.1916  57  LEU A CB  
334  C CG  . LEU A 41  ? 0.5686 0.7468 0.8298 -0.0054 0.1041  0.1649  57  LEU A CG  
335  C CD1 . LEU A 41  ? 0.5926 0.7575 0.8988 -0.0243 0.1073  0.1691  57  LEU A CD1 
336  C CD2 . LEU A 41  ? 0.5341 0.6809 0.7686 0.0024  0.0923  0.1474  57  LEU A CD2 
337  N N   . PRO A 42  ? 0.5650 0.8367 0.7617 0.0292  0.1311  0.2293  58  PRO A N   
338  C CA  . PRO A 42  ? 0.5585 0.8512 0.7310 0.0407  0.1361  0.2490  58  PRO A CA  
339  C C   . PRO A 42  ? 0.5852 0.8922 0.7176 0.0599  0.1280  0.2263  58  PRO A C   
340  O O   . PRO A 42  ? 0.5813 0.8871 0.6904 0.0696  0.1246  0.2304  58  PRO A O   
341  C CB  . PRO A 42  ? 0.5418 0.8810 0.7307 0.0360  0.1525  0.2776  58  PRO A CB  
342  C CG  . PRO A 42  ? 0.5858 0.9103 0.8186 0.0164  0.1563  0.2814  58  PRO A CG  
343  C CD  . PRO A 42  ? 0.5606 0.8584 0.7913 0.0164  0.1427  0.2441  58  PRO A CD  
344  N N   . VAL A 43  ? 0.5444 0.8653 0.6711 0.0661  0.1243  0.2017  59  VAL A N   
345  C CA  . VAL A 43  ? 0.5582 0.8860 0.6532 0.0839  0.1150  0.1762  59  VAL A CA  
346  C C   . VAL A 43  ? 0.5370 0.8180 0.6198 0.0848  0.1013  0.1613  59  VAL A C   
347  O O   . VAL A 43  ? 0.5509 0.8329 0.6096 0.0958  0.0957  0.1545  59  VAL A O   
348  C CB  . VAL A 43  ? 0.5335 0.8790 0.6321 0.0900  0.1128  0.1535  59  VAL A CB  
349  C CG1 . VAL A 43  ? 0.5383 0.8743 0.6126 0.1062  0.0999  0.1236  59  VAL A CG1 
350  C CG2 . VAL A 43  ? 0.5530 0.9559 0.6569 0.0940  0.1267  0.1656  59  VAL A CG2 
351  N N   . ARG A 44  ? 0.5423 0.7853 0.6426 0.0728  0.0959  0.1553  60  ARG A N   
352  C CA  . ARG A 44  ? 0.5808 0.7839 0.6702 0.0732  0.0841  0.1416  60  ARG A CA  
353  C C   . ARG A 44  ? 0.5377 0.7271 0.6250 0.0707  0.0855  0.1591  60  ARG A C   
354  O O   . ARG A 44  ? 0.5255 0.7009 0.5947 0.0773  0.0775  0.1502  60  ARG A O   
355  C CB  . ARG A 44  ? 0.5079 0.6816 0.6141 0.0625  0.0781  0.1295  60  ARG A CB  
356  C CG  . ARG A 44  ? 0.5309 0.7158 0.6364 0.0680  0.0734  0.1109  60  ARG A CG  
357  C CD  . ARG A 44  ? 0.5040 0.6639 0.6212 0.0596  0.0656  0.0988  60  ARG A CD  
358  N NE  . ARG A 44  ? 0.4980 0.6739 0.6190 0.0650  0.0620  0.0860  60  ARG A NE  
359  C CZ  . ARG A 44  ? 0.4978 0.6601 0.6228 0.0629  0.0531  0.0739  60  ARG A CZ  
360  N NH1 . ARG A 44  ? 0.4921 0.6257 0.6153 0.0555  0.0473  0.0708  60  ARG A NH1 
361  N NH2 . ARG A 44  ? 0.4855 0.6668 0.6165 0.0691  0.0501  0.0651  60  ARG A NH2 
362  N N   . LEU A 45  ? 0.5557 0.7491 0.6644 0.0612  0.0953  0.1845  61  LEU A N   
363  C CA  . LEU A 45  ? 0.5704 0.7531 0.6792 0.0612  0.0966  0.2042  61  LEU A CA  
364  C C   . LEU A 45  ? 0.5690 0.7828 0.6487 0.0763  0.0967  0.2103  61  LEU A C   
365  O O   . LEU A 45  ? 0.6253 0.8273 0.6899 0.0827  0.0893  0.2064  61  LEU A O   
366  C CB  . LEU A 45  ? 0.6098 0.7926 0.7511 0.0490  0.1076  0.2333  61  LEU A CB  
367  C CG  . LEU A 45  ? 0.6341 0.7834 0.8080 0.0335  0.1059  0.2250  61  LEU A CG  
368  C CD1 . LEU A 45  ? 0.6674 0.8233 0.8781 0.0210  0.1177  0.2527  61  LEU A CD1 
369  C CD2 . LEU A 45  ? 0.5738 0.6842 0.7480 0.0330  0.0970  0.2149  61  LEU A CD2 
370  N N   . ALA A 46  ? 0.5832 0.8412 0.6549 0.0827  0.1048  0.2177  62  ALA A N   
371  C CA  . ALA A 46  ? 0.6205 0.9169 0.6647 0.0977  0.1057  0.2238  62  ALA A CA  
372  C C   . ALA A 46  ? 0.6083 0.9001 0.6264 0.1100  0.0924  0.1908  62  ALA A C   
373  O O   . ALA A 46  ? 0.6148 0.9172 0.6136 0.1195  0.0873  0.1909  62  ALA A O   
374  C CB  . ALA A 46  ? 0.6090 0.9596 0.6503 0.1023  0.1180  0.2360  62  ALA A CB  
375  N N   . ASN A 47  ? 0.5607 0.8378 0.5799 0.1101  0.0862  0.1630  63  ASN A N   
376  C CA  . ASN A 47  ? 0.6645 0.9337 0.6646 0.1205  0.0736  0.1329  63  ASN A CA  
377  C C   . ASN A 47  ? 0.6161 0.8507 0.6134 0.1173  0.0644  0.1307  63  ASN A C   
378  O O   . ASN A 47  ? 0.6045 0.8477 0.5844 0.1267  0.0568  0.1188  63  ASN A O   
379  C CB  . ASN A 47  ? 0.6420 0.8957 0.6490 0.1203  0.0683  0.1085  63  ASN A CB  
380  C CG  . ASN A 47  ? 0.6801 0.9761 0.6802 0.1329  0.0720  0.0963  63  ASN A CG  
381  O OD1 . ASN A 47  ? 0.6530 0.9582 0.6393 0.1459  0.0641  0.0719  63  ASN A OD1 
382  N ND2 . ASN A 47  ? 0.6446 0.9686 0.6568 0.1292  0.0842  0.1127  63  ASN A ND2 
383  N N   . ILE A 48  ? 0.5887 0.7876 0.6043 0.1042  0.0649  0.1405  64  ILE A N   
384  C CA  . ILE A 48  ? 0.6423 0.8127 0.6560 0.1021  0.0568  0.1370  64  ILE A CA  
385  C C   . ILE A 48  ? 0.6467 0.8331 0.6564 0.1063  0.0599  0.1601  64  ILE A C   
386  O O   . ILE A 48  ? 0.5642 0.7469 0.5635 0.1115  0.0520  0.1541  64  ILE A O   
387  C CB  . ILE A 48  ? 0.6024 0.7324 0.6358 0.0887  0.0553  0.1346  64  ILE A CB  
388  C CG1 . ILE A 48  ? 0.5538 0.6588 0.5826 0.0881  0.0460  0.1235  64  ILE A CG1 
389  C CG2 . ILE A 48  ? 0.5976 0.7218 0.6544 0.0790  0.0646  0.1583  64  ILE A CG2 
390  C CD1 . ILE A 48  ? 0.6200 0.7226 0.6340 0.0940  0.0363  0.0988  64  ILE A CD1 
391  N N   . MET A 49  ? 0.6514 0.8586 0.6699 0.1047  0.0710  0.1880  65  MET A N   
392  C CA  . MET A 49  ? 0.6492 0.8751 0.6630 0.1108  0.0735  0.2137  65  MET A CA  
393  C C   . MET A 49  ? 0.6662 0.9327 0.6498 0.1266  0.0683  0.2039  65  MET A C   
394  O O   . MET A 49  ? 0.6700 0.9434 0.6439 0.1336  0.0623  0.2089  65  MET A O   
395  C CB  . MET A 49  ? 0.6002 0.8420 0.6320 0.1053  0.0873  0.2492  65  MET A CB  
396  C CG  . MET A 49  ? 0.6964 0.8966 0.7638 0.0893  0.0912  0.2587  65  MET A CG  
397  S SD  . MET A 49  ? 0.7924 1.0078 0.8890 0.0776  0.1071  0.2870  65  MET A SD  
398  C CE  . MET A 49  ? 0.7234 0.9604 0.8258 0.0824  0.1152  0.3343  65  MET A CE  
399  N N   . LYS A 50  ? 0.6909 0.9861 0.6608 0.1333  0.0693  0.1866  66  LYS A N   
400  C CA  . LYS A 50  ? 0.6992 1.0347 0.6419 0.1490  0.0632  0.1701  66  LYS A CA  
401  C C   . LYS A 50  ? 0.7156 1.0266 0.6521 0.1513  0.0480  0.1408  66  LYS A C   
402  O O   . LYS A 50  ? 0.6957 1.0320 0.6154 0.1618  0.0406  0.1334  66  LYS A O   
403  C CB  . LYS A 50  ? 0.7102 1.0790 0.6440 0.1564  0.0671  0.1526  66  LYS A CB  
404  C CG  . LYS A 50  ? 0.8134 1.2379 0.7392 0.1626  0.0803  0.1782  66  LYS A CG  
405  C CD  . LYS A 50  ? 0.8974 1.3711 0.7962 0.1783  0.0767  0.1797  66  LYS A CD  
406  C CE  . LYS A 50  ? 0.9309 1.4543 0.8094 0.1937  0.0754  0.1500  66  LYS A CE  
407  N NZ  . LYS A 50  ? 0.9991 1.5793 0.8498 0.2097  0.0720  0.1506  66  LYS A NZ  
408  N N   . GLU A 51  ? 0.6969 0.9622 0.6473 0.1414  0.0431  0.1239  67  GLU A N   
409  C CA  . GLU A 51  ? 0.7470 0.9885 0.6952 0.1414  0.0299  0.0992  67  GLU A CA  
410  C C   . GLU A 51  ? 0.7307 0.9606 0.6828 0.1388  0.0266  0.1138  67  GLU A C   
411  O O   . GLU A 51  ? 0.7147 0.9506 0.6589 0.1440  0.0164  0.0992  67  GLU A O   
412  C CB  . GLU A 51  ? 0.7141 0.9137 0.6761 0.1315  0.0266  0.0824  67  GLU A CB  
413  C CG  . GLU A 51  ? 0.7865 0.9651 0.7480 0.1311  0.0139  0.0574  67  GLU A CG  
414  C CD  . GLU A 51  ? 0.8060 0.9623 0.7744 0.1287  0.0095  0.0362  67  GLU A CD  
415  O OE1 . GLU A 51  ? 0.7988 0.9627 0.7693 0.1305  0.0153  0.0371  67  GLU A OE1 
416  O OE2 . GLU A 51  ? 0.7542 0.8867 0.7277 0.1251  0.0002  0.0201  67  GLU A OE2 
417  N N   . ILE A 52  ? 0.6874 0.9020 0.6545 0.1312  0.0347  0.1415  68  ILE A N   
418  C CA  . ILE A 52  ? 0.7221 0.9268 0.6965 0.1307  0.0323  0.1572  68  ILE A CA  
419  C C   . ILE A 52  ? 0.7439 0.9923 0.7003 0.1447  0.0292  0.1677  68  ILE A C   
420  O O   . ILE A 52  ? 0.7802 1.0282 0.7363 0.1483  0.0215  0.1674  68  ILE A O   
421  C CB  . ILE A 52  ? 0.6799 0.8612 0.6781 0.1213  0.0421  0.1842  68  ILE A CB  
422  C CG1 . ILE A 52  ? 0.6720 0.8119 0.6872 0.1082  0.0420  0.1690  68  ILE A CG1 
423  C CG2 . ILE A 52  ? 0.7098 0.8869 0.7175 0.1244  0.0404  0.2045  68  ILE A CG2 
424  C CD1 . ILE A 52  ? 0.5804 0.7003 0.6214 0.0979  0.0514  0.1880  68  ILE A CD1 
425  N N   . ASN A 53  ? 0.7888 1.0804 0.7296 0.1535  0.0349  0.1760  69  ASN A N   
426  C CA  . ASN A 53  ? 0.7688 1.1102 0.6891 0.1682  0.0315  0.1853  69  ASN A CA  
427  C C   . ASN A 53  ? 0.7131 1.0741 0.6159 0.1770  0.0176  0.1484  69  ASN A C   
428  O O   . ASN A 53  ? 0.8257 1.2233 0.7140 0.1883  0.0110  0.1508  69  ASN A O   
429  C CB  . ASN A 53  ? 0.7682 1.1570 0.6761 0.1753  0.0429  0.2073  69  ASN A CB  
430  C CG  . ASN A 53  ? 0.7977 1.1709 0.7273 0.1657  0.0569  0.2464  69  ASN A CG  
431  O OD1 . ASN A 53  ? 0.8655 1.1985 0.8176 0.1572  0.0570  0.2608  69  ASN A OD1 
432  N ND2 . ASN A 53  ? 0.9026 1.3089 0.8283 0.1668  0.0691  0.2625  69  ASN A ND2 
433  N N   . LEU A 54  ? 0.8260 1.1640 0.7321 0.1721  0.0125  0.1148  70  LEU A N   
434  C CA  . LEU A 54  ? 0.8397 1.1870 0.7376 0.1778  -0.0017 0.0781  70  LEU A CA  
435  C C   . LEU A 54  ? 0.8363 1.1609 0.7445 0.1729  -0.0117 0.0738  70  LEU A C   
436  O O   . LEU A 54  ? 0.8492 1.1875 0.7530 0.1774  -0.0241 0.0468  70  LEU A O   
437  C CB  . LEU A 54  ? 0.8979 1.2196 0.8029 0.1730  -0.0045 0.0469  70  LEU A CB  
438  C CG  . LEU A 54  ? 0.9497 1.2988 0.8455 0.1807  0.0017  0.0381  70  LEU A CG  
439  C CD1 . LEU A 54  ? 1.0625 1.3779 0.9707 0.1761  -0.0030 0.0089  70  LEU A CD1 
440  C CD2 . LEU A 54  ? 0.9724 1.3824 0.8459 0.1976  -0.0026 0.0245  70  LEU A CD2 
441  N N   . LEU A 55  ? 0.7933 1.0844 0.7179 0.1636  -0.0067 0.0970  71  LEU A N   
442  C CA  . LEU A 55  ? 0.7896 1.0639 0.7254 0.1601  -0.0147 0.0949  71  LEU A CA  
443  C C   . LEU A 55  ? 0.7579 1.0774 0.6812 0.1737  -0.0214 0.1038  71  LEU A C   
444  O O   . LEU A 55  ? 0.7112 1.0642 0.6224 0.1833  -0.0153 0.1295  71  LEU A O   
445  C CB  . LEU A 55  ? 0.7151 0.9502 0.6715 0.1500  -0.0068 0.1180  71  LEU A CB  
446  C CG  . LEU A 55  ? 0.7243 0.9166 0.6939 0.1363  -0.0016 0.1090  71  LEU A CG  
447  C CD1 . LEU A 55  ? 0.6269 0.7883 0.6169 0.1282  0.0054  0.1293  71  LEU A CD1 
448  C CD2 . LEU A 55  ? 0.6920 0.8665 0.6650 0.1302  -0.0111 0.0785  71  LEU A CD2 
449  N N   . PRO A 56  ? 0.6678 0.9916 0.5950 0.1746  -0.0337 0.0853  72  PRO A N   
450  C CA  . PRO A 56  ? 0.7510 1.1212 0.6672 0.1882  -0.0417 0.0933  72  PRO A CA  
451  C C   . PRO A 56  ? 0.7464 1.1158 0.6695 0.1923  -0.0346 0.1353  72  PRO A C   
452  O O   . PRO A 56  ? 0.6786 1.0048 0.6217 0.1826  -0.0268 0.1506  72  PRO A O   
453  C CB  . PRO A 56  ? 0.7538 1.1172 0.6821 0.1838  -0.0554 0.0650  72  PRO A CB  
454  C CG  . PRO A 56  ? 0.7758 1.0958 0.7169 0.1690  -0.0549 0.0392  72  PRO A CG  
455  C CD  . PRO A 56  ? 0.7294 1.0175 0.6733 0.1624  -0.0407 0.0587  72  PRO A CD  
456  N N   . ASP A 57  ? 0.6834 1.1029 0.5910 0.2078  -0.0382 0.1534  73  ASP A N   
457  C CA  . ASP A 57  ? 0.6926 1.1140 0.6083 0.2137  -0.0317 0.1975  73  ASP A CA  
458  C C   . ASP A 57  ? 0.6874 1.0709 0.6305 0.2082  -0.0349 0.2018  73  ASP A C   
459  O O   . ASP A 57  ? 0.6673 1.0239 0.6293 0.2063  -0.0264 0.2320  73  ASP A O   
460  C CB  . ASP A 57  ? 0.7401 1.2267 0.6338 0.2327  -0.0373 0.2158  73  ASP A CB  
461  C CG  . ASP A 57  ? 0.8900 1.3781 0.7942 0.2399  -0.0305 0.2668  73  ASP A CG  
462  O OD1 . ASP A 57  ? 0.9338 1.3997 0.8471 0.2339  -0.0162 0.2946  73  ASP A OD1 
463  O OD2 . ASP A 57  ? 0.9743 1.4848 0.8811 0.2513  -0.0398 0.2793  73  ASP A OD2 
464  N N   . ARG A 58  ? 0.6513 1.0331 0.6001 0.2055  -0.0468 0.1711  74  ARG A N   
465  C CA  . ARG A 58  ? 0.6920 1.0439 0.6673 0.2011  -0.0492 0.1737  74  ARG A CA  
466  C C   . ARG A 58  ? 0.6316 0.9255 0.6274 0.1848  -0.0389 0.1709  74  ARG A C   
467  O O   . ARG A 58  ? 0.6722 0.9404 0.6915 0.1822  -0.0374 0.1786  74  ARG A O   
468  C CB  . ARG A 58  ? 0.6376 1.0063 0.6161 0.2006  -0.0637 0.1416  74  ARG A CB  
469  C CG  . ARG A 58  ? 0.6338 0.9791 0.6142 0.1855  -0.0656 0.1042  74  ARG A CG  
470  C CD  . ARG A 58  ? 0.6692 1.0335 0.6571 0.1838  -0.0801 0.0740  74  ARG A CD  
471  N NE  . ARG A 58  ? 0.6627 1.0038 0.6553 0.1692  -0.0820 0.0412  74  ARG A NE  
472  C CZ  . ARG A 58  ? 0.7529 1.1095 0.7307 0.1703  -0.0863 0.0190  74  ARG A CZ  
473  N NH1 . ARG A 58  ? 0.7046 1.1050 0.6588 0.1852  -0.0887 0.0235  74  ARG A NH1 
474  N NH2 . ARG A 58  ? 0.7510 1.0799 0.7390 0.1569  -0.0881 -0.0080 74  ARG A NH2 
475  N N   . VAL A 59  ? 0.6472 0.9234 0.6352 0.1751  -0.0323 0.1590  75  VAL A N   
476  C CA  . VAL A 59  ? 0.6272 0.8549 0.6320 0.1614  -0.0220 0.1604  75  VAL A CA  
477  C C   . VAL A 59  ? 0.6785 0.9000 0.6864 0.1630  -0.0101 0.1923  75  VAL A C   
478  O O   . VAL A 59  ? 0.6041 0.7934 0.6348 0.1576  -0.0033 0.2066  75  VAL A O   
479  C CB  . VAL A 59  ? 0.6093 0.8205 0.6073 0.1499  -0.0224 0.1304  75  VAL A CB  
480  C CG1 . VAL A 59  ? 0.6312 0.7995 0.6431 0.1370  -0.0122 0.1329  75  VAL A CG1 
481  C CG2 . VAL A 59  ? 0.6136 0.8257 0.6157 0.1457  -0.0332 0.1022  75  VAL A CG2 
482  N N   . LEU A 60  ? 0.6740 0.9295 0.6609 0.1705  -0.0078 0.2026  76  LEU A N   
483  C CA  . LEU A 60  ? 0.7093 0.9652 0.6992 0.1707  0.0045  0.2340  76  LEU A CA  
484  C C   . LEU A 60  ? 0.6737 0.9240 0.6839 0.1766  0.0077  0.2707  76  LEU A C   
485  O O   . LEU A 60  ? 0.7789 1.0039 0.8092 0.1703  0.0181  0.2929  76  LEU A O   
486  C CB  . LEU A 60  ? 0.7660 1.0714 0.7271 0.1801  0.0055  0.2372  76  LEU A CB  
487  C CG  . LEU A 60  ? 0.9064 1.2219 0.8632 0.1779  0.0187  0.2571  76  LEU A CG  
488  C CD1 . LEU A 60  ? 0.8172 1.1830 0.7428 0.1873  0.0159  0.2403  76  LEU A CD1 
489  C CD2 . LEU A 60  ? 0.9631 1.2888 0.9314 0.1830  0.0269  0.3048  76  LEU A CD2 
490  N N   . SER A 61  ? 0.6093 0.8815 0.6183 0.1887  -0.0017 0.2772  77  SER A N   
491  C CA  . SER A 61  ? 0.7697 1.0393 0.7991 0.1974  0.0002  0.3148  77  SER A CA  
492  C C   . SER A 61  ? 0.7202 0.9455 0.7833 0.1925  -0.0012 0.3088  77  SER A C   
493  O O   . SER A 61  ? 0.8265 1.0491 0.9099 0.2021  -0.0025 0.3346  77  SER A O   
494  C CB  . SER A 61  ? 0.7501 1.0728 0.7615 0.2160  -0.0096 0.3294  77  SER A CB  
495  O OG  . SER A 61  ? 0.8060 1.1354 0.8163 0.2187  -0.0227 0.2995  77  SER A OG  
496  N N   . THR A 62  ? 0.7400 0.9329 0.8101 0.1790  -0.0008 0.2763  78  THR A N   
497  C CA  . THR A 62  ? 0.7269 0.8822 0.8288 0.1749  -0.0005 0.2705  78  THR A CA  
498  C C   . THR A 62  ? 0.7152 0.8330 0.8437 0.1666  0.0110  0.2869  78  THR A C   
499  O O   . THR A 62  ? 0.6955 0.8110 0.8162 0.1588  0.0188  0.2925  78  THR A O   
500  C CB  . THR A 62  ? 0.7042 0.8451 0.8035 0.1641  -0.0045 0.2311  78  THR A CB  
501  O OG1 . THR A 62  ? 0.6719 0.7999 0.7588 0.1513  0.0013  0.2164  78  THR A OG1 
502  C CG2 . THR A 62  ? 0.7695 0.9453 0.8507 0.1708  -0.0165 0.2140  78  THR A CG2 
503  N N   . PRO A 63  ? 0.6650 0.7545 0.8281 0.1683  0.0118  0.2932  79  PRO A N   
504  C CA  . PRO A 63  ? 0.6073 0.6625 0.8011 0.1612  0.0217  0.3097  79  PRO A CA  
505  C C   . PRO A 63  ? 0.6971 0.7287 0.8903 0.1437  0.0282  0.2857  79  PRO A C   
506  O O   . PRO A 63  ? 0.6484 0.6670 0.8544 0.1361  0.0366  0.3006  79  PRO A O   
507  C CB  . PRO A 63  ? 0.6163 0.6474 0.8478 0.1680  0.0188  0.3104  79  PRO A CB  
508  C CG  . PRO A 63  ? 0.6213 0.6854 0.8399 0.1840  0.0081  0.3142  79  PRO A CG  
509  C CD  . PRO A 63  ? 0.6357 0.7266 0.8147 0.1785  0.0037  0.2876  79  PRO A CD  
510  N N   . SER A 64  ? 0.6049 0.6324 0.7859 0.1368  0.0244  0.2505  80  SER A N   
511  C CA  . SER A 64  ? 0.6298 0.6360 0.8122 0.1216  0.0297  0.2295  80  SER A CA  
512  C C   . SER A 64  ? 0.6393 0.6615 0.7968 0.1164  0.0337  0.2340  80  SER A C   
513  O O   . SER A 64  ? 0.6373 0.6446 0.8048 0.1064  0.0407  0.2349  80  SER A O   
514  C CB  . SER A 64  ? 0.5796 0.5807 0.7551 0.1162  0.0251  0.1952  80  SER A CB  
515  O OG  . SER A 64  ? 0.6604 0.6880 0.8068 0.1199  0.0181  0.1859  80  SER A OG  
516  N N   . VAL A 65  ? 0.6226 0.6775 0.7496 0.1238  0.0290  0.2356  81  VAL A N   
517  C CA  . VAL A 65  ? 0.6566 0.7304 0.7609 0.1210  0.0327  0.2374  81  VAL A CA  
518  C C   . VAL A 65  ? 0.6883 0.7709 0.8027 0.1231  0.0415  0.2726  81  VAL A C   
519  O O   . VAL A 65  ? 0.6071 0.6887 0.7221 0.1150  0.0491  0.2758  81  VAL A O   
520  C CB  . VAL A 65  ? 0.7097 0.8179 0.7813 0.1291  0.0246  0.2248  81  VAL A CB  
521  C CG1 . VAL A 65  ? 0.6710 0.8040 0.7210 0.1295  0.0289  0.2274  81  VAL A CG1 
522  C CG2 . VAL A 65  ? 0.6246 0.7206 0.6908 0.1232  0.0173  0.1905  81  VAL A CG2 
523  N N   . GLN A 66  ? 0.6598 0.7519 0.7847 0.1339  0.0407  0.3013  82  GLN A N   
524  C CA  . GLN A 66  ? 0.6727 0.7708 0.8126 0.1351  0.0497  0.3404  82  GLN A CA  
525  C C   . GLN A 66  ? 0.6611 0.7195 0.8382 0.1209  0.0579  0.3427  82  GLN A C   
526  O O   . GLN A 66  ? 0.6973 0.7601 0.8821 0.1138  0.0673  0.3609  82  GLN A O   
527  C CB  . GLN A 66  ? 0.6378 0.7483 0.7874 0.1498  0.0461  0.3719  82  GLN A CB  
528  C CG  . GLN A 66  ? 0.7077 0.8670 0.8207 0.1647  0.0380  0.3739  82  GLN A CG  
529  C CD  . GLN A 66  ? 0.9036 1.0778 1.0265 0.1809  0.0327  0.4051  82  GLN A CD  
530  O OE1 . GLN A 66  ? 0.8348 0.9764 0.9940 0.1820  0.0331  0.4190  82  GLN A OE1 
531  N NE2 . GLN A 66  ? 0.9839 1.2095 1.0754 0.1948  0.0269  0.4151  82  GLN A NE2 
532  N N   . LEU A 67  ? 0.6260 0.6488 0.8275 0.1165  0.0545  0.3224  83  LEU A N   
533  C CA  . LEU A 67  ? 0.6892 0.6761 0.9277 0.1033  0.0608  0.3183  83  LEU A CA  
534  C C   . LEU A 67  ? 0.6776 0.6666 0.9037 0.0900  0.0652  0.2992  83  LEU A C   
535  O O   . LEU A 67  ? 0.6598 0.6430 0.9061 0.0804  0.0734  0.3128  83  LEU A O   
536  C CB  . LEU A 67  ? 0.6499 0.6060 0.9117 0.1028  0.0554  0.2934  83  LEU A CB  
537  C CG  . LEU A 67  ? 0.7179 0.6384 1.0206 0.0905  0.0600  0.2824  83  LEU A CG  
538  C CD1 . LEU A 67  ? 0.6792 0.5842 1.0230 0.0904  0.0661  0.3188  83  LEU A CD1 
539  C CD2 . LEU A 67  ? 0.6801 0.5801 0.9980 0.0920  0.0543  0.2510  83  LEU A CD2 
540  N N   . VAL A 68  ? 0.6748 0.6733 0.8702 0.0894  0.0597  0.2691  84  VAL A N   
541  C CA  . VAL A 68  ? 0.6450 0.6463 0.8287 0.0790  0.0626  0.2510  84  VAL A CA  
542  C C   . VAL A 68  ? 0.6566 0.6881 0.8261 0.0802  0.0692  0.2722  84  VAL A C   
543  O O   . VAL A 68  ? 0.6400 0.6705 0.8210 0.0702  0.0761  0.2741  84  VAL A O   
544  C CB  . VAL A 68  ? 0.6393 0.6443 0.7949 0.0797  0.0547  0.2186  84  VAL A CB  
545  C CG1 . VAL A 68  ? 0.5477 0.5618 0.6872 0.0730  0.0567  0.2048  84  VAL A CG1 
546  C CG2 . VAL A 68  ? 0.5636 0.5419 0.7358 0.0755  0.0508  0.1969  84  VAL A CG2 
547  N N   . GLN A 69  ? 0.6154 0.6785 0.7599 0.0927  0.0673  0.2871  85  GLN A N   
548  C CA  . GLN A 69  ? 0.6579 0.7573 0.7880 0.0959  0.0744  0.3090  85  GLN A CA  
549  C C   . GLN A 69  ? 0.6917 0.7848 0.8551 0.0885  0.0855  0.3428  85  GLN A C   
550  O O   . GLN A 69  ? 0.7163 0.8285 0.8797 0.0827  0.0942  0.3527  85  GLN A O   
551  C CB  . GLN A 69  ? 0.7593 0.8963 0.8609 0.1120  0.0698  0.3217  85  GLN A CB  
552  C CG  . GLN A 69  ? 0.8248 0.9951 0.8884 0.1185  0.0652  0.2983  85  GLN A CG  
553  C CD  . GLN A 69  ? 0.9193 1.1277 0.9567 0.1347  0.0581  0.3045  85  GLN A CD  
554  O OE1 . GLN A 69  ? 0.9304 1.1374 0.9767 0.1415  0.0549  0.3237  85  GLN A OE1 
555  N NE2 . GLN A 69  ? 0.9210 1.1652 0.9278 0.1418  0.0548  0.2864  85  GLN A NE2 
556  N N   . SER A 70  ? 0.6396 0.7063 0.8350 0.0885  0.0855  0.3611  86  SER A N   
557  C CA  . SER A 70  ? 0.7260 0.7830 0.9596 0.0805  0.0958  0.3955  86  SER A CA  
558  C C   . SER A 70  ? 0.7064 0.7392 0.9676 0.0627  0.1007  0.3781  86  SER A C   
559  O O   . SER A 70  ? 0.7721 0.8108 1.0565 0.0531  0.1109  0.4013  86  SER A O   
560  C CB  . SER A 70  ? 0.7494 0.7799 1.0161 0.0858  0.0935  0.4177  86  SER A CB  
561  O OG  . SER A 70  ? 0.6936 0.6828 0.9835 0.0811  0.0872  0.3871  86  SER A OG  
562  N N   . TRP A 71  ? 0.6936 0.7033 0.9531 0.0578  0.0937  0.3384  87  TRP A N   
563  C CA  . TRP A 71  ? 0.7563 0.7493 1.0379 0.0421  0.0966  0.3183  87  TRP A CA  
564  C C   . TRP A 71  ? 0.7135 0.7387 0.9723 0.0385  0.1015  0.3148  87  TRP A C   
565  O O   . TRP A 71  ? 0.7606 0.7889 1.0440 0.0265  0.1094  0.3235  87  TRP A O   
566  C CB  . TRP A 71  ? 0.6794 0.6469 0.9599 0.0399  0.0875  0.2782  87  TRP A CB  
567  C CG  . TRP A 71  ? 0.7326 0.6684 1.0439 0.0419  0.0839  0.2770  87  TRP A CG  
568  C CD1 . TRP A 71  ? 0.7325 0.6516 1.0830 0.0418  0.0881  0.3053  87  TRP A CD1 
569  C CD2 . TRP A 71  ? 0.7079 0.6261 1.0164 0.0451  0.0757  0.2463  87  TRP A CD2 
570  N NE1 . TRP A 71  ? 0.7466 0.6373 1.1196 0.0460  0.0822  0.2914  87  TRP A NE1 
571  C CE2 . TRP A 71  ? 0.7415 0.6337 1.0883 0.0479  0.0750  0.2547  87  TRP A CE2 
572  C CE3 . TRP A 71  ? 0.7619 0.6850 1.0411 0.0459  0.0692  0.2141  87  TRP A CE3 
573  C CZ2 . TRP A 71  ? 0.7828 0.6575 1.1379 0.0523  0.0685  0.2290  87  TRP A CZ2 
574  C CZ3 . TRP A 71  ? 0.7485 0.6553 1.0351 0.0487  0.0635  0.1920  87  TRP A CZ3 
575  C CH2 . TRP A 71  ? 0.7575 0.6422 1.0809 0.0523  0.0634  0.1980  87  TRP A CH2 
576  N N   . TYR A 72  ? 0.7232 0.7731 0.9385 0.0487  0.0966  0.3006  88  TYR A N   
577  C CA  . TYR A 72  ? 0.6580 0.7393 0.8524 0.0480  0.1006  0.2945  88  TYR A CA  
578  C C   . TYR A 72  ? 0.7980 0.9121 0.9988 0.0479  0.1125  0.3308  88  TYR A C   
579  O O   . TYR A 72  ? 0.7162 0.8477 0.9252 0.0401  0.1199  0.3322  88  TYR A O   
580  C CB  . TYR A 72  ? 0.6571 0.7570 0.8080 0.0606  0.0924  0.2730  88  TYR A CB  
581  C CG  . TYR A 72  ? 0.6466 0.7223 0.7920 0.0568  0.0835  0.2368  88  TYR A CG  
582  C CD1 . TYR A 72  ? 0.6424 0.6862 0.7995 0.0545  0.0773  0.2254  88  TYR A CD1 
583  C CD2 . TYR A 72  ? 0.6664 0.7533 0.7962 0.0562  0.0816  0.2156  88  TYR A CD2 
584  C CE1 . TYR A 72  ? 0.6964 0.7231 0.8477 0.0508  0.0703  0.1956  88  TYR A CE1 
585  C CE2 . TYR A 72  ? 0.7009 0.7670 0.8260 0.0529  0.0736  0.1871  88  TYR A CE2 
586  C CZ  . TYR A 72  ? 0.6639 0.7013 0.7988 0.0498  0.0684  0.1781  88  TYR A CZ  
587  O OH  . TYR A 72  ? 0.6554 0.6772 0.7848 0.0464  0.0615  0.1528  88  TYR A OH  
588  N N   . VAL A 73  ? 0.7243 0.8511 0.9214 0.0570  0.1147  0.3617  89  VAL A N   
589  C CA  . VAL A 73  ? 0.7632 0.9254 0.9658 0.0572  0.1270  0.4014  89  VAL A CA  
590  C C   . VAL A 73  ? 0.8005 0.9430 1.0530 0.0392  0.1367  0.4196  89  VAL A C   
591  O O   . VAL A 73  ? 0.7509 0.9211 1.0112 0.0317  0.1472  0.4323  89  VAL A O   
592  C CB  . VAL A 73  ? 0.7958 0.9741 0.9875 0.0708  0.1263  0.4340  89  VAL A CB  
593  C CG1 . VAL A 73  ? 0.7691 0.9768 0.9780 0.0681  0.1405  0.4837  89  VAL A CG1 
594  C CG2 . VAL A 73  ? 0.7376 0.9513 0.8789 0.0881  0.1184  0.4167  89  VAL A CG2 
595  N N   . GLN A 74  ? 0.8000 0.8954 1.0896 0.0316  0.1329  0.4177  90  GLN A N   
596  C CA  . GLN A 74  ? 0.8151 0.8882 1.1587 0.0136  0.1407  0.4318  90  GLN A CA  
597  C C   . GLN A 74  ? 0.7411 0.8160 1.0920 0.0006  0.1415  0.4012  90  GLN A C   
598  O O   . GLN A 74  ? 0.7431 0.8325 1.1210 -0.0123 0.1517  0.4171  90  GLN A O   
599  C CB  . GLN A 74  ? 0.8432 0.8651 1.2257 0.0105  0.1346  0.4288  90  GLN A CB  
600  C CG  . GLN A 74  ? 0.8163 0.8120 1.2622 -0.0076 0.1420  0.4459  90  GLN A CG  
601  C CD  . GLN A 74  ? 0.9054 0.9213 1.3718 -0.0099 0.1548  0.5021  90  GLN A CD  
602  O OE1 . GLN A 74  ? 0.9371 0.9509 1.4038 0.0015  0.1522  0.5254  90  GLN A OE1 
603  N NE2 . GLN A 74  ? 0.8597 0.9021 1.3392 -0.0230 0.1656  0.5143  90  GLN A NE2 
604  N N   . SER A 75  ? 0.7952 0.8578 1.1235 0.0037  0.1308  0.3588  91  SER A N   
605  C CA  . SER A 75  ? 0.7280 0.7949 1.0601 -0.0063 0.1298  0.3297  91  SER A CA  
606  C C   . SER A 75  ? 0.7158 0.8302 1.0296 -0.0050 0.1383  0.3401  91  SER A C   
607  O O   . SER A 75  ? 0.7185 0.8439 1.0561 -0.0174 0.1439  0.3371  91  SER A O   
608  C CB  . SER A 75  ? 0.7050 0.7571 1.0085 0.0001  0.1170  0.2886  91  SER A CB  
609  O OG  . SER A 75  ? 0.7575 0.7700 1.0834 -0.0032 0.1104  0.2752  91  SER A OG  
610  N N   . LEU A 76  ? 0.7102 0.8565 0.9832 0.0106  0.1393  0.3504  92  LEU A N   
611  C CA  . LEU A 76  ? 0.7128 0.9092 0.9672 0.0145  0.1477  0.3581  92  LEU A CA  
612  C C   . LEU A 76  ? 0.7778 0.9960 1.0658 0.0035  0.1631  0.3988  92  LEU A C   
613  O O   . LEU A 76  ? 0.7752 1.0219 1.0748 -0.0042 0.1714  0.3997  92  LEU A O   
614  C CB  . LEU A 76  ? 0.6632 0.8900 0.8687 0.0344  0.1444  0.3579  92  LEU A CB  
615  C CG  . LEU A 76  ? 0.7666 1.0516 0.9486 0.0426  0.1529  0.3642  92  LEU A CG  
616  C CD1 . LEU A 76  ? 0.7327 1.0247 0.9170 0.0382  0.1517  0.3340  92  LEU A CD1 
617  C CD2 . LEU A 76  ? 0.7931 1.1041 0.9290 0.0627  0.1466  0.3564  92  LEU A CD2 
618  N N   . LEU A 77  ? 0.6860 0.8912 0.9929 0.0025  0.1672  0.4341  93  LEU A N   
619  C CA  . LEU A 77  ? 0.7706 0.9937 1.1138 -0.0090 0.1824  0.4787  93  LEU A CA  
620  C C   . LEU A 77  ? 0.7464 0.9449 1.1442 -0.0316 0.1859  0.4719  93  LEU A C   
621  O O   . LEU A 77  ? 0.7869 1.0148 1.2097 -0.0435 0.1987  0.4933  93  LEU A O   
622  C CB  . LEU A 77  ? 0.7740 0.9817 1.1293 -0.0043 0.1839  0.5183  93  LEU A CB  
623  C CG  . LEU A 77  ? 0.8441 1.0852 1.1476 0.0180  0.1809  0.5298  93  LEU A CG  
624  C CD1 . LEU A 77  ? 0.8886 1.1137 1.2071 0.0237  0.1801  0.5672  93  LEU A CD1 
625  C CD2 . LEU A 77  ? 0.9012 1.2114 1.1750 0.0245  0.1923  0.5454  93  LEU A CD2 
626  N N   . ASP A 78  ? 0.7355 0.8838 1.1539 -0.0379 0.1746  0.4414  94  ASP A N   
627  C CA  . ASP A 78  ? 0.7191 0.8462 1.1887 -0.0587 0.1755  0.4273  94  ASP A CA  
628  C C   . ASP A 78  ? 0.7572 0.9222 1.2184 -0.0635 0.1788  0.4083  94  ASP A C   
629  O O   . ASP A 78  ? 0.7662 0.9457 1.2680 -0.0803 0.1882  0.4207  94  ASP A O   
630  C CB  . ASP A 78  ? 0.7364 0.8135 1.2180 -0.0607 0.1612  0.3888  94  ASP A CB  
631  C CG  . ASP A 78  ? 0.7214 0.7571 1.2277 -0.0588 0.1583  0.4053  94  ASP A CG  
632  O OD1 . ASP A 78  ? 0.7644 0.8033 1.2923 -0.0603 0.1678  0.4499  94  ASP A OD1 
633  O OD2 . ASP A 78  ? 0.7474 0.7488 1.2524 -0.0551 0.1466  0.3738  94  ASP A OD2 
634  N N   . ILE A 79  ? 0.7173 0.8993 1.1287 -0.0488 0.1710  0.3786  95  ILE A N   
635  C CA  . ILE A 79  ? 0.7338 0.9478 1.1390 -0.0512 0.1719  0.3565  95  ILE A CA  
636  C C   . ILE A 79  ? 0.7581 1.0279 1.1609 -0.0507 0.1874  0.3865  95  ILE A C   
637  O O   . ILE A 79  ? 0.7525 1.0461 1.1854 -0.0638 0.1950  0.3883  95  ILE A O   
638  C CB  . ILE A 79  ? 0.7657 0.9794 1.1225 -0.0350 0.1589  0.3184  95  ILE A CB  
639  C CG1 . ILE A 79  ? 0.6955 0.8627 1.0609 -0.0392 0.1452  0.2866  95  ILE A CG1 
640  C CG2 . ILE A 79  ? 0.6970 0.9505 1.0448 -0.0331 0.1609  0.3018  95  ILE A CG2 
641  C CD1 . ILE A 79  ? 0.7259 0.8875 1.0457 -0.0238 0.1329  0.2565  95  ILE A CD1 
642  N N   . MET A 80  ? 0.7496 1.0459 1.1169 -0.0354 0.1924  0.4095  96  MET A N   
643  C CA  . MET A 80  ? 0.8395 1.1978 1.1985 -0.0324 0.2071  0.4327  96  MET A CA  
644  C C   . MET A 80  ? 0.8677 1.2394 1.2776 -0.0518 0.2235  0.4763  96  MET A C   
645  O O   . MET A 80  ? 0.7879 1.2158 1.1947 -0.0512 0.2380  0.5006  96  MET A O   
646  C CB  . MET A 80  ? 0.8580 1.2495 1.1645 -0.0101 0.2079  0.4435  96  MET A CB  
647  C CG  . MET A 80  ? 0.9061 1.2747 1.2037 -0.0036 0.2052  0.4690  96  MET A CG  
648  S SD  . MET A 80  ? 0.9554 1.3630 1.1849 0.0249  0.1998  0.4619  96  MET A SD  
649  C CE  . MET A 80  ? 0.8997 1.3708 1.1278 0.0277  0.2191  0.5202  96  MET A CE  
650  N N   . GLU A 81  ? 0.8685 1.1921 1.3277 -0.0694 0.2218  0.4854  97  GLU A N   
651  C CA  . GLU A 81  ? 0.8564 1.1860 1.3714 -0.0905 0.2339  0.5161  97  GLU A CA  
652  C C   . GLU A 81  ? 0.8598 1.2200 1.4001 -0.1042 0.2393  0.4980  97  GLU A C   
653  O O   . GLU A 81  ? 0.8670 1.2596 1.4237 -0.1120 0.2483  0.5159  97  GLU A O   
654  C CB  . GLU A 81  ? 0.8834 1.1480 1.4450 -0.1036 0.2258  0.5165  97  GLU A CB  
655  C CG  . GLU A 81  ? 0.9836 1.2208 1.5324 -0.0913 0.2211  0.5404  97  GLU A CG  
656  C CD  . GLU A 81  ? 1.1221 1.3608 1.7011 -0.0973 0.2264  0.5774  97  GLU A CD  
657  O OE1 . GLU A 81  ? 1.1949 1.4253 1.8225 -0.1165 0.2298  0.5781  97  GLU A OE1 
658  O OE2 . GLU A 81  ? 1.1627 1.4128 1.7180 -0.0827 0.2270  0.6059  97  GLU A OE2 
659  N N   . PHE A 82  ? 0.7647 1.1079 1.2957 -0.1020 0.2257  0.4499  98  PHE A N   
660  C CA  . PHE A 82  ? 0.7889 1.1548 1.3456 -0.1138 0.2261  0.4262  98  PHE A CA  
