data_9M3O
# 
_entry.id   9M3O 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9M3O         pdb_00009m3o 10.2210/pdb9m3o/pdb 
WWPDB D_1300057118 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9M3O 
_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 1, mitochondrial'            43788.898 1   
2.7.11.2 ? ? ? 
2 non-polymer syn 'POTASSIUM ION'                                                                             39.098    1   ? ? ? 
? 
3 non-polymer syn '6-fluoranyl-8-(methylamino)-N-(pyrimidin-5-ylmethyl)-9H-pyrido[2,3-b]indole-3-carboxamide' 350.350   1   ? ? ? 
? 
4 non-polymer syn GLYCEROL                                                                                    92.094    3   ? ? ? 
? 
5 water       nat water                                                                                       18.015    243 ? ? ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Pyruvate dehydrogenase kinase isoform 1,PDH kinase 1' 
# 
_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       
;GVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQE
LLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSL
LFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFEL
FKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLP
ISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDWCVP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQE
LLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSL
LFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFEL
FKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLP
ISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDWCVP
;
_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 'POTASSIUM ION'                                                                             K     
3 '6-fluoranyl-8-(methylamino)-N-(pyrimidin-5-ylmethyl)-9H-pyrido[2,3-b]indole-3-carboxamide' A1EMR 
4 GLYCEROL                                                                                    GOL   
5 water                                                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   VAL n 
1 3   PRO n 
1 4   GLY n 
1 5   GLN n 
1 6   VAL n 
1 7   ASP n 
1 8   PHE n 
1 9   TYR n 
1 10  ALA n 
1 11  ARG n 
1 12  PHE n 
1 13  SER n 
1 14  PRO n 
1 15  SER n 
1 16  PRO n 
1 17  LEU n 
1 18  SER n 
1 19  MET n 
1 20  LYS n 
1 21  GLN n 
1 22  PHE n 
1 23  LEU n 
1 24  ASP n 
1 25  PHE n 
1 26  GLY n 
1 27  SER n 
1 28  VAL n 
1 29  ASN n 
1 30  ALA n 
1 31  CYS n 
1 32  GLU n 
1 33  LYS n 
1 34  THR n 
1 35  SER n 
1 36  PHE n 
1 37  MET n 
1 38  PHE n 
1 39  LEU n 
1 40  ARG n 
1 41  GLN n 
1 42  GLU n 
1 43  LEU n 
1 44  PRO n 
1 45  VAL n 
1 46  ARG n 
1 47  LEU n 
1 48  ALA n 
1 49  ASN n 
1 50  ILE n 
1 51  MET n 
1 52  LYS n 
1 53  GLU n 
1 54  ILE n 
1 55  SER n 
1 56  LEU n 
1 57  LEU n 
1 58  PRO n 
1 59  ASP n 
1 60  ASN n 
1 61  LEU n 
1 62  LEU n 
1 63  ARG n 
1 64  THR n 
1 65  PRO n 
1 66  SER n 
1 67  VAL n 
1 68  GLN n 
1 69  LEU n 
1 70  VAL n 
1 71  GLN n 
1 72  SER n 
1 73  TRP n 
1 74  TYR n 
1 75  ILE n 
1 76  GLN n 
1 77  SER n 
1 78  LEU n 
1 79  GLN n 
1 80  GLU n 
1 81  LEU n 
1 82  LEU n 
1 83  ASP n 
1 84  PHE n 
1 85  LYS n 
1 86  ASP n 
1 87  LYS n 
1 88  SER n 
1 89  ALA n 
1 90  GLU n 
1 91  ASP n 
1 92  ALA n 
1 93  LYS n 
1 94  ALA n 
1 95  ILE n 
1 96  TYR n 
1 97  ASP n 
1 98  PHE n 
1 99  THR n 
1 100 ASP n 
1 101 THR n 
1 102 VAL n 
1 103 ILE n 
1 104 ARG n 
1 105 ILE n 
1 106 ARG n 
1 107 ASN n 
1 108 ARG n 
1 109 HIS n 
1 110 ASN n 
1 111 ASP n 
1 112 VAL n 
1 113 ILE n 
1 114 PRO n 
1 115 THR n 
1 116 MET n 
1 117 ALA n 
1 118 GLN n 
1 119 GLY n 
1 120 VAL n 
1 121 ILE n 
1 122 GLU n 
1 123 TYR n 
1 124 LYS n 
1 125 GLU n 
1 126 SER n 
1 127 PHE n 
1 128 GLY n 
1 129 VAL n 
1 130 ASP n 
1 131 PRO n 
1 132 VAL n 
1 133 THR n 
1 134 SER n 
1 135 GLN n 
1 136 ASN n 
1 137 VAL n 
1 138 GLN n 
1 139 TYR n 
1 140 PHE n 
1 141 LEU n 
1 142 ASP n 
1 143 ARG n 
1 144 PHE n 
1 145 TYR n 
1 146 MET n 
1 147 SER n 
1 148 ARG n 
1 149 ILE n 
1 150 SER n 
1 151 ILE n 
1 152 ARG n 
1 153 MET n 
1 154 LEU n 
1 155 LEU n 
1 156 ASN n 
1 157 GLN n 
1 158 HIS n 
1 159 SER n 
1 160 LEU n 
1 161 LEU n 
1 162 PHE n 
1 163 GLY n 
1 164 GLY n 
1 165 LYS n 
1 166 GLY n 
1 167 LYS n 
1 168 GLY n 
1 169 SER n 
1 170 PRO n 
1 171 SER n 
1 172 HIS n 
1 173 ARG n 
1 174 LYS n 
1 175 HIS n 
1 176 ILE n 
1 177 GLY n 
1 178 SER n 
1 179 ILE n 
1 180 ASN n 
1 181 PRO n 
1 182 ASN n 
1 183 CYS n 
1 184 ASN n 
1 185 VAL n 
1 186 LEU n 
1 187 GLU n 
1 188 VAL n 
1 189 ILE n 
1 190 LYS n 
1 191 ASP n 
1 192 GLY n 
1 193 TYR n 
1 194 GLU n 
1 195 ASN n 
1 196 ALA n 
1 197 ARG n 
1 198 ARG n 
1 199 LEU n 
1 200 CYS n 
1 201 ASP n 
1 202 LEU n 
1 203 TYR n 
1 204 TYR n 
1 205 ILE n 
1 206 ASN n 
1 207 SER n 
1 208 PRO n 
1 209 GLU n 
1 210 LEU n 
1 211 GLU n 
1 212 LEU n 
1 213 GLU n 
1 214 GLU n 
1 215 LEU n 
1 216 ASN n 
1 217 ALA n 
1 218 LYS n 
1 219 SER n 
1 220 PRO n 
1 221 GLY n 
1 222 GLN n 
1 223 PRO n 
1 224 ILE n 
1 225 GLN n 
1 226 VAL n 
1 227 VAL n 
1 228 TYR n 
1 229 VAL n 
1 230 PRO n 
1 231 SER n 
1 232 HIS n 
1 233 LEU n 
1 234 TYR n 
1 235 HIS n 
1 236 MET n 
1 237 VAL n 
1 238 PHE n 
1 239 GLU n 
1 240 LEU n 
1 241 PHE n 
1 242 LYS n 
1 243 ASN n 
1 244 ALA n 
1 245 MET n 
1 246 ARG n 
1 247 ALA n 
1 248 THR n 
1 249 MET n 
1 250 GLU n 
1 251 HIS n 
1 252 HIS n 
1 253 ALA n 
1 254 ASN n 
1 255 ARG n 
1 256 GLY n 
1 257 VAL n 
1 258 TYR n 
1 259 PRO n 
1 260 PRO n 
1 261 ILE n 
1 262 GLN n 
1 263 VAL n 
1 264 HIS n 
1 265 VAL n 
1 266 THR n 
1 267 LEU n 
1 268 GLY n 
1 269 ASN n 
1 270 GLU n 
1 271 ASP n 
1 272 LEU n 
1 273 THR n 
1 274 VAL n 
1 275 LYS n 
1 276 MET n 
1 277 SER n 
1 278 ASP n 
1 279 ARG n 
1 280 GLY n 
1 281 GLY n 
1 282 GLY n 
1 283 VAL n 
1 284 PRO n 
1 285 LEU n 
1 286 ARG n 
1 287 LYS n 
1 288 ILE n 
1 289 ASP n 
1 290 ARG n 
1 291 LEU n 
1 292 PHE n 
1 293 ASN n 
1 294 TYR n 
1 295 MET n 
1 296 TYR n 
1 297 SER n 
1 298 THR n 
1 299 ALA n 
1 300 PRO n 
1 301 ARG n 
1 302 PRO n 
1 303 ARG n 
1 304 VAL n 
1 305 GLU n 
1 306 THR n 
1 307 SER n 
1 308 ARG n 
1 309 ALA n 
1 310 VAL n 
1 311 PRO n 
1 312 LEU n 
1 313 ALA n 
1 314 GLY n 
1 315 PHE n 
1 316 GLY n 
1 317 TYR n 
1 318 GLY n 
1 319 LEU n 
1 320 PRO n 
1 321 ILE n 
1 322 SER n 
1 323 ARG n 
1 324 LEU n 
1 325 TYR n 
1 326 ALA n 
1 327 GLN n 
1 328 TYR n 
1 329 PHE n 
1 330 GLN n 
1 331 GLY n 
1 332 ASP n 
1 333 LEU n 
1 334 LYS n 
1 335 LEU n 
1 336 TYR n 
1 337 SER n 
1 338 LEU n 
1 339 GLU n 
1 340 GLY n 
1 341 TYR n 
1 342 GLY n 
1 343 THR n 
1 344 ASP n 
1 345 ALA n 
1 346 VAL n 
1 347 ILE n 
1 348 TYR n 
1 349 ILE n 
1 350 LYS n 
1 351 ALA n 
1 352 LEU n 
1 353 SER n 
1 354 THR n 
1 355 ASP n 
1 356 SER n 
1 357 ILE n 
1 358 GLU n 
1 359 ARG n 
1 360 LEU n 
1 361 PRO n 
1 362 VAL n 
1 363 TYR n 
1 364 ASN n 
1 365 LYS n 
1 366 ALA n 
1 367 ALA n 
1 368 TRP n 
1 369 LYS n 
1 370 HIS n 
1 371 TYR n 
1 372 ASN n 
1 373 THR n 
1 374 ASN n 
1 375 HIS n 
1 376 GLU n 
1 377 ALA n 
1 378 ASP n 
1 379 ASP n 
1 380 TRP n 
1 381 CYS n 
1 382 VAL n 
1 383 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                   383 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PDK1, PDHK1' 
_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 
A1EMR non-polymer         . '6-fluoranyl-8-(methylamino)-N-(pyrimidin-5-ylmethyl)-9H-pyrido[2,3-b]indole-3-carboxamide' ? 
'C18 H15 F N6 O' 350.350 
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 
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 
K     non-polymer         . 'POTASSIUM ION'                                                                             ? 'K 1' 
39.098  
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 
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   GLY 1   41  41  GLY GLY A . n 
A 1 2   VAL 2   42  42  VAL VAL A . n 
A 1 3   PRO 3   43  43  PRO PRO A . n 
A 1 4   GLY 4   44  44  GLY GLY A . n 
A 1 5   GLN 5   45  45  GLN GLN A . n 
A 1 6   VAL 6   46  46  VAL VAL A . n 
A 1 7   ASP 7   47  47  ASP ASP A . n 
A 1 8   PHE 8   48  48  PHE PHE A . n 
A 1 9   TYR 9   49  49  TYR TYR A . n 
A 1 10  ALA 10  50  50  ALA ALA A . n 
A 1 11  ARG 11  51  51  ARG ARG A . n 
A 1 12  PHE 12  52  52  PHE PHE A . n 
A 1 13  SER 13  53  53  SER SER A . n 
A 1 14  PRO 14  54  54  PRO PRO A . n 
A 1 15  SER 15  55  55  SER SER A . n 
A 1 16  PRO 16  56  56  PRO PRO A . n 
A 1 17  LEU 17  57  57  LEU LEU A . n 
A 1 18  SER 18  58  58  SER SER A . n 
A 1 19  MET 19  59  59  MET MET A . n 
A 1 20  LYS 20  60  60  LYS LYS A . n 
A 1 21  GLN 21  61  61  GLN GLN A . n 
A 1 22  PHE 22  62  62  PHE PHE A . n 
A 1 23  LEU 23  63  63  LEU LEU A . n 
A 1 24  ASP 24  64  64  ASP ASP A . n 
A 1 25  PHE 25  65  65  PHE PHE A . n 
A 1 26  GLY 26  66  66  GLY GLY A . n 
A 1 27  SER 27  67  67  SER SER A . n 
A 1 28  VAL 28  68  68  VAL VAL A . n 
A 1 29  ASN 29  69  69  ASN ASN A . n 
A 1 30  ALA 30  70  70  ALA ALA A . n 
A 1 31  CYS 31  71  71  CYS CYS A . n 
A 1 32  GLU 32  72  72  GLU GLU A . n 
A 1 33  LYS 33  73  73  LYS LYS A . n 
A 1 34  THR 34  74  74  THR THR A . n 
A 1 35  SER 35  75  75  SER SER A . n 
A 1 36  PHE 36  76  76  PHE PHE A . n 
A 1 37  MET 37  77  77  MET MET A . n 
A 1 38  PHE 38  78  78  PHE PHE A . n 
A 1 39  LEU 39  79  79  LEU LEU A . n 
A 1 40  ARG 40  80  80  ARG ARG A . n 
A 1 41  GLN 41  81  81  GLN GLN A . n 
A 1 42  GLU 42  82  82  GLU GLU A . n 
A 1 43  LEU 43  83  83  LEU LEU A . n 
A 1 44  PRO 44  84  84  PRO PRO A . n 
A 1 45  VAL 45  85  85  VAL VAL A . n 
A 1 46  ARG 46  86  86  ARG ARG A . n 
A 1 47  LEU 47  87  87  LEU LEU A . n 
A 1 48  ALA 48  88  88  ALA ALA A . n 
A 1 49  ASN 49  89  89  ASN ASN A . n 
A 1 50  ILE 50  90  90  ILE ILE A . n 
A 1 51  MET 51  91  91  MET MET A . n 
A 1 52  LYS 52  92  92  LYS LYS A . n 
A 1 53  GLU 53  93  93  GLU GLU A . n 
A 1 54  ILE 54  94  94  ILE ILE A . n 
A 1 55  SER 55  95  95  SER SER A . n 
A 1 56  LEU 56  96  96  LEU LEU A . n 
A 1 57  LEU 57  97  97  LEU LEU A . n 
A 1 58  PRO 58  98  98  PRO PRO A . n 
A 1 59  ASP 59  99  99  ASP ASP A . n 
A 1 60  ASN 60  100 100 ASN ASN A . n 
A 1 61  LEU 61  101 101 LEU LEU A . n 
A 1 62  LEU 62  102 102 LEU LEU A . n 
A 1 63  ARG 63  103 103 ARG ARG A . n 
A 1 64  THR 64  104 104 THR THR A . n 
A 1 65  PRO 65  105 105 PRO PRO A . n 
A 1 66  SER 66  106 106 SER SER A . n 
A 1 67  VAL 67  107 107 VAL VAL A . n 
A 1 68  GLN 68  108 108 GLN GLN A . n 
A 1 69  LEU 69  109 109 LEU LEU A . n 
A 1 70  VAL 70  110 110 VAL VAL A . n 
A 1 71  GLN 71  111 111 GLN GLN A . n 
A 1 72  SER 72  112 112 SER SER A . n 
A 1 73  TRP 73  113 113 TRP TRP A . n 
A 1 74  TYR 74  114 114 TYR TYR A . n 
A 1 75  ILE 75  115 115 ILE ILE A . n 
A 1 76  GLN 76  116 116 GLN GLN A . n 
A 1 77  SER 77  117 117 SER SER A . n 
A 1 78  LEU 78  118 118 LEU LEU A . n 
A 1 79  GLN 79  119 119 GLN GLN A . n 
A 1 80  GLU 80  120 120 GLU GLU A . n 
A 1 81  LEU 81  121 121 LEU LEU A . n 
A 1 82  LEU 82  122 122 LEU LEU A . n 
A 1 83  ASP 83  123 123 ASP ASP A . n 
A 1 84  PHE 84  124 124 PHE PHE A . n 
A 1 85  LYS 85  125 125 LYS LYS A . n 
A 1 86  ASP 86  126 126 ASP ASP A . n 
A 1 87  LYS 87  127 127 LYS LYS A . n 
A 1 88  SER 88  128 128 SER SER A . n 
A 1 89  ALA 89  129 129 ALA ALA A . n 
A 1 90  GLU 90  130 130 GLU GLU A . n 
A 1 91  ASP 91  131 131 ASP ASP A . n 
A 1 92  ALA 92  132 132 ALA ALA A . n 
A 1 93  LYS 93  133 133 LYS LYS A . n 
A 1 94  ALA 94  134 134 ALA ALA A . n 
A 1 95  ILE 95  135 135 ILE ILE A . n 
A 1 96  TYR 96  136 136 TYR TYR A . n 
A 1 97  ASP 97  137 137 ASP ASP A . n 
A 1 98  PHE 98  138 138 PHE PHE A . n 
A 1 99  THR 99  139 139 THR THR A . n 
A 1 100 ASP 100 140 140 ASP ASP A . n 
A 1 101 THR 101 141 141 THR THR A . n 
A 1 102 VAL 102 142 142 VAL VAL A . n 
A 1 103 ILE 103 143 143 ILE ILE A . n 
A 1 104 ARG 104 144 144 ARG ARG A . n 
A 1 105 ILE 105 145 145 ILE ILE A . n 
A 1 106 ARG 106 146 146 ARG ARG A . n 
A 1 107 ASN 107 147 147 ASN ASN A . n 
A 1 108 ARG 108 148 148 ARG ARG A . n 
A 1 109 HIS 109 149 149 HIS HIS A . n 
A 1 110 ASN 110 150 150 ASN ASN A . n 
A 1 111 ASP 111 151 151 ASP ASP A . n 
A 1 112 VAL 112 152 152 VAL VAL A . n 
A 1 113 ILE 113 153 153 ILE ILE A . n 
A 1 114 PRO 114 154 154 PRO PRO A . n 
A 1 115 THR 115 155 155 THR THR A . n 
A 1 116 MET 116 156 156 MET MET A . n 
A 1 117 ALA 117 157 157 ALA ALA A . n 
A 1 118 GLN 118 158 158 GLN GLN A . n 
A 1 119 GLY 119 159 159 GLY GLY A . n 
A 1 120 VAL 120 160 160 VAL VAL A . n 
A 1 121 ILE 121 161 161 ILE ILE A . n 
A 1 122 GLU 122 162 162 GLU GLU A . n 
A 1 123 TYR 123 163 163 TYR TYR A . n 
A 1 124 LYS 124 164 164 LYS LYS A . n 
A 1 125 GLU 125 165 165 GLU GLU A . n 
A 1 126 SER 126 166 166 SER SER A . n 
A 1 127 PHE 127 167 167 PHE PHE A . n 
A 1 128 GLY 128 168 168 GLY GLY A . n 
A 1 129 VAL 129 169 169 VAL VAL A . n 
A 1 130 ASP 130 170 170 ASP ASP A . n 
A 1 131 PRO 131 171 171 PRO PRO A . n 
A 1 132 VAL 132 172 172 VAL VAL A . n 
A 1 133 THR 133 173 173 THR THR A . n 
A 1 134 SER 134 174 174 SER SER A . n 
A 1 135 GLN 135 175 175 GLN GLN A . n 
A 1 136 ASN 136 176 176 ASN ASN A . n 
A 1 137 VAL 137 177 177 VAL VAL A . n 
A 1 138 GLN 138 178 178 GLN GLN A . n 
A 1 139 TYR 139 179 179 TYR TYR A . n 
A 1 140 PHE 140 180 180 PHE PHE A . n 
A 1 141 LEU 141 181 181 LEU LEU A . n 
A 1 142 ASP 142 182 182 ASP ASP A . n 
A 1 143 ARG 143 183 183 ARG ARG A . n 
A 1 144 PHE 144 184 184 PHE PHE A . n 
A 1 145 TYR 145 185 185 TYR TYR A . n 
A 1 146 MET 146 186 186 MET MET A . n 
A 1 147 SER 147 187 187 SER SER A . n 
A 1 148 ARG 148 188 188 ARG ARG A . n 
A 1 149 ILE 149 189 189 ILE ILE A . n 
A 1 150 SER 150 190 190 SER SER A . n 
A 1 151 ILE 151 191 191 ILE ILE A . n 
A 1 152 ARG 152 192 192 ARG ARG A . n 
A 1 153 MET 153 193 193 MET MET A . n 
A 1 154 LEU 154 194 194 LEU LEU A . n 
A 1 155 LEU 155 195 195 LEU LEU A . n 
A 1 156 ASN 156 196 196 ASN ASN A . n 
A 1 157 GLN 157 197 197 GLN GLN A . n 
A 1 158 HIS 158 198 198 HIS HIS A . n 
A 1 159 SER 159 199 199 SER SER A . n 
A 1 160 LEU 160 200 200 LEU LEU A . n 
A 1 161 LEU 161 201 201 LEU LEU A . n 
A 1 162 PHE 162 202 202 PHE PHE A . n 
A 1 163 GLY 163 203 203 GLY GLY A . n 
A 1 164 GLY 164 204 ?   ?   ?   A . n 
A 1 165 LYS 165 205 ?   ?   ?   A . n 
A 1 166 GLY 166 206 ?   ?   ?   A . n 
A 1 167 LYS 167 207 ?   ?   ?   A . n 
A 1 168 GLY 168 208 ?   ?   ?   A . n 
A 1 169 SER 169 209 ?   ?   ?   A . n 
A 1 170 PRO 170 210 ?   ?   ?   A . n 
A 1 171 SER 171 211 ?   ?   ?   A . n 
A 1 172 HIS 172 212 ?   ?   ?   A . n 
A 1 173 ARG 173 213 ?   ?   ?   A . n 
A 1 174 LYS 174 214 ?   ?   ?   A . n 
A 1 175 HIS 175 215 215 HIS HIS A . n 
A 1 176 ILE 176 216 216 ILE ILE A . n 
A 1 177 GLY 177 217 217 GLY GLY A . n 
A 1 178 SER 178 218 218 SER SER A . n 
A 1 179 ILE 179 219 219 ILE ILE A . n 
A 1 180 ASN 180 220 220 ASN ASN A . n 
A 1 181 PRO 181 221 221 PRO PRO A . n 
A 1 182 ASN 182 222 222 ASN ASN A . n 
A 1 183 CYS 183 223 223 CYS CYS A . n 
A 1 184 ASN 184 224 224 ASN ASN A . n 
A 1 185 VAL 185 225 225 VAL VAL A . n 
A 1 186 LEU 186 226 226 LEU LEU A . n 
A 1 187 GLU 187 227 227 GLU GLU A . n 
A 1 188 VAL 188 228 228 VAL VAL A . n 
A 1 189 ILE 189 229 229 ILE ILE A . n 
A 1 190 LYS 190 230 230 LYS LYS A . n 
A 1 191 ASP 191 231 231 ASP ASP A . n 
A 1 192 GLY 192 232 232 GLY GLY A . n 
A 1 193 TYR 193 233 233 TYR TYR A . n 
A 1 194 GLU 194 234 234 GLU GLU A . n 
A 1 195 ASN 195 235 235 ASN ASN A . n 
A 1 196 ALA 196 236 236 ALA ALA A . n 
A 1 197 ARG 197 237 237 ARG ARG A . n 
A 1 198 ARG 198 238 238 ARG ARG A . n 
A 1 199 LEU 199 239 239 LEU LEU A . n 
A 1 200 CYS 200 240 240 CYS CYS A . n 
A 1 201 ASP 201 241 241 ASP ASP A . n 
A 1 202 LEU 202 242 242 LEU LEU A . n 
A 1 203 TYR 203 243 243 TYR TYR A . n 
A 1 204 TYR 204 244 244 TYR TYR A . n 
A 1 205 ILE 205 245 245 ILE ILE A . n 
A 1 206 ASN 206 246 246 ASN ASN A . n 
A 1 207 SER 207 247 247 SER SER A . n 
A 1 208 PRO 208 248 248 PRO PRO A . n 
A 1 209 GLU 209 249 249 GLU GLU A . n 
A 1 210 LEU 210 250 250 LEU LEU A . n 
A 1 211 GLU 211 251 251 GLU GLU A . n 
A 1 212 LEU 212 252 252 LEU LEU A . n 
A 1 213 GLU 213 253 253 GLU GLU A . n 
A 1 214 GLU 214 254 254 GLU GLU A . n 
A 1 215 LEU 215 255 255 LEU LEU A . n 
A 1 216 ASN 216 256 256 ASN ASN A . n 
A 1 217 ALA 217 257 257 ALA ALA A . n 
A 1 218 LYS 218 258 258 LYS LYS A . n 
A 1 219 SER 219 259 259 SER SER A . n 
A 1 220 PRO 220 260 260 PRO PRO A . n 
A 1 221 GLY 221 261 261 GLY GLY A . n 
A 1 222 GLN 222 262 262 GLN GLN A . n 
A 1 223 PRO 223 263 263 PRO PRO A . n 
A 1 224 ILE 224 264 264 ILE ILE A . n 
A 1 225 GLN 225 265 265 GLN GLN A . n 
A 1 226 VAL 226 266 266 VAL VAL A . n 
A 1 227 VAL 227 267 267 VAL VAL A . n 
A 1 228 TYR 228 268 268 TYR TYR A . n 
A 1 229 VAL 229 269 269 VAL VAL A . n 
A 1 230 PRO 230 270 270 PRO PRO A . n 
A 1 231 SER 231 271 271 SER SER A . n 
A 1 232 HIS 232 272 272 HIS HIS A . n 
A 1 233 LEU 233 273 273 LEU LEU A . n 
A 1 234 TYR 234 274 274 TYR TYR A . n 
A 1 235 HIS 235 275 275 HIS HIS A . n 
A 1 236 MET 236 276 276 MET MET A . n 
A 1 237 VAL 237 277 277 VAL VAL A . n 
A 1 238 PHE 238 278 278 PHE PHE A . n 
A 1 239 GLU 239 279 279 GLU GLU A . n 
A 1 240 LEU 240 280 280 LEU LEU A . n 
A 1 241 PHE 241 281 281 PHE PHE A . n 
A 1 242 LYS 242 282 282 LYS LYS A . n 
A 1 243 ASN 243 283 283 ASN ASN A . n 
A 1 244 ALA 244 284 284 ALA ALA A . n 
A 1 245 MET 245 285 285 MET MET A . n 
A 1 246 ARG 246 286 286 ARG ARG A . n 
A 1 247 ALA 247 287 287 ALA ALA A . n 
A 1 248 THR 248 288 288 THR THR A . n 
A 1 249 MET 249 289 289 MET MET A . n 
A 1 250 GLU 250 290 290 GLU GLU A . n 
A 1 251 HIS 251 291 291 HIS HIS A . n 
A 1 252 HIS 252 292 292 HIS HIS A . n 
A 1 253 ALA 253 293 293 ALA ALA A . n 
A 1 254 ASN 254 294 294 ASN ASN A . n 
A 1 255 ARG 255 295 295 ARG ARG A . n 
A 1 256 GLY 256 296 296 GLY GLY A . n 
A 1 257 VAL 257 297 297 VAL VAL A . n 
A 1 258 TYR 258 298 298 TYR TYR A . n 
A 1 259 PRO 259 299 299 PRO PRO A . n 
A 1 260 PRO 260 300 300 PRO PRO A . n 
A 1 261 ILE 261 301 301 ILE ILE A . n 
A 1 262 GLN 262 302 302 GLN GLN A . n 
A 1 263 VAL 263 303 303 VAL VAL A . n 
A 1 264 HIS 264 304 304 HIS HIS A . n 
A 1 265 VAL 265 305 305 VAL VAL A . n 
A 1 266 THR 266 306 306 THR THR A . n 
A 1 267 LEU 267 307 307 LEU LEU A . n 
A 1 268 GLY 268 308 308 GLY GLY A . n 
A 1 269 ASN 269 309 309 ASN ASN A . n 
A 1 270 GLU 270 310 310 GLU GLU A . n 
A 1 271 ASP 271 311 311 ASP ASP A . n 
A 1 272 LEU 272 312 312 LEU LEU A . n 
A 1 273 THR 273 313 313 THR THR A . n 
A 1 274 VAL 274 314 314 VAL VAL A . n 
A 1 275 LYS 275 315 315 LYS LYS A . n 
A 1 276 MET 276 316 316 MET MET A . n 
A 1 277 SER 277 317 317 SER SER A . n 
A 1 278 ASP 278 318 318 ASP ASP A . n 
A 1 279 ARG 279 319 319 ARG ARG A . n 
A 1 280 GLY 280 320 320 GLY GLY A . n 
A 1 281 GLY 281 321 321 GLY GLY A . n 
A 1 282 GLY 282 322 322 GLY GLY A . n 
A 1 283 VAL 283 323 323 VAL VAL A . n 
A 1 284 PRO 284 324 324 PRO PRO A . n 
A 1 285 LEU 285 325 325 LEU LEU A . n 
A 1 286 ARG 286 326 326 ARG ARG A . n 
A 1 287 LYS 287 327 327 LYS LYS A . n 
A 1 288 ILE 288 328 328 ILE ILE A . n 
A 1 289 ASP 289 329 329 ASP ASP A . n 
A 1 290 ARG 290 330 330 ARG ARG A . n 
A 1 291 LEU 291 331 331 LEU LEU A . n 
A 1 292 PHE 292 332 332 PHE PHE A . n 
A 1 293 ASN 293 333 333 ASN ASN A . n 
A 1 294 TYR 294 334 334 TYR TYR A . n 
A 1 295 MET 295 335 335 MET MET A . n 
A 1 296 TYR 296 336 336 TYR TYR A . n 
A 1 297 SER 297 337 337 SER SER A . n 
A 1 298 THR 298 338 338 THR THR A . n 
A 1 299 ALA 299 339 339 ALA ALA A . n 
A 1 300 PRO 300 340 340 PRO PRO A . n 
A 1 301 ARG 301 341 341 ARG ARG A . n 
A 1 302 PRO 302 342 342 PRO PRO A . n 
A 1 303 ARG 303 343 343 ARG ARG A . n 
A 1 304 VAL 304 344 344 VAL VAL A . n 
A 1 305 GLU 305 345 345 GLU GLU A . n 
A 1 306 THR 306 346 346 THR THR A . n 
A 1 307 SER 307 347 347 SER SER A . n 
A 1 308 ARG 308 348 348 ARG ARG A . n 
A 1 309 ALA 309 349 349 ALA ALA A . n 
A 1 310 VAL 310 350 350 VAL VAL A . n 
A 1 311 PRO 311 351 351 PRO PRO A . n 
A 1 312 LEU 312 352 352 LEU LEU A . n 
A 1 313 ALA 313 353 353 ALA ALA A . n 
A 1 314 GLY 314 354 354 GLY GLY A . n 
A 1 315 PHE 315 355 355 PHE PHE A . n 
A 1 316 GLY 316 356 356 GLY GLY A . n 
A 1 317 TYR 317 357 357 TYR TYR A . n 
A 1 318 GLY 318 358 358 GLY GLY A . n 
A 1 319 LEU 319 359 359 LEU LEU A . n 
A 1 320 PRO 320 360 360 PRO PRO A . n 
A 1 321 ILE 321 361 361 ILE ILE A . n 
A 1 322 SER 322 362 362 SER SER A . n 
A 1 323 ARG 323 363 363 ARG ARG A . n 
A 1 324 LEU 324 364 364 LEU LEU A . n 
A 1 325 TYR 325 365 365 TYR TYR A . n 
A 1 326 ALA 326 366 366 ALA ALA A . n 
A 1 327 GLN 327 367 367 GLN GLN A . n 
A 1 328 TYR 328 368 368 TYR TYR A . n 
A 1 329 PHE 329 369 369 PHE PHE A . n 
A 1 330 GLN 330 370 370 GLN GLN A . n 
A 1 331 GLY 331 371 371 GLY GLY A . n 
A 1 332 ASP 332 372 372 ASP ASP A . n 
A 1 333 LEU 333 373 373 LEU LEU A . n 
A 1 334 LYS 334 374 374 LYS LYS A . n 
A 1 335 LEU 335 375 375 LEU LEU A . n 
A 1 336 TYR 336 376 376 TYR TYR A . n 
A 1 337 SER 337 377 377 SER SER A . n 
A 1 338 LEU 338 378 378 LEU LEU A . n 
A 1 339 GLU 339 379 379 GLU GLU A . n 
A 1 340 GLY 340 380 380 GLY GLY A . n 
A 1 341 TYR 341 381 381 TYR TYR A . n 
A 1 342 GLY 342 382 382 GLY GLY A . n 
A 1 343 THR 343 383 383 THR THR A . n 
A 1 344 ASP 344 384 384 ASP ASP A . n 
A 1 345 ALA 345 385 385 ALA ALA A . n 
A 1 346 VAL 346 386 386 VAL VAL A . n 
A 1 347 ILE 347 387 387 ILE ILE A . n 
A 1 348 TYR 348 388 388 TYR TYR A . n 
A 1 349 ILE 349 389 389 ILE ILE A . n 
A 1 350 LYS 350 390 390 LYS LYS A . n 
A 1 351 ALA 351 391 391 ALA ALA A . n 
A 1 352 LEU 352 392 392 LEU LEU A . n 
A 1 353 SER 353 393 393 SER SER A . n 
A 1 354 THR 354 394 394 THR THR A . n 
A 1 355 ASP 355 395 395 ASP ASP A . n 
A 1 356 SER 356 396 396 SER SER A . n 
A 1 357 ILE 357 397 397 ILE ILE A . n 
A 1 358 GLU 358 398 398 GLU GLU A . n 
A 1 359 ARG 359 399 399 ARG ARG A . n 
A 1 360 LEU 360 400 400 LEU LEU A . n 
A 1 361 PRO 361 401 401 PRO PRO A . n 
A 1 362 VAL 362 402 402 VAL VAL A . n 
A 1 363 TYR 363 403 403 TYR TYR A . n 
A 1 364 ASN 364 404 404 ASN ASN A . n 
A 1 365 LYS 365 405 405 LYS LYS A . n 
A 1 366 ALA 366 406 406 ALA ALA A . n 
A 1 367 ALA 367 407 407 ALA ALA A . n 
A 1 368 TRP 368 408 408 TRP TRP A . n 
A 1 369 LYS 369 409 409 LYS LYS A . n 
A 1 370 HIS 370 410 410 HIS HIS A . n 
A 1 371 TYR 371 411 411 TYR TYR A . n 
A 1 372 ASN 372 412 412 ASN ASN A . n 
A 1 373 THR 373 413 413 THR THR A . n 
A 1 374 ASN 374 414 414 ASN ASN A . n 
A 1 375 HIS 375 415 415 HIS HIS A . n 
A 1 376 GLU 376 416 416 GLU GLU A . n 
A 1 377 ALA 377 417 417 ALA ALA A . n 
A 1 378 ASP 378 418 418 ASP ASP A . n 
A 1 379 ASP 379 419 419 ASP ASP A . n 
A 1 380 TRP 380 420 420 TRP TRP A . n 
A 1 381 CYS 381 421 421 CYS CYS A . n 
A 1 382 VAL 382 422 422 VAL VAL A . n 
A 1 383 PRO 383 423 423 PRO PRO A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EMR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EMR 
_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 K     1   501 501 K     K   A . 
C 3 A1EMR 1   502 601 A1EMR L0R A . 
D 4 GOL   1   503 701 GOL   GOL A . 
E 4 GOL   1   504 801 GOL   GOL A . 
F 4 GOL   1   505 901 GOL   GOL A . 
G 5 HOH   1   601 57  HOH   HOH A . 
G 5 HOH   2   602 84  HOH   HOH A . 
G 5 HOH   3   603 213 HOH   HOH A . 
G 5 HOH   4   604 136 HOH   HOH A . 
G 5 HOH   5   605 17  HOH   HOH A . 
G 5 HOH   6   606 43  HOH   HOH A . 
G 5 HOH   7   607 86  HOH   HOH A . 
G 5 HOH   8   608 243 HOH   HOH A . 
G 5 HOH   9   609 190 HOH   HOH A . 
G 5 HOH   10  610 170 HOH   HOH A . 
G 5 HOH   11  611 33  HOH   HOH A . 
G 5 HOH   12  612 152 HOH   HOH A . 
G 5 HOH   13  613 54  HOH   HOH A . 
G 5 HOH   14  614 78  HOH   HOH A . 
G 5 HOH   15  615 37  HOH   HOH A . 
G 5 HOH   16  616 151 HOH   HOH A . 
G 5 HOH   17  617 96  HOH   HOH A . 
G 5 HOH   18  618 89  HOH   HOH A . 
G 5 HOH   19  619 134 HOH   HOH A . 
G 5 HOH   20  620 237 HOH   HOH A . 
G 5 HOH   21  621 93  HOH   HOH A . 
G 5 HOH   22  622 167 HOH   HOH A . 
G 5 HOH   23  623 85  HOH   HOH A . 
G 5 HOH   24  624 77  HOH   HOH A . 
G 5 HOH   25  625 178 HOH   HOH A . 
G 5 HOH   26  626 234 HOH   HOH A . 
G 5 HOH   27  627 187 HOH   HOH A . 
G 5 HOH   28  628 129 HOH   HOH A . 
G 5 HOH   29  629 64  HOH   HOH A . 
G 5 HOH   30  630 28  HOH   HOH A . 
G 5 HOH   31  631 215 HOH   HOH A . 
G 5 HOH   32  632 216 HOH   HOH A . 
G 5 HOH   33  633 208 HOH   HOH A . 
G 5 HOH   34  634 119 HOH   HOH A . 
G 5 HOH   35  635 39  HOH   HOH A . 
G 5 HOH   36  636 26  HOH   HOH A . 
G 5 HOH   37  637 109 HOH   HOH A . 
G 5 HOH   38  638 48  HOH   HOH A . 
G 5 HOH   39  639 30  HOH   HOH A . 
G 5 HOH   40  640 81  HOH   HOH A . 
G 5 HOH   41  641 87  HOH   HOH A . 
G 5 HOH   42  642 22  HOH   HOH A . 
G 5 HOH   43  643 74  HOH   HOH A . 
G 5 HOH   44  644 139 HOH   HOH A . 
G 5 HOH   45  645 113 HOH   HOH A . 
G 5 HOH   46  646 212 HOH   HOH A . 
G 5 HOH   47  647 80  HOH   HOH A . 
G 5 HOH   48  648 32  HOH   HOH A . 
G 5 HOH   49  649 47  HOH   HOH A . 
G 5 HOH   50  650 209 HOH   HOH A . 
G 5 HOH   51  651 25  HOH   HOH A . 
G 5 HOH   52  652 41  HOH   HOH A . 
G 5 HOH   53  653 181 HOH   HOH A . 
G 5 HOH   54  654 65  HOH   HOH A . 
G 5 HOH   55  655 88  HOH   HOH A . 
G 5 HOH   56  656 52  HOH   HOH A . 
G 5 HOH   57  657 117 HOH   HOH A . 
G 5 HOH   58  658 21  HOH   HOH A . 
G 5 HOH   59  659 118 HOH   HOH A . 
G 5 HOH   60  660 210 HOH   HOH A . 
G 5 HOH   61  661 63  HOH   HOH A . 
G 5 HOH   62  662 27  HOH   HOH A . 
G 5 HOH   63  663 50  HOH   HOH A . 
G 5 HOH   64  664 114 HOH   HOH A . 
G 5 HOH   65  665 46  HOH   HOH A . 
G 5 HOH   66  666 103 HOH   HOH A . 
G 5 HOH   67  667 29  HOH   HOH A . 
G 5 HOH   68  668 104 HOH   HOH A . 
G 5 HOH   69  669 76  HOH   HOH A . 
G 5 HOH   70  670 135 HOH   HOH A . 
G 5 HOH   71  671 13  HOH   HOH A . 
G 5 HOH   72  672 179 HOH   HOH A . 
G 5 HOH   73  673 225 HOH   HOH A . 
G 5 HOH   74  674 241 HOH   HOH A . 
G 5 HOH   75  675 137 HOH   HOH A . 
G 5 HOH   76  676 149 HOH   HOH A . 
G 5 HOH   77  677 11  HOH   HOH A . 
G 5 HOH   78  678 49  HOH   HOH A . 
G 5 HOH   79  679 53  HOH   HOH A . 
G 5 HOH   80  680 36  HOH   HOH A . 
G 5 HOH   81  681 9   HOH   HOH A . 
G 5 HOH   82  682 20  HOH   HOH A . 
G 5 HOH   83  683 34  HOH   HOH A . 
G 5 HOH   84  684 133 HOH   HOH A . 
G 5 HOH   85  685 45  HOH   HOH A . 
G 5 HOH   86  686 24  HOH   HOH A . 
G 5 HOH   87  687 155 HOH   HOH A . 
G 5 HOH   88  688 98  HOH   HOH A . 
G 5 HOH   89  689 165 HOH   HOH A . 
G 5 HOH   90  690 220 HOH   HOH A . 
G 5 HOH   91  691 6   HOH   HOH A . 
G 5 HOH   92  692 235 HOH   HOH A . 
G 5 HOH   93  693 40  HOH   HOH A . 
G 5 HOH   94  694 12  HOH   HOH A . 
G 5 HOH   95  695 157 HOH   HOH A . 
G 5 HOH   96  696 55  HOH   HOH A . 
G 5 HOH   97  697 224 HOH   HOH A . 
G 5 HOH   98  698 219 HOH   HOH A . 
G 5 HOH   99  699 145 HOH   HOH A . 
G 5 HOH   100 700 51  HOH   HOH A . 
G 5 HOH   101 701 90  HOH   HOH A . 
G 5 HOH   102 702 199 HOH   HOH A . 
G 5 HOH   103 703 228 HOH   HOH A . 
G 5 HOH   104 704 173 HOH   HOH A . 
G 5 HOH   105 705 183 HOH   HOH A . 
G 5 HOH   106 706 8   HOH   HOH A . 
G 5 HOH   107 707 66  HOH   HOH A . 
G 5 HOH   108 708 95  HOH   HOH A . 
G 5 HOH   109 709 67  HOH   HOH A . 
G 5 HOH   110 710 172 HOH   HOH A . 
G 5 HOH   111 711 160 HOH   HOH A . 
G 5 HOH   112 712 62  HOH   HOH A . 
G 5 HOH   113 713 19  HOH   HOH A . 
G 5 HOH   114 714 23  HOH   HOH A . 
G 5 HOH   115 715 143 HOH   HOH A . 
G 5 HOH   116 716 218 HOH   HOH A . 
G 5 HOH   117 717 79  HOH   HOH A . 
G 5 HOH   118 718 116 HOH   HOH A . 
G 5 HOH   119 719 164 HOH   HOH A . 
G 5 HOH   120 720 231 HOH   HOH A . 
G 5 HOH   121 721 161 HOH   HOH A . 
G 5 HOH   122 722 14  HOH   HOH A . 
G 5 HOH   123 723 61  HOH   HOH A . 
G 5 HOH   124 724 128 HOH   HOH A . 
G 5 HOH   125 725 15  HOH   HOH A . 
G 5 HOH   126 726 168 HOH   HOH A . 
G 5 HOH   127 727 91  HOH   HOH A . 
G 5 HOH   128 728 125 HOH   HOH A . 
G 5 HOH   129 729 72  HOH   HOH A . 
G 5 HOH   130 730 75  HOH   HOH A . 
G 5 HOH   131 731 10  HOH   HOH A . 
G 5 HOH   132 732 60  HOH   HOH A . 
G 5 HOH   133 733 130 HOH   HOH A . 
G 5 HOH   134 734 123 HOH   HOH A . 
G 5 HOH   135 735 112 HOH   HOH A . 
G 5 HOH   136 736 156 HOH   HOH A . 
G 5 HOH   137 737 131 HOH   HOH A . 
G 5 HOH   138 738 56  HOH   HOH A . 
G 5 HOH   139 739 222 HOH   HOH A . 
G 5 HOH   140 740 35  HOH   HOH A . 
G 5 HOH   141 741 106 HOH   HOH A . 
G 5 HOH   142 742 144 HOH   HOH A . 
G 5 HOH   143 743 138 HOH   HOH A . 
G 5 HOH   144 744 127 HOH   HOH A . 
G 5 HOH   145 745 42  HOH   HOH A . 
G 5 HOH   146 746 221 HOH   HOH A . 
G 5 HOH   147 747 97  HOH   HOH A . 
G 5 HOH   148 748 140 HOH   HOH A . 
G 5 HOH   149 749 174 HOH   HOH A . 
G 5 HOH   150 750 101 HOH   HOH A . 
G 5 HOH   151 751 115 HOH   HOH A . 
G 5 HOH   152 752 192 HOH   HOH A . 
G 5 HOH   153 753 122 HOH   HOH A . 
G 5 HOH   154 754 18  HOH   HOH A . 
G 5 HOH   155 755 31  HOH   HOH A . 
G 5 HOH   156 756 124 HOH   HOH A . 
G 5 HOH   157 757 99  HOH   HOH A . 
G 5 HOH   158 758 185 HOH   HOH A . 
G 5 HOH   159 759 94  HOH   HOH A . 
G 5 HOH   160 760 111 HOH   HOH A . 
G 5 HOH   161 761 44  HOH   HOH A . 
G 5 HOH   162 762 69  HOH   HOH A . 
G 5 HOH   163 763 71  HOH   HOH A . 
G 5 HOH   164 764 7   HOH   HOH A . 
G 5 HOH   165 765 105 HOH   HOH A . 
G 5 HOH   166 766 4   HOH   HOH A . 
G 5 HOH   167 767 146 HOH   HOH A . 
G 5 HOH   168 768 2   HOH   HOH A . 
G 5 HOH   169 769 132 HOH   HOH A . 
G 5 HOH   170 770 154 HOH   HOH A . 
G 5 HOH   171 771 38  HOH   HOH A . 
G 5 HOH   172 772 211 HOH   HOH A . 
G 5 HOH   173 773 198 HOH   HOH A . 
G 5 HOH   174 774 184 HOH   HOH A . 
G 5 HOH   175 775 141 HOH   HOH A . 
G 5 HOH   176 776 227 HOH   HOH A . 
G 5 HOH   177 777 150 HOH   HOH A . 
G 5 HOH   178 778 240 HOH   HOH A . 
G 5 HOH   179 779 159 HOH   HOH A . 
G 5 HOH   180 780 182 HOH   HOH A . 
G 5 HOH   181 781 189 HOH   HOH A . 
G 5 HOH   182 782 153 HOH   HOH A . 
G 5 HOH   183 783 176 HOH   HOH A . 
G 5 HOH   184 784 202 HOH   HOH A . 
G 5 HOH   185 785 148 HOH   HOH A . 
G 5 HOH   186 786 207 HOH   HOH A . 
G 5 HOH   187 787 92  HOH   HOH A . 
G 5 HOH   188 788 193 HOH   HOH A . 
G 5 HOH   189 789 58  HOH   HOH A . 
G 5 HOH   190 790 142 HOH   HOH A . 
G 5 HOH   191 791 171 HOH   HOH A . 
G 5 HOH   192 792 191 HOH   HOH A . 
G 5 HOH   193 793 175 HOH   HOH A . 
G 5 HOH   194 794 163 HOH   HOH A . 
G 5 HOH   195 795 1   HOH   HOH A . 
G 5 HOH   196 796 238 HOH   HOH A . 
G 5 HOH   197 797 197 HOH   HOH A . 
G 5 HOH   198 798 242 HOH   HOH A . 
G 5 HOH   199 799 206 HOH   HOH A . 
G 5 HOH   200 800 194 HOH   HOH A . 
G 5 HOH   201 801 203 HOH   HOH A . 
G 5 HOH   202 802 232 HOH   HOH A . 
G 5 HOH   203 803 230 HOH   HOH A . 
G 5 HOH   204 804 83  HOH   HOH A . 
G 5 HOH   205 805 169 HOH   HOH A . 
G 5 HOH   206 806 239 HOH   HOH A . 
G 5 HOH   207 807 223 HOH   HOH A . 
G 5 HOH   208 808 162 HOH   HOH A . 
G 5 HOH   209 809 166 HOH   HOH A . 
G 5 HOH   210 810 229 HOH   HOH A . 
G 5 HOH   211 811 102 HOH   HOH A . 
G 5 HOH   212 812 200 HOH   HOH A . 
G 5 HOH   213 813 120 HOH   HOH A . 
G 5 HOH   214 814 217 HOH   HOH A . 
G 5 HOH   215 815 180 HOH   HOH A . 
G 5 HOH   216 816 201 HOH   HOH A . 
G 5 HOH   217 817 158 HOH   HOH A . 
G 5 HOH   218 818 205 HOH   HOH A . 
G 5 HOH   219 819 126 HOH   HOH A . 
G 5 HOH   220 820 196 HOH   HOH A . 
G 5 HOH   221 821 188 HOH   HOH A . 
G 5 HOH   222 822 186 HOH   HOH A . 
G 5 HOH   223 823 214 HOH   HOH A . 
G 5 HOH   224 824 147 HOH   HOH A . 
G 5 HOH   225 825 233 HOH   HOH A . 
G 5 HOH   226 826 82  HOH   HOH A . 
G 5 HOH   227 827 236 HOH   HOH A . 
G 5 HOH   228 828 100 HOH   HOH A . 
G 5 HOH   229 829 5   HOH   HOH A . 
G 5 HOH   230 830 204 HOH   HOH A . 
G 5 HOH   231 831 68  HOH   HOH A . 
G 5 HOH   232 832 195 HOH   HOH A . 
G 5 HOH   233 833 59  HOH   HOH A . 
G 5 HOH   234 834 16  HOH   HOH A . 
G 5 HOH   235 835 226 HOH   HOH A . 
G 5 HOH   236 836 73  HOH   HOH A . 
G 5 HOH   237 837 110 HOH   HOH A . 
G 5 HOH   238 838 3   HOH   HOH A . 
G 5 HOH   239 839 107 HOH   HOH A . 
G 5 HOH   240 840 121 HOH   HOH A . 
G 5 HOH   241 841 70  HOH   HOH A . 
G 5 HOH   242 842 108 HOH   HOH A . 
G 5 HOH   243 843 177 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.14_3260: ???)' 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                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M3O 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     98.880 
_cell.length_a_esd                 ? 
_cell.length_b                     98.880 
_cell.length_b_esd                 ? 
_cell.length_c                     110.339 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9M3O 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9M3O 
_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          61.09 
_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                                       9M3O 
_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                                 9M3O 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.762 
_refine.ls_d_res_low                             27.585 
_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                     38944 
_refine.ls_number_reflns_R_free                  1932 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    71.44 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1782 
_refine.ls_R_factor_R_free                       0.1978 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1771 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 28.18 
_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                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.762 
_refine_hist.d_res_low                        27.585 
_refine_hist.number_atoms_solvent             243 
_refine_hist.number_atoms_total               3292 
_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        3004 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 3177 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.703  ? 4319 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.504 ? 1931 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 460  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 560  ? 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' 1.7623 1.8064 . . 8   218  6.00   . . . . 0.3081 . . . . . . . . . . . . . . . 0.2739 
'X-RAY DIFFRACTION' 1.8064 1.8552 . . 24  403  11.00  . . . . 0.2525 . . . . . . . . . . . . . . . 0.2160 
'X-RAY DIFFRACTION' 1.8552 1.9098 . . 25  641  17.00  . . . . 0.2493 . . . . . . . . . . . . . . . 0.3011 
'X-RAY DIFFRACTION' 1.9098 1.9714 . . 39  1086 29.00  . . . . 0.2592 . . . . . . . . . . . . . . . 0.2833 
'X-RAY DIFFRACTION' 1.9714 2.0419 . . 92  1895 52.00  . . . . 0.2580 . . . . . . . . . . . . . . . 0.2697 
'X-RAY DIFFRACTION' 2.0419 2.1236 . . 122 2914 79.00  . . . . 0.2419 . . . . . . . . . . . . . . . 0.2807 
'X-RAY DIFFRACTION' 2.1236 2.2202 . . 215 3618 100.00 . . . . 0.2273 . . . . . . . . . . . . . . . 0.2641 
'X-RAY DIFFRACTION' 2.2202 2.3372 . . 209 3659 100.00 . . . . 0.2046 . . . . . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 2.3372 2.4835 . . 183 3701 100.00 . . . . 0.2010 . . . . . . . . . . . . . . . 0.2508 
'X-RAY DIFFRACTION' 2.4835 2.6751 . . 198 3682 100.00 . . . . 0.2029 . . . . . . . . . . . . . . . 0.2333 
'X-RAY DIFFRACTION' 2.6751 2.9441 . . 208 3709 100.00 . . . . 0.1932 . . . . . . . . . . . . . . . 0.2449 
'X-RAY DIFFRACTION' 2.9441 3.3694 . . 198 3734 100.00 . . . . 0.1767 . . . . . . . . . . . . . . . 0.1814 
'X-RAY DIFFRACTION' 3.3694 4.2427 . . 193 3801 100.00 . . . . 0.1495 . . . . . . . . . . . . . . . 0.1900 
'X-RAY DIFFRACTION' 4.2427 27.585 . . 218 3951 100.00 . . . . 0.1574 . . . . . . . . . . . . . . . 0.1547 
# 
_struct.entry_id                     9M3O 
_struct.title                        
'Crystal structure of human pyruvate dehydrogenase kinase isoform 1 in complex with ATP competitive inhibitor 8' 
_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        9M3O 
_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 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PDK1_HUMAN 
_struct_ref.pdbx_db_accession          Q15118 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQE
LLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSL
LFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFEL
FKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLP
ISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDWCVP
;
_struct_ref.pdbx_align_begin           41 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9M3O 
_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                 383 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q15118 
_struct_ref_seq.db_align_beg                  41 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  423 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       41 
_struct_ref_seq.pdbx_auth_seq_align_end       423 
# 
_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)' 7200  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  32210 ? 
# 
_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 
# 
_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' 7_555 y,x,-z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
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 GLY A 1   ? ARG A 11  ? GLY A 41  ARG A 51  1 ? 11 
HELX_P HELX_P2  AA2 SER A 18  ? VAL A 28  ? SER A 58  VAL A 68  1 ? 11 
HELX_P HELX_P3  AA3 CYS A 31  ? SER A 55  ? CYS A 71  SER A 95  1 ? 25 
HELX_P HELX_P4  AA4 PRO A 58  ? ARG A 63  ? PRO A 98  ARG A 103 1 ? 6  
HELX_P HELX_P5  AA5 THR A 64  ? ASP A 83  ? THR A 104 ASP A 123 1 ? 20 
HELX_P HELX_P6  AA6 ASP A 91  ? HIS A 109 ? ASP A 131 HIS A 149 1 ? 19 
HELX_P HELX_P7  AA7 ASP A 111 ? GLY A 128 ? ASP A 151 GLY A 168 1 ? 18 
HELX_P HELX_P8  AA8 ASP A 130 ? GLY A 163 ? ASP A 170 GLY A 203 1 ? 34 
HELX_P HELX_P9  AA9 VAL A 185 ? ILE A 205 ? VAL A 225 ILE A 245 1 ? 21 
HELX_P HELX_P10 AB1 VAL A 229 ? HIS A 252 ? VAL A 269 HIS A 292 1 ? 24 
HELX_P HELX_P11 AB2 PRO A 284 ? PHE A 292 ? PRO A 324 PHE A 332 5 ? 9  
HELX_P HELX_P12 AB3 ASN A 293 ? THR A 298 ? ASN A 333 THR A 338 1 ? 6  
HELX_P HELX_P13 AB4 TYR A 317 ? PHE A 329 ? TYR A 357 PHE A 369 1 ? 13 
HELX_P HELX_P14 AB5 LEU A 352 ? SER A 356 ? LEU A 392 SER A 396 5 ? 5  
HELX_P HELX_P15 AB6 ASN A 364 ? ASN A 372 ? ASN A 404 ASN A 412 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A ALA 10  O   ? ? ? 1_555 B K   . K ? ? A ALA 50  A K   501 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc2 metalc ? ? A ARG 11  O   ? ? ? 1_555 B K   . K ? ? A ARG 51  A K   501 1_555 ? ? ? ? ? ? ? 3.496 ? ? 
metalc3 metalc ? ? A PHE 12  O   ? ? ? 1_555 B K   . K ? ? A PHE 52  A K   501 1_555 ? ? ? ? ? ? ? 2.628 ? ? 
metalc4 metalc ? ? A ASN 49  OD1 ? ? ? 1_555 B K   . K ? ? A ASN 89  A K   501 1_555 ? ? ? ? ? ? ? 2.721 ? ? 
metalc5 metalc ? ? A TYR 363 O   ? ? ? 1_555 B K   . K ? ? A TYR 403 A K   501 1_555 ? ? ? ? ? ? ? 2.581 ? ? 
metalc6 metalc ? ? B K   .   K   ? ? ? 1_555 G HOH . O ? ? A K   501 A HOH 795 1_555 ? ? ? ? ? ? ? 2.625 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ALA 10  ? A ALA 50  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? A ARG 11  ? A ARG 51  ? 1_555 71.7  ? 
2  O   ? A ALA 10  ? A ALA 50  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? A PHE 12  ? A PHE 52  ? 1_555 85.9  ? 
3  O   ? A ARG 11  ? A ARG 51  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? A PHE 12  ? A PHE 52  ? 1_555 68.2  ? 
4  O   ? A ALA 10  ? A ALA 50  ? 1_555 K ? B K . ? A K 501 ? 1_555 OD1 ? A ASN 49  ? A ASN 89  ? 1_555 91.4  ? 
5  O   ? A ARG 11  ? A ARG 51  ? 1_555 K ? B K . ? A K 501 ? 1_555 OD1 ? A ASN 49  ? A ASN 89  ? 1_555 144.3 ? 
6  O   ? A PHE 12  ? A PHE 52  ? 1_555 K ? B K . ? A K 501 ? 1_555 OD1 ? A ASN 49  ? A ASN 89  ? 1_555 79.6  ? 
7  O   ? A ALA 10  ? A ALA 50  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? A TYR 363 ? A TYR 403 ? 1_555 99.4  ? 
8  O   ? A ARG 11  ? A ARG 51  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? A TYR 363 ? A TYR 403 ? 1_555 124.5 ? 
9  O   ? A PHE 12  ? A PHE 52  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? A TYR 363 ? A TYR 403 ? 1_555 167.2 ? 
10 OD1 ? A ASN 49  ? A ASN 89  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? A TYR 363 ? A TYR 403 ? 1_555 88.6  ? 
11 O   ? A ALA 10  ? A ALA 50  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? G HOH .   ? A HOH 795 ? 1_555 134.4 ? 
12 O   ? A ARG 11  ? A ARG 51  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? G HOH .   ? A HOH 795 ? 1_555 63.6  ? 
13 O   ? A PHE 12  ? A PHE 52  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? G HOH .   ? A HOH 795 ? 1_555 85.8  ? 
14 OD1 ? A ASN 49  ? A ASN 89  ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? G HOH .   ? A HOH 795 ? 1_555 130.7 ? 
15 O   ? A TYR 363 ? A TYR 403 ? 1_555 K ? B K . ? A K 501 ? 1_555 O   ? G HOH .   ? A HOH 795 ? 1_555 98.3  ? 
# 
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 ASN A 180 ? ASN A 184 ? ASN A 220 ASN A 224 
AA1 2 GLN A 225 ? TYR A 228 ? GLN A 265 TYR A 268 
AA2 1 LEU A 210 ? ASN A 216 ? LEU A 250 ASN A 256 
AA2 2 ILE A 261 ? LEU A 267 ? ILE A 301 LEU A 307 
AA2 3 ASP A 271 ? ASP A 278 ? ASP A 311 ASP A 318 
AA2 4 GLY A 342 ? LYS A 350 ? GLY A 382 LYS A 390 
AA2 5 ASP A 332 ? LEU A 338 ? ASP A 372 LEU A 378 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASN A 180 ? N ASN A 220 O TYR A 228 ? O TYR A 268 
AA2 1 2 N GLU A 211 ? N GLU A 251 O VAL A 263 ? O VAL A 303 
AA2 2 3 N GLN A 262 ? N GLN A 302 O SER A 277 ? O SER A 317 
AA2 3 4 N LEU A 272 ? N LEU A 312 O ILE A 349 ? O ILE A 389 
AA2 4 5 O GLY A 342 ? O GLY A 382 N LEU A 338 ? N LEU A 378 
# 
_pdbx_entry_details.entry_id                   9M3O 
_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   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 68  ? ? -104.99 -68.02 
2 1 PHE A 167 ? ? -141.17 -10.09 
3 1 GLU A 310 ? ? -130.00 -35.74 
4 1 ARG A 319 ? ? -112.46 52.29  
5 1 TYR A 381 ? ? -120.96 -66.17 
# 
_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    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     692 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 2.6255  42.8613 3.1731   0.4209 ? 0.1285  ? 0.0421  ? 0.3572 ? -0.1569 ? 0.4479 ? 2.0329 ? 1.3780  
? 0.5705  ? 4.0539 ? -0.8922 ? 2.8676 ? 0.1026  ? -0.2209 ? 0.4093  ? 0.5140  ? -0.0242 ? 0.3967  ? -0.5036 ? -0.1331 ? -0.1757 ? 
2 'X-RAY DIFFRACTION' ? refined 2.4596  46.6588 -8.0915  0.3549 ? 0.0470  ? -0.0707 ? 0.3179 ? -0.0128 ? 0.4597 ? 3.4620 ? -0.2896 
? -0.9888 ? 3.4829 ? 0.7678  ? 3.9810 ? -0.0475 ? 0.1353  ? 0.8044  ? 0.0272  ? 0.0730  ? 0.4535  ? -0.7346 ? -0.4082 ? -0.0413 ? 
3 'X-RAY DIFFRACTION' ? refined 8.7429  31.2604 -21.4539 0.4266 ? -0.0868 ? -0.0807 ? 0.5133 ? 0.0004  ? 0.3011 ? 5.5232 ? 0.4083  
? -2.1670 ? 6.7770 ? 1.9539  ? 7.9814 ? -0.0799 ? 0.6125  ? -0.0868 ? -0.6314 ? 0.0111  ? 0.0152  ? 0.0293  ? -0.3455 ? 0.1386  ? 
4 'X-RAY DIFFRACTION' ? refined -2.9743 26.0482 -7.6141  0.2341 ? 0.0974  ? -0.0422 ? 0.3200 ? -0.0201 ? 0.2941 ? 0.8595 ? 1.1233  
? 0.2237  ? 3.0309 ? 0.6085  ? 0.9799 ? -0.0770 ? -0.2299 ? 0.1584  ? 0.0502  ? 0.0077  ? 0.3717  ? -0.0998 ? -0.0439 ? 0.0955  ? 
5 'X-RAY DIFFRACTION' ? refined -0.1969 13.4112 -7.9101  0.2844 ? 0.0757  ? 0.0240  ? 0.2839 ? -0.0114 ? 0.2689 ? 1.4559 ? -0.1051 
? 0.4288  ? 1.4205 ? 0.1744  ? 1.7152 ? -0.0503 ? -0.0495 ? -0.0013 ? -0.0894 ? 0.0903  ? 0.1021  ? 0.1060  ? 0.0815  ? -0.0369 ? 
6 'X-RAY DIFFRACTION' ? refined 19.0752 28.4294 -1.3291  0.3440 ? 0.0401  ? -0.0016 ? 0.4213 ? -0.1053 ? 0.3444 ? 0.3109 ? -0.1877 
? 0.3438  ? 2.2913 ? -0.8242 ? 0.6951 ? -0.1586 ? -0.1035 ? 0.0126  ? 0.0049  ? -0.0479 ? -0.3230 ? 0.1566  ? 0.2126  ? 0.2487  ? 
# 
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 41 through 71 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 72 through 148 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 149 through 170 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 171 through 244 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 245 through 390 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 391 through 423 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 842 ? 5.91 . 
2 1 O ? A HOH 843 ? 6.54 . 
# 
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 GLY 204 ? A GLY 164 
2  1 Y 1 A LYS 205 ? A LYS 165 
3  1 Y 1 A GLY 206 ? A GLY 166 
4  1 Y 1 A LYS 207 ? A LYS 167 
5  1 Y 1 A GLY 208 ? A GLY 168 
6  1 Y 1 A SER 209 ? A SER 169 
7  1 Y 1 A PRO 210 ? A PRO 170 
8  1 Y 1 A SER 211 ? A SER 171 
9  1 Y 1 A HIS 212 ? A HIS 172 
10 1 Y 1 A ARG 213 ? A ARG 173 
11 1 Y 1 A LYS 214 ? A LYS 174 
# 
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 
A1EMR C10  C N N 1   
A1EMR C11  C Y N 2   
A1EMR C16  C Y N 3   
A1EMR C18  C Y N 4   
A1EMR C20  C Y N 5   
A1EMR C22  C Y N 6   
A1EMR C23  C Y N 7   
A1EMR C25  C N N 8   
A1EMR C26  C Y N 9   
A1EMR C12  C Y N 10  
A1EMR C14  C Y N 11  
A1EMR C2   C Y N 12  
A1EMR C3   C Y N 13  
A1EMR C4   C Y N 14  
A1EMR C5   C Y N 15  
A1EMR C6   C Y N 16  
A1EMR C7   C Y N 17  
A1EMR C8   C N N 18  
A1EMR F1   F N N 19  
A1EMR N13  N Y N 20  
A1EMR N15  N Y N 21  
A1EMR N19  N Y N 22  
A1EMR N21  N Y N 23  
A1EMR N24  N N N 24  
A1EMR N9   N N N 25  
A1EMR O17  O N N 26  
A1EMR H1   H N N 27  
A1EMR H2   H N N 28  
A1EMR H3   H N N 29  
A1EMR H4   H N N 30  
A1EMR H5   H N N 31  
A1EMR H6   H N N 32  
A1EMR H7   H N N 33  
A1EMR H8   H N N 34  
A1EMR H9   H N N 35  
A1EMR H10  H N N 36  
A1EMR H11  H N N 37  
A1EMR H12  H N N 38  
A1EMR H13  H N N 39  
A1EMR H14  H N N 40  
A1EMR H15  H N N 41  
ALA   N    N N N 42  
ALA   CA   C N S 43  
ALA   C    C N N 44  
ALA   O    O N N 45  
ALA   CB   C N N 46  
ALA   OXT  O N N 47  
ALA   H    H N N 48  
ALA   H2   H N N 49  
ALA   HA   H N N 50  
ALA   HB1  H N N 51  
ALA   HB2  H N N 52  
ALA   HB3  H N N 53  
ALA   HXT  H N N 54  
ARG   N    N N N 55  
ARG   CA   C N S 56  
ARG   C    C N N 57  
ARG   O    O N N 58  
ARG   CB   C N N 59  
ARG   CG   C N N 60  
ARG   CD   C N N 61  
ARG   NE   N N N 62  
ARG   CZ   C N N 63  
ARG   NH1  N N N 64  
ARG   NH2  N N N 65  
ARG   OXT  O N N 66  
ARG   H    H N N 67  
ARG   H2   H N N 68  
ARG   HA   H N N 69  
ARG   HB2  H N N 70  
ARG   HB3  H N N 71  
ARG   HG2  H N N 72  
ARG   HG3  H N N 73  
ARG   HD2  H N N 74  
ARG   HD3  H N N 75  
ARG   HE   H N N 76  
ARG   HH11 H N N 77  
ARG   HH12 H N N 78  
ARG   HH21 H N N 79  
ARG   HH22 H N N 80  
ARG   HXT  H N N 81  
ASN   N    N N N 82  
ASN   CA   C N S 83  
ASN   C    C N N 84  
ASN   O    O N N 85  
ASN   CB   C N N 86  
ASN   CG   C N N 87  
ASN   OD1  O N N 88  
ASN   ND2  N N N 89  
ASN   OXT  O N N 90  
ASN   H    H N N 91  
ASN   H2   H N N 92  
ASN   HA   H N N 93  
ASN   HB2  H N N 94  
ASN   HB3  H N N 95  
ASN   HD21 H N N 96  
ASN   HD22 H N N 97  
ASN   HXT  H N N 98  
ASP   N    N N N 99  
ASP   CA   C N S 100 
ASP   C    C N N 101 
ASP   O    O N N 102 
ASP   CB   C N N 103 
ASP   CG   C N N 104 
ASP   OD1  O N N 105 
ASP   OD2  O N N 106 
ASP   OXT  O N N 107 
ASP   H    H N N 108 
ASP   H2   H N N 109 
ASP   HA   H N N 110 
ASP   HB2  H N N 111 
ASP   HB3  H N N 112 
ASP   HD2  H N N 113 
ASP   HXT  H N N 114 
CYS   N    N N N 115 
CYS   CA   C N R 116 
CYS   C    C N N 117 
CYS   O    O N N 118 
CYS   CB   C N N 119 
CYS   SG   S N N 120 
CYS   OXT  O N N 121 
CYS   H    H N N 122 
CYS   H2   H N N 123 
CYS   HA   H N N 124 
CYS   HB2  H N N 125 
CYS   HB3  H N N 126 
CYS   HG   H N N 127 
CYS   HXT  H N N 128 
GLN   N    N N N 129 
GLN   CA   C N S 130 
GLN   C    C N N 131 
GLN   O    O N N 132 
GLN   CB   C N N 133 
GLN   CG   C N N 134 
GLN   CD   C N N 135 
GLN   OE1  O N N 136 
GLN   NE2  N N N 137 
GLN   OXT  O N N 138 
GLN   H    H N N 139 
GLN   H2   H N N 140 
GLN   HA   H N N 141 
GLN   HB2  H N N 142 
GLN   HB3  H N N 143 
GLN   HG2  H N N 144 
GLN   HG3  H N N 145 
GLN   HE21 H N N 146 
GLN   HE22 H N N 147 
GLN   HXT  H N N 148 
GLU   N    N N N 149 
GLU   CA   C N S 150 
GLU   C    C N N 151 
GLU   O    O N N 152 
GLU   CB   C N N 153 
GLU   CG   C N N 154 
GLU   CD   C N N 155 
GLU   OE1  O N N 156 
GLU   OE2  O N N 157 
GLU   OXT  O N N 158 
GLU   H    H N N 159 
GLU   H2   H N N 160 
GLU   HA   H N N 161 
GLU   HB2  H N N 162 
GLU   HB3  H N N 163 
GLU   HG2  H N N 164 
GLU   HG3  H N N 165 
GLU   HE2  H N N 166 
GLU   HXT  H N N 167 
GLY   N    N N N 168 
GLY   CA   C N N 169 
GLY   C    C N N 170 
GLY   O    O N N 171 
GLY   OXT  O N N 172 
GLY   H    H N N 173 
GLY   H2   H N N 174 
GLY   HA2  H N N 175 
GLY   HA3  H N N 176 
GLY   HXT  H N N 177 
GOL   C1   C N N 178 
GOL   O1   O N N 179 
GOL   C2   C N N 180 
GOL   O2   O N N 181 
GOL   C3   C N N 182 
GOL   O3   O N N 183 
GOL   H11  H N N 184 
GOL   H12  H N N 185 
GOL   HO1  H N N 186 
GOL   H2   H N N 187 
GOL   HO2  H N N 188 
GOL   H31  H N N 189 
GOL   H32  H N N 190 
GOL   HO3  H N N 191 
HIS   N    N N N 192 
HIS   CA   C N S 193 
HIS   C    C N N 194 
HIS   O    O N N 195 
HIS   CB   C N N 196 
HIS   CG   C Y N 197 
HIS   ND1  N Y N 198 
HIS   CD2  C Y N 199 
HIS   CE1  C Y N 200 
HIS   NE2  N Y N 201 
HIS   OXT  O N N 202 
HIS   H    H N N 203 
HIS   H2   H N N 204 
HIS   HA   H N N 205 
HIS   HB2  H N N 206 
HIS   HB3  H N N 207 
HIS   HD1  H N N 208 
HIS   HD2  H N N 209 
HIS   HE1  H N N 210 
HIS   HE2  H N N 211 
HIS   HXT  H N N 212 
HOH   O    O N N 213 
HOH   H1   H N N 214 
HOH   H2   H N N 215 
ILE   N    N N N 216 
ILE   CA   C N S 217 
ILE   C    C N N 218 
ILE   O    O N N 219 
ILE   CB   C N S 220 
ILE   CG1  C N N 221 
ILE   CG2  C N N 222 
ILE   CD1  C N N 223 
ILE   OXT  O N N 224 
ILE   H    H N N 225 
ILE   H2   H N N 226 
ILE   HA   H N N 227 
ILE   HB   H N N 228 
ILE   HG12 H N N 229 
ILE   HG13 H N N 230 
ILE   HG21 H N N 231 
ILE   HG22 H N N 232 
ILE   HG23 H N N 233 
ILE   HD11 H N N 234 
ILE   HD12 H N N 235 
ILE   HD13 H N N 236 
ILE   HXT  H N N 237 
K     K    K N N 238 
LEU   N    N N N 239 
LEU   CA   C N S 240 
LEU   C    C N N 241 
LEU   O    O N N 242 
LEU   CB   C N N 243 
LEU   CG   C N N 244 
LEU   CD1  C N N 245 
LEU   CD2  C N N 246 
LEU   OXT  O N N 247 
LEU   H    H N N 248 
LEU   H2   H N N 249 
LEU   HA   H N N 250 
LEU   HB2  H N N 251 
LEU   HB3  H N N 252 
LEU   HG   H N N 253 
LEU   HD11 H N N 254 
LEU   HD12 H N N 255 
LEU   HD13 H N N 256 
LEU   HD21 H N N 257 
LEU   HD22 H N N 258 
LEU   HD23 H N N 259 
LEU   HXT  H N N 260 
LYS   N    N N N 261 
LYS   CA   C N S 262 
LYS   C    C N N 263 
LYS   O    O N N 264 
LYS   CB   C N N 265 
LYS   CG   C N N 266 
LYS   CD   C N N 267 
LYS   CE   C N N 268 
LYS   NZ   N N N 269 
LYS   OXT  O N N 270 
LYS   H    H N N 271 
LYS   H2   H N N 272 
LYS   HA   H N N 273 
LYS   HB2  H N N 274 
LYS   HB3  H N N 275 
LYS   HG2  H N N 276 
LYS   HG3  H N N 277 
LYS   HD2  H N N 278 
LYS   HD3  H N N 279 
LYS   HE2  H N N 280 
LYS   HE3  H N N 281 
LYS   HZ1  H N N 282 
LYS   HZ2  H N N 283 
LYS   HZ3  H N N 284 
LYS   HXT  H N N 285 
MET   N    N N N 286 
MET   CA   C N S 287 
MET   C    C N N 288 
MET   O    O N N 289 
MET   CB   C N N 290 
MET   CG   C N N 291 
MET   SD   S N N 292 
MET   CE   C N N 293 
MET   OXT  O N N 294 
MET   H    H N N 295 
MET   H2   H N N 296 
MET   HA   H N N 297 
MET   HB2  H N N 298 
MET   HB3  H N N 299 
MET   HG2  H N N 300 
MET   HG3  H N N 301 
MET   HE1  H N N 302 
MET   HE2  H N N 303 
MET   HE3  H N N 304 
MET   HXT  H N N 305 
PHE   N    N N N 306 
PHE   CA   C N S 307 
PHE   C    C N N 308 
PHE   O    O N N 309 
PHE   CB   C N N 310 
PHE   CG   C Y N 311 
PHE   CD1  C Y N 312 
PHE   CD2  C Y N 313 
PHE   CE1  C Y N 314 
PHE   CE2  C Y N 315 
PHE   CZ   C Y N 316 
PHE   OXT  O N N 317 
PHE   H    H N N 318 
PHE   H2   H N N 319 
PHE   HA   H N N 320 
PHE   HB2  H N N 321 
PHE   HB3  H N N 322 
PHE   HD1  H N N 323 
PHE   HD2  H N N 324 
PHE   HE1  H N N 325 
PHE   HE2  H N N 326 
PHE   HZ   H N N 327 
PHE   HXT  H N N 328 
PRO   N    N N N 329 
PRO   CA   C N S 330 
PRO   C    C N N 331 
PRO   O    O N N 332 
PRO   CB   C N N 333 
PRO   CG   C N N 334 
PRO   CD   C N N 335 
PRO   OXT  O N N 336 
PRO   H    H N N 337 
PRO   HA   H N N 338 
PRO   HB2  H N N 339 
PRO   HB3  H N N 340 
PRO   HG2  H N N 341 
PRO   HG3  H N N 342 
PRO   HD2  H N N 343 
PRO   HD3  H N N 344 
PRO   HXT  H N N 345 
SER   N    N N N 346 
SER   CA   C N S 347 
SER   C    C N N 348 
SER   O    O N N 349 
SER   CB   C N N 350 
SER   OG   O N N 351 
SER   OXT  O N N 352 
SER   H    H N N 353 
SER   H2   H N N 354 
SER   HA   H N N 355 
SER   HB2  H N N 356 
SER   HB3  H N N 357 
SER   HG   H N N 358 
SER   HXT  H N N 359 
THR   N    N N N 360 
THR   CA   C N S 361 
THR   C    C N N 362 
THR   O    O N N 363 
THR   CB   C N R 364 
THR   OG1  O N N 365 
THR   CG2  C N N 366 
THR   OXT  O N N 367 
THR   H    H N N 368 
THR   H2   H N N 369 
THR   HA   H N N 370 
THR   HB   H N N 371 
THR   HG1  H N N 372 
THR   HG21 H N N 373 
THR   HG22 H N N 374 
THR   HG23 H N N 375 
THR   HXT  H N N 376 
TRP   N    N N N 377 
TRP   CA   C N S 378 
TRP   C    C N N 379 
TRP   O    O N N 380 
TRP   CB   C N N 381 
TRP   CG   C Y N 382 
TRP   CD1  C Y N 383 
TRP   CD2  C Y N 384 
TRP   NE1  N Y N 385 
TRP   CE2  C Y N 386 
TRP   CE3  C Y N 387 
TRP   CZ2  C Y N 388 
TRP   CZ3  C Y N 389 
TRP   CH2  C Y N 390 
TRP   OXT  O N N 391 
TRP   H    H N N 392 
TRP   H2   H N N 393 
TRP   HA   H N N 394 
TRP   HB2  H N N 395 
TRP   HB3  H N N 396 
TRP   HD1  H N N 397 
TRP   HE1  H N N 398 
TRP   HE3  H N N 399 
TRP   HZ2  H N N 400 
TRP   HZ3  H N N 401 
TRP   HH2  H N N 402 
TRP   HXT  H N N 403 
TYR   N    N N N 404 
TYR   CA   C N S 405 
TYR   C    C N N 406 
TYR   O    O N N 407 
TYR   CB   C N N 408 
TYR   CG   C Y N 409 
TYR   CD1  C Y N 410 
TYR   CD2  C Y N 411 
TYR   CE1  C Y N 412 
TYR   CE2  C Y N 413 
TYR   CZ   C Y N 414 
TYR   OH   O N N 415 
TYR   OXT  O N N 416 
TYR   H    H N N 417 
TYR   H2   H N N 418 
TYR   HA   H N N 419 
TYR   HB2  H N N 420 
TYR   HB3  H N N 421 
TYR   HD1  H N N 422 
TYR   HD2  H N N 423 
TYR   HE1  H N N 424 
TYR   HE2  H N N 425 
TYR   HH   H N N 426 
TYR   HXT  H N N 427 
VAL   N    N N N 428 
VAL   CA   C N S 429 
VAL   C    C N N 430 
VAL   O    O N N 431 
VAL   CB   C N N 432 
VAL   CG1  C N N 433 
VAL   CG2  C N N 434 
VAL   OXT  O N N 435 
VAL   H    H N N 436 
VAL   H2   H N N 437 
VAL   HA   H N N 438 
VAL   HB   H N N 439 
VAL   HG11 H N N 440 
VAL   HG12 H N N 441 
VAL   HG13 H N N 442 
VAL   HG21 H N N 443 
VAL   HG22 H N N 444 
VAL   HG23 H N N 445 
VAL   HXT  H N N 446 
# 
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 
A1EMR N13 C12  doub Y N 1   
A1EMR N13 C14  sing Y N 2   
A1EMR C12 C11  sing Y N 3   
A1EMR C10 C11  sing N N 4   
A1EMR C10 N9   sing N N 5   
A1EMR C14 N15  doub Y N 6   
A1EMR C11 C16  doub Y N 7   
A1EMR N15 C16  sing Y N 8   
A1EMR N9  C8   sing N N 9   
A1EMR C8  O17  doub N N 10  
A1EMR C8  C7   sing N N 11  
A1EMR C7  C18  doub Y N 12  
A1EMR C7  C6   sing Y N 13  
A1EMR C18 N19  sing Y N 14  
A1EMR C6  C5   doub Y N 15  
A1EMR N19 C20  doub Y N 16  
A1EMR C5  C20  sing Y N 17  
A1EMR C5  C4   sing Y N 18  
A1EMR C20 N21  sing Y N 19  
A1EMR C4  C3   doub Y N 20  
A1EMR C4  C22  sing Y N 21  
A1EMR N21 C22  sing Y N 22  
A1EMR C3  C2   sing Y N 23  
A1EMR C22 C23  doub Y N 24  
A1EMR C2  F1   sing N N 25  
A1EMR C2  C26  doub Y N 26  
A1EMR C23 C26  sing Y N 27  
A1EMR C23 N24  sing N N 28  
A1EMR N24 C25  sing N N 29  
A1EMR C10 H1   sing N N 30  
A1EMR C10 H2   sing N N 31  
A1EMR C16 H3   sing N N 32  
A1EMR C18 H4   sing N N 33  
A1EMR C25 H5   sing N N 34  
A1EMR C25 H6   sing N N 35  
A1EMR C25 H7   sing N N 36  
A1EMR C26 H8   sing N N 37  
A1EMR C12 H9   sing N N 38  
A1EMR C14 H10  sing N N 39  
A1EMR C3  H11  sing N N 40  
A1EMR C6  H12  sing N N 41  
A1EMR N21 H13  sing N N 42  
A1EMR N24 H14  sing N N 43  
A1EMR N9  H15  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
GOL   C1  O1   sing N N 173 
GOL   C1  C2   sing N N 174 
GOL   C1  H11  sing N N 175 
GOL   C1  H12  sing N N 176 
GOL   O1  HO1  sing N N 177 
GOL   C2  O2   sing N N 178 
GOL   C2  C3   sing N N 179 
GOL   C2  H2   sing N N 180 
GOL   O2  HO2  sing N N 181 
GOL   C3  O3   sing N N 182 
GOL   C3  H31  sing N N 183 
GOL   C3  H32  sing N N 184 
GOL   O3  HO3  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
HOH   O   H1   sing N N 207 
HOH   O   H2   sing N N 208 
ILE   N   CA   sing N N 209 
ILE   N   H    sing N N 210 
ILE   N   H2   sing N N 211 
ILE   CA  C    sing N N 212 
ILE   CA  CB   sing N N 213 
ILE   CA  HA   sing N N 214 
ILE   C   O    doub N N 215 
ILE   C   OXT  sing N N 216 
ILE   CB  CG1  sing N N 217 
ILE   CB  CG2  sing N N 218 
ILE   CB  HB   sing N N 219 
ILE   CG1 CD1  sing N N 220 
ILE   CG1 HG12 sing N N 221 
ILE   CG1 HG13 sing N N 222 
ILE   CG2 HG21 sing N N 223 
ILE   CG2 HG22 sing N N 224 
ILE   CG2 HG23 sing N N 225 
ILE   CD1 HD11 sing N N 226 
ILE   CD1 HD12 sing N N 227 
ILE   CD1 HD13 sing N N 228 
ILE   OXT HXT  sing N N 229 
LEU   N   CA   sing N N 230 
LEU   N   H    sing N N 231 
LEU   N   H2   sing N N 232 
LEU   CA  C    sing N N 233 
LEU   CA  CB   sing N N 234 
LEU   CA  HA   sing N N 235 
LEU   C   O    doub N N 236 
LEU   C   OXT  sing N N 237 
LEU   CB  CG   sing N N 238 
LEU   CB  HB2  sing N N 239 
LEU   CB  HB3  sing N N 240 
LEU   CG  CD1  sing N N 241 
LEU   CG  CD2  sing N N 242 
LEU   CG  HG   sing N N 243 
LEU   CD1 HD11 sing N N 244 
LEU   CD1 HD12 sing N N 245 
LEU   CD1 HD13 sing N N 246 
LEU   CD2 HD21 sing N N 247 
LEU   CD2 HD22 sing N N 248 
LEU   CD2 HD23 sing N N 249 
LEU   OXT HXT  sing N N 250 
LYS   N   CA   sing N N 251 
LYS   N   H    sing N N 252 
LYS   N   H2   sing N N 253 
LYS   CA  C    sing N N 254 
LYS   CA  CB   sing N N 255 
LYS   CA  HA   sing N N 256 
LYS   C   O    doub N N 257 
LYS   C   OXT  sing N N 258 
LYS   CB  CG   sing N N 259 
LYS   CB  HB2  sing N N 260 
LYS   CB  HB3  sing N N 261 
LYS   CG  CD   sing N N 262 
LYS   CG  HG2  sing N N 263 
LYS   CG  HG3  sing N N 264 
LYS   CD  CE   sing N N 265 
LYS   CD  HD2  sing N N 266 
LYS   CD  HD3  sing N N 267 
LYS   CE  NZ   sing N N 268 
LYS   CE  HE2  sing N N 269 
LYS   CE  HE3  sing N N 270 
LYS   NZ  HZ1  sing N N 271 
LYS   NZ  HZ2  sing N N 272 
LYS   NZ  HZ3  sing N N 273 
LYS   OXT HXT  sing N N 274 
MET   N   CA   sing N N 275 
MET   N   H    sing N N 276 
MET   N   H2   sing N N 277 
MET   CA  C    sing N N 278 
MET   CA  CB   sing N N 279 
MET   CA  HA   sing N N 280 
MET   C   O    doub N N 281 
MET   C   OXT  sing N N 282 
MET   CB  CG   sing N N 283 
MET   CB  HB2  sing N N 284 
MET   CB  HB3  sing N N 285 
MET   CG  SD   sing N N 286 
MET   CG  HG2  sing N N 287 
MET   CG  HG3  sing N N 288 
MET   SD  CE   sing N N 289 
MET   CE  HE1  sing N N 290 
MET   CE  HE2  sing N N 291 
MET   CE  HE3  sing N N 292 
MET   OXT HXT  sing N N 293 
PHE   N   CA   sing N N 294 
PHE   N   H    sing N N 295 
PHE   N   H2   sing N N 296 
PHE   CA  C    sing N N 297 
PHE   CA  CB   sing N N 298 
PHE   CA  HA   sing N N 299 
PHE   C   O    doub N N 300 
PHE   C   OXT  sing N N 301 
PHE   CB  CG   sing N N 302 
PHE   CB  HB2  sing N N 303 
PHE   CB  HB3  sing N N 304 
PHE   CG  CD1  doub Y N 305 