661  C C   . PHE A 82  ? 0.7866 1.2172 1.3101 -0.1009 0.2335  0.4228  98  PHE A C   
662  O O   . PHE A 82  ? 0.8075 1.2636 1.3503 -0.1081 0.2338  0.4033  98  PHE A O   
663  C CB  . PHE A 82  ? 0.7371 1.0636 1.2913 -0.1134 0.2070  0.3761  98  PHE A CB  
664  C CG  . PHE A 82  ? 0.7464 1.0143 1.3388 -0.1266 0.1994  0.3715  98  PHE A CG  
665  C CD1 . PHE A 82  ? 0.7014 0.9293 1.2722 -0.1159 0.1929  0.3758  98  PHE A CD1 
666  C CD2 . PHE A 82  ? 0.7639 1.0189 1.4165 -0.1495 0.1985  0.3609  98  PHE A CD2 
667  C CE1 . PHE A 82  ? 0.7018 0.8775 1.3099 -0.1263 0.1860  0.3694  98  PHE A CE1 
668  C CE2 . PHE A 82  ? 0.8047 1.0065 1.4952 -0.1606 0.1909  0.3524  98  PHE A CE2 
669  C CZ  . PHE A 82  ? 0.7305 0.8924 1.3984 -0.1483 0.1850  0.3566  98  PHE A CZ  
670  N N   . LEU A 83  ? 0.7571 1.2174 1.2334 -0.0815 0.2389  0.4396  99  LEU A N   
671  C CA  . LEU A 83  ? 0.7987 1.3190 1.2393 -0.0652 0.2437  0.4283  99  LEU A CA  
672  C C   . LEU A 83  ? 0.8202 1.3994 1.2952 -0.0781 0.2620  0.4515  99  LEU A C   
673  O O   . LEU A 83  ? 0.7777 1.4021 1.2413 -0.0698 0.2638  0.4306  99  LEU A O   
674  C CB  . LEU A 83  ? 0.7210 1.2625 1.1069 -0.0422 0.2452  0.4403  99  LEU A CB  
675  C CG  . LEU A 83  ? 0.8724 1.3731 1.2146 -0.0243 0.2262  0.4059  99  LEU A CG  
676  C CD1 . LEU A 83  ? 0.8618 1.3835 1.1587 -0.0050 0.2280  0.4221  99  LEU A CD1 
677  C CD2 . LEU A 83  ? 0.7935 1.3004 1.1161 -0.0133 0.2149  0.3590  99  LEU A CD2 
678  N N   . ASP A 84  ? 0.7652 1.3352 1.2757 -0.0955 0.2701  0.4861  100 ASP A N   
679  C CA  . ASP A 84  ? 0.8231 1.4340 1.3581 -0.1068 0.2808  0.4998  100 ASP A CA  
680  C C   . ASP A 84  ? 0.8461 1.4330 1.4443 -0.1336 0.2792  0.4910  100 ASP A C   
681  O O   . ASP A 84  ? 0.8872 1.5053 1.5120 -0.1459 0.2881  0.5018  100 ASP A O   
682  C CB  . ASP A 84  ? 0.7849 1.4070 1.3112 -0.1054 0.2888  0.5424  100 ASP A CB  
683  C CG  . ASP A 84  ? 0.9341 1.4938 1.4870 -0.1161 0.2834  0.5650  100 ASP A CG  
684  O OD1 . ASP A 84  ? 0.9176 1.4241 1.4850 -0.1209 0.2728  0.5457  100 ASP A OD1 
685  O OD2 . ASP A 84  ? 0.9393 1.5049 1.4996 -0.1187 0.2896  0.6018  100 ASP A OD2 
686  N N   . LYS A 85  ? 0.8173 1.3522 1.4410 -0.1430 0.2678  0.4700  101 LYS A N   
687  C CA  . LYS A 85  ? 0.8576 1.3668 1.5430 -0.1687 0.2643  0.4599  101 LYS A CA  
688  C C   . LYS A 85  ? 0.8355 1.3823 1.5390 -0.1733 0.2624  0.4268  101 LYS A C   
689  O O   . LYS A 85  ? 0.7746 1.3557 1.4450 -0.1553 0.2609  0.4075  101 LYS A O   
690  C CB  . LYS A 85  ? 0.8284 1.2673 1.5366 -0.1766 0.2517  0.4484  101 LYS A CB  
691  C CG  . LYS A 85  ? 0.9301 1.3271 1.6537 -0.1826 0.2531  0.4812  101 LYS A CG  
692  C CD  . LYS A 85  ? 1.0153 1.3449 1.7560 -0.1856 0.2397  0.4646  101 LYS A CD  
693  C CE  . LYS A 85  ? 1.0517 1.3407 1.8055 -0.1863 0.2397  0.4961  101 LYS A CE  
694  N NZ  . LYS A 85  ? 0.9861 1.2147 1.7466 -0.1833 0.2264  0.4765  101 LYS A NZ  
695  N N   . ASP A 86  ? 0.8649 1.4060 1.6235 -0.1968 0.2614  0.4194  102 ASP A N   
696  C CA  . ASP A 86  ? 0.8455 1.4316 1.6272 -0.2029 0.2609  0.3934  102 ASP A CA  
697  C C   . ASP A 86  ? 0.8154 1.3787 1.6172 -0.2061 0.2444  0.3527  102 ASP A C   
698  O O   . ASP A 86  ? 0.7961 1.3093 1.6339 -0.2224 0.2353  0.3424  102 ASP A O   
699  C CB  . ASP A 86  ? 0.8207 1.4186 1.6522 -0.2271 0.2683  0.4059  102 ASP A CB  
700  C CG  . ASP A 86  ? 0.8311 1.4879 1.6815 -0.2311 0.2706  0.3845  102 ASP A CG  
701  O OD1 . ASP A 86  ? 0.8313 1.5157 1.6607 -0.2149 0.2640  0.3572  102 ASP A OD1 
702  O OD2 . ASP A 86  ? 0.8583 1.5351 1.7463 -0.2498 0.2788  0.3955  102 ASP A OD2 
703  N N   . PRO A 87  ? 0.8327 1.4172 1.5929 -0.1854 0.2336  0.3184  103 PRO A N   
704  C CA  . PRO A 87  ? 0.8099 1.3620 1.5663 -0.1827 0.2113  0.2721  103 PRO A CA  
705  C C   . PRO A 87  ? 0.8316 1.3971 1.6517 -0.2064 0.2068  0.2530  103 PRO A C   
706  O O   . PRO A 87  ? 0.8158 1.3487 1.6442 -0.2101 0.1892  0.2190  103 PRO A O   
707  C CB  . PRO A 87  ? 0.7900 1.3686 1.4881 -0.1537 0.2034  0.2483  103 PRO A CB  
708  C CG  . PRO A 87  ? 0.8045 1.4106 1.4656 -0.1382 0.2188  0.2788  103 PRO A CG  
709  C CD  . PRO A 87  ? 0.8134 1.4460 1.5219 -0.1602 0.2396  0.3203  103 PRO A CD  
710  N N   . GLU A 88  ? 0.8043 1.4203 1.6701 -0.2228 0.2219  0.2725  104 GLU A N   
711  C CA  . GLU A 88  ? 0.7881 1.4205 1.7199 -0.2472 0.2174  0.2536  104 GLU A CA  
712  C C   . GLU A 88  ? 0.8144 1.3917 1.7913 -0.2722 0.2143  0.2568  104 GLU A C   
713  O O   . GLU A 88  ? 0.8513 1.4298 1.8750 -0.2915 0.2060  0.2330  104 GLU A O   
714  C CB  . GLU A 88  ? 0.7513 1.4477 1.7016 -0.2535 0.2317  0.2675  104 GLU A CB  
715  C CG  . GLU A 88  ? 0.7787 1.5339 1.6864 -0.2270 0.2375  0.2677  104 GLU A CG  
716  C CD  . GLU A 88  ? 0.8748 1.6327 1.7535 -0.2076 0.2160  0.2213  104 GLU A CD  
717  O OE1 . GLU A 88  ? 0.8729 1.6324 1.7905 -0.2211 0.2030  0.1929  104 GLU A OE1 
718  O OE2 . GLU A 88  ? 0.9045 1.6626 1.7212 -0.1784 0.2111  0.2128  104 GLU A OE2 
719  N N   . ASP A 89  ? 0.8526 1.3811 1.8121 -0.2700 0.2188  0.2828  105 ASP A N   
720  C CA  . ASP A 89  ? 0.8950 1.3645 1.8905 -0.2884 0.2142  0.2856  105 ASP A CA  
721  C C   . ASP A 89  ? 0.9169 1.3381 1.9098 -0.2836 0.1970  0.2531  105 ASP A C   
722  O O   . ASP A 89  ? 0.8625 1.2632 1.8149 -0.2659 0.1962  0.2600  105 ASP A O   
723  C CB  . ASP A 89  ? 0.8805 1.3274 1.8605 -0.2861 0.2279  0.3331  105 ASP A CB  
724  C CG  . ASP A 89  ? 0.9398 1.3311 1.9640 -0.3043 0.2246  0.3404  105 ASP A CG  
725  O OD1 . ASP A 89  ? 0.9986 1.3630 2.0611 -0.3173 0.2109  0.3054  105 ASP A OD1 
726  O OD2 . ASP A 89  ? 0.9416 1.3183 1.9626 -0.3041 0.2352  0.3809  105 ASP A OD2 
727  N N   . HIS A 90  ? 0.9094 1.3154 1.9447 -0.2992 0.1829  0.2161  106 HIS A N   
728  C CA  . HIS A 90  ? 0.9441 1.3094 1.9784 -0.2953 0.1657  0.1799  106 HIS A CA  
729  C C   . HIS A 90  ? 0.9285 1.2288 1.9585 -0.2934 0.1660  0.1959  106 HIS A C   
730  O O   . HIS A 90  ? 0.9341 1.2010 1.9519 -0.2854 0.1544  0.1714  106 HIS A O   
731  C CB  . HIS A 90  ? 1.0405 1.4097 2.1197 -0.3117 0.1501  0.1349  106 HIS A CB  
732  C CG  . HIS A 90  ? 1.1714 1.6041 2.2523 -0.3098 0.1452  0.1115  106 HIS A CG  
733  N ND1 . HIS A 90  ? 1.2552 1.7052 2.3701 -0.3217 0.1300  0.0697  106 HIS A ND1 
734  C CD2 . HIS A 90  ? 1.1371 1.6179 2.1776 -0.2923 0.1509  0.1218  106 HIS A CD2 
735  C CE1 . HIS A 90  ? 1.2378 1.7481 2.3456 -0.3145 0.1278  0.0581  106 HIS A CE1 
736  N NE2 . HIS A 90  ? 1.2136 1.7389 2.2685 -0.2943 0.1395  0.0883  106 HIS A NE2 
737  N N   . ARG A 91  ? 0.9350 1.2194 1.9751 -0.2993 0.1786  0.2363  107 ARG A N   
738  C CA  . ARG A 91  ? 0.9814 1.2101 2.0124 -0.2924 0.1794  0.2571  107 ARG A CA  
739  C C   . ARG A 91  ? 0.9127 1.1451 1.8841 -0.2696 0.1853  0.2795  107 ARG A C   
740  O O   . ARG A 91  ? 0.9024 1.0918 1.8574 -0.2593 0.1797  0.2779  107 ARG A O   
741  C CB  . ARG A 91  ? 1.0272 1.2422 2.0886 -0.3041 0.1902  0.2953  107 ARG A CB  
742  C CG  . ARG A 91  ? 1.1229 1.2781 2.1897 -0.2983 0.1879  0.3115  107 ARG A CG  
743  C CD  . ARG A 91  ? 1.2169 1.3275 2.3314 -0.3092 0.1731  0.2729  107 ARG A CD  
744  N NE  . ARG A 91  ? 1.2513 1.3630 2.4231 -0.3306 0.1755  0.2763  107 ARG A NE  
745  C CZ  . ARG A 91  ? 1.3534 1.4270 2.5756 -0.3416 0.1653  0.2507  107 ARG A CZ  
746  N NH1 . ARG A 91  ? 1.3898 1.4226 2.6121 -0.3325 0.1520  0.2182  107 ARG A NH1 
747  N NH2 . ARG A 91  ? 1.3152 1.3935 2.5900 -0.3617 0.1689  0.2571  107 ARG A NH2 
748  N N   . THR A 92  ? 0.8577 1.1430 1.7967 -0.2605 0.1963  0.2987  108 THR A N   
749  C CA  . THR A 92  ? 0.8267 1.1213 1.7081 -0.2377 0.2008  0.3147  108 THR A CA  
750  C C   . THR A 92  ? 0.7711 1.0472 1.6067 -0.2202 0.1816  0.2682  108 THR A C   
751  O O   . THR A 92  ? 0.8334 1.0805 1.6224 -0.2020 0.1765  0.2686  108 THR A O   
752  C CB  . THR A 92  ? 0.8341 1.1926 1.6863 -0.2288 0.2146  0.3372  108 THR A CB  
753  O OG1 . THR A 92  ? 0.8770 1.2432 1.7395 -0.2360 0.2274  0.3757  108 THR A OG1 
754  C CG2 . THR A 92  ? 0.7539 1.1182 1.5276 -0.1989 0.2127  0.3389  108 THR A CG2 
755  N N   . LEU A 93  ? 0.7656 1.0591 1.6130 -0.2250 0.1700  0.2281  109 LEU A N   
756  C CA  . LEU A 93  ? 0.7524 1.0345 1.5524 -0.2073 0.1518  0.1867  109 LEU A CA  
757  C C   . LEU A 93  ? 0.8280 1.0543 1.6366 -0.2090 0.1404  0.1666  109 LEU A C   
758  O O   . LEU A 93  ? 0.8061 1.0119 1.5636 -0.1902 0.1309  0.1513  109 LEU A O   
759  C CB  . LEU A 93  ? 0.7112 1.0318 1.5238 -0.2116 0.1423  0.1523  109 LEU A CB  
760  C CG  . LEU A 93  ? 0.7257 1.1054 1.5249 -0.2053 0.1515  0.1653  109 LEU A CG  
761  C CD1 . LEU A 93  ? 0.5823 0.9978 1.3872 -0.2046 0.1386  0.1284  109 LEU A CD1 
762  C CD2 . LEU A 93  ? 0.6943 1.0802 1.4251 -0.1790 0.1559  0.1819  109 LEU A CD2 
763  N N   . SER A 94  ? 0.7850 0.9870 1.6605 -0.2313 0.1414  0.1658  110 SER A N   
764  C CA  . SER A 94  ? 0.7632 0.9141 1.6522 -0.2322 0.1305  0.1432  110 SER A CA  
765  C C   . SER A 94  ? 0.7869 0.8995 1.6563 -0.2215 0.1374  0.1757  110 SER A C   
766  O O   . SER A 94  ? 0.7817 0.8624 1.6221 -0.2082 0.1278  0.1577  110 SER A O   
767  C CB  . SER A 94  ? 0.8230 0.9595 1.7953 -0.2590 0.1281  0.1273  110 SER A CB  
768  O OG  . SER A 94  ? 0.9213 1.0508 1.9299 -0.2716 0.1421  0.1685  110 SER A OG  
769  N N   . GLN A 95  ? 0.7959 0.9147 1.6810 -0.2269 0.1539  0.2245  111 GLN A N   
770  C CA  . GLN A 95  ? 0.7994 0.8904 1.6597 -0.2140 0.1602  0.2589  111 GLN A CA  
771  C C   . GLN A 95  ? 0.7646 0.8676 1.5425 -0.1870 0.1559  0.2541  111 GLN A C   
772  O O   . GLN A 95  ? 0.7681 0.8425 1.5182 -0.1731 0.1540  0.2640  111 GLN A O   
773  C CB  . GLN A 95  ? 0.8408 0.9463 1.7188 -0.2204 0.1769  0.3111  111 GLN A CB  
774  C CG  . GLN A 95  ? 0.8760 0.9588 1.8104 -0.2375 0.1760  0.3136  111 GLN A CG  
775  C CD  . GLN A 95  ? 0.9523 1.0632 1.8920 -0.2423 0.1906  0.3584  111 GLN A CD  
776  O OE1 . GLN A 95  ? 0.9183 1.0697 1.8173 -0.2321 0.2011  0.3843  111 GLN A OE1 
777  N NE2 . GLN A 95  ? 0.9948 1.0865 1.9853 -0.2574 0.1914  0.3669  111 GLN A NE2 
778  N N   . PHE A 96  ? 0.7558 0.9008 1.4973 -0.1792 0.1540  0.2392  112 PHE A N   
779  C CA  . PHE A 96  ? 0.7085 0.8625 1.3771 -0.1545 0.1487  0.2312  112 PHE A CA  
780  C C   . PHE A 96  ? 0.7440 0.8663 1.3904 -0.1457 0.1321  0.1922  112 PHE A C   
781  O O   . PHE A 96  ? 0.7406 0.8423 1.3463 -0.1297 0.1285  0.1943  112 PHE A O   
782  C CB  . PHE A 96  ? 0.6589 0.8640 1.3013 -0.1480 0.1504  0.2244  112 PHE A CB  
783  C CG  . PHE A 96  ? 0.6676 0.8812 1.2412 -0.1233 0.1448  0.2156  112 PHE A CG  
784  C CD1 . PHE A 96  ? 0.6543 0.8733 1.1925 -0.1094 0.1529  0.2441  112 PHE A CD1 
785  C CD2 . PHE A 96  ? 0.6289 0.8462 1.1752 -0.1140 0.1309  0.1791  112 PHE A CD2 
786  C CE1 . PHE A 96  ? 0.6150 0.8408 1.0950 -0.0877 0.1468  0.2331  112 PHE A CE1 
787  C CE2 . PHE A 96  ? 0.6100 0.8318 1.0988 -0.0925 0.1256  0.1723  112 PHE A CE2 
788  C CZ  . PHE A 96  ? 0.5601 0.7850 1.0174 -0.0798 0.1334  0.1977  112 PHE A CZ  
789  N N   . THR A 97  ? 0.7271 0.8490 1.4005 -0.1562 0.1219  0.1561  113 THR A N   
790  C CA  . THR A 97  ? 0.7099 0.8066 1.3656 -0.1491 0.1070  0.1193  113 THR A CA  
791  C C   . THR A 97  ? 0.7129 0.7631 1.3844 -0.1489 0.1068  0.1256  113 THR A C   
792  O O   . THR A 97  ? 0.7649 0.7963 1.3978 -0.1340 0.1002  0.1150  113 THR A O   
793  C CB  . THR A 97  ? 0.7114 0.8210 1.4010 -0.1621 0.0967  0.0809  113 THR A CB  
794  O OG1 . THR A 97  ? 0.7088 0.8642 1.3905 -0.1625 0.0977  0.0793  113 THR A OG1 
795  C CG2 . THR A 97  ? 0.7350 0.8317 1.3952 -0.1517 0.0817  0.0431  113 THR A CG2 
796  N N   . ASP A 98  ? 0.7410 0.7723 1.4719 -0.1652 0.1142  0.1439  114 ASP A N   
797  C CA  . ASP A 98  ? 0.7594 0.7458 1.5107 -0.1636 0.1148  0.1547  114 ASP A CA  
798  C C   . ASP A 98  ? 0.7733 0.7542 1.4726 -0.1440 0.1193  0.1841  114 ASP A C   
799  O O   . ASP A 98  ? 0.7980 0.7506 1.4805 -0.1325 0.1132  0.1751  114 ASP A O   
800  C CB  . ASP A 98  ? 0.8233 0.7934 1.6475 -0.1838 0.1244  0.1809  114 ASP A CB  
801  C CG  . ASP A 98  ? 0.8464 0.8052 1.7334 -0.2030 0.1166  0.1444  114 ASP A CG  
802  O OD1 . ASP A 98  ? 0.9309 0.8824 1.8062 -0.1977 0.1030  0.0993  114 ASP A OD1 
803  O OD2 . ASP A 98  ? 0.9606 0.9199 1.9093 -0.2235 0.1238  0.1602  114 ASP A OD2 
804  N N   . ALA A 99  ? 0.7302 0.7418 1.4045 -0.1396 0.1299  0.2176  115 ALA A N   
805  C CA  . ALA A 99  ? 0.7768 0.7896 1.4024 -0.1209 0.1337  0.2441  115 ALA A CA  
806  C C   . ALA A 99  ? 0.7604 0.7753 1.3257 -0.1028 0.1226  0.2154  115 ALA A C   
807  O O   . ALA A 99  ? 0.7824 0.7827 1.3165 -0.0884 0.1206  0.2236  115 ALA A O   
808  C CB  . ALA A 99  ? 0.6999 0.7529 1.3123 -0.1200 0.1473  0.2816  115 ALA A CB  
809  N N   . LEU A 100 ? 0.7423 0.7762 1.2927 -0.1034 0.1151  0.1831  116 LEU A N   
810  C CA  . LEU A 100 ? 0.7474 0.7831 1.2438 -0.0873 0.1051  0.1595  116 LEU A CA  
811  C C   . LEU A 100 ? 0.7726 0.7741 1.2723 -0.0848 0.0956  0.1354  116 LEU A C   
812  O O   . LEU A 100 ? 0.7544 0.7466 1.2149 -0.0706 0.0911  0.1319  116 LEU A O   
813  C CB  . LEU A 100 ? 0.6210 0.6873 1.1028 -0.0876 0.0995  0.1355  116 LEU A CB  
814  C CG  . LEU A 100 ? 0.6318 0.7365 1.0945 -0.0827 0.1072  0.1541  116 LEU A CG  
815  C CD1 . LEU A 100 ? 0.6037 0.7335 1.0468 -0.0782 0.0989  0.1278  116 LEU A CD1 
816  C CD2 . LEU A 100 ? 0.6596 0.7664 1.0795 -0.0662 0.1116  0.1761  116 LEU A CD2 
817  N N   . VAL A 101 ? 0.7838 0.7684 1.3325 -0.0987 0.0926  0.1173  117 VAL A N   
818  C CA  . VAL A 101 ? 0.8229 0.7784 1.3795 -0.0959 0.0842  0.0917  117 VAL A CA  
819  C C   . VAL A 101 ? 0.8303 0.7574 1.3872 -0.0873 0.0884  0.1163  117 VAL A C   
820  O O   . VAL A 101 ? 0.8051 0.7185 1.3371 -0.0755 0.0826  0.1039  117 VAL A O   
821  C CB  . VAL A 101 ? 0.7849 0.7304 1.4004 -0.1127 0.0802  0.0654  117 VAL A CB  
822  C CG1 . VAL A 101 ? 0.8292 0.7503 1.4510 -0.1079 0.0714  0.0338  117 VAL A CG1 
823  C CG2 . VAL A 101 ? 0.7342 0.7138 1.3500 -0.1208 0.0755  0.0425  117 VAL A CG2 
824  N N   . THR A 102 ? 0.8363 0.7570 1.4227 -0.0929 0.0985  0.1532  118 THR A N   
825  C CA  . THR A 102 ? 0.8211 0.7186 1.4085 -0.0835 0.1022  0.1815  118 THR A CA  
826  C C   . THR A 102 ? 0.8242 0.7365 1.3481 -0.0649 0.1011  0.1915  118 THR A C   
827  O O   . THR A 102 ? 0.8493 0.7439 1.3586 -0.0531 0.0968  0.1892  118 THR A O   
828  C CB  . THR A 102 ? 0.8053 0.7006 1.4333 -0.0933 0.1140  0.2245  118 THR A CB  
829  O OG1 . THR A 102 ? 0.8042 0.6802 1.4988 -0.1118 0.1139  0.2127  118 THR A OG1 
830  C CG2 . THR A 102 ? 0.7852 0.6612 1.4115 -0.0814 0.1175  0.2590  118 THR A CG2 
831  N N   . ILE A 103 ? 0.8190 0.7652 1.3072 -0.0618 0.1045  0.2003  119 ILE A N   
832  C CA  . ILE A 103 ? 0.7755 0.7364 1.2068 -0.0447 0.1026  0.2062  119 ILE A CA  
833  C C   . ILE A 103 ? 0.8127 0.7637 1.2157 -0.0369 0.0915  0.1716  119 ILE A C   
834  O O   . ILE A 103 ? 0.7744 0.7172 1.1518 -0.0247 0.0881  0.1740  119 ILE A O   
835  C CB  . ILE A 103 ? 0.7286 0.7282 1.1321 -0.0426 0.1078  0.2164  119 ILE A CB  
836  C CG1 . ILE A 103 ? 0.7413 0.7564 1.1652 -0.0469 0.1205  0.2574  119 ILE A CG1 
837  C CG2 . ILE A 103 ? 0.6911 0.7040 1.0386 -0.0257 0.1028  0.2103  119 ILE A CG2 
838  C CD1 . ILE A 103 ? 0.7448 0.8013 1.1568 -0.0488 0.1275  0.2650  119 ILE A CD1 
839  N N   . ARG A 104 ? 0.7684 0.7228 1.1767 -0.0441 0.0855  0.1400  120 ARG A N   
840  C CA  . ARG A 104 ? 0.7875 0.7368 1.1693 -0.0373 0.0759  0.1100  120 ARG A CA  
841  C C   . ARG A 104 ? 0.8270 0.7483 1.2248 -0.0338 0.0732  0.1034  120 ARG A C   
842  O O   . ARG A 104 ? 0.7983 0.7162 1.1658 -0.0227 0.0692  0.0985  120 ARG A O   
843  C CB  . ARG A 104 ? 0.8356 0.7965 1.2250 -0.0456 0.0699  0.0791  120 ARG A CB  
844  C CG  . ARG A 104 ? 0.8187 0.7799 1.1783 -0.0385 0.0608  0.0517  120 ARG A CG  
845  C CD  . ARG A 104 ? 0.7837 0.7622 1.1490 -0.0456 0.0543  0.0233  120 ARG A CD  
846  N NE  . ARG A 104 ? 0.8210 0.7920 1.2374 -0.0587 0.0545  0.0099  120 ARG A NE  
847  C CZ  . ARG A 104 ? 0.8089 0.7985 1.2472 -0.0692 0.0520  -0.0045 120 ARG A CZ  
848  N NH1 . ARG A 104 ? 0.7661 0.7836 1.1788 -0.0670 0.0491  -0.0064 120 ARG A NH1 
849  N NH2 . ARG A 104 ? 0.8475 0.8275 1.3373 -0.0819 0.0519  -0.0181 120 ARG A NH2 
850  N N   . ASN A 105 ? 0.7856 0.6866 1.2342 -0.0430 0.0752  0.1027  121 ASN A N   
851  C CA  . ASN A 105 ? 0.8669 0.7411 1.3362 -0.0384 0.0720  0.0922  121 ASN A CA  
852  C C   . ASN A 105 ? 0.8548 0.7190 1.3121 -0.0261 0.0752  0.1226  121 ASN A C   
853  O O   . ASN A 105 ? 0.7414 0.5939 1.1917 -0.0163 0.0710  0.1126  121 ASN A O   
854  C CB  . ASN A 105 ? 0.8476 0.7001 1.3804 -0.0508 0.0729  0.0834  121 ASN A CB  
855  C CG  . ASN A 105 ? 0.9071 0.7736 1.4559 -0.0637 0.0688  0.0519  121 ASN A CG  
856  O OD1 . ASN A 105 ? 0.9893 0.8494 1.5866 -0.0777 0.0712  0.0524  121 ASN A OD1 
857  N ND2 . ASN A 105 ? 0.8831 0.7708 1.3931 -0.0593 0.0621  0.0253  121 ASN A ND2 
858  N N   . ARG A 106 ? 0.8287 0.7015 1.2840 -0.0259 0.0826  0.1596  122 ARG A N   
859  C CA  . ARG A 106 ? 0.8107 0.6814 1.2517 -0.0132 0.0851  0.1906  122 ARG A CA  
860  C C   . ARG A 106 ? 0.8185 0.7026 1.2072 0.0003  0.0793  0.1798  122 ARG A C   
861  O O   . ARG A 106 ? 0.7508 0.6267 1.1335 0.0115  0.0767  0.1872  122 ARG A O   
862  C CB  . ARG A 106 ? 0.8161 0.7056 1.2566 -0.0155 0.0944  0.2301  122 ARG A CB  
863  C CG  . ARG A 106 ? 0.7736 0.6725 1.1905 -0.0011 0.0965  0.2628  122 ARG A CG  
864  C CD  . ARG A 106 ? 0.7824 0.7101 1.1918 -0.0023 0.1062  0.2998  122 ARG A CD  
865  N NE  . ARG A 106 ? 0.7754 0.6926 1.2367 -0.0156 0.1149  0.3251  122 ARG A NE  
866  C CZ  . ARG A 106 ? 0.8028 0.7411 1.2746 -0.0274 0.1230  0.3357  122 ARG A CZ  
867  N NH1 . ARG A 106 ? 0.7562 0.7273 1.1900 -0.0260 0.1235  0.3228  122 ARG A NH1 
868  N NH2 . ARG A 106 ? 0.7448 0.6715 1.2695 -0.0409 0.1310  0.3603  122 ARG A NH2 
869  N N   . HIS A 107 ? 0.7932 0.6977 1.1473 -0.0008 0.0766  0.1622  123 HIS A N   
870  C CA  . HIS A 107 ? 0.7540 0.6710 1.0618 0.0099  0.0712  0.1526  123 HIS A CA  
871  C C   . HIS A 107 ? 0.8064 0.7146 1.1083 0.0105  0.0641  0.1200  123 HIS A C   
872  O O   . HIS A 107 ? 0.7658 0.6851 1.0321 0.0161  0.0597  0.1098  123 HIS A O   
873  C CB  . HIS A 107 ? 0.6610 0.6037 0.9368 0.0097  0.0718  0.1527  123 HIS A CB  
874  C CG  . HIS A 107 ? 0.7219 0.6830 0.9936 0.0120  0.0791  0.1831  123 HIS A CG  
875  N ND1 . HIS A 107 ? 0.6897 0.6724 0.9243 0.0229  0.0784  0.1922  123 HIS A ND1 
876  C CD2 . HIS A 107 ? 0.7160 0.6804 1.0169 0.0048  0.0874  0.2064  123 HIS A CD2 
877  C CE1 . HIS A 107 ? 0.7474 0.7496 0.9854 0.0234  0.0863  0.2190  123 HIS A CE1 
878  N NE2 . HIS A 107 ? 0.7058 0.6973 0.9838 0.0121  0.0924  0.2303  123 HIS A NE2 
879  N N   . ASN A 108 ? 0.7595 0.6500 1.0967 0.0050  0.0630  0.1030  124 ASN A N   
880  C CA  . ASN A 108 ? 0.7781 0.6698 1.1082 0.0045  0.0573  0.0694  124 ASN A CA  
881  C C   . ASN A 108 ? 0.7740 0.6657 1.0823 0.0154  0.0540  0.0654  124 ASN A C   
882  O O   . ASN A 108 ? 0.7482 0.6506 1.0347 0.0161  0.0501  0.0445  124 ASN A O   
883  C CB  . ASN A 108 ? 0.7711 0.6478 1.1461 -0.0031 0.0565  0.0481  124 ASN A CB  
884  C CG  . ASN A 108 ? 0.9006 0.7900 1.2823 -0.0147 0.0550  0.0290  124 ASN A CG  
885  O OD1 . ASN A 108 ? 0.8772 0.7873 1.2250 -0.0150 0.0529  0.0252  124 ASN A OD1 
886  N ND2 . ASN A 108 ? 0.9171 0.7946 1.3454 -0.0240 0.0553  0.0166  124 ASN A ND2 
887  N N   . ASP A 109 ? 0.7996 0.6827 1.1139 0.0240  0.0554  0.0867  125 ASP A N   
888  C CA  . ASP A 109 ? 0.7659 0.6497 1.0679 0.0344  0.0521  0.0826  125 ASP A CA  
889  C C   . ASP A 109 ? 0.7201 0.6208 0.9824 0.0413  0.0503  0.0972  125 ASP A C   
890  O O   . ASP A 109 ? 0.7019 0.6045 0.9586 0.0506  0.0480  0.1027  125 ASP A O   
891  C CB  . ASP A 109 ? 0.7430 0.6077 1.0815 0.0413  0.0532  0.0942  125 ASP A CB  
892  C CG  . ASP A 109 ? 0.8025 0.6486 1.1847 0.0360  0.0534  0.0725  125 ASP A CG  
893  O OD1 . ASP A 109 ? 0.8489 0.7027 1.2262 0.0312  0.0511  0.0412  125 ASP A OD1 
894  O OD2 . ASP A 109 ? 0.8820 0.7071 1.3048 0.0371  0.0555  0.0864  125 ASP A OD2 
895  N N   . VAL A 110 ? 0.6365 0.5505 0.8737 0.0375  0.0508  0.1016  126 VAL A N   
896  C CA  . VAL A 110 ? 0.6589 0.5885 0.8640 0.0445  0.0489  0.1146  126 VAL A CA  
897  C C   . VAL A 110 ? 0.6668 0.6025 0.8504 0.0479  0.0434  0.0987  126 VAL A C   
898  O O   . VAL A 110 ? 0.6686 0.6126 0.8388 0.0558  0.0405  0.1066  126 VAL A O   
899  C CB  . VAL A 110 ? 0.6749 0.6177 0.8624 0.0408  0.0507  0.1200  126 VAL A CB  
900  C CG1 . VAL A 110 ? 0.7237 0.6828 0.8780 0.0480  0.0470  0.1229  126 VAL A CG1 
901  C CG2 . VAL A 110 ? 0.7155 0.6595 0.9219 0.0392  0.0572  0.1435  126 VAL A CG2 
902  N N   . VAL A 111 ? 0.6454 0.5803 0.8267 0.0418  0.0420  0.0769  127 VAL A N   
903  C CA  . VAL A 111 ? 0.5974 0.5409 0.7581 0.0428  0.0380  0.0649  127 VAL A CA  
904  C C   . VAL A 111 ? 0.6393 0.5823 0.8103 0.0496  0.0368  0.0639  127 VAL A C   
905  O O   . VAL A 111 ? 0.6270 0.5792 0.7830 0.0544  0.0334  0.0687  127 VAL A O   
906  C CB  . VAL A 111 ? 0.6752 0.6226 0.8309 0.0352  0.0374  0.0454  127 VAL A CB  
907  C CG1 . VAL A 111 ? 0.5960 0.5532 0.7354 0.0353  0.0347  0.0367  127 VAL A CG1 
908  C CG2 . VAL A 111 ? 0.5745 0.5259 0.7170 0.0306  0.0369  0.0479  127 VAL A CG2 
909  N N   . PRO A 112 ? 0.6635 0.5975 0.8622 0.0509  0.0389  0.0564  128 PRO A N   
910  C CA  . PRO A 112 ? 0.6317 0.5674 0.8423 0.0597  0.0375  0.0566  128 PRO A CA  
911  C C   . PRO A 112 ? 0.6129 0.5478 0.8265 0.0691  0.0361  0.0810  128 PRO A C   
912  O O   . PRO A 112 ? 0.6066 0.5497 0.8211 0.0772  0.0330  0.0834  128 PRO A O   
913  C CB  . PRO A 112 ? 0.6061 0.5304 0.8500 0.0598  0.0400  0.0413  128 PRO A CB  
914  C CG  . PRO A 112 ? 0.6353 0.5469 0.8920 0.0528  0.0426  0.0444  128 PRO A CG  
915  C CD  . PRO A 112 ? 0.6646 0.5871 0.8892 0.0456  0.0419  0.0463  128 PRO A CD  
916  N N   . THR A 113 ? 0.6299 0.5592 0.8456 0.0685  0.0384  0.0999  129 THR A N   
917  C CA  . THR A 113 ? 0.6059 0.5416 0.8199 0.0781  0.0372  0.1257  129 THR A CA  
918  C C   . THR A 113 ? 0.6036 0.5610 0.7840 0.0815  0.0323  0.1269  129 THR A C   
919  O O   . THR A 113 ? 0.5226 0.4923 0.6999 0.0908  0.0279  0.1333  129 THR A O   
920  C CB  . THR A 113 ? 0.6255 0.5551 0.8496 0.0757  0.0423  0.1472  129 THR A CB  
921  O OG1 . THR A 113 ? 0.6162 0.5233 0.8787 0.0722  0.0459  0.1458  129 THR A OG1 
922  C CG2 . THR A 113 ? 0.5192 0.4627 0.7369 0.0864  0.0415  0.1767  129 THR A CG2 
923  N N   . MET A 114 ? 0.5555 0.5185 0.7132 0.0744  0.0323  0.1188  130 MET A N   
924  C CA  . MET A 114 ? 0.6325 0.6129 0.7628 0.0768  0.0268  0.1149  130 MET A CA  
925  C C   . MET A 114 ? 0.6239 0.6087 0.7528 0.0763  0.0223  0.0991  130 MET A C   
926  O O   . MET A 114 ? 0.6158 0.6162 0.7330 0.0811  0.0165  0.0988  130 MET A O   
927  C CB  . MET A 114 ? 0.5870 0.5687 0.6991 0.0698  0.0274  0.1076  130 MET A CB  
928  C CG  . MET A 114 ? 0.6488 0.6325 0.7618 0.0700  0.0323  0.1223  130 MET A CG  
929  S SD  . MET A 114 ? 0.7191 0.7271 0.8190 0.0820  0.0311  0.1436  130 MET A SD  
930  C CE  . MET A 114 ? 0.7228 0.7474 0.7936 0.0839  0.0237  0.1262  130 MET A CE  
931  N N   . ALA A 115 ? 0.5805 0.5556 0.7217 0.0704  0.0247  0.0847  131 ALA A N   
932  C CA  . ALA A 115 ? 0.5875 0.5713 0.7295 0.0695  0.0221  0.0715  131 ALA A CA  
933  C C   . ALA A 115 ? 0.5816 0.5741 0.7374 0.0802  0.0192  0.0783  131 ALA A C   
934  O O   . ALA A 115 ? 0.6082 0.6162 0.7595 0.0819  0.0145  0.0733  131 ALA A O   
935  C CB  . ALA A 115 ? 0.5792 0.5572 0.7317 0.0626  0.0264  0.0554  131 ALA A CB  
936  N N   . GLN A 116 ? 0.5382 0.5212 0.7144 0.0875  0.0215  0.0902  132 GLN A N   
937  C CA  . GLN A 116 ? 0.5957 0.5872 0.7865 0.1000  0.0180  0.1005  132 GLN A CA  
938  C C   . GLN A 116 ? 0.5777 0.5898 0.7487 0.1066  0.0117  0.1138  132 GLN A C   
939  O O   . GLN A 116 ? 0.5716 0.6016 0.7454 0.1146  0.0059  0.1144  132 GLN A O   
940  C CB  . GLN A 116 ? 0.5762 0.5497 0.7954 0.1065  0.0216  0.1144  132 GLN A CB  
941  C CG  . GLN A 116 ? 0.6021 0.5833 0.8371 0.1214  0.0175  0.1314  132 GLN A CG  
942  C CD  . GLN A 116 ? 0.6580 0.6489 0.9083 0.1271  0.0146  0.1151  132 GLN A CD  
943  O OE1 . GLN A 116 ? 0.6477 0.6357 0.9028 0.1198  0.0177  0.0917  132 GLN A OE1 
944  N NE2 . GLN A 116 ? 0.5547 0.5614 0.8125 0.1409  0.0086  0.1278  132 GLN A NE2 
945  N N   . GLY A 117 ? 0.5656 0.5793 0.7172 0.1040  0.0124  0.1227  133 GLY A N   
946  C CA  . GLY A 117 ? 0.5586 0.5968 0.6894 0.1106  0.0061  0.1302  133 GLY A CA  
947  C C   . GLY A 117 ? 0.6119 0.6641 0.7296 0.1061  -0.0004 0.1101  133 GLY A C   
948  O O   . GLY A 117 ? 0.5681 0.6436 0.6812 0.1134  -0.0080 0.1101  133 GLY A O   
949  N N   . VAL A 118 ? 0.5485 0.5879 0.6626 0.0939  0.0020  0.0935  134 VAL A N   
950  C CA  . VAL A 118 ? 0.5305 0.5794 0.6380 0.0873  -0.0033 0.0767  134 VAL A CA  
951  C C   . VAL A 118 ? 0.5576 0.6193 0.6819 0.0904  -0.0062 0.0716  134 VAL A C   
952  O O   . VAL A 118 ? 0.5054 0.5872 0.6280 0.0916  -0.0137 0.0651  134 VAL A O   
953  C CB  . VAL A 118 ? 0.5970 0.6292 0.7003 0.0742  0.0009  0.0653  134 VAL A CB  
954  C CG1 . VAL A 118 ? 0.5613 0.6012 0.6629 0.0661  -0.0038 0.0518  134 VAL A CG1 
955  C CG2 . VAL A 118 ? 0.5571 0.5799 0.6454 0.0725  0.0028  0.0694  134 VAL A CG2 
956  N N   . LEU A 119 ? 0.5451 0.5975 0.6884 0.0918  -0.0006 0.0722  135 LEU A N   
957  C CA  . LEU A 119 ? 0.5562 0.6231 0.7185 0.0969  -0.0027 0.0671  135 LEU A CA  
958  C C   . LEU A 119 ? 0.6040 0.6920 0.7688 0.1106  -0.0107 0.0783  135 LEU A C   
959  O O   . LEU A 119 ? 0.5292 0.6399 0.7000 0.1125  -0.0168 0.0708  135 LEU A O   
960  C CB  . LEU A 119 ? 0.6366 0.6899 0.8211 0.0998  0.0043  0.0655  135 LEU A CB  
961  C CG  . LEU A 119 ? 0.8688 0.9197 1.0576 0.0888  0.0105  0.0477  135 LEU A CG  
962  C CD1 . LEU A 119 ? 0.7773 0.8082 0.9782 0.0885  0.0177  0.0440  135 LEU A CD1 
963  C CD2 . LEU A 119 ? 0.8729 0.9468 1.0780 0.0915  0.0092  0.0377  135 LEU A CD2 
964  N N   . GLU A 120 ? 0.5277 0.6118 0.6887 0.1203  -0.0108 0.0975  136 GLU A N   
965  C CA  . GLU A 120 ? 0.6026 0.7112 0.7639 0.1350  -0.0186 0.1117  136 GLU A CA  
966  C C   . GLU A 120 ? 0.5563 0.6918 0.6973 0.1336  -0.0276 0.1025  136 GLU A C   
967  O O   . GLU A 120 ? 0.5679 0.7313 0.7139 0.1413  -0.0363 0.1002  136 GLU A O   
968  C CB  . GLU A 120 ? 0.5358 0.6369 0.6958 0.1442  -0.0156 0.1377  136 GLU A CB  
969  C CG  . GLU A 120 ? 0.5722 0.6502 0.7608 0.1488  -0.0096 0.1473  136 GLU A CG  
970  C CD  . GLU A 120 ? 0.6447 0.7117 0.8367 0.1548  -0.0055 0.1752  136 GLU A CD  
971  O OE1 . GLU A 120 ? 0.6319 0.7166 0.8011 0.1578  -0.0075 0.1895  136 GLU A OE1 
972  O OE2 . GLU A 120 ? 0.6308 0.6725 0.8504 0.1563  -0.0001 0.1819  136 GLU A OE2 
973  N N   . TYR A 121 ? 0.5554 0.6839 0.6762 0.1244  -0.0265 0.0952  137 TYR A N   
974  C CA  . TYR A 121 ? 0.5420 0.6943 0.6465 0.1235  -0.0357 0.0830  137 TYR A CA  
975  C C   . TYR A 121 ? 0.5750 0.7376 0.6917 0.1152  -0.0413 0.0625  137 TYR A C   
976  O O   . TYR A 121 ? 0.5636 0.7559 0.6804 0.1197  -0.0517 0.0545  137 TYR A O   
977  C CB  . TYR A 121 ? 0.5488 0.6884 0.6340 0.1160  -0.0330 0.0773  137 TYR A CB  
978  C CG  . TYR A 121 ? 0.6353 0.7997 0.7060 0.1175  -0.0432 0.0623  137 TYR A CG  
979  C CD1 . TYR A 121 ? 0.6054 0.7680 0.6816 0.1061  -0.0485 0.0395  137 TYR A CD1 
980  C CD2 . TYR A 121 ? 0.6141 0.8064 0.6676 0.1305  -0.0476 0.0706  137 TYR A CD2 
981  C CE1 . TYR A 121 ? 0.6235 0.8077 0.6918 0.1074  -0.0590 0.0220  137 TYR A CE1 
982  C CE2 . TYR A 121 ? 0.5804 0.7994 0.6216 0.1329  -0.0577 0.0521  137 TYR A CE2 
983  C CZ  . TYR A 121 ? 0.6444 0.8572 0.6946 0.1213  -0.0639 0.0260  137 TYR A CZ  
984  O OH  . TYR A 121 ? 0.7190 0.9566 0.7621 0.1234  -0.0749 0.0039  137 TYR A OH  
985  N N   . LYS A 122 ? 0.5729 0.7149 0.7012 0.1029  -0.0345 0.0541  138 LYS A N   
986  C CA  . LYS A 122 ? 0.5992 0.7526 0.7425 0.0935  -0.0376 0.0383  138 LYS A CA  
987  C C   . LYS A 122 ? 0.6067 0.7895 0.7667 0.1041  -0.0439 0.0394  138 LYS A C   