PHE   CG  CD2  sing Y N 306 
PHE   CD1 CE1  sing Y N 307 
PHE   CD1 HD1  sing N N 308 
PHE   CD2 CE2  doub Y N 309 
PHE   CD2 HD2  sing N N 310 
PHE   CE1 CZ   doub Y N 311 
PHE   CE1 HE1  sing N N 312 
PHE   CE2 CZ   sing Y N 313 
PHE   CE2 HE2  sing N N 314 
PHE   CZ  HZ   sing N N 315 
PHE   OXT HXT  sing N N 316 
PRO   N   CA   sing N N 317 
PRO   N   CD   sing N N 318 
PRO   N   H    sing N N 319 
PRO   CA  C    sing N N 320 
PRO   CA  CB   sing N N 321 
PRO   CA  HA   sing N N 322 
PRO   C   O    doub N N 323 
PRO   C   OXT  sing N N 324 
PRO   CB  CG   sing N N 325 
PRO   CB  HB2  sing N N 326 
PRO   CB  HB3  sing N N 327 
PRO   CG  CD   sing N N 328 
PRO   CG  HG2  sing N N 329 
PRO   CG  HG3  sing N N 330 
PRO   CD  HD2  sing N N 331 
PRO   CD  HD3  sing N N 332 
PRO   OXT HXT  sing N N 333 
SER   N   CA   sing N N 334 
SER   N   H    sing N N 335 
SER   N   H2   sing N N 336 
SER   CA  C    sing N N 337 
SER   CA  CB   sing N N 338 
SER   CA  HA   sing N N 339 
SER   C   O    doub N N 340 
SER   C   OXT  sing N N 341 
SER   CB  OG   sing N N 342 
SER   CB  HB2  sing N N 343 
SER   CB  HB3  sing N N 344 
SER   OG  HG   sing N N 345 
SER   OXT HXT  sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TRP   N   CA   sing N N 363 
TRP   N   H    sing N N 364 
TRP   N   H2   sing N N 365 
TRP   CA  C    sing N N 366 
TRP   CA  CB   sing N N 367 
TRP   CA  HA   sing N N 368 
TRP   C   O    doub N N 369 
TRP   C   OXT  sing N N 370 
TRP   CB  CG   sing N N 371 
TRP   CB  HB2  sing N N 372 
TRP   CB  HB3  sing N N 373 
TRP   CG  CD1  doub Y N 374 
TRP   CG  CD2  sing Y N 375 
TRP   CD1 NE1  sing Y N 376 
TRP   CD1 HD1  sing N N 377 
TRP   CD2 CE2  doub Y N 378 
TRP   CD2 CE3  sing Y N 379 
TRP   NE1 CE2  sing Y N 380 
TRP   NE1 HE1  sing N N 381 
TRP   CE2 CZ2  sing Y N 382 
TRP   CE3 CZ3  doub Y N 383 
TRP   CE3 HE3  sing N N 384 
TRP   CZ2 CH2  doub Y N 385 
TRP   CZ2 HZ2  sing N N 386 
TRP   CZ3 CH2  sing Y N 387 
TRP   CZ3 HZ3  sing N N 388 
TRP   CH2 HH2  sing N N 389 
TRP   OXT HXT  sing N N 390 
TYR   N   CA   sing N N 391 
TYR   N   H    sing N N 392 
TYR   N   H2   sing N N 393 
TYR   CA  C    sing N N 394 
TYR   CA  CB   sing N N 395 
TYR   CA  HA   sing N N 396 
TYR   C   O    doub N N 397 
TYR   C   OXT  sing N N 398 
TYR   CB  CG   sing N N 399 
TYR   CB  HB2  sing N N 400 
TYR   CB  HB3  sing N N 401 
TYR   CG  CD1  doub Y N 402 
TYR   CG  CD2  sing Y N 403 
TYR   CD1 CE1  sing Y N 404 
TYR   CD1 HD1  sing N N 405 
TYR   CD2 CE2  doub Y N 406 
TYR   CD2 HD2  sing N N 407 
TYR   CE1 CZ   doub Y N 408 
TYR   CE1 HE1  sing N N 409 
TYR   CE2 CZ   sing Y N 410 
TYR   CE2 HE2  sing N N 411 
TYR   CZ  OH   sing N N 412 
TYR   OH  HH   sing N N 413 
TYR   OXT HXT  sing N N 414 
VAL   N   CA   sing N N 415 
VAL   N   H    sing N N 416 
VAL   N   H2   sing N N 417 
VAL   CA  C    sing N N 418 
VAL   CA  CB   sing N N 419 
VAL   CA  HA   sing N N 420 
VAL   C   O    doub N N 421 
VAL   C   OXT  sing N N 422 
VAL   CB  CG1  sing N N 423 
VAL   CB  CG2  sing N N 424 
VAL   CB  HB   sing N N 425 
VAL   CG1 HG11 sing N N 426 
VAL   CG1 HG12 sing N N 427 
VAL   CG1 HG13 sing N N 428 
VAL   CG2 HG21 sing N N 429 
VAL   CG2 HG22 sing N N 430 
VAL   CG2 HG23 sing N N 431 
VAL   OXT HXT  sing N N 432 
# 
_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                    9M3O 
_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]   0.010113 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010113 
_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]   0.009063 
_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 
F 
K 
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   . GLY   A 1 1   ? 15.395  56.382 -11.792 1.00 73.73  ? 41  GLY   A N   1 
ATOM   2    C CA  . GLY   A 1 1   ? 13.981  56.419 -12.123 1.00 76.86  ? 41  GLY   A CA  1 
ATOM   3    C C   . GLY   A 1 1   ? 13.243  55.176 -11.662 1.00 79.22  ? 41  GLY   A C   1 
ATOM   4    O O   . GLY   A 1 1   ? 13.016  54.987 -10.466 1.00 79.85  ? 41  GLY   A O   1 
ATOM   5    N N   . VAL   A 1 2   ? 12.864  54.327 -12.612 1.00 80.38  ? 42  VAL   A N   1 
ATOM   6    C CA  . VAL   A 1 2   ? 12.237  53.043 -12.299 1.00 76.66  ? 42  VAL   A CA  1 
ATOM   7    C C   . VAL   A 1 2   ? 13.228  52.132 -11.578 1.00 70.43  ? 42  VAL   A C   1 
ATOM   8    O O   . VAL   A 1 2   ? 12.848  51.500 -10.582 1.00 66.12  ? 42  VAL   A O   1 
ATOM   9    C CB  . VAL   A 1 2   ? 11.674  52.367 -13.560 1.00 76.03  ? 42  VAL   A CB  1 
ATOM   10   C CG1 . VAL   A 1 2   ? 11.277  50.926 -13.260 1.00 70.63  ? 42  VAL   A CG1 1 
ATOM   11   C CG2 . VAL   A 1 2   ? 10.492  53.156 -14.094 1.00 76.72  ? 42  VAL   A CG2 1 
ATOM   12   N N   . PRO   A 1 3   ? 14.486  52.012 -12.027 1.00 71.02  ? 43  PRO   A N   1 
ATOM   13   C CA  . PRO   A 1 3   ? 15.461  51.253 -11.222 1.00 73.78  ? 43  PRO   A CA  1 
ATOM   14   C C   . PRO   A 1 3   ? 15.626  51.776 -9.801  1.00 68.08  ? 43  PRO   A C   1 
ATOM   15   O O   . PRO   A 1 3   ? 15.904  50.983 -8.890  1.00 59.94  ? 43  PRO   A O   1 
ATOM   16   C CB  . PRO   A 1 3   ? 16.760  51.391 -12.028 1.00 79.43  ? 43  PRO   A CB  1 
ATOM   17   C CG  . PRO   A 1 3   ? 16.300  51.538 -13.427 1.00 79.72  ? 43  PRO   A CG  1 
ATOM   18   C CD  . PRO   A 1 3   ? 15.048  52.365 -13.347 1.00 75.46  ? 43  PRO   A CD  1 
ATOM   19   N N   . GLY   A 1 4   ? 15.463  53.083 -9.581  1.00 64.59  ? 44  GLY   A N   1 
ATOM   20   C CA  . GLY   A 1 4   ? 15.546  53.607 -8.227  1.00 56.73  ? 44  GLY   A CA  1 
ATOM   21   C C   . GLY   A 1 4   ? 14.386  53.160 -7.358  1.00 52.95  ? 44  GLY   A C   1 
ATOM   22   O O   . GLY   A 1 4   ? 14.570  52.833 -6.181  1.00 51.23  ? 44  GLY   A O   1 
ATOM   23   N N   . GLN   A 1 5   ? 13.177  53.140 -7.923  1.00 53.54  ? 45  GLN   A N   1 
ATOM   24   C CA  . GLN   A 1 5   ? 12.012  52.676 -7.178  1.00 55.33  ? 45  GLN   A CA  1 
ATOM   25   C C   . GLN   A 1 5   ? 12.142  51.201 -6.818  1.00 50.64  ? 45  GLN   A C   1 
ATOM   26   O O   . GLN   A 1 5   ? 11.886  50.807 -5.675  1.00 47.61  ? 45  GLN   A O   1 
ATOM   27   C CB  . GLN   A 1 5   ? 10.739  52.930 -7.988  1.00 63.21  ? 45  GLN   A CB  1 
ATOM   28   C CG  . GLN   A 1 5   ? 10.284  54.381 -7.973  1.00 74.59  ? 45  GLN   A CG  1 
ATOM   29   C CD  . GLN   A 1 5   ? 9.297   54.698 -9.077  1.00 82.34  ? 45  GLN   A CD  1 
ATOM   30   O OE1 . GLN   A 1 5   ? 9.458   54.256 -10.216 1.00 84.82  ? 45  GLN   A OE1 1 
ATOM   31   N NE2 . GLN   A 1 5   ? 8.264   55.466 -8.746  1.00 84.06  ? 45  GLN   A NE2 1 
ATOM   32   N N   . VAL   A 1 6   ? 12.545  50.371 -7.784  1.00 45.40  ? 46  VAL   A N   1 
ATOM   33   C CA  . VAL   A 1 6   ? 12.729  48.946 -7.521  1.00 42.90  ? 46  VAL   A CA  1 
ATOM   34   C C   . VAL   A 1 6   ? 13.765  48.732 -6.426  1.00 43.54  ? 46  VAL   A C   1 
ATOM   35   O O   . VAL   A 1 6   ? 13.572  47.905 -5.528  1.00 40.99  ? 46  VAL   A O   1 
ATOM   36   C CB  . VAL   A 1 6   ? 13.119  48.205 -8.814  1.00 44.71  ? 46  VAL   A CB  1 
ATOM   37   C CG1 . VAL   A 1 6   ? 13.451  46.772 -8.505  1.00 45.38  ? 46  VAL   A CG1 1 
ATOM   38   C CG2 . VAL   A 1 6   ? 11.992  48.262 -9.816  1.00 44.16  ? 46  VAL   A CG2 1 
ATOM   39   N N   . ASP   A 1 7   ? 14.876  49.475 -6.475  1.00 42.75  ? 47  ASP   A N   1 
ATOM   40   C CA  . ASP   A 1 7   ? 15.932  49.291 -5.483  1.00 46.64  ? 47  ASP   A CA  1 
ATOM   41   C C   . ASP   A 1 7   ? 15.467  49.683 -4.087  1.00 43.30  ? 47  ASP   A C   1 
ATOM   42   O O   . ASP   A 1 7   ? 15.832  49.030 -3.105  1.00 43.47  ? 47  ASP   A O   1 
ATOM   43   C CB  . ASP   A 1 7   ? 17.169  50.095 -5.870  1.00 54.71  ? 47  ASP   A CB  1 
ATOM   44   C CG  . ASP   A 1 7   ? 17.878  49.519 -7.072  1.00 71.83  ? 47  ASP   A CG  1 
ATOM   45   O OD1 . ASP   A 1 7   ? 17.776  48.291 -7.289  1.00 77.00  ? 47  ASP   A OD1 1 
ATOM   46   O OD2 . ASP   A 1 7   ? 18.533  50.292 -7.803  1.00 77.86  ? 47  ASP   A OD2 1 
ATOM   47   N N   . PHE   A 1 8   ? 14.666  50.745 -3.977  1.00 39.06  ? 48  PHE   A N   1 
ATOM   48   C CA  . PHE   A 1 8   ? 14.178  51.160 -2.667  1.00 44.12  ? 48  PHE   A CA  1 
ATOM   49   C C   . PHE   A 1 8   ? 13.362  50.053 -2.011  1.00 43.37  ? 48  PHE   A C   1 
ATOM   50   O O   . PHE   A 1 8   ? 13.594  49.699 -0.849  1.00 37.67  ? 48  PHE   A O   1 
ATOM   51   C CB  . PHE   A 1 8   ? 13.347  52.436 -2.795  1.00 41.50  ? 48  PHE   A CB  1 
ATOM   52   C CG  . PHE   A 1 8   ? 12.825  52.957 -1.481  1.00 48.38  ? 48  PHE   A CG  1 
ATOM   53   C CD1 . PHE   A 1 8   ? 13.591  53.817 -0.706  1.00 51.85  ? 48  PHE   A CD1 1 
ATOM   54   C CD2 . PHE   A 1 8   ? 11.563  52.601 -1.026  1.00 47.19  ? 48  PHE   A CD2 1 
ATOM   55   C CE1 . PHE   A 1 8   ? 13.112  54.307 0.497   1.00 49.11  ? 48  PHE   A CE1 1 
ATOM   56   C CE2 . PHE   A 1 8   ? 11.085  53.085 0.181   1.00 44.91  ? 48  PHE   A CE2 1 
ATOM   57   C CZ  . PHE   A 1 8   ? 11.861  53.941 0.940   1.00 45.41  ? 48  PHE   A CZ  1 
ATOM   58   N N   . TYR   A 1 9   ? 12.410  49.479 -2.745  1.00 42.32  ? 49  TYR   A N   1 
ATOM   59   C CA  . TYR   A 1 9   ? 11.514  48.508 -2.129  1.00 37.99  ? 49  TYR   A CA  1 
ATOM   60   C C   . TYR   A 1 9   ? 12.125  47.118 -2.058  1.00 34.49  ? 49  TYR   A C   1 
ATOM   61   O O   . TYR   A 1 9   ? 11.768  46.336 -1.167  1.00 37.72  ? 49  TYR   A O   1 
ATOM   62   C CB  . TYR   A 1 9   ? 10.177  48.497 -2.869  1.00 37.86  ? 49  TYR   A CB  1 
ATOM   63   C CG  . TYR   A 1 9   ? 9.416   49.759 -2.564  1.00 45.99  ? 49  TYR   A CG  1 
ATOM   64   C CD1 . TYR   A 1 9   ? 8.761   49.913 -1.347  1.00 46.36  ? 49  TYR   A CD1 1 
ATOM   65   C CD2 . TYR   A 1 9   ? 9.412   50.827 -3.451  1.00 49.23  ? 49  TYR   A CD2 1 
ATOM   66   C CE1 . TYR   A 1 9   ? 8.093   51.079 -1.039  1.00 48.06  ? 49  TYR   A CE1 1 
ATOM   67   C CE2 . TYR   A 1 9   ? 8.750   52.002 -3.148  1.00 46.82  ? 49  TYR   A CE2 1 
ATOM   68   C CZ  . TYR   A 1 9   ? 8.087   52.118 -1.942  1.00 51.26  ? 49  TYR   A CZ  1 
ATOM   69   O OH  . TYR   A 1 9   ? 7.422   53.279 -1.627  1.00 61.23  ? 49  TYR   A OH  1 
ATOM   70   N N   . ALA   A 1 10  ? 13.065  46.797 -2.950  1.00 34.17  ? 50  ALA   A N   1 
ATOM   71   C CA  . ALA   A 1 10  ? 13.733  45.504 -2.861  1.00 33.64  ? 50  ALA   A CA  1 
ATOM   72   C C   . ALA   A 1 10  ? 14.671  45.428 -1.668  1.00 36.49  ? 50  ALA   A C   1 
ATOM   73   O O   . ALA   A 1 10  ? 15.098  44.327 -1.301  1.00 37.00  ? 50  ALA   A O   1 
ATOM   74   C CB  . ALA   A 1 10  ? 14.511  45.210 -4.140  1.00 34.11  ? 50  ALA   A CB  1 
ATOM   75   N N   . ARG   A 1 11  ? 15.019  46.568 -1.067  1.00 37.77  ? 51  ARG   A N   1 
ATOM   76   C CA  . ARG   A 1 11  ? 15.800  46.524 0.160   1.00 36.69  ? 51  ARG   A CA  1 
ATOM   77   C C   . ARG   A 1 11  ? 15.021  45.841 1.274   1.00 37.69  ? 51  ARG   A C   1 
ATOM   78   O O   . ARG   A 1 11  ? 15.612  45.176 2.127   1.00 40.31  ? 51  ARG   A O   1 
ATOM   79   C CB  . ARG   A 1 11  ? 16.214  47.935 0.579   1.00 38.35  ? 51  ARG   A CB  1 
ATOM   80   C CG  . ARG   A 1 11  ? 17.202  47.965 1.731   1.00 49.64  ? 51  ARG   A CG  1 
ATOM   81   C CD  . ARG   A 1 11  ? 17.529  49.390 2.200   1.00 58.49  ? 51  ARG   A CD  1 
ATOM   82   N NE  . ARG   A 1 11  ? 16.420  50.032 2.910   1.00 57.85  ? 51  ARG   A NE  1 
ATOM   83   C CZ  . ARG   A 1 11  ? 16.107  49.800 4.184   1.00 54.83  ? 51  ARG   A CZ  1 
ATOM   84   N NH1 . ARG   A 1 11  ? 15.085  50.435 4.742   1.00 46.17  ? 51  ARG   A NH1 1 
ATOM   85   N NH2 . ARG   A 1 11  ? 16.807  48.926 4.901   1.00 55.76  ? 51  ARG   A NH2 1 
ATOM   86   N N   . PHE   A 1 12  ? 13.700  45.971 1.274   1.00 35.22  ? 52  PHE   A N   1 
ATOM   87   C CA  . PHE   A 1 12  ? 12.914  45.408 2.358   1.00 35.56  ? 52  PHE   A CA  1 
ATOM   88   C C   . PHE   A 1 12  ? 12.694  43.915 2.167   1.00 35.95  ? 52  PHE   A C   1 
ATOM   89   O O   . PHE   A 1 12  ? 12.795  43.374 1.065   1.00 32.71  ? 52  PHE   A O   1 
ATOM   90   C CB  . PHE   A 1 12  ? 11.575  46.121 2.472   1.00 34.44  ? 52  PHE   A CB  1 
ATOM   91   C CG  . PHE   A 1 12  ? 11.714  47.544 2.864   1.00 36.08  ? 52  PHE   A CG  1 
ATOM   92   C CD1 . PHE   A 1 12  ? 11.936  47.883 4.185   1.00 37.43  ? 52  PHE   A CD1 1 
ATOM   93   C CD2 . PHE   A 1 12  ? 11.673  48.544 1.910   1.00 39.51  ? 52  PHE   A CD2 1 
ATOM   94   C CE1 . PHE   A 1 12  ? 12.090  49.194 4.556   1.00 44.91  ? 52  PHE   A CE1 1 
ATOM   95   C CE2 . PHE   A 1 12  ? 11.824  49.869 2.279   1.00 39.84  ? 52  PHE   A CE2 1 
ATOM   96   C CZ  . PHE   A 1 12  ? 12.033  50.190 3.599   1.00 43.86  ? 52  PHE   A CZ  1 
ATOM   97   N N   . SER   A 1 13  ? 12.409  43.246 3.273   1.00 37.96  ? 53  SER   A N   1 
ATOM   98   C CA  . SER   A 1 13  ? 12.049  41.846 3.122   1.00 38.65  ? 53  SER   A CA  1 
ATOM   99   C C   . SER   A 1 13  ? 10.532  41.705 3.038   1.00 36.95  ? 53  SER   A C   1 
ATOM   100  O O   . SER   A 1 13  ? 9.805   42.445 3.711   1.00 39.11  ? 53  SER   A O   1 
ATOM   101  C CB  . SER   A 1 13  ? 12.569  41.028 4.299   1.00 45.75  ? 53  SER   A CB  1 
ATOM   102  O OG  . SER   A 1 13  ? 12.053  39.709 4.245   1.00 54.37  ? 53  SER   A OG  1 
ATOM   103  N N   . PRO   A 1 14  ? 10.023  40.784 2.221   1.00 37.51  ? 54  PRO   A N   1 
ATOM   104  C CA  . PRO   A 1 14  ? 8.601   40.436 2.311   1.00 39.87  ? 54  PRO   A CA  1 
ATOM   105  C C   . PRO   A 1 14  ? 8.242   40.041 3.737   1.00 41.47  ? 54  PRO   A C   1 
ATOM   106  O O   . PRO   A 1 14  ? 9.074   39.525 4.488   1.00 42.43  ? 54  PRO   A O   1 
ATOM   107  C CB  . PRO   A 1 14  ? 8.462   39.257 1.342   1.00 36.13  ? 54  PRO   A CB  1 
ATOM   108  C CG  . PRO   A 1 14  ? 9.559   39.471 0.340   1.00 37.43  ? 54  PRO   A CG  1 
ATOM   109  C CD  . PRO   A 1 14  ? 10.702  40.073 1.125   1.00 34.69  ? 54  PRO   A CD  1 
ATOM   110  N N   . SER   A 1 15  ? 7.000   40.322 4.123   1.00 37.89  ? 55  SER   A N   1 
ATOM   111  C CA  A SER   A 1 15  ? 6.509   40.005 5.461   0.40 38.84  ? 55  SER   A CA  1 
ATOM   112  C CA  B SER   A 1 15  ? 6.515   39.996 5.460   0.60 38.62  ? 55  SER   A CA  1 
ATOM   113  C C   . SER   A 1 15  ? 5.517   38.850 5.372   1.00 41.30  ? 55  SER   A C   1 
ATOM   114  O O   . SER   A 1 15  ? 4.364   39.058 4.961   1.00 41.91  ? 55  SER   A O   1 
ATOM   115  C CB  A SER   A 1 15  ? 5.852   41.237 6.093   0.40 39.75  ? 55  SER   A CB  1 
ATOM   116  C CB  B SER   A 1 15  ? 5.878   41.224 6.113   0.60 39.99  ? 55  SER   A CB  1 
ATOM   117  O OG  A SER   A 1 15  ? 5.397   40.975 7.410   0.40 37.90  ? 55  SER   A OG  1 
ATOM   118  O OG  B SER   A 1 15  ? 6.848   42.234 6.322   0.60 40.00  ? 55  SER   A OG  1 
ATOM   119  N N   . PRO   A 1 16  ? 5.903   37.625 5.737   1.00 38.05  ? 56  PRO   A N   1 
ATOM   120  C CA  . PRO   A 1 16  ? 4.983   36.494 5.596   1.00 38.33  ? 56  PRO   A CA  1 
ATOM   121  C C   . PRO   A 1 16  ? 3.831   36.598 6.575   1.00 41.58  ? 56  PRO   A C   1 
ATOM   122  O O   . PRO   A 1 16  ? 3.987   37.063 7.704   1.00 40.69  ? 56  PRO   A O   1 
ATOM   123  C CB  . PRO   A 1 16  ? 5.852   35.273 5.919   1.00 38.41  ? 56  PRO   A CB  1 
ATOM   124  C CG  . PRO   A 1 16  ? 7.238   35.788 6.140   1.00 41.95  ? 56  PRO   A CG  1 
ATOM   125  C CD  . PRO   A 1 16  ? 7.133   37.240 6.445   1.00 37.55  ? 56  PRO   A CD  1 
ATOM   126  N N   . LEU   A 1 17  ? 2.667   36.140 6.134   1.00 39.24  ? 57  LEU   A N   1 
ATOM   127  C CA  . LEU   A 1 17  ? 1.486   36.072 6.977   1.00 40.14  ? 57  LEU   A CA  1 
ATOM   128  C C   . LEU   A 1 17  ? 1.144   34.618 7.262   1.00 42.28  ? 57  LEU   A C   1 
ATOM   129  O O   . LEU   A 1 17  ? 1.397   33.734 6.444   1.00 41.79  ? 57  LEU   A O   1 
ATOM   130  C CB  . LEU   A 1 17  ? 0.289   36.757 6.310   1.00 42.95  ? 57  LEU   A CB  1 
ATOM   131  C CG  . LEU   A 1 17  ? 0.416   38.253 6.024   1.00 47.29  ? 57  LEU   A CG  1 
ATOM   132  C CD1 . LEU   A 1 17  ? -0.782  38.743 5.225   1.00 53.39  ? 57  LEU   A CD1 1 
ATOM   133  C CD2 . LEU   A 1 17  ? 0.534   39.027 7.324   1.00 45.14  ? 57  LEU   A CD2 1 
ATOM   134  N N   . SER   A 1 18  ? 0.563   34.371 8.428   1.00 41.20  ? 58  SER   A N   1 
ATOM   135  C CA  . SER   A 1 18  ? 0.026   33.043 8.668   1.00 42.57  ? 58  SER   A CA  1 
ATOM   136  C C   . SER   A 1 18  ? -1.379  32.932 8.089   1.00 45.87  ? 58  SER   A C   1 
ATOM   137  O O   . SER   A 1 18  ? -2.063  33.931 7.844   1.00 44.05  ? 58  SER   A O   1 
ATOM   138  C CB  . SER   A 1 18  ? -0.023  32.734 10.157  1.00 42.09  ? 58  SER   A CB  1 
ATOM   139  O OG  . SER   A 1 18  ? -1.048  33.499 10.759  1.00 48.90  ? 58  SER   A OG  1 
ATOM   140  N N   . MET   A 1 19  ? -1.804  31.689 7.867   1.00 49.73  ? 59  MET   A N   1 
ATOM   141  C CA  . MET   A 1 19  ? -3.183  31.441 7.465   1.00 49.05  ? 59  MET   A CA  1 
ATOM   142  C C   . MET   A 1 19  ? -4.155  32.022 8.478   1.00 48.66  ? 59  MET   A C   1 
ATOM   143  O O   . MET   A 1 19  ? -5.206  32.556 8.107   1.00 52.31  ? 59  MET   A O   1 
ATOM   144  C CB  . MET   A 1 19  ? -3.416  29.942 7.307   1.00 53.33  ? 59  MET   A CB  1 
ATOM   145  C CG  . MET   A 1 19  ? -4.794  29.588 6.834   1.00 52.21  ? 59  MET   A CG  1 
ATOM   146  S SD  . MET   A 1 19  ? -4.808  29.348 5.060   1.00 58.22  ? 59  MET   A SD  1 
ATOM   147  C CE  . MET   A 1 19  ? -3.734  27.918 4.907   1.00 52.45  ? 59  MET   A CE  1 
ATOM   148  N N   . LYS   A 1 20  ? -3.817  31.929 9.766   1.00 51.38  ? 60  LYS   A N   1 
ATOM   149  C CA  . LYS   A 1 20  ? -4.671  32.503 10.801  1.00 57.83  ? 60  LYS   A CA  1 
ATOM   150  C C   . LYS   A 1 20  ? -4.799  34.015 10.637  1.00 54.97  ? 60  LYS   A C   1 
ATOM   151  O O   . LYS   A 1 20  ? -5.890  34.573 10.792  1.00 55.11  ? 60  LYS   A O   1 
ATOM   152  C CB  . LYS   A 1 20  ? -4.115  32.157 12.184  1.00 64.89  ? 60  LYS   A CB  1 
ATOM   153  C CG  . LYS   A 1 20  ? -4.891  32.772 13.344  1.00 65.46  ? 60  LYS   A CG  1 
ATOM   154  C CD  . LYS   A 1 20  ? -5.981  31.842 13.839  1.00 71.53  ? 60  LYS   A CD  1 
ATOM   155  C CE  . LYS   A 1 20  ? -6.761  32.469 14.987  1.00 79.09  ? 60  LYS   A CE  1 
ATOM   156  N NZ  . LYS   A 1 20  ? -5.857  33.138 15.970  1.00 77.84  ? 60  LYS   A NZ  1 
ATOM   157  N N   . GLN   A 1 21  ? -3.696  34.695 10.319  1.00 53.11  ? 61  GLN   A N   1 
ATOM   158  C CA  . GLN   A 1 21  ? -3.751  36.139 10.118  1.00 47.43  ? 61  GLN   A CA  1 
ATOM   159  C C   . GLN   A 1 21  ? -4.651  36.497 8.942   1.00 48.69  ? 61  GLN   A C   1 
ATOM   160  O O   . GLN   A 1 21  ? -5.495  37.394 9.044   1.00 53.20  ? 61  GLN   A O   1 
ATOM   161  C CB  . GLN   A 1 21  ? -2.344  36.687 9.902   1.00 48.28  ? 61  GLN   A CB  1 
ATOM   162  C CG  . GLN   A 1 21  ? -1.467  36.628 11.131  1.00 56.72  ? 61  GLN   A CG  1 
ATOM   163  C CD  . GLN   A 1 21  ? -0.057  37.097 10.846  1.00 61.40  ? 61  GLN   A CD  1 
ATOM   164  O OE1 . GLN   A 1 21  ? 0.673   36.472 10.080  1.00 56.71  ? 61  GLN   A OE1 1 
ATOM   165  N NE2 . GLN   A 1 21  ? 0.330   38.211 11.454  1.00 63.20  ? 61  GLN   A NE2 1 
ATOM   166  N N   . PHE   A 1 22  ? -4.462  35.819 7.805   1.00 45.36  ? 62  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 22  ? -5.366  35.968 6.668   1.00 45.95  ? 62  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 22  ? -6.817  35.804 7.100   1.00 52.39  ? 62  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 22  ? -7.685  36.618 6.761   1.00 58.22  ? 62  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 22  ? -5.038  34.923 5.599   1.00 40.09  ? 62  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 22  ? -3.939  35.306 4.652   1.00 41.46  ? 62  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 22  ? -4.101  36.355 3.759   1.00 44.44  ? 62  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 22  ? -2.770  34.560 4.596   1.00 40.40  ? 62  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 22  ? -3.094  36.685 2.863   1.00 41.69  ? 62  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 22  ? -1.759  34.879 3.698   1.00 41.12  ? 62  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 22  ? -1.920  35.942 2.832   1.00 44.00  ? 62  PHE   A CZ  1 
ATOM   177  N N   . LEU   A 1 23  ? -7.088  34.746 7.863   1.00 52.70  ? 63  LEU   A N   1 
ATOM   178  C CA  . LEU   A 1 23  ? -8.452  34.413 8.253   1.00 60.29  ? 63  LEU   A CA  1 
ATOM   179  C C   . LEU   A 1 23  ? -8.994  35.415 9.266   1.00 71.06  ? 63  LEU   A C   1 
ATOM   180  O O   . LEU   A 1 23  ? -10.101 35.942 9.103   1.00 74.04  ? 63  LEU   A O   1 
ATOM   181  C CB  . LEU   A 1 23  ? -8.477  32.991 8.815   1.00 57.77  ? 63  LEU   A CB  1 
ATOM   182  C CG  . LEU   A 1 23  ? -9.791  32.236 8.965   1.00 63.01  ? 63  LEU   A CG  1 
ATOM   183  C CD1 . LEU   A 1 23  ? -10.409 31.993 7.611   1.00 62.50  ? 63  LEU   A CD1 1 
ATOM   184  C CD2 . LEU   A 1 23  ? -9.528  30.920 9.674   1.00 66.40  ? 63  LEU   A CD2 1 
ATOM   185  N N   . ASP   A 1 24  ? -8.222  35.692 10.323  1.00 74.94  ? 64  ASP   A N   1 
ATOM   186  C CA  . ASP   A 1 24  ? -8.677  36.618 11.356  1.00 78.08  ? 64  ASP   A CA  1 
ATOM   187  C C   . ASP   A 1 24  ? -8.976  37.993 10.787  1.00 83.27  ? 64  ASP   A C   1 
ATOM   188  O O   . ASP   A 1 24  ? -9.862  38.692 11.290  1.00 93.79  ? 64  ASP   A O   1 
ATOM   189  C CB  . ASP   A 1 24  ? -7.635  36.732 12.469  1.00 77.48  ? 64  ASP   A CB  1 
ATOM   190  C CG  . ASP   A 1 24  ? -7.646  35.537 13.405  1.00 82.22  ? 64  ASP   A CG  1 
ATOM   191  O OD1 . ASP   A 1 24  ? -8.446  34.599 13.174  1.00 82.21  ? 64  ASP   A OD1 1 
ATOM   192  O OD2 . ASP   A 1 24  ? -6.857  35.540 14.376  1.00 83.34  ? 64  ASP   A OD2 1 
ATOM   193  N N   . PHE   A 1 25  ? -8.262  38.397 9.739   1.00 83.48  ? 65  PHE   A N   1 
ATOM   194  C CA  . PHE   A 1 25  ? -8.483  39.719 9.170   1.00 91.69  ? 65  PHE   A CA  1 
ATOM   195  C C   . PHE   A 1 25  ? -9.878  39.833 8.566   1.00 100.74 ? 65  PHE   A C   1 
ATOM   196  O O   . PHE   A 1 25  ? -10.701 40.641 9.014   1.00 109.22 ? 65  PHE   A O   1 
ATOM   197  C CB  . PHE   A 1 25  ? -7.416  40.028 8.125   1.00 92.27  ? 65  PHE   A CB  1 
ATOM   198  C CG  . PHE   A 1 25  ? -7.628  41.335 7.437   1.00 103.77 ? 65  PHE   A CG  1 
ATOM   199  C CD1 . PHE   A 1 25  ? -7.587  42.521 8.155   1.00 113.67 ? 65  PHE   A CD1 1 
ATOM   200  C CD2 . PHE   A 1 25  ? -7.887  41.384 6.081   1.00 106.32 ? 65  PHE   A CD2 1 
ATOM   201  C CE1 . PHE   A 1 25  ? -7.794  43.735 7.529   1.00 115.81 ? 65  PHE   A CE1 1 
ATOM   202  C CE2 . PHE   A 1 25  ? -8.093  42.595 5.448   1.00 111.44 ? 65  PHE   A CE2 1 
ATOM   203  C CZ  . PHE   A 1 25  ? -8.047  43.772 6.174   1.00 114.14 ? 65  PHE   A CZ  1 
ATOM   204  N N   . GLY   A 1 26  ? -10.167 39.023 7.550   1.00 97.34  ? 66  GLY   A N   1 
ATOM   205  C CA  . GLY   A 1 26  ? -11.416 39.138 6.823   1.00 98.95  ? 66  GLY   A CA  1 
ATOM   206  C C   . GLY   A 1 26  ? -12.650 38.560 7.480   1.00 102.56 ? 66  GLY   A C   1 
ATOM   207  O O   . GLY   A 1 26  ? -13.722 38.577 6.869   1.00 103.20 ? 66  GLY   A O   1 
ATOM   208  N N   . SER   A 1 27  ? -12.552 38.056 8.711   1.00 106.82 ? 67  SER   A N   1 
ATOM   209  C CA  . SER   A 1 27  ? -13.700 37.401 9.329   1.00 113.53 ? 67  SER   A CA  1 
ATOM   210  C C   . SER   A 1 27  ? -14.665 38.411 9.945   1.00 126.09 ? 67  SER   A C   1 
ATOM   211  O O   . SER   A 1 27  ? -15.814 38.534 9.507   1.00 128.35 ? 67  SER   A O   1 
ATOM   212  C CB  . SER   A 1 27  ? -13.228 36.393 10.380  1.00 108.60 ? 67  SER   A CB  1 
ATOM   213  O OG  . SER   A 1 27  ? -12.692 35.235 9.764   1.00 101.88 ? 67  SER   A OG  1 
ATOM   214  N N   . VAL   A 1 28  ? -14.217 39.141 10.965  1.00 133.60 ? 68  VAL   A N   1 
ATOM   215  C CA  . VAL   A 1 28  ? -15.102 40.036 11.704  1.00 145.53 ? 68  VAL   A CA  1 
ATOM   216  C C   . VAL   A 1 28  ? -14.829 41.482 11.318  1.00 153.00 ? 68  VAL   A C   1 
ATOM   217  O O   . VAL   A 1 28  ? -15.674 42.141 10.698  1.00 149.67 ? 68  VAL   A O   1 
ATOM   218  C CB  . VAL   A 1 28  ? -14.949 39.842 13.224  1.00 144.86 ? 68  VAL   A CB  1 
ATOM   219  C CG1 . VAL   A 1 28  ? -15.848 40.817 13.976  1.00 146.48 ? 68  VAL   A CG1 1 
ATOM   220  C CG2 . VAL   A 1 28  ? -15.262 38.403 13.610  1.00 143.19 ? 68  VAL   A CG2 1 
ATOM   221  N N   . ASN   A 1 29  ? -13.650 41.984 11.696  1.00 162.19 ? 69  ASN   A N   1 
ATOM   222  C CA  . ASN   A 1 29  ? -13.294 43.374 11.435  1.00 165.99 ? 69  ASN   A CA  1 
ATOM   223  C C   . ASN   A 1 29  ? -13.442 43.710 9.958   1.00 161.97 ? 69  ASN   A C   1 
ATOM   224  O O   . ASN   A 1 29  ? -14.286 44.528 9.573   1.00 165.53 ? 69  ASN   A O   1 
ATOM   225  C CB  . ASN   A 1 29  ? -11.864 43.645 11.911  1.00 167.89 ? 69  ASN   A CB  1 
ATOM   226  C CG  . ASN   A 1 29  ? -11.714 43.508 13.413  1.00 171.61 ? 69  ASN   A CG  1 
ATOM   227  O OD1 . ASN   A 1 29  ? -12.495 42.816 14.066  1.00 174.16 ? 69  ASN   A OD1 1 
ATOM   228  N ND2 . ASN   A 1 29  ? -10.709 44.172 13.971  1.00 171.64 ? 69  ASN   A ND2 1 
ATOM   229  N N   . ALA   A 1 30  ? -12.635 43.064 9.116   1.00 152.04 ? 70  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30  ? -12.652 43.276 7.673   1.00 140.85 ? 70  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30  ? -12.524 44.764 7.351   1.00 129.95 ? 70  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30  ? -13.374 45.370 6.696   1.00 136.09 ? 70  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30  ? -13.915 42.676 7.047   1.00 144.42 ? 70  ALA   A CB  1 
ATOM   234  N N   . CYS   A 1 31  ? -11.442 45.356 7.851   1.00 106.24 ? 71  CYS   A N   1 
ATOM   235  C CA  . CYS   A 1 31  ? -11.209 46.786 7.700   1.00 89.15  ? 71  CYS   A CA  1 
ATOM   236  C C   . CYS   A 1 31  ? -10.442 47.034 6.407   1.00 74.46  ? 71  CYS   A C   1 
ATOM   237  O O   . CYS   A 1 31  ? -9.275  46.645 6.283   1.00 66.97  ? 71  CYS   A O   1 
ATOM   238  C CB  . CYS   A 1 31  ? -10.449 47.346 8.896   1.00 89.36  ? 71  CYS   A CB  1 
ATOM   239  S SG  . CYS   A 1 31  ? -10.330 49.146 8.852   1.00 95.74  ? 71  CYS   A SG  1 
ATOM   240  N N   . GLU   A 1 32  ? -11.098 47.690 5.447   1.00 70.15  ? 72  GLU   A N   1 
ATOM   241  C CA  . GLU   A 1 32  ? -10.444 48.007 4.183   1.00 63.81  ? 72  GLU   A CA  1 
ATOM   242  C C   . GLU   A 1 32  ? -9.290  48.982 4.382   1.00 66.46  ? 72  GLU   A C   1 
ATOM   243  O O   . GLU   A 1 32  ? -8.303  48.923 3.639   1.00 64.14  ? 72  GLU   A O   1 
ATOM   244  C CB  . GLU   A 1 32  ? -11.468 48.573 3.197   1.00 61.36  ? 72  GLU   A CB  1 
ATOM   245  C CG  . GLU   A 1 32  ? -10.966 48.709 1.768   1.00 62.02  ? 72  GLU   A CG  1 
ATOM   246  C CD  . GLU   A 1 32  ? -12.014 49.304 0.833   1.00 68.03  ? 72  GLU   A CD  1 
ATOM   247  O OE1 . GLU   A 1 32  ? -13.116 49.643 1.308   1.00 71.89  ? 72  GLU   A OE1 1 
ATOM   248  O OE2 . GLU   A 1 32  ? -11.736 49.428 -0.379  1.00 68.75  ? 72  GLU   A OE2 1 
ATOM   249  N N   . LYS   A 1 33  ? -9.392  49.879 5.371   1.00 62.67  ? 73  LYS   A N   1 
ATOM   250  C CA  . LYS   A 1 33  ? -8.278  50.773 5.684   1.00 63.69  ? 73  LYS   A CA  1 
ATOM   251  C C   . LYS   A 1 33  ? -7.052  49.980 6.120   1.00 65.13  ? 73  LYS   A C   1 
ATOM   252  O O   . LYS   A 1 33  ? -5.933  50.245 5.668   1.00 63.38  ? 73  LYS   A O   1 
ATOM   253  C CB  . LYS   A 1 33  ? -8.676  51.770 6.780   1.00 63.03  ? 73  LYS   A CB  1 
ATOM   254  C CG  . LYS   A 1 33  ? -9.693  52.830 6.385   1.00 71.89  ? 73  LYS   A CG  1 
ATOM   255  C CD  . LYS   A 1 33  ? -9.878  53.840 7.522   1.00 79.80  ? 73  LYS   A CD  1 
ATOM   256  C CE  . LYS   A 1 33  ? -11.209 54.599 7.437   1.00 92.74  ? 73  LYS   A CE  1 
ATOM   257  N NZ  . LYS   A 1 33  ? -11.217 55.722 6.452   1.00 97.36  ? 73  LYS   A NZ  1 
ATOM   258  N N   . THR   A 1 34  ? -7.252  48.998 7.005   1.00 65.88  ? 74  THR   A N   1 
ATOM   259  C CA  . THR   A 1 34  ? -6.149  48.164 7.474   1.00 63.93  ? 74  THR   A CA  1 
ATOM   260  C C   . THR   A 1 34  ? -5.478  47.429 6.323   1.00 62.18  ? 74  THR   A C   1 
ATOM   261  O O   . THR   A 1 34  ? -4.243  47.357 6.256   1.00 56.50  ? 74  THR   A O   1 
ATOM   262  C CB  . THR   A 1 34  ? -6.659  47.163 8.513   1.00 64.92  ? 74  THR   A CB  1 
ATOM   263  O OG1 . THR   A 1 34  ? -7.294  47.870 9.583   1.00 71.63  ? 74  THR   A OG1 1 
ATOM   264  C CG2 . THR   A 1 34  ? -5.514  46.337 9.072   1.00 60.89  ? 74  THR   A CG2 1 
ATOM   265  N N   . SER   A 1 35  ? -6.274  46.860 5.413   1.00 58.68  ? 75  SER   A N   1 
ATOM   266  C CA  . SER   A 1 35  ? -5.698  46.168 4.265   1.00 54.21  ? 75  SER   A CA  1 
ATOM   267  C C   . SER   A 1 35  ? -4.890  47.126 3.401   1.00 50.76  ? 75  SER   A C   1 
ATOM   268  O O   . SER   A 1 35  ? -3.796  46.785 2.934   1.00 46.11  ? 75  SER   A O   1 
ATOM   269  C CB  . SER   A 1 35  ? -6.805  45.509 3.446   1.00 58.96  ? 75  SER   A CB  1 
ATOM   270  O OG  . SER   A 1 35  ? -6.264  44.715 2.406   1.00 56.98  ? 75  SER   A OG  1 
ATOM   271  N N   . PHE   A 1 36  ? -5.421  48.332 3.183   1.00 54.41  ? 76  PHE   A N   1 
ATOM   272  C CA  . PHE   A 1 36  ? -4.711  49.380 2.458   1.00 53.46  ? 76  PHE   A CA  1 
ATOM   273  C C   . PHE   A 1 36  ? -3.337  49.647 3.067   1.00 52.60  ? 76  PHE   A C   1 
ATOM   274  O O   . PHE   A 1 36  ? -2.313  49.571 2.379   1.00 53.82  ? 76  PHE   A O   1 
ATOM   275  C CB  . PHE   A 1 36  ? -5.566  50.651 2.454   1.00 55.37  ? 76  PHE   A CB  1 
ATOM   276  C CG  . PHE   A 1 36  ? -4.864  51.866 1.908   1.00 59.75  ? 76  PHE   A CG  1 
ATOM   277  C CD1 . PHE   A 1 36  ? -4.526  51.948 0.565   1.00 59.52  ? 76  PHE   A CD1 1 
ATOM   278  C CD2 . PHE   A 1 36  ? -4.566  52.937 2.735   1.00 63.08  ? 76  PHE   A CD2 1 
ATOM   279  C CE1 . PHE   A 1 36  ? -3.887  53.068 0.062   1.00 63.48  ? 76  PHE   A CE1 1 
ATOM   280  C CE2 . PHE   A 1 36  ? -3.932  54.066 2.236   1.00 68.86  ? 76  PHE   A CE2 1 
ATOM   281  C CZ  . PHE   A 1 36  ? -3.591  54.129 0.899   1.00 67.65  ? 76  PHE   A CZ  1 