988  O O   . LYS A 122 ? 0.5552 0.7619 0.7236 0.1003  -0.0520 0.0265  138 LYS A O   
989  C CB  . LYS A 122 ? 0.5773 0.7098 0.7300 0.0816  -0.0272 0.0344  138 LYS A CB  
990  C CG  . LYS A 122 ? 0.7456 0.8951 0.9184 0.0733  -0.0274 0.0231  138 LYS A CG  
991  C CD  . LYS A 122 ? 0.8357 0.9719 1.0155 0.0633  -0.0160 0.0205  138 LYS A CD  
992  C CE  . LYS A 122 ? 0.7776 0.8905 0.9416 0.0507  -0.0120 0.0201  138 LYS A CE  
993  N NZ  . LYS A 122 ? 0.8555 0.9626 1.0237 0.0416  -0.0017 0.0182  138 LYS A NZ  
994  N N   . ASP A 123 ? 0.5600 0.7419 0.7285 0.1177  -0.0410 0.0546  139 ASP A N   
995  C CA  . ASP A 123 ? 0.5607 0.7708 0.7474 0.1302  -0.0476 0.0574  139 ASP A CA  
996  C C   . ASP A 123 ? 0.5111 0.7485 0.6866 0.1458  -0.0583 0.0691  139 ASP A C   
997  O O   . ASP A 123 ? 0.4938 0.7643 0.6806 0.1542  -0.0677 0.0662  139 ASP A O   
998  C CB  . ASP A 123 ? 0.6001 0.7962 0.8077 0.1385  -0.0399 0.0666  139 ASP A CB  
999  C CG  . ASP A 123 ? 0.6214 0.8010 0.8399 0.1249  -0.0298 0.0523  139 ASP A CG  
1000 O OD1 . ASP A 123 ? 0.6565 0.8447 0.8730 0.1106  -0.0302 0.0377  139 ASP A OD1 
1001 O OD2 . ASP A 123 ? 0.6484 0.8082 0.8784 0.1282  -0.0217 0.0556  139 ASP A OD2 
1002 N N   . THR A 124 ? 0.4961 0.7259 0.6499 0.1503  -0.0573 0.0824  140 THR A N   
1003 C CA  . THR A 124 ? 0.5414 0.8051 0.6826 0.1658  -0.0673 0.0941  140 THR A CA  
1004 C C   . THR A 124 ? 0.5380 0.8268 0.6608 0.1609  -0.0770 0.0746  140 THR A C   
1005 O O   . THR A 124 ? 0.5478 0.8767 0.6641 0.1730  -0.0884 0.0754  140 THR A O   
1006 C CB  . THR A 124 ? 0.5259 0.7781 0.6557 0.1762  -0.0613 0.1226  140 THR A CB  
1007 O OG1 . THR A 124 ? 0.6148 0.8386 0.7298 0.1643  -0.0526 0.1195  140 THR A OG1 
1008 C CG2 . THR A 124 ? 0.5472 0.7794 0.7026 0.1843  -0.0551 0.1414  140 THR A CG2 
1009 N N   . TYR A 125 ? 0.5411 0.8090 0.6577 0.1443  -0.0737 0.0561  141 TYR A N   
1010 C CA  . TYR A 125 ? 0.5782 0.8645 0.6832 0.1389  -0.0832 0.0337  141 TYR A CA  
1011 C C   . TYR A 125 ? 0.6305 0.9008 0.7500 0.1192  -0.0834 0.0097  141 TYR A C   
1012 O O   . TYR A 125 ? 0.6605 0.9486 0.7805 0.1146  -0.0937 -0.0118 141 TYR A O   
1013 C CB  . TYR A 125 ? 0.5218 0.8029 0.6001 0.1422  -0.0805 0.0382  141 TYR A CB  
1014 C CG  . TYR A 125 ? 0.5835 0.8941 0.6468 0.1618  -0.0827 0.0616  141 TYR A CG  
1015 C CD1 . TYR A 125 ? 0.5740 0.9330 0.6308 0.1740  -0.0960 0.0562  141 TYR A CD1 
1016 C CD2 . TYR A 125 ? 0.5524 0.8443 0.6107 0.1677  -0.0718 0.0903  141 TYR A CD2 
1017 C CE1 . TYR A 125 ? 0.6081 0.9988 0.6504 0.1928  -0.0981 0.0817  141 TYR A CE1 
1018 C CE2 . TYR A 125 ? 0.6064 0.9255 0.6538 0.1847  -0.0731 0.1165  141 TYR A CE2 
1019 C CZ  . TYR A 125 ? 0.5979 0.9673 0.6357 0.1979  -0.0860 0.1136  141 TYR A CZ  
1020 O OH  . TYR A 125 ? 0.7350 1.1364 0.7607 0.2159  -0.0875 0.1432  141 TYR A OH  
1021 N N   . GLY A 126 ? 0.6136 0.8540 0.7468 0.1077  -0.0731 0.0122  142 GLY A N   
1022 C CA  . GLY A 126 ? 0.6349 0.8662 0.7849 0.0895  -0.0727 -0.0051 142 GLY A CA  
1023 C C   . GLY A 126 ? 0.6581 0.8536 0.7994 0.0766  -0.0652 -0.0075 142 GLY A C   
1024 O O   . GLY A 126 ? 0.7317 0.9113 0.8536 0.0816  -0.0612 0.0008  142 GLY A O   
1025 N N   . ASP A 127 ? 0.7250 0.9100 0.8822 0.0597  -0.0634 -0.0175 143 ASP A N   
1026 C CA  . ASP A 127 ? 0.8253 0.9777 0.9771 0.0473  -0.0570 -0.0179 143 ASP A CA  
1027 C C   . ASP A 127 ? 0.8529 1.0046 1.0172 0.0346  -0.0654 -0.0358 143 ASP A C   
1028 O O   . ASP A 127 ? 1.0093 1.1527 1.1921 0.0189  -0.0624 -0.0377 143 ASP A O   
1029 C CB  . ASP A 127 ? 0.8531 0.9892 1.0126 0.0385  -0.0443 -0.0078 143 ASP A CB  
1030 C CG  . ASP A 127 ? 0.9476 1.1042 1.1316 0.0308  -0.0436 -0.0119 143 ASP A CG  
1031 O OD1 . ASP A 127 ? 1.0421 1.2252 1.2391 0.0327  -0.0532 -0.0217 143 ASP A OD1 
1032 O OD2 . ASP A 127 ? 1.0259 1.1761 1.2166 0.0231  -0.0333 -0.0062 143 ASP A OD2 
1033 N N   . ASP A 128 ? 0.7918 0.9528 0.9475 0.0414  -0.0757 -0.0487 144 ASP A N   
1034 C CA  . ASP A 128 ? 0.8842 1.0395 1.0541 0.0305  -0.0845 -0.0688 144 ASP A CA  
1035 C C   . ASP A 128 ? 0.9714 1.0920 1.1310 0.0270  -0.0803 -0.0671 144 ASP A C   
1036 O O   . ASP A 128 ? 0.8974 1.0073 1.0344 0.0362  -0.0732 -0.0545 144 ASP A O   
1037 C CB  . ASP A 128 ? 0.8474 1.0347 1.0152 0.0407  -0.0991 -0.0891 144 ASP A CB  
1038 C CG  . ASP A 128 ? 0.9064 1.1009 1.0433 0.0587  -0.0994 -0.0855 144 ASP A CG  
1039 O OD1 . ASP A 128 ? 0.9129 1.1194 1.0345 0.0709  -0.0940 -0.0666 144 ASP A OD1 
1040 O OD2 . ASP A 128 ? 0.9490 1.1378 1.0794 0.0607  -0.1046 -0.1010 144 ASP A OD2 
1041 N N   . PRO A 129 ? 0.9682 1.3094 1.0387 -0.0248 -0.1445 0.0046  145 PRO A N   
1042 C CA  . PRO A 129 ? 0.9534 1.2512 1.0020 -0.0281 -0.1301 -0.0086 145 PRO A CA  
1043 C C   . PRO A 129 ? 0.9752 1.2592 0.9881 -0.0262 -0.1296 -0.0098 145 PRO A C   
1044 O O   . PRO A 129 ? 0.9813 1.2321 0.9830 -0.0206 -0.1166 -0.0119 145 PRO A O   
1045 C CB  . PRO A 129 ? 0.9448 1.2398 0.9948 -0.0478 -0.1299 -0.0293 145 PRO A CB  
1046 C CG  . PRO A 129 ? 0.9674 1.2953 1.0530 -0.0505 -0.1364 -0.0238 145 PRO A CG  
1047 C CD  . PRO A 129 ? 0.9264 1.2913 1.0192 -0.0396 -0.1505 -0.0055 145 PRO A CD  
1048 N N   . VAL A 130 ? 0.8130 1.1228 0.8079 -0.0307 -0.1431 -0.0080 146 VAL A N   
1049 C CA  . VAL A 130 ? 0.8672 1.1651 0.8266 -0.0290 -0.1407 -0.0087 146 VAL A CA  
1050 C C   . VAL A 130 ? 0.8778 1.1678 0.8382 -0.0109 -0.1353 0.0131  146 VAL A C   
1051 O O   . VAL A 130 ? 0.8629 1.1262 0.8070 -0.0064 -0.1234 0.0123  146 VAL A O   
1052 C CB  . VAL A 130 ? 0.9442 1.2720 0.8797 -0.0399 -0.1567 -0.0133 146 VAL A CB  
1053 C CG1 . VAL A 130 ? 0.8568 1.1763 0.7547 -0.0357 -0.1534 -0.0097 146 VAL A CG1 
1054 C CG2 . VAL A 130 ? 0.9177 1.2439 0.8470 -0.0600 -0.1593 -0.0390 146 VAL A CG2 
1055 N N   . SER A 131 ? 0.8204 1.1338 0.8014 -0.0003 -0.1437 0.0331  147 SER A N   
1056 C CA  . SER A 131 ? 0.8215 1.1220 0.8082 0.0168  -0.1370 0.0535  147 SER A CA  
1057 C C   . SER A 131 ? 0.7096 0.9734 0.7080 0.0217  -0.1200 0.0486  147 SER A C   
1058 O O   . SER A 131 ? 0.6749 0.9158 0.6630 0.0285  -0.1105 0.0548  147 SER A O   
1059 C CB  . SER A 131 ? 0.7633 1.0916 0.7767 0.0285  -0.1473 0.0741  147 SER A CB  
1060 O OG  . SER A 131 ? 0.8395 1.2052 0.8428 0.0241  -0.1653 0.0797  147 SER A OG  
1061 N N   . ASN A 132 ? 0.6960 0.9550 0.7156 0.0174  -0.1164 0.0380  148 ASN A N   
1062 C CA  . ASN A 132 ? 0.6978 0.9239 0.7265 0.0215  -0.1018 0.0336  148 ASN A CA  
1063 C C   . ASN A 132 ? 0.6377 0.8359 0.6424 0.0165  -0.0925 0.0214  148 ASN A C   
1064 O O   . ASN A 132 ? 0.5629 0.7368 0.5672 0.0237  -0.0826 0.0252  148 ASN A O   
1065 C CB  . ASN A 132 ? 0.6265 0.8543 0.6777 0.0158  -0.0995 0.0239  148 ASN A CB  
1066 C CG  . ASN A 132 ? 0.8088 1.0017 0.8624 0.0174  -0.0852 0.0168  148 ASN A CG  
1067 O OD1 . ASN A 132 ? 0.8014 0.9815 0.8669 0.0286  -0.0784 0.0258  148 ASN A OD1 
1068 N ND2 . ASN A 132 ? 0.8495 1.0258 0.8908 0.0064  -0.0808 0.0003  148 ASN A ND2 
1069 N N   . GLN A 133 ? 0.6596 0.8612 0.6452 0.0041  -0.0955 0.0062  149 GLN A N   
1070 C CA  . GLN A 133 ? 0.7388 0.9151 0.7037 0.0007  -0.0858 -0.0060 149 GLN A CA  
1071 C C   . GLN A 133 ? 0.6781 0.8507 0.6267 0.0085  -0.0821 0.0050  149 GLN A C   
1072 O O   . GLN A 133 ? 0.6626 0.8125 0.6064 0.0118  -0.0711 0.0023  149 GLN A O   
1073 C CB  . GLN A 133 ? 0.7963 0.9766 0.7432 -0.0137 -0.0894 -0.0252 149 GLN A CB  
1074 C CG  . GLN A 133 ? 0.9037 1.0750 0.8641 -0.0236 -0.0879 -0.0397 149 GLN A CG  
1075 C CD  . GLN A 133 ? 1.1156 1.2873 1.0574 -0.0392 -0.0911 -0.0599 149 GLN A CD  
1076 O OE1 . GLN A 133 ? 1.0457 1.2428 0.9753 -0.0465 -0.1025 -0.0621 149 GLN A OE1 
1077 N NE2 . GLN A 133 ? 1.1281 1.2706 1.0669 -0.0443 -0.0813 -0.0749 149 GLN A NE2 
1078 N N   . ASN A 134 ? 0.6612 0.8572 0.6017 0.0112  -0.0911 0.0183  150 ASN A N   
1079 C CA  . ASN A 134 ? 0.6446 0.8368 0.5694 0.0178  -0.0864 0.0309  150 ASN A CA  
1080 C C   . ASN A 134 ? 0.5892 0.7656 0.5332 0.0295  -0.0796 0.0463  150 ASN A C   
1081 O O   . ASN A 134 ? 0.6191 0.7790 0.5566 0.0326  -0.0697 0.0498  150 ASN A O   
1082 C CB  . ASN A 134 ? 0.6630 0.8838 0.5709 0.0174  -0.0984 0.0425  150 ASN A CB  
1083 C CG  . ASN A 134 ? 0.7641 0.9943 0.6414 0.0053  -0.1015 0.0261  150 ASN A CG  
1084 O OD1 . ASN A 134 ? 0.7833 1.0027 0.6376 0.0040  -0.0922 0.0213  150 ASN A OD1 
1085 N ND2 . ASN A 134 ? 0.7849 1.0355 0.6628 -0.0041 -0.1140 0.0164  150 ASN A ND2 
1086 N N   . ILE A 135 ? 0.5782 0.7595 0.5469 0.0355  -0.0839 0.0547  151 ILE A N   
1087 C CA  . ILE A 135 ? 0.5507 0.7132 0.5372 0.0458  -0.0767 0.0660  151 ILE A CA  
1088 C C   . ILE A 135 ? 0.5480 0.6826 0.5375 0.0435  -0.0654 0.0532  151 ILE A C   
1089 O O   . ILE A 135 ? 0.4974 0.6143 0.4872 0.0476  -0.0576 0.0587  151 ILE A O   
1090 C CB  . ILE A 135 ? 0.5244 0.6980 0.5369 0.0531  -0.0821 0.0746  151 ILE A CB  
1091 C CG1 . ILE A 135 ? 0.6069 0.8087 0.6176 0.0582  -0.0940 0.0916  151 ILE A CG1 
1092 C CG2 . ILE A 135 ? 0.4907 0.6401 0.5202 0.0628  -0.0731 0.0819  151 ILE A CG2 
1093 C CD1 . ILE A 135 ? 0.5121 0.7347 0.5503 0.0654  -0.1018 0.0999  151 ILE A CD1 
1094 N N   . GLN A 136 ? 0.5483 0.6792 0.5406 0.0365  -0.0647 0.0366  152 GLN A N   
1095 C CA  . GLN A 136 ? 0.5637 0.6692 0.5576 0.0349  -0.0554 0.0255  152 GLN A CA  
1096 C C   . GLN A 136 ? 0.5715 0.6676 0.5491 0.0337  -0.0490 0.0226  152 GLN A C   
1097 O O   . GLN A 136 ? 0.5426 0.6214 0.5252 0.0371  -0.0418 0.0241  152 GLN A O   
1098 C CB  . GLN A 136 ? 0.5554 0.6579 0.5505 0.0266  -0.0557 0.0091  152 GLN A CB  
1099 C CG  . GLN A 136 ? 0.6399 0.7481 0.6541 0.0266  -0.0583 0.0096  152 GLN A CG  
1100 C CD  . GLN A 136 ? 0.5810 0.6737 0.6096 0.0354  -0.0525 0.0170  152 GLN A CD  
1101 O OE1 . GLN A 136 ? 0.5634 0.6654 0.6052 0.0426  -0.0546 0.0283  152 GLN A OE1 
1102 N NE2 . GLN A 136 ? 0.5514 0.6201 0.5770 0.0353  -0.0453 0.0106  152 GLN A NE2 
1103 N N   . TYR A 137 ? 0.5588 0.6671 0.5173 0.0280  -0.0511 0.0167  153 TYR A N   
1104 C CA  . TYR A 137 ? 0.5983 0.6996 0.5413 0.0270  -0.0430 0.0122  153 TYR A CA  
1105 C C   . TYR A 137 ? 0.5829 0.6832 0.5272 0.0331  -0.0387 0.0289  153 TYR A C   
1106 O O   . TYR A 137 ? 0.5416 0.6287 0.4899 0.0349  -0.0300 0.0283  153 TYR A O   
1107 C CB  . TYR A 137 ? 0.6158 0.7313 0.5349 0.0198  -0.0458 0.0026  153 TYR A CB  
1108 C CG  . TYR A 137 ? 0.7403 0.8507 0.6420 0.0193  -0.0355 -0.0031 153 TYR A CG  
1109 C CD1 . TYR A 137 ? 0.7428 0.8360 0.6455 0.0184  -0.0267 -0.0186 153 TYR A CD1 
1110 C CD2 . TYR A 137 ? 0.6917 0.8148 0.5768 0.0205  -0.0337 0.0079  153 TYR A CD2 
1111 C CE1 . TYR A 137 ? 0.8273 0.9178 0.7175 0.0193  -0.0159 -0.0240 153 TYR A CE1 
1112 C CE2 . TYR A 137 ? 0.7832 0.9034 0.6534 0.0201  -0.0221 0.0025  153 TYR A CE2 
1113 C CZ  . TYR A 137 ? 0.8473 0.9519 0.7213 0.0198  -0.0131 -0.0141 153 TYR A CZ  
1114 O OH  . TYR A 137 ? 0.8588 0.9622 0.7216 0.0209  -0.0003 -0.0196 153 TYR A OH  
1115 N N   . PHE A 138 ? 0.5779 0.6920 0.5213 0.0364  -0.0450 0.0448  154 PHE A N   
1116 C CA  . PHE A 138 ? 0.5690 0.6803 0.5117 0.0412  -0.0404 0.0620  154 PHE A CA  
1117 C C   . PHE A 138 ? 0.5452 0.6364 0.5099 0.0460  -0.0357 0.0673  154 PHE A C   
1118 O O   . PHE A 138 ? 0.5425 0.6229 0.5094 0.0459  -0.0274 0.0709  154 PHE A O   
1119 C CB  . PHE A 138 ? 0.5623 0.6914 0.4982 0.0447  -0.0489 0.0797  154 PHE A CB  
1120 C CG  . PHE A 138 ? 0.5927 0.7137 0.5323 0.0504  -0.0440 0.0999  154 PHE A CG  
1121 C CD1 . PHE A 138 ? 0.6217 0.7417 0.5458 0.0476  -0.0352 0.1053  154 PHE A CD1 
1122 C CD2 . PHE A 138 ? 0.5440 0.6566 0.5036 0.0581  -0.0465 0.1130  154 PHE A CD2 
1123 C CE1 . PHE A 138 ? 0.5784 0.6889 0.5070 0.0511  -0.0297 0.1244  154 PHE A CE1 
1124 C CE2 . PHE A 138 ? 0.5565 0.6569 0.5199 0.0625  -0.0411 0.1309  154 PHE A CE2 
1125 C CZ  . PHE A 138 ? 0.5861 0.6854 0.5341 0.0582  -0.0329 0.1371  154 PHE A CZ  
1126 N N   . LEU A 139 ? 0.5353 0.6223 0.5165 0.0496  -0.0405 0.0676  155 LEU A N   
1127 C CA  . LEU A 139 ? 0.5235 0.5906 0.5224 0.0541  -0.0362 0.0722  155 LEU A CA  
1128 C C   . LEU A 139 ? 0.4793 0.5301 0.4823 0.0505  -0.0300 0.0588  155 LEU A C   
1129 O O   . LEU A 139 ? 0.4714 0.5080 0.4821 0.0511  -0.0250 0.0626  155 LEU A O   
1130 C CB  . LEU A 139 ? 0.5603 0.6278 0.5746 0.0597  -0.0412 0.0750  155 LEU A CB  
1131 C CG  . LEU A 139 ? 0.5461 0.6233 0.5648 0.0675  -0.0458 0.0940  155 LEU A CG  
1132 C CD1 . LEU A 139 ? 0.5081 0.5852 0.5465 0.0749  -0.0484 0.0961  155 LEU A CD1 
1133 C CD2 . LEU A 139 ? 0.5247 0.5865 0.5431 0.0703  -0.0396 0.1082  155 LEU A CD2 
1134 N N   . ASP A 140 ? 0.4929 0.5454 0.4911 0.0465  -0.0307 0.0437  156 ASP A N   
1135 C CA  . ASP A 140 ? 0.5141 0.5527 0.5151 0.0444  -0.0254 0.0330  156 ASP A CA  
1136 C C   . ASP A 140 ? 0.5360 0.5752 0.5337 0.0433  -0.0188 0.0367  156 ASP A C   
1137 O O   . ASP A 140 ? 0.4836 0.5121 0.4917 0.0434  -0.0151 0.0367  156 ASP A O   
1138 C CB  . ASP A 140 ? 0.5089 0.5482 0.5031 0.0406  -0.0262 0.0177  156 ASP A CB  
1139 C CG  . ASP A 140 ? 0.5221 0.5556 0.5241 0.0404  -0.0300 0.0126  156 ASP A CG  
1140 O OD1 . ASP A 140 ? 0.4923 0.5222 0.5047 0.0440  -0.0315 0.0197  156 ASP A OD1 
1141 O OD2 . ASP A 140 ? 0.5369 0.5689 0.5343 0.0363  -0.0305 0.0013  156 ASP A OD2 
1142 N N   . ARG A 141 ? 0.5399 0.5934 0.5231 0.0416  -0.0171 0.0397  157 ARG A N   
1143 C CA  . ARG A 141 ? 0.5927 0.6491 0.5728 0.0403  -0.0086 0.0432  157 ARG A CA  
1144 C C   . ARG A 141 ? 0.5144 0.5663 0.5033 0.0412  -0.0064 0.0599  157 ARG A C   
1145 O O   . ARG A 141 ? 0.5275 0.5738 0.5270 0.0394  -0.0002 0.0617  157 ARG A O   
1146 C CB  . ARG A 141 ? 0.5301 0.6023 0.4883 0.0379  -0.0060 0.0409  157 ARG A CB  
1147 C CG  . ARG A 141 ? 0.6173 0.6892 0.5671 0.0359  -0.0054 0.0218  157 ARG A CG  
1148 C CD  . ARG A 141 ? 0.6195 0.7062 0.5439 0.0323  -0.0064 0.0174  157 ARG A CD  
1149 N NE  . ARG A 141 ? 0.6239 0.7197 0.5352 0.0318  0.0032  0.0226  157 ARG A NE  
1150 C CZ  . ARG A 141 ? 0.7457 0.8399 0.6552 0.0321  0.0146  0.0126  157 ARG A CZ  
1151 N NH1 . ARG A 141 ? 0.7244 0.8070 0.6446 0.0338  0.0168  -0.0022 157 ARG A NH1 
1152 N NH2 . ARG A 141 ? 0.7039 0.8087 0.6013 0.0313  0.0247  0.0185  157 ARG A NH2 
1153 N N   . PHE A 142 ? 0.5551 0.6092 0.5416 0.0440  -0.0116 0.0725  158 PHE A N   
1154 C CA  . PHE A 142 ? 0.5112 0.5569 0.5056 0.0453  -0.0090 0.0893  158 PHE A CA  
1155 C C   . PHE A 142 ? 0.5473 0.5731 0.5614 0.0450  -0.0078 0.0862  158 PHE A C   
1156 O O   . PHE A 142 ? 0.5305 0.5476 0.5532 0.0419  -0.0022 0.0931  158 PHE A O   
1157 C CB  . PHE A 142 ? 0.5397 0.5905 0.5299 0.0507  -0.0157 0.1035  158 PHE A CB  
1158 C CG  . PHE A 142 ? 0.5712 0.6075 0.5716 0.0535  -0.0129 0.1207  158 PHE A CG  
1159 C CD1 . PHE A 142 ? 0.5594 0.5974 0.5518 0.0512  -0.0068 0.1360  158 PHE A CD1 
1160 C CD2 . PHE A 142 ? 0.5424 0.5608 0.5596 0.0579  -0.0149 0.1209  158 PHE A CD2 
1161 C CE1 . PHE A 142 ? 0.6206 0.6413 0.6227 0.0530  -0.0034 0.1524  158 PHE A CE1 
1162 C CE2 . PHE A 142 ? 0.5898 0.5906 0.6163 0.0602  -0.0113 0.1351  158 PHE A CE2 
1163 C CZ  . PHE A 142 ? 0.6145 0.6155 0.6342 0.0575  -0.0058 0.1514  158 PHE A CZ  
1164 N N   . TYR A 143 ? 0.5330 0.5515 0.5535 0.0473  -0.0129 0.0757  159 TYR A N   
1165 C CA  . TYR A 143 ? 0.4847 0.4842 0.5196 0.0468  -0.0124 0.0718  159 TYR A CA  
1166 C C   . TYR A 143 ? 0.4951 0.4929 0.5353 0.0416  -0.0093 0.0621  159 TYR A C   
1167 O O   . TYR A 143 ? 0.5354 0.5216 0.5868 0.0383  -0.0076 0.0629  159 TYR A O   
1168 C CB  . TYR A 143 ? 0.4473 0.4406 0.4852 0.0508  -0.0175 0.0641  159 TYR A CB  
1169 C CG  . TYR A 143 ? 0.5140 0.5049 0.5558 0.0573  -0.0197 0.0747  159 TYR A CG  
1170 C CD1 . TYR A 143 ? 0.5625 0.5432 0.6095 0.0593  -0.0167 0.0888  159 TYR A CD1 
1171 C CD2 . TYR A 143 ? 0.4695 0.4684 0.5119 0.0617  -0.0242 0.0714  159 TYR A CD2 
1172 C CE1 . TYR A 143 ? 0.5352 0.5129 0.5876 0.0674  -0.0183 0.0999  159 TYR A CE1 
1173 C CE2 . TYR A 143 ? 0.5080 0.5078 0.5580 0.0695  -0.0260 0.0821  159 TYR A CE2 
1174 C CZ  . TYR A 143 ? 0.5387 0.5273 0.5934 0.0732  -0.0231 0.0965  159 TYR A CZ  
1175 O OH  . TYR A 143 ? 0.5612 0.5493 0.6251 0.0829  -0.0245 0.1082  159 TYR A OH  
1176 N N   . LEU A 144 ? 0.5018 0.5107 0.5353 0.0411  -0.0087 0.0523  160 LEU A N   
1177 C CA  . LEU A 144 ? 0.5198 0.5297 0.5611 0.0382  -0.0056 0.0448  160 LEU A CA  
1178 C C   . LEU A 144 ? 0.5017 0.5185 0.5493 0.0340  0.0016  0.0537  160 LEU A C   
1179 O O   . LEU A 144 ? 0.5062 0.5201 0.5686 0.0302  0.0030  0.0528  160 LEU A O   
1180 C CB  . LEU A 144 ? 0.4786 0.4973 0.5115 0.0399  -0.0047 0.0334  160 LEU A CB  
1181 C CG  . LEU A 144 ? 0.5746 0.5839 0.6093 0.0419  -0.0094 0.0219  160 LEU A CG  
1182 C CD1 . LEU A 144 ? 0.5497 0.5651 0.5741 0.0433  -0.0073 0.0121  160 LEU A CD1 
1183 C CD2 . LEU A 144 ? 0.4793 0.4823 0.5286 0.0410  -0.0104 0.0195  160 LEU A CD2 
1184 N N   . SER A 145 ? 0.5078 0.5350 0.5440 0.0339  0.0061  0.0629  161 SER A N   
1185 C CA  . SER A 145 ? 0.5586 0.5911 0.5993 0.0292  0.0143  0.0745  161 SER A CA  
1186 C C   . SER A 145 ? 0.5707 0.5867 0.6262 0.0255  0.0134  0.0830  161 SER A C   
1187 O O   . SER A 145 ? 0.5475 0.5635 0.6182 0.0191  0.0179  0.0845  161 SER A O   
1188 C CB  . SER A 145 ? 0.5134 0.5565 0.5346 0.0304  0.0176  0.0856  161 SER A CB  
1189 O OG  . SER A 145 ? 0.5814 0.6255 0.6054 0.0258  0.0256  0.1009  161 SER A OG  
1190 N N   . ARG A 146 ? 0.5354 0.5373 0.5883 0.0292  0.0077  0.0875  162 ARG A N   
1191 C CA  . ARG A 146 ? 0.5260 0.5078 0.5910 0.0262  0.0077  0.0944  162 ARG A CA  
1192 C C   . ARG A 146 ? 0.5331 0.5056 0.6126 0.0214  0.0048  0.0821  162 ARG A C   
1193 O O   . ARG A 146 ? 0.5063 0.4696 0.5987 0.0138  0.0074  0.0854  162 ARG A O   
1194 C CB  . ARG A 146 ? 0.5623 0.5312 0.6227 0.0336  0.0030  0.0999  162 ARG A CB  
1195 C CG  . ARG A 146 ? 0.5529 0.4964 0.6251 0.0317  0.0037  0.1035  162 ARG A CG  
1196 C CD  . ARG A 146 ? 0.7000 0.6316 0.7700 0.0411  0.0008  0.1090  162 ARG A CD  
1197 N NE  . ARG A 146 ? 0.8018 0.7101 0.8804 0.0411  -0.0003 0.1000  162 ARG A NE  
1198 C CZ  . ARG A 146 ? 0.7896 0.6735 0.8762 0.0393  0.0034  0.1060  162 ARG A CZ  
1199 N NH1 . ARG A 146 ? 0.7766 0.6551 0.8651 0.0377  0.0086  0.1231  162 ARG A NH1 
1200 N NH2 . ARG A 146 ? 0.8593 0.7219 0.9505 0.0387  0.0026  0.0946  162 ARG A NH2 
1201 N N   . ILE A 147 ? 0.5075 0.4824 0.5844 0.0248  -0.0009 0.0683  163 ILE A N   
1202 C CA  . ILE A 147 ? 0.4969 0.4657 0.5843 0.0209  -0.0053 0.0572  163 ILE A CA  
1203 C C   . ILE A 147 ? 0.5063 0.4894 0.6075 0.0141  -0.0017 0.0570  163 ILE A C   
1204 O O   . ILE A 147 ? 0.4905 0.4684 0.6058 0.0067  -0.0038 0.0547  163 ILE A O   
1205 C CB  . ILE A 147 ? 0.5330 0.5030 0.6124 0.0266  -0.0111 0.0451  163 ILE A CB  
1206 C CG1 . ILE A 147 ? 0.5203 0.4759 0.5913 0.0317  -0.0143 0.0441  163 ILE A CG1 
1207 C CG2 . ILE A 147 ? 0.4752 0.4453 0.5638 0.0232  -0.0160 0.0352  163 ILE A CG2 
1208 C CD1 . ILE A 147 ? 0.5510 0.5105 0.6125 0.0368  -0.0179 0.0350  163 ILE A CD1 
1209 N N   . SER A 148 ? 0.5167 0.5193 0.6147 0.0162  0.0041  0.0586  164 SER A N   
1210 C CA  . SER A 148 ? 0.4994 0.5193 0.6130 0.0113  0.0094  0.0583  164 SER A CA  
1211 C C   . SER A 148 ? 0.5384 0.5572 0.6641 0.0017  0.0158  0.0701  164 SER A C   
1212 O O   . SER A 148 ? 0.5300 0.5572 0.6763 -0.0061 0.0169  0.0689  164 SER A O   
1213 C CB  . SER A 148 ? 0.4802 0.5192 0.5851 0.0165  0.0167  0.0568  164 SER A CB  
1214 O OG  . SER A 148 ? 0.5331 0.5772 0.6271 0.0151  0.0251  0.0686  164 SER A OG  
1215 N N   . ILE A 149 ? 0.5151 0.5245 0.6294 0.0018  0.0201  0.0824  165 ILE A N   
1216 C CA  . ILE A 149 ? 0.5303 0.5346 0.6545 -0.0076 0.0273  0.0957  165 ILE A CA  
1217 C C   . ILE A 149 ? 0.5520 0.5347 0.6900 -0.0150 0.0215  0.0927  165 ILE A C   
1218 O O   . ILE A 149 ? 0.5851 0.5684 0.7415 -0.0267 0.0250  0.0958  165 ILE A O   
1219 C CB  . ILE A 149 ? 0.5458 0.5441 0.6521 -0.0038 0.0325  0.1115  165 ILE A CB  
1220 C CG1 . ILE A 149 ? 0.5291 0.5513 0.6214 -0.0004 0.0401  0.1148  165 ILE A CG1 
1221 C CG2 . ILE A 149 ? 0.5112 0.4955 0.6270 -0.0130 0.0390  0.1265  165 ILE A CG2 
1222 C CD1 . ILE A 149 ? 0.5208 0.5416 0.5893 0.0055  0.0414  0.1282  165 ILE A CD1 
1223 N N   . ARG A 150 ? 0.5877 0.5516 0.7173 -0.0094 0.0131  0.0855  166 ARG A N   
1224 C CA  . ARG A 150 ? 0.5612 0.5030 0.7002 -0.0164 0.0078  0.0795  166 ARG A CA  
1225 C C   . ARG A 150 ? 0.5212 0.4752 0.6754 -0.0236 0.0016  0.0672  166 ARG A C   
1226 O O   . ARG A 150 ? 0.6038 0.5501 0.7728 -0.0355 0.0000  0.0652  166 ARG A O   
1227 C CB  . ARG A 150 ? 0.6175 0.5387 0.7426 -0.0074 0.0019  0.0737  166 ARG A CB  
1228 C CG  . ARG A 150 ? 0.7305 0.6442 0.8439 0.0011  0.0063  0.0867  166 ARG A CG  
1229 C CD  . ARG A 150 ? 0.8302 0.7262 0.9345 0.0104  0.0020  0.0817  166 ARG A CD  
1230 N NE  . ARG A 150 ? 0.9786 0.8459 1.0878 0.0083  0.0051  0.0873  166 ARG A NE  
1231 C CZ  . ARG A 150 ? 1.0149 0.8603 1.1283 0.0032  0.0027  0.0761  166 ARG A CZ  
1232 N NH1 . ARG A 150 ? 0.9608 0.8108 1.0721 0.0008  -0.0041 0.0600  166 ARG A NH1 
1233 N NH2 . ARG A 150 ? 0.9645 0.7814 1.0828 0.0006  0.0074  0.0815  166 ARG A NH2 
1234 N N   . MET A 151 ? 0.5089 0.4819 0.6604 -0.0167 -0.0022 0.0591  167 MET A N   
1235 C CA  . MET A 151 ? 0.4983 0.4866 0.6658 -0.0214 -0.0087 0.0496  167 MET A CA  
1236 C C   . MET A 151 ? 0.5501 0.5559 0.7418 -0.0331 -0.0027 0.0558  167 MET A C   
1237 O O   . MET A 151 ? 0.5572 0.5637 0.7663 -0.0442 -0.0085 0.0513  167 MET A O   
1238 C CB  . MET A 151 ? 0.4640 0.4694 0.6254 -0.0104 -0.0110 0.0432  167 MET A CB  
1239 C CG  . MET A 151 ? 0.4961 0.5195 0.6746 -0.0118 -0.0184 0.0352  167 MET A CG  
1240 S SD  . MET A 151 ? 0.5890 0.5940 0.7625 -0.0154 -0.0338 0.0243  167 MET A SD  
1241 C CE  . MET A 151 ? 0.5201 0.5535 0.7195 -0.0190 -0.0427 0.0198  167 MET A CE  
1242 N N   . LEU A 152 ? 0.5490 0.5703 0.7418 -0.0315 0.0091  0.0659  168 LEU A N   
1243 C CA  . LEU A 152 ? 0.5024 0.5427 0.7190 -0.0427 0.0175  0.0729  168 LEU A CA  
1244 C C   . LEU A 152 ? 0.5347 0.5553 0.7615 -0.0576 0.0182  0.0786  168 LEU A C   
1245 O O   . LEU A 152 ? 0.5737 0.6053 0.8258 -0.0708 0.0171  0.0772  168 LEU A O   
1246 C CB  . LEU A 152 ? 0.4999 0.5557 0.7094 -0.0386 0.0321  0.0838  168 LEU A CB  
1247 C CG  . LEU A 152 ? 0.5760 0.6546 0.7796 -0.0266 0.0356  0.0780  168 LEU A CG  
1248 C CD1 . LEU A 152 ? 0.5283 0.6220 0.7255 -0.0263 0.0518  0.0888  168 LEU A CD1 
1249 C CD2 . LEU A 152 ? 0.5288 0.6296 0.7574 -0.0267 0.0308  0.0683  168 LEU A CD2 
1250 N N   . ILE A 153 ? 0.5732 0.5648 0.7822 -0.0556 0.0201  0.0853  169 ILE A N   
1251 C CA  . ILE A 153 ? 0.6219 0.5888 0.8391 -0.0688 0.0223  0.0912  169 ILE A CA  
1252 C C   . ILE A 153 ? 0.6337 0.5874 0.8599 -0.0772 0.0099  0.0763  169 ILE A C   
1253 O O   . ILE A 153 ? 0.6633 0.6137 0.9092 -0.0937 0.0096  0.0755  169 ILE A O   
1254 C CB  . ILE A 153 ? 0.6071 0.5454 0.8034 -0.0614 0.0270  0.1024  169 ILE A CB  
1255 C CG1 . ILE A 153 ? 0.5981 0.5506 0.7859 -0.0570 0.0392  0.1194  169 ILE A CG1 
1256 C CG2 . ILE A 153 ? 0.6550 0.5602 0.8581 -0.0727 0.0282  0.1057  169 ILE A CG2 
1257 C CD1 . ILE A 153 ? 0.6513 0.5811 0.8185 -0.0477 0.0422  0.1326  169 ILE A CD1 
1258 N N   . ASN A 154 ? 0.6146 0.5608 0.8254 -0.0671 -0.0005 0.0640  170 ASN A N   
1259 C CA  . ASN A 154 ? 0.6727 0.6069 0.8863 -0.0744 -0.0129 0.0490  170 ASN A CA  
1260 C C   . ASN A 154 ? 0.6403 0.6034 0.8789 -0.0854 -0.0196 0.0429  170 ASN A C   
1261 O O   . ASN A 154 ? 0.6263 0.5820 0.8772 -0.1005 -0.0263 0.0358  170 ASN A O   
1262 C CB  . ASN A 154 ? 0.6934 0.6197 0.8847 -0.0605 -0.0212 0.0386  170 ASN A CB  
1263 C CG  . ASN A 154 ? 0.7639 0.6606 0.9346 -0.0512 -0.0165 0.0420  170 ASN A CG  
1264 O OD1 . ASN A 154 ? 0.8353 0.7090 1.0077 -0.0565 -0.0100 0.0490  170 ASN A OD1 
1265 N ND2 . ASN A 154 ? 0.6898 0.5869 0.8426 -0.0373 -0.0196 0.0376  170 ASN A ND2 
1266 N N   . GLN A 155 ? 0.5803 0.5769 0.8274 -0.0779 -0.0183 0.0449  171 GLN A N   
1267 C CA  . GLN A 155 ? 0.5982 0.6262 0.8725 -0.0859 -0.0251 0.0401  171 GLN A CA  
1268 C C   . GLN A 155 ? 0.6019 0.6391 0.9043 -0.1045 -0.0183 0.0471  171 GLN A C   
1269 O O   . GLN A 155 ? 0.6523 0.7037 0.9778 -0.1180 -0.0275 0.0406  171 GLN A O   
1270 C CB  . GLN A 155 ? 0.5473 0.6072 0.8265 -0.0721 -0.0222 0.0418  171 GLN A CB  
1271 C CG  . GLN A 155 ? 0.5318 0.5873 0.7909 -0.0572 -0.0323 0.0328  171 GLN A CG  
1272 C CD  . GLN A 155 ? 0.5913 0.6375 0.8486 -0.0632 -0.0490 0.0214  171 GLN A CD  
1273 O OE1 . GLN A 155 ? 0.5830 0.5993 0.8171 -0.0625 -0.0534 0.0159  171 GLN A OE1 
1274 N NE2 . GLN A 155 ? 0.5709 0.6440 0.8527 -0.0690 -0.0584 0.0179  171 GLN A NE2 
1275 N N   . HIS A 156 ? 0.5703 0.5998 0.8709 -0.1066 -0.0028 0.0608  172 HIS A N   
1276 C CA  . HIS A 156 ? 0.6106 0.6464 0.9375 -0.1257 0.0054  0.0690  172 HIS A CA  
1277 C C   . HIS A 156 ? 0.7105 0.7107 1.0371 -0.1416 0.0003  0.0644  172 HIS A C   
1278 O O   . HIS A 156 ? 0.6885 0.6968 1.0406 -0.1606 -0.0049 0.0594  172 HIS A O   
1279 C CB  . HIS A 156 ? 0.6257 0.6644 0.9482 -0.1228 0.0245  0.0868  172 HIS A CB  
1280 C CG  . HIS A 156 ? 0.6737 0.7250 1.0250 -0.1420 0.0356  0.0971  172 HIS A CG  
1281 N ND1 . HIS A 156 ? 0.6670 0.7612 1.0463 -0.1458 0.0424  0.1000  172 HIS A ND1 
1282 C CD2 . HIS A 156 ? 0.6902 0.7164 1.0482 -0.1588 0.0420  0.1053  172 HIS A CD2 
1283 C CE1 . HIS A 156 ? 0.7196 0.8168 1.1220 -0.1652 0.0527  0.1099  172 HIS A CE1 
1284 N NE2 . HIS A 156 ? 0.7065 0.7614 1.0959 -0.1739 0.0525  0.1135  172 HIS A NE2 
1285 N N   . THR A 157 ? 0.6887 0.6493 0.9878 -0.1345 0.0018  0.0654  173 THR A N   
1286 C CA  . THR A 157 ? 0.7141 0.6361 1.0127 -0.1488 0.0009  0.0623  173 THR A CA  
1287 C C   . THR A 157 ? 0.7648 0.6794 1.0637 -0.1569 -0.0161 0.0420  173 THR A C   
1288 O O   . THR A 157 ? 0.8001 0.6954 1.1098 -0.1760 -0.0189 0.0358  173 THR A O   
1289 C CB  . THR A 157 ? 0.7581 0.6411 1.0296 -0.1366 0.0081  0.0698  173 THR A CB  
1290 O OG1 . THR A 157 ? 0.7648 0.6454 1.0126 -0.1181 0.0001  0.0605  173 THR A OG1 
1291 C CG2 . THR A 157 ? 0.7057 0.5952 0.9749 -0.1305 0.0240  0.0915  173 THR A CG2 
1292 N N   . LEU A 158 ? 0.7276 0.6559 1.0132 -0.1436 -0.0276 0.0313  174 LEU A N   
1293 C CA  . LEU A 158 ? 0.7618 0.6848 1.0431 -0.1504 -0.0445 0.0128  174 LEU A CA  
1294 C C   . LEU A 158 ? 0.7824 0.7404 1.0953 -0.1671 -0.0547 0.0077  174 LEU A C   
1295 O O   . LEU A 158 ? 0.8235 0.7721 1.1407 -0.1835 -0.0664 -0.0055 174 LEU A O   
1296 C CB  . LEU A 158 ? 0.7155 0.6421 0.9719 -0.1308 -0.0527 0.0055  174 LEU A CB  
1297 C CG  . LEU A 158 ? 0.7165 0.6076 0.9420 -0.1163 -0.0464 0.0059  174 LEU A CG  
1298 C CD1 . LEU A 158 ? 0.7001 0.6024 0.9061 -0.0979 -0.0522 0.0017  174 LEU A CD1 
1299 C CD2 . LEU A 158 ? 0.7664 0.6175 0.9796 -0.1261 -0.0496 -0.0062 174 LEU A CD2 
1300 N N   . ILE A 159 ? 0.7610 0.7603 1.0969 -0.1636 -0.0503 0.0173  175 ILE A N   
1301 C CA  . ILE A 159 ? 0.7721 0.8123 1.1419 -0.1760 -0.0606 0.0133  175 ILE A CA  
1302 C C   . ILE A 159 ? 0.8379 0.8827 1.2395 -0.2005 -0.0537 0.0185  175 ILE A C   
1303 O O   . ILE A 159 ? 0.8266 0.8814 1.2484 -0.2199 -0.0663 0.0087  175 ILE A O   
1304 C CB  . ILE A 159 ? 0.7369 0.8196 1.1189 -0.1592 -0.0578 0.0204  175 ILE A CB  
1305 C CG1 . ILE A 159 ? 0.6462 0.7268 1.0023 -0.1399 -0.0697 0.0121  175 ILE A CG1 
1306 C CG2 . ILE A 159 ? 0.7213 0.8506 1.1469 -0.1715 -0.0628 0.0211  175 ILE A CG2 
1307 C CD1 . ILE A 159 ? 0.6104 0.7196 0.9700 -0.1204 -0.0643 0.0187  175 ILE A CD1 
1308 N N   . PHE A 160 ? 0.8114 0.8482 1.2166 -0.2011 -0.0341 0.0340  176 PHE A N   
1309 C CA  . PHE A 160 ? 0.8478 0.8890 1.2835 -0.2244 -0.0245 0.0419  176 PHE A CA  
1310 C C   . PHE A 160 ? 0.9526 0.9395 1.3728 -0.2367 -0.0193 0.0416  176 PHE A C   
1311 O O   . PHE A 160 ? 0.9429 0.9098 1.3609 -0.2389 -0.0019 0.0571  176 PHE A O   
1312 C CB  . PHE A 160 ? 0.7939 0.8628 1.2441 -0.2183 -0.0051 0.0605  176 PHE A CB  
1313 C CG  . PHE A 160 ? 0.7551 0.8720 1.2174 -0.2027 -0.0081 0.0598  176 PHE A CG  
1314 C CD1 . PHE A 160 ? 0.8210 0.9804 1.3196 -0.2121 -0.0193 0.0530  176 PHE A CD1 