ATOM   282  N N   . MET   A 1 37  ? -3.304  49.958 4.368   1.00 53.82  ? 77  MET   A N   1 
ATOM   283  C CA  . MET   A 1 37  ? -2.050  50.290 5.039   1.00 54.21  ? 77  MET   A CA  1 
ATOM   284  C C   . MET   A 1 37  ? -1.015  49.195 4.855   1.00 51.84  ? 77  MET   A C   1 
ATOM   285  O O   . MET   A 1 37  ? 0.169   49.475 4.637   1.00 56.32  ? 77  MET   A O   1 
ATOM   286  C CB  . MET   A 1 37  ? -2.296  50.523 6.530   1.00 62.86  ? 77  MET   A CB  1 
ATOM   287  C CG  . MET   A 1 37  ? -3.035  51.807 6.873   1.00 77.05  ? 77  MET   A CG  1 
ATOM   288  S SD  . MET   A 1 37  ? -1.947  53.243 6.916   1.00 87.07  ? 77  MET   A SD  1 
ATOM   289  C CE  . MET   A 1 37  ? -2.095  53.855 5.242   1.00 84.60  ? 77  MET   A CE  1 
ATOM   290  N N   . PHE   A 1 38  ? -1.445  47.939 4.944   1.00 47.33  ? 78  PHE   A N   1 
ATOM   291  C CA  . PHE   A 1 38  ? -0.518  46.831 4.773   1.00 46.88  ? 78  PHE   A CA  1 
ATOM   292  C C   . PHE   A 1 38  ? -0.083  46.699 3.319   1.00 47.05  ? 78  PHE   A C   1 
ATOM   293  O O   . PHE   A 1 38  ? 1.113   46.604 3.022   1.00 48.19  ? 78  PHE   A O   1 
ATOM   294  C CB  . PHE   A 1 38  ? -1.163  45.537 5.259   1.00 45.71  ? 78  PHE   A CB  1 
ATOM   295  C CG  . PHE   A 1 38  ? -0.298  44.330 5.077   1.00 40.15  ? 78  PHE   A CG  1 
ATOM   296  C CD1 . PHE   A 1 38  ? 0.740   44.069 5.955   1.00 48.85  ? 78  PHE   A CD1 1 
ATOM   297  C CD2 . PHE   A 1 38  ? -0.516  43.457 4.030   1.00 39.26  ? 78  PHE   A CD2 1 
ATOM   298  C CE1 . PHE   A 1 38  ? 1.549   42.950 5.785   1.00 46.02  ? 78  PHE   A CE1 1 
ATOM   299  C CE2 . PHE   A 1 38  ? 0.284   42.347 3.857   1.00 43.07  ? 78  PHE   A CE2 1 
ATOM   300  C CZ  . PHE   A 1 38  ? 1.313   42.091 4.738   1.00 43.12  ? 78  PHE   A CZ  1 
ATOM   301  N N   . LEU   A 1 39  ? -1.042  46.706 2.394   1.00 43.89  ? 79  LEU   A N   1 
ATOM   302  C CA  . LEU   A 1 39  ? -0.718  46.343 1.021   1.00 42.64  ? 79  LEU   A CA  1 
ATOM   303  C C   . LEU   A 1 39  ? 0.021   47.454 0.287   1.00 43.32  ? 79  LEU   A C   1 
ATOM   304  O O   . LEU   A 1 39  ? 0.803   47.167 -0.623  1.00 43.92  ? 79  LEU   A O   1 
ATOM   305  C CB  . LEU   A 1 39  ? -1.988  45.960 0.263   1.00 40.86  ? 79  LEU   A CB  1 
ATOM   306  C CG  . LEU   A 1 39  ? -2.645  44.651 0.710   1.00 39.61  ? 79  LEU   A CG  1 
ATOM   307  C CD1 . LEU   A 1 39  ? -3.959  44.440 -0.027  1.00 36.79  ? 79  LEU   A CD1 1 
ATOM   308  C CD2 . LEU   A 1 39  ? -1.715  43.469 0.497   1.00 39.03  ? 79  LEU   A CD2 1 
ATOM   309  N N   . ARG   A 1 40  ? -0.206  48.721 0.644   1.00 44.18  ? 80  ARG   A N   1 
ATOM   310  C CA  . ARG   A 1 40  ? 0.475   49.776 -0.096  1.00 44.45  ? 80  ARG   A CA  1 
ATOM   311  C C   . ARG   A 1 40  ? 1.984   49.730 0.109   1.00 47.87  ? 80  ARG   A C   1 
ATOM   312  O O   . ARG   A 1 40  ? 2.726   50.306 -0.693  1.00 43.37  ? 80  ARG   A O   1 
ATOM   313  C CB  . ARG   A 1 40  ? -0.072  51.149 0.284   1.00 45.01  ? 80  ARG   A CB  1 
ATOM   314  C CG  . ARG   A 1 40  ? 0.286   51.614 1.671   1.00 45.88  ? 80  ARG   A CG  1 
ATOM   315  C CD  . ARG   A 1 40  ? 0.070   53.099 1.758   1.00 55.79  ? 80  ARG   A CD  1 
ATOM   316  N NE  . ARG   A 1 40  ? 0.517   53.659 3.024   1.00 66.29  ? 80  ARG   A NE  1 
ATOM   317  C CZ  . ARG   A 1 40  ? 0.394   54.943 3.339   1.00 77.51  ? 80  ARG   A CZ  1 
ATOM   318  N NH1 . ARG   A 1 40  ? -0.171  55.782 2.477   1.00 78.76  ? 80  ARG   A NH1 1 
ATOM   319  N NH2 . ARG   A 1 40  ? 0.823   55.387 4.513   1.00 80.84  ? 80  ARG   A NH2 1 
ATOM   320  N N   . GLN   A 1 41  ? 2.450   49.045 1.152   1.00 44.26  ? 81  GLN   A N   1 
ATOM   321  C CA  . GLN   A 1 41  ? 3.863   48.739 1.326   1.00 41.39  ? 81  GLN   A CA  1 
ATOM   322  C C   . GLN   A 1 41  ? 4.210   47.325 0.890   1.00 41.29  ? 81  GLN   A C   1 
ATOM   323  O O   . GLN   A 1 41  ? 5.207   47.128 0.194   1.00 45.14  ? 81  GLN   A O   1 
ATOM   324  C CB  . GLN   A 1 41  ? 4.277   48.932 2.791   1.00 44.96  ? 81  GLN   A CB  1 
ATOM   325  C CG  . GLN   A 1 41  ? 5.705   48.460 3.119   1.00 50.91  ? 81  GLN   A CG  1 
ATOM   326  C CD  . GLN   A 1 41  ? 6.785   49.437 2.662   1.00 54.96  ? 81  GLN   A CD  1 
ATOM   327  O OE1 . GLN   A 1 41  ? 6.489   50.486 2.089   1.00 62.87  ? 81  GLN   A OE1 1 
ATOM   328  N NE2 . GLN   A 1 41  ? 8.045   49.096 2.925   1.00 46.66  ? 81  GLN   A NE2 1 
ATOM   329  N N   . GLU   A 1 42  ? 3.385   46.339 1.252   1.00 40.42  ? 82  GLU   A N   1 
ATOM   330  C CA  . GLU   A 1 42  ? 3.771   44.944 1.058   1.00 37.13  ? 82  GLU   A CA  1 
ATOM   331  C C   . GLU   A 1 42  ? 3.763   44.547 -0.414  1.00 37.27  ? 82  GLU   A C   1 
ATOM   332  O O   . GLU   A 1 42  ? 4.642   43.801 -0.860  1.00 34.94  ? 82  GLU   A O   1 
ATOM   333  C CB  . GLU   A 1 42  ? 2.853   44.029 1.867   1.00 40.08  ? 82  GLU   A CB  1 
ATOM   334  C CG  . GLU   A 1 42  ? 3.261   42.567 1.827   1.00 41.45  ? 82  GLU   A CG  1 
ATOM   335  C CD  . GLU   A 1 42  ? 4.616   42.315 2.472   1.00 46.43  ? 82  GLU   A CD  1 
ATOM   336  O OE1 . GLU   A 1 42  ? 5.086   43.176 3.250   1.00 46.27  ? 82  GLU   A OE1 1 
ATOM   337  O OE2 . GLU   A 1 42  ? 5.213   41.255 2.201   1.00 43.86  ? 82  GLU   A OE2 1 
ATOM   338  N N   . LEU   A 1 43  ? 2.777   45.012 -1.185  1.00 35.81  ? 83  LEU   A N   1 
ATOM   339  C CA  . LEU   A 1 43  ? 2.775   44.683 -2.610  1.00 36.55  ? 83  LEU   A CA  1 
ATOM   340  C C   . LEU   A 1 43  ? 3.985   45.263 -3.329  1.00 38.20  ? 83  LEU   A C   1 
ATOM   341  O O   . LEU   A 1 43  ? 4.661   44.509 -4.052  1.00 36.49  ? 83  LEU   A O   1 
ATOM   342  C CB  . LEU   A 1 43  ? 1.455   45.122 -3.255  1.00 37.30  ? 83  LEU   A CB  1 
ATOM   343  C CG  . LEU   A 1 43  ? 0.243   44.223 -2.989  1.00 42.03  ? 83  LEU   A CG  1 
ATOM   344  C CD1 . LEU   A 1 43  ? -1.011  44.834 -3.602  1.00 41.72  ? 83  LEU   A CD1 1 
ATOM   345  C CD2 . LEU   A 1 43  ? 0.463   42.807 -3.518  1.00 37.90  ? 83  LEU   A CD2 1 
ATOM   346  N N   . PRO   A 1 44  ? 4.327   46.554 -3.186  1.00 38.71  ? 84  PRO   A N   1 
ATOM   347  C CA  . PRO   A 1 44  ? 5.584   47.032 -3.793  1.00 36.88  ? 84  PRO   A CA  1 
ATOM   348  C C   . PRO   A 1 44  ? 6.806   46.240 -3.357  1.00 38.02  ? 84  PRO   A C   1 
ATOM   349  O O   . PRO   A 1 44  ? 7.681   45.952 -4.184  1.00 36.76  ? 84  PRO   A O   1 
ATOM   350  C CB  . PRO   A 1 44  ? 5.662   48.491 -3.324  1.00 39.96  ? 84  PRO   A CB  1 
ATOM   351  C CG  . PRO   A 1 44  ? 4.240   48.887 -3.124  1.00 39.53  ? 84  PRO   A CG  1 
ATOM   352  C CD  . PRO   A 1 44  ? 3.560   47.665 -2.583  1.00 39.14  ? 84  PRO   A CD  1 
ATOM   353  N N   . VAL   A 1 45  ? 6.889   45.878 -2.074  1.00 34.47  ? 85  VAL   A N   1 
ATOM   354  C CA  . VAL   A 1 45  ? 8.040   45.124 -1.585  1.00 32.04  ? 85  VAL   A CA  1 
ATOM   355  C C   . VAL   A 1 45  ? 8.138   43.777 -2.295  1.00 32.74  ? 85  VAL   A C   1 
ATOM   356  O O   . VAL   A 1 45  ? 9.212   43.377 -2.761  1.00 35.94  ? 85  VAL   A O   1 
ATOM   357  C CB  . VAL   A 1 45  ? 7.961   44.949 -0.058  1.00 29.91  ? 85  VAL   A CB  1 
ATOM   358  C CG1 . VAL   A 1 45  ? 8.979   43.912 0.402   1.00 33.20  ? 85  VAL   A CG1 1 
ATOM   359  C CG2 . VAL   A 1 45  ? 8.193   46.287 0.664   1.00 30.94  ? 85  VAL   A CG2 1 
ATOM   360  N N   . ARG   A 1 46  ? 7.020   43.053 -2.386  1.00 31.14  ? 86  ARG   A N   1 
ATOM   361  C CA  . ARG   A 1 46  ? 7.056   41.735 -3.020  1.00 34.53  ? 86  ARG   A CA  1 
ATOM   362  C C   . ARG   A 1 46  ? 7.295   41.835 -4.523  1.00 35.95  ? 86  ARG   A C   1 
ATOM   363  O O   . ARG   A 1 46  ? 8.017   41.008 -5.095  1.00 34.52  ? 86  ARG   A O   1 
ATOM   364  C CB  . ARG   A 1 46  ? 5.766   40.970 -2.729  1.00 32.09  ? 86  ARG   A CB  1 
ATOM   365  C CG  . ARG   A 1 46  ? 5.571   40.702 -1.248  1.00 32.38  ? 86  ARG   A CG  1 
ATOM   366  C CD  . ARG   A 1 46  ? 4.474   39.684 -1.007  1.00 34.25  ? 86  ARG   A CD  1 
ATOM   367  N NE  . ARG   A 1 46  ? 4.192   39.545 0.416   1.00 33.25  ? 86  ARG   A NE  1 
ATOM   368  C CZ  . ARG   A 1 46  ? 3.413   38.603 0.932   1.00 33.49  ? 86  ARG   A CZ  1 
ATOM   369  N NH1 . ARG   A 1 46  ? 2.840   37.705 0.135   1.00 33.84  ? 86  ARG   A NH1 1 
ATOM   370  N NH2 . ARG   A 1 46  ? 3.214   38.552 2.238   1.00 34.46  ? 86  ARG   A NH2 1 
ATOM   371  N N   . LEU   A 1 47  ? 6.715   42.844 -5.182  1.00 35.07  ? 87  LEU   A N   1 
ATOM   372  C CA  . LEU   A 1 47  ? 6.986   43.035 -6.604  1.00 33.87  ? 87  LEU   A CA  1 
ATOM   373  C C   . LEU   A 1 47  ? 8.454   43.363 -6.840  1.00 34.53  ? 87  LEU   A C   1 
ATOM   374  O O   . LEU   A 1 47  ? 9.102   42.762 -7.702  1.00 34.55  ? 87  LEU   A O   1 
ATOM   375  C CB  . LEU   A 1 47  ? 6.089   44.132 -7.178  1.00 30.67  ? 87  LEU   A CB  1 
ATOM   376  C CG  . LEU   A 1 47  ? 4.627   43.749 -7.434  1.00 37.65  ? 87  LEU   A CG  1 
ATOM   377  C CD1 . LEU   A 1 47  ? 3.815   44.976 -7.827  1.00 43.35  ? 87  LEU   A CD1 1 
ATOM   378  C CD2 . LEU   A 1 47  ? 4.525   42.712 -8.515  1.00 38.21  ? 87  LEU   A CD2 1 
ATOM   379  N N   . ALA   A 1 48  ? 9.008   44.293 -6.055  1.00 36.13  ? 88  ALA   A N   1 
ATOM   380  C CA  . ALA   A 1 48  ? 10.370  44.759 -6.307  1.00 36.63  ? 88  ALA   A CA  1 
ATOM   381  C C   . ALA   A 1 48  ? 11.411  43.689 -5.987  1.00 35.98  ? 88  ALA   A C   1 
ATOM   382  O O   . ALA   A 1 48  ? 12.445  43.604 -6.664  1.00 34.75  ? 88  ALA   A O   1 
ATOM   383  C CB  . ALA   A 1 48  ? 10.650  46.027 -5.502  1.00 34.81  ? 88  ALA   A CB  1 
ATOM   384  N N   . ASN   A 1 49  ? 11.171  42.880 -4.951  1.00 32.24  ? 89  ASN   A N   1 
ATOM   385  C CA  . ASN   A 1 49  ? 12.114  41.813 -4.620  1.00 34.26  ? 89  ASN   A CA  1 
ATOM   386  C C   . ASN   A 1 49  ? 12.268  40.834 -5.781  1.00 35.61  ? 89  ASN   A C   1 
ATOM   387  O O   . ASN   A 1 49  ? 13.388  40.465 -6.151  1.00 37.30  ? 89  ASN   A O   1 
ATOM   388  C CB  . ASN   A 1 49  ? 11.666  41.079 -3.355  1.00 33.07  ? 89  ASN   A CB  1 
ATOM   389  C CG  . ASN   A 1 49  ? 12.247  41.684 -2.086  1.00 35.96  ? 89  ASN   A CG  1 
ATOM   390  O OD1 . ASN   A 1 49  ? 13.223  41.171 -1.524  1.00 32.72  ? 89  ASN   A OD1 1 
ATOM   391  N ND2 . ASN   A 1 49  ? 11.643  42.774 -1.619  1.00 34.66  ? 89  ASN   A ND2 1 
ATOM   392  N N   . ILE   A 1 50  ? 11.155  40.412 -6.379  1.00 29.69  ? 90  ILE   A N   1 
ATOM   393  C CA  . ILE   A 1 50  ? 11.254  39.466 -7.485  1.00 36.55  ? 90  ILE   A CA  1 
ATOM   394  C C   . ILE   A 1 50  ? 11.731  40.153 -8.763  1.00 35.26  ? 90  ILE   A C   1 
ATOM   395  O O   . ILE   A 1 50  ? 12.368  39.514 -9.608  1.00 34.15  ? 90  ILE   A O   1 
ATOM   396  C CB  . ILE   A 1 50  ? 9.917   38.735 -7.701  1.00 35.34  ? 90  ILE   A CB  1 
ATOM   397  C CG1 . ILE   A 1 50  ? 10.159  37.422 -8.454  1.00 34.09  ? 90  ILE   A CG1 1 
ATOM   398  C CG2 . ILE   A 1 50  ? 8.914   39.606 -8.446  1.00 33.87  ? 90  ILE   A CG2 1 
ATOM   399  C CD1 . ILE   A 1 50  ? 11.147  36.512 -7.739  1.00 34.36  ? 90  ILE   A CD1 1 
ATOM   400  N N   . MET   A 1 51  ? 11.454  41.450 -8.932  1.00 32.50  ? 91  MET   A N   1 
ATOM   401  C CA  . MET   A 1 51  ? 11.911  42.138 -10.139 1.00 34.01  ? 91  MET   A CA  1 
ATOM   402  C C   . MET   A 1 51  ? 13.432  42.227 -10.201 1.00 36.66  ? 91  MET   A C   1 
ATOM   403  O O   . MET   A 1 51  ? 14.007  42.184 -11.297 1.00 38.67  ? 91  MET   A O   1 
ATOM   404  C CB  . MET   A 1 51  ? 11.277  43.527 -10.218 1.00 33.68  ? 91  MET   A CB  1 
ATOM   405  C CG  . MET   A 1 51  ? 9.786   43.479 -10.557 1.00 36.13  ? 91  MET   A CG  1 
ATOM   406  S SD  . MET   A 1 51  ? 8.913   45.015 -10.168 1.00 40.71  ? 91  MET   A SD  1 
ATOM   407  C CE  . MET   A 1 51  ? 9.505   46.093 -11.462 1.00 33.98  ? 91  MET   A CE  1 
ATOM   408  N N   . LYS   A 1 52  ? 14.105  42.334 -9.050  1.00 32.68  ? 92  LYS   A N   1 
ATOM   409  C CA  . LYS   A 1 52  ? 15.566  42.309 -9.055  1.00 37.15  ? 92  LYS   A CA  1 
ATOM   410  C C   . LYS   A 1 52  ? 16.097  40.986 -9.591  1.00 39.29  ? 92  LYS   A C   1 
ATOM   411  O O   . LYS   A 1 52  ? 17.182  40.943 -10.183 1.00 39.00  ? 92  LYS   A O   1 
ATOM   412  C CB  . LYS   A 1 52  ? 16.123  42.549 -7.650  1.00 34.37  ? 92  LYS   A CB  1 
ATOM   413  C CG  . LYS   A 1 52  ? 15.798  43.905 -7.073  1.00 40.09  ? 92  LYS   A CG  1 
ATOM   414  C CD  . LYS   A 1 52  ? 16.454  45.019 -7.861  1.00 48.42  ? 92  LYS   A CD  1 
ATOM   415  C CE  . LYS   A 1 52  ? 17.953  45.000 -7.706  1.00 59.83  ? 92  LYS   A CE  1 
ATOM   416  N NZ  . LYS   A 1 52  ? 18.604  46.079 -8.507  1.00 69.38  ? 92  LYS   A NZ  1 
ATOM   417  N N   . GLU   A 1 53  ? 15.356  39.896 -9.392  1.00 33.93  ? 93  GLU   A N   1 
ATOM   418  C CA  . GLU   A 1 53  ? 15.846  38.610 -9.868  1.00 32.97  ? 93  GLU   A CA  1 
ATOM   419  C C   . GLU   A 1 53  ? 15.505  38.374 -11.332 1.00 35.16  ? 93  GLU   A C   1 
ATOM   420  O O   . GLU   A 1 53  ? 16.248  37.669 -12.021 1.00 36.52  ? 93  GLU   A O   1 
ATOM   421  C CB  . GLU   A 1 53  ? 15.309  37.489 -8.979  1.00 35.64  ? 93  GLU   A CB  1 
ATOM   422  C CG  . GLU   A 1 53  ? 15.899  37.573 -7.574  1.00 35.87  ? 93  GLU   A CG  1 
ATOM   423  C CD  . GLU   A 1 53  ? 15.528  36.411 -6.678  1.00 39.05  ? 93  GLU   A CD  1 
ATOM   424  O OE1 . GLU   A 1 53  ? 15.295  36.656 -5.473  1.00 38.23  ? 93  GLU   A OE1 1 
ATOM   425  O OE2 . GLU   A 1 53  ? 15.492  35.258 -7.162  1.00 36.32  ? 93  GLU   A OE2 1 
ATOM   426  N N   . ILE   A 1 54  ? 14.409  38.951 -11.831 1.00 35.20  ? 94  ILE   A N   1 
ATOM   427  C CA  . ILE   A 1 54  ? 14.166  38.923 -13.272 1.00 38.44  ? 94  ILE   A CA  1 
ATOM   428  C C   . ILE   A 1 54  ? 15.370  39.486 -14.009 1.00 39.23  ? 94  ILE   A C   1 
ATOM   429  O O   . ILE   A 1 54  ? 15.809  38.938 -15.027 1.00 40.48  ? 94  ILE   A O   1 
ATOM   430  C CB  . ILE   A 1 54  ? 12.876  39.690 -13.619 1.00 38.54  ? 94  ILE   A CB  1 
ATOM   431  C CG1 . ILE   A 1 54  ? 11.669  39.060 -12.922 1.00 35.50  ? 94  ILE   A CG1 1 
ATOM   432  C CG2 . ILE   A 1 54  ? 12.656  39.729 -15.136 1.00 36.79  ? 94  ILE   A CG2 1 
ATOM   433  C CD1 . ILE   A 1 54  ? 10.374  39.805 -13.156 1.00 35.78  ? 94  ILE   A CD1 1 
ATOM   434  N N   . SER   A 1 55  ? 15.957  40.562 -13.477 1.00 37.93  ? 95  SER   A N   1 
ATOM   435  C CA  . SER   A 1 55  ? 17.087  41.219 -14.123 1.00 42.02  ? 95  SER   A CA  1 
ATOM   436  C C   . SER   A 1 55  ? 18.353  40.371 -14.134 1.00 45.15  ? 95  SER   A C   1 
ATOM   437  O O   . SER   A 1 55  ? 19.292  40.706 -14.866 1.00 43.90  ? 95  SER   A O   1 
ATOM   438  C CB  . SER   A 1 55  ? 17.379  42.551 -13.431 1.00 44.18  ? 95  SER   A CB  1 
ATOM   439  O OG  . SER   A 1 55  ? 16.226  43.371 -13.412 1.00 47.72  ? 95  SER   A OG  1 
ATOM   440  N N   . LEU   A 1 56  ? 18.416  39.299 -13.348 1.00 39.99  ? 96  LEU   A N   1 
ATOM   441  C CA  . LEU   A 1 56  ? 19.603  38.459 -13.307 1.00 42.16  ? 96  LEU   A CA  1 
ATOM   442  C C   . LEU   A 1 56  ? 19.498  37.255 -14.231 1.00 43.61  ? 96  LEU   A C   1 
ATOM   443  O O   . LEU   A 1 56  ? 20.443  36.462 -14.302 1.00 45.93  ? 96  LEU   A O   1 
ATOM   444  C CB  . LEU   A 1 56  ? 19.869  37.998 -11.867 1.00 41.12  ? 96  LEU   A CB  1 
ATOM   445  C CG  . LEU   A 1 56  ? 20.108  39.147 -10.879 1.00 40.30  ? 96  LEU   A CG  1 
ATOM   446  C CD1 . LEU   A 1 56  ? 20.133  38.648 -9.437  1.00 39.94  ? 96  LEU   A CD1 1 
ATOM   447  C CD2 . LEU   A 1 56  ? 21.395  39.898 -11.209 1.00 41.69  ? 96  LEU   A CD2 1 
ATOM   448  N N   . LEU   A 1 57  ? 18.380  37.111 -14.936 1.00 38.83  ? 97  LEU   A N   1 
ATOM   449  C CA  . LEU   A 1 57  ? 18.184  35.995 -15.846 1.00 37.74  ? 97  LEU   A CA  1 
ATOM   450  C C   . LEU   A 1 57  ? 19.223  36.023 -16.969 1.00 38.47  ? 97  LEU   A C   1 
ATOM   451  O O   . LEU   A 1 57  ? 19.744  37.088 -17.320 1.00 40.94  ? 97  LEU   A O   1 
ATOM   452  C CB  . LEU   A 1 57  ? 16.780  36.057 -16.446 1.00 38.23  ? 97  LEU   A CB  1 
ATOM   453  C CG  . LEU   A 1 57  ? 15.652  35.710 -15.477 1.00 39.68  ? 97  LEU   A CG  1 
ATOM   454  C CD1 . LEU   A 1 57  ? 14.308  35.880 -16.154 1.00 36.85  ? 97  LEU   A CD1 1 
ATOM   455  C CD2 . LEU   A 1 57  ? 15.828  34.287 -14.965 1.00 40.32  ? 97  LEU   A CD2 1 
ATOM   456  N N   . PRO   A 1 58  ? 19.541  34.868 -17.556 1.00 42.48  ? 98  PRO   A N   1 
ATOM   457  C CA  . PRO   A 1 58  ? 20.373  34.871 -18.764 1.00 45.11  ? 98  PRO   A CA  1 
ATOM   458  C C   . PRO   A 1 58  ? 19.759  35.789 -19.803 1.00 45.05  ? 98  PRO   A C   1 
ATOM   459  O O   . PRO   A 1 58  ? 18.537  35.835 -19.965 1.00 46.51  ? 98  PRO   A O   1 
ATOM   460  C CB  . PRO   A 1 58  ? 20.352  33.409 -19.223 1.00 46.33  ? 98  PRO   A CB  1 
ATOM   461  C CG  . PRO   A 1 58  ? 19.896  32.634 -18.048 1.00 46.70  ? 98  PRO   A CG  1 
ATOM   462  C CD  . PRO   A 1 58  ? 19.018  33.528 -17.244 1.00 41.30  ? 98  PRO   A CD  1 
ATOM   463  N N   . ASP   A 1 59  ? 20.616  36.528 -20.505 1.00 43.90  ? 99  ASP   A N   1 
ATOM   464  C CA  . ASP   A 1 59  ? 20.118  37.580 -21.381 1.00 48.08  ? 99  ASP   A CA  1 
ATOM   465  C C   . ASP   A 1 59  ? 19.162  37.029 -22.429 1.00 47.53  ? 99  ASP   A C   1 
ATOM   466  O O   . ASP   A 1 59  ? 18.141  37.655 -22.737 1.00 46.09  ? 99  ASP   A O   1 
ATOM   467  C CB  . ASP   A 1 59  ? 21.280  38.310 -22.047 1.00 49.86  ? 99  ASP   A CB  1 
ATOM   468  C CG  . ASP   A 1 59  ? 20.868  39.663 -22.583 1.00 63.30  ? 99  ASP   A CG  1 
ATOM   469  O OD1 . ASP   A 1 59  ? 20.659  40.584 -21.764 1.00 65.65  ? 99  ASP   A OD1 1 
ATOM   470  O OD2 . ASP   A 1 59  ? 20.723  39.802 -23.817 1.00 70.70  ? 99  ASP   A OD2 1 
ATOM   471  N N   . ASN   A 1 60  ? 19.461  35.850 -22.976 1.00 47.81  ? 100 ASN   A N   1 
ATOM   472  C CA  . ASN   A 1 60  ? 18.600  35.273 -23.999 1.00 49.68  ? 100 ASN   A CA  1 
ATOM   473  C C   . ASN   A 1 60  ? 17.237  34.868 -23.455 1.00 48.30  ? 100 ASN   A C   1 
ATOM   474  O O   . ASN   A 1 60  ? 16.288  34.741 -24.237 1.00 47.46  ? 100 ASN   A O   1 
ATOM   475  C CB  . ASN   A 1 60  ? 19.290  34.076 -24.649 1.00 51.70  ? 100 ASN   A CB  1 
ATOM   476  C CG  . ASN   A 1 60  ? 20.474  34.485 -25.497 1.00 59.71  ? 100 ASN   A CG  1 
ATOM   477  O OD1 . ASN   A 1 60  ? 20.548  35.623 -25.975 1.00 54.42  ? 100 ASN   A OD1 1 
ATOM   478  N ND2 . ASN   A 1 60  ? 21.410  33.560 -25.691 1.00 65.13  ? 100 ASN   A ND2 1 
ATOM   479  N N   . LEU   A 1 61  ? 17.113  34.660 -22.147 1.00 42.63  ? 101 LEU   A N   1 
ATOM   480  C CA  . LEU   A 1 61  ? 15.803  34.430 -21.551 1.00 43.66  ? 101 LEU   A CA  1 
ATOM   481  C C   . LEU   A 1 61  ? 15.114  35.749 -21.214 1.00 42.05  ? 101 LEU   A C   1 
ATOM   482  O O   . LEU   A 1 61  ? 13.937  35.937 -21.535 1.00 38.80  ? 101 LEU   A O   1 
ATOM   483  C CB  . LEU   A 1 61  ? 15.937  33.559 -20.296 1.00 40.38  ? 101 LEU   A CB  1 
ATOM   484  C CG  . LEU   A 1 61  ? 14.661  33.342 -19.483 1.00 37.82  ? 101 LEU   A CG  1 
ATOM   485  C CD1 . LEU   A 1 61  ? 13.536  32.804 -20.365 1.00 40.08  ? 101 LEU   A CD1 1 
ATOM   486  C CD2 . LEU   A 1 61  ? 14.917  32.394 -18.315 1.00 38.59  ? 101 LEU   A CD2 1 
ATOM   487  N N   . LEU   A 1 62  ? 15.852  36.675 -20.598 1.00 40.79  ? 102 LEU   A N   1 
ATOM   488  C CA  . LEU   A 1 62  ? 15.299  37.983 -20.259 1.00 39.94  ? 102 LEU   A CA  1 
ATOM   489  C C   . LEU   A 1 62  ? 14.729  38.683 -21.483 1.00 44.64  ? 102 LEU   A C   1 
ATOM   490  O O   . LEU   A 1 62  ? 13.659  39.300 -21.415 1.00 44.92  ? 102 LEU   A O   1 
ATOM   491  C CB  . LEU   A 1 62  ? 16.383  38.847 -19.613 1.00 44.02  ? 102 LEU   A CB  1 
ATOM   492  C CG  . LEU   A 1 62  ? 16.009  40.249 -19.139 1.00 42.04  ? 102 LEU   A CG  1 
ATOM   493  C CD1 . LEU   A 1 62  ? 14.822  40.173 -18.199 1.00 40.81  ? 102 LEU   A CD1 1 
ATOM   494  C CD2 . LEU   A 1 62  ? 17.196  40.900 -18.444 1.00 38.96  ? 102 LEU   A CD2 1 
ATOM   495  N N   . ARG   A 1 63  ? 15.420  38.582 -22.618 1.00 41.18  ? 103 ARG   A N   1 
ATOM   496  C CA  . ARG   A 1 63  ? 15.056  39.316 -23.824 1.00 43.81  ? 103 ARG   A CA  1 
ATOM   497  C C   . ARG   A 1 63  ? 13.902  38.693 -24.598 1.00 40.84  ? 103 ARG   A C   1 
ATOM   498  O O   . ARG   A 1 63  ? 13.493  39.273 -25.605 1.00 44.35  ? 103 ARG   A O   1 
ATOM   499  C CB  . ARG   A 1 63  ? 16.266  39.441 -24.757 1.00 53.36  ? 103 ARG   A CB  1 
ATOM   500  C CG  . ARG   A 1 63  ? 17.394  40.323 -24.237 1.00 66.63  ? 103 ARG   A CG  1 
ATOM   501  C CD  . ARG   A 1 63  ? 17.061  41.812 -24.364 1.00 82.15  ? 103 ARG   A CD  1 
ATOM   502  N NE  . ARG   A 1 63  ? 18.228  42.651 -24.090 1.00 94.79  ? 103 ARG   A NE  1 
ATOM   503  C CZ  . ARG   A 1 63  ? 19.058  43.112 -25.024 1.00 102.16 ? 103 ARG   A CZ  1 
ATOM   504  N NH1 . ARG   A 1 63  ? 20.099  43.860 -24.679 1.00 105.27 ? 103 ARG   A NH1 1 
ATOM   505  N NH2 . ARG   A 1 63  ? 18.847  42.831 -26.304 1.00 101.40 ? 103 ARG   A NH2 1 
ATOM   506  N N   . THR   A 1 64  ? 13.372  37.542 -24.184 1.00 40.54  ? 104 THR   A N   1 
ATOM   507  C CA  . THR   A 1 64  ? 12.269  36.954 -24.936 1.00 45.29  ? 104 THR   A CA  1 
ATOM   508  C C   . THR   A 1 64  ? 11.042  37.863 -24.854 1.00 44.06  ? 104 THR   A C   1 
ATOM   509  O O   . THR   A 1 64  ? 10.850  38.572 -23.863 1.00 45.09  ? 104 THR   A O   1 
ATOM   510  C CB  . THR   A 1 64  ? 11.910  35.558 -24.414 1.00 42.37  ? 104 THR   A CB  1 
ATOM   511  O OG1 . THR   A 1 64  ? 11.489  35.640 -23.047 1.00 41.23  ? 104 THR   A OG1 1 
ATOM   512  C CG2 . THR   A 1 64  ? 13.092  34.606 -24.528 1.00 43.84  ? 104 THR   A CG2 1 
ATOM   513  N N   . PRO   A 1 65  ? 10.201  37.870 -25.890 1.00 44.36  ? 105 PRO   A N   1 
ATOM   514  C CA  . PRO   A 1 65  ? 9.001   38.720 -25.832 1.00 46.86  ? 105 PRO   A CA  1 
ATOM   515  C C   . PRO   A 1 65  ? 8.109   38.426 -24.635 1.00 45.86  ? 105 PRO   A C   1 
ATOM   516  O O   . PRO   A 1 65  ? 7.509   39.358 -24.081 1.00 46.60  ? 105 PRO   A O   1 
ATOM   517  C CB  . PRO   A 1 65  ? 8.291   38.429 -27.165 1.00 50.44  ? 105 PRO   A CB  1 
ATOM   518  C CG  . PRO   A 1 65  ? 8.943   37.192 -27.714 1.00 52.59  ? 105 PRO   A CG  1 
ATOM   519  C CD  . PRO   A 1 65  ? 10.342  37.192 -27.188 1.00 50.23  ? 105 PRO   A CD  1 
ATOM   520  N N   . SER   A 1 66  ? 8.019   37.165 -24.202 1.00 39.71  ? 106 SER   A N   1 
ATOM   521  C CA  . SER   A 1 66  ? 7.128   36.831 -23.095 1.00 40.80  ? 106 SER   A CA  1 
ATOM   522  C C   . SER   A 1 66  ? 7.681   37.306 -21.756 1.00 41.03  ? 106 SER   A C   1 
ATOM   523  O O   . SER   A 1 66  ? 6.922   37.799 -20.911 1.00 41.46  ? 106 SER   A O   1 
ATOM   524  C CB  . SER   A 1 66  ? 6.865   35.327 -23.066 1.00 36.98  ? 106 SER   A CB  1 
ATOM   525  O OG  . SER   A 1 66  ? 6.187   34.913 -24.233 1.00 41.44  ? 106 SER   A OG  1 
ATOM   526  N N   . VAL   A 1 67  ? 8.988   37.154 -21.521 1.00 39.72  ? 107 VAL   A N   1 
ATOM   527  C CA  . VAL   A 1 67  ? 9.548   37.656 -20.269 1.00 39.18  ? 107 VAL   A CA  1 
ATOM   528  C C   . VAL   A 1 67  ? 9.512   39.179 -20.247 1.00 38.93  ? 107 VAL   A C   1 
ATOM   529  O O   . VAL   A 1 67  ? 9.221   39.791 -19.213 1.00 39.67  ? 107 VAL   A O   1 
ATOM   530  C CB  . VAL   A 1 67  ? 10.970  37.114 -20.046 1.00 38.22  ? 107 VAL   A CB  1 
ATOM   531  C CG1 . VAL   A 1 67  ? 11.627  37.791 -18.836 1.00 38.51  ? 107 VAL   A CG1 1 
ATOM   532  C CG2 . VAL   A 1 67  ? 10.923  35.610 -19.843 1.00 37.31  ? 107 VAL   A CG2 1 
ATOM   533  N N   . GLN   A 1 68  ? 9.776   39.812 -21.393 1.00 38.64  ? 108 GLN   A N   1 
ATOM   534  C CA  . GLN   A 1 68  ? 9.695   41.267 -21.466 1.00 43.49  ? 108 GLN   A CA  1 
ATOM   535  C C   . GLN   A 1 68  ? 8.290   41.754 -21.144 1.00 47.96  ? 108 GLN   A C   1 
ATOM   536  O O   . GLN   A 1 68  ? 8.114   42.788 -20.487 1.00 45.00  ? 108 GLN   A O   1 
ATOM   537  C CB  . GLN   A 1 68  ? 10.123  41.746 -22.851 1.00 43.66  ? 108 GLN   A CB  1 
ATOM   538  C CG  . GLN   A 1 68  ? 11.619  41.676 -23.067 1.00 47.93  ? 108 GLN   A CG  1 
ATOM   539  C CD  . GLN   A 1 68  ? 12.371  42.613 -22.139 1.00 47.57  ? 108 GLN   A CD  1 
ATOM   540  O OE1 . GLN   A 1 68  ? 12.143  43.823 -22.148 1.00 49.74  ? 108 GLN   A OE1 1 
ATOM   541  N NE2 . GLN   A 1 68  ? 13.267  42.061 -21.331 1.00 44.42  ? 108 GLN   A NE2 1 
ATOM   542  N N   . LEU   A 1 69  ? 7.276   41.013 -21.591 1.00 44.69  ? 109 LEU   A N   1 
ATOM   543  C CA  . LEU   A 1 69  ? 5.905   41.396 -21.289 1.00 43.74  ? 109 LEU   A CA  1 
ATOM   544  C C   . LEU   A 1 69  ? 5.601   41.240 -19.801 1.00 43.28  ? 109 LEU   A C   1 
ATOM   545  O O   . LEU   A 1 69  ? 5.013   42.140 -19.187 1.00 43.30  ? 109 LEU   A O   1 
ATOM   546  C CB  . LEU   A 1 69  ? 4.944   40.573 -22.143 1.00 41.78  ? 109 LEU   A CB  1 
ATOM   547  C CG  . LEU   A 1 69  ? 3.472   40.965 -22.111 1.00 46.95  ? 109 LEU   A CG  1 
ATOM   548  C CD1 . LEU   A 1 69  ? 3.274   42.415 -22.535 1.00 52.43  ? 109 LEU   A CD1 1 
ATOM   549  C CD2 . LEU   A 1 69  ? 2.703   40.044 -23.022 1.00 48.72  ? 109 LEU   A CD2 1 
ATOM   550  N N   . VAL   A 1 70  ? 6.008   40.118 -19.194 1.00 37.23  ? 110 VAL   A N   1 
ATOM   551  C CA  . VAL   A 1 70  ? 5.788   39.933 -17.762 1.00 37.36  ? 110 VAL   A CA  1 
ATOM   552  C C   . VAL   A 1 70  ? 6.477   41.040 -16.976 1.00 40.67  ? 110 VAL   A C   1 
ATOM   553  O O   . VAL   A 1 70  ? 5.894   41.639 -16.061 1.00 40.33  ? 110 VAL   A O   1 
ATOM   554  C CB  . VAL   A 1 70  ? 6.274   38.544 -17.315 1.00 35.89  ? 110 VAL   A CB  1 
ATOM   555  C CG1 . VAL   A 1 70  ? 6.344   38.466 -15.787 1.00 36.28  ? 110 VAL   A CG1 1 
ATOM   556  C CG2 . VAL   A 1 70  ? 5.364   37.468 -17.880 1.00 32.55  ? 110 VAL   A CG2 1 
ATOM   557  N N   . GLN   A 1 71  ? 7.730   41.336 -17.330 1.00 40.26  ? 111 GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 71  ? 8.453   42.391 -16.633 1.00 40.32  ? 111 GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 71  ? 7.756   43.735 -16.796 1.00 43.10  ? 111 GLN   A C   1 
ATOM   560  O O   . GLN   A 1 71  ? 7.697   44.527 -15.850 1.00 40.21  ? 111 GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 71  ? 9.892   42.473 -17.136 1.00 43.87  ? 111 GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 71  ? 10.742  43.463 -16.362 1.00 45.38  ? 111 GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 71  ? 12.132  43.608 -16.940 1.00 44.41  ? 111 GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 71  ? 12.298  43.945 -18.113 1.00 43.85  ? 111 GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 71  ? 13.141  43.344 -16.121 1.00 42.05  ? 111 GLN   A NE2 1 
ATOM   566  N N   . SER   A 1 72  ? 7.205   44.007 -17.981 1.00 40.25  ? 112 SER   A N   1 
ATOM   567  C CA  . SER   A 1 72  ? 6.520   45.282 -18.154 1.00 42.10  ? 112 SER   A CA  1 
ATOM   568  C C   . SER   A 1 72  ? 5.229   45.330 -17.346 1.00 44.01  ? 112 SER   A C   1 
ATOM   569  O O   . SER   A 1 72  ? 4.855   46.399 -16.848 1.00 46.09  ? 112 SER   A O   1 
ATOM   570  C CB  . SER   A 1 72  ? 6.250   45.548 -19.634 1.00 51.24  ? 112 SER   A CB  1 
ATOM   571  O OG  . SER   A 1 72  ? 5.173   44.760 -20.107 1.00 65.75  ? 112 SER   A OG  1 
ATOM   572  N N   . TRP   A 1 73  ? 4.545   44.191 -17.189 1.00 40.95  ? 113 TRP   A N   1 
ATOM   573  C CA  . TRP   A 1 73  ? 3.385   44.146 -16.302 1.00 42.91  ? 113 TRP   A CA  1 
ATOM   574  C C   . TRP   A 1 73  ? 3.784   44.481 -14.870 1.00 42.60  ? 113 TRP   A C   1 
ATOM   575  O O   . TRP   A 1 73  ? 3.115   45.274 -14.195 1.00 40.50  ? 113 TRP   A O   1 
ATOM   576  C CB  . TRP   A 1 73  ? 2.718   42.767 -16.357 1.00 36.15  ? 113 TRP   A CB  1 
ATOM   577  C CG  . TRP   A 1 73  ? 1.994   42.492 -17.633 1.00 42.40  ? 113 TRP   A CG  1 
ATOM   578  C CD1 . TRP   A 1 73  ? 1.556   43.408 -18.541 1.00 44.38  ? 113 TRP   A CD1 1 
ATOM   579  C CD2 . TRP   A 1 73  ? 1.629   41.206 -18.151 1.00 42.94  ? 113 TRP   A CD2 1 
ATOM   580  N NE1 . TRP   A 1 73  ? 0.931   42.773 -19.587 1.00 49.50  ? 113 TRP   A NE1 1 
ATOM   581  C CE2 . TRP   A 1 73  ? 0.969   41.420 -19.373 1.00 47.99  ? 113 TRP   A CE2 1 
ATOM   582  C CE3 . TRP   A 1 73  ? 1.794   39.894 -17.694 1.00 44.41  ? 113 TRP   A CE3 1 
ATOM   583  C CZ2 . TRP   A 1 73  ? 0.474   40.374 -20.146 1.00 51.55  ? 113 TRP   A CZ2 1 
ATOM   584  C CZ3 . TRP   A 1 73  ? 1.305   38.858 -18.463 1.00 44.67  ? 113 TRP   A CZ3 1 
ATOM   585  C CH2 . TRP   A 1 73  ? 0.655   39.103 -19.675 1.00 48.90  ? 113 TRP   A CH2 1 
ATOM   586  N N   . TYR   A 1 74  ? 4.881   43.887 -14.389 1.00 37.28  ? 114 TYR   A N   1 
ATOM   587  C CA  . TYR   A 1 74  ? 5.311   44.134 -13.017 1.00 39.72  ? 114 TYR   A CA  1 
ATOM   588  C C   . TYR   A 1 74  ? 5.713   45.591 -12.825 1.00 42.41  ? 114 TYR   A C   1 
ATOM   589  O O   . TYR   A 1 74  ? 5.340   46.219 -11.826 1.00 43.29  ? 114 TYR   A O   1 
ATOM   590  C CB  . TYR   A 1 74  ? 6.461   43.191 -12.646 1.00 30.42  ? 114 TYR   A CB  1 
ATOM   591  C CG  . TYR   A 1 74  ? 5.994   41.835 -12.145 1.00 35.70  ? 114 TYR   A CG  1 
ATOM   592  C CD1 . TYR   A 1 74  ? 4.992   41.136 -12.802 1.00 38.50  ? 114 TYR   A CD1 1 
ATOM   593  C CD2 . TYR   A 1 74  ? 6.557   41.256 -11.017 1.00 36.87  ? 114 TYR   A CD2 1 
ATOM   594  C CE1 . TYR   A 1 74  ? 4.556   39.901 -12.343 1.00 40.17  ? 114 TYR   A CE1 1 
ATOM   595  C CE2 . TYR   A 1 74  ? 6.122   40.017 -10.549 1.00 34.00  ? 114 TYR   A CE2 1 
ATOM   596  C CZ  . TYR   A 1 74  ? 5.128   39.348 -11.219 1.00 35.55  ? 114 TYR   A CZ  1 
ATOM   597  O OH  . TYR   A 1 74  ? 4.692   38.117 -10.756 1.00 35.21  ? 114 TYR   A OH  1 
ATOM   598  N N   . ILE   A 1 75  ? 6.453   46.147 -13.784 1.00 39.56  ? 115 ILE   A N   1 
ATOM   599  C CA  . ILE   A 1 75  ? 6.875   47.542 -13.703 1.00 40.46  ? 115 ILE   A CA  1 
ATOM   600  C C   . ILE   A 1 75  ? 5.666   48.463 -13.615 1.00 46.02  ? 115 ILE   A C   1 
ATOM   601  O O   . ILE   A 1 75  ? 5.640   49.412 -12.818 1.00 44.47  ? 115 ILE   A O   1 
ATOM   602  C CB  . ILE   A 1 75  ? 7.766   47.887 -14.910 1.00 44.46  ? 115 ILE   A CB  1 
ATOM   603  C CG1 . ILE   A 1 75  ? 9.096   47.131 -14.826 1.00 45.47  ? 115 ILE   A CG1 1 
ATOM   604  C CG2 . ILE   A 1 75  ? 7.987   49.394 -15.001 1.00 47.00  ? 115 ILE   A CG2 1 
ATOM   605  C CD1 . ILE   A 1 75  ? 9.991   47.329 -16.032 1.00 50.47  ? 115 ILE   A CD1 1 
ATOM   606  N N   . GLN   A 1 76  ? 4.641   48.190 -14.418 1.00 48.57  ? 116 GLN   A N   1 
ATOM   607  C CA  . GLN   A 1 76  ? 3.468   49.056 -14.441 1.00 49.38  ? 116 GLN   A CA  1 
ATOM   608  C C   . GLN   A 1 76  ? 2.667   48.938 -13.152 1.00 47.87  ? 116 GLN   A C   1 
ATOM   609  O O   . GLN   A 1 76  ? 2.172   49.944 -12.626 1.00 48.96  ? 116 GLN   A O   1 
ATOM   610  C CB  . GLN   A 1 76  ? 2.598   48.718 -15.648 1.00 50.41  ? 116 GLN   A CB  1 
ATOM   611  C CG  . GLN   A 1 76  ? 1.340   49.549 -15.739 1.00 60.72  ? 116 GLN   A CG  1 
ATOM   612  C CD  . GLN   A 1 76  ? 0.748   49.534 -17.126 1.00 71.58  ? 116 GLN   A CD  1 
ATOM   613  O OE1 . GLN   A 1 76  ? 0.743   48.502 -17.803 1.00 76.79  ? 116 GLN   A OE1 1 
ATOM   614  N NE2 . GLN   A 1 76  ? 0.260   50.687 -17.568 1.00 73.62  ? 116 GLN   A NE2 1 
ATOM   615  N N   . SER   A 1 77  ? 2.523   47.719 -12.628 1.00 41.26  ? 117 SER   A N   1 
ATOM   616  C CA  . SER   A 1 77  ? 1.800   47.543 -11.375 1.00 40.75  ? 117 SER   A CA  1 
ATOM   617  C C   . SER   A 1 77  ? 2.536   48.209 -10.222 1.00 45.12  ? 117 SER   A C   1 
ATOM   618  O O   . SER   A 1 77  ? 1.913   48.855 -9.371  1.00 43.51  ? 117 SER   A O   1 
ATOM   619  C CB  . SER   A 1 77  ? 1.590   46.058 -11.099 1.00 43.50  ? 117 SER   A CB  1 
ATOM   620  O OG  . SER   A 1 77  ? 0.818   45.474 -12.133 1.00 51.35  ? 117 SER   A OG  1 
ATOM   621  N N   . LEU   A 1 78  ? 3.864   48.070 -10.186 1.00 42.51  ? 118 LEU   A N   1 
ATOM   622  C CA  . LEU   A 1 78  ? 4.651   48.708 -9.138  1.00 40.85  ? 118 LEU   A CA  1 
ATOM   623  C C   . LEU   A 1 78  ? 4.442   50.215 -9.145  1.00 43.78  ? 118 LEU   A C   1 
ATOM   624  O O   . LEU   A 1 78  ? 4.180   50.819 -8.100  1.00 43.27  ? 118 LEU   A O   1 
ATOM   625  C CB  . LEU   A 1 78  ? 6.131   48.367 -9.313  1.00 38.65  ? 118 LEU   A CB  1 
ATOM   626  C CG  . LEU   A 1 78  ? 7.081   49.058 -8.336  1.00 42.05  ? 118 LEU   A CG  1 
ATOM   627  C CD1 . LEU   A 1 78  ? 6.709   48.682 -6.915  1.00 39.30  ? 118 LEU   A CD1 1 
ATOM   628  C CD2 . LEU   A 1 78  ? 8.536   48.693 -8.626  1.00 41.86  ? 118 LEU   A CD2 1 
ATOM   629  N N   . GLN   A 1 79  ? 4.536   50.837 -10.324 1.00 47.86  ? 119 GLN   A N   1 
ATOM   630  C CA  . GLN   A 1 79  ? 4.374   52.285 -10.419 1.00 51.69  ? 119 GLN   A CA  1 
ATOM   631  C C   . GLN   A 1 79  ? 2.976   52.720 -10.004 1.00 48.94  ? 119 GLN   A C   1 
ATOM   632  O O   . GLN   A 1 79  ? 2.810   53.761 -9.358  1.00 50.75  ? 119 GLN   A O   1 
ATOM   633  C CB  . GLN   A 1 79  ? 4.674   52.761 -11.839 1.00 60.54  ? 119 GLN   A CB  1 
ATOM   634  C CG  . GLN   A 1 79  ? 6.152   52.748 -12.204 1.00 70.63  ? 119 GLN   A CG  1 
ATOM   635  C CD  . GLN   A 1 79  ? 6.404   53.189 -13.636 1.00 78.60  ? 119 GLN   A CD  1 
ATOM   636  O OE1 . GLN   A 1 79  ? 7.432   53.793 -13.939 1.00 81.80  ? 119 GLN   A OE1 1 
ATOM   637  N NE2 . GLN   A 1 79  ? 5.461   52.885 -14.526 1.00 79.50  ? 119 GLN   A NE2 1 
ATOM   638  N N   . GLU   A 1 80  ? 1.957   51.938 -10.362 1.00 47.41  ? 120 GLU   A N   1 
ATOM   639  C CA  . GLU   A 1 80  ? 0.598   52.291 -9.966  1.00 51.94  ? 120 GLU   A CA  1 
ATOM   640  C C   . GLU   A 1 80  ? 0.418   52.189 -8.457  1.00 51.89  ? 120 GLU   A C   1 
ATOM   641  O O   . GLU   A 1 80  ? -0.315  52.983 -7.860  1.00 54.88  ? 120 GLU   A O   1 
ATOM   642  C CB  . GLU   A 1 80  ? -0.410  51.398 -10.686 1.00 54.78  ? 120 GLU   A CB  1 
ATOM   643  C CG  . GLU   A 1 80  ? -0.509  51.684 -12.169 1.00 63.14  ? 120 GLU   A CG  1 
ATOM   644  C CD  . GLU   A 1 80  ? -1.406  50.707 -12.898 1.00 67.39  ? 120 GLU   A CD  1 
ATOM   645  O OE1 . GLU   A 1 80  ? -1.783  49.676 -12.303 1.00 69.57  ? 120 GLU   A OE1 1 
ATOM   646  O OE2 . GLU   A 1 80  ? -1.729  50.974 -14.073 1.00 72.36  ? 120 GLU   A OE2 1 
ATOM   647  N N   . LEU   A 1 81  ? 1.080   51.221 -7.823  1.00 50.39  ? 121 LEU   A N   1 
ATOM   648  C CA  . LEU   A 1 81  ? 0.973   51.091 -6.374  1.00 47.90  ? 121 LEU   A CA  1 
ATOM   649  C C   . LEU   A 1 81  ? 1.703   52.223 -5.658  1.00 45.44  ? 121 LEU   A C   1 
ATOM   650  O O   . LEU   A 1 81  ? 1.214   52.744 -4.648  1.00 50.86  ? 121 LEU   A O   1 
ATOM   651  C CB  . LEU   A 1 81  ? 1.509   49.728 -5.933  1.00 46.88  ? 121 LEU   A CB  1 
ATOM   652  C CG  . LEU   A 1 81  ? 0.638   48.555 -6.389  1.00 47.09  ? 121 LEU   A CG  1 
ATOM   653  C CD1 . LEU   A 1 81  ? 1.416   47.257 -6.330  1.00 49.13  ? 121 LEU   A CD1 1 
ATOM   654  C CD2 . LEU   A 1 81  ? -0.632  48.456 -5.547  1.00 42.20  ? 121 LEU   A CD2 1 
ATOM   655  N N   . LEU   A 1 82  ? 2.860   52.636 -6.178  1.00 47.13  ? 122 LEU   A N   1 
ATOM   656  C CA  . LEU   A 1 82  ? 3.654   53.657 -5.506  1.00 55.64  ? 122 LEU   A CA  1 
ATOM   657  C C   . LEU   A 1 82  ? 2.969   55.016 -5.468  1.00 62.44  ? 122 LEU   A C   1 
ATOM   658  O O   . LEU   A 1 82  ? 3.392   55.879 -4.691  1.00 69.63  ? 122 LEU   A O   1 
ATOM   659  C CB  . LEU   A 1 82  ? 5.020   53.790 -6.176  1.00 58.69  ? 122 LEU   A CB  1 
ATOM   660  C CG  . LEU   A 1 82  ? 5.854   52.519 -6.042  1.00 60.53  ? 122 LEU   A CG  1 
ATOM   661  C CD1 . LEU   A 1 82  ? 7.308   52.754 -6.438  1.00 58.88  ? 122 LEU   A CD1 1 
ATOM   662  C CD2 . LEU   A 1 82  ? 5.740   51.990 -4.620  1.00 62.32  ? 122 LEU   A CD2 1 
ATOM   663  N N   . ASP   A 1 83  ? 1.929   55.233 -6.277  1.00 63.76  ? 123 ASP   A N   1 
ATOM   664  C CA  . ASP   A 1 83  ? 1.222   56.509 -6.231  1.00 72.45  ? 123 ASP   A CA  1 
ATOM   665  C C   . ASP   A 1 83  ? 0.471   56.725 -4.924  1.00 69.53  ? 123 ASP   A C   1 
ATOM   666  O O   . ASP   A 1 83  ? 0.058   57.854 -4.649  1.00 77.08  ? 123 ASP   A O   1 
ATOM   667  C CB  . ASP   A 1 83  ? 0.247   56.621 -7.406  1.00 84.22  ? 123 ASP   A CB  1 
ATOM   668  C CG  . ASP   A 1 83  ? 0.952   56.848 -8.731  1.00 93.49  ? 123 ASP   A CG  1 
ATOM   669  O OD1 . ASP   A 1 83  ? 2.088   57.372 -8.715  1.00 96.26  ? 123 ASP   A OD1 1 
ATOM   670  O OD2 . ASP   A 1 83  ? 0.371   56.508 -9.787  1.00 97.15  ? 123 ASP   A OD2 1 
ATOM   671  N N   . PHE   A 1 84  ? 0.290   55.684 -4.116  1.00 63.71  ? 124 PHE   A N   1 
ATOM   672  C CA  . PHE   A 1 84  ? -0.423  55.785 -2.850  1.00 69.52  ? 124 PHE   A CA  1 
ATOM   673  C C   . PHE   A 1 84  ? 0.509   55.931 -1.653  1.00 75.34  ? 124 PHE   A C   1 
ATOM   674  O O   . PHE   A 1 84  ? 0.025   56.004 -0.517  1.00 73.57  ? 124 PHE   A O   1 
ATOM   675  C CB  . PHE   A 1 84  ? -1.319  54.556 -2.652  1.00 63.23  ? 124 PHE   A CB  1 
ATOM   676  C CG  . PHE   A 1 84  ? -2.387  54.400 -3.704  1.00 60.64  ? 124 PHE   A CG  1 
ATOM   677  C CD1 . PHE   A 1 84  ? -2.114  53.751 -4.898  1.00 58.76  ? 124 PHE   A CD1 1 
ATOM   678  C CD2 . PHE   A 1 84  ? -3.667  54.883 -3.489  1.00 61.29  ? 124 PHE   A CD2 1 
ATOM   679  C CE1 . PHE   A 1 84  ? -3.094  53.597 -5.863  1.00 56.88  ? 124 PHE   A CE1 1 
ATOM   680  C CE2 . PHE   A 1 84  ? -4.652  54.734 -4.450  1.00 63.26  ? 124 PHE   A CE2 1 
ATOM   681  C CZ  . PHE   A 1 84  ? -4.364  54.090 -5.638  1.00 63.22  ? 124 PHE   A CZ  1 
ATOM   682  N N   . LYS   A 1 85  ? 1.827   55.984 -1.889  1.00 75.43  ? 125 LYS   A N   1 
ATOM   683  C CA  . LYS   A 1 85  ? 2.811   55.975 -0.806  1.00 75.09  ? 125 LYS   A CA  1 
ATOM   684  C C   . LYS   A 1 85  ? 2.557   57.089 0.204   1.00 82.30  ? 125 LYS   A C   1 
ATOM   685  O O   . LYS   A 1 85  ? 2.700   56.883 1.417   1.00 80.70  ? 125 LYS   A O   1 
ATOM   686  C CB  . LYS   A 1 85  ? 4.219   56.097 -1.396  1.00 77.12  ? 125 LYS   A CB  1 
ATOM   687  C CG  . LYS   A 1 85  ? 5.296   56.606 -0.436  1.00 86.88  ? 125 LYS   A CG  1 
ATOM   688  C CD  . LYS   A 1 85  ? 6.008   55.461 0.289   1.00 87.17  ? 125 LYS   A CD  1 
ATOM   689  C CE  . LYS   A 1 85  ? 7.332   55.912 0.926   1.00 87.09  ? 125 LYS   A CE  1 
ATOM   690  N NZ  . LYS   A 1 85  ? 7.166   56.667 2.205   1.00 82.12  ? 125 LYS   A NZ  1 
ATOM   691  N N   . ASP   A 1 86  ? 2.179   58.274 -0.270  1.00 86.01  ? 126 ASP   A N   1 
ATOM   692  C CA  . ASP   A 1 86  ? 1.982   59.423 0.599   1.00 93.18  ? 126 ASP   A CA  1 
ATOM   693  C C   . ASP   A 1 86  ? 0.520   59.786 0.805   1.00 91.81  ? 126 ASP   A C   1 
ATOM   694  O O   . ASP   A 1 86  ? 0.236   60.792 1.465   1.00 95.05  ? 126 ASP   A O   1 
ATOM   695  C CB  . ASP   A 1 86  ? 2.740   60.636 0.049   1.00 104.71 ? 126 ASP   A CB  1 
ATOM   696  C CG  . ASP   A 1 86  ? 4.221   60.599 0.380   1.00 110.22 ? 126 ASP   A CG  1 
ATOM   697  O OD1 . ASP   A 1 86  ? 4.648   59.677 1.109   1.00 108.43 ? 126 ASP   A OD1 1 
ATOM   698  O OD2 . ASP   A 1 86  ? 4.955   61.497 -0.087  1.00 114.77 ? 126 ASP   A OD2 1 
ATOM   699  N N   . LYS   A 1 87  ? -0.414  59.006 0.271   1.00 85.71  ? 127 LYS   A N   1 
ATOM   700  C CA  . LYS   A 1 87  ? -1.814  59.361 0.438   1.00 83.87  ? 127 LYS   A CA  1 
ATOM   701  C C   . LYS   A 1 87  ? -2.347  58.841 1.772   1.00 83.09  ? 127 LYS   A C   1 
ATOM   702  O O   . LYS   A 1 87  ? -1.817  57.894 2.359   1.00 81.77  ? 127 LYS   A O   1 
ATOM   703  C CB  . LYS   A 1 87  ? -2.637  58.844 -0.741  1.00 77.74  ? 127 LYS   A CB  1 
ATOM   704  C CG  . LYS   A 1 87  ? -2.500  59.757 -1.947  1.00 83.72  ? 127 LYS   A CG  1 
ATOM   705  C CD  . LYS   A 1 87  ? -3.165  59.223 -3.194  1.00 87.74  ? 127 LYS   A CD  1 
ATOM   706  C CE  . LYS   A 1 87  ? -3.083  60.265 -4.303  1.00 95.65  ? 127 LYS   A CE  1 
ATOM   707  N NZ  . LYS   A 1 87  ? -3.521  59.737 -5.623  1.00 98.88  ? 127 LYS   A NZ  1 
ATOM   708  N N   . SER   A 1 88  ? -3.399  59.496 2.261   1.00 87.10  ? 128 SER   A N   1 
ATOM   709  C CA  . SER   A 1 88  ? -3.894  59.274 3.614   1.00 81.81  ? 128 SER   A CA  1 
ATOM   710  C C   . SER   A 1 88  ? -4.909  58.141 3.672   1.00 81.09  ? 128 SER   A C   1 
ATOM   711  O O   . SER   A 1 88  ? -5.793  58.033 2.817   1.00 79.73  ? 128 SER   A O   1 
ATOM   712  C CB  . SER   A 1 88  ? -4.534  60.545 4.165   1.00 80.65  ? 128 SER   A CB  1 
ATOM   713  O OG  . SER   A 1 88  ? -5.341  60.236 5.286   1.00 80.35  ? 128 SER   A OG  1 
ATOM   714  N N   . ALA   A 1 89  ? -4.789  57.311 4.715   1.00 80.40  ? 129 ALA   A N   1 
ATOM   715  C CA  . ALA   A 1 89  ? -5.742  56.228 4.934   1.00 82.59  ? 129 ALA   A CA  1 
ATOM   716  C C   . ALA   A 1 89  ? -7.146  56.743 5.231   1.00 90.05  ? 129 ALA   A C   1 
ATOM   717  O O   . ALA   A 1 89  ? -8.120  56.003 5.048   1.00 87.15  ? 129 ALA   A O   1 
ATOM   718  C CB  . ALA   A 1 89  ? -5.266  55.334 6.079   1.00 80.61  ? 129 ALA   A CB  1 
ATOM   719  N N   . GLU   A 1 90  ? -7.271  57.989 5.687   1.00 94.42  ? 130 GLU   A N   1 
ATOM   720  C CA  . GLU   A 1 90  ? -8.580  58.575 5.931   1.00 98.81  ? 130 GLU   A CA  1 
ATOM   721  C C   . GLU   A 1 90  ? -9.203  59.155 4.669   1.00 99.29  ? 130 GLU   A C   1 
ATOM   722  O O   . GLU   A 1 90  ? -10.428 59.321 4.618   1.00 102.44 ? 130 GLU   A O   1 
ATOM   723  C CB  . GLU   A 1 90  ? -8.463  59.650 7.009   1.00 104.72 ? 130 GLU   A CB  1 
ATOM   724  C CG  . GLU   A 1 90  ? -7.898  59.115 8.310   1.00 107.21 ? 130 GLU   A CG  1 
ATOM   725  C CD  . GLU   A 1 90  ? -8.836  58.132 8.985   1.00 112.28 ? 130 GLU   A CD  1 
ATOM   726  O OE1 . GLU   A 1 90  ? -9.722  58.583 9.745   1.00 119.59 ? 130 GLU   A OE1 1 
ATOM   727  O OE2 . GLU   A 1 90  ? -8.700  56.912 8.747   1.00 109.00 ? 130 GLU   A OE2 1 
ATOM   728  N N   . ASP   A 1 91  ? -8.388  59.469 3.662   1.00 93.45  ? 131 ASP   A N   1 
ATOM   729  C CA  . ASP   A 1 91  ? -8.878  59.881 2.353   1.00 88.38  ? 131 ASP   A CA  1 
ATOM   730  C C   . ASP   A 1 91  ? -9.697  58.747 1.749   1.00 82.91  ? 131 ASP   A C   1 
ATOM   731  O O   . ASP   A 1 91  ? -9.140  57.766 1.249   1.00 83.53  ? 131 ASP   A O   1 
ATOM   732  C CB  . ASP   A 1 91  ? -7.703  60.269 1.447   1.00 89.20  ? 131 ASP   A CB  1 
ATOM   733  C CG  . ASP   A 1 91  ? -8.137  60.692 0.051   1.00 95.13  ? 131 ASP   A CG  1 
ATOM   734  O OD1 . ASP   A 1 91  ? -9.349  60.887 -0.181  1.00 100.45 ? 131 ASP   A OD1 1 
ATOM   735  O OD2 . ASP   A 1 91  ? -7.251  60.830 -0.823  1.00 95.54  ? 131 ASP   A OD2 1 
ATOM   736  N N   . ALA   A 1 92  ? -11.025 58.875 1.803   1.00 82.62  ? 132 ALA   A N   1 
ATOM   737  C CA  . ALA   A 1 92  ? -11.894 57.794 1.353   1.00 79.21  ? 132 ALA   A CA  1 
ATOM   738  C C   . ALA   A 1 92  ? -11.722 57.504 -0.131  1.00 77.93  ? 132 ALA   A C   1 
ATOM   739  O O   . ALA   A 1 92  ? -11.806 56.342 -0.547  1.00 77.73  ? 132 ALA   A O   1 
ATOM   740  C CB  . ALA   A 1 92  ? -13.353 58.132 1.659   1.00 81.02  ? 132 ALA   A CB  1 
ATOM   741  N N   . LYS   A 1 93  ? -11.491 58.537 -0.947  1.00 80.34  ? 133 LYS   A N   1 
ATOM   742  C CA  . LYS   A 1 93  ? -11.258 58.293 -2.367  1.00 79.16  ? 133 LYS   A CA  1 
ATOM   743  C C   . LYS   A 1 93  ? -9.966  57.522 -2.582  1.00 71.83  ? 133 LYS   A C   1 
ATOM   744  O O   . LYS   A 1 93  ? -9.884  56.673 -3.476  1.00 70.52  ? 133 LYS   A O   1 
ATOM   745  C CB  . LYS   A 1 93  ? -11.222 59.604 -3.150  1.00 85.26  ? 133 LYS   A CB  1 
ATOM   746  C CG  . LYS   A 1 93  ? -10.990 59.369 -4.636  1.00 89.63  ? 133 LYS   A CG  1 
ATOM   747  C CD  . LYS   A 1 93  ? -10.704 60.635 -5.412  1.00 97.51  ? 133 LYS   A CD  1 
ATOM   748  C CE  . LYS   A 1 93  ? -10.421 60.293 -6.869  1.00 101.07 ? 133 LYS   A CE  1 
ATOM   749  N NZ  . LYS   A 1 93  ? -10.251 61.505 -7.715  1.00 109.62 ? 133 LYS   A NZ  1 
ATOM   750  N N   . ALA   A 1 94  ? -8.943  57.806 -1.774  1.00 70.45  ? 134 ALA   A N   1 
ATOM   751  C CA  . ALA   A 1 94  ? -7.692  57.067 -1.884  1.00 66.10  ? 134 ALA   A CA  1 
ATOM   752  C C   . ALA   A 1 94  ? -7.909  55.586 -1.603  1.00 66.72  ? 134 ALA   A C   1 
ATOM   753  O O   . ALA   A 1 94  ? -7.397  54.727 -2.331  1.00 62.39  ? 134 ALA   A O   1 
ATOM   754  C CB  . ALA   A 1 94  ? -6.651  57.652 -0.932  1.00 67.36  ? 134 ALA   A CB  1 
ATOM   755  N N   . ILE   A 1 95  ? -8.676  55.268 -0.556  1.00 73.23  ? 135 ILE   A N   1 
ATOM   756  C CA  . ILE   A 1 95  ? -9.015  53.873 -0.272  1.00 72.05  ? 135 ILE   A CA  1 
ATOM   757  C C   . ILE   A 1 95  ? -9.735  53.259 -1.463  1.00 71.27  ? 135 ILE   A C   1 
ATOM   758  O O   . ILE   A 1 95  ? -9.408  52.155 -1.916  1.00 65.69  ? 135 ILE   A O   1 
ATOM   759  C CB  . ILE   A 1 95  ? -9.875  53.774 1.002   1.00 74.56  ? 135 ILE   A CB  1 
ATOM   760  C CG1 . ILE   A 1 95  ? -9.155  54.389 2.201   1.00 74.34  ? 135 ILE   A CG1 1 
ATOM   761  C CG2 . ILE   A 1 95  ? -10.236 52.322 1.281   1.00 71.10  ? 135 ILE   A CG2 1 
ATOM   762  C CD1 . ILE   A 1 95  ? -7.992  53.564 2.696   1.00 71.54  ? 135 ILE   A CD1 1 
ATOM   763  N N   . TYR   A 1 96  ? -10.726 53.976 -1.989  1.00 75.74  ? 136 TYR   A N   1 
ATOM   764  C CA  . TYR   A 1 96  ? -11.500 53.473 -3.117  1.00 77.83  ? 136 TYR   A CA  1 
ATOM   765  C C   . TYR   A 1 96  ? -10.621 53.292 -4.348  1.00 69.44  ? 136 TYR   A C   1 
ATOM   766  O O   . TYR   A 1 96  ? -10.707 52.273 -5.041  1.00 68.61  ? 136 TYR   A O   1 
ATOM   767  C CB  . TYR   A 1 96  ? -12.658 54.427 -3.407  1.00 88.42  ? 136 TYR   A CB  1 
ATOM   768  C CG  . TYR   A 1 96  ? -13.623 53.920 -4.444  1.00 93.88  ? 136 TYR   A CG  1 
ATOM   769  C CD1 . TYR   A 1 96  ? -13.537 54.342 -5.763  1.00 97.42  ? 136 TYR   A CD1 1 
ATOM   770  C CD2 . TYR   A 1 96  ? -14.618 53.015 -4.107  1.00 99.67  ? 136 TYR   A CD2 1 
ATOM   771  C CE1 . TYR   A 1 96  ? -14.421 53.882 -6.719  1.00 104.43 ? 136 TYR   A CE1 1 
ATOM   772  C CE2 . TYR   A 1 96  ? -15.507 52.547 -5.055  1.00 106.56 ? 136 TYR   A CE2 1 
ATOM   773  C CZ  . TYR   A 1 96  ? -15.404 52.984 -6.361  1.00 109.23 ? 136 TYR   A CZ  1 
ATOM   774  O OH  . TYR   A 1 96  ? -16.286 52.526 -7.314  1.00 113.91 ? 136 TYR   A OH  1 
ATOM   775  N N   . ASP   A 1 97  ? -9.768  54.279 -4.638  1.00 71.31  ? 137 ASP   A N   1 
ATOM   776  C CA  . ASP   A 1 97  ? -8.876  54.167 -5.788  1.00 70.52  ? 137 ASP   A CA  1 
ATOM   777  C C   . ASP   A 1 97  ? -7.882  53.030 -5.616  1.00 65.37  ? 137 ASP   A C   1 
ATOM   778  O O   . ASP   A 1 97  ? -7.470  52.413 -6.605  1.00 64.14  ? 137 ASP   A O   1 
ATOM   779  C CB  . ASP   A 1 97  ? -8.125  55.481 -6.014  1.00 73.52  ? 137 ASP   A CB  1 
ATOM   780  C CG  . ASP   A 1 97  ? -9.038  56.616 -6.430  1.00 80.80  ? 137 ASP   A CG  1 
ATOM   781  O OD1 . ASP   A 1 97  ? -10.272 56.436 -6.391  1.00 86.83  ? 137 ASP   A OD1 1 
ATOM   782  O OD2 . ASP   A 1 97  ? -8.518  57.689 -6.798  1.00 84.33  ? 137 ASP   A OD2 1 
ATOM   783  N N   . PHE   A 1 98  ? -7.479  52.741 -4.376  1.00 66.25  ? 138 PHE   A N   1 
ATOM   784  C CA  . PHE   A 1 98  ? -6.526  51.658 -4.150  1.00 63.98  ? 138 PHE   A CA  1 
ATOM   785  C C   . PHE   A 1 98  ? -7.166  50.302 -4.409  1.00 59.90  ? 138 PHE   A C   1 
ATOM   786  O O   . PHE   A 1 98  ? -6.592  49.458 -5.107  1.00 55.46  ? 138 PHE   A O   1 
ATOM   787  C CB  . PHE   A 1 98  ? -5.969  51.718 -2.729  1.00 61.22  ? 138 PHE   A CB  1 
ATOM   788  C CG  . PHE   A 1 98  ? -4.945  50.659 -2.445  1.00 55.53  ? 138 PHE   A CG  1 
ATOM   789  C CD1 . PHE   A 1 98  ? -3.615  50.859 -2.775  1.00 56.48  ? 138 PHE   A CD1 1 
ATOM   790  C CD2 . PHE   A 1 98  ? -5.311  49.459 -1.859  1.00 53.53  ? 138 PHE   A CD2 1 
ATOM   791  C CE1 . PHE   A 1 98  ? -2.666  49.882 -2.523  1.00 51.71  ? 138 PHE   A CE1 1 
ATOM   792  C CE2 . PHE   A 1 98  ? -4.366  48.478 -1.602  1.00 48.14  ? 138 PHE   A CE2 1 
ATOM   793  C CZ  . PHE   A 1 98  ? -3.043  48.690 -1.934  1.00 46.60  ? 138 PHE   A CZ  1 
ATOM   794  N N   . THR   A 1 99  ? -8.353  50.070 -3.841  1.00 59.98  ? 139 THR   A N   1 
ATOM   795  C CA  . THR   A 1 99  ? -9.068  48.828 -4.115  1.00 57.91  ? 139 THR   A CA  1 
ATOM   796  C C   . THR   A 1 99  ? -9.306  48.660 -5.608  1.00 59.45  ? 139 THR   A C   1 
ATOM   797  O O   . THR   A 1 99  ? -9.191  47.552 -6.146  1.00 57.70  ? 139 THR   A O   1 
ATOM   798  C CB  . THR   A 1 99  ? -10.389 48.806 -3.351  1.00 61.66  ? 139 THR   A CB  1 
ATOM   799  O OG1 . THR   A 1 99  ? -10.122 48.786 -1.944  1.00 61.08  ? 139 THR   A OG1 1 
ATOM   800  C CG2 . THR   A 1 99  ? -11.201 47.579 -3.727  1.00 61.20  ? 139 THR   A CG2 1 
ATOM   801  N N   . ASP   A 1 100 ? -9.611  49.757 -6.300  1.00 62.22  ? 140 ASP   A N   1 
ATOM   802  C CA  . ASP   A 1 100 ? -9.743  49.701 -7.749  1.00 65.67  ? 140 ASP   A CA  1 
ATOM   803  C C   . ASP   A 1 100 ? -8.430  49.295 -8.408  1.00 59.17  ? 140 ASP   A C   1 
ATOM   804  O O   . ASP   A 1 100 ? -8.424  48.527 -9.377  1.00 57.56  ? 140 ASP   A O   1 
ATOM   805  C CB  . ASP   A 1 100 ? -10.214 51.054 -8.275  1.00 80.38  ? 140 ASP   A CB  1 
ATOM   806  C CG  . ASP   A 1 100 ? -10.784 50.968 -9.671  1.00 93.75  ? 140 ASP   A CG  1 
ATOM   807  O OD1 . ASP   A 1 100 ? -10.919 49.838 -10.187 1.00 96.60  ? 140 ASP   A OD1 1 
ATOM   808  O OD2 . ASP   A 1 100 ? -11.101 52.029 -10.249 1.00 103.59 ? 140 ASP   A OD2 1 
ATOM   809  N N   . THR   A 1 101 ? -7.304  49.795 -7.891  1.00 55.97  ? 141 THR   A N   1 
ATOM   810  C CA  . THR   A 1 101 ? -6.010  49.469 -8.485  1.00 53.36  ? 141 THR   A CA  1 
ATOM   811  C C   . THR   A 1 101 ? -5.643  48.010 -8.243  1.00 52.78  ? 141 THR   A C   1 
ATOM   812  O O   . THR   A 1 101 ? -5.081  47.352 -9.128  1.00 51.08  ? 141 THR   A O   1 
ATOM   813  C CB  . THR   A 1 101 ? -4.929  50.397 -7.928  1.00 52.50  ? 141 THR   A CB  1 
ATOM   814  O OG1 . THR   A 1 101 ? -5.254  51.753 -8.257  1.00 59.90  ? 141 THR   A OG1 1 
ATOM   815  C CG2 . THR   A 1 101 ? -3.571  50.060 -8.517  1.00 50.76  ? 141 THR   A CG2 1 
ATOM   816  N N   . VAL   A 1 102 ? -5.951  47.489 -7.052  1.00 55.80  ? 142 VAL   A N   1 
ATOM   817  C CA  . VAL   A 1 102 ? -5.700  46.076 -6.767  1.00 55.29  ? 142 VAL   A CA  1 
ATOM   818  C C   . VAL   A 1 102 ? -6.431  45.195 -7.772  1.00 53.29  ? 142 VAL   A C   1 
ATOM   819  O O   . VAL   A 1 102 ? -5.865  44.238 -8.312  1.00 50.08  ? 142 VAL   A O   1 
ATOM   820  C CB  . VAL   A 1 102 ? -6.108  45.747 -5.317  1.00 52.45  ? 142 VAL   A CB  1 
ATOM   821  C CG1 . VAL   A 1 102 ? -6.139  44.250 -5.096  1.00 47.22  ? 142 VAL   A CG1 1 
ATOM   822  C CG2 . VAL   A 1 102 ? -5.152  46.407 -4.338  1.00 50.42  ? 142 VAL   A CG2 1 
ATOM   823  N N   . ILE   A 1 103 ? -7.691  45.522 -8.057  1.00 56.32  ? 143 ILE   A N   1 
ATOM   824  C CA  . ILE   A 1 103 ? -8.472  44.744 -9.016  1.00 58.90  ? 143 ILE   A CA  1 
ATOM   825  C C   . ILE   A 1 103 ? -7.860  44.835 -10.410 1.00 60.62  ? 143 ILE   A C   1 
ATOM   826  O O   . ILE   A 1 103 ? -7.757  43.830 -11.125 1.00 59.47  ? 143 ILE   A O   1 
ATOM   827  C CB  . ILE   A 1 103 ? -9.936  45.219 -8.996  1.00 59.11  ? 143 ILE   A CB  1 
ATOM   828  C CG1 . ILE   A 1 103 ? -10.571 44.875 -7.648  1.00 58.49  ? 143 ILE   A CG1 1 
ATOM   829  C CG2 . ILE   A 1 103 ? -10.728 44.633 -10.161 1.00 58.71  ? 143 ILE   A CG2 1 
ATOM   830  C CD1 . ILE   A 1 103 ? -11.836 45.650 -7.353  1.00 62.19  ? 143 ILE   A CD1 1 
ATOM   831  N N   . ARG   A 1 104 ? -7.433  46.035 -10.811 1.00 59.30  ? 144 ARG   A N   1 
ATOM   832  C CA  . ARG   A 1 104 ? -6.804  46.208 -12.117 1.00 59.12  ? 144 ARG   A CA  1 
ATOM   833  C C   . ARG   A 1 104 ? -5.547  45.356 -12.233 1.00 55.19  ? 144 ARG   A C   1 
ATOM   834  O O   . ARG   A 1 104 ? -5.344  44.656 -13.233 1.00 53.21  ? 144 ARG   A O   1 
ATOM   835  C CB  . ARG   A 1 104 ? -6.478  47.687 -12.348 1.00 65.80  ? 144 ARG   A CB  1 
ATOM   836  C CG  . ARG   A 1 104 ? -5.881  48.003 -13.718 1.00 73.31  ? 144 ARG   A CG  1 
ATOM   837  C CD  . ARG   A 1 104 ? -5.521  49.484 -13.872 1.00 78.30  ? 144 ARG   A CD  1 
ATOM   838  N NE  . ARG   A 1 104 ? -6.388  50.358 -13.083 1.00 84.88  ? 144 ARG   A NE  1 
ATOM   839  C CZ  . ARG   A 1 104 ? -5.965  51.107 -12.067 1.00 87.52  ? 144 ARG   A CZ  1 
ATOM   840  N NH1 . ARG   A 1 104 ? -4.681  51.101 -11.726 1.00 85.46  ? 144 ARG   A NH1 1 
ATOM   841  N NH2 . ARG   A 1 104 ? -6.822  51.870 -11.399 1.00 89.37  ? 144 ARG   A NH2 1 
ATOM   842  N N   . ILE   A 1 105 ? -4.692  45.399 -11.209 1.00 53.28  ? 145 ILE   A N   1 
ATOM   843  C CA  . ILE   A 1 105 ? -3.459  44.617 -11.227 1.00 49.12  ? 145 ILE   A CA  1 
ATOM   844  C C   . ILE   A 1 105 ? -3.771  43.127 -11.266 1.00 50.38  ? 145 ILE   A C   1 
ATOM   845  O O   . ILE   A 1 105 ? -3.133  42.364 -12.004 1.00 50.60  ? 145 ILE   A O   1 
ATOM   846  C CB  . ILE   A 1 105 ? -2.581  44.985 -10.018 1.00 43.51  ? 145 ILE   A CB  1 
ATOM   847  C CG1 . ILE   A 1 105 ? -2.066  46.416 -10.170 1.00 42.79  ? 145 ILE   A CG1 1 
ATOM   848  C CG2 . ILE   A 1 105 ? -1.423  44.003 -9.871  1.00 38.06  ? 145 ILE   A CG2 1 
ATOM   849  C CD1 . ILE   A 1 105 ? -1.404  46.962 -8.929  1.00 42.99  ? 145 ILE   A CD1 1 
ATOM   850  N N   . ARG   A 1 106 ? -4.759  42.690 -10.481 1.00 49.37  ? 146 ARG   A N   1 
ATOM   851  C CA  . ARG   A 1 106 ? -5.118  41.277 -10.471 1.00 49.22  ? 146 ARG   A CA  1 
ATOM   852  C C   . ARG   A 1 106 ? -5.455  40.788 -11.874 1.00 52.85  ? 146 ARG   A C   1 
ATOM   853  O O   . ARG   A 1 106 ? -4.972  39.738 -12.311 1.00 54.02  ? 146 ARG   A O   1 
ATOM   854  C CB  . ARG   A 1 106 ? -6.292  41.027 -9.524  1.00 47.82  ? 146 ARG   A CB  1 
ATOM   855  C CG  . ARG   A 1 106 ? -6.671  39.562 -9.484  1.00 53.22  ? 146 ARG   A CG  1 
ATOM   856  C CD  . ARG   A 1 106 ? -7.733  39.233 -8.460  1.00 58.70  ? 146 ARG   A CD  1 
ATOM   857  N NE  . ARG   A 1 106 ? -9.075  39.520 -8.947  1.00 71.14  ? 146 ARG   A NE  1 
ATOM   858  C CZ  . ARG   A 1 106 ? -10.172 38.944 -8.470  1.00 75.30  ? 146 ARG   A CZ  1 
ATOM   859  N NH1 . ARG   A 1 106 ? -10.079 38.036 -7.507  1.00 74.37  ? 146 ARG   A NH1 1 
ATOM   860  N NH2 . ARG   A 1 106 ? -11.358 39.267 -8.963  1.00 78.69  ? 146 ARG   A NH2 1 
ATOM   861  N N   . ASN   A 1 107 ? -6.274  41.546 -12.603 1.00 52.28  ? 147 ASN   A N   1 
ATOM   862  C CA  . ASN   A 1 107 ? -6.628  41.131 -13.955 1.00 52.81  ? 147 ASN   A CA  1 
ATOM   863  C C   . ASN   A 1 107 ? -5.432  41.217 -14.897 1.00 51.81  ? 147 ASN   A C   1 
ATOM   864  O O   . ASN   A 1 107 ? -5.224  40.318 -15.718 1.00 51.93  ? 147 ASN   A O   1 
ATOM   865  C CB  . ASN   A 1 107 ? -7.794  41.970 -14.473 1.00 58.56  ? 147 ASN   A CB  1 
ATOM   866  C CG  . ASN   A 1 107 ? -9.068  41.731 -13.691 1.00 65.88  ? 147 ASN   A CG  1 
ATOM   867  O OD1 . ASN   A 1 107 ? -9.261  40.662 -13.110 1.00 70.53  ? 147 ASN   A OD1 1 
ATOM   868  N ND2 . ASN   A 1 107 ? -9.945  42.728 -13.668 1.00 71.94  ? 147 ASN   A ND2 1 
ATOM   869  N N   . ARG   A 1 108 ? -4.626  42.280 -14.788 1.00 53.06  ? 148 ARG   A N   1 
ATOM   870  C CA  . ARG   A 1 108 ? -3.443  42.401 -15.641 1.00 56.76  ? 148 ARG   A CA  1 
ATOM   871  C C   . ARG   A 1 108 ? -2.512  41.203 -15.481 1.00 52.55  ? 148 ARG   A C   1 
ATOM   872  O O   . ARG   A 1 108 ? -1.882  40.768 -16.454 1.00 53.79  ? 148 ARG   A O   1 
ATOM   873  C CB  . ARG   A 1 108 ? -2.690  43.701 -15.325 1.00 60.52  ? 148 ARG   A CB  1 
ATOM   874  C CG  . ARG   A 1 108 ? -1.436  43.927 -16.178 1.00 61.57  ? 148 ARG   A CG  1 
ATOM   875  C CD  . ARG   A 1 108 ? -0.642  45.175 -15.761 1.00 62.07  ? 148 ARG   A CD  1 
ATOM   876  N NE  . ARG   A 1 108 ? -1.385  46.421 -15.958 1.00 67.90  ? 148 ARG   A NE  1 
ATOM   877  C CZ  . ARG   A 1 108 ? -1.652  47.300 -14.994 1.00 68.81  ? 148 ARG   A CZ  1 
ATOM   878  N NH1 . ARG   A 1 108 ? -1.225  47.091 -13.753 1.00 62.11  ? 148 ARG   A NH1 1 
ATOM   879  N NH2 . ARG   A 1 108 ? -2.338  48.401 -15.272 1.00 69.68  ? 148 ARG   A NH2 1 
ATOM   880  N N   . HIS   A 1 109 ? -2.433  40.642 -14.275 1.00 60.21  ? 149 HIS   A N   1 
ATOM   881  C CA  . HIS   A 1 109 ? -1.514  39.556 -13.964 1.00 56.01  ? 149 HIS   A CA  1 
ATOM   882  C C   . HIS   A 1 109 ? -2.154  38.173 -14.071 1.00 53.80  ? 149 HIS   A C   1 
ATOM   883  O O   . HIS   A 1 109 ? -1.493  37.179 -13.745 1.00 47.63  ? 149 HIS   A O   1 
ATOM   884  C CB  . HIS   A 1 109 ? -0.929  39.749 -12.556 1.00 46.65  ? 149 HIS   A CB  1 
ATOM   885  C CG  . HIS   A 1 109 ? -0.005  40.923 -12.433 1.00 48.42  ? 149 HIS   A CG  1 
ATOM   886  N ND1 . HIS   A 1 109 ? 1.156   40.881 -11.693 1.00 52.87  ? 149 HIS   A ND1 1 
ATOM   887  C CD2 . HIS   A 1 109 ? -0.073  42.172 -12.949 1.00 53.60  ? 149 HIS   A CD2 1 
ATOM   888  C CE1 . HIS   A 1 109 ? 1.768   42.050 -11.765 1.00 51.68  ? 149 HIS   A CE1 1 
ATOM   889  N NE2 . HIS   A 1 109 ? 1.042   42.852 -12.521 1.00 51.69  ? 149 HIS   A NE2 1 
ATOM   890  N N   . ASN   A 1 110 ? -3.411  38.081 -14.534 1.00 53.26  ? 150 ASN   A N   1 
ATOM   891  C CA  A ASN   A 1 110 ? -4.122  36.803 -14.615 0.50 52.26  ? 150 ASN   A CA  1 
ATOM   892  C CA  B ASN   A 1 110 ? -4.065  36.778 -14.520 0.50 52.02  ? 150 ASN   A CA  1 
ATOM   893  C C   . ASN   A 1 110 ? -3.328  35.746 -15.367 1.00 49.62  ? 150 ASN   A C   1 
ATOM   894  O O   . ASN   A 1 110 ? -3.466  34.548 -15.100 1.00 53.82  ? 150 ASN   A O   1 
ATOM   895  C CB  A ASN   A 1 110 ? -5.471  37.000 -15.313 0.50 57.61  ? 150 ASN   A CB  1 
ATOM   896  C CB  B ASN   A 1 110 ? -5.536  36.887 -14.957 0.50 57.24  ? 150 ASN   A CB  1 
ATOM   897  C CG  A ASN   A 1 110 ? -6.636  37.023 -14.349 0.50 61.84  ? 150 ASN   A CG  1 
ATOM   898  C CG  B ASN   A 1 110 ? -5.715  37.512 -16.334 0.50 59.59  ? 150 ASN   A CG  1 
ATOM   899  O OD1 A ASN   A 1 110 ? -6.620  36.349 -13.320 0.50 60.04  ? 150 ASN   A OD1 1 
ATOM   900  O OD1 B ASN   A 1 110 ? -4.789  37.576 -17.139 0.50 57.04  ? 150 ASN   A OD1 1 
ATOM   901  N ND2 A ASN   A 1 110 ? -7.668  37.792 -14.688 0.50 70.44  ? 150 ASN   A ND2 1 
ATOM   902  N ND2 B ASN   A 1 110 ? -6.929  37.978 -16.606 0.50 68.25  ? 150 ASN   A ND2 1 
ATOM   903  N N   . ASP   A 1 111 ? -2.517  36.168 -16.335 1.00 47.79  ? 151 ASP   A N   1 
ATOM   904  C CA  . ASP   A 1 111 ? -1.848  35.231 -17.226 1.00 46.40  ? 151 ASP   A CA  1 
ATOM   905  C C   . ASP   A 1 111 ? -0.338  35.166 -17.010 1.00 44.12  ? 151 ASP   A C   1 
ATOM   906  O O   . ASP   A 1 111 ? 0.394   34.756 -17.918 1.00 42.15  ? 151 ASP   A O   1 
ATOM   907  C CB  . ASP   A 1 111 ? -2.162  35.588 -18.676 1.00 58.26  ? 151 ASP   A CB  1 
ATOM   908  C CG  . ASP   A 1 111 ? -2.281  34.367 -19.549 1.00 71.53  ? 151 ASP   A CG  1 
ATOM   909  O OD1 . ASP   A 1 111 ? -3.072  33.470 -19.186 1.00 80.38  ? 151 ASP   A OD1 1 
ATOM   910  O OD2 . ASP   A 1 111 ? -1.586  34.296 -20.585 1.00 72.54  ? 151 ASP   A OD2 1 
ATOM   911  N N   . VAL   A 1 112 ? 0.138   35.533 -15.817 1.00 42.46  ? 152 VAL   A N   1 
ATOM   912  C CA  . VAL   A 1 112 ? 1.575   35.611 -15.572 1.00 38.93  ? 152 VAL   A CA  1 
ATOM   913  C C   . VAL   A 1 112 ? 2.222   34.236 -15.699 1.00 39.61  ? 152 VAL   A C   1 
ATOM   914  O O   . VAL   A 1 112 ? 3.268   34.084 -16.342 1.00 39.68  ? 152 VAL   A O   1 
ATOM   915  C CB  . VAL   A 1 112 ? 1.852   36.242 -14.195 1.00 40.68  ? 152 VAL   A CB  1 
ATOM   916  C CG1 . VAL   A 1 112 ? 3.221   35.839 -13.682 1.00 40.32  ? 152 VAL   A CG1 1 
ATOM   917  C CG2 . VAL   A 1 112 ? 1.766   37.761 -14.285 1.00 47.57  ? 152 VAL   A CG2 1 
ATOM   918  N N   . ILE   A 1 113 ? 1.623   33.215 -15.080 1.00 41.91  ? 153 ILE   A N   1 
ATOM   919  C CA  . ILE   A 1 113 ? 2.254   31.892 -15.070 1.00 40.42  ? 153 ILE   A CA  1 
ATOM   920  C C   . ILE   A 1 113 ? 2.415   31.324 -16.476 1.00 39.10  ? 153 ILE   A C   1 
ATOM   921  O O   . ILE   A 1 113 ? 3.541   30.941 -16.834 1.00 37.83  ? 153 ILE   A O   1 
ATOM   922  C CB  . ILE   A 1 113 ? 1.502   30.946 -14.115 1.00 38.84  ? 153 ILE   A CB  1 
ATOM   923  C CG1 . ILE   A 1 113 ? 1.767   31.342 -12.663 1.00 39.28  ? 153 ILE   A CG1 1 