1315 C CD2 . PHE A 160 ? 0.7001 0.8191 1.1382 -0.1785 -0.0005 0.0653  176 PHE A CD2 
1316 C CE1 . PHE A 160 ? 0.8401 1.0415 1.3513 -0.1957 -0.0215 0.0529  176 PHE A CE1 
1317 C CE2 . PHE A 160 ? 0.6970 0.8554 1.1457 -0.1637 -0.0024 0.0636  176 PHE A CE2 
1318 C CZ  . PHE A 160 ? 0.7678 0.9665 1.2534 -0.1713 -0.0123 0.0579  176 PHE A CZ  
1319 N N   . ASP A 161 ? 1.0958 1.0582 1.5046 -0.2449 -0.0347 0.0236  177 ASP A N   
1320 C CA  . ASP A 161 ? 1.1036 1.0108 1.4963 -0.2556 -0.0315 0.0186  177 ASP A CA  
1321 C C   . ASP A 161 ? 1.1459 1.0484 1.5692 -0.2872 -0.0308 0.0163  177 ASP A C   
1322 O O   . ASP A 161 ? 1.2366 1.1027 1.6601 -0.2971 -0.0167 0.0255  177 ASP A O   
1323 C CB  . ASP A 161 ? 1.1338 1.0148 1.4957 -0.2485 -0.0468 -0.0016 177 ASP A CB  
1324 C CG  . ASP A 161 ? 1.1485 1.0648 1.5201 -0.2548 -0.0683 -0.0176 177 ASP A CG  
1325 O OD1 . ASP A 161 ? 1.1828 1.1227 1.5860 -0.2775 -0.0755 -0.0217 177 ASP A OD1 
1326 O OD2 . ASP A 161 ? 1.1533 1.0743 1.5012 -0.2374 -0.0785 -0.0255 177 ASP A OD2 
1327 N N   . GLY A 162 ? 1.1947 1.1335 1.6446 -0.3036 -0.0462 0.0047  178 GLY A N   
1328 C CA  . GLY A 162 ? 1.1649 1.1048 1.6474 -0.3361 -0.0477 0.0007  178 GLY A CA  
1329 C C   . GLY A 162 ? 1.1913 1.1492 1.6836 -0.3527 -0.0724 -0.0218 178 GLY A C   
1330 O O   . GLY A 162 ? 1.1695 1.1790 1.6788 -0.3478 -0.0858 -0.0244 178 GLY A O   
1331 N N   . PRO A 169 ? 1.3455 1.5558 1.7528 -0.2125 -0.2327 -0.0626 185 PRO A N   
1332 C CA  . PRO A 169 ? 1.2903 1.4521 1.6549 -0.1967 -0.2154 -0.0619 185 PRO A CA  
1333 C C   . PRO A 169 ? 1.1754 1.3400 1.5158 -0.1689 -0.2176 -0.0557 185 PRO A C   
1334 O O   . PRO A 169 ? 1.1624 1.3574 1.5256 -0.1528 -0.2122 -0.0432 185 PRO A O   
1335 C CB  . PRO A 169 ? 1.2503 1.4090 1.6375 -0.1960 -0.1900 -0.0501 185 PRO A CB  
1336 C CG  . PRO A 169 ? 1.3795 1.5667 1.8128 -0.2220 -0.1933 -0.0507 185 PRO A CG  
1337 C CD  . PRO A 169 ? 1.3318 1.5492 1.7761 -0.2343 -0.2217 -0.0609 185 PRO A CD  
1338 N N   . LYS A 170 ? 0.9720 1.1039 1.2663 -0.1637 -0.2245 -0.0649 186 LYS A N   
1339 C CA  . LYS A 170 ? 0.8179 0.9477 1.0867 -0.1393 -0.2256 -0.0589 186 LYS A CA  
1340 C C   . LYS A 170 ? 0.7847 0.8926 1.0436 -0.1222 -0.2013 -0.0501 186 LYS A C   
1341 O O   . LYS A 170 ? 0.7464 0.8749 1.0199 -0.1051 -0.1946 -0.0386 186 LYS A O   
1342 C CB  . LYS A 170 ? 0.8100 0.9131 1.0325 -0.1409 -0.2394 -0.0712 186 LYS A CB  
1343 C CG  . LYS A 170 ? 0.9338 1.0636 1.1623 -0.1558 -0.2668 -0.0790 186 LYS A CG  
1344 C CD  . LYS A 170 ? 1.0070 1.1089 1.1844 -0.1589 -0.2797 -0.0922 186 LYS A CD  
1345 C CE  . LYS A 170 ? 1.0504 1.1138 1.2076 -0.1804 -0.2759 -0.1107 186 LYS A CE  
1346 N NZ  . LYS A 170 ? 1.1635 1.2467 1.3432 -0.2075 -0.2938 -0.1218 186 LYS A NZ  
1347 N N   . HIS A 171 ? 0.7103 0.7768 0.9453 -0.1265 -0.1880 -0.0557 187 HIS A N   
1348 C CA  . HIS A 171 ? 0.7542 0.8041 0.9840 -0.1126 -0.1662 -0.0467 187 HIS A CA  
1349 C C   . HIS A 171 ? 0.6891 0.7608 0.9577 -0.1176 -0.1538 -0.0367 187 HIS A C   
1350 O O   . HIS A 171 ? 0.7014 0.7863 0.9965 -0.1363 -0.1576 -0.0389 187 HIS A O   
1351 C CB  . HIS A 171 ? 0.6982 0.7008 0.8956 -0.1151 -0.1561 -0.0542 187 HIS A CB  
1352 C CG  . HIS A 171 ? 0.6981 0.6791 0.8552 -0.1064 -0.1627 -0.0621 187 HIS A CG  
1353 N ND1 . HIS A 171 ? 0.6566 0.6138 0.7882 -0.0908 -0.1501 -0.0594 187 HIS A ND1 
1354 C CD2 . HIS A 171 ? 0.7102 0.6918 0.8480 -0.1115 -0.1805 -0.0721 187 HIS A CD2 
1355 C CE1 . HIS A 171 ? 0.7004 0.6437 0.7995 -0.0868 -0.1582 -0.0672 187 HIS A CE1 
1356 N NE2 . HIS A 171 ? 0.7695 0.7262 0.8696 -0.0989 -0.1767 -0.0749 187 HIS A NE2 
1357 N N   . ILE A 172 ? 0.6478 0.7245 0.9194 -0.1014 -0.1386 -0.0258 188 ILE A N   
1358 C CA  . ILE A 172 ? 0.5902 0.6876 0.8937 -0.1036 -0.1242 -0.0153 188 ILE A CA  
1359 C C   . ILE A 172 ? 0.5921 0.6581 0.8764 -0.0984 -0.1052 -0.0103 188 ILE A C   
1360 O O   . ILE A 172 ? 0.5275 0.5916 0.7993 -0.0814 -0.0959 -0.0044 188 ILE A O   
1361 C CB  . ILE A 172 ? 0.5893 0.7251 0.9151 -0.0887 -0.1231 -0.0071 188 ILE A CB  
1362 C CG1 . ILE A 172 ? 0.6054 0.7717 0.9479 -0.0904 -0.1443 -0.0109 188 ILE A CG1 
1363 C CG2 . ILE A 172 ? 0.5575 0.7163 0.9159 -0.0927 -0.1067 0.0027  188 ILE A CG2 
1364 C CD1 . ILE A 172 ? 0.6409 0.8281 1.0145 -0.1132 -0.1540 -0.0146 188 ILE A CD1 
1365 N N   . GLY A 173 ? 0.5435 0.5842 0.8256 -0.1133 -0.1000 -0.0124 189 GLY A N   
1366 C CA  . GLY A 173 ? 0.5877 0.5960 0.8494 -0.1072 -0.0845 -0.0073 189 GLY A CA  
1367 C C   . GLY A 173 ? 0.5968 0.5806 0.8224 -0.0928 -0.0876 -0.0134 189 GLY A C   
1368 O O   . GLY A 173 ? 0.6394 0.6079 0.8481 -0.0968 -0.0992 -0.0251 189 GLY A O   
1369 N N   . SER A 174 ? 0.5436 0.5248 0.7566 -0.0764 -0.0772 -0.0059 190 SER A N   
1370 C CA  . SER A 174 ? 0.5422 0.5029 0.7241 -0.0632 -0.0785 -0.0106 190 SER A CA  
1371 C C   . SER A 174 ? 0.5788 0.5584 0.7553 -0.0521 -0.0881 -0.0132 190 SER A C   
1372 O O   . SER A 174 ? 0.5870 0.5519 0.7387 -0.0415 -0.0886 -0.0162 190 SER A O   
1373 C CB  . SER A 174 ? 0.5885 0.5365 0.7593 -0.0522 -0.0638 -0.0017 190 SER A CB  
1374 O OG  . SER A 174 ? 0.5727 0.5446 0.7493 -0.0411 -0.0588 0.0055  190 SER A OG  
1375 N N   . ILE A 175 ? 0.5706 0.5820 0.7707 -0.0542 -0.0953 -0.0114 191 ILE A N   
1376 C CA  . ILE A 175 ? 0.5545 0.5833 0.7522 -0.0423 -0.1042 -0.0118 191 ILE A CA  
1377 C C   . ILE A 175 ? 0.6252 0.6579 0.8198 -0.0501 -0.1230 -0.0200 191 ILE A C   
1378 O O   . ILE A 175 ? 0.5947 0.6368 0.8070 -0.0657 -0.1305 -0.0237 191 ILE A O   
1379 C CB  . ILE A 175 ? 0.5950 0.6581 0.8217 -0.0360 -0.0994 -0.0037 191 ILE A CB  
1380 C CG1 . ILE A 175 ? 0.5489 0.6068 0.7709 -0.0274 -0.0814 0.0032  191 ILE A CG1 
1381 C CG2 . ILE A 175 ? 0.4821 0.5627 0.7106 -0.0241 -0.1102 -0.0038 191 ILE A CG2 
1382 C CD1 . ILE A 175 ? 0.5205 0.6093 0.7706 -0.0246 -0.0727 0.0101  191 ILE A CD1 
1383 N N   . ASP A 176 ? 0.6144 0.6394 0.7852 -0.0402 -0.1309 -0.0229 192 ASP A N   
1384 C CA  . ASP A 176 ? 0.6090 0.6416 0.7735 -0.0447 -0.1501 -0.0286 192 ASP A CA  
1385 C C   . ASP A 176 ? 0.5136 0.5741 0.6916 -0.0313 -0.1571 -0.0210 192 ASP A C   
1386 O O   . ASP A 176 ? 0.5569 0.6081 0.7181 -0.0163 -0.1521 -0.0171 192 ASP A O   
1387 C CB  . ASP A 176 ? 0.6076 0.6081 0.7312 -0.0438 -0.1533 -0.0367 192 ASP A CB  
1388 C CG  . ASP A 176 ? 0.6656 0.6715 0.7769 -0.0510 -0.1737 -0.0438 192 ASP A CG  
1389 O OD1 . ASP A 176 ? 0.5926 0.6299 0.7271 -0.0532 -0.1872 -0.0404 192 ASP A OD1 
1390 O OD2 . ASP A 176 ? 0.6525 0.6320 0.7303 -0.0545 -0.1760 -0.0528 192 ASP A OD2 
1391 N N   . PRO A 177 ? 0.5855 0.6802 0.7952 -0.0358 -0.1681 -0.0184 193 PRO A N   
1392 C CA  . PRO A 177 ? 0.6113 0.7326 0.8365 -0.0206 -0.1747 -0.0103 193 PRO A CA  
1393 C C   . PRO A 177 ? 0.6128 0.7271 0.8113 -0.0135 -0.1908 -0.0106 193 PRO A C   
1394 O O   . PRO A 177 ? 0.6051 0.7351 0.8120 0.0015  -0.1956 -0.0025 193 PRO A O   
1395 C CB  . PRO A 177 ? 0.5630 0.7246 0.8322 -0.0297 -0.1827 -0.0081 193 PRO A CB  
1396 C CG  . PRO A 177 ? 0.6109 0.7632 0.8763 -0.0523 -0.1898 -0.0177 193 PRO A CG  
1397 C CD  . PRO A 177 ? 0.5693 0.6803 0.8047 -0.0550 -0.1745 -0.0224 193 PRO A CD  
1398 N N   . ASN A 178 ? 0.6056 0.6958 0.7715 -0.0232 -0.1983 -0.0193 194 ASN A N   
1399 C CA  . ASN A 178 ? 0.6556 0.7369 0.7902 -0.0187 -0.2130 -0.0198 194 ASN A CA  
1400 C C   . ASN A 178 ? 0.6859 0.7266 0.7773 -0.0201 -0.2042 -0.0271 194 ASN A C   
1401 O O   . ASN A 178 ? 0.6452 0.6720 0.7077 -0.0283 -0.2144 -0.0350 194 ASN A O   
1402 C CB  . ASN A 178 ? 0.6697 0.7711 0.8092 -0.0320 -0.2361 -0.0247 194 ASN A CB  
1403 C CG  . ASN A 178 ? 0.7840 0.9293 0.9646 -0.0270 -0.2481 -0.0155 194 ASN A CG  
1404 O OD1 . ASN A 178 ? 0.9777 1.1344 1.1586 -0.0106 -0.2549 -0.0053 194 ASN A OD1 
1405 N ND2 . ASN A 178 ? 0.8546 1.0257 1.0722 -0.0409 -0.2505 -0.0184 194 ASN A ND2 
1406 N N   . CYS A 179 ? 0.6283 0.6512 0.7159 -0.0127 -0.1845 -0.0250 195 CYS A N   
1407 C CA  . CYS A 179 ? 0.6176 0.6057 0.6704 -0.0125 -0.1740 -0.0308 195 CYS A CA  
1408 C C   . CYS A 179 ? 0.6655 0.6414 0.6851 -0.0038 -0.1800 -0.0284 195 CYS A C   
1409 O O   . CYS A 179 ? 0.6255 0.6059 0.6469 0.0098  -0.1777 -0.0188 195 CYS A O   
1410 C CB  . CYS A 179 ? 0.6147 0.5933 0.6750 -0.0052 -0.1537 -0.0270 195 CYS A CB  
1411 S SG  . CYS A 179 ? 0.6535 0.5954 0.6772 -0.0031 -0.1407 -0.0325 195 CYS A SG  
1412 N N   . ASN A 180 ? 0.6371 0.5958 0.6254 -0.0122 -0.1864 -0.0373 196 ASN A N   
1413 C CA  . ASN A 180 ? 0.7145 0.6576 0.6649 -0.0062 -0.1899 -0.0358 196 ASN A CA  
1414 C C   . ASN A 180 ? 0.7049 0.6219 0.6376 0.0002  -0.1699 -0.0362 196 ASN A C   
1415 O O   . ASN A 180 ? 0.6668 0.5637 0.5855 -0.0065 -0.1605 -0.0462 196 ASN A O   
1416 C CB  . ASN A 180 ? 0.7364 0.6716 0.6585 -0.0190 -0.2031 -0.0471 196 ASN A CB  
1417 C CG  . ASN A 180 ? 0.8259 0.7486 0.7064 -0.0136 -0.2087 -0.0442 196 ASN A CG  
1418 O OD1 . ASN A 180 ? 0.8059 0.7118 0.6696 -0.0039 -0.1955 -0.0388 196 ASN A OD1 
1419 N ND2 . ASN A 180 ? 0.8732 0.8048 0.7364 -0.0211 -0.2287 -0.0475 196 ASN A ND2 
1420 N N   . VAL A 181 ? 0.6556 0.5728 0.5900 0.0131  -0.1632 -0.0257 197 VAL A N   
1421 C CA  . VAL A 181 ? 0.6558 0.5543 0.5825 0.0181  -0.1442 -0.0258 197 VAL A CA  
1422 C C   . VAL A 181 ? 0.6805 0.5546 0.5696 0.0151  -0.1387 -0.0323 197 VAL A C   
1423 O O   . VAL A 181 ? 0.6701 0.5297 0.5553 0.0134  -0.1245 -0.0383 197 VAL A O   
1424 C CB  . VAL A 181 ? 0.6099 0.5130 0.5461 0.0308  -0.1392 -0.0144 197 VAL A CB  
1425 C CG1 . VAL A 181 ? 0.5813 0.4658 0.5055 0.0342  -0.1219 -0.0148 197 VAL A CG1 
1426 C CG2 . VAL A 181 ? 0.6544 0.5795 0.6286 0.0336  -0.1389 -0.0109 197 VAL A CG2 
1427 N N   . SER A 182 ? 0.6706 0.5409 0.5315 0.0147  -0.1494 -0.0309 198 SER A N   
1428 C CA  . SER A 182 ? 0.7255 0.5732 0.5482 0.0123  -0.1422 -0.0369 198 SER A CA  
1429 C C   . SER A 182 ? 0.7201 0.5560 0.5338 0.0014  -0.1393 -0.0526 198 SER A C   
1430 O O   . SER A 182 ? 0.7202 0.5364 0.5131 0.0009  -0.1256 -0.0595 198 SER A O   
1431 C CB  . SER A 182 ? 0.7750 0.6217 0.5664 0.0136  -0.1551 -0.0311 198 SER A CB  
1432 O OG  . SER A 182 ? 0.9023 0.7469 0.6920 0.0245  -0.1503 -0.0171 198 SER A OG  
1433 N N   . GLU A 183 ? 0.7503 0.5977 0.5805 -0.0073 -0.1512 -0.0586 199 GLU A N   
1434 C CA  A GLU A 183 ? 0.7985 0.6312 0.6225 -0.0185 -0.1478 -0.0741 199 GLU A CA  
1435 C CA  B GLU A 183 ? 0.7961 0.6287 0.6199 -0.0184 -0.1478 -0.0741 199 GLU A CA  
1436 C C   . GLU A 183 ? 0.7705 0.5929 0.6145 -0.0157 -0.1290 -0.0757 199 GLU A C   
1437 O O   . GLU A 183 ? 0.7579 0.5586 0.5877 -0.0185 -0.1178 -0.0863 199 GLU A O   
1438 C CB  A GLU A 183 ? 0.7866 0.6349 0.6269 -0.0304 -0.1656 -0.0795 199 GLU A CB  
1439 C CB  B GLU A 183 ? 0.7889 0.6371 0.6281 -0.0304 -0.1658 -0.0796 199 GLU A CB  
1440 C CG  A GLU A 183 ? 0.8216 0.6521 0.6589 -0.0434 -0.1619 -0.0961 199 GLU A CG  
1441 C CG  B GLU A 183 ? 0.8300 0.6761 0.6354 -0.0388 -0.1822 -0.0875 199 GLU A CG  
1442 C CD  A GLU A 183 ? 0.9358 0.7404 0.7281 -0.0478 -0.1589 -0.1099 199 GLU A CD  
1443 C CD  B GLU A 183 ? 0.9519 0.7670 0.7183 -0.0433 -0.1712 -0.1023 199 GLU A CD  
1444 O OE1 A GLU A 183 ? 0.9737 0.7810 0.7358 -0.0458 -0.1678 -0.1075 199 GLU A OE1 
1445 O OE1 B GLU A 183 ? 0.9647 0.7623 0.7392 -0.0476 -0.1581 -0.1127 199 GLU A OE1 
1446 O OE2 A GLU A 183 ? 0.9268 0.7076 0.7132 -0.0527 -0.1468 -0.1227 199 GLU A OE2 
1447 O OE2 B GLU A 183 ? 0.9043 0.7118 0.6319 -0.0416 -0.1744 -0.1029 199 GLU A OE2 
1448 N N   . VAL A 184 ? 0.7009 0.5385 0.5770 -0.0095 -0.1252 -0.0653 200 VAL A N   
1449 C CA  . VAL A 184 ? 0.7193 0.5492 0.6123 -0.0063 -0.1087 -0.0650 200 VAL A CA  
1450 C C   . VAL A 184 ? 0.6908 0.5067 0.5658 0.0021  -0.0942 -0.0638 200 VAL A C   
1451 O O   . VAL A 184 ? 0.6971 0.4990 0.5721 0.0032  -0.0810 -0.0686 200 VAL A O   
1452 C CB  . VAL A 184 ? 0.6220 0.4727 0.5501 -0.0023 -0.1083 -0.0546 200 VAL A CB  
1453 C CG1 . VAL A 184 ? 0.6128 0.4565 0.5549 0.0014  -0.0925 -0.0528 200 VAL A CG1 
1454 C CG2 . VAL A 184 ? 0.6123 0.4784 0.5612 -0.0118 -0.1208 -0.0562 200 VAL A CG2 
1455 N N   . VAL A 185 ? 0.6885 0.5080 0.5486 0.0080  -0.0961 -0.0568 201 VAL A N   
1456 C CA  . VAL A 185 ? 0.7125 0.5198 0.5544 0.0139  -0.0824 -0.0557 201 VAL A CA  
1457 C C   . VAL A 185 ? 0.7117 0.4986 0.5260 0.0096  -0.0758 -0.0681 201 VAL A C   
1458 O O   . VAL A 185 ? 0.6536 0.4300 0.4671 0.0131  -0.0601 -0.0715 201 VAL A O   
1459 C CB  . VAL A 185 ? 0.7149 0.5265 0.5429 0.0189  -0.0869 -0.0457 201 VAL A CB  
1460 C CG1 . VAL A 185 ? 0.6918 0.4903 0.4990 0.0224  -0.0722 -0.0450 201 VAL A CG1 
1461 C CG2 . VAL A 185 ? 0.6199 0.4481 0.4761 0.0247  -0.0898 -0.0351 201 VAL A CG2 
1462 N N   . LYS A 186 ? 0.7179 0.5000 0.5097 0.0022  -0.0877 -0.0756 202 LYS A N   
1463 C CA  . LYS A 186 ? 0.7816 0.5426 0.5428 -0.0024 -0.0811 -0.0895 202 LYS A CA  
1464 C C   . LYS A 186 ? 0.7800 0.5283 0.5562 -0.0054 -0.0722 -0.1003 202 LYS A C   
1465 O O   . LYS A 186 ? 0.7946 0.5246 0.5569 -0.0032 -0.0573 -0.1090 202 LYS A O   
1466 C CB  . LYS A 186 ? 0.8435 0.6031 0.5754 -0.0111 -0.0979 -0.0962 202 LYS A CB  
1467 C CG  . LYS A 186 ? 0.9639 0.7307 0.6722 -0.0074 -0.1059 -0.0854 202 LYS A CG  
1468 C CD  . LYS A 186 ? 1.0984 0.8676 0.7795 -0.0166 -0.1260 -0.0913 202 LYS A CD  
1469 C CE  . LYS A 186 ? 1.1535 0.9323 0.8145 -0.0117 -0.1372 -0.0769 202 LYS A CE  
1470 N NZ  . LYS A 186 ? 1.1923 0.9840 0.8415 -0.0193 -0.1622 -0.0784 202 LYS A NZ  
1471 N N   . ASP A 187 ? 0.7802 0.5371 0.5848 -0.0104 -0.0805 -0.0995 203 ASP A N   
1472 C CA  . ASP A 187 ? 0.7551 0.4977 0.5756 -0.0132 -0.0718 -0.1073 203 ASP A CA  
1473 C C   . ASP A 187 ? 0.7293 0.4679 0.5635 -0.0018 -0.0533 -0.1016 203 ASP A C   
1474 O O   . ASP A 187 ? 0.7519 0.4708 0.5822 0.0003  -0.0403 -0.1099 203 ASP A O   
1475 C CB  . ASP A 187 ? 0.7275 0.4837 0.5803 -0.0196 -0.0818 -0.1028 203 ASP A CB  
1476 C CG  . ASP A 187 ? 0.8004 0.5607 0.6470 -0.0332 -0.0998 -0.1108 203 ASP A CG  
1477 O OD1 . ASP A 187 ? 0.8013 0.5495 0.6162 -0.0393 -0.1051 -0.1226 203 ASP A OD1 
1478 O OD2 . ASP A 187 ? 0.8009 0.5785 0.6758 -0.0383 -0.1085 -0.1051 203 ASP A OD2 
1479 N N   . ALA A 188 ? 0.6713 0.4292 0.5240 0.0054  -0.0524 -0.0875 204 ALA A N   
1480 C CA  . ALA A 188 ? 0.6720 0.4315 0.5396 0.0153  -0.0374 -0.0810 204 ALA A CA  
1481 C C   . ALA A 188 ? 0.7204 0.4692 0.5659 0.0207  -0.0244 -0.0855 204 ALA A C   
1482 O O   . ALA A 188 ? 0.6889 0.4304 0.5424 0.0271  -0.0102 -0.0872 204 ALA A O   
1483 C CB  . ALA A 188 ? 0.6363 0.4184 0.5234 0.0200  -0.0407 -0.0672 204 ALA A CB  
1484 N N   . TYR A 189 ? 0.6876 0.4366 0.5063 0.0188  -0.0284 -0.0863 205 TYR A N   
1485 C CA  . TYR A 189 ? 0.7098 0.4490 0.5052 0.0227  -0.0146 -0.0904 205 TYR A CA  
1486 C C   . TYR A 189 ? 0.7903 0.5068 0.5703 0.0212  -0.0055 -0.1060 205 TYR A C   
1487 O O   . TYR A 189 ? 0.7467 0.4561 0.5278 0.0281  0.0118  -0.1094 205 TYR A O   
1488 C CB  . TYR A 189 ? 0.7337 0.4748 0.4991 0.0197  -0.0217 -0.0873 205 TYR A CB  
1489 C CG  . TYR A 189 ? 0.8047 0.5320 0.5381 0.0209  -0.0077 -0.0943 205 TYR A CG  
1490 C CD1 . TYR A 189 ? 0.7768 0.5093 0.5139 0.0271  0.0078  -0.0877 205 TYR A CD1 
1491 C CD2 . TYR A 189 ? 0.8307 0.5404 0.5304 0.0150  -0.0090 -0.1085 205 TYR A CD2 
1492 C CE1 . TYR A 189 ? 0.7712 0.4932 0.4812 0.0281  0.0229  -0.0935 205 TYR A CE1 
1493 C CE2 . TYR A 189 ? 0.8593 0.5564 0.5278 0.0164  0.0061  -0.1156 205 TYR A CE2 
1494 C CZ  . TYR A 189 ? 0.8492 0.5532 0.5243 0.0234  0.0229  -0.1073 205 TYR A CZ  
1495 O OH  . TYR A 189 ? 0.8330 0.5272 0.4801 0.0250  0.0403  -0.1133 205 TYR A OH  
1496 N N   . ASP A 190 ? 0.7770 0.4823 0.5435 0.0119  -0.0168 -0.1165 206 ASP A N   
1497 C CA  . ASP A 190 ? 0.7995 0.4791 0.5475 0.0089  -0.0087 -0.1341 206 ASP A CA  
1498 C C   . ASP A 190 ? 0.8060 0.4757 0.5816 0.0160  0.0052  -0.1355 206 ASP A C   
1499 O O   . ASP A 190 ? 0.7915 0.4432 0.5576 0.0214  0.0216  -0.1456 206 ASP A O   
1500 C CB  . ASP A 190 ? 0.7696 0.4413 0.5038 -0.0046 -0.0259 -0.1447 206 ASP A CB  
1501 C CG  . ASP A 190 ? 0.9079 0.5844 0.6059 -0.0110 -0.0385 -0.1466 206 ASP A CG  
1502 O OD1 . ASP A 190 ? 0.9173 0.5954 0.5938 -0.0054 -0.0303 -0.1425 206 ASP A OD1 
1503 O OD2 . ASP A 190 ? 0.9719 0.6512 0.6629 -0.0221 -0.0569 -0.1514 206 ASP A OD2 
1504 N N   . MET A 191 ? 0.6952 0.3767 0.5049 0.0169  -0.0005 -0.1249 207 MET A N   
1505 C CA  . MET A 191 ? 0.7716 0.4444 0.6072 0.0246  0.0115  -0.1232 207 MET A CA  
1506 C C   . MET A 191 ? 0.7395 0.4211 0.5842 0.0381  0.0276  -0.1164 207 MET A C   
1507 O O   . MET A 191 ? 0.8005 0.4675 0.6501 0.0463  0.0428  -0.1219 207 MET A O   
1508 C CB  . MET A 191 ? 0.6880 0.3739 0.5552 0.0225  0.0020  -0.1112 207 MET A CB  
1509 C CG  . MET A 191 ? 0.7230 0.3972 0.6145 0.0293  0.0123  -0.1081 207 MET A CG  
1510 S SD  . MET A 191 ? 0.8405 0.4743 0.7201 0.0225  0.0172  -0.1270 207 MET A SD  
1511 C CE  . MET A 191 ? 0.8021 0.4212 0.6925 0.0405  0.0400  -0.1268 207 MET A CE  
1512 N N   . ALA A 192 ? 0.7238 0.4295 0.5727 0.0404  0.0247  -0.1046 208 ALA A N   
1513 C CA  . ALA A 192 ? 0.7278 0.4457 0.5879 0.0509  0.0387  -0.0979 208 ALA A CA  
1514 C C   . ALA A 192 ? 0.7676 0.4719 0.6028 0.0540  0.0540  -0.1092 208 ALA A C   
1515 O O   . ALA A 192 ? 0.7455 0.4504 0.5935 0.0641  0.0702  -0.1095 208 ALA A O   
1516 C CB  . ALA A 192 ? 0.6757 0.4185 0.5417 0.0500  0.0318  -0.0850 208 ALA A CB  
1517 N N   . LYS A 193 ? 0.7780 0.4714 0.5775 0.0458  0.0492  -0.1183 209 LYS A N   
1518 C CA  . LYS A 193 ? 0.8099 0.4889 0.5799 0.0476  0.0643  -0.1302 209 LYS A CA  
1519 C C   . LYS A 193 ? 0.8500 0.5050 0.6221 0.0528  0.0774  -0.1442 209 LYS A C   
1520 O O   . LYS A 193 ? 0.9134 0.5633 0.6834 0.0617  0.0972  -0.1497 209 LYS A O   
1521 C CB  . LYS A 193 ? 0.8377 0.5080 0.5659 0.0367  0.0537  -0.1374 209 LYS A CB  
1522 C CG  . LYS A 193 ? 0.9039 0.5539 0.5947 0.0369  0.0690  -0.1534 209 LYS A CG  
1523 C CD  . LYS A 193 ? 0.9703 0.6164 0.6170 0.0265  0.0574  -0.1571 209 LYS A CD  
1524 C CE  . LYS A 193 ? 1.0266 0.6499 0.6311 0.0248  0.0711  -0.1756 209 LYS A CE  
1525 N NZ  . LYS A 193 ? 1.1408 0.7671 0.7471 0.0352  0.0970  -0.1746 209 LYS A NZ  
1526 N N   . LEU A 194 ? 0.8561 0.4954 0.6334 0.0473  0.0675  -0.1503 210 LEU A N   
1527 C CA  . LEU A 194 ? 0.8469 0.4585 0.6275 0.0518  0.0795  -0.1636 210 LEU A CA  
1528 C C   . LEU A 194 ? 0.9073 0.5264 0.7235 0.0681  0.0954  -0.1546 210 LEU A C   
1529 O O   . LEU A 194 ? 0.8836 0.4874 0.6976 0.0778  0.1145  -0.1641 210 LEU A O   
1530 C CB  . LEU A 194 ? 0.8513 0.4485 0.6383 0.0414  0.0644  -0.1674 210 LEU A CB  
1531 C CG  . LEU A 194 ? 1.0749 0.6352 0.8547 0.0392  0.0715  -0.1853 210 LEU A CG  
1532 C CD1 . LEU A 194 ? 1.0913 0.6433 0.8598 0.0211  0.0515  -0.1923 210 LEU A CD1 
1533 C CD2 . LEU A 194 ? 1.0938 0.6476 0.9117 0.0513  0.0816  -0.1768 210 LEU A CD2 
1534 N N   . LEU A 195 ? 0.8657 0.5101 0.7145 0.0717  0.0879  -0.1360 211 LEU A N   
1535 C CA  . LEU A 195 ? 0.8579 0.5149 0.7411 0.0869  0.1001  -0.1255 211 LEU A CA  
1536 C C   . LEU A 195 ? 0.8669 0.5416 0.7485 0.0946  0.1150  -0.1240 211 LEU A C   
1537 O O   . LEU A 195 ? 0.8503 0.5246 0.7483 0.1080  0.1323  -0.1252 211 LEU A O   
1538 C CB  . LEU A 195 ? 0.7689 0.4498 0.6824 0.0869  0.0867  -0.1067 211 LEU A CB  
1539 C CG  . LEU A 195 ? 0.8664 0.5337 0.7882 0.0802  0.0742  -0.1049 211 LEU A CG  
1540 C CD1 . LEU A 195 ? 0.7438 0.4378 0.6900 0.0793  0.0618  -0.0866 211 LEU A CD1 
1541 C CD2 . LEU A 195 ? 0.8723 0.5122 0.8065 0.0889  0.0856  -0.1097 211 LEU A CD2 
1542 N N   . CYS A 196 ? 0.7969 0.4877 0.6607 0.0866  0.1091  -0.1206 212 CYS A N   
1543 C CA  . CYS A 196 ? 0.8593 0.5691 0.7240 0.0916  0.1229  -0.1169 212 CYS A CA  
1544 C C   . CYS A 196 ? 0.8549 0.5459 0.6959 0.0961  0.1432  -0.1326 212 CYS A C   
1545 O O   . CYS A 196 ? 0.8494 0.5514 0.7071 0.1071  0.1617  -0.1316 212 CYS A O   
1546 C CB  . CYS A 196 ? 0.8583 0.5845 0.7075 0.0809  0.1114  -0.1088 212 CYS A CB  
1547 S SG  . CYS A 196 ? 0.8443 0.5971 0.7003 0.0835  0.1258  -0.1002 212 CYS A SG  
1548 N N   . ASP A 197 ? 0.8547 0.5181 0.6572 0.0877  0.1402  -0.1481 213 ASP A N   
1549 C CA  . ASP A 197 ? 0.9461 0.5867 0.7219 0.0916  0.1599  -0.1661 213 ASP A CA  
1550 C C   . ASP A 197 ? 0.9626 0.5903 0.7656 0.1067  0.1762  -0.1718 213 ASP A C   
1551 O O   . ASP A 197 ? 0.9777 0.6030 0.7798 0.1171  0.1991  -0.1793 213 ASP A O   
1552 C CB  . ASP A 197 ? 0.9415 0.5538 0.6725 0.0786  0.1501  -0.1827 213 ASP A CB  
1553 C CG  . ASP A 197 ? 1.0043 0.6263 0.6999 0.0667  0.1399  -0.1793 213 ASP A CG  
1554 O OD1 . ASP A 197 ? 0.9868 0.6312 0.6865 0.0693  0.1470  -0.1677 213 ASP A OD1 
1555 O OD2 . ASP A 197 ? 1.0295 0.6368 0.6939 0.0547  0.1246  -0.1879 213 ASP A OD2 
1556 N N   . LYS A 198 ? 0.9613 0.5803 0.7889 0.1085  0.1657  -0.1677 214 LYS A N   
1557 C CA  . LYS A 198 ? 0.9651 0.5674 0.8183 0.1235  0.1799  -0.1715 214 LYS A CA  
1558 C C   . LYS A 198 ? 0.9421 0.5738 0.8339 0.1403  0.1941  -0.1583 214 LYS A C   
1559 O O   . LYS A 198 ? 0.9890 0.6121 0.8896 0.1546  0.2157  -0.1659 214 LYS A O   
1560 C CB  . LYS A 198 ? 1.0068 0.5964 0.8793 0.1207  0.1643  -0.1654 214 LYS A CB  
1561 C CG  . LYS A 198 ? 1.0369 0.5828 0.8873 0.1142  0.1645  -0.1844 214 LYS A CG  
1562 C CD  . LYS A 198 ? 1.0791 0.6004 0.9540 0.1302  0.1804  -0.1875 214 LYS A CD  
1563 C CE  . LYS A 198 ? 1.1168 0.5899 0.9619 0.1238  0.1869  -0.2125 214 LYS A CE  
1564 N NZ  . LYS A 198 ? 1.2591 0.7036 1.1291 0.1380  0.1999  -0.2145 214 LYS A NZ  
1565 N N   . TYR A 199 ? 0.9506 0.6179 0.8669 0.1389  0.1823  -0.1390 215 TYR A N   
1566 C CA  . TYR A 199 ? 0.9367 0.6348 0.8950 0.1538  0.1918  -0.1252 215 TYR A CA  
1567 C C   . TYR A 199 ? 0.8628 0.5881 0.8193 0.1541  0.2047  -0.1237 215 TYR A C   
1568 O O   . TYR A 199 ? 0.8905 0.6358 0.8774 0.1681  0.2203  -0.1192 215 TYR A O   
1569 C CB  . TYR A 199 ? 0.9545 0.6761 0.9429 0.1524  0.1722  -0.1055 215 TYR A CB  
1570 C CG  . TYR A 199 ? 1.0456 0.7405 1.0380 0.1525  0.1621  -0.1053 215 TYR A CG  
1571 C CD1 . TYR A 199 ? 1.0321 0.6967 1.0304 0.1644  0.1754  -0.1140 215 TYR A CD1 
1572 C CD2 . TYR A 199 ? 1.0312 0.7288 1.0205 0.1402  0.1409  -0.0973 215 TYR A CD2 
1573 C CE1 . TYR A 199 ? 1.0997 0.7366 1.1014 0.1631  0.1672  -0.1134 215 TYR A CE1 
1574 C CE2 . TYR A 199 ? 1.0763 0.7499 1.0696 0.1387  0.1330  -0.0965 215 TYR A CE2 
1575 C CZ  . TYR A 199 ? 1.1484 0.7912 1.1478 0.1494  0.1459  -0.1042 215 TYR A CZ  
1576 O OH  . TYR A 199 ? 1.1600 0.7768 1.1638 0.1464  0.1386  -0.1025 215 TYR A OH  
1577 N N   . TYR A 200 ? 0.9034 0.6305 0.8263 0.1392  0.1992  -0.1267 216 TYR A N   
1578 C CA  . TYR A 200 ? 0.9047 0.6560 0.8242 0.1372  0.2113  -0.1236 216 TYR A CA  
1579 C C   . TYR A 200 ? 0.9255 0.6565 0.8026 0.1340  0.2284  -0.1400 216 TYR A C   
1580 O O   . TYR A 200 ? 1.0140 0.7633 0.8875 0.1330  0.2426  -0.1377 216 TYR A O   
1581 C CB  . TYR A 200 ? 0.8894 0.6615 0.8048 0.1230  0.1933  -0.1107 216 TYR A CB  
1582 C CG  . TYR A 200 ? 0.8561 0.6577 0.8135 0.1257  0.1810  -0.0939 216 TYR A CG  
1583 C CD1 . TYR A 200 ? 0.8488 0.6832 0.8428 0.1337  0.1915  -0.0850 216 TYR A CD1 
1584 C CD2 . TYR A 200 ? 0.8821 0.6810 0.8421 0.1193  0.1587  -0.0871 216 TYR A CD2 
1585 C CE1 . TYR A 200 ? 0.8607 0.7233 0.8902 0.1350  0.1788  -0.0704 216 TYR A CE1 
1586 C CE2 . TYR A 200 ? 0.9063 0.7318 0.9003 0.1211  0.1478  -0.0727 216 TYR A CE2 
1587 C CZ  . TYR A 200 ? 0.9083 0.7654 0.9357 0.1286  0.1571  -0.0646 216 TYR A CZ  
1588 O OH  . TYR A 200 ? 0.9227 0.8075 0.9816 0.1295  0.1448  -0.0509 216 TYR A OH  
1589 N N   . MET A 201 ? 0.9493 0.6434 0.7931 0.1310  0.2273  -0.1565 217 MET A N   
1590 C CA  . MET A 201 ? 1.0424 0.7140 0.8393 0.1271  0.2423  -0.1743 217 MET A CA  
1591 C C   . MET A 201 ? 1.0562 0.7369 0.8178 0.1119  0.2346  -0.1694 217 MET A C   
1592 O O   . MET A 201 ? 1.1293 0.8059 0.8590 0.1098  0.2512  -0.1771 217 MET A O   
1593 C CB  . MET A 201 ? 1.1280 0.8038 0.9366 0.1421  0.2734  -0.1818 217 MET A CB  
1594 C CG  . MET A 201 ? 1.1819 0.8552 1.0346 0.1604  0.2818  -0.1816 217 MET A CG  
1595 S SD  . MET A 201 ? 1.3880 1.0140 1.2264 0.1594  0.2700  -0.1960 217 MET A SD  
1596 C CE  . MET A 201 ? 1.2933 0.8803 1.0694 0.1535  0.2870  -0.2249 217 MET A CE  
1597 N N   . ALA A 202 ? 0.9717 0.6637 0.7383 0.1018  0.2102  -0.1561 218 ALA A N   
1598 C CA  . ALA A 202 ? 1.0096 0.7102 0.7480 0.0888  0.2009  -0.1482 218 ALA A CA  
1599 C C   . ALA A 202 ? 0.9025 0.6121 0.6531 0.0808  0.1735  -0.1352 218 ALA A C   
1600 O O   . ALA A 202 ? 0.9335 0.6539 0.7225 0.0858  0.1651  -0.1277 218 ALA A O   
1601 C CB  . ALA A 202 ? 0.9840 0.7112 0.7347 0.0907  0.2180  -0.1378 218 ALA A CB  
1602 N N   . SER A 203 ? 0.9124 0.6182 0.6303 0.0691  0.1599  -0.1318 219 SER A N   
1603 C CA  . SER A 203 ? 0.9129 0.6273 0.6428 0.0626  0.1355  -0.1202 219 SER A CA  
1604 C C   . SER A 203 ? 0.9028 0.6196 0.6016 0.0530  0.1279  -0.1123 219 SER A C   
1605 O O   . SER A 203 ? 0.9529 0.6546 0.6090 0.0487  0.1330  -0.1202 219 SER A O   
1606 C CB  . SER A 203 ? 0.9340 0.6298 0.6581 0.0593  0.1190  -0.1292 219 SER A CB  
1607 O OG  . SER A 203 ? 1.0248 0.6968 0.7035 0.0538  0.1209  -0.1447 219 SER A OG  
1608 N N   . PRO A 204 ? 0.8835 0.6173 0.6006 0.0497  0.1163  -0.0969 220 PRO A N   
1609 C CA  . PRO A 204 ? 0.8672 0.5994 0.5556 0.0415  0.1066  -0.0880 220 PRO A CA  
1610 C C   . PRO A 204 ? 0.8860 0.6033 0.5468 0.0358  0.0862  -0.0932 220 PRO A C   
1611 O O   . PRO A 204 ? 0.8357 0.5489 0.5101 0.0363  0.0751  -0.0999 220 PRO A O   
1612 C CB  . PRO A 204 ? 0.8294 0.5812 0.5514 0.0408  0.0985  -0.0726 220 PRO A CB  
1613 C CG  . PRO A 204 ? 0.8128 0.5796 0.5781 0.0482  0.1066  -0.0734 220 PRO A CG  
1614 C CD  . PRO A 204 ? 0.8321 0.5856 0.5957 0.0538  0.1107  -0.0873 220 PRO A CD  
1615 N N   . ASP A 205 ? 0.8977 0.6082 0.5202 0.0299  0.0810  -0.0890 221 ASP A N   
1616 C CA  . ASP A 205 ? 0.9005 0.6027 0.4987 0.0241  0.0586  -0.0905 221 ASP A CA  
1617 C C   . ASP A 205 ? 0.8730 0.5886 0.4975 0.0236  0.0394  -0.0763 221 ASP A C   
1618 O O   . ASP A 205 ? 0.8329 0.5613 0.4875 0.0266  0.0440  -0.0657 221 ASP A O   
1619 C CB  . ASP A 205 ? 0.9317 0.6230 0.4778 0.0191  0.0596  -0.0895 221 ASP A CB  
1620 C CG  . ASP A 205 ? 1.0423 0.7178 0.5559 0.0186  0.0761  -0.1072 221 ASP A CG  
1621 O OD1 . ASP A 205 ? 1.0147 0.6842 0.5448 0.0219  0.0829  -0.1217 221 ASP A OD1 
1622 O OD2 . ASP A 205 ? 1.1115 0.7789 0.5816 0.0152  0.0830  -0.1064 221 ASP A OD2 
1623 N N   . LEU A 206 ? 0.8853 0.5986 0.4980 0.0194  0.0179  -0.0768 222 LEU A N   
1624 C CA  . LEU A 206 ? 0.9213 0.6472 0.5577 0.0198  -0.0004 -0.0649 222 LEU A CA  
1625 C C   . LEU A 206 ? 0.9474 0.6716 0.5543 0.0174  -0.0137 -0.0540 222 LEU A C   
1626 O O   . LEU A 206 ? 0.9302 0.6453 0.4992 0.0130  -0.0200 -0.0597 222 LEU A O   
1627 C CB  . LEU A 206 ? 0.8230 0.5520 0.4791 0.0177  -0.0153 -0.0730 222 LEU A CB  
1628 C CG  . LEU A 206 ? 0.8543 0.5978 0.5343 0.0181  -0.0342 -0.0623 222 LEU A CG  
1629 C CD1 . LEU A 206 ? 0.7961 0.5518 0.5130 0.0237  -0.0275 -0.0521 222 LEU A CD1 
1630 C CD2 . LEU A 206 ? 0.7786 0.5248 0.4715 0.0136  -0.0484 -0.0712 222 LEU A CD2 
1631 N N   . GLU A 207 ? 0.8493 0.5816 0.4727 0.0204  -0.0183 -0.0382 223 GLU A N   
1632 C CA  . GLU A 207 ? 0.9118 0.6433 0.5148 0.0204  -0.0336 -0.0254 223 GLU A CA  
1633 C C   . GLU A 207 ? 0.8526 0.5973 0.4905 0.0241  -0.0494 -0.0180 223 GLU A C   
1634 O O   . GLU A 207 ? 0.8829 0.6340 0.5532 0.0273  -0.0425 -0.0139 223 GLU A O   
1635 C CB  . GLU A 207 ? 0.8608 0.5843 0.4446 0.0213  -0.0216 -0.0116 223 GLU A CB  
1636 C CG  . GLU A 207 ? 1.0043 0.7157 0.5490 0.0176  -0.0055 -0.0176 223 GLU A CG  
1637 C CD  . GLU A 207 ? 0.9897 0.6936 0.5177 0.0171  0.0089  -0.0030 223 GLU A CD  
1638 O OE1 . GLU A 207 ? 1.0442 0.7494 0.5893 0.0194  0.0052  0.0118  223 GLU A OE1 
1639 O OE2 . GLU A 207 ? 1.1354 0.8311 0.6332 0.0141  0.0253  -0.0069 223 GLU A OE2 
1640 N N   . ILE A 208 ? 0.8163 0.5668 0.4480 0.0233  -0.0703 -0.0168 224 ILE A N   
1641 C CA  . ILE A 208 ? 0.9077 0.6729 0.5727 0.0274  -0.0850 -0.0100 224 ILE A CA  