ATOM   924  C CG2 . ILE   A 1 113 ? 1.940   29.513 -14.344 1.00 38.58  ? 153 ILE   A CG2 1 
ATOM   925  C CD1 . ILE   A 1 113 ? 1.269   30.326 -11.649 1.00 41.99  ? 153 ILE   A CD1 1 
ATOM   926  N N   . PRO   A 1 114 ? 1.378   31.259 -17.323 1.00 43.58  ? 154 PRO   A N   1 
ATOM   927  C CA  . PRO   A 1 114 ? 1.610   30.735 -18.682 1.00 43.94  ? 154 PRO   A CA  1 
ATOM   928  C C   . PRO   A 1 114 ? 2.444   31.656 -19.560 1.00 41.81  ? 154 PRO   A C   1 
ATOM   929  O O   . PRO   A 1 114 ? 3.135   31.164 -20.460 1.00 40.17  ? 154 PRO   A O   1 
ATOM   930  C CB  . PRO   A 1 114 ? 0.192   30.539 -19.240 1.00 47.53  ? 154 PRO   A CB  1 
ATOM   931  C CG  . PRO   A 1 114 ? -0.675  31.408 -18.424 1.00 55.29  ? 154 PRO   A CG  1 
ATOM   932  C CD  . PRO   A 1 114 ? -0.058  31.478 -17.061 1.00 47.72  ? 154 PRO   A CD  1 
ATOM   933  N N   . THR   A 1 115 ? 2.423   32.973 -19.329 1.00 43.02  ? 155 THR   A N   1 
ATOM   934  C CA  . THR   A 1 115 ? 3.256   33.852 -20.145 1.00 45.73  ? 155 THR   A CA  1 
ATOM   935  C C   . THR   A 1 115 ? 4.730   33.672 -19.807 1.00 37.79  ? 155 THR   A C   1 
ATOM   936  O O   . THR   A 1 115 ? 5.579   33.637 -20.709 1.00 39.54  ? 155 THR   A O   1 
ATOM   937  C CB  . THR   A 1 115 ? 2.830   35.313 -19.975 1.00 46.61  ? 155 THR   A CB  1 
ATOM   938  O OG1 . THR   A 1 115 ? 1.439   35.449 -20.302 1.00 45.33  ? 155 THR   A OG1 1 
ATOM   939  C CG2 . THR   A 1 115 ? 3.631   36.212 -20.907 1.00 42.62  ? 155 THR   A CG2 1 
ATOM   940  N N   . MET   A 1 116 ? 5.051   33.548 -18.518 1.00 34.71  ? 156 MET   A N   1 
ATOM   941  C CA  . MET   A 1 116 ? 6.414   33.211 -18.124 1.00 37.81  ? 156 MET   A CA  1 
ATOM   942  C C   . MET   A 1 116 ? 6.831   31.867 -18.713 1.00 38.32  ? 156 MET   A C   1 
ATOM   943  O O   . MET   A 1 116 ? 7.940   31.732 -19.249 1.00 37.46  ? 156 MET   A O   1 
ATOM   944  C CB  . MET   A 1 116 ? 6.527   33.207 -16.597 1.00 36.67  ? 156 MET   A CB  1 
ATOM   945  C CG  . MET   A 1 116 ? 7.900   32.822 -16.050 1.00 37.24  ? 156 MET   A CG  1 
ATOM   946  S SD  . MET   A 1 116 ? 9.258   33.819 -16.705 1.00 39.00  ? 156 MET   A SD  1 
ATOM   947  C CE  . MET   A 1 116 ? 9.072   35.357 -15.796 1.00 39.32  ? 156 MET   A CE  1 
ATOM   948  N N   . ALA   A 1 117 ? 5.947   30.868 -18.643 1.00 36.43  ? 157 ALA   A N   1 
ATOM   949  C CA  . ALA   A 1 117 ? 6.237   29.580 -19.264 1.00 38.96  ? 157 ALA   A CA  1 
ATOM   950  C C   . ALA   A 1 117 ? 6.452   29.721 -20.763 1.00 40.45  ? 157 ALA   A C   1 
ATOM   951  O O   . ALA   A 1 117 ? 7.254   28.985 -21.349 1.00 40.45  ? 157 ALA   A O   1 
ATOM   952  C CB  . ALA   A 1 117 ? 5.103   28.590 -18.987 1.00 43.72  ? 157 ALA   A CB  1 
ATOM   953  N N   . GLN   A 1 118 ? 5.740   30.648 -21.406 1.00 43.17  ? 158 GLN   A N   1 
ATOM   954  C CA  . GLN   A 1 118 ? 5.962   30.867 -22.828 1.00 44.26  ? 158 GLN   A CA  1 
ATOM   955  C C   . GLN   A 1 118 ? 7.353   31.429 -23.090 1.00 42.91  ? 158 GLN   A C   1 
ATOM   956  O O   . GLN   A 1 118 ? 7.953   31.136 -24.131 1.00 44.37  ? 158 GLN   A O   1 
ATOM   957  C CB  . GLN   A 1 118 ? 4.894   31.802 -23.393 1.00 41.11  ? 158 GLN   A CB  1 
ATOM   958  C CG  . GLN   A 1 118 ? 4.940   31.914 -24.896 1.00 50.08  ? 158 GLN   A CG  1 
ATOM   959  C CD  . GLN   A 1 118 ? 4.624   30.597 -25.570 1.00 58.34  ? 158 GLN   A CD  1 
ATOM   960  O OE1 . GLN   A 1 118 ? 3.630   29.946 -25.242 1.00 60.81  ? 158 GLN   A OE1 1 
ATOM   961  N NE2 . GLN   A 1 118 ? 5.476   30.188 -26.507 1.00 58.47  ? 158 GLN   A NE2 1 
ATOM   962  N N   . GLY   A 1 119 ? 7.880   32.226 -22.160 1.00 43.54  ? 159 GLY   A N   1 
ATOM   963  C CA  . GLY   A 1 119 ? 9.221   32.761 -22.333 1.00 47.61  ? 159 GLY   A CA  1 
ATOM   964  C C   . GLY   A 1 119 ? 10.292  31.691 -22.255 1.00 41.19  ? 159 GLY   A C   1 
ATOM   965  O O   . GLY   A 1 119 ? 11.289  31.742 -22.985 1.00 39.97  ? 159 GLY   A O   1 
ATOM   966  N N   . VAL   A 1 120 ? 10.103  30.708 -21.371 1.00 35.71  ? 160 VAL   A N   1 
ATOM   967  C CA  . VAL   A 1 120 ? 11.032  29.584 -21.301 1.00 38.69  ? 160 VAL   A CA  1 
ATOM   968  C C   . VAL   A 1 120 ? 10.991  28.788 -22.595 1.00 38.11  ? 160 VAL   A C   1 
ATOM   969  O O   . VAL   A 1 120 ? 12.021  28.296 -23.075 1.00 42.79  ? 160 VAL   A O   1 
ATOM   970  C CB  . VAL   A 1 120 ? 10.714  28.700 -20.082 1.00 39.69  ? 160 VAL   A CB  1 
ATOM   971  C CG1 . VAL   A 1 120 ? 11.690  27.529 -19.999 1.00 36.42  ? 160 VAL   A CG1 1 
ATOM   972  C CG2 . VAL   A 1 120 ? 10.761  29.523 -18.811 1.00 40.27  ? 160 VAL   A CG2 1 
ATOM   973  N N   . ILE   A 1 121 ? 9.804   28.647 -23.185 1.00 39.96  ? 161 ILE   A N   1 
ATOM   974  C CA  . ILE   A 1 121 ? 9.699   27.976 -24.477 1.00 41.21  ? 161 ILE   A CA  1 
ATOM   975  C C   . ILE   A 1 121 ? 10.479  28.751 -25.530 1.00 42.04  ? 161 ILE   A C   1 
ATOM   976  O O   . ILE   A 1 121 ? 11.254  28.177 -26.306 1.00 42.11  ? 161 ILE   A O   1 
ATOM   977  C CB  . ILE   A 1 121 ? 8.222   27.806 -24.872 1.00 44.58  ? 161 ILE   A CB  1 
ATOM   978  C CG1 . ILE   A 1 121 ? 7.508   26.888 -23.882 1.00 46.93  ? 161 ILE   A CG1 1 
ATOM   979  C CG2 . ILE   A 1 121 ? 8.095   27.282 -26.294 1.00 48.86  ? 161 ILE   A CG2 1 
ATOM   980  C CD1 . ILE   A 1 121 ? 6.037   26.748 -24.151 1.00 50.54  ? 161 ILE   A CD1 1 
ATOM   981  N N   . GLU   A 1 122 ? 10.295  30.075 -25.562 1.00 42.82  ? 162 GLU   A N   1 
ATOM   982  C CA  . GLU   A 1 122 ? 10.995  30.902 -26.540 1.00 44.56  ? 162 GLU   A CA  1 
ATOM   983  C C   . GLU   A 1 122 ? 12.502  30.808 -26.349 1.00 43.52  ? 162 GLU   A C   1 
ATOM   984  O O   . GLU   A 1 122 ? 13.259  30.694 -27.322 1.00 46.97  ? 162 GLU   A O   1 
ATOM   985  C CB  . GLU   A 1 122 ? 10.533  32.357 -26.423 1.00 46.66  ? 162 GLU   A CB  1 
ATOM   986  C CG  . GLU   A 1 122 ? 9.139   32.638 -26.973 1.00 50.39  ? 162 GLU   A CG  1 
ATOM   987  C CD  . GLU   A 1 122 ? 8.423   33.774 -26.240 1.00 55.17  ? 162 GLU   A CD  1 
ATOM   988  O OE1 . GLU   A 1 122 ? 7.191   33.889 -26.394 1.00 60.65  ? 162 GLU   A OE1 1 
ATOM   989  O OE2 . GLU   A 1 122 ? 9.078   34.545 -25.507 1.00 52.07  ? 162 GLU   A OE2 1 
ATOM   990  N N   . TYR   A 1 123 ? 12.944  30.859 -25.093 1.00 41.25  ? 163 TYR   A N   1 
ATOM   991  C CA  . TYR   A 1 123 ? 14.354  30.717 -24.751 1.00 43.67  ? 163 TYR   A CA  1 
ATOM   992  C C   . TYR   A 1 123 ? 14.905  29.378 -25.222 1.00 41.64  ? 163 TYR   A C   1 
ATOM   993  O O   . TYR   A 1 123 ? 15.933  29.319 -25.907 1.00 44.41  ? 163 TYR   A O   1 
ATOM   994  C CB  . TYR   A 1 123 ? 14.497  30.871 -23.238 1.00 37.14  ? 163 TYR   A CB  1 
ATOM   995  C CG  . TYR   A 1 123 ? 15.858  30.596 -22.664 1.00 39.89  ? 163 TYR   A CG  1 
ATOM   996  C CD1 . TYR   A 1 123 ? 16.977  31.268 -23.124 1.00 46.24  ? 163 TYR   A CD1 1 
ATOM   997  C CD2 . TYR   A 1 123 ? 16.015  29.695 -21.621 1.00 39.44  ? 163 TYR   A CD2 1 
ATOM   998  C CE1 . TYR   A 1 123 ? 18.224  31.029 -22.579 1.00 47.07  ? 163 TYR   A CE1 1 
ATOM   999  C CE2 . TYR   A 1 123 ? 17.253  29.455 -21.066 1.00 38.77  ? 163 TYR   A CE2 1 
ATOM   1000 C CZ  . TYR   A 1 123 ? 18.350  30.124 -21.548 1.00 44.40  ? 163 TYR   A CZ  1 
ATOM   1001 O OH  . TYR   A 1 123 ? 19.582  29.886 -21.000 1.00 54.30  ? 163 TYR   A OH  1 
ATOM   1002 N N   . LYS   A 1 124 ? 14.226  28.290 -24.862 1.00 42.33  ? 164 LYS   A N   1 
ATOM   1003 C CA  . LYS   A 1 124 ? 14.679  26.957 -25.241 1.00 54.29  ? 164 LYS   A CA  1 
ATOM   1004 C C   . LYS   A 1 124 ? 14.668  26.766 -26.754 1.00 62.14  ? 164 LYS   A C   1 
ATOM   1005 O O   . LYS   A 1 124 ? 15.527  26.060 -27.298 1.00 58.76  ? 164 LYS   A O   1 
ATOM   1006 C CB  . LYS   A 1 124 ? 13.796  25.916 -24.549 1.00 51.84  ? 164 LYS   A CB  1 
ATOM   1007 C CG  . LYS   A 1 124 ? 14.441  24.564 -24.316 1.00 54.31  ? 164 LYS   A CG  1 
ATOM   1008 C CD  . LYS   A 1 124 ? 13.604  23.732 -23.347 1.00 50.58  ? 164 LYS   A CD  1 
ATOM   1009 C CE  . LYS   A 1 124 ? 13.838  22.241 -23.565 1.00 54.73  ? 164 LYS   A CE  1 
ATOM   1010 N NZ  . LYS   A 1 124 ? 12.833  21.386 -22.861 1.00 54.94  ? 164 LYS   A NZ  1 
ATOM   1011 N N   . GLU   A 1 125 ? 13.718  27.398 -27.451 1.00 67.63  ? 165 GLU   A N   1 
ATOM   1012 C CA  . GLU   A 1 125 ? 13.609  27.231 -28.898 1.00 70.64  ? 165 GLU   A CA  1 
ATOM   1013 C C   . GLU   A 1 125 ? 14.824  27.786 -29.627 1.00 71.11  ? 165 GLU   A C   1 
ATOM   1014 O O   . GLU   A 1 125 ? 15.318  27.170 -30.578 1.00 77.85  ? 165 GLU   A O   1 
ATOM   1015 C CB  . GLU   A 1 125 ? 12.344  27.914 -29.418 1.00 74.20  ? 165 GLU   A CB  1 
ATOM   1016 C CG  . GLU   A 1 125 ? 11.077  27.077 -29.340 1.00 84.19  ? 165 GLU   A CG  1 
ATOM   1017 C CD  . GLU   A 1 125 ? 9.842   27.849 -29.784 1.00 91.49  ? 165 GLU   A CD  1 
ATOM   1018 O OE1 . GLU   A 1 125 ? 9.951   29.079 -29.994 1.00 90.40  ? 165 GLU   A OE1 1 
ATOM   1019 O OE2 . GLU   A 1 125 ? 8.765   27.225 -29.920 1.00 94.27  ? 165 GLU   A OE2 1 
ATOM   1020 N N   . SER   A 1 126 ? 15.314  28.947 -29.209 1.00 69.23  ? 166 SER   A N   1 
ATOM   1021 C CA  . SER   A 1 126 ? 16.255  29.702 -30.020 1.00 78.20  ? 166 SER   A CA  1 
ATOM   1022 C C   . SER   A 1 126 ? 17.698  29.596 -29.548 1.00 79.91  ? 166 SER   A C   1 
ATOM   1023 O O   . SER   A 1 126 ? 18.595  30.084 -30.244 1.00 85.10  ? 166 SER   A O   1 
ATOM   1024 C CB  . SER   A 1 126 ? 15.836  31.173 -30.053 1.00 85.40  ? 166 SER   A CB  1 
ATOM   1025 O OG  . SER   A 1 126 ? 14.424  31.282 -30.119 1.00 87.09  ? 166 SER   A OG  1 
ATOM   1026 N N   . PHE   A 1 127 ? 17.947  28.982 -28.395 1.00 78.44  ? 167 PHE   A N   1 
ATOM   1027 C CA  . PHE   A 1 127 ? 19.298  28.930 -27.852 1.00 85.12  ? 167 PHE   A CA  1 
ATOM   1028 C C   . PHE   A 1 127 ? 19.643  27.603 -27.200 1.00 95.37  ? 167 PHE   A C   1 
ATOM   1029 O O   . PHE   A 1 127 ? 20.815  27.391 -26.873 1.00 95.95  ? 167 PHE   A O   1 
ATOM   1030 C CB  . PHE   A 1 127 ? 19.502  30.061 -26.831 1.00 81.36  ? 167 PHE   A CB  1 
ATOM   1031 C CG  . PHE   A 1 127 ? 18.976  31.391 -27.294 1.00 79.00  ? 167 PHE   A CG  1 
ATOM   1032 C CD1 . PHE   A 1 127 ? 19.760  32.227 -28.074 1.00 85.19  ? 167 PHE   A CD1 1 
ATOM   1033 C CD2 . PHE   A 1 127 ? 17.691  31.795 -26.969 1.00 73.61  ? 167 PHE   A CD2 1 
ATOM   1034 C CE1 . PHE   A 1 127 ? 19.275  33.451 -28.512 1.00 85.63  ? 167 PHE   A CE1 1 
ATOM   1035 C CE2 . PHE   A 1 127 ? 17.199  33.017 -27.402 1.00 76.89  ? 167 PHE   A CE2 1 
ATOM   1036 C CZ  . PHE   A 1 127 ? 17.992  33.846 -28.176 1.00 81.92  ? 167 PHE   A CZ  1 
ATOM   1037 N N   . GLY   A 1 128 ? 18.678  26.712 -26.993 1.00 105.00 ? 168 GLY   A N   1 
ATOM   1038 C CA  . GLY   A 1 128 ? 18.954  25.412 -26.423 1.00 119.95 ? 168 GLY   A CA  1 
ATOM   1039 C C   . GLY   A 1 128 ? 19.225  25.470 -24.932 1.00 130.59 ? 168 GLY   A C   1 
ATOM   1040 O O   . GLY   A 1 128 ? 19.215  26.524 -24.289 1.00 123.61 ? 168 GLY   A O   1 
ATOM   1041 N N   . VAL   A 1 129 ? 19.472  24.286 -24.373 1.00 145.84 ? 169 VAL   A N   1 
ATOM   1042 C CA  . VAL   A 1 129 ? 19.806  24.186 -22.960 1.00 142.91 ? 169 VAL   A CA  1 
ATOM   1043 C C   . VAL   A 1 129 ? 21.244  24.644 -22.754 1.00 137.82 ? 169 VAL   A C   1 
ATOM   1044 O O   . VAL   A 1 129 ? 22.162  24.226 -23.472 1.00 143.16 ? 169 VAL   A O   1 
ATOM   1045 C CB  . VAL   A 1 129 ? 19.573  22.753 -22.448 1.00 148.72 ? 169 VAL   A CB  1 
ATOM   1046 C CG1 . VAL   A 1 129 ? 20.441  21.744 -23.198 1.00 153.69 ? 169 VAL   A CG1 1 
ATOM   1047 C CG2 . VAL   A 1 129 ? 19.809  22.673 -20.943 1.00 149.17 ? 169 VAL   A CG2 1 
ATOM   1048 N N   . ASP   A 1 130 ? 21.437  25.542 -21.796 1.00 127.85 ? 170 ASP   A N   1 
ATOM   1049 C CA  . ASP   A 1 130 ? 22.764  26.005 -21.414 1.00 120.80 ? 170 ASP   A CA  1 
ATOM   1050 C C   . ASP   A 1 130 ? 23.043  25.511 -20.003 1.00 126.71 ? 170 ASP   A C   1 
ATOM   1051 O O   . ASP   A 1 130 ? 22.408  25.992 -19.051 1.00 121.88 ? 170 ASP   A O   1 
ATOM   1052 C CB  . ASP   A 1 130 ? 22.842  27.531 -21.486 1.00 109.36 ? 170 ASP   A CB  1 
ATOM   1053 C CG  . ASP   A 1 130 ? 24.223  28.072 -21.158 1.00 108.34 ? 170 ASP   A CG  1 
ATOM   1054 O OD1 . ASP   A 1 130 ? 25.117  27.291 -20.766 1.00 109.46 ? 170 ASP   A OD1 1 
ATOM   1055 O OD2 . ASP   A 1 130 ? 24.413  29.298 -21.299 1.00 106.78 ? 170 ASP   A OD2 1 
ATOM   1056 N N   . PRO   A 1 131 ? 23.972  24.569 -19.814 1.00 113.19 ? 171 PRO   A N   1 
ATOM   1057 C CA  . PRO   A 1 131 ? 24.118  23.941 -18.489 1.00 115.15 ? 171 PRO   A CA  1 
ATOM   1058 C C   . PRO   A 1 131 ? 24.553  24.900 -17.398 1.00 114.49 ? 171 PRO   A C   1 
ATOM   1059 O O   . PRO   A 1 131 ? 24.244  24.661 -16.223 1.00 113.95 ? 171 PRO   A O   1 
ATOM   1060 C CB  . PRO   A 1 131 ? 25.172  22.852 -18.735 1.00 119.28 ? 171 PRO   A CB  1 
ATOM   1061 C CG  . PRO   A 1 131 ? 25.937  23.326 -19.931 1.00 120.27 ? 171 PRO   A CG  1 
ATOM   1062 C CD  . PRO   A 1 131 ? 24.936  24.039 -20.794 1.00 117.27 ? 171 PRO   A CD  1 
ATOM   1063 N N   . VAL   A 1 132 ? 25.257  25.978 -17.744 1.00 114.82 ? 172 VAL   A N   1 
ATOM   1064 C CA  . VAL   A 1 132 ? 25.662  26.951 -16.733 1.00 116.07 ? 172 VAL   A CA  1 
ATOM   1065 C C   . VAL   A 1 132 ? 24.456  27.750 -16.254 1.00 114.04 ? 172 VAL   A C   1 
ATOM   1066 O O   . VAL   A 1 132 ? 24.199  27.863 -15.048 1.00 115.87 ? 172 VAL   A O   1 
ATOM   1067 C CB  . VAL   A 1 132 ? 26.764  27.870 -17.289 1.00 117.12 ? 172 VAL   A CB  1 
ATOM   1068 C CG1 . VAL   A 1 132 ? 27.387  28.689 -16.168 1.00 116.65 ? 172 VAL   A CG1 1 
ATOM   1069 C CG2 . VAL   A 1 132 ? 27.816  27.050 -18.021 1.00 118.23 ? 172 VAL   A CG2 1 
ATOM   1070 N N   . THR   A 1 133 ? 23.691  28.307 -17.194 1.00 109.99 ? 173 THR   A N   1 
ATOM   1071 C CA  . THR   A 1 133 ? 22.556  29.145 -16.829 1.00 100.66 ? 173 THR   A CA  1 
ATOM   1072 C C   . THR   A 1 133 ? 21.376  28.324 -16.322 1.00 91.29  ? 173 THR   A C   1 
ATOM   1073 O O   . THR   A 1 133 ? 20.585  28.822 -15.514 1.00 90.45  ? 173 THR   A O   1 
ATOM   1074 C CB  . THR   A 1 133 ? 22.123  29.986 -18.029 1.00 97.49  ? 173 THR   A CB  1 
ATOM   1075 O OG1 . THR   A 1 133 ? 21.567  29.132 -19.037 1.00 97.88  ? 173 THR   A OG1 1 
ATOM   1076 C CG2 . THR   A 1 133 ? 23.306  30.750 -18.609 1.00 94.55  ? 173 THR   A CG2 1 
ATOM   1077 N N   . SER   A 1 134 ? 21.243  27.073 -16.778 1.00 84.12  ? 174 SER   A N   1 
ATOM   1078 C CA  . SER   A 1 134 ? 20.040  26.292 -16.496 1.00 79.48  ? 174 SER   A CA  1 
ATOM   1079 C C   . SER   A 1 134 ? 19.829  26.076 -15.001 1.00 71.19  ? 174 SER   A C   1 
ATOM   1080 O O   . SER   A 1 134 ? 18.685  25.913 -14.557 1.00 61.71  ? 174 SER   A O   1 
ATOM   1081 C CB  . SER   A 1 134 ? 20.102  24.945 -17.223 1.00 83.34  ? 174 SER   A CB  1 
ATOM   1082 O OG  . SER   A 1 134 ? 21.283  24.233 -16.889 1.00 87.75  ? 174 SER   A OG  1 
ATOM   1083 N N   . GLN   A 1 135 ? 20.909  26.049 -14.213 1.00 67.83  ? 175 GLN   A N   1 
ATOM   1084 C CA  . GLN   A 1 135 ? 20.751  26.027 -12.762 1.00 64.54  ? 175 GLN   A CA  1 
ATOM   1085 C C   . GLN   A 1 135 ? 20.123  27.323 -12.271 1.00 54.13  ? 175 GLN   A C   1 
ATOM   1086 O O   . GLN   A 1 135 ? 19.291  27.309 -11.353 1.00 47.18  ? 175 GLN   A O   1 
ATOM   1087 C CB  . GLN   A 1 135 ? 22.099  25.802 -12.077 1.00 73.73  ? 175 GLN   A CB  1 
ATOM   1088 C CG  . GLN   A 1 135 ? 22.725  24.442 -12.330 1.00 85.57  ? 175 GLN   A CG  1 
ATOM   1089 C CD  . GLN   A 1 135 ? 24.158  24.363 -11.821 1.00 95.47  ? 175 GLN   A CD  1 
ATOM   1090 O OE1 . GLN   A 1 135 ? 25.053  23.879 -12.520 1.00 97.93  ? 175 GLN   A OE1 1 
ATOM   1091 N NE2 . GLN   A 1 135 ? 24.382  24.844 -10.599 1.00 96.86  ? 175 GLN   A NE2 1 
ATOM   1092 N N   . ASN   A 1 136 ? 20.509  28.455 -12.872 1.00 44.61  ? 176 ASN   A N   1 
ATOM   1093 C CA  . ASN   A 1 136 ? 19.908  29.729 -12.492 1.00 41.86  ? 176 ASN   A CA  1 
ATOM   1094 C C   . ASN   A 1 136 ? 18.446  29.799 -12.911 1.00 38.54  ? 176 ASN   A C   1 
ATOM   1095 O O   . ASN   A 1 136 ? 17.627  30.385 -12.199 1.00 39.98  ? 176 ASN   A O   1 
ATOM   1096 C CB  . ASN   A 1 136 ? 20.700  30.884 -13.095 1.00 40.06  ? 176 ASN   A CB  1 
ATOM   1097 C CG  . ASN   A 1 136 ? 22.003  31.119 -12.383 1.00 47.36  ? 176 ASN   A CG  1 
ATOM   1098 O OD1 . ASN   A 1 136 ? 22.360  30.380 -11.469 1.00 53.22  ? 176 ASN   A OD1 1 
ATOM   1099 N ND2 . ASN   A 1 136 ? 22.730  32.147 -12.799 1.00 47.65  ? 176 ASN   A ND2 1 
ATOM   1100 N N   . VAL   A 1 137 ? 18.095  29.211 -14.061 1.00 33.91  ? 177 VAL   A N   1 
ATOM   1101 C CA  . VAL   A 1 137 ? 16.700  29.245 -14.494 1.00 33.69  ? 177 VAL   A CA  1 
ATOM   1102 C C   . VAL   A 1 137 ? 15.825  28.457 -13.529 1.00 28.68  ? 177 VAL   A C   1 
ATOM   1103 O O   . VAL   A 1 137 ? 14.738  28.903 -13.155 1.00 30.26  ? 177 VAL   A O   1 
ATOM   1104 C CB  . VAL   A 1 137 ? 16.572  28.724 -15.935 1.00 41.76  ? 177 VAL   A CB  1 
ATOM   1105 C CG1 . VAL   A 1 137 ? 15.105  28.579 -16.307 1.00 35.48  ? 177 VAL   A CG1 1 
ATOM   1106 C CG2 . VAL   A 1 137 ? 17.293  29.667 -16.901 1.00 40.37  ? 177 VAL   A CG2 1 
ATOM   1107 N N   . GLN   A 1 138 ? 16.283  27.276 -13.110 1.00 33.25  ? 178 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 138 ? 15.537  26.490 -12.129 1.00 33.41  ? 178 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 138 ? 15.376  27.256 -10.819 1.00 34.45  ? 178 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 138 ? 14.287  27.298 -10.239 1.00 32.71  ? 178 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 138 ? 16.250  25.157 -11.887 1.00 32.61  ? 178 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 138 ? 15.538  24.256 -10.884 1.00 36.99  ? 178 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 138 ? 14.280  23.643 -11.459 1.00 39.00  ? 178 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 138 ? 14.099  23.605 -12.679 1.00 34.76  ? 178 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 138 ? 13.397  23.163 -10.586 1.00 35.85  ? 178 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 139 ? 16.457  27.869 -10.340 1.00 29.73  ? 179 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 139 ? 16.393  28.659 -9.112  1.00 28.97  ? 179 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 139 ? 15.412  29.818 -9.252  1.00 30.38  ? 179 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 139 ? 14.577  30.050 -8.369  1.00 30.47  ? 179 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 139 ? 17.799  29.154 -8.769  1.00 32.61  ? 179 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 139 ? 17.938  29.990 -7.507  1.00 35.13  ? 179 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 139 ? 17.984  29.394 -6.251  1.00 34.38  ? 179 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 139 ? 18.076  31.369 -7.583  1.00 33.53  ? 179 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 139 ? 18.140  30.157 -5.100  1.00 34.84  ? 179 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 139 ? 18.230  32.140 -6.443  1.00 34.23  ? 179 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 139 ? 18.256  31.528 -5.207  1.00 33.40  ? 179 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 139 ? 18.413  32.291 -4.075  1.00 36.65  ? 179 TYR   A OH  1 
ATOM   1128 N N   . PHE   A 1 140 ? 15.472  30.538 -10.373 1.00 29.32  ? 180 PHE   A N   1 
ATOM   1129 C CA  . PHE   A 1 140 ? 14.588  31.685 -10.556 1.00 30.83  ? 180 PHE   A CA  1 
ATOM   1130 C C   . PHE   A 1 140 ? 13.122  31.268 -10.597 1.00 30.57  ? 180 PHE   A C   1 
ATOM   1131 O O   . PHE   A 1 140 ? 12.271  31.902 -9.967  1.00 32.27  ? 180 PHE   A O   1 
ATOM   1132 C CB  . PHE   A 1 140 ? 14.950  32.438 -11.834 1.00 30.59  ? 180 PHE   A CB  1 
ATOM   1133 C CG  . PHE   A 1 140 ? 13.913  33.448 -12.247 1.00 32.90  ? 180 PHE   A CG  1 
ATOM   1134 C CD1 . PHE   A 1 140 ? 13.895  34.707 -11.682 1.00 33.76  ? 180 PHE   A CD1 1 
ATOM   1135 C CD2 . PHE   A 1 140 ? 12.949  33.132 -13.199 1.00 34.23  ? 180 PHE   A CD2 1 
ATOM   1136 C CE1 . PHE   A 1 140 ? 12.936  35.637 -12.051 1.00 34.40  ? 180 PHE   A CE1 1 
ATOM   1137 C CE2 . PHE   A 1 140 ? 11.994  34.061 -13.579 1.00 31.98  ? 180 PHE   A CE2 1 
ATOM   1138 C CZ  . PHE   A 1 140 ? 11.991  35.315 -13.010 1.00 31.69  ? 180 PHE   A CZ  1 
ATOM   1139 N N   . LEU   A 1 141 ? 12.796  30.223 -11.361 1.00 31.78  ? 181 LEU   A N   1 
ATOM   1140 C CA  . LEU   A 1 141 ? 11.385  29.925 -11.603 1.00 29.24  ? 181 LEU   A CA  1 
ATOM   1141 C C   . LEU   A 1 141 ? 10.690  29.429 -10.342 1.00 27.78  ? 181 LEU   A C   1 
ATOM   1142 O O   . LEU   A 1 141 ? 9.507   29.724 -10.127 1.00 33.15  ? 181 LEU   A O   1 
ATOM   1143 C CB  . LEU   A 1 141 ? 11.242  28.906 -12.734 1.00 27.95  ? 181 LEU   A CB  1 
ATOM   1144 C CG  . LEU   A 1 141 ? 11.484  29.450 -14.147 1.00 32.39  ? 181 LEU   A CG  1 
ATOM   1145 C CD1 . LEU   A 1 141 ? 11.419  28.339 -15.188 1.00 32.68  ? 181 LEU   A CD1 1 
ATOM   1146 C CD2 . LEU   A 1 141 ? 10.484  30.539 -14.498 1.00 31.23  ? 181 LEU   A CD2 1 
ATOM   1147 N N   . ASP   A 1 142 ? 11.385  28.652 -9.509  1.00 28.38  ? 182 ASP   A N   1 
ATOM   1148 C CA  . ASP   A 1 142 ? 10.821  28.306 -8.206  1.00 30.61  ? 182 ASP   A CA  1 
ATOM   1149 C C   . ASP   A 1 142 ? 10.455  29.570 -7.439  1.00 34.04  ? 182 ASP   A C   1 
ATOM   1150 O O   . ASP   A 1 142 ? 9.346   29.702 -6.907  1.00 33.53  ? 182 ASP   A O   1 
ATOM   1151 C CB  . ASP   A 1 142 ? 11.813  27.468 -7.395  1.00 35.55  ? 182 ASP   A CB  1 
ATOM   1152 C CG  . ASP   A 1 142 ? 11.759  25.982 -7.733  1.00 41.85  ? 182 ASP   A CG  1 
ATOM   1153 O OD1 . ASP   A 1 142 ? 10.768  25.524 -8.339  1.00 38.23  ? 182 ASP   A OD1 1 
ATOM   1154 O OD2 . ASP   A 1 142 ? 12.717  25.269 -7.366  1.00 43.38  ? 182 ASP   A OD2 1 
ATOM   1155 N N   . ARG   A 1 143 ? 11.380  30.529 -7.400  1.00 30.88  ? 183 ARG   A N   1 
ATOM   1156 C CA  . ARG   A 1 143 ? 11.161  31.738 -6.614  1.00 33.60  ? 183 ARG   A CA  1 
ATOM   1157 C C   . ARG   A 1 143 ? 10.148  32.661 -7.279  1.00 25.98  ? 183 ARG   A C   1 
ATOM   1158 O O   . ARG   A 1 143 ? 9.284   33.227 -6.599  1.00 29.59  ? 183 ARG   A O   1 
ATOM   1159 C CB  . ARG   A 1 143 ? 12.500  32.439 -6.385  1.00 28.23  ? 183 ARG   A CB  1 
ATOM   1160 C CG  . ARG   A 1 143 ? 13.455  31.574 -5.575  1.00 29.70  ? 183 ARG   A CG  1 
ATOM   1161 C CD  . ARG   A 1 143 ? 14.897  32.030 -5.706  1.00 29.38  ? 183 ARG   A CD  1 
ATOM   1162 N NE  . ARG   A 1 143 ? 15.117  33.343 -5.098  1.00 32.23  ? 183 ARG   A NE  1 
ATOM   1163 C CZ  . ARG   A 1 143 ? 15.259  33.550 -3.788  1.00 34.89  ? 183 ARG   A CZ  1 
ATOM   1164 N NH1 . ARG   A 1 143 ? 15.198  32.532 -2.929  1.00 34.22  ? 183 ARG   A NH1 1 
ATOM   1165 N NH2 . ARG   A 1 143 ? 15.470  34.780 -3.330  1.00 35.80  ? 183 ARG   A NH2 1 
ATOM   1166 N N   . PHE   A 1 144 ? 10.224  32.813 -8.605  1.00 27.76  ? 184 PHE   A N   1 
ATOM   1167 C CA  . PHE   A 1 144 ? 9.261   33.656 -9.302  1.00 28.73  ? 184 PHE   A CA  1 
ATOM   1168 C C   . PHE   A 1 144 ? 7.845   33.120 -9.142  1.00 32.67  ? 184 PHE   A C   1 
ATOM   1169 O O   . PHE   A 1 144 ? 6.904   33.887 -8.903  1.00 33.69  ? 184 PHE   A O   1 
ATOM   1170 C CB  . PHE   A 1 144 ? 9.608   33.775 -10.786 1.00 32.06  ? 184 PHE   A CB  1 
ATOM   1171 C CG  . PHE   A 1 144 ? 8.592   34.556 -11.568 1.00 31.84  ? 184 PHE   A CG  1 
ATOM   1172 C CD1 . PHE   A 1 144 ? 8.620   35.939 -11.569 1.00 34.44  ? 184 PHE   A CD1 1 
ATOM   1173 C CD2 . PHE   A 1 144 ? 7.581   33.909 -12.265 1.00 34.99  ? 184 PHE   A CD2 1 
ATOM   1174 C CE1 . PHE   A 1 144 ? 7.671   36.668 -12.268 1.00 34.27  ? 184 PHE   A CE1 1 
ATOM   1175 C CE2 . PHE   A 1 144 ? 6.630   34.635 -12.970 1.00 34.95  ? 184 PHE   A CE2 1 
ATOM   1176 C CZ  . PHE   A 1 144 ? 6.674   36.018 -12.966 1.00 31.60  ? 184 PHE   A CZ  1 
ATOM   1177 N N   . TYR   A 1 145 ? 7.671   31.805 -9.262  1.00 30.09  ? 185 TYR   A N   1 
ATOM   1178 C CA  . TYR   A 1 145 ? 6.326   31.250 -9.175  1.00 29.21  ? 185 TYR   A CA  1 
ATOM   1179 C C   . TYR   A 1 145 ? 5.820   31.236 -7.734  1.00 30.36  ? 185 TYR   A C   1 
ATOM   1180 O O   . TYR   A 1 145 ? 4.632   31.471 -7.492  1.00 32.95  ? 185 TYR   A O   1 
ATOM   1181 C CB  . TYR   A 1 145 ? 6.306   29.850 -9.789  1.00 28.75  ? 185 TYR   A CB  1 
ATOM   1182 C CG  . TYR   A 1 145 ? 6.269   29.834 -11.309 1.00 29.53  ? 185 TYR   A CG  1 
ATOM   1183 C CD1 . TYR   A 1 145 ? 5.501   30.755 -12.025 1.00 30.99  ? 185 TYR   A CD1 1 
ATOM   1184 C CD2 . TYR   A 1 145 ? 7.006   28.898 -12.034 1.00 32.54  ? 185 TYR   A CD2 1 
ATOM   1185 C CE1 . TYR   A 1 145 ? 5.463   30.736 -13.420 1.00 27.32  ? 185 TYR   A CE1 1 
ATOM   1186 C CE2 . TYR   A 1 145 ? 6.970   28.872 -13.426 1.00 30.48  ? 185 TYR   A CE2 1 
ATOM   1187 C CZ  . TYR   A 1 145 ? 6.201   29.793 -14.109 1.00 30.24  ? 185 TYR   A CZ  1 
ATOM   1188 O OH  . TYR   A 1 145 ? 6.172   29.758 -15.486 1.00 37.17  ? 185 TYR   A OH  1 
ATOM   1189 N N   . MET   A 1 146 ? 6.696   30.977 -6.762  1.00 29.98  ? 186 MET   A N   1 
ATOM   1190 C CA  . MET   A 1 146 ? 6.278   31.104 -5.366  1.00 32.68  ? 186 MET   A CA  1 
ATOM   1191 C C   . MET   A 1 146 ? 5.911   32.544 -5.046  1.00 34.70  ? 186 MET   A C   1 
ATOM   1192 O O   . MET   A 1 146 ? 4.886   32.809 -4.405  1.00 32.27  ? 186 MET   A O   1 
ATOM   1193 C CB  . MET   A 1 146 ? 7.379   30.629 -4.422  1.00 29.09  ? 186 MET   A CB  1 
ATOM   1194 C CG  . MET   A 1 146 ? 6.943   30.631 -2.967  1.00 35.28  ? 186 MET   A CG  1 
ATOM   1195 S SD  . MET   A 1 146 ? 5.770   29.303 -2.625  1.00 36.71  ? 186 MET   A SD  1 
ATOM   1196 C CE  . MET   A 1 146 ? 6.892   27.962 -2.218  1.00 34.16  ? 186 MET   A CE  1 
ATOM   1197 N N   . SER   A 1 147 ? 6.729   33.491 -5.509  1.00 33.92  ? 187 SER   A N   1 
ATOM   1198 C CA  . SER   A 1 147 ? 6.400   34.901 -5.348  1.00 34.53  ? 187 SER   A CA  1 
ATOM   1199 C C   . SER   A 1 147 ? 5.042   35.222 -5.964  1.00 33.24  ? 187 SER   A C   1 
ATOM   1200 O O   . SER   A 1 147 ? 4.207   35.883 -5.336  1.00 34.54  ? 187 SER   A O   1 
ATOM   1201 C CB  . SER   A 1 147 ? 7.496   35.767 -5.969  1.00 32.13  ? 187 SER   A CB  1 
ATOM   1202 O OG  . SER   A 1 147 ? 6.977   37.025 -6.367  1.00 35.33  ? 187 SER   A OG  1 
ATOM   1203 N N   . ARG   A 1 148 ? 4.804   34.760 -7.198  1.00 31.14  ? 188 ARG   A N   1 
ATOM   1204 C CA  . ARG   A 1 148 ? 3.527   35.020 -7.860  1.00 32.46  ? 188 ARG   A CA  1 
ATOM   1205 C C   . ARG   A 1 148 ? 2.362   34.442 -7.069  1.00 29.18  ? 188 ARG   A C   1 
ATOM   1206 O O   . ARG   A 1 148 ? 1.315   35.084 -6.938  1.00 32.21  ? 188 ARG   A O   1 
ATOM   1207 C CB  . ARG   A 1 148 ? 3.542   34.446 -9.278  1.00 31.17  ? 188 ARG   A CB  1 
ATOM   1208 C CG  . ARG   A 1 148 ? 2.168   34.264 -9.914  1.00 36.56  ? 188 ARG   A CG  1 
ATOM   1209 C CD  . ARG   A 1 148 ? 1.459   35.593 -10.084 1.00 45.76  ? 188 ARG   A CD  1 
ATOM   1210 N NE  . ARG   A 1 148 ? 0.183   35.451 -10.779 1.00 50.28  ? 188 ARG   A NE  1 
ATOM   1211 C CZ  . ARG   A 1 148 ? -0.793  36.354 -10.732 1.00 51.76  ? 188 ARG   A CZ  1 
ATOM   1212 N NH1 . ARG   A 1 148 ? -1.920  36.134 -11.405 1.00 54.24  ? 188 ARG   A NH1 1 
ATOM   1213 N NH2 . ARG   A 1 148 ? -0.650  37.466 -10.000 1.00 36.03  ? 188 ARG   A NH2 1 
ATOM   1214 N N   . ILE   A 1 149 ? 2.519   33.222 -6.555  1.00 33.17  ? 189 ILE   A N   1 
ATOM   1215 C CA  . ILE   A 1 149 ? 1.478   32.626 -5.724  1.00 34.01  ? 189 ILE   A CA  1 
ATOM   1216 C C   . ILE   A 1 149 ? 1.157   33.530 -4.543  1.00 34.11  ? 189 ILE   A C   1 
ATOM   1217 O O   . ILE   A 1 149 ? -0.014  33.761 -4.217  1.00 33.54  ? 189 ILE   A O   1 
ATOM   1218 C CB  . ILE   A 1 149 ? 1.910   31.221 -5.270  1.00 32.13  ? 189 ILE   A CB  1 
ATOM   1219 C CG1 . ILE   A 1 149 ? 1.793   30.237 -6.434  1.00 33.06  ? 189 ILE   A CG1 1 
ATOM   1220 C CG2 . ILE   A 1 149 ? 1.095   30.764 -4.070  1.00 32.37  ? 189 ILE   A CG2 1 
ATOM   1221 C CD1 . ILE   A 1 149 ? 2.505   28.940 -6.189  1.00 34.17  ? 189 ILE   A CD1 1 
ATOM   1222 N N   . SER   A 1 150 ? 2.189   34.082 -3.899  1.00 30.29  ? 190 SER   A N   1 
ATOM   1223 C CA  . SER   A 1 150 ? 1.962   34.912 -2.725  1.00 31.51  ? 190 SER   A CA  1 
ATOM   1224 C C   . SER   A 1 150 ? 1.335   36.248 -3.093  1.00 32.08  ? 190 SER   A C   1 
ATOM   1225 O O   . SER   A 1 150 ? 0.519   36.783 -2.330  1.00 33.91  ? 190 SER   A O   1 
ATOM   1226 C CB  . SER   A 1 150 ? 3.274   35.137 -1.974  1.00 31.12  ? 190 SER   A CB  1 
ATOM   1227 O OG  . SER   A 1 150 ? 4.046   36.156 -2.584  1.00 32.57  ? 190 SER   A OG  1 
ATOM   1228 N N   . ILE   A 1 151 ? 1.728   36.822 -4.232  1.00 30.50  ? 191 ILE   A N   1 
ATOM   1229 C CA  . ILE   A 1 151 ? 1.146   38.095 -4.654  1.00 34.02  ? 191 ILE   A CA  1 
ATOM   1230 C C   . ILE   A 1 151 ? -0.300  37.888 -5.075  1.00 37.44  ? 191 ILE   A C   1 
ATOM   1231 O O   . ILE   A 1 151 ? -1.185  38.692 -4.747  1.00 37.83  ? 191 ILE   A O   1 
ATOM   1232 C CB  . ILE   A 1 151 ? 1.985   38.718 -5.787  1.00 35.09  ? 191 ILE   A CB  1 
ATOM   1233 C CG1 . ILE   A 1 151 ? 3.346   39.190 -5.268  1.00 36.02  ? 191 ILE   A CG1 1 
ATOM   1234 C CG2 . ILE   A 1 151 ? 1.234   39.859 -6.456  1.00 34.31  ? 191 ILE   A CG2 1 
ATOM   1235 C CD1 . ILE   A 1 151 ? 4.353   39.473 -6.387  1.00 36.88  ? 191 ILE   A CD1 1 
ATOM   1236 N N   . ARG   A 1 152 ? -0.557  36.795 -5.795  1.00 35.59  ? 192 ARG   A N   1 
ATOM   1237 C CA  . ARG   A 1 152 ? -1.914  36.422 -6.174  1.00 38.25  ? 192 ARG   A CA  1 
ATOM   1238 C C   . ARG   A 1 152 ? -2.799  36.267 -4.949  1.00 39.30  ? 192 ARG   A C   1 
ATOM   1239 O O   . ARG   A 1 152 ? -3.955  36.711 -4.942  1.00 41.63  ? 192 ARG   A O   1 
ATOM   1240 C CB  . ARG   A 1 152 ? -1.881  35.115 -6.962  1.00 38.11  ? 192 ARG   A CB  1 
ATOM   1241 C CG  . ARG   A 1 152 ? -3.148  34.830 -7.681  1.00 50.74  ? 192 ARG   A CG  1 
ATOM   1242 C CD  . ARG   A 1 152 ? -3.435  36.008 -8.567  1.00 67.18  ? 192 ARG   A CD  1 