1642 C C   . ILE A 208 ? 0.8905 0.6566 0.5402 0.0317  -0.0996 0.0055  224 ILE A C   
1643 O O   . ILE A 208 ? 0.8881 0.6501 0.5025 0.0290  -0.1092 0.0066  224 ILE A O   
1644 C CB  . ILE A 208 ? 0.9119 0.6884 0.5943 0.0233  -0.0978 -0.0217 224 ILE A CB  
1645 C CG1 . ILE A 208 ? 0.9718 0.7433 0.6646 0.0195  -0.0839 -0.0365 224 ILE A CG1 
1646 C CG2 . ILE A 208 ? 0.8409 0.6349 0.5629 0.0280  -0.1081 -0.0147 224 ILE A CG2 
1647 C CD1 . ILE A 208 ? 0.9953 0.7767 0.7127 0.0151  -0.0945 -0.0456 224 ILE A CD1 
1648 N N   . GLN A 209 ? 0.8633 0.6348 0.5394 0.0389  -0.1017 0.0173  225 GLN A N   
1649 C CA  . GLN A 209 ? 0.8825 0.6577 0.5558 0.0457  -0.1176 0.0325  225 GLN A CA  
1650 C C   . GLN A 209 ? 0.8250 0.6175 0.5418 0.0516  -0.1263 0.0341  225 GLN A C   
1651 O O   . GLN A 209 ? 0.7886 0.5852 0.5346 0.0514  -0.1160 0.0277  225 GLN A O   
1652 C CB  . GLN A 209 ? 0.9621 0.7204 0.6206 0.0505  -0.1083 0.0483  225 GLN A CB  
1653 C CG  . GLN A 209 ? 1.0618 0.8028 0.6838 0.0447  -0.0926 0.0478  225 GLN A CG  
1654 C CD  . GLN A 209 ? 1.2911 1.0154 0.9036 0.0484  -0.0832 0.0649  225 GLN A CD  
1655 O OE1 . GLN A 209 ? 1.2762 0.9989 0.8985 0.0564  -0.0930 0.0788  225 GLN A OE1 
1656 N NE2 . GLN A 209 ? 1.3669 1.0782 0.9623 0.0427  -0.0632 0.0642  225 GLN A NE2 
1657 N N   . GLU A 210 ? 0.8275 0.6314 0.5481 0.0575  -0.1452 0.0436  226 GLU A N   
1658 C CA  . GLU A 210 ? 0.8017 0.6236 0.5630 0.0647  -0.1533 0.0467  226 GLU A CA  
1659 C C   . GLU A 210 ? 0.8683 0.6854 0.6319 0.0771  -0.1585 0.0651  226 GLU A C   
1660 O O   . GLU A 210 ? 0.7991 0.6080 0.5326 0.0797  -0.1667 0.0765  226 GLU A O   
1661 C CB  . GLU A 210 ? 0.8312 0.6769 0.6044 0.0608  -0.1724 0.0404  226 GLU A CB  
1662 C CG  . GLU A 210 ? 0.8289 0.6777 0.6054 0.0489  -0.1676 0.0224  226 GLU A CG  
1663 C CD  . GLU A 210 ? 0.8027 0.6764 0.6049 0.0447  -0.1835 0.0165  226 GLU A CD  
1664 O OE1 . GLU A 210 ? 0.7231 0.6153 0.5395 0.0509  -0.1998 0.0261  226 GLU A OE1 
1665 O OE2 . GLU A 210 ? 0.8626 0.7377 0.6727 0.0352  -0.1791 0.0027  226 GLU A OE2 
1666 N N   . ILE A 211 ? 0.8235 0.6446 0.6214 0.0852  -0.1534 0.0681  227 ILE A N   
1667 C CA  . ILE A 211 ? 0.8188 0.6369 0.6267 0.0991  -0.1593 0.0843  227 ILE A CA  
1668 C C   . ILE A 211 ? 0.7869 0.6314 0.6367 0.1059  -0.1682 0.0821  227 ILE A C   
1669 O O   . ILE A 211 ? 0.7466 0.5951 0.6240 0.1061  -0.1567 0.0739  227 ILE A O   
1670 C CB  . ILE A 211 ? 0.8854 0.6781 0.6936 0.1032  -0.1413 0.0899  227 ILE A CB  
1671 C CG1 . ILE A 211 ? 0.9291 0.6992 0.7019 0.0936  -0.1283 0.0893  227 ILE A CG1 
1672 C CG2 . ILE A 211 ? 0.8149 0.5988 0.6281 0.1183  -0.1480 0.1081  227 ILE A CG2 
1673 C CD1 . ILE A 211 ? 0.9112 0.6673 0.6453 0.0958  -0.1358 0.1048  227 ILE A CD1 
1674 N N   . ASN A 212 ? 0.7393 0.6038 0.5939 0.1110  -0.1885 0.0894  228 ASN A N   
1675 C CA  . ASN A 212 ? 0.7716 0.6646 0.6686 0.1190  -0.1975 0.0898  228 ASN A CA  
1676 C C   . ASN A 212 ? 0.7976 0.6844 0.7041 0.1372  -0.2011 0.1076  228 ASN A C   
1677 O O   . ASN A 212 ? 0.8534 0.7475 0.7506 0.1445  -0.2187 0.1213  228 ASN A O   
1678 C CB  . ASN A 212 ? 0.8167 0.7390 0.7176 0.1121  -0.2182 0.0860  228 ASN A CB  
1679 C CG  . ASN A 212 ? 0.7848 0.7403 0.7336 0.1172  -0.2249 0.0844  228 ASN A CG  
1680 O OD1 . ASN A 212 ? 0.7660 0.7243 0.7427 0.1309  -0.2187 0.0909  228 ASN A OD1 
1681 N ND2 . ASN A 212 ? 0.7591 0.7396 0.7179 0.1056  -0.2368 0.0750  228 ASN A ND2 
1682 N N   . ALA A 213 ? 0.7975 0.6697 0.7221 0.1447  -0.1843 0.1073  229 ALA A N   
1683 C CA  . ALA A 213 ? 0.7842 0.6393 0.7128 0.1615  -0.1829 0.1232  229 ALA A CA  
1684 C C   . ALA A 213 ? 0.8381 0.7200 0.7936 0.1769  -0.2014 0.1352  229 ALA A C   
1685 O O   . ALA A 213 ? 0.8090 0.6824 0.7531 0.1891  -0.2119 0.1535  229 ALA A O   
1686 C CB  . ALA A 213 ? 0.7302 0.5677 0.6772 0.1651  -0.1617 0.1162  229 ALA A CB  
1687 N N   . ALA A 214 ? 0.8026 0.7185 0.7949 0.1768  -0.2057 0.1262  230 ALA A N   
1688 C CA  . ALA A 214 ? 0.8327 0.7793 0.8587 0.1920  -0.2217 0.1369  230 ALA A CA  
1689 C C   . ALA A 214 ? 0.8052 0.7759 0.8182 0.1879  -0.2478 0.1444  230 ALA A C   
1690 O O   . ALA A 214 ? 0.8587 0.8463 0.8861 0.2029  -0.2643 0.1603  230 ALA A O   
1691 C CB  . ALA A 214 ? 0.7733 0.7494 0.8453 0.1927  -0.2150 0.1250  230 ALA A CB  
1692 N N   . ASN A 215 ? 0.8347 0.8077 0.8210 0.1680  -0.2524 0.1330  231 ASN A N   
1693 C CA  . ASN A 215 ? 0.8919 0.8856 0.8598 0.1608  -0.2772 0.1367  231 ASN A CA  
1694 C C   . ASN A 215 ? 0.9127 0.8786 0.8262 0.1458  -0.2740 0.1314  231 ASN A C   
1695 O O   . ASN A 215 ? 0.8762 0.8436 0.7806 0.1284  -0.2694 0.1140  231 ASN A O   
1696 C CB  . ASN A 215 ? 0.9156 0.9497 0.9156 0.1501  -0.2880 0.1242  231 ASN A CB  
1697 C CG  . ASN A 215 ? 0.9508 1.0165 1.0067 0.1643  -0.2897 0.1289  231 ASN A CG  
1698 O OD1 . ASN A 215 ? 0.9194 1.0145 0.9955 0.1748  -0.3099 0.1415  231 ASN A OD1 
1699 N ND2 . ASN A 215 ? 0.7577 0.8195 0.8394 0.1650  -0.2683 0.1190  231 ASN A ND2 
1700 N N   . SER A 216 ? 0.9504 0.8919 0.8279 0.1528  -0.2767 0.1472  232 SER A N   
1701 C CA  . SER A 216 ? 1.0067 0.9170 0.8332 0.1406  -0.2669 0.1432  232 SER A CA  
1702 C C   . SER A 216 ? 1.0798 1.0025 0.8784 0.1229  -0.2796 0.1308  232 SER A C   
1703 O O   . SER A 216 ? 1.0252 0.9266 0.7909 0.1101  -0.2669 0.1198  232 SER A O   
1704 C CB  . SER A 216 ? 0.9658 0.8494 0.7595 0.1517  -0.2681 0.1650  232 SER A CB  
1705 O OG  . SER A 216 ? 1.1244 1.0276 0.9093 0.1595  -0.2945 0.1810  232 SER A OG  
1706 N N   . LYS A 217 ? 1.2291 1.1860 1.0408 0.1214  -0.3038 0.1311  233 LYS A N   
1707 C CA  . LYS A 217 ? 1.2128 1.1785 0.9954 0.1032  -0.3160 0.1175  233 LYS A CA  
1708 C C   . LYS A 217 ? 1.2172 1.1982 1.0272 0.0884  -0.3109 0.0949  233 LYS A C   
1709 O O   . LYS A 217 ? 1.2524 1.2306 1.0363 0.0717  -0.3140 0.0796  233 LYS A O   
1710 C CB  . LYS A 217 ? 1.2569 1.2501 1.0309 0.1063  -0.3475 0.1294  233 LYS A CB  
1711 C CG  . LYS A 217 ? 1.3383 1.3104 1.0634 0.1146  -0.3539 0.1494  233 LYS A CG  
1712 C CD  . LYS A 217 ? 1.4772 1.4762 1.2141 0.1302  -0.3814 0.1721  233 LYS A CD  
1713 C CE  . LYS A 217 ? 1.4915 1.4868 1.2691 0.1532  -0.3728 0.1899  233 LYS A CE  
1714 N NZ  . LYS A 217 ? 1.3082 1.3245 1.0949 0.1718  -0.3977 0.2154  233 LYS A NZ  
1715 N N   . GLN A 218 ? 1.0072 1.0013 0.8668 0.0940  -0.3012 0.0921  234 GLN A N   
1716 C CA  . GLN A 218 ? 0.9481 0.9616 0.8359 0.0802  -0.3003 0.0741  234 GLN A CA  
1717 C C   . GLN A 218 ? 0.9059 0.8920 0.7803 0.0693  -0.2763 0.0582  234 GLN A C   
1718 O O   . GLN A 218 ? 0.8246 0.7908 0.7037 0.0770  -0.2560 0.0609  234 GLN A O   
1719 C CB  . GLN A 218 ? 0.8907 0.9331 0.8364 0.0897  -0.3000 0.0779  234 GLN A CB  
1720 C CG  . GLN A 218 ? 1.0648 1.1461 1.0348 0.0966  -0.3265 0.0893  234 GLN A CG  
1721 C CD  . GLN A 218 ? 1.0716 1.1864 1.1024 0.1026  -0.3247 0.0893  234 GLN A CD  
1722 O OE1 . GLN A 218 ? 1.0464 1.1561 1.0979 0.0984  -0.3048 0.0788  234 GLN A OE1 
1723 N NE2 . GLN A 218 ? 1.0284 1.1790 1.0881 0.1130  -0.3452 0.1019  234 GLN A NE2 
1724 N N   . PRO A 219 ? 0.8770 0.8614 0.7356 0.0517  -0.2783 0.0415  235 PRO A N   
1725 C CA  . PRO A 219 ? 0.8786 0.8429 0.7359 0.0427  -0.2563 0.0266  235 PRO A CA  
1726 C C   . PRO A 219 ? 0.7819 0.7570 0.6860 0.0483  -0.2434 0.0267  235 PRO A C   
1727 O O   . PRO A 219 ? 0.7954 0.7999 0.7375 0.0514  -0.2532 0.0303  235 PRO A O   
1728 C CB  . PRO A 219 ? 0.8941 0.8634 0.7407 0.0241  -0.2657 0.0095  235 PRO A CB  
1729 C CG  . PRO A 219 ? 0.9202 0.9186 0.7695 0.0222  -0.2941 0.0148  235 PRO A CG  
1730 C CD  . PRO A 219 ? 0.9559 0.9562 0.7966 0.0394  -0.3014 0.0353  235 PRO A CD  
1731 N N   . ILE A 220 ? 0.6901 0.6427 0.5909 0.0497  -0.2211 0.0228  236 ILE A N   
1732 C CA  . ILE A 220 ? 0.7540 0.7130 0.6917 0.0563  -0.2071 0.0240  236 ILE A CA  
1733 C C   . ILE A 220 ? 0.6819 0.6527 0.6432 0.0443  -0.2034 0.0115  236 ILE A C   
1734 O O   . ILE A 220 ? 0.6510 0.6054 0.5951 0.0336  -0.1956 0.0004  236 ILE A O   
1735 C CB  . ILE A 220 ? 0.6835 0.6153 0.6073 0.0622  -0.1867 0.0258  236 ILE A CB  
1736 C CG1 . ILE A 220 ? 0.6690 0.5907 0.5794 0.0754  -0.1895 0.0408  236 ILE A CG1 
1737 C CG2 . ILE A 220 ? 0.6104 0.5469 0.5660 0.0642  -0.1712 0.0219  236 ILE A CG2 
1738 C CD1 . ILE A 220 ? 0.6735 0.5662 0.5645 0.0783  -0.1711 0.0427  236 ILE A CD1 
1739 N N   . HIS A 221 ? 0.6599 0.6586 0.6612 0.0466  -0.2080 0.0141  237 HIS A N   
1740 C CA  . HIS A 221 ? 0.6468 0.6587 0.6753 0.0359  -0.2033 0.0052  237 HIS A CA  
1741 C C   . HIS A 221 ? 0.6125 0.6338 0.6731 0.0453  -0.1888 0.0097  237 HIS A C   
1742 O O   . HIS A 221 ? 0.6200 0.6447 0.6887 0.0598  -0.1873 0.0190  237 HIS A O   
1743 C CB  . HIS A 221 ? 0.6179 0.6599 0.6670 0.0266  -0.2229 0.0033  237 HIS A CB  
1744 C CG  . HIS A 221 ? 0.7880 0.8223 0.8047 0.0148  -0.2385 -0.0038 237 HIS A CG  
1745 N ND1 . HIS A 221 ? 0.8150 0.8424 0.8252 -0.0031 -0.2392 -0.0179 237 HIS A ND1 
1746 C CD2 . HIS A 221 ? 0.8203 0.8523 0.8080 0.0180  -0.2539 0.0011  237 HIS A CD2 
1747 C CE1 . HIS A 221 ? 0.8284 0.8490 0.8057 -0.0107 -0.2539 -0.0234 237 HIS A CE1 
1748 N NE2 . HIS A 221 ? 0.7832 0.8077 0.7454 0.0017  -0.2634 -0.0115 237 HIS A NE2 
1749 N N   . MET A 222 ? 0.5938 0.6182 0.6716 0.0370  -0.1779 0.0031  238 MET A N   
1750 C CA  . MET A 222 ? 0.5919 0.6263 0.6973 0.0441  -0.1636 0.0061  238 MET A CA  
1751 C C   . MET A 222 ? 0.6183 0.6665 0.7471 0.0315  -0.1593 0.0007  238 MET A C   
1752 O O   . MET A 222 ? 0.5953 0.6375 0.7155 0.0175  -0.1647 -0.0064 238 MET A O   
1753 C CB  . MET A 222 ? 0.4995 0.5081 0.5863 0.0503  -0.1463 0.0056  238 MET A CB  
1754 C CG  . MET A 222 ? 0.5604 0.5503 0.6312 0.0394  -0.1372 -0.0023 238 MET A CG  
1755 S SD  . MET A 222 ? 0.6250 0.5905 0.6778 0.0451  -0.1185 -0.0030 238 MET A SD  
1756 C CE  . MET A 222 ? 0.5212 0.5036 0.6021 0.0554  -0.1089 0.0017  238 MET A CE  
1757 N N   . VAL A 223 ? 0.6091 0.6734 0.7660 0.0364  -0.1483 0.0040  239 VAL A N   
1758 C CA  . VAL A 223 ? 0.5480 0.6206 0.7237 0.0254  -0.1392 0.0009  239 VAL A CA  
1759 C C   . VAL A 223 ? 0.5519 0.5988 0.7078 0.0256  -0.1227 -0.0016 239 VAL A C   
1760 O O   . VAL A 223 ? 0.5501 0.5912 0.7015 0.0367  -0.1124 0.0011  239 VAL A O   
1761 C CB  . VAL A 223 ? 0.5383 0.6436 0.7535 0.0300  -0.1343 0.0060  239 VAL A CB  
1762 C CG1 . VAL A 223 ? 0.5174 0.6298 0.7494 0.0168  -0.1248 0.0042  239 VAL A CG1 
1763 C CG2 . VAL A 223 ? 0.4799 0.6157 0.7195 0.0323  -0.1518 0.0099  239 VAL A CG2 
1764 N N   . TYR A 224 ? 0.5356 0.5668 0.6804 0.0135  -0.1204 -0.0068 240 TYR A N   
1765 C CA  . TYR A 224 ? 0.5414 0.5512 0.6702 0.0146  -0.1059 -0.0077 240 TYR A CA  
1766 C C   . TYR A 224 ? 0.5437 0.5434 0.6734 0.0013  -0.1025 -0.0112 240 TYR A C   
1767 O O   . TYR A 224 ? 0.5514 0.5589 0.6935 -0.0102 -0.1108 -0.0141 240 TYR A O   
1768 C CB  . TYR A 224 ? 0.5276 0.5137 0.6250 0.0215  -0.1055 -0.0097 240 TYR A CB  
1769 C CG  . TYR A 224 ? 0.5453 0.5197 0.6341 0.0272  -0.0908 -0.0083 240 TYR A CG  
1770 C CD1 . TYR A 224 ? 0.5309 0.5157 0.6296 0.0362  -0.0835 -0.0044 240 TYR A CD1 
1771 C CD2 . TYR A 224 ? 0.5248 0.4790 0.5966 0.0236  -0.0845 -0.0113 240 TYR A CD2 
1772 C CE1 . TYR A 224 ? 0.5100 0.4862 0.6000 0.0397  -0.0718 -0.0041 240 TYR A CE1 
1773 C CE2 . TYR A 224 ? 0.5066 0.4545 0.5730 0.0284  -0.0730 -0.0093 240 TYR A CE2 
1774 C CZ  . TYR A 224 ? 0.5215 0.4811 0.5962 0.0356  -0.0675 -0.0060 240 TYR A CZ  
1775 O OH  . TYR A 224 ? 0.5477 0.5029 0.6158 0.0390  -0.0578 -0.0050 240 TYR A OH  
1776 N N   . VAL A 225 ? 0.4776 0.4601 0.5958 0.0028  -0.0903 -0.0105 241 VAL A N   
1777 C CA  . VAL A 225 ? 0.4875 0.4536 0.6027 -0.0066 -0.0850 -0.0124 241 VAL A CA  
1778 C C   . VAL A 225 ? 0.5169 0.4561 0.6040 -0.0060 -0.0867 -0.0192 241 VAL A C   
1779 O O   . VAL A 225 ? 0.5237 0.4515 0.5958 0.0022  -0.0792 -0.0180 241 VAL A O   
1780 C CB  . VAL A 225 ? 0.5527 0.5189 0.6736 -0.0036 -0.0707 -0.0054 241 VAL A CB  
1781 C CG1 . VAL A 225 ? 0.5085 0.4543 0.6263 -0.0118 -0.0653 -0.0055 241 VAL A CG1 
1782 C CG2 . VAL A 225 ? 0.5422 0.5357 0.6888 -0.0039 -0.0666 0.0010  241 VAL A CG2 
1783 N N   . PRO A 226 ? 0.5553 0.4853 0.6343 -0.0148 -0.0962 -0.0271 242 PRO A N   
1784 C CA  . PRO A 226 ? 0.5242 0.4312 0.5736 -0.0126 -0.0974 -0.0342 242 PRO A CA  
1785 C C   . PRO A 226 ? 0.5204 0.4045 0.5597 -0.0105 -0.0845 -0.0353 242 PRO A C   
1786 O O   . PRO A 226 ? 0.5356 0.4059 0.5541 -0.0040 -0.0806 -0.0380 242 PRO A O   
1787 C CB  . PRO A 226 ? 0.5624 0.4662 0.6057 -0.0244 -0.1107 -0.0435 242 PRO A CB  
1788 C CG  . PRO A 226 ? 0.5515 0.4733 0.6252 -0.0353 -0.1146 -0.0415 242 PRO A CG  
1789 C CD  . PRO A 226 ? 0.4964 0.4409 0.5921 -0.0266 -0.1078 -0.0302 242 PRO A CD  
1790 N N   . SER A 227 ? 0.5128 0.3934 0.5674 -0.0150 -0.0772 -0.0319 243 SER A N   
1791 C CA  . SER A 227 ? 0.5329 0.3925 0.5798 -0.0108 -0.0656 -0.0311 243 SER A CA  
1792 C C   . SER A 227 ? 0.5688 0.4357 0.6125 0.0017  -0.0581 -0.0237 243 SER A C   
1793 O O   . SER A 227 ? 0.5629 0.4159 0.5946 0.0079  -0.0513 -0.0249 243 SER A O   
1794 C CB  . SER A 227 ? 0.5536 0.4066 0.6175 -0.0181 -0.0599 -0.0268 243 SER A CB  
1795 O OG  . SER A 227 ? 0.6825 0.5578 0.7656 -0.0172 -0.0571 -0.0159 243 SER A OG  
1796 N N   . HIS A 228 ? 0.5384 0.4274 0.5937 0.0052  -0.0587 -0.0168 244 HIS A N   
1797 C CA  . HIS A 228 ? 0.5222 0.4177 0.5724 0.0153  -0.0529 -0.0121 244 HIS A CA  
1798 C C   . HIS A 228 ? 0.5775 0.4664 0.6091 0.0201  -0.0557 -0.0173 244 HIS A C   
1799 O O   . HIS A 228 ? 0.5520 0.4353 0.5744 0.0260  -0.0495 -0.0167 244 HIS A O   
1800 C CB  . HIS A 228 ? 0.5112 0.4295 0.5752 0.0177  -0.0526 -0.0062 244 HIS A CB  
1801 C CG  . HIS A 228 ? 0.5285 0.4553 0.6086 0.0138  -0.0471 0.0010  244 HIS A CG  
1802 N ND1 . HIS A 228 ? 0.5111 0.4581 0.6027 0.0159  -0.0437 0.0062  244 HIS A ND1 
1803 C CD2 . HIS A 228 ? 0.5940 0.5104 0.6797 0.0080  -0.0432 0.0042  244 HIS A CD2 
1804 C CE1 . HIS A 228 ? 0.5437 0.4941 0.6461 0.0110  -0.0379 0.0130  244 HIS A CE1 
1805 N NE2 . HIS A 228 ? 0.5638 0.4951 0.6635 0.0061  -0.0378 0.0127  244 HIS A NE2 
1806 N N   . LEU A 229 ? 0.5328 0.4244 0.5595 0.0174  -0.0653 -0.0214 245 LEU A N   
1807 C CA  . LEU A 229 ? 0.5470 0.4317 0.5539 0.0217  -0.0677 -0.0244 245 LEU A CA  
1808 C C   . LEU A 229 ? 0.5439 0.4077 0.5323 0.0206  -0.0632 -0.0308 245 LEU A C   
1809 O O   . LEU A 229 ? 0.5531 0.4104 0.5280 0.0258  -0.0577 -0.0311 245 LEU A O   
1810 C CB  . LEU A 229 ? 0.5568 0.4497 0.5621 0.0196  -0.0803 -0.0256 245 LEU A CB  
1811 C CG  . LEU A 229 ? 0.6139 0.4994 0.5967 0.0232  -0.0851 -0.0267 245 LEU A CG  
1812 C CD1 . LEU A 229 ? 0.5362 0.4223 0.5162 0.0317  -0.0783 -0.0215 245 LEU A CD1 
1813 C CD2 . LEU A 229 ? 0.5901 0.4871 0.5748 0.0212  -0.1000 -0.0260 245 LEU A CD2 
1814 N N   . TYR A 230 ? 0.5460 0.3988 0.5348 0.0138  -0.0642 -0.0364 246 TYR A N   
1815 C CA  . TYR A 230 ? 0.6168 0.4479 0.5898 0.0139  -0.0573 -0.0435 246 TYR A CA  
1816 C C   . TYR A 230 ? 0.6130 0.4420 0.5913 0.0220  -0.0449 -0.0385 246 TYR A C   
1817 O O   . TYR A 230 ? 0.6145 0.4353 0.5796 0.0269  -0.0382 -0.0413 246 TYR A O   
1818 C CB  . TYR A 230 ? 0.5555 0.3727 0.5309 0.0046  -0.0596 -0.0508 246 TYR A CB  
1819 C CG  . TYR A 230 ? 0.6754 0.4669 0.6354 0.0055  -0.0508 -0.0597 246 TYR A CG  
1820 C CD1 . TYR A 230 ? 0.6869 0.4698 0.6565 0.0122  -0.0385 -0.0558 246 TYR A CD1 
1821 C CD2 . TYR A 230 ? 0.6913 0.4677 0.6269 0.0004  -0.0545 -0.0720 246 TYR A CD2 
1822 C CE1 . TYR A 230 ? 0.6949 0.4546 0.6532 0.0151  -0.0290 -0.0638 246 TYR A CE1 
1823 C CE2 . TYR A 230 ? 0.7180 0.4699 0.6389 0.0020  -0.0443 -0.0816 246 TYR A CE2 
1824 C CZ  . TYR A 230 ? 0.7656 0.5092 0.6997 0.0101  -0.0310 -0.0774 246 TYR A CZ  
1825 O OH  . TYR A 230 ? 0.7358 0.4557 0.6588 0.0139  -0.0195 -0.0866 246 TYR A OH  
1826 N N   . HIS A 231 ? 0.5893 0.4276 0.5872 0.0235  -0.0418 -0.0306 247 HIS A N   
1827 C CA  . HIS A 231 ? 0.6212 0.4609 0.6254 0.0312  -0.0322 -0.0246 247 HIS A CA  
1828 C C   . HIS A 231 ? 0.6046 0.4535 0.6016 0.0370  -0.0298 -0.0232 247 HIS A C   
1829 O O   . HIS A 231 ? 0.5802 0.4249 0.5738 0.0423  -0.0222 -0.0237 247 HIS A O   
1830 C CB  . HIS A 231 ? 0.6293 0.4819 0.6520 0.0315  -0.0312 -0.0146 247 HIS A CB  
1831 C CG  . HIS A 231 ? 0.7283 0.5710 0.7607 0.0254  -0.0311 -0.0134 247 HIS A CG  
1832 N ND1 . HIS A 231 ? 0.8170 0.6361 0.8445 0.0230  -0.0282 -0.0199 247 HIS A ND1 
1833 C CD2 . HIS A 231 ? 0.6631 0.5149 0.7100 0.0204  -0.0324 -0.0065 247 HIS A CD2 
1834 C CE1 . HIS A 231 ? 0.7821 0.5949 0.8213 0.0161  -0.0284 -0.0169 247 HIS A CE1 
1835 N NE2 . HIS A 231 ? 0.7456 0.5791 0.7970 0.0142  -0.0308 -0.0082 247 HIS A NE2 
1836 N N   . MET A 232 ? 0.5323 0.3941 0.5290 0.0363  -0.0354 -0.0212 248 MET A N   
1837 C CA  . MET A 232 ? 0.5788 0.4468 0.5694 0.0403  -0.0329 -0.0198 248 MET A CA  
1838 C C   . MET A 232 ? 0.6137 0.4688 0.5855 0.0405  -0.0303 -0.0255 248 MET A C   
1839 O O   . MET A 232 ? 0.5784 0.4335 0.5474 0.0437  -0.0228 -0.0252 248 MET A O   
1840 C CB  . MET A 232 ? 0.5491 0.4287 0.5426 0.0399  -0.0388 -0.0173 248 MET A CB  
1841 C CG  . MET A 232 ? 0.5749 0.4684 0.5849 0.0396  -0.0397 -0.0125 248 MET A CG  
1842 S SD  . MET A 232 ? 0.6009 0.5060 0.6141 0.0414  -0.0442 -0.0113 248 MET A SD  
1843 C CE  . MET A 232 ? 0.5429 0.4493 0.5606 0.0376  -0.0538 -0.0128 248 MET A CE  
1844 N N   . LEU A 233 ? 0.5959 0.4418 0.5545 0.0365  -0.0367 -0.0305 249 LEU A N   
1845 C CA  . LEU A 233 ? 0.6588 0.4920 0.5947 0.0361  -0.0344 -0.0357 249 LEU A CA  
1846 C C   . LEU A 233 ? 0.5739 0.3953 0.5058 0.0382  -0.0237 -0.0409 249 LEU A C   
1847 O O   . LEU A 233 ? 0.6042 0.4220 0.5256 0.0409  -0.0152 -0.0422 249 LEU A O   
1848 C CB  . LEU A 233 ? 0.5968 0.4239 0.5183 0.0307  -0.0454 -0.0402 249 LEU A CB  
1849 C CG  . LEU A 233 ? 0.6179 0.4569 0.5421 0.0314  -0.0552 -0.0340 249 LEU A CG  
1850 C CD1 . LEU A 233 ? 0.6387 0.4792 0.5584 0.0261  -0.0689 -0.0368 249 LEU A CD1 
1851 C CD2 . LEU A 233 ? 0.6016 0.4367 0.5096 0.0347  -0.0520 -0.0305 249 LEU A CD2 
1852 N N   . PHE A 234 ? 0.5662 0.3807 0.5074 0.0371  -0.0228 -0.0437 250 PHE A N   
1853 C CA  . PHE A 234 ? 0.6284 0.4296 0.5682 0.0410  -0.0117 -0.0486 250 PHE A CA  
1854 C C   . PHE A 234 ? 0.6372 0.4499 0.5897 0.0489  -0.0020 -0.0423 250 PHE A C   
1855 O O   . PHE A 234 ? 0.5806 0.3883 0.5266 0.0530  0.0084  -0.0459 250 PHE A O   
1856 C CB  . PHE A 234 ? 0.6176 0.4084 0.5693 0.0392  -0.0122 -0.0502 250 PHE A CB  
1857 C CG  . PHE A 234 ? 0.6328 0.4071 0.5855 0.0450  -0.0001 -0.0549 250 PHE A CG  
1858 C CD1 . PHE A 234 ? 0.6498 0.4050 0.5810 0.0442  0.0057  -0.0671 250 PHE A CD1 
1859 C CD2 . PHE A 234 ? 0.6619 0.4394 0.6362 0.0520  0.0059  -0.0468 250 PHE A CD2 
1860 C CE1 . PHE A 234 ? 0.6506 0.3889 0.5838 0.0510  0.0187  -0.0725 250 PHE A CE1 
1861 C CE2 . PHE A 234 ? 0.7233 0.4850 0.7011 0.0595  0.0174  -0.0502 250 PHE A CE2 
1862 C CZ  . PHE A 234 ? 0.7175 0.4592 0.6760 0.0594  0.0245  -0.0636 250 PHE A CZ  
1863 N N   . GLU A 235 ? 0.6240 0.4539 0.5949 0.0505  -0.0051 -0.0332 251 GLU A N   
1864 C CA  . GLU A 235 ? 0.6225 0.4674 0.6067 0.0564  0.0014  -0.0271 251 GLU A CA  
1865 C C   . GLU A 235 ? 0.6104 0.4607 0.5846 0.0555  0.0051  -0.0283 251 GLU A C   
1866 O O   . GLU A 235 ? 0.5759 0.4313 0.5550 0.0596  0.0145  -0.0281 251 GLU A O   
1867 C CB  . GLU A 235 ? 0.5577 0.4197 0.5582 0.0563  -0.0045 -0.0183 251 GLU A CB  
1868 C CG  . GLU A 235 ? 0.6393 0.5186 0.6545 0.0616  -0.0002 -0.0119 251 GLU A CG  
1869 C CD  . GLU A 235 ? 0.7037 0.5791 0.7307 0.0694  0.0068  -0.0093 251 GLU A CD  
1870 O OE1 . GLU A 235 ? 0.7070 0.5665 0.7346 0.0702  0.0070  -0.0098 251 GLU A OE1 
1871 O OE2 . GLU A 235 ? 0.7750 0.6632 0.8120 0.0746  0.0123  -0.0067 251 GLU A OE2 
1872 N N   . LEU A 236 ? 0.5385 0.3882 0.5004 0.0505  -0.0017 -0.0287 252 LEU A N   
1873 C CA  . LEU A 236 ? 0.5663 0.4170 0.5168 0.0488  0.0022  -0.0287 252 LEU A CA  
1874 C C   . LEU A 236 ? 0.5819 0.4191 0.5145 0.0494  0.0112  -0.0348 252 LEU A C   
1875 O O   . LEU A 236 ? 0.5928 0.4345 0.5255 0.0505  0.0212  -0.0341 252 LEU A O   
1876 C CB  . LEU A 236 ? 0.5421 0.3913 0.4827 0.0448  -0.0071 -0.0267 252 LEU A CB  
1877 C CG  . LEU A 236 ? 0.6018 0.4651 0.5594 0.0449  -0.0127 -0.0217 252 LEU A CG  
1878 C CD1 . LEU A 236 ? 0.4731 0.3343 0.4245 0.0432  -0.0214 -0.0202 252 LEU A CD1 
1879 C CD2 . LEU A 236 ? 0.5322 0.4077 0.5002 0.0449  -0.0066 -0.0190 252 LEU A CD2 
1880 N N   . PHE A 237 ? 0.5692 0.3904 0.4858 0.0477  0.0081  -0.0414 253 PHE A N   
1881 C CA  . PHE A 237 ? 0.6157 0.4222 0.5106 0.0479  0.0171  -0.0491 253 PHE A CA  
1882 C C   . PHE A 237 ? 0.6796 0.4879 0.5877 0.0547  0.0316  -0.0513 253 PHE A C   
1883 O O   . PHE A 237 ? 0.6583 0.4648 0.5566 0.0563  0.0438  -0.0541 253 PHE A O   
1884 C CB  . PHE A 237 ? 0.6268 0.4161 0.5038 0.0440  0.0100  -0.0577 253 PHE A CB  
1885 C CG  . PHE A 237 ? 0.5867 0.3723 0.4409 0.0381  -0.0013 -0.0573 253 PHE A CG  
1886 C CD1 . PHE A 237 ? 0.6634 0.4462 0.4954 0.0372  0.0029  -0.0553 253 PHE A CD1 
1887 C CD2 . PHE A 237 ? 0.5817 0.3679 0.4380 0.0337  -0.0161 -0.0578 253 PHE A CD2 
1888 C CE1 . PHE A 237 ? 0.6737 0.4529 0.4839 0.0331  -0.0086 -0.0528 253 PHE A CE1 
1889 C CE2 . PHE A 237 ? 0.6150 0.4009 0.4528 0.0296  -0.0281 -0.0561 253 PHE A CE2 
1890 C CZ  . PHE A 237 ? 0.6387 0.4206 0.4529 0.0300  -0.0249 -0.0531 253 PHE A CZ  
1891 N N   . LYS A 238 ? 0.5903 0.4030 0.5214 0.0593  0.0311  -0.0491 254 LYS A N   
1892 C CA  . LYS A 238 ? 0.6470 0.4627 0.5943 0.0679  0.0439  -0.0495 254 LYS A CA  
1893 C C   . LYS A 238 ? 0.6484 0.4855 0.6087 0.0700  0.0512  -0.0434 254 LYS A C   
1894 O O   . LYS A 238 ? 0.6097 0.4483 0.5708 0.0744  0.0650  -0.0465 254 LYS A O   
1895 C CB  . LYS A 238 ? 0.7385 0.5557 0.7082 0.0725  0.0398  -0.0448 254 LYS A CB  
1896 C CG  . LYS A 238 ? 0.8841 0.7070 0.8757 0.0835  0.0506  -0.0418 254 LYS A CG  
1897 C CD  . LYS A 238 ? 0.9813 0.7970 0.9879 0.0873  0.0461  -0.0371 254 LYS A CD  
1898 C CE  . LYS A 238 ? 0.9844 0.8231 1.0097 0.0872  0.0367  -0.0242 254 LYS A CE  
1899 N NZ  . LYS A 238 ? 0.9673 0.7962 1.0026 0.0893  0.0325  -0.0187 254 LYS A NZ  
1900 N N   . ASN A 239 ? 0.5537 0.4078 0.5244 0.0661  0.0426  -0.0356 255 ASN A N   
1901 C CA  . ASN A 239 ? 0.5611 0.4357 0.5449 0.0655  0.0483  -0.0308 255 ASN A CA  
1902 C C   . ASN A 239 ? 0.5471 0.4152 0.5105 0.0604  0.0564  -0.0338 255 ASN A C   
1903 O O   . ASN A 239 ? 0.5865 0.4650 0.5579 0.0619  0.0689  -0.0335 255 ASN A O   
1904 C CB  . ASN A 239 ? 0.5508 0.4406 0.5456 0.0608  0.0371  -0.0241 255 ASN A CB  
1905 C CG  . ASN A 239 ? 0.6256 0.5305 0.6442 0.0661  0.0325  -0.0185 255 ASN A CG  
1906 O OD1 . ASN A 239 ? 0.6040 0.5285 0.6427 0.0698  0.0368  -0.0146 255 ASN A OD1 
1907 N ND2 . ASN A 239 ? 0.5715 0.4690 0.5885 0.0664  0.0237  -0.0172 255 ASN A ND2 
1908 N N   . ALA A 240 ? 0.5415 0.3934 0.4789 0.0547  0.0498  -0.0359 256 ALA A N   
1909 C CA  . ALA A 240 ? 0.6186 0.4632 0.5335 0.0497  0.0568  -0.0363 256 ALA A CA  
1910 C C   . ALA A 240 ? 0.6698 0.5043 0.5697 0.0530  0.0715  -0.0436 256 ALA A C   
1911 O O   . ALA A 240 ? 0.6331 0.4696 0.5242 0.0505  0.0838  -0.0426 256 ALA A O   
1912 C CB  . ALA A 240 ? 0.5899 0.4203 0.4808 0.0444  0.0445  -0.0352 256 ALA A CB  
1913 N N   . MET A 241 ? 0.6693 0.4913 0.5650 0.0580  0.0718  -0.0513 257 MET A N   
1914 C CA  . MET A 241 ? 0.6638 0.4732 0.5427 0.0615  0.0870  -0.0605 257 MET A CA  
1915 C C   . MET A 241 ? 0.6584 0.4844 0.5642 0.0693  0.1034  -0.0596 257 MET A C   
1916 O O   . MET A 241 ? 0.6953 0.5227 0.5924 0.0700  0.1197  -0.0623 257 MET A O   
1917 C CB  . MET A 241 ? 0.6821 0.4703 0.5486 0.0636  0.0826  -0.0707 257 MET A CB  
1918 C CG  . MET A 241 ? 0.7351 0.5090 0.5735 0.0554  0.0677  -0.0732 257 MET A CG  
1919 S SD  . MET A 241 ? 0.9266 0.6768 0.7539 0.0553  0.0629  -0.0867 257 MET A SD  
1920 C CE  . MET A 241 ? 0.7315 0.4747 0.5285 0.0445  0.0438  -0.0868 257 MET A CE  
1921 N N   . ARG A 242 ? 0.6233 0.4632 0.5622 0.0757  0.0996  -0.0551 258 ARG A N   
1922 C CA  . ARG A 242 ? 0.6781 0.5388 0.6477 0.0844  0.1126  -0.0522 258 ARG A CA  
1923 C C   . ARG A 242 ? 0.6817 0.5651 0.6607 0.0785  0.1188  -0.0458 258 ARG A C   
1924 O O   . ARG A 242 ? 0.6757 0.5705 0.6643 0.0822  0.1359  -0.0470 258 ARG A O   
1925 C CB  . ARG A 242 ? 0.6711 0.5443 0.6723 0.0913  0.1034  -0.0455 258 ARG A CB  
1926 C CG  . ARG A 242 ? 0.7367 0.6410 0.7753 0.0987  0.1103  -0.0381 258 ARG A CG  
1927 C CD  . ARG A 242 ? 0.7841 0.6974 0.8490 0.1069  0.1003  -0.0306 258 ARG A CD  
1928 N NE  . ARG A 242 ? 0.9108 0.8314 0.9755 0.0987  0.0825  -0.0239 258 ARG A NE  
1929 C CZ  . ARG A 242 ? 0.8986 0.8076 0.9601 0.0990  0.0708  -0.0216 258 ARG A CZ  
1930 N NH1 . ARG A 242 ? 0.9438 0.8316 1.0029 0.1063  0.0735  -0.0247 258 ARG A NH1 
1931 N NH2 . ARG A 242 ? 0.8566 0.7749 0.9178 0.0915  0.0570  -0.0162 258 ARG A NH2 
1932 N N   . ALA A 243 ? 0.6060 0.4951 0.5825 0.0688  0.1062  -0.0394 259 ALA A N   
1933 C CA  . ALA A 243 ? 0.6261 0.5322 0.6095 0.0608  0.1115  -0.0339 259 ALA A CA  
1934 C C   . ALA A 243 ? 0.6508 0.5440 0.6060 0.0562  0.1258  -0.0370 259 ALA A C   
1935 O O   . ALA A 243 ? 0.6328 0.5417 0.5990 0.0536  0.1401  -0.0346 259 ALA A O   
1936 C CB  . ALA A 243 ? 0.5804 0.4880 0.5624 0.0517  0.0954  -0.0281 259 ALA A CB  
1937 N N   . THR A 244 ? 0.5960 0.4622 0.5144 0.0545  0.1220  -0.0419 260 THR A N   
1938 C CA  . THR A 244 ? 0.6729 0.5262 0.5594 0.0499  0.1348  -0.0439 260 THR A CA  
1939 C C   . THR A 244 ? 0.7371 0.5937 0.6263 0.0575  0.1564  -0.0513 260 THR A C   
1940 O O   . THR A 244 ? 0.6844 0.5485 0.5699 0.0542  0.1734  -0.0494 260 THR A O   
1941 C CB  . THR A 244 ? 0.6595 0.4855 0.5052 0.0467  0.1237  -0.0474 260 THR A CB  
1942 O OG1 . THR A 244 ? 0.6732 0.4981 0.5194 0.0411  0.1054  -0.0400 260 THR A OG1 
1943 C CG2 . THR A 244 ? 0.7132 0.5256 0.5206 0.0420  0.1367  -0.0485 260 THR A CG2 
1944 N N   . VAL A 245 ? 0.7053 0.5558 0.6024 0.0678  0.1573  -0.0595 261 VAL A N   
1945 C CA  . VAL A 245 ? 0.7880 0.6385 0.6878 0.0771  0.1790  -0.0680 261 VAL A CA  
1946 C C   . VAL A 245 ? 0.8116 0.6957 0.7536 0.0813  0.1922  -0.0615 261 VAL A C   
1947 O O   . VAL A 245 ? 0.7787 0.6714 0.7197 0.0817  0.2129  -0.0630 261 VAL A O   
1948 C CB  . VAL A 245 ? 0.7944 0.6274 0.6956 0.0875  0.1764  -0.0779 261 VAL A CB  
1949 C CG1 . VAL A 245 ? 0.8327 0.6652 0.7408 0.0992  0.2005  -0.0871 261 VAL A CG1 
1950 C CG2 . VAL A 245 ? 0.7964 0.5983 0.6561 0.0813  0.1637  -0.0858 261 VAL A CG2 
1951 N N   . GLU A 246 ? 0.7498 0.6553 0.7294 0.0839  0.1801  -0.0538 262 GLU A N   
1952 C CA  . GLU A 246 ? 0.7852 0.7263 0.8088 0.0886  0.1898  -0.0479 262 GLU A CA  
1953 C C   . GLU A 246 ? 0.7860 0.7460 0.8134 0.0760  0.1974  -0.0414 262 GLU A C   
1954 O O   . GLU A 246 ? 0.8320 0.8184 0.8867 0.0785  0.2138  -0.0395 262 GLU A O   
1955 C CB  . GLU A 246 ? 0.7380 0.6969 0.7957 0.0933  0.1724  -0.0408 262 GLU A CB  
1956 C CG  . GLU A 246 ? 0.7447 0.6866 0.8049 0.1072  0.1693  -0.0456 262 GLU A CG  
1957 C CD  . GLU A 246 ? 0.7815 0.7431 0.8773 0.1143  0.1557  -0.0367 262 GLU A CD  
1958 O OE1 . GLU A 246 ? 0.8384 0.8191 0.9461 0.1058  0.1416  -0.0286 262 GLU A OE1 
1959 O OE2 . GLU A 246 ? 0.8555 0.8116 0.9655 0.1286  0.1594  -0.0379 262 GLU A OE2 
1960 N N   . SER A 247 ? 0.7279 0.6747 0.7301 0.0626  0.1867  -0.0376 263 SER A N   
1961 C CA  . SER A 247 ? 0.7453 0.7049 0.7493 0.0495  0.1948  -0.0310 263 SER A CA  
1962 C C   . SER A 247 ? 0.8204 0.7667 0.7935 0.0466  0.2161  -0.0339 263 SER A C   
1963 O O   . SER A 247 ? 0.8408 0.7969 0.8152 0.0355  0.2265  -0.0276 263 SER A O   
1964 C CB  . SER A 247 ? 0.7168 0.6648 0.7066 0.0373  0.1762  -0.0250 263 SER A CB  
1965 O OG  . SER A 247 ? 0.7318 0.6464 0.6763 0.0354  0.1718  -0.0275 263 SER A OG  
1966 N N   . HIS A 248 ? 0.8535 0.7767 0.7971 0.0551  0.2231  -0.0435 264 HIS A N   
1967 C CA  . HIS A 248 ? 0.9134 0.8218 0.8207 0.0526  0.2430  -0.0475 264 HIS A CA  
1968 C C   . HIS A 248 ? 0.9731 0.8852 0.8874 0.0662  0.2644  -0.0583 264 HIS A C   
1969 O O   . HIS A 248 ? 0.9575 0.8462 0.8322 0.0684  0.2758  -0.0676 264 HIS A O   
1970 C CB  . HIS A 248 ? 0.8794 0.7519 0.7329 0.0477  0.2315  -0.0502 264 HIS A CB  
1971 C CG  . HIS A 248 ? 0.9066 0.7728 0.7481 0.0350  0.2159  -0.0388 264 HIS A CG  
1972 N ND1 . HIS A 248 ? 0.8418 0.7115 0.7027 0.0333  0.1934  -0.0342 264 HIS A ND1 
1973 C CD2 . HIS A 248 ? 0.8947 0.7495 0.7060 0.0242  0.2204  -0.0308 264 HIS A CD2 
1974 C CE1 . HIS A 248 ? 0.7624 0.6227 0.6073 0.0227  0.1852  -0.0249 264 HIS A CE1 
1975 N NE2 . HIS A 248 ? 0.8779 0.7285 0.6931 0.0171  0.2007  -0.0218 264 HIS A NE2 
1976 N N   . GLU A 249 ? 1.1618 1.1033 1.1259 0.0758  0.2699  -0.0573 265 GLU A N   
1977 C CA  . GLU A 249 ? 1.1842 1.1307 1.1613 0.0912  0.2915  -0.0669 265 GLU A CA  
1978 C C   . GLU A 249 ? 1.1868 1.1306 1.1386 0.0881  0.3194  -0.0711 265 GLU A C   
1979 O O   . GLU A 249 ? 1.2671 1.1934 1.1974 0.0979  0.3359  -0.0839 265 GLU A O   
1980 C CB  . GLU A 249 ? 1.1287 1.1154 1.1682 0.1007  0.2941  -0.0609 265 GLU A CB  
1981 C CG  . GLU A 249 ? 1.1571 1.1514 1.2236 0.1037  0.2678  -0.0548 265 GLU A CG  
1982 C CD  . GLU A 249 ? 1.2017 1.1716 1.2624 0.1183  0.2611  -0.0628 265 GLU A CD  
1983 O OE1 . GLU A 249 ? 1.2548 1.1942 1.2811 0.1230  0.2724  -0.0750 265 GLU A OE1 
1984 O OE2 . GLU A 249 ? 1.1583 1.1387 1.2477 0.1244  0.2445  -0.0570 265 GLU A OE2 
1985 N N   . SER A 250 ? 1.0753 1.0343 1.0272 0.0739  0.3255  -0.0609 266 SER A N   
1986 C CA  . SER A 250 ? 1.1621 1.1246 1.0957 0.0694  0.3541  -0.0618 266 SER A CA  
1987 C C   . SER A 250 ? 1.1578 1.0868 1.0280 0.0570  0.3525  -0.0608 266 SER A C   
1988 O O   . SER A 250 ? 1.2193 1.1486 1.0671 0.0508  0.3752  -0.0591 266 SER A O   
1989 C CB  . SER A 250 ? 1.2373 1.2412 1.2166 0.0610  0.3649  -0.0499 266 SER A CB  
1990 O OG  . SER A 250 ? 1.2783 1.3151 1.3169 0.0705  0.3571  -0.0479 266 SER A OG  
1991 N N   . SER A 251 ? 1.1508 1.0527 0.9922 0.0536  0.3266  -0.0609 267 SER A N   
1992 C CA  . SER A 251 ? 1.1762 1.0465 0.9574 0.0440  0.3214  -0.0595 267 SER A CA  
1993 C C   . SER A 251 ? 1.2131 1.0536 0.9525 0.0524  0.3208  -0.0757 267 SER A C   
1994 O O   . SER A 251 ? 1.2026 1.0402 0.9602 0.0640  0.3149  -0.0864 267 SER A O   
1995 C CB  . SER A 251 ? 1.0764 0.9375 0.8532 0.0342  0.2925  -0.0484 267 SER A CB  
1996 O OG  . SER A 251 ? 1.1106 0.9855 0.9003 0.0214  0.2966  -0.0337 267 SER A OG  
1997 N N   . LEU A 252 ? 1.2696 1.0869 0.9517 0.0456  0.3265  -0.0772 268 LEU A N   
1998 C CA  . LEU A 252 ? 1.3168 1.1038 0.9517 0.0501  0.3234  -0.0932 268 LEU A CA  
1999 C C   . LEU A 252 ? 1.3337 1.0996 0.9431 0.0443  0.2908  -0.0906 268 LEU A C   
2000 O O   . LEU A 252 ? 1.3240 1.0745 0.9278 0.0498  0.2773  -0.1032 268 LEU A O   
2001 C CB  . LEU A 252 ? 1.3603 1.1353 0.9433 0.0462  0.3476  -0.0975 268 LEU A CB  
2002 C CG  . LEU A 252 ? 1.3144 1.1126 0.9228 0.0519  0.3830  -0.1000 268 LEU A CG  
2003 C CD1 . LEU A 252 ? 1.3168 1.1053 0.8721 0.0455  0.4081  -0.1006 268 LEU A CD1 
2004 C CD2 . LEU A 252 ? 1.2534 1.0537 0.8898 0.0686  0.3931  -0.1181 268 LEU A CD2 
2005 N N   . ILE A 253 ? 1.4227 1.1878 1.0192 0.0334  0.2785  -0.0742 269 ILE A N   
2006 C CA  . ILE A 253 ? 1.4162 1.1655 0.9945 0.0289  0.2478  -0.0695 269 ILE A CA  
2007 C C   . ILE A 253 ? 1.2958 1.0596 0.9262 0.0319  0.2290  -0.0651 269 ILE A C   
2008 O O   . ILE A 253 ? 1.2528 1.0387 0.9241 0.0306  0.2342  -0.0555 269 ILE A O   
2009 C CB  . ILE A 253 ? 1.4694 1.2106 1.0142 0.0180  0.2431  -0.0524 269 ILE A CB  
2010 C CG1 . ILE A 253 ? 1.5398 1.2710 1.0355 0.0144  0.2664  -0.0537 269 ILE A CG1 
2011 C CG2 . ILE A 253 ? 1.4807 1.2053 1.0024 0.0153  0.2124  -0.0486 269 ILE A CG2 
2012 C CD1 . ILE A 253 ? 1.6442 1.3709 1.1151 0.0037  0.2687  -0.0329 269 ILE A CD1 
2013 N N   . LEU A 254 ? 1.1375 0.8897 0.7661 0.0352  0.2073  -0.0725 270 LEU A N   
2014 C CA  . LEU A 254 ? 1.0310 0.7942 0.6997 0.0362  0.1869  -0.0662 270 LEU A CA  
2015 C C   . LEU A 254 ? 0.9828 0.7367 0.6319 0.0287  0.1650  -0.0548 270 LEU A C   
2016 O O   . LEU A 254 ? 0.9918 0.7273 0.6014 0.0266  0.1537  -0.0588 270 LEU A O   
2017 C CB  . LEU A 254 ? 1.0120 0.7700 0.6962 0.0440  0.1771  -0.0791 270 LEU A CB  
2018 C CG  . LEU A 254 ? 0.9882 0.7568 0.7066 0.0547  0.1932  -0.0880 270 LEU A CG  
2019 C CD1 . LEU A 254 ? 0.9120 0.6669 0.6363 0.0606  0.1808  -0.0994 270 LEU A CD1 
2020 C CD2 . LEU A 254 ? 0.9323 0.7300 0.7006 0.0562  0.1955  -0.0764 270 LEU A CD2 
2021 N N   . PRO A 255 ? 0.8976 0.6634 0.5728 0.0248  0.1582  -0.0413 271 PRO A N   
2022 C CA  . PRO A 255 ? 0.9269 0.6834 0.5898 0.0203  0.1365  -0.0312 271 PRO A CA  
2023 C C   . PRO A 255 ? 0.8778 0.6291 0.5442 0.0244  0.1150  -0.0388 271 PRO A C   
2024 O O   . PRO A 255 ? 0.8550 0.6145 0.5500 0.0299  0.1145  -0.0475 271 PRO A O   
2025 C CB  . PRO A 255 ? 0.8746 0.6466 0.5754 0.0169  0.1359  -0.0198 271 PRO A CB  
2026 C CG  . PRO A 255 ? 0.8837 0.6720 0.6049 0.0161  0.1595  -0.0208 271 PRO A CG  
2027 C CD  . PRO A 255 ? 0.8714 0.6605 0.5901 0.0242  0.1698  -0.0355 271 PRO A CD  
2028 N N   . PRO A 256 ? 0.9164 0.6551 0.5555 0.0219  0.0971  -0.0348 272 PRO A N   
2029 C CA  . PRO A 256 ? 0.8450 0.5822 0.4923 0.0242  0.0761  -0.0407 272 PRO A CA  
2030 C C   . PRO A 256 ? 0.8168 0.5674 0.5054 0.0258  0.0654  -0.0337 272 PRO A C   
2031 O O   . PRO A 256 ? 0.7990 0.5574 0.5054 0.0241  0.0707  -0.0239 272 PRO A O   
2032 C CB  . PRO A 256 ? 0.8850 0.6089 0.4917 0.0208  0.0607  -0.0363 272 PRO A CB  
2033 C CG  . PRO A 256 ? 0.9664 0.6866 0.5563 0.0175  0.0693  -0.0212 272 PRO A CG  
2034 C CD  . PRO A 256 ? 0.9307 0.6567 0.5297 0.0170  0.0954  -0.0241 272 PRO A CD  
2035 N N   . ILE A 257 ? 0.8249 0.5777 0.5281 0.0282  0.0508  -0.0396 273 ILE A N   
2036 C CA  . ILE A 257 ? 0.7445 0.5079 0.4790 0.0294  0.0376  -0.0334 273 ILE A CA  
2037 C C   . ILE A 257 ? 0.8213 0.5785 0.5387 0.0280  0.0188  -0.0271 273 ILE A C   
2038 O O   . ILE A 257 ? 0.7712 0.5208 0.4657 0.0267  0.0092  -0.0330 273 ILE A O   
2039 C CB  . ILE A 257 ? 0.7595 0.5307 0.5225 0.0331  0.0346  -0.0418 273 ILE A CB  
2040 C CG1 . ILE A 257 ? 0.6771 0.4568 0.4598 0.0364  0.0531  -0.0454 273 ILE A CG1 
2041 C CG2 . ILE A 257 ? 0.7135 0.4958 0.5044 0.0339  0.0209  -0.0354 273 ILE A CG2 
2042 C CD1 . ILE A 257 ? 0.6871 0.4707 0.4928 0.0413  0.0530  -0.0526 273 ILE A CD1 
2043 N N   . LYS A 258 ? 0.7586 0.5190 0.4870 0.0281  0.0135  -0.0155 274 LYS A N   
2044 C CA  . LYS A 258 ? 0.7872 0.5425 0.5021 0.0289  -0.0031 -0.0071 274 LYS A CA  
2045 C C   . LYS A 258 ? 0.8063 0.5728 0.5524 0.0320  -0.0164 -0.0065 274 LYS A C   
2046 O O   . LYS A 258 ? 0.7121 0.4878 0.4876 0.0330  -0.0112 -0.0069 274 LYS A O   
2047 C CB  . LYS A 258 ? 0.7978 0.5441 0.4994 0.0278  0.0018  0.0067  274 LYS A CB  
2048 C CG  . LYS A 258 ? 0.8453 0.5799 0.5109 0.0241  0.0151  0.0087  274 LYS A CG  
2049 C CD  . LYS A 258 ? 0.8901 0.6140 0.5448 0.0222  0.0203  0.0245  274 LYS A CD  
2050 C CE  . LYS A 258 ? 1.0338 0.7453 0.6471 0.0184  0.0320  0.0287  274 LYS A CE  
2051 N NZ  . LYS A 258 ? 1.1492 0.8470 0.7492 0.0161  0.0368  0.0464  274 LYS A NZ  
2052 N N   . VAL A 259 ? 0.7533 0.5209 0.4930 0.0333  -0.0336 -0.0058 275 VAL A N   
2053 C CA  . VAL A 259 ? 0.6992 0.4789 0.4677 0.0365  -0.0458 -0.0046 275 VAL A CA  
2054 C C   . VAL A 259 ? 0.7557 0.5339 0.5156 0.0402  -0.0598 0.0064  275 VAL A C   
2055 O O   . VAL A 259 ? 0.7615 0.5348 0.4939 0.0392  -0.0689 0.0084  275 VAL A O   
2056 C CB  . VAL A 259 ? 0.7216 0.5093 0.5007 0.0344  -0.0531 -0.0155 275 VAL A CB  
2057 C CG1 . VAL A 259 ? 0.6613 0.4630 0.4695 0.0373  -0.0644 -0.0128 275 VAL A CG1 
2058 C CG2 . VAL A 259 ? 0.7208 0.5086 0.5113 0.0330  -0.0392 -0.0247 275 VAL A CG2 
2059 N N   . MET A 260 ? 0.6987 0.4811 0.4814 0.0449  -0.0618 0.0134  276 MET A N   
2060 C CA  . MET A 260 ? 0.7510 0.5344 0.5345 0.0512  -0.0754 0.0239  276 MET A CA  
2061 C C   . MET A 260 ? 0.7689 0.5703 0.5847 0.0544  -0.0846 0.0202  276 MET A C   
2062 O O   . MET A 260 ? 0.6867 0.4943 0.5267 0.0543  -0.0769 0.0155  276 MET A O   
2063 C CB  . MET A 260 ? 0.7419 0.5118 0.5248 0.0549  -0.0680 0.0351  276 MET A CB  
2064 C CG  . MET A 260 ? 0.8024 0.5706 0.5915 0.0641  -0.0797 0.0472  276 MET A CG  
2065 S SD  . MET A 260 ? 1.1020 0.8633 0.8548 0.0670  -0.0941 0.0593  276 MET A SD  
2066 C CE  . MET A 260 ? 0.9563 0.6909 0.6771 0.0630  -0.0779 0.0689  276 MET A CE  
2067 N N   . VAL A 261 ? 0.7278 0.5394 0.5438 0.0565  -0.1011 0.0221  277 VAL A N   
2068 C CA  . VAL A 261 ? 0.7029 0.5338 0.5509 0.0597  -0.1097 0.0205  277 VAL A CA  
2069 C C   . VAL A 261 ? 0.7230 0.5563 0.5785 0.0700  -0.1187 0.0330  277 VAL A C   
2070 O O   . VAL A 261 ? 0.7355 0.5680 0.5732 0.0726  -0.1312 0.0408  277 VAL A O   
2071 C CB  . VAL A 261 ? 0.7395 0.5837 0.5886 0.0534  -0.1216 0.0124  277 VAL A CB  
2072 C CG1 . VAL A 261 ? 0.6335 0.5000 0.5184 0.0561  -0.1294 0.0122  277 VAL A CG1 
2073 C CG2 . VAL A 261 ? 0.6788 0.5160 0.5195 0.0445  -0.1113 0.0000  277 VAL A CG2 
2074 N N   . ALA A 262 ? 0.6719 0.5078 0.5529 0.0764  -0.1125 0.0350  278 ALA A N   
2075 C CA  . ALA A 262 ? 0.7327 0.5681 0.6245 0.0882  -0.1181 0.0463  278 ALA A CA  
2076 C C   . ALA A 262 ? 0.6811 0.5397 0.6088 0.0938  -0.1230 0.0438  278 ALA A C   
2077 O O   . ALA A 262 ? 0.6198 0.4871 0.5654 0.0897  -0.1147 0.0346  278 ALA A O   
2078 C CB  . ALA A 262 ? 0.6958 0.5091 0.5843 0.0918  -0.1042 0.0506  278 ALA A CB  
2079 N N   . LEU A 263 ? 0.6860 0.5561 0.6248 0.1035  -0.1362 0.0530  279 LEU A N   
2080 C CA  . LEU A 263 ? 0.6773 0.5722 0.6528 0.1100  -0.1401 0.0519  279 LEU A CA  
2081 C C   . LEU A 263 ? 0.6598 0.5482 0.6488 0.1258  -0.1382 0.0619  279 LEU A C   
2082 O O   . LEU A 263 ? 0.6758 0.5592 0.6554 0.1344  -0.1488 0.0745  279 LEU A O   
2083 C CB  . LEU A 263 ? 0.6696 0.5910 0.6538 0.1073  -0.1586 0.0528  279 LEU A CB  
2084 C CG  . LEU A 263 ? 0.6110 0.5625 0.6366 0.1136  -0.1629 0.0529  279 LEU A CG  
2085 C CD1 . LEU A 263 ? 0.5927 0.5516 0.6361 0.1060  -0.1493 0.0411  279 LEU A CD1 
2086 C CD2 . LEU A 263 ? 0.6355 0.6142 0.6696 0.1105  -0.1838 0.0556  279 LEU A CD2 
2087 N N   . GLY A 264 ? 0.6059 0.4928 0.6153 0.1300  -0.1245 0.0563  280 GLY A N   
2088 C CA  . GLY A 264 ? 0.6570 0.5371 0.6829 0.1455  -0.1205 0.0629  280 GLY A CA  
2089 C C   . GLY A 264 ? 0.6491 0.5586 0.7133 0.1540  -0.1219 0.0607  280 GLY A C   
2090 O O   . GLY A 264 ? 0.6342 0.5717 0.7131 0.1475  -0.1286 0.0563  280 GLY A O   
2091 N N   . GLU A 265 ? 0.6304 0.5322 0.7114 0.1685  -0.1138 0.0633  281 GLU A N   
2092 C CA  . GLU A 265 ? 0.6458 0.5756 0.7648 0.1785  -0.1122 0.0612  281 GLU A CA  
2093 C C   . GLU A 265 ? 0.5945 0.5378 0.7239 0.1682  -0.0997 0.0468  281 GLU A C   
2094 O O   . GLU A 265 ? 0.6023 0.5770 0.7600 0.1693  -0.1009 0.0445  281 GLU A O   
2095 C CB  . GLU A 265 ? 0.6235 0.5381 0.7567 0.1976  -0.1039 0.0659  281 GLU A CB  
2096 C CG  . GLU A 265 ? 0.8391 0.7460 0.9707 0.2123  -0.1174 0.0834  281 GLU A CG  
2097 C CD  . GLU A 265 ? 0.9129 0.8573 1.0608 0.2141  -0.1382 0.0922  281 GLU A CD  
2098 O OE1 . GLU A 265 ? 0.8811 0.8594 1.0657 0.2204  -0.1394 0.0901  281 GLU A OE1 
2099 O OE2 . GLU A 265 ? 0.8915 0.8323 1.0149 0.2082  -0.1532 0.1006  281 GLU A OE2 
2100 N N   . GLU A 266 ? 0.6061 0.5274 0.7142 0.1582  -0.0876 0.0380  282 GLU A N   
2101 C CA  . GLU A 266 ? 0.5920 0.5241 0.7065 0.1491  -0.0760 0.0259  282 GLU A CA  
2102 C C   . GLU A 266 ? 0.5867 0.5143 0.6792 0.1319  -0.0764 0.0208  282 GLU A C   
2103 O O   . GLU A 266 ? 0.5325 0.4786 0.6337 0.1235  -0.0742 0.0152  282 GLU A O   
2104 C CB  . GLU A 266 ? 0.5812 0.4949 0.6956 0.1549  -0.0591 0.0182  282 GLU A CB  
2105 C CG  . GLU A 266 ? 0.6794 0.5981 0.7901 0.1440  -0.0472 0.0061  282 GLU A CG  
2106 C CD  . GLU A 266 ? 0.6821 0.5859 0.7929 0.1496  -0.0316 -0.0031 282 GLU A CD  
2107 O OE1 . GLU A 266 ? 0.6406 0.5367 0.7637 0.1642  -0.0282 -0.0012 282 GLU A OE1 
2108 O OE2 . GLU A 266 ? 0.7212 0.6207 0.8193 0.1394  -0.0231 -0.0126 282 GLU A OE2 
2109 N N   . ASP A 267 ? 0.5469 0.4734 0.6483 0.0391  -0.0599 0.0012  283 ASP A N   
2110 C CA  . ASP A 267 ? 0.5413 0.4597 0.6086 0.0363  -0.0583 -0.0010 283 ASP A CA  
2111 C C   . ASP A 267 ? 0.5841 0.4933 0.6377 0.0272  -0.0697 0.0068  283 ASP A C   
2112 O O   . ASP A 267 ? 0.5750 0.4812 0.6355 0.0224  -0.0814 0.0139  283 ASP A O   
2113 C CB  . ASP A 267 ? 0.5326 0.4455 0.5844 0.0387  -0.0564 -0.0070 283 ASP A CB  
2114 C CG  . ASP A 267 ? 0.5683 0.4889 0.6293 0.0465  -0.0466 -0.0174 283 ASP A CG  
2115 O OD1 . ASP A 267 ? 0.5832 0.5141 0.6579 0.0507  -0.0391 -0.0209 283 ASP A OD1 
2116 O OD2 . ASP A 267 ? 0.5298 0.4467 0.5845 0.0480  -0.0464 -0.0227 283 ASP A OD2 
2117 N N   . LEU A 268 ? 0.5639 0.4679 0.5970 0.0248  -0.0664 0.0051  284 LEU A N   
2118 C CA  . LEU A 268 ? 0.4877 0.3794 0.4977 0.0171  -0.0742 0.0069  284 LEU A CA  
2119 C C   . LEU A 268 ? 0.5321 0.4174 0.5174 0.0203  -0.0663 0.0006  284 LEU A C   
2120 O O   . LEU A 268 ? 0.5386 0.4260 0.5197 0.0248  -0.0568 -0.0032 284 LEU A O   
2121 C CB  . LEU A 268 ? 0.5625 0.4515 0.5732 0.0115  -0.0768 0.0091  284 LEU A CB  
2122 C CG  . LEU A 268 ? 0.6358 0.5119 0.6260 0.0018  -0.0875 0.0094  284 LEU A CG  
2123 C CD1 . LEU A 268 ? 0.6284 0.5052 0.6330 -0.0052 -0.0949 0.0131  284 LEU A CD1 
2124 C CD2 . LEU A 268 ? 0.6357 0.5001 0.5980 0.0027  -0.0799 0.0018  284 LEU A CD2 
2125 N N   . SER A 269 ? 0.5464 0.4255 0.5175 0.0182  -0.0701 0.0009  285 SER A N   
2126 C CA  . SER A 269 ? 0.5572 0.4326 0.5103 0.0215  -0.0624 -0.0043 285 SER A CA  
2127 C C   . SER A 269 ? 0.6205 0.4842 0.5480 0.0158  -0.0641 -0.0052 285 SER A C   
2128 O O   . SER A 269 ? 0.6155 0.4748 0.5353 0.0087  -0.0734 -0.0012 285 SER A O   
2129 C CB  . SER A 269 ? 0.5109 0.3900 0.4713 0.0245  -0.0623 -0.0039 285 SER A CB  
2130 O OG  . SER A 269 ? 0.5750 0.4630 0.5610 0.0287  -0.0624 -0.0043 285 SER A OG  
2131 N N   . ILE A 270 ? 0.5846 0.4441 0.4991 0.0192  -0.0550 -0.0106 286 ILE A N   
2132 C CA  . ILE A 270 ? 0.6302 0.4783 0.5214 0.0156  -0.0529 -0.0144 286 ILE A CA  
2133 C C   . ILE A 270 ? 0.6376 0.4876 0.5224 0.0208  -0.0441 -0.0166 286 ILE A C   
2134 O O   . ILE A 270 ? 0.5985 0.4525 0.4895 0.0274  -0.0366 -0.0189 286 ILE A O   
2135 C CB  . ILE A 270 ? 0.6201 0.4599 0.5079 0.0150  -0.0497 -0.0187 286 ILE A CB  
2136 C CG1 . ILE A 270 ? 0.6034 0.4438 0.5038 0.0097  -0.0584 -0.0154 286 ILE A CG1 
2137 C CG2 . ILE A 270 ? 0.6062 0.4324 0.4704 0.0112  -0.0470 -0.0254 286 ILE A CG2 
2138 C CD1 . ILE A 270 ? 0.6760 0.5135 0.5858 0.0113  -0.0537 -0.0163 286 ILE A CD1 
2139 N N   . LYS A 271 ? 0.5724 0.4210 0.4460 0.0175  -0.0453 -0.0146 287 LYS A N   
2140 C CA  . LYS A 271 ? 0.6319 0.4833 0.5020 0.0215  -0.0367 -0.0157 287 LYS A CA  
2141 C C   . LYS A 271 ? 0.6925 0.5347 0.5407 0.0198  -0.0295 -0.0207 287 LYS A C   
2142 O O   . LYS A 271 ? 0.6671 0.5026 0.4967 0.0127  -0.0333 -0.0210 287 LYS A O   
2143 C CB  . LYS A 271 ? 0.5918 0.4488 0.4673 0.0193  -0.0406 -0.0090 287 LYS A CB  
2144 C CG  . LYS A 271 ? 0.6888 0.5501 0.5646 0.0226  -0.0318 -0.0092 287 LYS A CG  
2145 C CD  . LYS A 271 ? 0.7079 0.5749 0.5955 0.0203  -0.0358 -0.0015 287 LYS A CD  
2146 C CE  . LYS A 271 ? 0.7408 0.6039 0.6117 0.0124  -0.0397 0.0064  287 LYS A CE  
2147 N NZ  . LYS A 271 ? 0.8745 0.7427 0.7590 0.0098  -0.0432 0.0168  287 LYS A NZ  
2148 N N   . MET A 272 ? 0.6619 0.5045 0.5126 0.0262  -0.0191 -0.0248 288 MET A N   
2149 C CA  . MET A 272 ? 0.6584 0.4935 0.4932 0.0265  -0.0092 -0.0305 288 MET A CA  
2150 C C   . MET A 272 ? 0.6629 0.5068 0.5020 0.0298  -0.0013 -0.0276 288 MET A C   
2151 O O   . MET A 272 ? 0.6199 0.4740 0.4782 0.0347  -0.0016 -0.0241 288 MET A O   
2152 C CB  . MET A 272 ? 0.6352 0.4634 0.4751 0.0317  -0.0030 -0.0365 288 MET A CB  
2153 C CG  . MET A 272 ? 0.5797 0.3966 0.4048 0.0321  0.0077  -0.0452 288 MET A CG  
2154 S SD  . MET A 272 ? 0.6305 0.4403 0.4717 0.0403  0.0156  -0.0493 288 MET A SD  
2155 C CE  . MET A 272 ? 0.5599 0.3617 0.4051 0.0354  0.0045  -0.0489 288 MET A CE  
2156 N N   . SER A 273 ? 0.6013 0.4420 0.4226 0.0268  0.0059  -0.0292 289 SER A N   
2157 C CA  . SER A 273 ? 0.6822 0.5325 0.5088 0.0284  0.0137  -0.0244 289 SER A CA  
2158 C C   . SER A 273 ? 0.6922 0.5387 0.5079 0.0312  0.0291  -0.0311 289 SER A C   
2159 O O   . SER A 273 ? 0.6975 0.5337 0.4887 0.0271  0.0326  -0.0381 289 SER A O   
2160 C CB  . SER A 273 ? 0.6783 0.5326 0.4960 0.0207  0.0079  -0.0154 289 SER A CB  
2161 O OG  . SER A 273 ? 0.7346 0.5913 0.5652 0.0184  -0.0059 -0.0097 289 SER A OG  
2162 N N   . ASP A 274 ? 0.6341 0.4896 0.4685 0.0380  0.0385  -0.0296 290 ASP A N   
2163 C CA  . ASP A 274 ? 0.6420 0.4960 0.4709 0.0416  0.0552  -0.0353 290 ASP A CA  
2164 C C   . ASP A 274 ? 0.6676 0.5360 0.5074 0.0418  0.0628  -0.0271 290 ASP A C   
2165 O O   . ASP A 274 ? 0.6393 0.5180 0.4953 0.0400  0.0544  -0.0179 290 ASP A O   
2166 C CB  . ASP A 274 ? 0.6404 0.4902 0.4858 0.0509  0.0617  -0.0416 290 ASP A CB  
2167 C CG  . ASP A 274 ? 0.6043 0.4687 0.4818 0.0579  0.0602  -0.0342 290 ASP A CG  
2168 O OD1 . ASP A 274 ? 0.6142 0.4920 0.5044 0.0583  0.0640  -0.0279 290 ASP A OD1 
2169 O OD2 . ASP A 274 ? 0.6264 0.4893 0.5170 0.0629  0.0554  -0.0343 290 ASP A OD2 
2170 N N   . ARG A 275 ? 0.6446 0.5133 0.4754 0.0433  0.0795  -0.0311 291 ARG A N   
2171 C CA  . ARG A 275 ? 0.7057 0.5896 0.5520 0.0445  0.0901  -0.0232 291 ARG A CA  
2172 C C   . ARG A 275 ? 0.7007 0.5887 0.5692 0.0547  0.1041  -0.0282 291 ARG A C   
2173 O O   . ARG A 275 ? 0.6900 0.5824 0.5568 0.0568  0.1219  -0.0301 291 ARG A O   
2174 C CB  . ARG A 275 ? 0.6903 0.5755 0.5093 0.0372  0.0994  -0.0206 291 ARG A CB  
2175 C CG  . ARG A 275 ? 0.8288 0.7120 0.6304 0.0272  0.0840  -0.0122 291 ARG A CG  
2176 C CD  . ARG A 275 ? 0.9375 0.8263 0.7154 0.0193  0.0919  -0.0043 291 ARG A CD  
2177 N NE  . ARG A 275 ? 1.0989 0.9861 0.8653 0.0102  0.0749  0.0064  291 ARG A NE  
2178 C CZ  . ARG A 275 ? 1.0963 0.9908 0.8500 0.0021  0.0754  0.0201  291 ARG A CZ  
2179 N NH1 . ARG A 275 ? 1.1841 1.0887 0.9323 0.0013  0.0931  0.0250  291 ARG A NH1 
2180 N NH2 . ARG A 275 ? 1.0670 0.9594 0.8153 -0.0052 0.0580  0.0307  291 ARG A NH2 
2181 N N   . GLY A 276 ? 0.6412 0.5288 0.5315 0.0612  0.0967  -0.0291 292 GLY A N   
2182 C CA  . GLY A 276 ? 0.6633 0.5537 0.5771 0.0714  0.1077  -0.0322 292 GLY A CA  
2183 C C   . GLY A 276 ? 0.6674 0.5776 0.6179 0.0760  0.1069  -0.0220 292 GLY A C   
2184 O O   . GLY A 276 ? 0.6451 0.5595 0.6204 0.0845  0.1090  -0.0214 292 GLY A O   
2185 N N   . GLY A 277 ? 0.6194 0.5423 0.5761 0.0701  0.1027  -0.0132 293 GLY A N   
2186 C CA  . GLY A 277 ? 0.6050 0.5474 0.5972 0.0728  0.1021  -0.0043 293 GLY A CA  
2187 C C   . GLY A 277 ? 0.6034 0.5531 0.6113 0.0711  0.0821  0.0005  293 GLY A C   
2188 O O   . GLY A 277 ? 0.6012 0.5668 0.6349 0.0697  0.0782  0.0076  293 GLY A O   
2189 N N   . GLY A 278 ? 0.5471 0.4863 0.5412 0.0710  0.0700  -0.0039 294 GLY A N   
2190 C CA  . GLY A 278 ? 0.5527 0.4985 0.5562 0.0687  0.0525  -0.0014 294 GLY A CA  
2191 C C   . GLY A 278 ? 0.5942 0.5538 0.6243 0.0750  0.0473  0.0021  294 GLY A C   
2192 O O   . GLY A 278 ? 0.5765 0.5399 0.6211 0.0821  0.0564  0.0038  294 GLY A O   
2193 N N   . VAL A 279 ? 0.5224 0.4898 0.5592 0.0723  0.0319  0.0029  295 VAL A N   
2194 C CA  . VAL A 279 ? 0.5207 0.5026 0.5776 0.0766  0.0229  0.0063  295 VAL A CA  
2195 C C   . VAL A 279 ? 0.4808 0.4733 0.5462 0.0704  0.0083  0.0053  295 VAL A C   
2196 O O   . VAL A 279 ? 0.4765 0.4604 0.5270 0.0648  0.0029  0.0004  295 VAL A O   
2197 C CB  . VAL A 279 ? 0.5448 0.5198 0.5895 0.0818  0.0193  0.0053  295 VAL A CB  
2198 C CG1 . VAL A 279 ? 0.5197 0.4806 0.5378 0.0772  0.0146  -0.0008 295 VAL A CG1 
2199 C CG2 . VAL A 279 ? 0.5876 0.5791 0.6470 0.0845  0.0066  0.0102  295 VAL A CG2 
2200 N N   . PRO A 280 ? 0.4724 0.4832 0.5632 0.0708  0.0012  0.0093  296 PRO A N   
2201 C CA  . PRO A 280 ? 0.5058 0.5253 0.6052 0.0639  -0.0130 0.0057  296 PRO A CA  
2202 C C   . PRO A 280 ? 0.5279 0.5436 0.6074 0.0631  -0.0248 -0.0018 296 PRO A C   
2203 O O   . PRO A 280 ? 0.5447 0.5600 0.6125 0.0683  -0.0259 -0.0005 296 PRO A O   
2204 C CB  . PRO A 280 ? 0.5399 0.5809 0.6708 0.0651  -0.0187 0.0118  296 PRO A CB  
2205 C CG  . PRO A 280 ? 0.5453 0.5892 0.6836 0.0740  -0.0089 0.0193  296 PRO A CG  
2206 C CD  . PRO A 280 ? 0.5248 0.5490 0.6413 0.0770  0.0067  0.0171  296 PRO A CD  
2207 N N   . LEU A 281 ? 0.4832 0.4962 0.5610 0.0564  -0.0328 -0.0092 297 LEU A N   
2208 C CA  . LEU A 281 ? 0.5362 0.5455 0.5957 0.0555  -0.0417 -0.0182 297 LEU A CA  
2209 C C   . LEU A 281 ? 0.5557 0.5803 0.6138 0.0585  -0.0515 -0.0184 297 LEU A C   
2210 O O   . LEU A 281 ? 0.5132 0.5355 0.5513 0.0613  -0.0530 -0.0204 297 LEU A O   
2211 C CB  . LEU A 281 ? 0.4775 0.4834 0.5436 0.0483  -0.0488 -0.0270 297 LEU A CB  
2212 C CG  . LEU A 281 ? 0.5986 0.6007 0.6488 0.0475  -0.0562 -0.0386 297 LEU A CG  
2213 C CD1 . LEU A 281 ? 0.5084 0.4952 0.5377 0.0502  -0.0484 -0.0380 297 LEU A CD1 
2214 C CD2 . LEU A 281 ? 0.5171 0.5182 0.5825 0.0407  -0.0646 -0.0489 297 LEU A CD2 
2215 N N   . ARG A 282 ? 0.5256 0.5672 0.6055 0.0575  -0.0584 -0.0146 298 ARG A N   
2216 C CA  . ARG A 282 ? 0.5676 0.6263 0.6459 0.0593  -0.0703 -0.0132 298 ARG A CA  
2217 C C   . ARG A 282 ? 0.5718 0.6304 0.6394 0.0674  -0.0647 -0.0029 298 ARG A C   
2218 O O   . ARG A 282 ? 0.5463 0.6141 0.6010 0.0690  -0.0727 -0.0014 298 ARG A O   
2219 C CB  . ARG A 282 ? 0.5547 0.6325 0.6632 0.0564  -0.0791 -0.0090 298 ARG A CB  
2220 C CG  . ARG A 282 ? 0.6440 0.7429 0.7539 0.0574  -0.0937 -0.0050 298 ARG A CG  
2221 C CD  . ARG A 282 ? 0.6133 0.7310 0.7577 0.0535  -0.1030 -0.0005 298 ARG A CD  
2222 N NE  . ARG A 282 ? 0.6280 0.7465 0.7993 0.0583  -0.0901 0.0123  298 ARG A NE  
2223 C CZ  . ARG A 282 ? 0.5749 0.7047 0.7615 0.0657  -0.0880 0.0263  298 ARG A CZ  
2224 N NH1 . ARG A 282 ? 0.6840 0.8255 0.8612 0.0690  -0.0988 0.0323  298 ARG A NH1 
2225 N NH2 . ARG A 282 ? 0.5613 0.6913 0.7741 0.0700  -0.0741 0.0353  298 ARG A NH2 
2226 N N   . LYS A 283 ? 0.5641 0.6115 0.6357 0.0722  -0.0506 0.0040  299 LYS A N   
2227 C CA  . LYS A 283 ? 0.5684 0.6140 0.6360 0.0799  -0.0452 0.0137  299 LYS A CA  
2228 C C   . LYS A 283 ? 0.5365 0.5637 0.5786 0.0814  -0.0380 0.0106  299 LYS A C   
2229 O O   . LYS A 283 ? 0.4702 0.4964 0.5072 0.0865  -0.0364 0.0182  299 LYS A O   
2230 C CB  . LYS A 283 ? 0.4694 0.5142 0.5602 0.0852  -0.0334 0.0221  299 LYS A CB  
2231 C CG  . LYS A 283 ? 0.5364 0.6027 0.6590 0.0855  -0.0401 0.0293  299 LYS A CG  
2232 C CD  . LYS A 283 ? 0.6201 0.6852 0.7672 0.0923  -0.0250 0.0372  299 LYS A CD  
2233 C CE  . LYS A 283 ? 0.7021 0.7902 0.8865 0.0926  -0.0305 0.0454  299 LYS A CE  
2234 N NZ  . LYS A 283 ? 0.6974 0.7841 0.9069 0.0995  -0.0125 0.0514  299 LYS A NZ  
2235 N N   . ILE A 284 ? 0.5583 0.5713 0.5870 0.0768  -0.0341 0.0012  300 ILE A N   
2236 C CA  . ILE A 284 ? 0.5219 0.5167 0.5327 0.0783  -0.0255 0.0001  300 ILE A CA  
2237 C C   . ILE A 284 ? 0.5940 0.5906 0.5890 0.0800  -0.0300 0.0017  300 ILE A C   
2238 O O   . ILE A 284 ? 0.5699 0.5564 0.5584 0.0834  -0.0237 0.0064  300 ILE A O   
2239 C CB  . ILE A 284 ? 0.5498 0.5313 0.5519 0.0726  -0.0223 -0.0082 300 ILE A CB  
2240 C CG1 . ILE A 284 ? 0.6155 0.5786 0.6029 0.0736  -0.0131 -0.0082 300 ILE A CG1 
2241 C CG2 . ILE A 284 ? 0.6038 0.5882 0.5981 0.0681  -0.0314 -0.0168 300 ILE A CG2 
2242 C CD1 . ILE A 284 ? 0.5998 0.5513 0.5807 0.0681  -0.0100 -0.0129 300 ILE A CD1 
2243 N N   . GLU A 285 ? 0.5185 0.5287 0.5078 0.0777  -0.0405 -0.0019 301 GLU A N   
2244 C CA  . GLU A 285 ? 0.6227 0.6363 0.5947 0.0789  -0.0428 0.0002  301 GLU A CA  
2245 C C   . GLU A 285 ? 0.5852 0.6065 0.5616 0.0846  -0.0431 0.0151  301 GLU A C   
2246 O O   . GLU A 285 ? 0.5498 0.5704 0.5139 0.0861  -0.0418 0.0205  301 GLU A O   
2247 C CB  . GLU A 285 ? 0.6413 0.6685 0.6030 0.0750  -0.0527 -0.0091 301 GLU A CB  
2248 C CG  . GLU A 285 ? 0.8556 0.8721 0.8093 0.0709  -0.0505 -0.0229 301 GLU A CG  
2249 C CD  . GLU A 285 ? 1.0280 1.0560 0.9704 0.0679  -0.0579 -0.0348 301 GLU A CD  
2250 O OE1 . GLU A 285 ? 1.0340 1.0780 0.9654 0.0689  -0.0634 -0.0312 301 GLU A OE1 
2251 O OE2 . GLU A 285 ? 1.0398 1.0607 0.9843 0.0644  -0.0581 -0.0477 301 GLU A OE2 
2252 N N   . ARG A 286 ? 0.5307 0.5599 0.5275 0.0878  -0.0447 0.0231  302 ARG A N   
2253 C CA  . ARG A 286 ? 0.5607 0.5955 0.5679 0.0940  -0.0445 0.0391  302 ARG A CA  
2254 C C   . ARG A 286 ? 0.5761 0.5910 0.5810 0.0976  -0.0329 0.0430  302 ARG A C   
2255 O O   . ARG A 286 ? 0.5201 0.5366 0.5282 0.1017  -0.0329 0.0560  302 ARG A O   
2256 C CB  . ARG A 286 ? 0.5555 0.5997 0.5911 0.0975  -0.0455 0.0459  302 ARG A CB  
2257 C CG  . ARG A 286 ? 0.5829 0.6490 0.6243 0.0935  -0.0596 0.0441  302 ARG A CG  
2258 C CD  . ARG A 286 ? 0.6294 0.7053 0.7038 0.0968  -0.0596 0.0516  302 ARG A CD  
2259 N NE  . ARG A 286 ? 0.5640 0.6588 0.6474 0.0910  -0.0730 0.0473  302 ARG A NE  
2260 C CZ  . ARG A 286 ? 0.6829 0.7908 0.7975 0.0921  -0.0758 0.0532  302 ARG A CZ  
2261 N NH1 . ARG A 286 ? 0.6002 0.7041 0.7400 0.0993  -0.0641 0.0625  302 ARG A NH1 
2262 N NH2 . ARG A 286 ? 0.6035 0.7292 0.7261 0.0855  -0.0902 0.0490  302 ARG A NH2 
2263 N N   . LEU A 287 ? 0.4803 0.4763 0.4802 0.0954  -0.0238 0.0326  303 LEU A N   
2264 C CA  . LEU A 287 ? 0.5733 0.5492 0.5698 0.0972  -0.0141 0.0336  303 LEU A CA  
2265 C C   . LEU A 287 ? 0.5863 0.5608 0.5671 0.0955  -0.0162 0.0369  303 LEU A C   
2266 O O   . LEU A 287 ? 0.5586 0.5198 0.5414 0.0973  -0.0104 0.0418  303 LEU A O   
2267 C CB  . LEU A 287 ? 0.5442 0.5028 0.5343 0.0935  -0.0063 0.0212  303 LEU A CB  
2268 C CG  . LEU A 287 ? 0.5604 0.5167 0.5658 0.0958  0.0008  0.0192  303 LEU A CG  
2269 C CD1 . LEU A 287 ? 0.5587 0.5024 0.5524 0.0905  0.0064  0.0083  303 LEU A CD1 
2270 C CD2 . LEU A 287 ? 0.6124 0.5598 0.6328 0.1028  0.0098  0.0253  303 LEU A CD2 
2271 N N   . PHE A 288 ? 0.5419 0.5299 0.5087 0.0919  -0.0236 0.0339  304 PHE A N   
2272 C CA  . PHE A 288 ? 0.5910 0.5806 0.5438 0.0905  -0.0237 0.0377  304 PHE A CA  
2273 C C   . PHE A 288 ? 0.5274 0.5371 0.4777 0.0928  -0.0304 0.0512  304 PHE A C   
2274 O O   . PHE A 288 ? 0.5516 0.5669 0.4888 0.0915  -0.0300 0.0560  304 PHE A O   
2275 C CB  . PHE A 288 ? 0.5290 0.5180 0.4664 0.0853  -0.0245 0.0240  304 PHE A CB  
2276 C CG  . PHE A 288 ? 0.5867 0.5559 0.5250 0.0824  -0.0188 0.0145  304 PHE A CG  
2277 C CD1 . PHE A 288 ? 0.5618 0.5156 0.5000 0.0820  -0.0128 0.0175  304 PHE A CD1 
2278 C CD2 . PHE A 288 ? 0.5908 0.5573 0.5309 0.0796  -0.0203 0.0038  304 PHE A CD2 
2279 C CE1 . PHE A 288 ? 0.6082 0.5453 0.5447 0.0785  -0.0095 0.0093  304 PHE A CE1 
2280 C CE2 . PHE A 288 ? 0.6270 0.5771 0.5659 0.0766  -0.0161 -0.0024 304 PHE A CE2 
2281 C CZ  . PHE A 288 ? 0.6238 0.5596 0.5594 0.0759  -0.0112 0.0000  304 PHE A CZ  
2282 N N   . SER A 289 ? 0.5423 0.5641 0.5060 0.0961  -0.0362 0.0591  305 SER A N   
2283 C CA  . SER A 289 ? 0.5478 0.5914 0.5088 0.0977  -0.0451 0.0737  305 SER A CA  
2284 C C   . SER A 289 ? 0.6005 0.6395 0.5774 0.1032  -0.0418 0.0938  305 SER A C   
2285 O O   . SER A 289 ? 0.5389 0.5669 0.5392 0.1078  -0.0372 0.0973  305 SER A O   
2286 C CB  . SER A 289 ? 0.5648 0.6260 0.5350 0.0976  -0.0558 0.0727  305 SER A CB  
2287 O OG  . SER A 289 ? 0.6197 0.6998 0.5963 0.1006  -0.0646 0.0918  305 SER A OG  
2288 N N   . TYR A 290 ? 0.5399 0.5880 0.5053 0.1027  -0.0433 0.1073  306 TYR A N   
2289 C CA  . TYR A 290 ? 0.5741 0.6194 0.5571 0.1076  -0.0414 0.1294  306 TYR A CA  
2290 C C   . TYR A 290 ? 0.6307 0.6892 0.6365 0.1130  -0.0497 0.1437  306 TYR A C   
2291 O O   . TYR A 290 ? 0.6492 0.6967 0.6828 0.1190  -0.0455 0.1555  306 TYR A O   
2292 C CB  . TYR A 290 ? 0.5628 0.6198 0.5283 0.1052  -0.0421 0.1436  306 TYR A CB  
2293 C CG  . TYR A 290 ? 0.6197 0.6644 0.5693 0.1006  -0.0330 0.1312  306 TYR A CG  
2294 C CD1 . TYR A 290 ? 0.5224 0.5426 0.4861 0.1009  -0.0235 0.1309  306 TYR A CD1 
2295 C CD2 . TYR A 290 ? 0.5880 0.6450 0.5109 0.0957  -0.0342 0.1182  306 TYR A CD2 