ATOM   1243 N NE  . ARG   A 1 152 ? -4.677  35.880 -9.313  1.00 79.87  ? 192 ARG   A NE  1 
ATOM   1244 C CZ  . ARG   A 1 152 ? -5.035  36.710 -10.283 1.00 79.42  ? 192 ARG   A CZ  1 
ATOM   1245 N NH1 . ARG   A 1 152 ? -6.186  36.529 -10.917 1.00 82.50  ? 192 ARG   A NH1 1 
ATOM   1246 N NH2 . ARG   A 1 152 ? -4.235  37.719 -10.617 1.00 74.10  ? 192 ARG   A NH2 1 
ATOM   1247 N N   . MET   A 1 153 ? -2.263  35.638 -3.900  1.00 36.58  ? 193 MET   A N   1 
ATOM   1248 C CA  . MET   A 1 153 ? -2.996  35.475 -2.652  1.00 37.27  ? 193 MET   A CA  1 
ATOM   1249 C C   . MET   A 1 153 ? -3.420  36.823 -2.074  1.00 39.58  ? 193 MET   A C   1 
ATOM   1250 O O   . MET   A 1 153 ? -4.573  37.004 -1.669  1.00 42.03  ? 193 MET   A O   1 
ATOM   1251 C CB  . MET   A 1 153 ? -2.125  34.705 -1.661  1.00 37.45  ? 193 MET   A CB  1 
ATOM   1252 C CG  . MET   A 1 153 ? -2.802  34.387 -0.350  1.00 42.05  ? 193 MET   A CG  1 
ATOM   1253 S SD  . MET   A 1 153 ? -3.936  33.005 -0.525  1.00 48.62  ? 193 MET   A SD  1 
ATOM   1254 C CE  . MET   A 1 153 ? -4.614  32.952 1.134   1.00 45.90  ? 193 MET   A CE  1 
ATOM   1255 N N   . LEU   A 1 154 ? -2.495  37.786 -2.021  1.00 39.50  ? 194 LEU   A N   1 
ATOM   1256 C CA  . LEU   A 1 154 ? -2.827  39.092 -1.457  1.00 39.48  ? 194 LEU   A CA  1 
ATOM   1257 C C   . LEU   A 1 154 ? -3.862  39.811 -2.308  1.00 39.01  ? 194 LEU   A C   1 
ATOM   1258 O O   . LEU   A 1 154 ? -4.821  40.384 -1.779  1.00 39.92  ? 194 LEU   A O   1 
ATOM   1259 C CB  . LEU   A 1 154 ? -1.567  39.949 -1.313  1.00 33.61  ? 194 LEU   A CB  1 
ATOM   1260 C CG  . LEU   A 1 154 ? -0.467  39.446 -0.373  1.00 34.65  ? 194 LEU   A CG  1 
ATOM   1261 C CD1 . LEU   A 1 154 ? 0.702   40.427 -0.347  1.00 32.98  ? 194 LEU   A CD1 1 
ATOM   1262 C CD2 . LEU   A 1 154 ? -0.995  39.218 1.036   1.00 41.80  ? 194 LEU   A CD2 1 
ATOM   1263 N N   . LEU   A 1 155 ? -3.689  39.785 -3.631  1.00 38.63  ? 195 LEU   A N   1 
ATOM   1264 C CA  . LEU   A 1 155 ? -4.644  40.448 -4.516  1.00 43.72  ? 195 LEU   A CA  1 
ATOM   1265 C C   . LEU   A 1 155 ? -6.029  39.812 -4.416  1.00 44.27  ? 195 LEU   A C   1 
ATOM   1266 O O   . LEU   A 1 155 ? -7.041  40.520 -4.350  1.00 46.36  ? 195 LEU   A O   1 
ATOM   1267 C CB  . LEU   A 1 155 ? -4.141  40.404 -5.964  1.00 41.66  ? 195 LEU   A CB  1 
ATOM   1268 C CG  . LEU   A 1 155 ? -2.772  41.003 -6.294  1.00 41.73  ? 195 LEU   A CG  1 
ATOM   1269 C CD1 . LEU   A 1 155 ? -2.361  40.636 -7.712  1.00 43.57  ? 195 LEU   A CD1 1 
ATOM   1270 C CD2 . LEU   A 1 155 ? -2.786  42.512 -6.110  1.00 38.32  ? 195 LEU   A CD2 1 
ATOM   1271 N N   . ASN   A 1 156 ? -6.093  38.476 -4.409  1.00 42.63  ? 196 ASN   A N   1 
ATOM   1272 C CA  . ASN   A 1 156 ? -7.382  37.794 -4.320  1.00 46.18  ? 196 ASN   A CA  1 
ATOM   1273 C C   . ASN   A 1 156 ? -8.099  38.144 -3.024  1.00 49.09  ? 196 ASN   A C   1 
ATOM   1274 O O   . ASN   A 1 156 ? -9.290  38.469 -3.032  1.00 53.01  ? 196 ASN   A O   1 
ATOM   1275 C CB  . ASN   A 1 156 ? -7.198  36.279 -4.416  1.00 41.22  ? 196 ASN   A CB  1 
ATOM   1276 C CG  . ASN   A 1 156 ? -6.957  35.795 -5.837  1.00 48.74  ? 196 ASN   A CG  1 
ATOM   1277 O OD1 . ASN   A 1 156 ? -7.220  36.505 -6.810  1.00 55.80  ? 196 ASN   A OD1 1 
ATOM   1278 N ND2 . ASN   A 1 156 ? -6.464  34.563 -5.958  1.00 43.14  ? 196 ASN   A ND2 1 
ATOM   1279 N N   . GLN   A 1 157 ? -7.389  38.065 -1.893  1.00 46.24  ? 197 GLN   A N   1 
ATOM   1280 C CA  . GLN   A 1 157 ? -8.009  38.363 -0.606  1.00 43.39  ? 197 GLN   A CA  1 
ATOM   1281 C C   . GLN   A 1 157 ? -8.604  39.761 -0.601  1.00 48.37  ? 197 GLN   A C   1 
ATOM   1282 O O   . GLN   A 1 157 ? -9.784  39.942 -0.280  1.00 53.96  ? 197 GLN   A O   1 
ATOM   1283 C CB  . GLN   A 1 157 ? -6.995  38.216 0.527   1.00 48.14  ? 197 GLN   A CB  1 
ATOM   1284 C CG  . GLN   A 1 157 ? -6.591  36.782 0.828   1.00 56.24  ? 197 GLN   A CG  1 
ATOM   1285 C CD  . GLN   A 1 157 ? -7.774  35.902 1.166   1.00 57.32  ? 197 GLN   A CD  1 
ATOM   1286 O OE1 . GLN   A 1 157 ? -8.114  34.990 0.411   1.00 64.18  ? 197 GLN   A OE1 1 
ATOM   1287 N NE2 . GLN   A 1 157 ? -8.405  36.163 2.306   1.00 55.30  ? 197 GLN   A NE2 1 
ATOM   1288 N N   . HIS   A 1 158 ? -7.803  40.768 -0.965  1.00 48.84  ? 198 HIS   A N   1 
ATOM   1289 C CA  . HIS   A 1 158 ? -8.311  42.137 -0.946  1.00 51.61  ? 198 HIS   A CA  1 
ATOM   1290 C C   . HIS   A 1 158 ? -9.456  42.310 -1.936  1.00 53.99  ? 198 HIS   A C   1 
ATOM   1291 O O   . HIS   A 1 158 ? -10.444 42.991 -1.637  1.00 54.27  ? 198 HIS   A O   1 
ATOM   1292 C CB  . HIS   A 1 158 ? -7.193  43.134 -1.248  1.00 48.77  ? 198 HIS   A CB  1 
ATOM   1293 C CG  . HIS   A 1 158 ? -7.626  44.566 -1.157  1.00 50.31  ? 198 HIS   A CG  1 
ATOM   1294 N ND1 . HIS   A 1 158 ? -7.454  45.324 -0.018  1.00 50.32  ? 198 HIS   A ND1 1 
ATOM   1295 C CD2 . HIS   A 1 158 ? -8.247  45.369 -2.053  1.00 49.64  ? 198 HIS   A CD2 1 
ATOM   1296 C CE1 . HIS   A 1 158 ? -7.944  46.534 -0.220  1.00 50.61  ? 198 HIS   A CE1 1 
ATOM   1297 N NE2 . HIS   A 1 158 ? -8.427  46.589 -1.448  1.00 52.86  ? 198 HIS   A NE2 1 
ATOM   1298 N N   . SER   A 1 159 ? -9.350  41.687 -3.114  1.00 51.78  ? 199 SER   A N   1 
ATOM   1299 C CA  . SER   A 1 159 ? -10.384 41.850 -4.132  1.00 52.78  ? 199 SER   A CA  1 
ATOM   1300 C C   . SER   A 1 159 ? -11.691 41.195 -3.707  1.00 49.24  ? 199 SER   A C   1 
ATOM   1301 O O   . SER   A 1 159 ? -12.770 41.753 -3.927  1.00 57.37  ? 199 SER   A O   1 
ATOM   1302 C CB  . SER   A 1 159 ? -9.911  41.272 -5.464  1.00 56.55  ? 199 SER   A CB  1 
ATOM   1303 O OG  . SER   A 1 159 ? -8.769  41.962 -5.936  1.00 63.35  ? 199 SER   A OG  1 
ATOM   1304 N N   . LEU   A 1 160 ? -11.617 40.013 -3.101  1.00 48.55  ? 200 LEU   A N   1 
ATOM   1305 C CA  . LEU   A 1 160 ? -12.836 39.331 -2.685  1.00 50.52  ? 200 LEU   A CA  1 
ATOM   1306 C C   . LEU   A 1 160 ? -13.456 40.000 -1.466  1.00 57.26  ? 200 LEU   A C   1 
ATOM   1307 O O   . LEU   A 1 160 ? -14.680 40.137 -1.384  1.00 62.40  ? 200 LEU   A O   1 
ATOM   1308 C CB  . LEU   A 1 160 ? -12.535 37.859 -2.416  1.00 43.98  ? 200 LEU   A CB  1 
ATOM   1309 C CG  . LEU   A 1 160 ? -12.098 37.162 -3.703  1.00 49.06  ? 200 LEU   A CG  1 
ATOM   1310 C CD1 . LEU   A 1 160 ? -11.579 35.764 -3.441  1.00 50.58  ? 200 LEU   A CD1 1 
ATOM   1311 C CD2 . LEU   A 1 160 ? -13.261 37.142 -4.690  1.00 54.70  ? 200 LEU   A CD2 1 
ATOM   1312 N N   . LEU   A 1 161 ? -12.629 40.449 -0.519  1.00 56.71  ? 201 LEU   A N   1 
ATOM   1313 C CA  . LEU   A 1 161 ? -13.172 41.048 0.694   1.00 55.93  ? 201 LEU   A CA  1 
ATOM   1314 C C   . LEU   A 1 161 ? -13.761 42.430 0.438   1.00 59.69  ? 201 LEU   A C   1 
ATOM   1315 O O   . LEU   A 1 161 ? -14.727 42.815 1.104   1.00 64.86  ? 201 LEU   A O   1 
ATOM   1316 C CB  . LEU   A 1 161 ? -12.094 41.134 1.777   1.00 54.57  ? 201 LEU   A CB  1 
ATOM   1317 C CG  . LEU   A 1 161 ? -11.575 39.834 2.400   1.00 54.00  ? 201 LEU   A CG  1 
ATOM   1318 C CD1 . LEU   A 1 161 ? -10.494 40.138 3.425   1.00 54.37  ? 201 LEU   A CD1 1 
ATOM   1319 C CD2 . LEU   A 1 161 ? -12.707 39.046 3.037   1.00 55.26  ? 201 LEU   A CD2 1 
ATOM   1320 N N   . PHE   A 1 162 ? -13.210 43.189 -0.517  1.00 61.20  ? 202 PHE   A N   1 
ATOM   1321 C CA  . PHE   A 1 162 ? -13.566 44.597 -0.666  1.00 59.61  ? 202 PHE   A CA  1 
ATOM   1322 C C   . PHE   A 1 162 ? -13.985 44.983 -2.080  1.00 64.05  ? 202 PHE   A C   1 
ATOM   1323 O O   . PHE   A 1 162 ? -14.208 46.171 -2.338  1.00 66.12  ? 202 PHE   A O   1 
ATOM   1324 C CB  . PHE   A 1 162 ? -12.403 45.489 -0.218  1.00 54.70  ? 202 PHE   A CB  1 
ATOM   1325 C CG  . PHE   A 1 162 ? -11.854 45.124 1.126   1.00 57.85  ? 202 PHE   A CG  1 
ATOM   1326 C CD1 . PHE   A 1 162 ? -12.624 45.282 2.268   1.00 61.64  ? 202 PHE   A CD1 1 
ATOM   1327 C CD2 . PHE   A 1 162 ? -10.571 44.614 1.251   1.00 57.70  ? 202 PHE   A CD2 1 
ATOM   1328 C CE1 . PHE   A 1 162 ? -12.127 44.941 3.511   1.00 61.56  ? 202 PHE   A CE1 1 
ATOM   1329 C CE2 . PHE   A 1 162 ? -10.066 44.274 2.492   1.00 61.24  ? 202 PHE   A CE2 1 
ATOM   1330 C CZ  . PHE   A 1 162 ? -10.848 44.439 3.626   1.00 61.03  ? 202 PHE   A CZ  1 
ATOM   1331 N N   . GLY   A 1 163 ? -14.106 44.029 -2.996  1.00 68.92  ? 203 GLY   A N   1 
ATOM   1332 C CA  . GLY   A 1 163 ? -14.559 44.337 -4.341  1.00 73.33  ? 203 GLY   A CA  1 
ATOM   1333 C C   . GLY   A 1 163 ? -16.066 44.489 -4.440  1.00 77.85  ? 203 GLY   A C   1 
ATOM   1334 O O   . GLY   A 1 163 ? -16.811 43.546 -4.169  1.00 83.05  ? 203 GLY   A O   1 
ATOM   1335 N N   . HIS   A 1 175 ? -16.684 31.222 4.139   1.00 62.36  ? 215 HIS   A N   1 
ATOM   1336 C CA  . HIS   A 1 175 ? -15.545 31.528 3.273   1.00 75.07  ? 215 HIS   A CA  1 
ATOM   1337 C C   . HIS   A 1 175 ? -14.992 32.925 3.551   1.00 81.05  ? 215 HIS   A C   1 
ATOM   1338 O O   . HIS   A 1 175 ? -15.752 33.891 3.641   1.00 90.36  ? 215 HIS   A O   1 
ATOM   1339 C CB  . HIS   A 1 175 ? -15.942 31.411 1.801   1.00 84.76  ? 215 HIS   A CB  1 
ATOM   1340 C CG  . HIS   A 1 175 ? -15.500 30.137 1.149   1.00 91.56  ? 215 HIS   A CG  1 
ATOM   1341 N ND1 . HIS   A 1 175 ? -14.319 30.032 0.444   1.00 92.02  ? 215 HIS   A ND1 1 
ATOM   1342 C CD2 . HIS   A 1 175 ? -16.087 28.918 1.080   1.00 93.43  ? 215 HIS   A CD2 1 
ATOM   1343 C CE1 . HIS   A 1 175 ? -14.194 28.803 -0.025  1.00 89.74  ? 215 HIS   A CE1 1 
ATOM   1344 N NE2 . HIS   A 1 175 ? -15.254 28.107 0.346   1.00 92.01  ? 215 HIS   A NE2 1 
ATOM   1345 N N   . ILE   A 1 176 ? -13.670 33.030 3.683   1.00 70.66  ? 216 ILE   A N   1 
ATOM   1346 C CA  . ILE   A 1 176 ? -12.997 34.284 4.020   1.00 64.34  ? 216 ILE   A CA  1 
ATOM   1347 C C   . ILE   A 1 176 ? -12.009 34.570 2.898   1.00 67.64  ? 216 ILE   A C   1 
ATOM   1348 O O   . ILE   A 1 176 ? -10.879 34.062 2.906   1.00 64.88  ? 216 ILE   A O   1 
ATOM   1349 C CB  . ILE   A 1 176 ? -12.295 34.219 5.381   1.00 58.94  ? 216 ILE   A CB  1 
ATOM   1350 C CG1 . ILE   A 1 176 ? -13.267 33.738 6.464   1.00 63.72  ? 216 ILE   A CG1 1 
ATOM   1351 C CG2 . ILE   A 1 176 ? -11.723 35.579 5.752   1.00 61.11  ? 216 ILE   A CG2 1 
ATOM   1352 C CD1 . ILE   A 1 176 ? -14.418 34.683 6.734   1.00 71.82  ? 216 ILE   A CD1 1 
ATOM   1353 N N   . GLY   A 1 177 ? -12.420 35.392 1.935   1.00 68.04  ? 217 GLY   A N   1 
ATOM   1354 C CA  . GLY   A 1 177 ? -11.638 35.519 0.714   1.00 68.27  ? 217 GLY   A CA  1 
ATOM   1355 C C   . GLY   A 1 177 ? -11.631 34.188 -0.012  1.00 67.76  ? 217 GLY   A C   1 
ATOM   1356 O O   . GLY   A 1 177 ? -12.670 33.535 -0.158  1.00 72.89  ? 217 GLY   A O   1 
ATOM   1357 N N   . SER   A 1 178 ? -10.453 33.757 -0.458  1.00 61.33  ? 218 SER   A N   1 
ATOM   1358 C CA  . SER   A 1 178 ? -10.307 32.445 -1.072  1.00 61.30  ? 218 SER   A CA  1 
ATOM   1359 C C   . SER   A 1 178 ? -9.999  31.352 -0.056  1.00 57.72  ? 218 SER   A C   1 
ATOM   1360 O O   . SER   A 1 178 ? -9.741  30.210 -0.450  1.00 57.13  ? 218 SER   A O   1 
ATOM   1361 C CB  . SER   A 1 178 ? -9.218  32.472 -2.148  1.00 61.83  ? 218 SER   A CB  1 
ATOM   1362 O OG  . SER   A 1 178 ? -7.956  32.780 -1.590  1.00 65.69  ? 218 SER   A OG  1 
ATOM   1363 N N   . ILE   A 1 179 ? -10.021 31.670 1.235   1.00 53.25  ? 219 ILE   A N   1 
ATOM   1364 C CA  . ILE   A 1 179 ? -9.758  30.691 2.283   1.00 49.00  ? 219 ILE   A CA  1 
ATOM   1365 C C   . ILE   A 1 179 ? -11.077 30.098 2.752   1.00 49.56  ? 219 ILE   A C   1 
ATOM   1366 O O   . ILE   A 1 179 ? -12.042 30.827 3.005   1.00 49.43  ? 219 ILE   A O   1 
ATOM   1367 C CB  . ILE   A 1 179 ? -9.003  31.333 3.455   1.00 46.14  ? 219 ILE   A CB  1 
ATOM   1368 C CG1 . ILE   A 1 179 ? -7.615  31.759 2.999   1.00 50.50  ? 219 ILE   A CG1 1 
ATOM   1369 C CG2 . ILE   A 1 179 ? -8.917  30.367 4.627   1.00 41.91  ? 219 ILE   A CG2 1 
ATOM   1370 C CD1 . ILE   A 1 179 ? -6.903  32.562 4.028   1.00 56.00  ? 219 ILE   A CD1 1 
ATOM   1371 N N   . ASN   A 1 180 ? -11.122 28.775 2.858   1.00 42.49  ? 220 ASN   A N   1 
ATOM   1372 C CA  . ASN   A 1 180 ? -12.249 28.091 3.462   1.00 42.65  ? 220 ASN   A CA  1 
ATOM   1373 C C   . ASN   A 1 180 ? -11.839 27.619 4.846   1.00 48.49  ? 220 ASN   A C   1 
ATOM   1374 O O   . ASN   A 1 180 ? -10.952 26.760 4.956   1.00 48.57  ? 220 ASN   A O   1 
ATOM   1375 C CB  . ASN   A 1 180 ? -12.700 26.908 2.602   1.00 42.65  ? 220 ASN   A CB  1 
ATOM   1376 C CG  . ASN   A 1 180 ? -13.971 26.263 3.121   1.00 45.94  ? 220 ASN   A CG  1 
ATOM   1377 O OD1 . ASN   A 1 180 ? -14.349 26.448 4.276   1.00 43.22  ? 220 ASN   A OD1 1 
ATOM   1378 N ND2 . ASN   A 1 180 ? -14.640 25.495 2.262   1.00 48.77  ? 220 ASN   A ND2 1 
ATOM   1379 N N   . PRO   A 1 181 ? -12.451 28.134 5.916   1.00 49.00  ? 221 PRO   A N   1 
ATOM   1380 C CA  . PRO   A 1 181 ? -12.098 27.662 7.262   1.00 43.17  ? 221 PRO   A CA  1 
ATOM   1381 C C   . PRO   A 1 181 ? -12.478 26.221 7.502   1.00 41.29  ? 221 PRO   A C   1 
ATOM   1382 O O   . PRO   A 1 181 ? -12.017 25.628 8.485   1.00 47.20  ? 221 PRO   A O   1 
ATOM   1383 C CB  . PRO   A 1 181 ? -12.894 28.593 8.194   1.00 49.07  ? 221 PRO   A CB  1 
ATOM   1384 C CG  . PRO   A 1 181 ? -13.383 29.702 7.327   1.00 55.76  ? 221 PRO   A CG  1 
ATOM   1385 C CD  . PRO   A 1 181 ? -13.516 29.146 5.953   1.00 53.23  ? 221 PRO   A CD  1 
ATOM   1386 N N   . ASN   A 1 182 ? -13.318 25.645 6.652   1.00 41.54  ? 222 ASN   A N   1 
ATOM   1387 C CA  . ASN   A 1 182 ? -13.800 24.280 6.817   1.00 43.49  ? 222 ASN   A CA  1 
ATOM   1388 C C   . ASN   A 1 182 ? -13.675 23.517 5.509   1.00 41.42  ? 222 ASN   A C   1 
ATOM   1389 O O   . ASN   A 1 182 ? -14.635 22.932 5.003   1.00 48.67  ? 222 ASN   A O   1 
ATOM   1390 C CB  . ASN   A 1 182 ? -15.241 24.285 7.316   1.00 47.18  ? 222 ASN   A CB  1 
ATOM   1391 C CG  . ASN   A 1 182 ? -15.372 24.890 8.694   1.00 57.06  ? 222 ASN   A CG  1 
ATOM   1392 O OD1 . ASN   A 1 182 ? -15.114 24.227 9.695   1.00 62.27  ? 222 ASN   A OD1 1 
ATOM   1393 N ND2 . ASN   A 1 182 ? -15.778 26.153 8.756   1.00 55.84  ? 222 ASN   A ND2 1 
ATOM   1394 N N   . CYS   A 1 183 ? -12.472 23.504 4.942   1.00 37.82  ? 223 CYS   A N   1 
ATOM   1395 C CA  . CYS   A 1 183 ? -12.265 22.839 3.664   1.00 39.45  ? 223 CYS   A CA  1 
ATOM   1396 C C   . CYS   A 1 183 ? -12.488 21.336 3.805   1.00 43.20  ? 223 CYS   A C   1 
ATOM   1397 O O   . CYS   A 1 183 ? -11.807 20.673 4.590   1.00 43.24  ? 223 CYS   A O   1 
ATOM   1398 C CB  . CYS   A 1 183 ? -10.857 23.133 3.148   1.00 42.31  ? 223 CYS   A CB  1 
ATOM   1399 S SG  . CYS   A 1 183 ? -10.489 22.445 1.518   1.00 43.28  ? 223 CYS   A SG  1 
ATOM   1400 N N   . ASN   A 1 184 ? -13.465 20.808 3.064   1.00 39.86  ? 224 ASN   A N   1 
ATOM   1401 C CA  A ASN   A 1 184 ? -13.761 19.377 3.069   0.51 41.49  ? 224 ASN   A CA  1 
ATOM   1402 C CA  B ASN   A 1 184 ? -13.769 19.378 3.065   0.49 41.51  ? 224 ASN   A CA  1 
ATOM   1403 C C   . ASN   A 1 184 ? -12.771 18.699 2.132   1.00 41.22  ? 224 ASN   A C   1 
ATOM   1404 O O   . ASN   A 1 184 ? -12.924 18.734 0.907   1.00 40.27  ? 224 ASN   A O   1 
ATOM   1405 C CB  A ASN   A 1 184 ? -15.204 19.121 2.654   0.51 43.16  ? 224 ASN   A CB  1 
ATOM   1406 C CB  B ASN   A 1 184 ? -15.213 19.130 2.630   0.49 43.16  ? 224 ASN   A CB  1 
ATOM   1407 C CG  A ASN   A 1 184 ? -15.626 17.680 2.866   0.51 45.26  ? 224 ASN   A CG  1 
ATOM   1408 C CG  B ASN   A 1 184 ? -16.243 19.721 3.599   0.49 48.81  ? 224 ASN   A CG  1 
ATOM   1409 O OD1 A ASN   A 1 184 ? -14.890 16.746 2.543   0.51 35.70  ? 224 ASN   A OD1 1 
ATOM   1410 O OD1 B ASN   A 1 184 ? -16.100 19.631 4.820   0.49 51.77  ? 224 ASN   A OD1 1 
ATOM   1411 N ND2 A ASN   A 1 184 ? -16.820 17.492 3.415   0.51 48.44  ? 224 ASN   A ND2 1 
ATOM   1412 N ND2 B ASN   A 1 184 ? -17.296 20.321 3.046   0.49 52.49  ? 224 ASN   A ND2 1 
ATOM   1413 N N   . VAL   A 1 185 ? -11.744 18.078 2.718   1.00 35.18  ? 225 VAL   A N   1 
ATOM   1414 C CA  . VAL   A 1 185 ? -10.615 17.564 1.943   1.00 34.53  ? 225 VAL   A CA  1 
ATOM   1415 C C   . VAL   A 1 185 ? -11.070 16.503 0.950   1.00 31.06  ? 225 VAL   A C   1 
ATOM   1416 O O   . VAL   A 1 185 ? -10.690 16.526 -0.227  1.00 32.01  ? 225 VAL   A O   1 
ATOM   1417 C CB  . VAL   A 1 185 ? -9.530  17.031 2.896   1.00 34.64  ? 225 VAL   A CB  1 
ATOM   1418 C CG1 . VAL   A 1 185 ? -8.448  16.282 2.124   1.00 32.89  ? 225 VAL   A CG1 1 
ATOM   1419 C CG2 . VAL   A 1 185 ? -8.931  18.191 3.678   1.00 34.82  ? 225 VAL   A CG2 1 
ATOM   1420 N N   . LEU   A 1 186 ? -11.900 15.563 1.400   1.00 33.14  ? 226 LEU   A N   1 
ATOM   1421 C CA  . LEU   A 1 186 ? -12.271 14.462 0.516   1.00 35.12  ? 226 LEU   A CA  1 
ATOM   1422 C C   . LEU   A 1 186 ? -13.122 14.933 -0.658  1.00 36.05  ? 226 LEU   A C   1 
ATOM   1423 O O   . LEU   A 1 186 ? -13.022 14.368 -1.754  1.00 33.37  ? 226 LEU   A O   1 
ATOM   1424 C CB  . LEU   A 1 186 ? -12.997 13.373 1.304   1.00 39.90  ? 226 LEU   A CB  1 
ATOM   1425 C CG  . LEU   A 1 186 ? -12.044 12.242 1.705   1.00 45.72  ? 226 LEU   A CG  1 
ATOM   1426 C CD1 . LEU   A 1 186 ? -11.084 12.708 2.796   1.00 41.23  ? 226 LEU   A CD1 1 
ATOM   1427 C CD2 . LEU   A 1 186 ? -12.831 11.028 2.146   1.00 52.45  ? 226 LEU   A CD2 1 
ATOM   1428 N N   . GLU   A 1 187 ? -13.949 15.964 -0.458  1.00 34.96  ? 227 GLU   A N   1 
ATOM   1429 C CA  . GLU   A 1 187 ? -14.745 16.496 -1.562  1.00 36.18  ? 227 GLU   A CA  1 
ATOM   1430 C C   . GLU   A 1 187 ? -13.863 17.139 -2.619  1.00 30.50  ? 227 GLU   A C   1 
ATOM   1431 O O   . GLU   A 1 187 ? -14.088 16.951 -3.819  1.00 33.24  ? 227 GLU   A O   1 
ATOM   1432 C CB  . GLU   A 1 187 ? -15.776 17.502 -1.046  1.00 44.27  ? 227 GLU   A CB  1 
ATOM   1433 C CG  . GLU   A 1 187 ? -16.892 16.882 -0.217  1.00 70.58  ? 227 GLU   A CG  1 
ATOM   1434 C CD  . GLU   A 1 187 ? -17.462 15.611 -0.841  1.00 89.06  ? 227 GLU   A CD  1 
ATOM   1435 O OE1 . GLU   A 1 187 ? -17.896 15.657 -2.017  1.00 91.09  ? 227 GLU   A OE1 1 
ATOM   1436 O OE2 . GLU   A 1 187 ? -17.467 14.563 -0.153  1.00 94.66  ? 227 GLU   A OE2 1 
ATOM   1437 N N   . VAL   A 1 188 ? -12.855 17.901 -2.203  1.00 31.84  ? 228 VAL   A N   1 
ATOM   1438 C CA  . VAL   A 1 188 ? -11.918 18.451 -3.173  1.00 32.30  ? 228 VAL   A CA  1 
ATOM   1439 C C   . VAL   A 1 188 ? -11.211 17.329 -3.922  1.00 37.53  ? 228 VAL   A C   1 
ATOM   1440 O O   . VAL   A 1 188 ? -11.001 17.410 -5.142  1.00 32.98  ? 228 VAL   A O   1 
ATOM   1441 C CB  . VAL   A 1 188 ? -10.913 19.380 -2.476  1.00 32.27  ? 228 VAL   A CB  1 
ATOM   1442 C CG1 . VAL   A 1 188 ? -9.889  19.882 -3.486  1.00 31.04  ? 228 VAL   A CG1 1 
ATOM   1443 C CG2 . VAL   A 1 188 ? -11.634 20.543 -1.813  1.00 33.86  ? 228 VAL   A CG2 1 
ATOM   1444 N N   . ILE   A 1 189 ? -10.833 16.267 -3.208  1.00 35.41  ? 229 ILE   A N   1 
ATOM   1445 C CA  . ILE   A 1 189 ? -10.117 15.159 -3.841  1.00 33.09  ? 229 ILE   A CA  1 
ATOM   1446 C C   . ILE   A 1 189 ? -10.992 14.492 -4.895  1.00 32.60  ? 229 ILE   A C   1 
ATOM   1447 O O   . ILE   A 1 189 ? -10.543 14.220 -6.017  1.00 34.33  ? 229 ILE   A O   1 
ATOM   1448 C CB  . ILE   A 1 189 ? -9.630  14.157 -2.780  1.00 32.65  ? 229 ILE   A CB  1 
ATOM   1449 C CG1 . ILE   A 1 189 ? -8.400  14.722 -2.072  1.00 31.83  ? 229 ILE   A CG1 1 
ATOM   1450 C CG2 . ILE   A 1 189 ? -9.298  12.801 -3.416  1.00 32.55  ? 229 ILE   A CG2 1 
ATOM   1451 C CD1 . ILE   A 1 189 ? -8.069  14.024 -0.803  1.00 30.71  ? 229 ILE   A CD1 1 
ATOM   1452 N N   . LYS   A 1 190 ? -12.259 14.232 -4.560  1.00 32.78  ? 230 LYS   A N   1 
ATOM   1453 C CA  . LYS   A 1 190 ? -13.154 13.618 -5.535  1.00 34.81  ? 230 LYS   A CA  1 
ATOM   1454 C C   . LYS   A 1 190 ? -13.344 14.520 -6.745  1.00 41.16  ? 230 LYS   A C   1 
ATOM   1455 O O   . LYS   A 1 190 ? -13.459 14.036 -7.877  1.00 38.75  ? 230 LYS   A O   1 
ATOM   1456 C CB  . LYS   A 1 190 ? -14.505 13.302 -4.896  1.00 35.55  ? 230 LYS   A CB  1 
ATOM   1457 C CG  . LYS   A 1 190 ? -14.472 12.246 -3.796  1.00 38.97  ? 230 LYS   A CG  1 
ATOM   1458 C CD  . LYS   A 1 190 ? -15.833 12.178 -3.084  1.00 45.73  ? 230 LYS   A CD  1 
ATOM   1459 C CE  . LYS   A 1 190 ? -15.795 11.268 -1.859  1.00 55.05  ? 230 LYS   A CE  1 
ATOM   1460 N NZ  . LYS   A 1 190 ? -17.069 11.295 -1.067  1.00 55.51  ? 230 LYS   A NZ  1 
ATOM   1461 N N   . ASP   A 1 191 ? -13.391 15.837 -6.519  1.00 40.62  ? 231 ASP   A N   1 
ATOM   1462 C CA  . ASP   A 1 191 ? -13.514 16.791 -7.616  1.00 36.72  ? 231 ASP   A CA  1 
ATOM   1463 C C   . ASP   A 1 191 ? -12.314 16.700 -8.551  1.00 36.56  ? 231 ASP   A C   1 
ATOM   1464 O O   . ASP   A 1 191 ? -12.465 16.658 -9.777  1.00 34.42  ? 231 ASP   A O   1 
ATOM   1465 C CB  . ASP   A 1 191 ? -13.654 18.208 -7.050  1.00 45.89  ? 231 ASP   A CB  1 
ATOM   1466 C CG  . ASP   A 1 191 ? -14.190 19.204 -8.067  1.00 65.89  ? 231 ASP   A CG  1 
ATOM   1467 O OD1 . ASP   A 1 191 ? -14.852 18.780 -9.038  1.00 75.40  ? 231 ASP   A OD1 1 
ATOM   1468 O OD2 . ASP   A 1 191 ? -13.947 20.419 -7.891  1.00 72.84  ? 231 ASP   A OD2 1 
ATOM   1469 N N   . GLY   A 1 192 ? -11.110 16.665 -7.985  1.00 30.83  ? 232 GLY   A N   1 
ATOM   1470 C CA  . GLY   A 1 192 ? -9.924  16.511 -8.807  1.00 36.06  ? 232 GLY   A CA  1 
ATOM   1471 C C   . GLY   A 1 192 ? -9.914  15.195 -9.559  1.00 38.76  ? 232 GLY   A C   1 
ATOM   1472 O O   . GLY   A 1 192 ? -9.544  15.147 -10.737 1.00 32.91  ? 232 GLY   A O   1 
ATOM   1473 N N   . TYR   A 1 193 ? -10.335 14.112 -8.893  1.00 35.66  ? 233 TYR   A N   1 
ATOM   1474 C CA  . TYR   A 1 193 ? -10.397 12.811 -9.553  1.00 33.55  ? 233 TYR   A CA  1 
ATOM   1475 C C   . TYR   A 1 193 ? -11.324 12.846 -10.758 1.00 31.49  ? 233 TYR   A C   1 
ATOM   1476 O O   . TYR   A 1 193 ? -10.974 12.357 -11.838 1.00 33.57  ? 233 TYR   A O   1 
ATOM   1477 C CB  . TYR   A 1 193 ? -10.868 11.723 -8.590  1.00 33.50  ? 233 TYR   A CB  1 
ATOM   1478 C CG  . TYR   A 1 193 ? -11.190 10.456 -9.352  1.00 34.76  ? 233 TYR   A CG  1 
ATOM   1479 C CD1 . TYR   A 1 193 ? -10.167 9.652  -9.846  1.00 34.30  ? 233 TYR   A CD1 1 
ATOM   1480 C CD2 . TYR   A 1 193 ? -12.507 10.089 -9.628  1.00 33.97  ? 233 TYR   A CD2 1 
ATOM   1481 C CE1 . TYR   A 1 193 ? -10.437 8.495  -10.565 1.00 33.10  ? 233 TYR   A CE1 1 
ATOM   1482 C CE2 . TYR   A 1 193 ? -12.789 8.929  -10.354 1.00 38.03  ? 233 TYR   A CE2 1 
ATOM   1483 C CZ  . TYR   A 1 193 ? -11.743 8.142  -10.822 1.00 38.00  ? 233 TYR   A CZ  1 
ATOM   1484 O OH  . TYR   A 1 193 ? -11.996 6.994  -11.549 1.00 37.29  ? 233 TYR   A OH  1 
ATOM   1485 N N   . GLU   A 1 194 ? -12.533 13.385 -10.583 1.00 30.16  ? 234 GLU   A N   1 
ATOM   1486 C CA  . GLU   A 1 194 ? -13.515 13.328 -11.660 1.00 36.78  ? 234 GLU   A CA  1 
ATOM   1487 C C   . GLU   A 1 194 ? -13.083 14.166 -12.854 1.00 36.40  ? 234 GLU   A C   1 
ATOM   1488 O O   . GLU   A 1 194 ? -13.334 13.786 -14.003 1.00 35.35  ? 234 GLU   A O   1 
ATOM   1489 C CB  . GLU   A 1 194 ? -14.888 13.781 -11.161 1.00 46.92  ? 234 GLU   A CB  1 
ATOM   1490 C CG  . GLU   A 1 194 ? -15.539 12.841 -10.153 1.00 60.57  ? 234 GLU   A CG  1 
ATOM   1491 C CD  . GLU   A 1 194 ? -15.926 11.491 -10.749 1.00 69.37  ? 234 GLU   A CD  1 
ATOM   1492 O OE1 . GLU   A 1 194 ? -15.924 11.344 -11.996 1.00 67.21  ? 234 GLU   A OE1 1 
ATOM   1493 O OE2 . GLU   A 1 194 ? -16.236 10.574 -9.957  1.00 70.92  ? 234 GLU   A OE2 1 
ATOM   1494 N N   . ASN   A 1 195 ? -12.435 15.307 -12.614 1.00 32.99  ? 235 ASN   A N   1 
ATOM   1495 C CA  . ASN   A 1 195 ? -11.985 16.120 -13.741 1.00 36.13  ? 235 ASN   A CA  1 
ATOM   1496 C C   . ASN   A 1 195 ? -10.778 15.498 -14.437 1.00 34.32  ? 235 ASN   A C   1 
ATOM   1497 O O   . ASN   A 1 195 ? -10.665 15.565 -15.666 1.00 34.23  ? 235 ASN   A O   1 
ATOM   1498 C CB  . ASN   A 1 195 ? -11.679 17.540 -13.276 1.00 40.04  ? 235 ASN   A CB  1 
ATOM   1499 C CG  . ASN   A 1 195 ? -12.939 18.338 -13.024 1.00 50.04  ? 235 ASN   A CG  1 
ATOM   1500 O OD1 . ASN   A 1 195 ? -13.041 19.073 -12.044 1.00 53.19  ? 235 ASN   A OD1 1 
ATOM   1501 N ND2 . ASN   A 1 195 ? -13.919 18.177 -13.900 1.00 55.11  ? 235 ASN   A ND2 1 
ATOM   1502 N N   . ALA   A 1 196 ? -9.865  14.889 -13.677 1.00 32.49  ? 236 ALA   A N   1 
ATOM   1503 C CA  . ALA   A 1 196 ? -8.774  14.155 -14.311 1.00 32.61  ? 236 ALA   A CA  1 
ATOM   1504 C C   . ALA   A 1 196 ? -9.301  12.948 -15.083 1.00 32.61  ? 236 ALA   A C   1 
ATOM   1505 O O   . ALA   A 1 196 ? -8.851  12.678 -16.204 1.00 32.74  ? 236 ALA   A O   1 
ATOM   1506 C CB  . ALA   A 1 196 ? -7.744  13.728 -13.264 1.00 26.59  ? 236 ALA   A CB  1 
ATOM   1507 N N   . ARG   A 1 197 ? -10.265 12.221 -14.508 1.00 32.81  ? 237 ARG   A N   1 
ATOM   1508 C CA  . ARG   A 1 197 ? -10.832 11.064 -15.196 1.00 39.73  ? 237 ARG   A CA  1 
ATOM   1509 C C   . ARG   A 1 197 ? -11.478 11.464 -16.516 1.00 38.90  ? 237 ARG   A C   1 
ATOM   1510 O O   . ARG   A 1 197 ? -11.403 10.719 -17.502 1.00 37.09  ? 237 ARG   A O   1 
ATOM   1511 C CB  . ARG   A 1 197 ? -11.853 10.344 -14.302 1.00 40.77  ? 237 ARG   A CB  1 
ATOM   1512 C CG  . ARG   A 1 197 ? -12.564 9.200  -15.027 1.00 39.48  ? 237 ARG   A CG  1 
ATOM   1513 C CD  . ARG   A 1 197 ? -13.468 8.346  -14.150 1.00 42.28  ? 237 ARG   A CD  1 
ATOM   1514 N NE  . ARG   A 1 197 ? -13.282 6.935  -14.492 1.00 56.62  ? 237 ARG   A NE  1 
ATOM   1515 C CZ  . ARG   A 1 197 ? -13.963 5.913  -13.978 1.00 53.36  ? 237 ARG   A CZ  1 
ATOM   1516 N NH1 . ARG   A 1 197 ? -14.919 6.118  -13.083 1.00 41.56  ? 237 ARG   A NH1 1 
ATOM   1517 N NH2 . ARG   A 1 197 ? -13.681 4.676  -14.371 1.00 55.93  ? 237 ARG   A NH2 1 
ATOM   1518 N N   . ARG   A 1 198 ? -12.132 12.628 -16.557 1.00 35.97  ? 238 ARG   A N   1 
ATOM   1519 C CA  A ARG   A 1 198 ? -12.749 13.087 -17.797 0.50 37.22  ? 238 ARG   A CA  1 
ATOM   1520 C CA  B ARG   A 1 198 ? -12.749 13.067 -17.804 0.50 37.21  ? 238 ARG   A CA  1 
ATOM   1521 C C   . ARG   A 1 198 ? -11.701 13.278 -18.886 1.00 35.43  ? 238 ARG   A C   1 
ATOM   1522 O O   . ARG   A 1 198 ? -11.891 12.856 -20.033 1.00 37.28  ? 238 ARG   A O   1 
ATOM   1523 C CB  A ARG   A 1 198 ? -13.520 14.382 -17.534 0.50 37.95  ? 238 ARG   A CB  1 
ATOM   1524 C CB  B ARG   A 1 198 ? -13.563 14.344 -17.584 0.50 37.96  ? 238 ARG   A CB  1 
ATOM   1525 C CG  A ARG   A 1 198 ? -14.120 15.048 -18.756 0.50 38.67  ? 238 ARG   A CG  1 
ATOM   1526 C CG  B ARG   A 1 198 ? -14.964 14.092 -17.054 0.50 38.79  ? 238 ARG   A CG  1 
ATOM   1527 C CD  A ARG   A 1 198 ? -14.644 16.428 -18.375 0.50 45.17  ? 238 ARG   A CD  1 
ATOM   1528 C CD  B ARG   A 1 198 ? -15.769 15.375 -16.925 0.50 45.87  ? 238 ARG   A CD  1 
ATOM   1529 N NE  A ARG   A 1 198 ? -13.784 17.036 -17.363 0.50 50.75  ? 238 ARG   A NE  1 
ATOM   1530 N NE  B ARG   A 1 198 ? -17.082 15.113 -16.344 0.50 50.69  ? 238 ARG   A NE  1 
ATOM   1531 C CZ  A ARG   A 1 198 ? -12.761 17.838 -17.634 0.50 46.62  ? 238 ARG   A CZ  1 
ATOM   1532 C CZ  B ARG   A 1 198 ? -17.377 15.287 -15.061 0.50 52.84  ? 238 ARG   A CZ  1 
ATOM   1533 N NH1 A ARG   A 1 198 ? -12.025 18.332 -16.648 0.50 36.97  ? 238 ARG   A NH1 1 
ATOM   1534 N NH1 B ARG   A 1 198 ? -18.597 15.013 -14.619 0.50 59.94  ? 238 ARG   A NH1 1 
ATOM   1535 N NH2 A ARG   A 1 198 ? -12.484 18.156 -18.894 0.50 50.14  ? 238 ARG   A NH2 1 
ATOM   1536 N NH2 B ARG   A 1 198 ? -16.459 15.745 -14.222 0.50 49.83  ? 238 ARG   A NH2 1 
ATOM   1537 N N   . LEU   A 1 199 ? -10.580 13.910 -18.539 1.00 31.75  ? 239 LEU   A N   1 
ATOM   1538 C CA  . LEU   A 1 199 ? -9.500  14.084 -19.505 1.00 35.13  ? 239 LEU   A CA  1 
ATOM   1539 C C   . LEU   A 1 199 ? -8.872  12.744 -19.867 1.00 34.70  ? 239 LEU   A C   1 
ATOM   1540 O O   . LEU   A 1 199 ? -8.500  12.519 -21.025 1.00 35.18  ? 239 LEU   A O   1 
ATOM   1541 C CB  . LEU   A 1 199 ? -8.451  15.039 -18.945 1.00 31.83  ? 239 LEU   A CB  1 
ATOM   1542 C CG  . LEU   A 1 199 ? -8.891  16.490 -18.747 1.00 34.39  ? 239 LEU   A CG  1 
ATOM   1543 C CD1 . LEU   A 1 199 ? -7.821  17.251 -17.996 1.00 34.97  ? 239 LEU   A CD1 1 
ATOM   1544 C CD2 . LEU   A 1 199 ? -9.170  17.152 -20.095 1.00 35.39  ? 239 LEU   A CD2 1 
ATOM   1545 N N   . CYS   A 1 200 ? -8.771  11.836 -18.895 1.00 32.24  ? 240 CYS   A N   1 
ATOM   1546 C CA  . CYS   A 1 200 ? -8.206  10.517 -19.157 1.00 34.23  ? 240 CYS   A CA  1 
ATOM   1547 C C   . CYS   A 1 200 ? -9.061  9.731  -20.149 1.00 36.67  ? 240 CYS   A C   1 
ATOM   1548 O O   . CYS   A 1 200 ? -8.534  9.124  -21.091 1.00 33.79  ? 240 CYS   A O   1 
ATOM   1549 C CB  . CYS   A 1 200 ? -8.051  9.755  -17.842 1.00 29.58  ? 240 CYS   A CB  1 
ATOM   1550 S SG  . CYS   A 1 200 ? -7.175  8.174  -17.984 1.00 31.56  ? 240 CYS   A SG  1 
ATOM   1551 N N   . ASP   A 1 201 ? -10.386 9.721  -19.948 1.00 35.23  ? 241 ASP   A N   1 
ATOM   1552 C CA  . ASP   A 1 201 ? -11.280 9.044  -20.889 1.00 36.84  ? 241 ASP   A CA  1 
ATOM   1553 C C   . ASP   A 1 201 ? -11.148 9.621  -22.292 1.00 35.45  ? 241 ASP   A C   1 
ATOM   1554 O O   . ASP   A 1 201 ? -11.206 8.886  -23.285 1.00 37.08  ? 241 ASP   A O   1 
ATOM   1555 C CB  . ASP   A 1 201 ? -12.736 9.155  -20.427 1.00 37.40  ? 241 ASP   A CB  1 
ATOM   1556 C CG  . ASP   A 1 201 ? -13.111 8.124  -19.383 1.00 45.18  ? 241 ASP   A CG  1 
ATOM   1557 O OD1 . ASP   A 1 201 ? -12.429 7.084  -19.284 1.00 45.33  ? 241 ASP   A OD1 1 
ATOM   1558 O OD2 . ASP   A 1 201 ? -14.111 8.355  -18.665 1.00 48.45  ? 241 ASP   A OD2 1 
ATOM   1559 N N   . LEU   A 1 202 ? -10.990 10.942 -22.395 1.00 33.65  ? 242 LEU   A N   1 
ATOM   1560 C CA  . LEU   A 1 202 ? -10.888 11.581 -23.701 1.00 36.70  ? 242 LEU   A CA  1 
ATOM   1561 C C   . LEU   A 1 202 ? -9.618  11.174 -24.440 1.00 36.36  ? 242 LEU   A C   1 
ATOM   1562 O O   . LEU   A 1 202 ? -9.627  11.092 -25.674 1.00 36.33  ? 242 LEU   A O   1 
ATOM   1563 C CB  . LEU   A 1 202 ? -10.937 13.101 -23.544 1.00 39.65  ? 242 LEU   A CB  1 
ATOM   1564 C CG  . LEU   A 1 202 ? -12.303 13.719 -23.246 1.00 41.65  ? 242 LEU   A CG  1 