2296 C CE1 . TYR A 290 ? 0.5333 0.5439 0.4857 0.0962  -0.0167 0.1206  306 TYR A CE1 
2297 C CE2 . TYR A 290 ? 0.6071 0.6538 0.5205 0.0921  -0.0257 0.1074  306 TYR A CE2 
2298 C CZ  . TYR A 290 ? 0.5524 0.5766 0.4813 0.0922  -0.0176 0.1097  306 TYR A CZ  
2299 O OH  . TYR A 290 ? 0.5659 0.5814 0.4888 0.0882  -0.0106 0.1005  306 TYR A OH  
2300 N N   . MET A 291 ? 0.6133 0.6953 0.6100 0.1108  -0.0618 0.1425  307 MET A N   
2301 C CA  . MET A 291 ? 0.6389 0.7367 0.6599 0.1155  -0.0716 0.1584  307 MET A CA  
2302 C C   . MET A 291 ? 0.6748 0.7607 0.7258 0.1198  -0.0664 0.1499  307 MET A C   
2303 O O   . MET A 291 ? 0.6395 0.7292 0.7219 0.1265  -0.0681 0.1651  307 MET A O   
2304 C CB  . MET A 291 ? 0.6478 0.7755 0.6508 0.1109  -0.0881 0.1593  307 MET A CB  
2305 C CG  . MET A 291 ? 0.8194 0.9686 0.8444 0.1151  -0.1011 0.1844  307 MET A CG  
2306 S SD  . MET A 291 ? 1.0784 1.2623 1.0685 0.1088  -0.1191 0.1959  307 MET A SD  
2307 C CE  . MET A 291 ? 0.7822 0.9702 0.7458 0.1003  -0.1232 0.1619  307 MET A CE  
2308 N N   . TYR A 292 ? 0.6305 0.7035 0.6737 0.1164  -0.0597 0.1271  308 TYR A N   
2309 C CA  . TYR A 292 ? 0.6773 0.7391 0.7468 0.1202  -0.0521 0.1198  308 TYR A CA  
2310 C C   . TYR A 292 ? 0.7362 0.7744 0.8238 0.1264  -0.0384 0.1244  308 TYR A C   
2311 O O   . TYR A 292 ? 0.7066 0.7428 0.8260 0.1336  -0.0343 0.1321  308 TYR A O   
2312 C CB  . TYR A 292 ? 0.6752 0.7280 0.7306 0.1144  -0.0476 0.0966  308 TYR A CB  
2313 C CG  . TYR A 292 ? 0.7027 0.7493 0.7820 0.1170  -0.0401 0.0894  308 TYR A CG  
2314 C CD1 . TYR A 292 ? 0.6924 0.7588 0.7912 0.1172  -0.0485 0.0924  308 TYR A CD1 
2315 C CD2 . TYR A 292 ? 0.6816 0.7040 0.7630 0.1185  -0.0248 0.0795  308 TYR A CD2 
2316 C CE1 . TYR A 292 ? 0.6929 0.7560 0.8152 0.1193  -0.0402 0.0870  308 TYR A CE1 
2317 C CE2 . TYR A 292 ? 0.7418 0.7604 0.8426 0.1207  -0.0160 0.0730  308 TYR A CE2 
2318 C CZ  . TYR A 292 ? 0.7704 0.8100 0.8929 0.1213  -0.0229 0.0773  308 TYR A CZ  
2319 O OH  . TYR A 292 ? 0.8682 0.9074 1.0122 0.1231  -0.0133 0.0724  308 TYR A OH  
2320 N N   . SER A 293 ? 0.8244 0.8447 0.8935 0.1236  -0.0312 0.1189  309 SER A N   
2321 C CA  . SER A 293 ? 0.8408 0.8350 0.9195 0.1266  -0.0188 0.1183  309 SER A CA  
2322 C C   . SER A 293 ? 0.8183 0.8117 0.9237 0.1337  -0.0187 0.1401  309 SER A C   
2323 O O   . SER A 293 ? 0.8611 0.8316 0.9767 0.1358  -0.0091 0.1397  309 SER A O   
2324 C CB  . SER A 293 ? 0.7861 0.7687 0.8376 0.1199  -0.0158 0.1101  309 SER A CB  
2325 O OG  . SER A 293 ? 0.7813 0.7623 0.8121 0.1139  -0.0153 0.0905  309 SER A OG  
2326 N N   . THR A 294 ? 0.8417 0.8586 0.9591 0.1368  -0.0301 0.1595  310 THR A N   
2327 C CA  . THR A 294 ? 0.9375 0.9550 1.0847 0.1440  -0.0313 0.1836  310 THR A CA  
2328 C C   . THR A 294 ? 0.9317 0.9641 1.1126 0.1513  -0.0360 0.1930  310 THR A C   
2329 O O   . THR A 294 ? 0.8932 0.9482 1.0675 0.1485  -0.0465 0.1908  310 THR A O   
2330 C CB  . THR A 294 ? 0.9316 0.9665 1.0634 0.1409  -0.0418 0.2055  310 THR A CB  
2331 O OG1 . THR A 294 ? 0.8242 0.8857 0.9271 0.1348  -0.0544 0.2030  310 THR A OG1 
2332 C CG2 . THR A 294 ? 0.8394 0.8560 0.9540 0.1363  -0.0337 0.2030  310 THR A CG2 
2333 N N   . ALA A 295 ? 1.0533 1.0726 1.2731 0.1604  -0.0282 0.2025  311 ALA A N   
2334 C CA  . ALA A 295 ? 1.0601 1.0933 1.3202 0.1689  -0.0313 0.2141  311 ALA A CA  
2335 C C   . ALA A 295 ? 1.0198 1.0391 1.3227 0.1791  -0.0249 0.2320  311 ALA A C   
2336 O O   . ALA A 295 ? 1.0291 1.0275 1.3287 0.1786  -0.0186 0.2346  311 ALA A O   
2337 C CB  . ALA A 295 ? 1.0538 1.0825 1.3212 0.1700  -0.0214 0.1918  311 ALA A CB  
2338 N N   A PRO A 306 ? 1.1449 0.8658 1.3933 0.1761  0.1387  -0.0159 322 PRO A N   
2339 N N   B PRO A 306 ? 1.1440 0.8522 1.3897 0.1742  0.1403  -0.0225 322 PRO A N   
2340 C CA  A PRO A 306 ? 1.1385 0.8514 1.3421 0.1668  0.1448  -0.0414 322 PRO A CA  
2341 C CA  B PRO A 306 ? 1.1399 0.8517 1.3392 0.1652  0.1432  -0.0418 322 PRO A CA  
2342 C C   A PRO A 306 ? 1.1288 0.8371 1.2952 0.1527  0.1299  -0.0427 322 PRO A C   
2343 C C   B PRO A 306 ? 1.1300 0.8403 1.2911 0.1511  0.1279  -0.0420 322 PRO A C   
2344 O O   A PRO A 306 ? 1.1165 0.8030 1.2863 0.1486  0.1265  -0.0459 322 PRO A O   
2345 O O   B PRO A 306 ? 1.1197 0.8089 1.2800 0.1459  0.1237  -0.0460 322 PRO A O   
2346 C CB  A PRO A 306 ? 1.1518 0.8938 1.3467 0.1685  0.1463  -0.0370 322 PRO A CB  
2347 C CB  B PRO A 306 ? 1.1460 0.8905 1.3494 0.1694  0.1417  -0.0289 322 PRO A CB  
2348 C CG  A PRO A 306 ? 1.1182 0.8866 1.3371 0.1724  0.1312  -0.0071 322 PRO A CG  
2349 C CG  B PRO A 306 ? 1.1297 0.8922 1.3630 0.1741  0.1271  0.0010  322 PRO A CG  
2350 C CD  A PRO A 306 ? 1.1372 0.8922 1.3851 0.1761  0.1253  0.0071  322 PRO A CD  
2351 C CD  B PRO A 306 ? 1.1396 0.8788 1.3979 0.1767  0.1261  0.0065  322 PRO A CD  
2352 N N   A LEU A 307 ? 1.1434 0.8723 1.2784 0.1455  0.1213  -0.0396 323 LEU A N   
2353 N N   B LEU A 307 ? 1.1429 0.8759 1.2762 0.1451  0.1196  -0.0374 323 LEU A N   
2354 C CA  A LEU A 307 ? 1.1369 0.8673 1.2411 0.1333  0.1065  -0.0374 323 LEU A CA  
2355 C CA  B LEU A 307 ? 1.1299 0.8679 1.2342 0.1335  0.1039  -0.0325 323 LEU A CA  
2356 C C   A LEU A 307 ? 1.0862 0.8371 1.2017 0.1336  0.0916  -0.0116 323 LEU A C   
2357 C C   B LEU A 307 ? 1.0874 0.8473 1.2084 0.1360  0.0907  -0.0059 323 LEU A C   
2358 O O   A LEU A 307 ? 1.0781 0.8340 1.1710 0.1245  0.0801  -0.0080 323 LEU A O   
2359 O O   B LEU A 307 ? 1.0875 0.8428 1.2388 0.1416  0.0892  0.0082  323 LEU A O   
2360 C CB  A LEU A 307 ? 1.1073 0.8474 1.1722 0.1252  0.1057  -0.0490 323 LEU A CB  
2361 C CB  B LEU A 307 ? 1.0997 0.8478 1.1655 0.1255  0.1028  -0.0436 323 LEU A CB  
2362 C CG  A LEU A 307 ? 1.1270 0.8508 1.1706 0.1228  0.1196  -0.0741 323 LEU A CG  
2363 C CG  B LEU A 307 ? 1.1229 0.8528 1.1677 0.1227  0.1164  -0.0688 323 LEU A CG  
2364 C CD1 A LEU A 307 ? 1.0323 0.7684 1.0378 0.1139  0.1162  -0.0798 323 LEU A CD1 
2365 C CD1 B LEU A 307 ? 1.0339 0.7750 1.0409 0.1140  0.1138  -0.0757 323 LEU A CD1 
2366 C CD2 A LEU A 307 ? 1.0791 0.7729 1.1165 0.1176  0.1207  -0.0898 323 LEU A CD2 
2367 C CD2 B LEU A 307 ? 1.0837 0.7841 1.1228 0.1174  0.1166  -0.0830 323 LEU A CD2 
2368 N N   A ALA A 308 ? 1.0674 0.8308 1.2175 0.1438  0.0917  0.0065  324 ALA A N   
2369 N N   B ALA A 308 ? 1.0950 0.8790 1.1970 0.1318  0.0811  0.0016  324 ALA A N   
2370 C CA  A ALA A 308 ? 1.0338 0.8215 1.1896 0.1439  0.0776  0.0309  324 ALA A CA  
2371 C CA  B ALA A 308 ? 1.0657 0.8724 1.1784 0.1336  0.0686  0.0247  324 ALA A CA  
2372 C C   A ALA A 308 ? 0.9969 0.7771 1.1473 0.1373  0.0682  0.0402  324 ALA A C   
2373 C C   B ALA A 308 ? 1.0329 0.8659 1.1366 0.1335  0.0641  0.0278  324 ALA A C   
2374 O O   A ALA A 308 ? 1.0007 0.7961 1.1290 0.1303  0.0576  0.0469  324 ALA A O   
2375 O O   B ALA A 308 ? 0.9774 0.8221 1.0566 0.1261  0.0549  0.0278  324 ALA A O   
2376 C CB  A ALA A 308 ? 1.0327 0.8331 1.2292 0.1558  0.0786  0.0495  324 ALA A CB  
2377 C CB  B ALA A 308 ? 1.0379 0.8430 1.1346 0.1253  0.0578  0.0310  324 ALA A CB  
2378 N N   A GLY A 309 ? 0.9358 0.6926 1.1082 0.1392  0.0728  0.0402  325 GLY A N   
2379 N N   B GLY A 309 ? 1.0522 0.8945 1.1796 0.1419  0.0709  0.0305  325 GLY A N   
2380 C CA  A GLY A 309 ? 0.9176 0.6699 1.0924 0.1334  0.0644  0.0534  325 GLY A CA  
2381 C CA  B GLY A 309 ? 0.9745 0.8437 1.1023 0.1422  0.0647  0.0372  325 GLY A CA  
2382 C C   A GLY A 309 ? 0.8511 0.5813 1.0062 0.1226  0.0642  0.0364  325 GLY A C   
2383 C C   B GLY A 309 ? 0.9303 0.8207 1.0622 0.1417  0.0488  0.0569  325 GLY A C   
2384 O O   A GLY A 309 ? 0.8348 0.5501 1.0062 0.1197  0.0623  0.0433  325 GLY A O   
2385 O O   B GLY A 309 ? 0.9443 0.8530 1.0598 0.1365  0.0391  0.0583  325 GLY A O   
2386 N N   A PHE A 310 ? 0.8210 0.5495 0.9428 0.1159  0.0651  0.0160  326 PHE A N   
2387 N N   B PHE A 310 ? 0.8986 0.7866 1.0519 0.1468  0.0460  0.0725  326 PHE A N   
2388 C CA  A PHE A 310 ? 0.8281 0.5366 0.9323 0.1051  0.0630  0.0003  326 PHE A CA  
2389 C CA  B PHE A 310 ? 0.8846 0.7918 1.0374 0.1457  0.0314  0.0925  326 PHE A CA  
2390 C C   A PHE A 310 ? 0.8564 0.5793 0.9376 0.0953  0.0514  0.0068  326 PHE A C   
2391 C C   B PHE A 310 ? 0.8645 0.7572 1.0043 0.1408  0.0294  0.0956  326 PHE A C   
2392 O O   A PHE A 310 ? 0.9599 0.6699 1.0404 0.0870  0.0470  0.0044  326 PHE A O   
2393 O O   B PHE A 310 ? 0.8902 0.7612 1.0466 0.1437  0.0369  0.0956  326 PHE A O   
2394 C CB  A PHE A 310 ? 0.7622 0.4559 0.8446 0.1026  0.0711  -0.0272 326 PHE A CB  
2395 C CB  B PHE A 310 ? 0.8552 0.7760 1.0459 0.1553  0.0279  0.1138  326 PHE A CB  
2396 C CG  A PHE A 310 ? 0.8272 0.4911 0.9281 0.1054  0.0814  -0.0425 326 PHE A CG  
2397 C CG  B PHE A 310 ? 0.8780 0.8148 1.0890 0.1607  0.0297  0.1129  326 PHE A CG  
2398 C CD1 A PHE A 310 ? 0.8237 0.4642 0.9281 0.0972  0.0776  -0.0502 326 PHE A CD1 
2399 C CD1 B PHE A 310 ? 0.8684 0.8332 1.0718 0.1573  0.0170  0.1186  326 PHE A CD1 
2400 C CD2 A PHE A 310 ? 0.8569 0.5160 0.9759 0.1164  0.0950  -0.0490 326 PHE A CD2 
2401 C CD2 B PHE A 310 ? 0.8790 0.8034 1.1186 0.1689  0.0447  0.1058  326 PHE A CD2 
2402 C CE1 A PHE A 310 ? 0.7734 0.3841 0.8967 0.0995  0.0870  -0.0664 326 PHE A CE1 
2403 C CE1 B PHE A 310 ? 0.8459 0.8264 1.0720 0.1614  0.0181  0.1188  326 PHE A CE1 
2404 C CE2 A PHE A 310 ? 0.8226 0.4529 0.9608 0.1197  0.1058  -0.0650 326 PHE A CE2 
2405 C CE2 B PHE A 310 ? 0.8559 0.7969 1.1177 0.1738  0.0477  0.1061  326 PHE A CE2 
2406 C CZ  A PHE A 310 ? 0.7778 0.3829 0.9175 0.1111  0.1015  -0.0745 326 PHE A CZ  
2407 C CZ  B PHE A 310 ? 0.8393 0.8087 1.0955 0.1698  0.0339  0.1135  326 PHE A CZ  
2408 N N   A GLY A 311 ? 0.8002 0.5492 0.8656 0.0961  0.0465  0.0146  327 GLY A N   
2409 N N   B GLY A 311 ? 0.8260 0.7306 0.9386 0.1332  0.0201  0.0977  327 GLY A N   
2410 C CA  A GLY A 311 ? 0.8278 0.5909 0.8738 0.0881  0.0373  0.0192  327 GLY A CA  
2411 C CA  B GLY A 311 ? 0.7303 0.6256 0.8319 0.1280  0.0183  0.1023  327 GLY A CA  
2412 C C   A GLY A 311 ? 0.7586 0.5454 0.8127 0.0912  0.0319  0.0423  327 GLY A C   
2413 C C   B GLY A 311 ? 0.6699 0.5778 0.7392 0.1197  0.0114  0.0974  327 GLY A C   
2414 O O   A GLY A 311 ? 0.7499 0.5436 0.8245 0.0992  0.0335  0.0568  327 GLY A O   
2415 O O   B GLY A 311 ? 0.6496 0.5665 0.7036 0.1171  0.0094  0.0856  327 GLY A O   
2416 N N   A TYR A 312 ? 0.7416 0.5419 0.7791 0.0848  0.0254  0.0453  328 TYR A N   
2417 N N   B TYR A 312 ? 0.6465 0.5551 0.7079 0.1156  0.0086  0.1067  328 TYR A N   
2418 C CA  A TYR A 312 ? 0.6906 0.5147 0.7295 0.0863  0.0209  0.0647  328 TYR A CA  
2419 C CA  B TYR A 312 ? 0.6232 0.5447 0.6573 0.1086  0.0037  0.1030  328 TYR A CA  
2420 C C   A TYR A 312 ? 0.6795 0.5262 0.7090 0.0917  0.0187  0.0674  328 TYR A C   
2421 C C   B TYR A 312 ? 0.6086 0.5131 0.6279 0.1019  0.0078  0.0847  328 TYR A C   
2422 O O   A TYR A 312 ? 0.6398 0.5065 0.6714 0.0944  0.0151  0.0837  328 TYR A O   
2423 O O   B TYR A 312 ? 0.4749 0.3863 0.4776 0.0964  0.0053  0.0831  328 TYR A O   
2424 C CB  A TYR A 312 ? 0.6920 0.5227 0.7181 0.0781  0.0168  0.0649  328 TYR A CB  
2425 C CB  B TYR A 312 ? 0.5229 0.4562 0.5561 0.1073  0.0003  0.1229  328 TYR A CB  
2426 C CG  A TYR A 312 ? 0.7691 0.5849 0.8113 0.0725  0.0173  0.0707  328 TYR A CG  
2427 C CG  B TYR A 312 ? 0.6012 0.5590 0.6384 0.1116  -0.0073 0.1419  328 TYR A CG  
2428 C CD1 A TYR A 312 ? 0.8348 0.6251 0.8806 0.0673  0.0181  0.0556  328 TYR A CD1 
2429 C CD1 B TYR A 312 ? 0.5945 0.5651 0.6348 0.1154  -0.0124 0.1390  328 TYR A CD1 
2430 C CD2 A TYR A 312 ? 0.7772 0.6050 0.8306 0.0718  0.0170  0.0912  328 TYR A CD2 
2431 C CD2 B TYR A 312 ? 0.5358 0.5056 0.5738 0.1112  -0.0100 0.1643  328 TYR A CD2 
2432 C CE1 A TYR A 312 ? 0.8094 0.5853 0.8728 0.0612  0.0174  0.0601  328 TYR A CE1 
2433 C CE1 B TYR A 312 ? 0.6066 0.6013 0.6507 0.1185  -0.0217 0.1570  328 TYR A CE1 
2434 C CE2 A TYR A 312 ? 0.8441 0.6585 0.9162 0.0661  0.0176  0.0978  328 TYR A CE2 
2435 C CE2 B TYR A 312 ? 0.5420 0.5360 0.5808 0.1144  -0.0184 0.1829  328 TYR A CE2 
2436 C CZ  A TYR A 312 ? 0.8663 0.6540 0.9447 0.0606  0.0172  0.0818  328 TYR A CZ  
2437 C CZ  B TYR A 312 ? 0.4984 0.5049 0.5402 0.1179  -0.0251 0.1788  328 TYR A CZ  
2438 O OH  A TYR A 312 ? 0.9363 0.7097 1.0358 0.0538  0.0166  0.0873  328 TYR A OH  
2439 O OH  B TYR A 312 ? 0.6047 0.6368 0.6473 0.1203  -0.0358 0.1979  328 TYR A OH  
2440 N N   A GLY A 313 ? 0.6413 0.4863 0.6604 0.0925  0.0203  0.0523  329 GLY A N   
2441 N N   B GLY A 313 ? 0.6163 0.4998 0.6414 0.1023  0.0140  0.0712  329 GLY A N   
2442 C CA  A GLY A 313 ? 0.6208 0.4865 0.6336 0.0963  0.0173  0.0538  329 GLY A CA  
2443 C CA  B GLY A 313 ? 0.6219 0.4889 0.6331 0.0953  0.0164  0.0553  329 GLY A CA  
2444 C C   A GLY A 313 ? 0.6169 0.4945 0.6070 0.0906  0.0124  0.0454  329 GLY A C   
2445 C C   B GLY A 313 ? 0.6160 0.4948 0.6051 0.0903  0.0119  0.0456  329 GLY A C   
2446 O O   A GLY A 313 ? 0.6124 0.4878 0.5931 0.0847  0.0104  0.0431  329 GLY A O   
2447 O O   B GLY A 313 ? 0.6116 0.4886 0.5902 0.0842  0.0099  0.0423  329 GLY A O   
2448 N N   . LEU A 314 ? 0.5752 0.4660 0.5603 0.0927  0.0103  0.0413  330 LEU A N   
2449 C CA  . LEU A 314 ? 0.5731 0.4738 0.5409 0.0879  0.0058  0.0324  330 LEU A CA  
2450 C C   . LEU A 314 ? 0.5674 0.4862 0.5275 0.0865  0.0003  0.0395  330 LEU A C   
2451 O O   . LEU A 314 ? 0.5151 0.4342 0.4643 0.0816  -0.0011 0.0328  330 LEU A O   
2452 C CB  . LEU A 314 ? 0.5877 0.4959 0.5563 0.0899  0.0054  0.0264  330 LEU A CB  
2453 C CG  . LEU A 314 ? 0.6273 0.5190 0.5965 0.0895  0.0125  0.0159  330 LEU A CG  
2454 C CD1 . LEU A 314 ? 0.5817 0.4838 0.5572 0.0922  0.0135  0.0138  330 LEU A CD1 
2455 C CD2 . LEU A 314 ? 0.6229 0.5037 0.5751 0.0820  0.0116  0.0054  330 LEU A CD2 
2456 N N   . PRO A 315 ? 0.5512 0.4865 0.5158 0.0905  -0.0029 0.0526  331 PRO A N   
2457 C CA  . PRO A 315 ? 0.5881 0.5410 0.5406 0.0884  -0.0064 0.0579  331 PRO A CA  
2458 C C   . PRO A 315 ? 0.5275 0.4727 0.4780 0.0845  -0.0025 0.0603  331 PRO A C   
2459 O O   . PRO A 315 ? 0.5349 0.4867 0.4743 0.0809  -0.0027 0.0537  331 PRO A O   
2460 C CB  . PRO A 315 ? 0.5418 0.5107 0.5008 0.0931  -0.0100 0.0755  331 PRO A CB  
2461 C CG  . PRO A 315 ? 0.5525 0.5176 0.5277 0.0979  -0.0106 0.0763  331 PRO A CG  
2462 C CD  . PRO A 315 ? 0.5083 0.4500 0.4882 0.0968  -0.0039 0.0624  331 PRO A CD  
2463 N N   . ILE A 316 ? 0.5043 0.4352 0.4685 0.0850  0.0012  0.0691  332 ILE A N   
2464 C CA  . ILE A 316 ? 0.5012 0.4254 0.4681 0.0806  0.0043  0.0733  332 ILE A CA  
2465 C C   . ILE A 316 ? 0.5684 0.4788 0.5305 0.0749  0.0047  0.0572  332 ILE A C   
2466 O O   . ILE A 316 ? 0.5892 0.5033 0.5485 0.0706  0.0052  0.0565  332 ILE A O   
2467 C CB  . ILE A 316 ? 0.5569 0.4681 0.5436 0.0822  0.0073  0.0870  332 ILE A CB  
2468 C CG1 . ILE A 316 ? 0.5287 0.4583 0.5197 0.0870  0.0056  0.1075  332 ILE A CG1 
2469 C CG2 . ILE A 316 ? 0.5623 0.4615 0.5564 0.0761  0.0100  0.0888  332 ILE A CG2 
2470 C CD1 . ILE A 316 ? 0.5448 0.4628 0.5603 0.0897  0.0080  0.1246  332 ILE A CD1 
2471 N N   . SER A 317 ? 0.5623 0.4584 0.5235 0.0749  0.0044  0.0451  333 SER A N   
2472 C CA  . SER A 317 ? 0.5496 0.4353 0.5035 0.0692  0.0030  0.0314  333 SER A CA  
2473 C C   . SER A 317 ? 0.5530 0.4540 0.4970 0.0673  0.0000  0.0267  333 SER A C   
2474 O O   . SER A 317 ? 0.5655 0.4641 0.5094 0.0625  -0.0012 0.0230  333 SER A O   
2475 C CB  . SER A 317 ? 0.5718 0.4445 0.5220 0.0697  0.0039  0.0203  333 SER A CB  
2476 O OG  . SER A 317 ? 0.6277 0.4820 0.5871 0.0704  0.0078  0.0205  333 SER A OG  
2477 N N   . ARG A 318 ? 0.5172 0.4340 0.4554 0.0711  -0.0015 0.0262  334 ARG A N   
2478 C CA  . ARG A 318 ? 0.5046 0.4342 0.4354 0.0696  -0.0036 0.0194  334 ARG A CA  
2479 C C   . ARG A 318 ? 0.5225 0.4637 0.4534 0.0688  -0.0008 0.0261  334 ARG A C   
2480 O O   . ARG A 318 ? 0.5099 0.4552 0.4404 0.0664  -0.0005 0.0198  334 ARG A O   
2481 C CB  . ARG A 318 ? 0.5082 0.4512 0.4333 0.0729  -0.0067 0.0157  334 ARG A CB  
2482 C CG  . ARG A 318 ? 0.5364 0.4903 0.4556 0.0714  -0.0088 0.0055  334 ARG A CG  
2483 C CD  . ARG A 318 ? 0.5759 0.5385 0.4924 0.0729  -0.0135 -0.0013 334 ARG A CD  
2484 N NE  . ARG A 318 ? 0.6106 0.5891 0.5225 0.0761  -0.0156 0.0060  334 ARG A NE  
2485 C CZ  . ARG A 318 ? 0.6926 0.6830 0.6020 0.0769  -0.0212 0.0014  334 ARG A CZ  
2486 N NH1 . ARG A 318 ? 0.5355 0.5224 0.4492 0.0748  -0.0244 -0.0101 334 ARG A NH1 
2487 N NH2 . ARG A 318 ? 0.5334 0.5402 0.4373 0.0791  -0.0246 0.0098  334 ARG A NH2 
2488 N N   . LEU A 319 ? 0.5042 0.4513 0.4380 0.0708  0.0019  0.0401  335 LEU A N   
2489 C CA  . LEU A 319 ? 0.5127 0.4720 0.4470 0.0695  0.0063  0.0485  335 LEU A CA  
2490 C C   . LEU A 319 ? 0.4855 0.4325 0.4320 0.0644  0.0083  0.0485  335 LEU A C   
2491 O O   . LEU A 319 ? 0.5280 0.4846 0.4767 0.0624  0.0116  0.0479  335 LEU A O   
2492 C CB  . LEU A 319 ? 0.4927 0.4611 0.4281 0.0723  0.0083  0.0666  335 LEU A CB  
2493 C CG  . LEU A 319 ? 0.5361 0.5221 0.4593 0.0767  0.0047  0.0704  335 LEU A CG  
2494 C CD1 . LEU A 319 ? 0.5095 0.5018 0.4381 0.0788  0.0056  0.0915  335 LEU A CD1 
2495 C CD2 . LEU A 319 ? 0.5110 0.5182 0.4166 0.0765  0.0054  0.0626  335 LEU A CD2 
2496 N N   . TYR A 320 ? 0.5060 0.4324 0.4616 0.0620  0.0063  0.0484  336 TYR A N   
2497 C CA  . TYR A 320 ? 0.5277 0.4423 0.4942 0.0557  0.0054  0.0461  336 TYR A CA  
2498 C C   . TYR A 320 ? 0.5142 0.4320 0.4775 0.0533  0.0024  0.0342  336 TYR A C   
2499 O O   . TYR A 320 ? 0.5171 0.4399 0.4903 0.0499  0.0034  0.0357  336 TYR A O   
2500 C CB  . TYR A 320 ? 0.5203 0.4110 0.4922 0.0531  0.0026  0.0427  336 TYR A CB  
2501 C CG  . TYR A 320 ? 0.5861 0.4687 0.5713 0.0536  0.0056  0.0554  336 TYR A CG  
2502 C CD1 . TYR A 320 ? 0.5189 0.4065 0.5182 0.0504  0.0084  0.0682  336 TYR A CD1 
2503 C CD2 . TYR A 320 ? 0.6475 0.5171 0.6349 0.0573  0.0063  0.0550  336 TYR A CD2 
2504 C CE1 . TYR A 320 ? 0.6466 0.5256 0.6617 0.0505  0.0109  0.0814  336 TYR A CE1 
2505 C CE2 . TYR A 320 ? 0.6792 0.5398 0.6831 0.0583  0.0091  0.0668  336 TYR A CE2 
2506 C CZ  . TYR A 320 ? 0.7167 0.5815 0.7345 0.0547  0.0109  0.0805  336 TYR A CZ  
2507 O OH  . TYR A 320 ? 0.7841 0.6388 0.8217 0.0554  0.0133  0.0938  336 TYR A OH  
2508 N N   . ALA A 321 ? 0.4985 0.4147 0.4514 0.0553  -0.0010 0.0235  337 ALA A N   
2509 C CA  . ALA A 321 ? 0.5343 0.4535 0.4870 0.0535  -0.0043 0.0138  337 ALA A CA  
2510 C C   . ALA A 321 ? 0.5461 0.4847 0.5009 0.0561  0.0003  0.0138  337 ALA A C   
2511 O O   . ALA A 321 ? 0.5180 0.4599 0.4834 0.0539  0.0003  0.0112  337 ALA A O   
2512 C CB  . ALA A 321 ? 0.4936 0.4083 0.4365 0.0551  -0.0080 0.0048  337 ALA A CB  
2513 N N   . LYS A 322 ? 0.5122 0.4646 0.4576 0.0607  0.0043  0.0166  338 LYS A N   
2514 C CA  . LYS A 322 ? 0.5181 0.4896 0.4610 0.0632  0.0099  0.0139  338 LYS A CA  
2515 C C   . LYS A 322 ? 0.5391 0.5193 0.4922 0.0616  0.0172  0.0240  338 LYS A C   
2516 O O   . LYS A 322 ? 0.4756 0.4695 0.4319 0.0629  0.0232  0.0197  338 LYS A O   
2517 C CB  . LYS A 322 ? 0.5145 0.4996 0.4408 0.0674  0.0107  0.0140  338 LYS A CB  
2518 C CG  . LYS A 322 ? 0.6113 0.5937 0.5309 0.0688  0.0045  0.0016  338 LYS A CG  
2519 C CD  . LYS A 322 ? 0.6177 0.6153 0.5221 0.0719  0.0031  0.0019  338 LYS A CD  
2520 C CE  . LYS A 322 ? 0.6189 0.6133 0.5214 0.0723  -0.0039 -0.0100 338 LYS A CE  
2521 N NZ  . LYS A 322 ? 0.7265 0.7356 0.6166 0.0743  -0.0078 -0.0094 338 LYS A NZ  
2522 N N   . TYR A 323 ? 0.5082 0.4803 0.4692 0.0587  0.0174  0.0367  339 TYR A N   
2523 C CA  . TYR A 323 ? 0.5574 0.5394 0.5297 0.0567  0.0250  0.0496  339 TYR A CA  
2524 C C   . TYR A 323 ? 0.5437 0.5309 0.5332 0.0542  0.0278  0.0455  339 TYR A C   
2525 O O   . TYR A 323 ? 0.4995 0.5040 0.4950 0.0549  0.0375  0.0516  339 TYR A O   
2526 C CB  . TYR A 323 ? 0.4905 0.4576 0.4735 0.0530  0.0227  0.0623  339 TYR A CB  
2527 C CG  . TYR A 323 ? 0.5353 0.5093 0.5358 0.0493  0.0292  0.0771  339 TYR A CG  
2528 C CD1 . TYR A 323 ? 0.5052 0.5025 0.5018 0.0517  0.0395  0.0868  339 TYR A CD1 
2529 C CD2 . TYR A 323 ? 0.5063 0.4641 0.5273 0.0427  0.0252  0.0815  339 TYR A CD2 
2530 C CE1 . TYR A 323 ? 0.5343 0.5396 0.5489 0.0479  0.0469  0.1024  339 TYR A CE1 
2531 C CE2 . TYR A 323 ? 0.5461 0.5108 0.5874 0.0385  0.0310  0.0964  339 TYR A CE2 
2532 C CZ  . TYR A 323 ? 0.5153 0.5041 0.5542 0.0413  0.0424  0.1077  339 TYR A CZ  
2533 O OH  . TYR A 323 ? 0.5394 0.5369 0.5998 0.0368  0.0495  0.1242  339 TYR A OH  
2534 N N   . PHE A 324 ? 0.5352 0.5088 0.5339 0.0512  0.0198  0.0366  340 PHE A N   
2535 C CA  . PHE A 324 ? 0.5506 0.5294 0.5687 0.0493  0.0204  0.0327  340 PHE A CA  
2536 C C   . PHE A 324 ? 0.5439 0.5240 0.5587 0.0529  0.0175  0.0180  340 PHE A C   
2537 O O   . PHE A 324 ? 0.5056 0.4797 0.5355 0.0503  0.0111  0.0140  340 PHE A O   
2538 C CB  . PHE A 324 ? 0.5152 0.4794 0.5512 0.0418  0.0116  0.0368  340 PHE A CB  
2539 C CG  . PHE A 324 ? 0.5477 0.5136 0.5986 0.0373  0.0156  0.0512  340 PHE A CG  
2540 C CD1 . PHE A 324 ? 0.5674 0.5518 0.6367 0.0373  0.0252  0.0591  340 PHE A CD1 
2541 C CD2 . PHE A 324 ? 0.5310 0.4798 0.5798 0.0330  0.0104  0.0566  340 PHE A CD2 
2542 C CE1 . PHE A 324 ? 0.5856 0.5721 0.6719 0.0324  0.0290  0.0741  340 PHE A CE1 
2543 C CE2 . PHE A 324 ? 0.5611 0.5098 0.6273 0.0283  0.0136  0.0702  340 PHE A CE2 
2544 C CZ  . PHE A 324 ? 0.5657 0.5337 0.6510 0.0276  0.0226  0.0799  340 PHE A CZ  
2545 N N   . GLN A 325 ? 0.5506 0.5390 0.5475 0.0583  0.0215  0.0107  341 GLN A N   
2546 C CA  . GLN A 325 ? 0.5327 0.5243 0.5283 0.0621  0.0209  -0.0040 341 GLN A CA  
2547 C C   . GLN A 325 ? 0.5727 0.5472 0.5655 0.0602  0.0094  -0.0101 341 GLN A C   
2548 O O   . GLN A 325 ? 0.5712 0.5446 0.5722 0.0616  0.0068  -0.0196 341 GLN A O   
2549 C CB  . GLN A 325 ? 0.5270 0.5281 0.5459 0.0635  0.0265  -0.0081 341 GLN A CB  
2550 C CG  . GLN A 325 ? 0.5594 0.5796 0.5841 0.0652  0.0404  -0.0019 341 GLN A CG  
2551 C CD  . GLN A 325 ? 0.6280 0.6634 0.6283 0.0700  0.0498  -0.0071 341 GLN A CD  
2552 O OE1 . GLN A 325 ? 0.6047 0.6408 0.5934 0.0734  0.0486  -0.0216 341 GLN A OE1 
2553 N NE2 . GLN A 325 ? 0.5528 0.6006 0.5450 0.0694  0.0583  0.0055  341 GLN A NE2 
2554 N N   . GLY A 326 ? 0.5431 0.5046 0.5260 0.0572  0.0034  -0.0046 342 GLY A N   
2555 C CA  . GLY A 326 ? 0.4825 0.4296 0.4593 0.0554  -0.0053 -0.0094 342 GLY A CA  
2556 C C   . GLY A 326 ? 0.5691 0.5178 0.5290 0.0589  -0.0052 -0.0137 342 GLY A C   
2557 O O   . GLY A 326 ? 0.5002 0.4622 0.4523 0.0627  0.0000  -0.0154 342 GLY A O   
2558 N N   . ASP A 327 ? 0.5354 0.4715 0.4893 0.0571  -0.0111 -0.0150 343 ASP A N   
2559 C CA  . ASP A 327 ? 0.5287 0.4669 0.4711 0.0599  -0.0116 -0.0181 343 ASP A CA  
2560 C C   . ASP A 327 ? 0.5415 0.4649 0.4791 0.0575  -0.0152 -0.0161 343 ASP A C   
2561 O O   . ASP A 327 ? 0.5058 0.4175 0.4458 0.0532  -0.0182 -0.0149 343 ASP A O   
2562 C CB  . ASP A 327 ? 0.5210 0.4663 0.4655 0.0619  -0.0131 -0.0287 343 ASP A CB  
2563 C CG  . ASP A 327 ? 0.5709 0.5251 0.5049 0.0648  -0.0134 -0.0317 343 ASP A CG  
2564 O OD1 . ASP A 327 ? 0.5334 0.4895 0.4596 0.0662  -0.0124 -0.0240 343 ASP A OD1 
2565 O OD2 . ASP A 327 ? 0.6361 0.5953 0.5722 0.0656  -0.0156 -0.0416 343 ASP A OD2 
2566 N N   . LEU A 328 ? 0.4872 0.4126 0.4179 0.0603  -0.0146 -0.0159 344 LEU A N   
2567 C CA  . LEU A 328 ? 0.4949 0.4086 0.4218 0.0593  -0.0153 -0.0151 344 LEU A CA  
2568 C C   . LEU A 328 ? 0.5667 0.4874 0.4930 0.0616  -0.0167 -0.0189 344 LEU A C   
2569 O O   . LEU A 328 ? 0.5358 0.4680 0.4611 0.0652  -0.0161 -0.0172 344 LEU A O   
2570 C CB  . LEU A 328 ? 0.5019 0.4099 0.4273 0.0608  -0.0116 -0.0080 344 LEU A CB  
2571 C CG  . LEU A 328 ? 0.5830 0.4758 0.5053 0.0597  -0.0100 -0.0088 344 LEU A CG  
2572 C CD1 . LEU A 328 ? 0.5905 0.4751 0.5163 0.0609  -0.0062 -0.0026 344 LEU A CD1 
2573 C CD2 . LEU A 328 ? 0.5881 0.4846 0.5098 0.0629  -0.0087 -0.0107 344 LEU A CD2 
2574 N N   . GLN A 329 ? 0.5378 0.4528 0.4657 0.0589  -0.0191 -0.0228 345 GLN A N   
2575 C CA  . GLN A 329 ? 0.5362 0.4580 0.4680 0.0598  -0.0210 -0.0263 345 GLN A CA  
2576 C C   . GLN A 329 ? 0.5834 0.4976 0.5140 0.0587  -0.0187 -0.0241 345 GLN A C   
2577 O O   . GLN A 329 ? 0.5686 0.4711 0.4936 0.0553  -0.0175 -0.0230 345 GLN A O   
2578 C CB  . GLN A 329 ? 0.5650 0.4890 0.5048 0.0576  -0.0252 -0.0327 345 GLN A CB  
2579 C CG  . GLN A 329 ? 0.5861 0.5191 0.5279 0.0595  -0.0253 -0.0374 345 GLN A CG  
2580 C CD  . GLN A 329 ? 0.6703 0.6039 0.6239 0.0583  -0.0284 -0.0454 345 GLN A CD  
2581 O OE1 . GLN A 329 ? 0.6098 0.5367 0.5717 0.0554  -0.0317 -0.0456 345 GLN A OE1 
2582 N NE2 . GLN A 329 ? 0.6721 0.6140 0.6278 0.0606  -0.0265 -0.0517 345 GLN A NE2 
2583 N N   . LEU A 330 ? 0.5595 0.4817 0.4953 0.0612  -0.0181 -0.0236 346 LEU A N   
2584 C CA  . LEU A 330 ? 0.5803 0.4987 0.5184 0.0606  -0.0143 -0.0217 346 LEU A CA  
2585 C C   . LEU A 330 ? 0.5797 0.5042 0.5281 0.0578  -0.0179 -0.0240 346 LEU A C   
2586 O O   . LEU A 330 ? 0.5679 0.5025 0.5238 0.0582  -0.0234 -0.0279 346 LEU A O   
2587 C CB  . LEU A 330 ? 0.5188 0.4424 0.4616 0.0658  -0.0100 -0.0175 346 LEU A CB  
2588 C CG  . LEU A 330 ? 0.6307 0.5482 0.5691 0.0693  -0.0060 -0.0136 346 LEU A CG  
2589 C CD1 . LEU A 330 ? 0.6204 0.5439 0.5698 0.0752  -0.0022 -0.0079 346 LEU A CD1 
2590 C CD2 . LEU A 330 ? 0.5730 0.4732 0.5011 0.0661  -0.0017 -0.0158 346 LEU A CD2 
2591 N N   A PHE A 331 ? 0.5684 0.4868 0.5168 0.0546  -0.0145 -0.0218 347 PHE A N   
2592 N N   B PHE A 331 ? 0.5671 0.4856 0.5157 0.0545  -0.0147 -0.0218 347 PHE A N   
2593 C CA  A PHE A 331 ? 0.5463 0.4693 0.5074 0.0512  -0.0167 -0.0212 347 PHE A CA  
2594 C CA  B PHE A 331 ? 0.5408 0.4660 0.5035 0.0520  -0.0169 -0.0215 347 PHE A CA  
2595 C C   A PHE A 331 ? 0.5638 0.4858 0.5249 0.0507  -0.0082 -0.0161 347 PHE A C   
2596 C C   B PHE A 331 ? 0.5636 0.4860 0.5257 0.0504  -0.0089 -0.0163 347 PHE A C   
2597 O O   A PHE A 331 ? 0.5721 0.4841 0.5186 0.0491  -0.0025 -0.0144 347 PHE A O   
2598 O O   B PHE A 331 ? 0.5731 0.4852 0.5211 0.0478  -0.0046 -0.0143 347 PHE A O   
2599 C CB  A PHE A 331 ? 0.5420 0.4583 0.5042 0.0460  -0.0217 -0.0214 347 PHE A CB  
2600 C CB  B PHE A 331 ? 0.5599 0.4826 0.5291 0.0476  -0.0238 -0.0242 347 PHE A CB  
2601 C CG  A PHE A 331 ? 0.5432 0.4594 0.5062 0.0470  -0.0276 -0.0270 347 PHE A CG  
2602 C CG  B PHE A 331 ? 0.5269 0.4380 0.4866 0.0438  -0.0237 -0.0207 347 PHE A CG  
2603 C CD1 A PHE A 331 ? 0.5441 0.4676 0.5207 0.0474  -0.0330 -0.0337 347 PHE A CD1 
2604 C CD1 B PHE A 331 ? 0.5584 0.4636 0.5074 0.0446  -0.0249 -0.0221 347 PHE A CD1 
2605 C CD2 A PHE A 331 ? 0.5512 0.4605 0.5027 0.0473  -0.0272 -0.0264 347 PHE A CD2 
2606 C CD2 B PHE A 331 ? 0.5887 0.4962 0.5523 0.0387  -0.0237 -0.0147 347 PHE A CD2 
2607 C CE1 A PHE A 331 ? 0.5511 0.4753 0.5283 0.0489  -0.0360 -0.0403 347 PHE A CE1 
2608 C CE1 B PHE A 331 ? 0.5703 0.4664 0.5123 0.0403  -0.0273 -0.0183 347 PHE A CE1 
2609 C CE2 A PHE A 331 ? 0.5552 0.4663 0.5102 0.0485  -0.0307 -0.0309 347 PHE A CE2 
2610 C CE2 B PHE A 331 ? 0.6086 0.5071 0.5628 0.0345  -0.0259 -0.0098 347 PHE A CE2 
2611 C CZ  A PHE A 331 ? 0.5513 0.4701 0.5186 0.0497  -0.0342 -0.0380 347 PHE A CZ  
2612 C CZ  B PHE A 331 ? 0.5686 0.4616 0.5122 0.0353  -0.0284 -0.0121 347 PHE A CZ  
2613 N N   . SER A 332 ? 0.5236 0.4565 0.5010 0.0516  -0.0070 -0.0142 348 SER A N   
2614 C CA  . SER A 332 ? 0.5913 0.5256 0.5717 0.0522  0.0034  -0.0094 348 SER A CA  
2615 C C   . SER A 332 ? 0.5929 0.5345 0.5906 0.0473  0.0029  -0.0050 348 SER A C   
2616 O O   . SER A 332 ? 0.5209 0.4674 0.5327 0.0444  -0.0065 -0.0069 348 SER A O   
2617 C CB  . SER A 332 ? 0.4780 0.4204 0.4671 0.0591  0.0075  -0.0087 348 SER A CB  
2618 O OG  . SER A 332 ? 0.5268 0.4690 0.5185 0.0609  0.0201  -0.0054 348 SER A OG  
2619 N N   . MET A 333 ? 0.5455 0.4875 0.5426 0.0462  0.0141  0.0005  349 MET A N   
2620 C CA  . MET A 333 ? 0.5387 0.4899 0.5555 0.0419  0.0167  0.0074  349 MET A CA  
2621 C C   . MET A 333 ? 0.5565 0.5174 0.5844 0.0466  0.0290  0.0104  349 MET A C   
2622 O O   . MET A 333 ? 0.5502 0.5062 0.5634 0.0480  0.0424  0.0115  349 MET A O   
2623 C CB  . MET A 333 ? 0.5334 0.4771 0.5387 0.0349  0.0197  0.0140  349 MET A CB  
2624 C CG  . MET A 333 ? 0.6306 0.5671 0.6364 0.0303  0.0065  0.0132  349 MET A CG  
2625 S SD  . MET A 333 ? 0.7591 0.6879 0.7533 0.0222  0.0078  0.0245  349 MET A SD  
2626 C CE  . MET A 333 ? 0.5670 0.5067 0.5945 0.0166  0.0085  0.0350  349 MET A CE  
2627 N N   . GLU A 334 ? 0.4788 0.4538 0.5327 0.0490  0.0244  0.0110  350 GLU A N   
2628 C CA  . GLU A 334 ? 0.5267 0.5129 0.5973 0.0545  0.0353  0.0148  350 GLU A CA  
2629 C C   . GLU A 334 ? 0.5699 0.5590 0.6441 0.0512  0.0503  0.0218  350 GLU A C   
2630 O O   . GLU A 334 ? 0.5342 0.5261 0.6170 0.0437  0.0475  0.0275  350 GLU A O   
2631 C CB  . GLU A 334 ? 0.4847 0.4886 0.5865 0.0556  0.0251  0.0165  350 GLU A CB  
2632 C CG  . GLU A 334 ? 0.5076 0.5242 0.6309 0.0627  0.0354  0.0216  350 GLU A CG  
2633 C CD  . GLU A 334 ? 0.5381 0.5758 0.6977 0.0618  0.0257  0.0263  350 GLU A CD  
2634 O OE1 . GLU A 334 ? 0.5240 0.5664 0.6939 0.0543  0.0129  0.0251  350 GLU A OE1 
2635 O OE2 . GLU A 334 ? 0.5692 0.6187 0.7490 0.0686  0.0301  0.0309  350 GLU A OE2 
2636 N N   . GLY A 335 ? 0.5744 0.5623 0.6420 0.0568  0.0669  0.0215  351 GLY A N   
2637 C CA  . GLY A 335 ? 0.5079 0.4985 0.5722 0.0543  0.0844  0.0269  351 GLY A CA  
2638 C C   . GLY A 335 ? 0.6121 0.5867 0.6371 0.0500  0.0901  0.0242  351 GLY A C   
2639 O O   . GLY A 335 ? 0.6011 0.5777 0.6162 0.0479  0.1058  0.0280  351 GLY A O   
2640 N N   . PHE A 336 ? 0.5891 0.5493 0.5913 0.0484  0.0778  0.0183  352 PHE A N   
2641 C CA  . PHE A 336 ? 0.6077 0.5541 0.5740 0.0433  0.0803  0.0168  352 PHE A CA  
2642 C C   . PHE A 336 ? 0.6476 0.5786 0.5907 0.0471  0.0772  0.0056  352 PHE A C   
2643 O O   . PHE A 336 ? 0.6381 0.5611 0.5610 0.0494  0.0896  -0.0009 352 PHE A O   
2644 C CB  . PHE A 336 ? 0.6380 0.5825 0.6024 0.0344  0.0670  0.0243  352 PHE A CB  
2645 C CG  . PHE A 336 ? 0.6925 0.6245 0.6217 0.0286  0.0660  0.0249  352 PHE A CG  
2646 C CD1 . PHE A 336 ? 0.7658 0.6975 0.6715 0.0258  0.0807  0.0273  352 PHE A CD1 
2647 C CD2 . PHE A 336 ? 0.7479 0.6700 0.6680 0.0257  0.0502  0.0233  352 PHE A CD2 
2648 C CE1 . PHE A 336 ? 0.7703 0.6920 0.6413 0.0194  0.0777  0.0283  352 PHE A CE1 
2649 C CE2 . PHE A 336 ? 0.7351 0.6474 0.6252 0.0198  0.0473  0.0252  352 PHE A CE2 
2650 C CZ  . PHE A 336 ? 0.7657 0.6779 0.6304 0.0163  0.0600  0.0278  352 PHE A CZ  
2651 N N   . GLY A 337 ? 0.5781 0.5045 0.5238 0.0475  0.0615  0.0029  353 GLY A N   
2652 C CA  . GLY A 337 ? 0.5441 0.4568 0.4710 0.0502  0.0582  -0.0058 353 GLY A CA  
2653 C C   . GLY A 337 ? 0.5726 0.4845 0.5069 0.0507  0.0421  -0.0069 353 GLY A C   
2654 O O   . GLY A 337 ? 0.5585 0.4807 0.5130 0.0500  0.0338  -0.0033 353 GLY A O   
2655 N N   . THR A 338 ? 0.5461 0.4459 0.4638 0.0513  0.0382  -0.0127 354 THR A N   
2656 C CA  . THR A 338 ? 0.5465 0.4458 0.4694 0.0529  0.0262  -0.0143 354 THR A CA  
2657 C C   . THR A 338 ? 0.5899 0.4770 0.4931 0.0481  0.0195  -0.0168 354 THR A C   
2658 O O   . THR A 338 ? 0.5738 0.4499 0.4575 0.0458  0.0245  -0.0203 354 THR A O   
2659 C CB  . THR A 338 ? 0.5593 0.4595 0.4910 0.0608  0.0293  -0.0167 354 THR A CB  
2660 O OG1 . THR A 338 ? 0.5133 0.4262 0.4660 0.0653  0.0351  -0.0131 354 THR A OG1 
2661 C CG2 . THR A 338 ? 0.5120 0.4150 0.4482 0.0622  0.0179  -0.0167 354 THR A CG2 
2662 N N   . ASP A 339 ? 0.5511 0.4407 0.4605 0.0463  0.0082  -0.0158 355 ASP A N   
2663 C CA  . ASP A 339 ? 0.5734 0.4543 0.4715 0.0429  0.0008  -0.0174 355 ASP A CA  
2664 C C   . ASP A 339 ? 0.5877 0.4704 0.4928 0.0474  -0.0031 -0.0200 355 ASP A C   
2665 O O   . ASP A 339 ? 0.5488 0.4418 0.4674 0.0516  -0.0043 -0.0198 355 ASP A O   
2666 C CB  . ASP A 339 ? 0.6229 0.5055 0.5256 0.0375  -0.0082 -0.0132 355 ASP A CB  
2667 C CG  . ASP A 339 ? 0.6154 0.4968 0.5104 0.0318  -0.0056 -0.0071 355 ASP A CG  
2668 O OD1 . ASP A 339 ? 0.6878 0.5651 0.5665 0.0309  0.0031  -0.0079 355 ASP A OD1 
2669 O OD2 . ASP A 339 ? 0.7386 0.6234 0.6444 0.0282  -0.0116 -0.0013 355 ASP A OD2 
2670 N N   . ALA A 340 ? 0.5712 0.4448 0.4664 0.0457  -0.0055 -0.0218 356 ALA A N   
2671 C CA  . ALA A 340 ? 0.5833 0.4590 0.4846 0.0484  -0.0092 -0.0223 356 ALA A CA  
2672 C C   . ALA A 340 ? 0.6015 0.4732 0.5002 0.0433  -0.0167 -0.0218 356 ALA A C   
2673 O O   . ALA A 340 ? 0.5999 0.4628 0.4870 0.0378  -0.0187 -0.0217 356 ALA A O   
2674 C CB  . ALA A 340 ? 0.5668 0.4356 0.4652 0.0517  -0.0036 -0.0233 356 ALA A CB  
2675 N N   . VAL A 341 ? 0.5800 0.4593 0.4895 0.0449  -0.0210 -0.0215 357 VAL A N   
2676 C CA  . VAL A 341 ? 0.5574 0.4348 0.4702 0.0412  -0.0275 -0.0204 357 VAL A CA  
2677 C C   . VAL A 341 ? 0.5617 0.4426 0.4797 0.0439  -0.0263 -0.0201 357 VAL A C   
2678 O O   . VAL A 341 ? 0.5351 0.4263 0.4592 0.0487  -0.0238 -0.0209 357 VAL A O   
2679 C CB  . VAL A 341 ? 0.5898 0.4736 0.5151 0.0404  -0.0325 -0.0202 357 VAL A CB  
2680 C CG1 . VAL A 341 ? 0.5791 0.4611 0.5117 0.0368  -0.0392 -0.0176 357 VAL A CG1 
2681 C CG2 . VAL A 341 ? 0.5932 0.4749 0.5160 0.0376  -0.0330 -0.0179 357 VAL A CG2 
2682 N N   . ILE A 342 ? 0.5681 0.4414 0.4836 0.0400  -0.0284 -0.0186 358 ILE A N   
2683 C CA  . ILE A 342 ? 0.5418 0.4192 0.4662 0.0410  -0.0280 -0.0161 358 ILE A CA  
2684 C C   . ILE A 342 ? 0.5753 0.4586 0.5123 0.0388  -0.0334 -0.0151 358 ILE A C   
2685 O O   . ILE A 342 ? 0.5698 0.4474 0.5068 0.0334  -0.0404 -0.0138 358 ILE A O   
2686 C CB  . ILE A 342 ? 0.5621 0.4277 0.4820 0.0373  -0.0279 -0.0149 358 ILE A CB  
2687 C CG1 . ILE A 342 ? 0.5792 0.4383 0.4917 0.0408  -0.0212 -0.0162 358 ILE A CG1 
2688 C CG2 . ILE A 342 ? 0.6060 0.4771 0.5390 0.0372  -0.0274 -0.0102 358 ILE A CG2 
2689 C CD1 . ILE A 342 ? 0.6209 0.4636 0.5282 0.0364  -0.0212 -0.0184 358 ILE A CD1 
2690 N N   . TYR A 343 ? 0.5530 0.4486 0.5011 0.0431  -0.0303 -0.0157 359 TYR A N   
2691 C CA  . TYR A 343 ? 0.5225 0.4248 0.4872 0.0426  -0.0331 -0.0156 359 TYR A CA  
2692 C C   . TYR A 343 ? 0.5320 0.4398 0.5061 0.0424  -0.0299 -0.0114 359 TYR A C   
2693 O O   . TYR A 343 ? 0.5517 0.4663 0.5223 0.0460  -0.0228 -0.0103 359 TYR A O   
2694 C CB  . TYR A 343 ? 0.5095 0.4219 0.4815 0.0477  -0.0302 -0.0217 359 TYR A CB  
2695 C CG  . TYR A 343 ? 0.5397 0.4480 0.5089 0.0474  -0.0336 -0.0251 359 TYR A CG  
2696 C CD1 . TYR A 343 ? 0.4815 0.3852 0.4615 0.0442  -0.0404 -0.0232 359 TYR A CD1 
2697 C CD2 . TYR A 343 ? 0.5058 0.4162 0.4647 0.0500  -0.0306 -0.0284 359 TYR A CD2 
2698 C CE1 . TYR A 343 ? 0.5405 0.4409 0.5204 0.0434  -0.0429 -0.0242 359 TYR A CE1 
2699 C CE2 . TYR A 343 ? 0.5585 0.4663 0.5185 0.0491  -0.0333 -0.0304 359 TYR A CE2 
2700 C CZ  . TYR A 343 ? 0.5694 0.4719 0.5396 0.0457  -0.0389 -0.0282 359 TYR A CZ  
2701 O OH  . TYR A 343 ? 0.6212 0.5214 0.5944 0.0442  -0.0411 -0.0282 359 TYR A OH  
2702 N N   . LEU A 344 ? 0.5107 0.4165 0.4976 0.0376  -0.0357 -0.0075 360 LEU A N   
2703 C CA  . LEU A 344 ? 0.5069 0.4188 0.5080 0.0362  -0.0333 -0.0022 360 LEU A CA  
2704 C C   . LEU A 344 ? 0.5299 0.4515 0.5554 0.0367  -0.0352 -0.0011 360 LEU A C   
2705 O O   . LEU A 344 ? 0.4916 0.4105 0.5238 0.0354  -0.0425 -0.0020 360 LEU A O   
2706 C CB  . LEU A 344 ? 0.5139 0.4134 0.5114 0.0287  -0.0395 0.0021  360 LEU A CB  
2707 C CG  . LEU A 344 ? 0.5590 0.4456 0.5355 0.0281  -0.0378 -0.0001 360 LEU A CG  
2708 C CD1 . LEU A 344 ? 0.5502 0.4225 0.5239 0.0196  -0.0452 0.0005  360 LEU A CD1 
2709 C CD2 . LEU A 344 ? 0.5206 0.4132 0.4958 0.0336  -0.0278 0.0026  360 LEU A CD2 
2710 N N   . LYS A 345 ? 0.4782 0.4120 0.5194 0.0387  -0.0278 0.0020  361 LYS A N   
2711 C CA  . LYS A 345 ? 0.5168 0.4608 0.5863 0.0395  -0.0283 0.0036  361 LYS A CA  
2712 C C   . LYS A 345 ? 0.5361 0.4736 0.6187 0.0312  -0.0413 0.0111  361 LYS A C   
2713 O O   . LYS A 345 ? 0.5263 0.4581 0.6049 0.0252  -0.0445 0.0160  361 LYS A O   
2714 C CB  . LYS A 345 ? 0.5310 0.4915 0.6139 0.0436  -0.0152 0.0055  361 LYS A CB  
2715 C CG  . LYS A 345 ? 0.5176 0.4877 0.5872 0.0515  -0.0031 -0.0031 361 LYS A CG  
2716 C CD  . LYS A 345 ? 0.6001 0.5726 0.6806 0.0563  -0.0032 -0.0133 361 LYS A CD  
2717 C CE  . LYS A 345 ? 0.5289 0.5115 0.5967 0.0633  0.0083  -0.0246 361 LYS A CE  
2718 N NZ  . LYS A 345 ? 0.5555 0.5341 0.6306 0.0667  0.0053  -0.0362 361 LYS A NZ  
2719 N N   . ALA A 346 ? 0.5619 0.5001 0.6611 0.0304  -0.0499 0.0123  362 ALA A N   
2720 C CA  . ALA A 346 ? 0.5739 0.5084 0.6857 0.0219  -0.0647 0.0205  362 ALA A CA  
2721 C C   . ALA A 346 ? 0.6071 0.5540 0.7504 0.0199  -0.0635 0.0277  362 ALA A C   
2722 O O   . ALA A 346 ? 0.6492 0.5926 0.7986 0.0110  -0.0750 0.0342  362 ALA A O   
2723 C CB  . ALA A 346 ? 0.5619 0.4951 0.6845 0.0219  -0.0749 0.0226  362 ALA A CB  
2724 N N   . LEU A 347 ? 0.5595 0.5215 0.7231 0.0276  -0.0496 0.0262  363 LEU A N   
2725 C CA  . LEU A 347 ? 0.6053 0.5826 0.8039 0.0268  -0.0457 0.0337  363 LEU A CA  
2726 C C   . LEU A 347 ? 0.6321 0.6153 0.8243 0.0270  -0.0324 0.0357  363 LEU A C   
2727 O O   . LEU A 347 ? 0.6226 0.6086 0.7954 0.0336  -0.0190 0.0296  363 LEU A O   
2728 C CB  . LEU A 347 ? 0.6048 0.5968 0.8341 0.0357  -0.0370 0.0308  363 LEU A CB  
2729 C CG  . LEU A 347 ? 0.6567 0.6438 0.8983 0.0373  -0.0480 0.0299  363 LEU A CG  
2730 C CD1 . LEU A 347 ? 0.6201 0.6222 0.9024 0.0460  -0.0389 0.0280  363 LEU A CD1 
2731 C CD2 . LEU A 347 ? 0.7008 0.6803 0.9472 0.0269  -0.0698 0.0409  363 LEU A CD2 
2732 N N   . SER A 348 ? 0.5752 0.5611 0.7855 0.0194  -0.0369 0.0453  364 SER A N   
2733 C CA  . SER A 348 ? 0.6334 0.6245 0.8422 0.0184  -0.0252 0.0505  364 SER A CA  
2734 C C   . SER A 348 ? 0.6147 0.6272 0.8374 0.0273  -0.0048 0.0507  364 SER A C   
2735 O O   . SER A 348 ? 0.6305 0.6485 0.8423 0.0287  0.0077  0.0544  364 SER A O   
2736 C CB  . SER A 348 ? 0.6501 0.6406 0.8827 0.0076  -0.0350 0.0611  364 SER A CB  
2737 O OG  . SER A 348 ? 0.7699 0.7755 1.0429 0.0068  -0.0387 0.0670  364 SER A OG  
2738 N N   . THR A 349 ? 0.5971 0.6222 0.8440 0.0334  -0.0006 0.0473  365 THR A N   
2739 C CA  . THR A 349 ? 0.6468 0.6920 0.9033 0.0424  0.0206  0.0441  365 THR A CA  
2740 C C   . THR A 349 ? 0.6396 0.6820 0.8605 0.0502  0.0299  0.0309  365 THR A C   
2741 O O   . THR A 349 ? 0.6196 0.6765 0.8328 0.0558  0.0477  0.0285  365 THR A O   
2742 C CB  . THR A 349 ? 0.6128 0.6720 0.9117 0.0469  0.0232  0.0436  365 THR A CB  
2743 O OG1 . THR A 349 ? 0.6649 0.7114 0.9657 0.0473  0.0079  0.0381  365 THR A OG1 
2744 C CG2 . THR A 349 ? 0.6535 0.7232 0.9924 0.0398  0.0188  0.0584  365 THR A CG2 
2745 N N   . ASP A 350 ? 0.5890 0.6141 0.7878 0.0502  0.0181  0.0230  366 ASP A N   
2746 C CA  . ASP A 350 ? 0.5938 0.6153 0.7596 0.0560  0.0241  0.0111  366 ASP A CA  
2747 C C   . ASP A 350 ? 0.5612 0.5749 0.6935 0.0529  0.0238  0.0150  366 ASP A C   
2748 O O   . ASP A 350 ? 0.5707 0.5852 0.6767 0.0575  0.0295  0.0073  366 ASP A O   
2749 C CB  . ASP A 350 ? 0.5546 0.5620 0.7149 0.0571  0.0123  0.0022  366 ASP A CB  
2750 C CG  . ASP A 350 ? 0.6266 0.6407 0.8192 0.0625  0.0140  -0.0036 366 ASP A CG  
2751 O OD1 . ASP A 350 ? 0.6287 0.6596 0.8450 0.0671  0.0272  -0.0043 366 ASP A OD1 
2752 O OD2 . ASP A 350 ? 0.6445 0.6472 0.8405 0.0622  0.0026  -0.0067 366 ASP A OD2 
2753 N N   . SER A 351 ? 0.5270 0.5327 0.6616 0.0451  0.0163  0.0263  367 SER A N   
2754 C CA  . SER A 351 ? 0.6104 0.6063 0.7187 0.0425  0.0154  0.0306  367 SER A CA  
2755 C C   . SER A 351 ? 0.5889 0.6008 0.6981 0.0442  0.0303  0.0396  367 SER A C   
2756 O O   . SER A 351 ? 0.6521 0.6669 0.7796 0.0388  0.0315  0.0518  367 SER A O   
2757 C CB  . SER A 351 ? 0.5704 0.5487 0.6816 0.0333  0.0013  0.0366  367 SER A CB  
2758 O OG  . SER A 351 ? 0.6928 0.6572 0.7964 0.0314  -0.0118 0.0292  367 SER A OG  
2759 N N   . VAL A 352 ? 0.5871 0.6099 0.6757 0.0510  0.0413  0.0343  368 VAL A N   
2760 C CA  . VAL A 352 ? 0.5020 0.5439 0.5875 0.0531  0.0568  0.0431  368 VAL A CA  
2761 C C   . VAL A 352 ? 0.5204 0.5593 0.5739 0.0545  0.0571  0.0463  368 VAL A C   
2762 O O   . VAL A 352 ? 0.5630 0.5935 0.5954 0.0574  0.0508  0.0358  368 VAL A O   
2763 C CB  . VAL A 352 ? 0.5882 0.6508 0.6785 0.0601  0.0711  0.0334  368 VAL A CB  
2764 C CG1 . VAL A 352 ? 0.6046 0.6892 0.6906 0.0616  0.0885  0.0437  368 VAL A CG1 
2765 C CG2 . VAL A 352 ? 0.5905 0.6546 0.7173 0.0599  0.0691  0.0297  368 VAL A CG2 
2766 N N   . GLU A 353 ? 0.5671 0.6137 0.6200 0.0524  0.0641  0.0625  369 GLU A N   
2767 C CA  . GLU A 353 ? 0.5153 0.5617 0.5420 0.0539  0.0645  0.0693  369 GLU A CA  
2768 C C   . GLU A 353 ? 0.5878 0.6469 0.5865 0.0606  0.0691  0.0572  369 GLU A C   
2769 O O   . GLU A 353 ? 0.5961 0.6736 0.5932 0.0641  0.0806  0.0505  369 GLU A O   
2770 C CB  . GLU A 353 ? 0.5422 0.6010 0.5760 0.0513  0.0744  0.0905  369 GLU A CB  
2771 C CG  . GLU A 353 ? 0.5440 0.5892 0.6056 0.0437  0.0691  0.1039  369 GLU A CG  
2772 C CD  . GLU A 353 ? 0.6006 0.6572 0.6677 0.0413  0.0786  0.1266  369 GLU A CD  
2773 O OE1 . GLU A 353 ? 0.6090 0.6874 0.6879 0.0411  0.0922  0.1348  369 GLU A OE1 
2774 O OE2 . GLU A 353 ? 0.5576 0.6026 0.6177 0.0402  0.0735  0.1370  369 GLU A OE2 
2775 N N   . ARG A 354 ? 0.5752 0.6245 0.5526 0.0621  0.0603  0.0537  370 ARG A N   
2776 C CA  . ARG A 354 ? 0.6460 0.7077 0.5958 0.0669  0.0623  0.0446  370 ARG A CA  
2777 C C   . ARG A 354 ? 0.6194 0.6927 0.5526 0.0669  0.0658  0.0625  370 ARG A C   
2778 O O   . ARG A 354 ? 0.6055 0.6668 0.5365 0.0659  0.0574  0.0721  370 ARG A O   
2779 C CB  . ARG A 354 ? 0.5945 0.6410 0.5344 0.0682  0.0499  0.0308  370 ARG A CB  
2780 C CG  . ARG A 354 ? 0.6745 0.7351 0.5869 0.0720  0.0505  0.0229  370 ARG A CG  
2781 C CD  . ARG A 354 ? 0.6707 0.7207 0.5768 0.0732  0.0403  0.0069  370 ARG A CD  
2782 N NE  . ARG A 354 ? 0.8178 0.8580 0.7419 0.0731  0.0392  -0.0069 370 ARG A NE  
2783 C CZ  . ARG A 354 ? 0.8637 0.8916 0.7900 0.0732  0.0305  -0.0193 370 ARG A CZ  
2784 N NH1 . ARG A 354 ? 0.7918 0.8168 0.7040 0.0736  0.0228  -0.0217 370 ARG A NH1 
2785 N NH2 . ARG A 354 ? 0.8898 0.9092 0.8355 0.0728  0.0293  -0.0278 370 ARG A NH2 
2786 N N   . LEU A 355 ? 0.5465 0.6436 0.4687 0.0683  0.0785  0.0675  371 LEU A N   
2787 C CA  . LEU A 355 ? 0.6339 0.7456 0.5417 0.0677  0.0828  0.0886  371 LEU A CA  
2788 C C   . LEU A 355 ? 0.6973 0.8289 0.5696 0.0709  0.0845  0.0821  371 LEU A C   
2789 O O   . LEU A 355 ? 0.7096 0.8549 0.5704 0.0733  0.0928  0.0653  371 LEU A O   
2790 C CB  . LEU A 355 ? 0.5752 0.7018 0.4980 0.0651  0.0975  0.1053  371 LEU A CB  
2791 C CG  . LEU A 355 ? 0.6598 0.7700 0.6201 0.0606  0.0960  0.1112  371 LEU A CG  
2792 C CD1 . LEU A 355 ? 0.5908 0.7177 0.5689 0.0574  0.1104  0.1301  371 LEU A CD1 
2793 C CD2 . LEU A 355 ? 0.5859 0.6714 0.5548 0.0578  0.0821  0.1196  371 LEU A CD2 
2794 N N   . PRO A 356 ? 0.6919 0.8271 0.5474 0.0710  0.0772  0.0958  372 PRO A N   
2795 C CA  . PRO A 356 ? 0.6336 0.7926 0.4536 0.0726  0.0786  0.0940  372 PRO A CA  
2796 C C   . PRO A 356 ? 0.7080 0.8932 0.5163 0.0716  0.0951  0.1074  372 PRO A C   
2797 O O   . PRO A 356 ? 0.7030 0.8883 0.5317 0.0691  0.1028  0.1277  372 PRO A O   
2798 C CB  . PRO A 356 ? 0.6978 0.8527 0.5115 0.0725  0.0652  0.1109  372 PRO A CB  
2799 C CG  . PRO A 356 ? 0.6877 0.8241 0.5338 0.0704  0.0647  0.1312  372 PRO A CG  
2800 C CD  . PRO A 356 ? 0.6553 0.7736 0.5252 0.0694  0.0674  0.1142  372 PRO A CD  
2801 N N   . VAL A 357 ? 0.7253 0.9335 0.5001 0.0730  0.1008  0.0958  373 VAL A N   
2802 C CA  . VAL A 357 ? 0.7956 1.0328 0.5507 0.0720  0.1172  0.1085  373 VAL A CA  
2803 C C   . VAL A 357 ? 0.8481 1.1068 0.5594 0.0716  0.1113  0.1109  373 VAL A C   
2804 O O   . VAL A 357 ? 0.9485 1.2035 0.6428 0.0728  0.0994  0.0901  373 VAL A O   
2805 C CB  . VAL A 357 ? 0.8248 1.0723 0.5831 0.0741  0.1358  0.0881  373 VAL A CB  
2806 C CG1 . VAL A 357 ? 0.9283 1.1758 0.6667 0.0772  0.1328  0.0536  373 VAL A CG1 
2807 C CG2 . VAL A 357 ? 0.8225 1.1014 0.5627 0.0729  0.1559  0.1042  373 VAL A CG2 
2808 N N   . TYR A 358 ? 0.8608 1.1424 0.5548 0.0693  0.1185  0.1377  374 TYR A N   
2809 C CA  . TYR A 358 ? 1.0037 1.3104 0.6528 0.0679  0.1132  0.1437  374 TYR A CA  
2810 C C   . TYR A 358 ? 1.0601 1.3939 0.6740 0.0681  0.1307  0.1255  374 TYR A C   
2811 O O   . TYR A 358 ? 1.1178 1.4657 0.7361 0.0678  0.1512  0.1348  374 TYR A O   
2812 C CB  . TYR A 358 ? 0.9362 1.2546 0.5842 0.0650  0.1106  0.1853  374 TYR A CB  
2813 C CG  . TYR A 358 ? 1.0098 1.3611 0.6083 0.0627  0.1084  0.1959  374 TYR A CG  
2814 C CD1 . TYR A 358 ? 1.0212 1.3750 0.5989 0.0623  0.0871  0.1940  374 TYR A CD1 
2815 C CD2 . TYR A 358 ? 1.0369 1.4186 0.6091 0.0605  0.1275  0.2079  374 TYR A CD2 
2816 C CE1 . TYR A 358 ? 1.1028 1.4819 0.6401 0.0582  0.0815  0.2008  374 TYR A CE1 
2817 C CE2 . TYR A 358 ? 1.0920 1.4912 0.6279 0.0554  0.1213  0.2107  374 TYR A CE2 
2818 C CZ  . TYR A 358 ? 1.1378 1.5353 0.6563 0.0542  0.0978  0.2072  374 TYR A CZ  
2819 O OH  . TYR A 358 ? 1.2257 1.6407 0.7087 0.0488  0.0908  0.2107  374 TYR A OH  
2820 N N   . ASN A 359 ? 1.2633 1.6046 0.8435 0.0685  0.1230  0.0994  375 ASN A N   
2821 C CA  . ASN A 359 ? 1.3003 1.6684 0.8389 0.0683  0.1375  0.0794  375 ASN A CA  
2822 C C   . ASN A 359 ? 1.4654 1.8419 0.9643 0.0661  0.1192  0.0630  375 ASN A C   
2823 O O   . ASN A 359 ? 1.4753 1.8446 0.9771 0.0644  0.0976  0.0773  375 ASN A O   
2824 C CB  . ASN A 359 ? 1.3309 1.6900 0.8889 0.0725  0.1549  0.0477  375 ASN A CB  
2825 C CG  . ASN A 359 ? 1.3306 1.6562 0.9230 0.0752  0.1415  0.0249  375 ASN A CG  
2826 O OD1 . ASN A 359 ? 1.3399 1.6516 0.9334 0.0739  0.1199  0.0252  375 ASN A OD1 
2827 N ND2 . ASN A 359 ? 1.2790 1.5932 0.9013 0.0790  0.1546  0.0065  375 ASN A ND2 
2828 N N   . LYS A 360 ? 1.5423 1.9244 1.0154 0.0643  0.1257  0.0315  376 LYS A N   
2829 C CA  . LYS A 360 ? 1.5412 1.9220 0.9864 0.0601  0.1064  0.0113  376 LYS A CA  
2830 C C   . LYS A 360 ? 1.5545 1.9158 1.0172 0.0635  0.0933  -0.0165 376 LYS A C   
2831 O O   . LYS A 360 ? 1.5911 1.9493 1.0408 0.0598  0.0723  -0.0258 376 LYS A O   
2832 C CB  . LYS A 360 ? 1.4916 1.8828 0.9021 0.0565  0.1180  -0.0123 376 LYS A CB  
2833 C CG  . LYS A 360 ? 1.6321 2.0439 1.0160 0.0516  0.1251  0.0152  376 LYS A CG  
2834 C CD  . LYS A 360 ? 1.6392 2.0564 1.0169 0.0473  0.1020  0.0475  376 LYS A CD  
2835 C CE  . LYS A 360 ? 1.7075 2.1451 1.0595 0.0423  0.1079  0.0758  376 LYS A CE  
2836 N NZ  . LYS A 360 ? 1.7150 2.1637 1.0227 0.0382  0.1157  0.0521  376 LYS A NZ  
2837 N N   . SER A 361 ? 1.4864 1.8314 0.9838 0.0695  0.1041  -0.0288 377 SER A N   
2838 C CA  . SER A 361 ? 1.5166 1.8325 1.0441 0.0709  0.0895  -0.0499 377 SER A CA  
2839 C C   . SER A 361 ? 1.5282 1.8301 1.0751 0.0693  0.0678  -0.0257 377 SER A C   
2840 O O   . SER A 361 ? 1.4985 1.7891 1.0492 0.0679  0.0495  -0.0390 377 SER A O   
2841 C CB  . SER A 361 ? 1.3893 1.6843 0.9590 0.0759  0.1040  -0.0626 377 SER A CB  
2842 O OG  . SER A 361 ? 1.3546 1.6232 0.9509 0.0770  0.0913  -0.0836 377 SER A OG  
2843 N N   . ALA A 362 ? 1.6241 1.9266 1.1858 0.0694  0.0701  0.0097  378 ALA A N   
2844 C CA  . ALA A 362 ? 1.5948 1.8874 1.1724 0.0684  0.0514  0.0345  378 ALA A CA  
2845 C C   . ALA A 362 ? 1.6599 1.9772 1.2015 0.0647  0.0373  0.0499  378 ALA A C   
2846 O O   . ALA A 362 ? 1.6484 1.9588 1.2005 0.0640  0.0181  0.0606  378 ALA A O   
2847 C CB  . ALA A 362 ? 1.4874 1.7700 1.0967 0.0698  0.0591  0.0653  378 ALA A CB  
2848 N N   . TRP A 363 ? 1.5964 1.9433 1.0959 0.0621  0.0465  0.0514  379 TRP A N   
2849 C CA  . TRP A 363 ? 1.6358 2.0026 1.1053 0.0567  0.0322  0.0687  379 TRP A CA  
2850 C C   . TRP A 363 ? 1.6291 1.9934 1.0871 0.0533  0.0100  0.0469  379 TRP A C   
2851 O O   . TRP A 363 ? 1.5928 1.9638 1.0470 0.0499  -0.0090 0.0658  379 TRP A O   
2852 C CB  . TRP A 363 ? 1.6738 2.0582 1.1121 0.0522  0.0474  0.0684  379 TRP A CB  
2853 C CG  . TRP A 363 ? 1.7099 2.1103 1.1193 0.0455  0.0334  0.0846  379 TRP A CG  
2854 C CD1 . TRP A 363 ? 1.7114 2.1239 1.1190 0.0432  0.0331  0.1225  379 TRP A CD1 
2855 C CD2 . TRP A 363 ? 1.7809 2.1866 1.1606 0.0401  0.0173  0.0639  379 TRP A CD2 
2856 N NE1 . TRP A 363 ? 1.8201 2.2462 1.1977 0.0372  0.0176  0.1272  379 TRP A NE1 
2857 C CE2 . TRP A 363 ? 1.8484 2.2709 1.2076 0.0350  0.0075  0.0915  379 TRP A CE2 
2858 C CE3 . TRP A 363 ? 1.7789 2.1761 1.1496 0.0387  0.0097  0.0250  379 TRP A CE3 
2859 C CZ2 . TRP A 363 ? 1.8574 2.2894 1.1851 0.0287  -0.0100 0.0816  379 TRP A CZ2 
2860 C CZ3 . TRP A 363 ? 1.7647 2.1702 1.1058 0.0319  -0.0075 0.0149  379 TRP A CZ3 
2861 C CH2 . TRP A 363 ? 1.8217 2.2449 1.1404 0.0271  -0.0173 0.0430  379 TRP A CH2 
2862 N N   . ARG A 364 ? 1.6350 1.9899 1.0901 0.0538  0.0120  0.0077  380 ARG A N   
2863 C CA  . ARG A 364 ? 1.6870 2.0397 1.1319 0.0492  -0.0081 -0.0149 380 ARG A CA  
2864 C C   . ARG A 364 ? 1.6090 1.9480 1.0840 0.0522  -0.0254 -0.0152 380 ARG A C   
2865 O O   . ARG A 364 ? 1.5753 1.9150 1.0474 0.0478  -0.0456 -0.0243 380 ARG A O   
2866 C CB  . ARG A 364 ? 1.7353 2.0821 1.1658 0.0475  0.0015  -0.0571 380 ARG A CB  
2867 C CG  . ARG A 364 ? 1.7385 2.0900 1.1427 0.0395  -0.0157 -0.0758 380 ARG A CG  
2868 C CD  . ARG A 364 ? 1.7914 2.1369 1.1789 0.0377  -0.0036 -0.1151 380 ARG A CD  
2869 N NE  . ARG A 364 ? 1.8097 2.1698 1.1633 0.0358  0.0130  -0.1116 380 ARG A NE  
2870 C CZ  . ARG A 364 ? 1.8287 2.1862 1.1811 0.0397  0.0382  -0.1271 380 ARG A CZ  
2871 N NH1 . ARG A 364 ? 1.8036 2.1440 1.1879 0.0459  0.0494  -0.1471 380 ARG A NH1 
2872 N NH2 . ARG A 364 ? 1.7886 2.1613 1.1082 0.0376  0.0525  -0.1219 380 ARG A NH2 
2873 N N   . HIS A 365 ? 1.5680 1.8824 1.0853 0.0574  -0.0173 -0.0050 381 HIS A N   
2874 C CA  . HIS A 365 ? 1.4647 1.7564 1.0211 0.0589  -0.0316 -0.0003 381 HIS A CA  
2875 C C   . HIS A 365 ? 1.4876 1.7922 1.0432 0.0573  -0.0504 0.0290  381 HIS A C   
2876 O O   . HIS A 365 ? 1.4760 1.7752 1.0467 0.0560  -0.0680 0.0249  381 HIS A O   
2877 C CB  . HIS A 365 ? 1.3689 1.6348 0.9653 0.0639  -0.0189 0.0093  381 HIS A CB  
2878 C CG  . HIS A 365 ? 1.4111 1.6574 1.0237 0.0658  -0.0077 -0.0203 381 HIS A CG  
2879 N ND1 . HIS A 365 ? 1.4132 1.6660 1.0116 0.0667  0.0106  -0.0356 381 HIS A ND1 
2880 C CD2 . HIS A 365 ? 1.2964 1.5175 0.9403 0.0670  -0.0119 -0.0356 381 HIS A CD2 
2881 C CE1 . HIS A 365 ? 1.4211 1.6531 1.0438 0.0689  0.0161  -0.0588 381 HIS A CE1 
2882 N NE2 . HIS A 365 ? 1.3736 1.5861 1.0227 0.0687  0.0023  -0.0586 381 HIS A NE2 
2883 N N   . TYR A 366 ? 1.5058 1.8282 1.0473 0.0574  -0.0466 0.0603  382 TYR A N   
2884 C CA  . TYR A 366 ? 1.3706 1.7062 0.9147 0.0566  -0.0641 0.0920  382 TYR A CA  
2885 C C   . TYR A 366 ? 1.4986 1.8569 1.0109 0.0501  -0.0830 0.0833  382 TYR A C   
2886 O O   . TYR A 366 ? 1.4388 1.8014 0.9649 0.0489  -0.1027 0.0983  382 TYR A O   
2887 C CB  . TYR A 366 ? 1.2360 1.5830 0.7763 0.0580  -0.0541 0.1288  382 TYR A CB  
2888 C CG  . TYR A 366 ? 1.2494 1.5688 0.8311 0.0631  -0.0392 0.1392  382 TYR A CG  
2889 C CD1 . TYR A 366 ? 1.1822 1.4917 0.7654 0.0642  -0.0182 0.1243  382 TYR A CD1 
2890 C CD2 . TYR A 366 ? 1.1755 1.4783 0.7966 0.0667  -0.0467 0.1620  382 TYR A CD2 
2891 C CE1 . TYR A 366 ? 1.0371 1.3221 0.6582 0.0677  -0.0071 0.1330  382 TYR A CE1 
2892 C CE2 . TYR A 366 ? 0.9863 1.2630 0.6433 0.0704  -0.0344 0.1686  382 TYR A CE2 
2893 C CZ  . TYR A 366 ? 0.9753 1.2435 0.6312 0.0703  -0.0157 0.1543  382 TYR A CZ  
2894 O OH  . TYR A 366 ? 0.8708 1.1141 0.5622 0.0729  -0.0059 0.1609  382 TYR A OH  
2895 N N   . GLN A 367 ? 1.6103 1.9750 1.0898 0.0448  -0.0763 0.0569  383 GLN A N   
2896 C CA  . GLN A 367 ? 1.6299 2.0061 1.0838 0.0368  -0.0927 0.0442  383 GLN A CA  
2897 C C   . GLN A 367 ? 1.6414 2.0093 1.1111 0.0351  -0.1106 0.0201  383 GLN A C   
2898 O O   . GLN A 367 ? 1.5957 1.9692 1.0795 0.0332  -0.1315 0.0343  383 GLN A O   
2899 C CB  . GLN A 367 ? 1.6304 2.0128 1.0455 0.0323  -0.0785 0.0206  383 GLN A CB  
2900 C CG  . GLN A 367 ? 1.7811 2.1714 1.1673 0.0239  -0.0946 0.0000  383 GLN A CG  
2901 C CD  . GLN A 367 ? 1.8259 2.2331 1.2024 0.0193  -0.1154 0.0290  383 GLN A CD  
2902 O OE1 . GLN A 367 ? 1.7646 2.1783 1.1544 0.0224  -0.1156 0.0659  383 GLN A OE1 
2903 N NE2 . GLN A 367 ? 1.8417 2.2553 1.1971 0.0119  -0.1332 0.0124  383 GLN A NE2 
2904 N N   . GLY A 373 ? 1.2474 1.5044 1.0045 -0.0081 -0.2414 -0.1963 389 GLY A N   
2905 C CA  . GLY A 373 ? 1.1516 1.4132 0.9345 -0.0183 -0.2628 -0.2090 389 GLY A CA  
2906 C C   . GLY A 373 ? 1.1551 1.4002 0.9410 -0.0254 -0.2635 -0.2486 389 GLY A C   
2907 O O   . GLY A 373 ? 1.1147 1.3687 0.8920 -0.0365 -0.2808 -0.2666 389 GLY A O   
2908 N N   . ASP A 374 ? 1.1202 1.3371 0.9219 -0.0197 -0.2430 -0.2590 390 ASP A N   
2909 C CA  . ASP A 374 ? 1.0814 1.2789 0.8923 -0.0248 -0.2411 -0.2952 390 ASP A CA  
2910 C C   . ASP A 374 ? 0.9799 1.1554 0.8470 -0.0269 -0.2413 -0.2946 390 ASP A C   
2911 O O   . ASP A 374 ? 0.9156 1.0713 0.7992 -0.0304 -0.2386 -0.3213 390 ASP A O   
2912 C CB  . ASP A 374 ? 1.0889 1.2722 0.8751 -0.0172 -0.2178 -0.3103 390 ASP A CB  
2913 C CG  . ASP A 374 ? 1.0837 1.2535 0.8834 -0.0056 -0.1969 -0.2840 390 ASP A CG  
2914 O OD1 . ASP A 374 ? 1.1346 1.3122 0.9460 -0.0026 -0.1997 -0.2527 390 ASP A OD1 
2915 O OD2 . ASP A 374 ? 1.0435 1.1952 0.8435 0.0004  -0.1780 -0.2948 390 ASP A OD2 
2916 N N   . TRP A 375 ? 0.9244 1.1031 0.8225 -0.0248 -0.2440 -0.2645 391 TRP A N   
2917 C CA  . TRP A 375 ? 0.8042 0.9675 0.7547 -0.0282 -0.2459 -0.2610 391 TRP A CA  
2918 C C   . TRP A 375 ? 0.8752 1.0593 0.8486 -0.0368 -0.2687 -0.2507 391 TRP A C   
2919 O O   . TRP A 375 ? 0.9306 1.1407 0.8824 -0.0378 -0.2813 -0.2387 391 TRP A O   
2920 C CB  . TRP A 375 ? 0.8301 0.9774 0.8012 -0.0181 -0.2261 -0.2358 391 TRP A CB  
2921 C CG  . TRP A 375 ? 0.9084 1.0361 0.8622 -0.0106 -0.2058 -0.2455 391 TRP A CG  
2922 C CD1 . TRP A 375 ? 0.9601 1.0927 0.8767 -0.0027 -0.1937 -0.2398 391 TRP A CD1 
2923 C CD2 . TRP A 375 ? 0.8676 0.9690 0.8439 -0.0105 -0.1957 -0.2617 391 TRP A CD2 
2924 N NE1 . TRP A 375 ? 0.8732 0.9850 0.7886 0.0024  -0.1765 -0.2518 391 TRP A NE1 
2925 C CE2 . TRP A 375 ? 0.8952 0.9875 0.8471 -0.0019 -0.1777 -0.2651 391 TRP A CE2 
2926 C CE3 . TRP A 375 ? 0.7645 0.8495 0.7823 -0.0169 -0.2001 -0.2718 391 TRP A CE3 
2927 C CZ2 . TRP A 375 ? 0.8594 0.9276 0.8277 0.0010  -0.1649 -0.2781 391 TRP A CZ2 
2928 C CZ3 . TRP A 375 ? 0.7509 0.8105 0.7840 -0.0141 -0.1873 -0.2843 391 TRP A CZ3 
2929 C CH2 . TRP A 375 ? 0.7647 0.8166 0.7733 -0.0050 -0.1702 -0.2873 391 TRP A CH2 
2930 N N   . CYS A 376 ? 0.8138 0.9874 0.8334 -0.0437 -0.2748 -0.2552 392 CYS A N   
2931 C CA  . CYS A 376 ? 0.8395 1.0326 0.8871 -0.0537 -0.2976 -0.2497 392 CYS A CA  
2932 C C   . CYS A 376 ? 0.9283 1.1327 1.0035 -0.0479 -0.2943 -0.2128 392 CYS A C   
2933 O O   . CYS A 376 ? 0.8024 0.9921 0.8878 -0.0384 -0.2738 -0.1955 392 CYS A O   
2934 C CB  . CYS A 376 ? 0.6724 0.8504 0.7625 -0.0645 -0.3055 -0.2692 392 CYS A CB  
2935 S SG  . CYS A 376 ? 0.8067 0.9749 0.8774 -0.0755 -0.3169 -0.3157 392 CYS A SG  
2936 N N   . VAL A 377 ? 1.0769 1.3081 1.1649 -0.0539 -0.3149 -0.2018 393 VAL A N   
2937 C CA  . VAL A 377 ? 1.0487 1.2926 1.1728 -0.0496 -0.3138 -0.1692 393 VAL A CA  
2938 C C   . VAL A 377 ? 0.9875 1.2441 1.1581 -0.0621 -0.3342 -0.1718 393 VAL A C   
2939 O O   . VAL A 377 ? 0.9662 1.2319 1.1288 -0.0739 -0.3557 -0.1944 393 VAL A O   
2940 C CB  . VAL A 377 ? 1.0396 1.3069 1.1377 -0.0420 -0.3173 -0.1462 393 VAL A CB  
2941 C CG1 . VAL A 377 ? 1.0429 1.2947 1.1064 -0.0294 -0.2937 -0.1393 393 VAL A CG1 
2942 C CG2 . VAL A 377 ? 1.0356 1.3276 1.1014 -0.0508 -0.3425 -0.1588 393 VAL A CG2 
2943 N N   . PRO A 378 ? 0.9603 1.2176 1.1809 -0.0607 -0.3279 -0.1505 394 PRO A N   
2944 C CA  . PRO A 378 ? 0.9452 1.2147 1.2171 -0.0728 -0.3453 -0.1508 394 PRO A CA  
2945 C C   . PRO A 378 ? 0.9461 1.2497 1.2194 -0.0814 -0.3755 -0.1491 394 PRO A C   
2946 O O   . PRO A 378 ? 0.9730 1.2974 1.2277 -0.0747 -0.3800 -0.1304 394 PRO A O   
2947 C CB  . PRO A 378 ? 0.9180 1.1865 1.2336 -0.0655 -0.3275 -0.1218 394 PRO A CB  
2948 C CG  . PRO A 378 ? 0.8932 1.1349 1.1830 -0.0535 -0.2995 -0.1190 394 PRO A CG  
2949 C CD  . PRO A 378 ? 0.9574 1.2000 1.1888 -0.0482 -0.3011 -0.1287 394 PRO A CD  
# 