ATOM   1565 C CD1 . LEU   A 1 202 ? -12.139 15.188 -22.900 1.00 43.98  ? 242 LEU   A CD1 1 
ATOM   1566 C CD2 . LEU   A 1 202 ? -13.237 13.550 -24.430 1.00 43.05  ? 242 LEU   A CD2 1 
ATOM   1567 N N   . TYR   A 1 203 ? -8.528  10.912 -23.717 1.00 34.22  ? 243 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 203 ? -7.261  10.588 -24.365 1.00 34.81  ? 243 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 203 ? -7.075  9.086  -24.560 1.00 35.80  ? 243 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 203 ? -6.700  8.646  -25.650 1.00 37.72  ? 243 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 203 ? -6.092  11.165 -23.563 1.00 36.08  ? 243 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 203 ? -4.797  11.215 -24.336 1.00 36.34  ? 243 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 203 ? -4.487  12.310 -25.131 1.00 38.79  ? 243 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 203 ? -3.889  10.165 -24.282 1.00 40.14  ? 243 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 203 ? -3.310  12.362 -25.848 1.00 41.05  ? 243 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 203 ? -2.705  10.208 -24.997 1.00 42.75  ? 243 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 203 ? -2.424  11.311 -25.775 1.00 42.13  ? 243 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 203 ? -1.259  11.367 -26.494 1.00 48.20  ? 243 TYR   A OH  1 
ATOM   1579 N N   . TYR   A 1 204 ? -7.350  8.286  -23.534 1.00 34.46  ? 244 TYR   A N   1 
ATOM   1580 C CA  . TYR   A 1 204 ? -7.078  6.855  -23.577 1.00 32.91  ? 244 TYR   A CA  1 
ATOM   1581 C C   . TYR   A 1 204 ? -8.323  6.005  -23.775 1.00 33.63  ? 244 TYR   A C   1 
ATOM   1582 O O   . TYR   A 1 204 ? -8.201  4.781  -23.884 1.00 38.20  ? 244 TYR   A O   1 
ATOM   1583 C CB  . TYR   A 1 204 ? -6.360  6.413  -22.299 1.00 30.52  ? 244 TYR   A CB  1 
ATOM   1584 C CG  . TYR   A 1 204 ? -5.023  7.079  -22.096 1.00 32.43  ? 244 TYR   A CG  1 
ATOM   1585 C CD1 . TYR   A 1 204 ? -3.905  6.670  -22.819 1.00 33.91  ? 244 TYR   A CD1 1 
ATOM   1586 C CD2 . TYR   A 1 204 ? -4.873  8.118  -21.184 1.00 32.16  ? 244 TYR   A CD2 1 
ATOM   1587 C CE1 . TYR   A 1 204 ? -2.669  7.288  -22.640 1.00 30.42  ? 244 TYR   A CE1 1 
ATOM   1588 C CE2 . TYR   A 1 204 ? -3.646  8.738  -20.997 1.00 33.98  ? 244 TYR   A CE2 1 
ATOM   1589 C CZ  . TYR   A 1 204 ? -2.550  8.314  -21.727 1.00 32.59  ? 244 TYR   A CZ  1 
ATOM   1590 O OH  . TYR   A 1 204 ? -1.332  8.926  -21.537 1.00 36.36  ? 244 TYR   A OH  1 
ATOM   1591 N N   . ILE   A 1 205 ? -9.511  6.614  -23.833 1.00 32.26  ? 245 ILE   A N   1 
ATOM   1592 C CA  . ILE   A 1 205 ? -10.780 5.922  -24.080 1.00 33.35  ? 245 ILE   A CA  1 
ATOM   1593 C C   . ILE   A 1 205 ? -11.076 4.946  -22.942 1.00 33.39  ? 245 ILE   A C   1 
ATOM   1594 O O   . ILE   A 1 205 ? -11.849 3.996  -23.102 1.00 39.11  ? 245 ILE   A O   1 
ATOM   1595 C CB  . ILE   A 1 205 ? -10.792 5.208  -25.448 1.00 39.09  ? 245 ILE   A CB  1 
ATOM   1596 C CG1 . ILE   A 1 205 ? -9.993  5.995  -26.499 1.00 42.25  ? 245 ILE   A CG1 1 
ATOM   1597 C CG2 . ILE   A 1 205 ? -12.233 5.022  -25.950 1.00 44.38  ? 245 ILE   A CG2 1 
ATOM   1598 C CD1 . ILE   A 1 205 ? -10.446 7.450  -26.729 1.00 42.52  ? 245 ILE   A CD1 1 
ATOM   1599 N N   . ASN   A 1 206 ? -10.476 5.188  -21.782 1.00 34.26  ? 246 ASN   A N   1 
ATOM   1600 C CA  . ASN   A 1 206 ? -10.689 4.398  -20.575 1.00 33.28  ? 246 ASN   A CA  1 
ATOM   1601 C C   . ASN   A 1 206 ? -9.941  5.114  -19.463 1.00 33.52  ? 246 ASN   A C   1 
ATOM   1602 O O   . ASN   A 1 206 ? -9.179  6.050  -19.718 1.00 36.74  ? 246 ASN   A O   1 
ATOM   1603 C CB  . ASN   A 1 206 ? -10.200 2.950  -20.730 1.00 40.34  ? 246 ASN   A CB  1 
ATOM   1604 C CG  . ASN   A 1 206 ? -10.883 1.995  -19.767 1.00 45.26  ? 246 ASN   A CG  1 
ATOM   1605 O OD1 . ASN   A 1 206 ? -11.379 2.404  -18.714 1.00 50.42  ? 246 ASN   A OD1 1 
ATOM   1606 N ND2 . ASN   A 1 206 ? -10.917 0.719  -20.123 1.00 46.09  ? 246 ASN   A ND2 1 
ATOM   1607 N N   . SER   A 1 207 ? -10.158 4.672  -18.225 1.00 32.03  ? 247 SER   A N   1 
ATOM   1608 C CA  . SER   A 1 207 ? -9.540  5.366  -17.102 1.00 36.10  ? 247 SER   A CA  1 
ATOM   1609 C C   . SER   A 1 207 ? -9.604  4.482  -15.870 1.00 34.20  ? 247 SER   A C   1 
ATOM   1610 O O   . SER   A 1 207 ? -10.482 3.617  -15.777 1.00 34.97  ? 247 SER   A O   1 
ATOM   1611 C CB  . SER   A 1 207 ? -10.225 6.719  -16.831 1.00 36.77  ? 247 SER   A CB  1 
ATOM   1612 O OG  . SER   A 1 207 ? -11.640 6.623  -16.880 1.00 42.31  ? 247 SER   A OG  1 
ATOM   1613 N N   . PRO   A 1 208 ? -8.696  4.671  -14.917 1.00 35.04  ? 248 PRO   A N   1 
ATOM   1614 C CA  . PRO   A 1 208 ? -8.726  3.876  -13.686 1.00 35.57  ? 248 PRO   A CA  1 
ATOM   1615 C C   . PRO   A 1 208 ? -9.807  4.359  -12.735 1.00 34.97  ? 248 PRO   A C   1 
ATOM   1616 O O   . PRO   A 1 208 ? -10.176 5.536  -12.718 1.00 33.17  ? 248 PRO   A O   1 
ATOM   1617 C CB  . PRO   A 1 208 ? -7.337  4.111  -13.071 1.00 33.43  ? 248 PRO   A CB  1 
ATOM   1618 C CG  . PRO   A 1 208 ? -6.561  4.941  -14.076 1.00 35.70  ? 248 PRO   A CG  1 
ATOM   1619 C CD  . PRO   A 1 208 ? -7.577  5.626  -14.934 1.00 31.44  ? 248 PRO   A CD  1 
ATOM   1620 N N   . GLU   A 1 209 ? -10.297 3.432  -11.916 1.00 35.48  ? 249 GLU   A N   1 
ATOM   1621 C CA  . GLU   A 1 209 ? -11.216 3.796  -10.848 1.00 35.07  ? 249 GLU   A CA  1 
ATOM   1622 C C   . GLU   A 1 209 ? -10.452 4.452  -9.693  1.00 36.97  ? 249 GLU   A C   1 
ATOM   1623 O O   . GLU   A 1 209 ? -9.219  4.438  -9.631  1.00 36.38  ? 249 GLU   A O   1 
ATOM   1624 C CB  . GLU   A 1 209 ? -11.973 2.568  -10.336 1.00 38.75  ? 249 GLU   A CB  1 
ATOM   1625 C CG  . GLU   A 1 209 ? -12.704 1.767  -11.400 1.00 45.77  ? 249 GLU   A CG  1 
ATOM   1626 C CD  . GLU   A 1 209 ? -13.885 2.513  -11.993 1.00 58.44  ? 249 GLU   A CD  1 
ATOM   1627 O OE1 . GLU   A 1 209 ? -14.410 3.431  -11.326 1.00 61.83  ? 249 GLU   A OE1 1 
ATOM   1628 O OE2 . GLU   A 1 209 ? -14.287 2.183  -13.131 1.00 63.99  ? 249 GLU   A OE2 1 
ATOM   1629 N N   . LEU   A 1 210 ? -11.206 5.030  -8.764  1.00 34.83  ? 250 LEU   A N   1 
ATOM   1630 C CA  . LEU   A 1 210 ? -10.663 5.638  -7.557  1.00 33.64  ? 250 LEU   A CA  1 
ATOM   1631 C C   . LEU   A 1 210 ? -11.009 4.767  -6.358  1.00 33.81  ? 250 LEU   A C   1 
ATOM   1632 O O   . LEU   A 1 210 ? -12.162 4.352  -6.202  1.00 38.17  ? 250 LEU   A O   1 
ATOM   1633 C CB  . LEU   A 1 210 ? -11.226 7.049  -7.364  1.00 33.31  ? 250 LEU   A CB  1 
ATOM   1634 C CG  . LEU   A 1 210 ? -10.925 7.710  -6.016  1.00 32.44  ? 250 LEU   A CG  1 
ATOM   1635 C CD1 . LEU   A 1 210 ? -9.444  8.047  -5.889  1.00 28.76  ? 250 LEU   A CD1 1 
ATOM   1636 C CD2 . LEU   A 1 210 ? -11.769 8.961  -5.844  1.00 31.71  ? 250 LEU   A CD2 1 
ATOM   1637 N N   . GLU   A 1 211 ? -10.015 4.478  -5.521  1.00 33.56  ? 251 GLU   A N   1 
ATOM   1638 C CA  . GLU   A 1 211 ? -10.234 3.861  -4.214  1.00 34.27  ? 251 GLU   A CA  1 
ATOM   1639 C C   . GLU   A 1 211 ? -9.757  4.843  -3.152  1.00 36.36  ? 251 GLU   A C   1 
ATOM   1640 O O   . GLU   A 1 211 ? -8.560  5.138  -3.069  1.00 38.59  ? 251 GLU   A O   1 
ATOM   1641 C CB  . GLU   A 1 211 ? -9.503  2.522  -4.096  1.00 33.89  ? 251 GLU   A CB  1 
ATOM   1642 C CG  . GLU   A 1 211 ? -9.971  1.477  -5.099  1.00 37.73  ? 251 GLU   A CG  1 
ATOM   1643 C CD  . GLU   A 1 211 ? -9.285  0.139  -4.917  1.00 45.43  ? 251 GLU   A CD  1 
ATOM   1644 O OE1 . GLU   A 1 211 ? -8.325  0.046  -4.117  1.00 48.24  ? 251 GLU   A OE1 1 
ATOM   1645 O OE2 . GLU   A 1 211 ? -9.715  -0.826 -5.575  1.00 49.89  ? 251 GLU   A OE2 1 
ATOM   1646 N N   . LEU   A 1 212 ? -10.691 5.344  -2.348  1.00 34.36  ? 252 LEU   A N   1 
ATOM   1647 C CA  . LEU   A 1 212 ? -10.446 6.413  -1.386  1.00 37.89  ? 252 LEU   A CA  1 
ATOM   1648 C C   . LEU   A 1 212 ? -10.613 5.876  0.033   1.00 41.44  ? 252 LEU   A C   1 
ATOM   1649 O O   . LEU   A 1 212 ? -11.653 5.295  0.363   1.00 48.37  ? 252 LEU   A O   1 
ATOM   1650 C CB  . LEU   A 1 212 ? -11.412 7.578  -1.619  1.00 37.95  ? 252 LEU   A CB  1 
ATOM   1651 C CG  . LEU   A 1 212 ? -10.942 9.030  -1.711  1.00 43.38  ? 252 LEU   A CG  1 
ATOM   1652 C CD1 . LEU   A 1 212 ? -12.136 9.945  -1.506  1.00 45.10  ? 252 LEU   A CD1 1 
ATOM   1653 C CD2 . LEU   A 1 212 ? -9.827  9.367  -0.730  1.00 42.11  ? 252 LEU   A CD2 1 
ATOM   1654 N N   . GLU   A 1 213 ? -9.595  6.082  0.865   1.00 35.96  ? 253 GLU   A N   1 
ATOM   1655 C CA  . GLU   A 1 213 ? -9.593  5.696  2.271   1.00 37.11  ? 253 GLU   A CA  1 
ATOM   1656 C C   . GLU   A 1 213 ? -9.282  6.919  3.114   1.00 36.87  ? 253 GLU   A C   1 
ATOM   1657 O O   . GLU   A 1 213 ? -8.453  7.748  2.729   1.00 37.59  ? 253 GLU   A O   1 
ATOM   1658 C CB  . GLU   A 1 213 ? -8.530  4.645  2.542   1.00 50.04  ? 253 GLU   A CB  1 
ATOM   1659 C CG  . GLU   A 1 213 ? -9.014  3.290  2.960   1.00 72.42  ? 253 GLU   A CG  1 
ATOM   1660 C CD  . GLU   A 1 213 ? -7.849  2.406  3.370   1.00 85.46  ? 253 GLU   A CD  1 
ATOM   1661 O OE1 . GLU   A 1 213 ? -6.974  2.885  4.126   1.00 86.07  ? 253 GLU   A OE1 1 
ATOM   1662 O OE2 . GLU   A 1 213 ? -7.794  1.243  2.918   1.00 91.73  ? 253 GLU   A OE2 1 
ATOM   1663 N N   . GLU   A 1 214 ? -9.906  7.029  4.279   1.00 38.30  ? 254 GLU   A N   1 
ATOM   1664 C CA  . GLU   A 1 214 ? -9.600  8.159  5.140   1.00 40.00  ? 254 GLU   A CA  1 
ATOM   1665 C C   . GLU   A 1 214 ? -9.480  7.703  6.587   1.00 42.03  ? 254 GLU   A C   1 
ATOM   1666 O O   . GLU   A 1 214 ? -10.120 6.737  7.020   1.00 40.19  ? 254 GLU   A O   1 
ATOM   1667 C CB  . GLU   A 1 214 ? -10.648 9.268  5.018   1.00 41.55  ? 254 GLU   A CB  1 
ATOM   1668 C CG  . GLU   A 1 214 ? -11.973 8.946  5.649   1.00 45.94  ? 254 GLU   A CG  1 
ATOM   1669 C CD  . GLU   A 1 214 ? -12.960 10.083 5.505   1.00 59.22  ? 254 GLU   A CD  1 
ATOM   1670 O OE1 . GLU   A 1 214 ? -13.984 9.899  4.811   1.00 64.39  ? 254 GLU   A OE1 1 
ATOM   1671 O OE2 . GLU   A 1 214 ? -12.706 11.166 6.076   1.00 60.06  ? 254 GLU   A OE2 1 
ATOM   1672 N N   . LEU   A 1 215 ? -8.638  8.412  7.330   1.00 36.13  ? 255 LEU   A N   1 
ATOM   1673 C CA  . LEU   A 1 215 ? -8.458  8.159  8.754   1.00 42.88  ? 255 LEU   A CA  1 
ATOM   1674 C C   . LEU   A 1 215 ? -8.317  9.507  9.441   1.00 40.40  ? 255 LEU   A C   1 
ATOM   1675 O O   . LEU   A 1 215 ? -7.364  10.247 9.177   1.00 36.06  ? 255 LEU   A O   1 
ATOM   1676 C CB  . LEU   A 1 215 ? -7.241  7.274  9.018   1.00 41.15  ? 255 LEU   A CB  1 
ATOM   1677 C CG  . LEU   A 1 215 ? -6.934  7.076  10.503  1.00 44.70  ? 255 LEU   A CG  1 
ATOM   1678 C CD1 . LEU   A 1 215 ? -8.130  6.496  11.247  1.00 44.32  ? 255 LEU   A CD1 1 
ATOM   1679 C CD2 . LEU   A 1 215 ? -5.692  6.201  10.674  1.00 45.37  ? 255 LEU   A CD2 1 
ATOM   1680 N N   . ASN   A 1 216 ? -9.281  9.837  10.285  1.00 37.80  ? 256 ASN   A N   1 
ATOM   1681 C CA  . ASN   A 1 216 ? -9.190  11.007 11.149  1.00 41.49  ? 256 ASN   A CA  1 
ATOM   1682 C C   . ASN   A 1 216 ? -8.627  10.517 12.475  1.00 41.61  ? 256 ASN   A C   1 
ATOM   1683 O O   . ASN   A 1 216 ? -9.362  10.176 13.401  1.00 39.44  ? 256 ASN   A O   1 
ATOM   1684 C CB  . ASN   A 1 216 ? -10.552 11.672 11.299  1.00 42.13  ? 256 ASN   A CB  1 
ATOM   1685 C CG  . ASN   A 1 216 ? -10.481 13.000 12.025  1.00 48.38  ? 256 ASN   A CG  1 
ATOM   1686 O OD1 . ASN   A 1 216 ? -9.578  13.238 12.825  1.00 50.28  ? 256 ASN   A OD1 1 
ATOM   1687 N ND2 . ASN   A 1 216 ? -11.454 13.872 11.761  1.00 48.13  ? 256 ASN   A ND2 1 
ATOM   1688 N N   . ALA   A 1 217 ? -7.299  10.464 12.570  1.00 41.53  ? 257 ALA   A N   1 
ATOM   1689 C CA  . ALA   A 1 217 ? -6.683  10.006 13.811  1.00 44.14  ? 257 ALA   A CA  1 
ATOM   1690 C C   . ALA   A 1 217 ? -6.990  10.964 14.951  1.00 53.00  ? 257 ALA   A C   1 
ATOM   1691 O O   . ALA   A 1 217 ? -7.194  10.539 16.094  1.00 53.84  ? 257 ALA   A O   1 
ATOM   1692 C CB  . ALA   A 1 217 ? -5.176  9.856  13.635  1.00 42.48  ? 257 ALA   A CB  1 
ATOM   1693 N N   . LYS   A 1 218 ? -7.036  12.264 14.643  1.00 61.59  ? 258 LYS   A N   1 
ATOM   1694 C CA  . LYS   A 1 218 ? -7.363  13.286 15.634  1.00 73.93  ? 258 LYS   A CA  1 
ATOM   1695 C C   . LYS   A 1 218 ? -8.722  13.016 16.283  1.00 76.17  ? 258 LYS   A C   1 
ATOM   1696 O O   . LYS   A 1 218 ? -8.836  12.983 17.514  1.00 76.55  ? 258 LYS   A O   1 
ATOM   1697 C CB  . LYS   A 1 218 ? -7.329  14.667 14.964  1.00 78.10  ? 258 LYS   A CB  1 
ATOM   1698 C CG  . LYS   A 1 218 ? -7.149  15.861 15.900  1.00 84.64  ? 258 LYS   A CG  1 
ATOM   1699 C CD  . LYS   A 1 218 ? -5.849  15.766 16.690  1.00 88.51  ? 258 LYS   A CD  1 
ATOM   1700 C CE  . LYS   A 1 218 ? -5.445  17.100 17.327  1.00 87.85  ? 258 LYS   A CE  1 
ATOM   1701 N NZ  . LYS   A 1 218 ? -4.818  18.056 16.361  1.00 84.24  ? 258 LYS   A NZ  1 
ATOM   1702 N N   . SER   A 1 219 ? -9.762  12.812 15.468  1.00 77.49  ? 259 SER   A N   1 
ATOM   1703 C CA  . SER   A 1 219 ? -11.122 12.557 15.953  1.00 72.41  ? 259 SER   A CA  1 
ATOM   1704 C C   . SER   A 1 219 ? -11.759 11.493 15.070  1.00 63.54  ? 259 SER   A C   1 
ATOM   1705 O O   . SER   A 1 219 ? -12.412 11.809 14.066  1.00 60.61  ? 259 SER   A O   1 
ATOM   1706 C CB  . SER   A 1 219 ? -11.967 13.832 15.947  1.00 74.63  ? 259 SER   A CB  1 
ATOM   1707 O OG  . SER   A 1 219 ? -11.206 14.975 16.305  1.00 76.39  ? 259 SER   A OG  1 
ATOM   1708 N N   . PRO   A 1 220 ? -11.597 10.216 15.417  1.00 59.57  ? 260 PRO   A N   1 
ATOM   1709 C CA  . PRO   A 1 220 ? -11.962 9.138  14.483  1.00 58.92  ? 260 PRO   A CA  1 
ATOM   1710 C C   . PRO   A 1 220 ? -13.424 9.170  14.058  1.00 65.39  ? 260 PRO   A C   1 
ATOM   1711 O O   . PRO   A 1 220 ? -14.319 9.510  14.835  1.00 70.30  ? 260 PRO   A O   1 
ATOM   1712 C CB  . PRO   A 1 220 ? -11.637 7.866  15.272  1.00 56.24  ? 260 PRO   A CB  1 
ATOM   1713 C CG  . PRO   A 1 220 ? -10.555 8.287  16.208  1.00 56.90  ? 260 PRO   A CG  1 
ATOM   1714 C CD  . PRO   A 1 220 ? -10.877 9.706  16.596  1.00 57.77  ? 260 PRO   A CD  1 
ATOM   1715 N N   . GLY   A 1 221 ? -13.656 8.810  12.792  1.00 62.67  ? 261 GLY   A N   1 
ATOM   1716 C CA  . GLY   A 1 221 ? -14.982 8.820  12.205  1.00 65.67  ? 261 GLY   A CA  1 
ATOM   1717 C C   . GLY   A 1 221 ? -15.538 10.184 11.856  1.00 62.86  ? 261 GLY   A C   1 
ATOM   1718 O O   . GLY   A 1 221 ? -16.550 10.255 11.150  1.00 63.13  ? 261 GLY   A O   1 
ATOM   1719 N N   . GLN   A 1 222 ? -14.918 11.273 12.325  1.00 56.70  ? 262 GLN   A N   1 
ATOM   1720 C CA  . GLN   A 1 222 ? -15.361 12.622 12.010  1.00 56.31  ? 262 GLN   A CA  1 
ATOM   1721 C C   . GLN   A 1 222 ? -14.854 13.051 10.634  1.00 51.14  ? 262 GLN   A C   1 
ATOM   1722 O O   . GLN   A 1 222 ? -13.785 12.618 10.197  1.00 46.91  ? 262 GLN   A O   1 
ATOM   1723 C CB  . GLN   A 1 222 ? -14.861 13.603 13.065  1.00 53.76  ? 262 GLN   A CB  1 
ATOM   1724 C CG  . GLN   A 1 222 ? -15.475 13.392 14.421  1.00 64.69  ? 262 GLN   A CG  1 
ATOM   1725 C CD  . GLN   A 1 222 ? -16.981 13.518 14.381  1.00 71.86  ? 262 GLN   A CD  1 
ATOM   1726 O OE1 . GLN   A 1 222 ? -17.521 14.626 14.401  1.00 69.72  ? 262 GLN   A OE1 1 
ATOM   1727 N NE2 . GLN   A 1 222 ? -17.672 12.382 14.306  1.00 72.31  ? 262 GLN   A NE2 1 
ATOM   1728 N N   . PRO   A 1 223 ? -15.597 13.910 9.934   1.00 50.32  ? 263 PRO   A N   1 
ATOM   1729 C CA  . PRO   A 1 223 ? -15.112 14.407 8.644   1.00 45.24  ? 263 PRO   A CA  1 
ATOM   1730 C C   . PRO   A 1 223 ? -13.776 15.118 8.806   1.00 43.44  ? 263 PRO   A C   1 
ATOM   1731 O O   . PRO   A 1 223 ? -13.476 15.701 9.851   1.00 45.11  ? 263 PRO   A O   1 
ATOM   1732 C CB  . PRO   A 1 223 ? -16.213 15.376 8.196   1.00 48.89  ? 263 PRO   A CB  1 
ATOM   1733 C CG  . PRO   A 1 223 ? -17.427 14.966 8.956   1.00 50.82  ? 263 PRO   A CG  1 
ATOM   1734 C CD  . PRO   A 1 223 ? -16.927 14.447 10.272  1.00 53.96  ? 263 PRO   A CD  1 
ATOM   1735 N N   . ILE   A 1 224 ? -12.965 15.056 7.757   1.00 40.18  ? 264 ILE   A N   1 
ATOM   1736 C CA  . ILE   A 1 224 ? -11.637 15.654 7.756   1.00 38.71  ? 264 ILE   A CA  1 
ATOM   1737 C C   . ILE   A 1 224 ? -11.739 17.029 7.108   1.00 39.55  ? 264 ILE   A C   1 
ATOM   1738 O O   . ILE   A 1 224 ? -11.994 17.145 5.904   1.00 41.07  ? 264 ILE   A O   1 
ATOM   1739 C CB  . ILE   A 1 224 ? -10.623 14.761 7.034   1.00 38.49  ? 264 ILE   A CB  1 
ATOM   1740 C CG1 . ILE   A 1 224 ? -10.347 13.503 7.866   1.00 36.92  ? 264 ILE   A CG1 1 
ATOM   1741 C CG2 . ILE   A 1 224 ? -9.334  15.532 6.740   1.00 32.23  ? 264 ILE   A CG2 1 
ATOM   1742 C CD1 . ILE   A 1 224 ? -9.391  12.530 7.174   1.00 37.23  ? 264 ILE   A CD1 1 
ATOM   1743 N N   . GLN   A 1 225 ? -11.541 18.074 7.907   1.00 40.03  ? 265 GLN   A N   1 
ATOM   1744 C CA  . GLN   A 1 225 ? -11.511 19.445 7.421   1.00 42.46  ? 265 GLN   A CA  1 
ATOM   1745 C C   . GLN   A 1 225 ? -10.277 20.159 7.951   1.00 46.50  ? 265 GLN   A C   1 
ATOM   1746 O O   . GLN   A 1 225 ? -9.763  19.831 9.023   1.00 50.68  ? 265 GLN   A O   1 
ATOM   1747 C CB  . GLN   A 1 225 ? -12.754 20.223 7.842   1.00 40.93  ? 265 GLN   A CB  1 
ATOM   1748 C CG  . GLN   A 1 225 ? -14.058 19.580 7.453   1.00 48.07  ? 265 GLN   A CG  1 
ATOM   1749 C CD  . GLN   A 1 225 ? -15.247 20.373 7.943   1.00 55.81  ? 265 GLN   A CD  1 
ATOM   1750 O OE1 . GLN   A 1 225 ? -15.254 20.862 9.074   1.00 56.28  ? 265 GLN   A OE1 1 
ATOM   1751 N NE2 . GLN   A 1 225 ? -16.256 20.522 7.087   1.00 57.96  ? 265 GLN   A NE2 1 
ATOM   1752 N N   . VAL   A 1 226 ? -9.804  21.143 7.185   1.00 41.59  ? 266 VAL   A N   1 
ATOM   1753 C CA  . VAL   A 1 226 ? -8.738  22.035 7.623   1.00 40.40  ? 266 VAL   A CA  1 
ATOM   1754 C C   . VAL   A 1 226 ? -9.028  23.428 7.084   1.00 41.89  ? 266 VAL   A C   1 
ATOM   1755 O O   . VAL   A 1 226 ? -9.855  23.616 6.188   1.00 41.39  ? 266 VAL   A O   1 
ATOM   1756 C CB  . VAL   A 1 226 ? -7.329  21.584 7.164   1.00 39.05  ? 266 VAL   A CB  1 
ATOM   1757 C CG1 . VAL   A 1 226 ? -6.876  20.354 7.936   1.00 45.98  ? 266 VAL   A CG1 1 
ATOM   1758 C CG2 . VAL   A 1 226 ? -7.309  21.323 5.673   1.00 32.66  ? 266 VAL   A CG2 1 
ATOM   1759 N N   . VAL   A 1 227 ? -8.345  24.413 7.659   1.00 43.06  ? 267 VAL   A N   1 
ATOM   1760 C CA  . VAL   A 1 227 ? -8.319  25.757 7.094   1.00 41.13  ? 267 VAL   A CA  1 
ATOM   1761 C C   . VAL   A 1 227 ? -7.363  25.734 5.911   1.00 41.00  ? 267 VAL   A C   1 
ATOM   1762 O O   . VAL   A 1 227 ? -6.173  25.449 6.078   1.00 44.47  ? 267 VAL   A O   1 
ATOM   1763 C CB  . VAL   A 1 227 ? -7.875  26.785 8.141   1.00 37.23  ? 267 VAL   A CB  1 
ATOM   1764 C CG1 . VAL   A 1 227 ? -8.006  28.183 7.582   1.00 43.40  ? 267 VAL   A CG1 1 
ATOM   1765 C CG2 . VAL   A 1 227 ? -8.687  26.634 9.427   1.00 37.96  ? 267 VAL   A CG2 1 
ATOM   1766 N N   . TYR   A 1 228 ? -7.872  26.005 4.710   1.00 40.15  ? 268 TYR   A N   1 
ATOM   1767 C CA  . TYR   A 1 228 ? -7.002  25.943 3.543   1.00 40.74  ? 268 TYR   A CA  1 
ATOM   1768 C C   . TYR   A 1 228 ? -7.612  26.742 2.401   1.00 42.12  ? 268 TYR   A C   1 
ATOM   1769 O O   . TYR   A 1 228 ? -8.758  27.188 2.471   1.00 38.80  ? 268 TYR   A O   1 
ATOM   1770 C CB  . TYR   A 1 228 ? -6.745  24.493 3.115   1.00 38.94  ? 268 TYR   A CB  1 
ATOM   1771 C CG  . TYR   A 1 228 ? -5.393  24.317 2.472   1.00 40.63  ? 268 TYR   A CG  1 
ATOM   1772 C CD1 . TYR   A 1 228 ? -4.229  24.431 3.225   1.00 38.15  ? 268 TYR   A CD1 1 
ATOM   1773 C CD2 . TYR   A 1 228 ? -5.274  24.055 1.111   1.00 37.53  ? 268 TYR   A CD2 1 
ATOM   1774 C CE1 . TYR   A 1 228 ? -2.983  24.280 2.646   1.00 36.28  ? 268 TYR   A CE1 1 
ATOM   1775 C CE2 . TYR   A 1 228 ? -4.025  23.894 0.518   1.00 37.03  ? 268 TYR   A CE2 1 
ATOM   1776 C CZ  . TYR   A 1 228 ? -2.889  24.013 1.292   1.00 36.35  ? 268 TYR   A CZ  1 
ATOM   1777 O OH  . TYR   A 1 228 ? -1.649  23.872 0.714   1.00 35.99  ? 268 TYR   A OH  1 
ATOM   1778 N N   . VAL   A 1 229 ? -6.817  26.922 1.346   1.00 41.57  ? 269 VAL   A N   1 
ATOM   1779 C CA  . VAL   A 1 229 ? -7.289  27.499 0.090   1.00 41.92  ? 269 VAL   A CA  1 
ATOM   1780 C C   . VAL   A 1 229 ? -7.699  26.342 -0.820  1.00 42.46  ? 269 VAL   A C   1 
ATOM   1781 O O   . VAL   A 1 229 ? -6.817  25.610 -1.305  1.00 39.25  ? 269 VAL   A O   1 
ATOM   1782 C CB  . VAL   A 1 229 ? -6.218  28.369 -0.580  1.00 41.12  ? 269 VAL   A CB  1 
ATOM   1783 C CG1 . VAL   A 1 229 ? -6.762  28.939 -1.884  1.00 37.81  ? 269 VAL   A CG1 1 
ATOM   1784 C CG2 . VAL   A 1 229 ? -5.793  29.501 0.352   1.00 48.29  ? 269 VAL   A CG2 1 
ATOM   1785 N N   . PRO   A 1 230 ? -8.995  26.139 -1.070  1.00 42.19  ? 270 PRO   A N   1 
ATOM   1786 C CA  . PRO   A 1 230 ? -9.416  24.924 -1.788  1.00 41.22  ? 270 PRO   A CA  1 
ATOM   1787 C C   . PRO   A 1 230 ? -8.829  24.813 -3.180  1.00 38.99  ? 270 PRO   A C   1 
ATOM   1788 O O   . PRO   A 1 230 ? -8.498  23.706 -3.617  1.00 37.28  ? 270 PRO   A O   1 
ATOM   1789 C CB  . PRO   A 1 230 ? -10.944 25.056 -1.819  1.00 43.11  ? 270 PRO   A CB  1 
ATOM   1790 C CG  . PRO   A 1 230 ? -11.265 25.969 -0.667  1.00 43.18  ? 270 PRO   A CG  1 
ATOM   1791 C CD  . PRO   A 1 230 ? -10.137 26.949 -0.625  1.00 41.40  ? 270 PRO   A CD  1 
ATOM   1792 N N   . SER   A 1 231 ? -8.685  25.927 -3.896  1.00 37.46  ? 271 SER   A N   1 
ATOM   1793 C CA  . SER   A 1 231 ? -8.139  25.834 -5.244  1.00 36.67  ? 271 SER   A CA  1 
ATOM   1794 C C   . SER   A 1 231 ? -6.677  25.404 -5.221  1.00 36.96  ? 271 SER   A C   1 
ATOM   1795 O O   . SER   A 1 231 ? -6.214  24.751 -6.163  1.00 38.50  ? 271 SER   A O   1 
ATOM   1796 C CB  . SER   A 1 231 ? -8.305  27.164 -5.978  1.00 36.52  ? 271 SER   A CB  1 
ATOM   1797 O OG  . SER   A 1 231 ? -7.549  28.188 -5.358  1.00 41.30  ? 271 SER   A OG  1 
ATOM   1798 N N   . HIS   A 1 232 ? -5.944  25.731 -4.154  1.00 33.77  ? 272 HIS   A N   1 
ATOM   1799 C CA  . HIS   A 1 232 ? -4.574  25.235 -4.030  1.00 36.82  ? 272 HIS   A CA  1 
ATOM   1800 C C   . HIS   A 1 232 ? -4.563  23.721 -3.875  1.00 36.08  ? 272 HIS   A C   1 
ATOM   1801 O O   . HIS   A 1 232 ? -3.765  23.023 -4.514  1.00 32.64  ? 272 HIS   A O   1 
ATOM   1802 C CB  . HIS   A 1 232 ? -3.866  25.888 -2.841  1.00 39.16  ? 272 HIS   A CB  1 
ATOM   1803 C CG  . HIS   A 1 232 ? -3.542  27.337 -3.035  1.00 43.80  ? 272 HIS   A CG  1 
ATOM   1804 N ND1 . HIS   A 1 232 ? -2.646  28.009 -2.231  1.00 44.58  ? 272 HIS   A ND1 1 
ATOM   1805 C CD2 . HIS   A 1 232 ? -4.003  28.247 -3.927  1.00 44.79  ? 272 HIS   A CD2 1 
ATOM   1806 C CE1 . HIS   A 1 232 ? -2.568  29.270 -2.619  1.00 45.78  ? 272 HIS   A CE1 1 
ATOM   1807 N NE2 . HIS   A 1 232 ? -3.378  29.440 -3.649  1.00 45.99  ? 272 HIS   A NE2 1 
ATOM   1808 N N   . LEU   A 1 233 ? -5.432  23.195 -3.008  1.00 32.36  ? 273 LEU   A N   1 
ATOM   1809 C CA  . LEU   A 1 233 ? -5.522  21.747 -2.844  1.00 33.63  ? 273 LEU   A CA  1 
ATOM   1810 C C   . LEU   A 1 233 ? -6.019  21.083 -4.122  1.00 30.16  ? 273 LEU   A C   1 
ATOM   1811 O O   . LEU   A 1 233 ? -5.519  20.023 -4.509  1.00 30.62  ? 273 LEU   A O   1 
ATOM   1812 C CB  . LEU   A 1 233 ? -6.442  21.406 -1.670  1.00 33.75  ? 273 LEU   A CB  1 
ATOM   1813 C CG  . LEU   A 1 233 ? -6.676  19.919 -1.383  1.00 32.82  ? 273 LEU   A CG  1 
ATOM   1814 C CD1 . LEU   A 1 233 ? -5.370  19.219 -1.061  1.00 33.42  ? 273 LEU   A CD1 1 
ATOM   1815 C CD2 . LEU   A 1 233 ? -7.668  19.753 -0.243  1.00 32.39  ? 273 LEU   A CD2 1 
ATOM   1816 N N   . TYR   A 1 234 ? -7.013  21.685 -4.784  1.00 29.88  ? 274 TYR   A N   1 
ATOM   1817 C CA  . TYR   A 1 234 ? -7.506  21.122 -6.036  1.00 33.44  ? 274 TYR   A CA  1 
ATOM   1818 C C   . TYR   A 1 234 ? -6.379  21.003 -7.052  1.00 33.69  ? 274 TYR   A C   1 
ATOM   1819 O O   . TYR   A 1 234 ? -6.202  19.953 -7.682  1.00 32.56  ? 274 TYR   A O   1 
ATOM   1820 C CB  . TYR   A 1 234 ? -8.643  21.977 -6.601  1.00 31.11  ? 274 TYR   A CB  1 
ATOM   1821 C CG  . TYR   A 1 234 ? -9.130  21.463 -7.943  1.00 35.43  ? 274 TYR   A CG  1 
ATOM   1822 C CD1 . TYR   A 1 234 ? -10.119 20.485 -8.017  1.00 37.11  ? 274 TYR   A CD1 1 
ATOM   1823 C CD2 . TYR   A 1 234 ? -8.582  21.933 -9.133  1.00 32.18  ? 274 TYR   A CD2 1 
ATOM   1824 C CE1 . TYR   A 1 234 ? -10.554 19.998 -9.241  1.00 39.18  ? 274 TYR   A CE1 1 
ATOM   1825 C CE2 . TYR   A 1 234 ? -9.002  21.446 -10.357 1.00 34.20  ? 274 TYR   A CE2 1 
ATOM   1826 C CZ  . TYR   A 1 234 ? -9.987  20.481 -10.404 1.00 38.32  ? 274 TYR   A CZ  1 
ATOM   1827 O OH  . TYR   A 1 234 ? -10.411 20.003 -11.618 1.00 40.49  ? 274 TYR   A OH  1 
ATOM   1828 N N   . HIS   A 1 235 ? -5.606  22.081 -7.225  1.00 32.49  ? 275 HIS   A N   1 
ATOM   1829 C CA  . HIS   A 1 235 ? -4.531  22.071 -8.213  1.00 34.77  ? 275 HIS   A CA  1 
ATOM   1830 C C   . HIS   A 1 235 ? -3.571  20.918 -7.965  1.00 30.91  ? 275 HIS   A C   1 
ATOM   1831 O O   . HIS   A 1 235 ? -3.173  20.213 -8.903  1.00 31.21  ? 275 HIS   A O   1 
ATOM   1832 C CB  . HIS   A 1 235 ? -3.781  23.404 -8.189  1.00 40.30  ? 275 HIS   A CB  1 
ATOM   1833 C CG  . HIS   A 1 235 ? -2.726  23.521 -9.248  1.00 52.49  ? 275 HIS   A CG  1 
ATOM   1834 N ND1 . HIS   A 1 235 ? -1.532  22.833 -9.193  1.00 55.14  ? 275 HIS   A ND1 1 
ATOM   1835 C CD2 . HIS   A 1 235 ? -2.686  24.250 -10.389 1.00 57.28  ? 275 HIS   A CD2 1 
ATOM   1836 C CE1 . HIS   A 1 235 ? -0.804  23.133 -10.253 1.00 56.97  ? 275 HIS   A CE1 1 
ATOM   1837 N NE2 . HIS   A 1 235 ? -1.482  23.989 -10.996 1.00 55.13  ? 275 HIS   A NE2 1 
ATOM   1838 N N   . MET   A 1 236 ? -3.189  20.704 -6.707  1.00 28.41  ? 276 MET   A N   1 
ATOM   1839 C CA  . MET   A 1 236 ? -2.237  19.647 -6.401  1.00 30.17  ? 276 MET   A CA  1 
ATOM   1840 C C   . MET   A 1 236 ? -2.802  18.276 -6.746  1.00 31.41  ? 276 MET   A C   1 
ATOM   1841 O O   . MET   A 1 236 ? -2.153  17.486 -7.438  1.00 33.21  ? 276 MET   A O   1 
ATOM   1842 C CB  . MET   A 1 236 ? -1.843  19.701 -4.931  1.00 27.48  ? 276 MET   A CB  1 
ATOM   1843 C CG  . MET   A 1 236 ? -1.102  20.955 -4.549  1.00 35.47  ? 276 MET   A CG  1 
ATOM   1844 S SD  . MET   A 1 236 ? -0.526  20.904 -2.839  1.00 40.20  ? 276 MET   A SD  1 
ATOM   1845 C CE  . MET   A 1 236 ? -2.059  21.026 -1.949  1.00 36.35  ? 276 MET   A CE  1 
ATOM   1846 N N   . VAL   A 1 237 ? -4.007  17.966 -6.266  1.00 29.36  ? 277 VAL   A N   1 
ATOM   1847 C CA  . VAL   A 1 237 ? -4.514  16.607 -6.442  1.00 32.37  ? 277 VAL   A CA  1 
ATOM   1848 C C   . VAL   A 1 237 ? -4.883  16.354 -7.901  1.00 28.53  ? 277 VAL   A C   1 
ATOM   1849 O O   . VAL   A 1 237 ? -4.685  15.249 -8.418  1.00 30.35  ? 277 VAL   A O   1 
ATOM   1850 C CB  . VAL   A 1 237 ? -5.697  16.339 -5.498  1.00 35.45  ? 277 VAL   A CB  1 
ATOM   1851 C CG1 . VAL   A 1 237 ? -5.245  16.445 -4.041  1.00 34.24  ? 277 VAL   A CG1 1 
ATOM   1852 C CG2 . VAL   A 1 237 ? -6.822  17.309 -5.770  1.00 45.15  ? 277 VAL   A CG2 1 
ATOM   1853 N N   . PHE   A 1 238 ? -5.419  17.372 -8.584  1.00 29.25  ? 278 PHE   A N   1 
ATOM   1854 C CA  . PHE   A 1 238 ? -5.752  17.255 -10.001 1.00 30.93  ? 278 PHE   A CA  1 
ATOM   1855 C C   . PHE   A 1 238 ? -4.508  16.948 -10.824 1.00 29.52  ? 278 PHE   A C   1 
ATOM   1856 O O   . PHE   A 1 238 ? -4.518  16.051 -11.670 1.00 30.37  ? 278 PHE   A O   1 
ATOM   1857 C CB  . PHE   A 1 238 ? -6.436  18.549 -10.470 1.00 30.28  ? 278 PHE   A CB  1 
ATOM   1858 C CG  . PHE   A 1 238 ? -6.750  18.616 -11.951 1.00 32.45  ? 278 PHE   A CG  1 
ATOM   1859 C CD1 . PHE   A 1 238 ? -7.611  17.706 -12.550 1.00 31.90  ? 278 PHE   A CD1 1 
ATOM   1860 C CD2 . PHE   A 1 238 ? -6.238  19.649 -12.726 1.00 33.54  ? 278 PHE   A CD2 1 
ATOM   1861 C CE1 . PHE   A 1 238 ? -7.915  17.795 -13.912 1.00 31.65  ? 278 PHE   A CE1 1 
ATOM   1862 C CE2 . PHE   A 1 238 ? -6.539  19.750 -14.087 1.00 34.64  ? 278 PHE   A CE2 1 
ATOM   1863 C CZ  . PHE   A 1 238 ? -7.384  18.817 -14.681 1.00 33.19  ? 278 PHE   A CZ  1 
ATOM   1864 N N   . GLU   A 1 239 ? -3.413  17.667 -10.572 1.00 27.64  ? 279 GLU   A N   1 
ATOM   1865 C CA  . GLU   A 1 239 ? -2.189  17.403 -11.318 1.00 29.66  ? 279 GLU   A CA  1 
ATOM   1866 C C   . GLU   A 1 239 ? -1.636  16.019 -11.001 1.00 31.95  ? 279 GLU   A C   1 
ATOM   1867 O O   . GLU   A 1 239 ? -1.182  15.307 -11.904 1.00 29.96  ? 279 GLU   A O   1 
ATOM   1868 C CB  . GLU   A 1 239 ? -1.145  18.482 -11.032 1.00 29.07  ? 279 GLU   A CB  1 
ATOM   1869 C CG  . GLU   A 1 239 ? -1.513  19.857 -11.614 1.00 41.00  ? 279 GLU   A CG  1 
ATOM   1870 C CD  . GLU   A 1 239 ? -1.580  19.853 -13.144 1.00 46.59  ? 279 GLU   A CD  1 
ATOM   1871 O OE1 . GLU   A 1 239 ? -0.820  19.074 -13.775 1.00 39.52  ? 279 GLU   A OE1 1 
ATOM   1872 O OE2 . GLU   A 1 239 ? -2.396  20.625 -13.706 1.00 37.46  ? 279 GLU   A OE2 1 
ATOM   1873 N N   . LEU   A 1 240 ? -1.673  15.617 -9.729  1.00 29.54  ? 280 LEU   A N   1 
ATOM   1874 C CA  . LEU   A 1 240 ? -1.193  14.289 -9.361  1.00 29.95  ? 280 LEU   A CA  1 
ATOM   1875 C C   . LEU   A 1 240 ? -2.040  13.195 -10.006 1.00 29.13  ? 280 LEU   A C   1 
ATOM   1876 O O   . LEU   A 1 240 ? -1.500  12.210 -10.526 1.00 31.25  ? 280 LEU   A O   1 
ATOM   1877 C CB  . LEU   A 1 240 ? -1.176  14.139 -7.838  1.00 29.16  ? 280 LEU   A CB  1 
ATOM   1878 C CG  . LEU   A 1 240 ? -0.105  14.948 -7.090  1.00 29.86  ? 280 LEU   A CG  1 
ATOM   1879 C CD1 . LEU   A 1 240 ? -0.212  14.757 -5.576  1.00 27.88  ? 280 LEU   A CD1 1 
ATOM   1880 C CD2 . LEU   A 1 240 ? 1.284   14.580 -7.585  1.00 31.11  ? 280 LEU   A CD2 1 
ATOM   1881 N N   . PHE   A 1 241 ? -3.368  13.354 -9.994  1.00 28.17  ? 281 PHE   A N   1 
ATOM   1882 C CA  . PHE   A 1 241 ? -4.235  12.366 -10.637 1.00 29.27  ? 281 PHE   A CA  1 
ATOM   1883 C C   . PHE   A 1 241 ? -3.900  12.205 -12.119 1.00 30.35  ? 281 PHE   A C   1 
ATOM   1884 O O   . PHE   A 1 241 ? -3.839  11.079 -12.631 1.00 30.59  ? 281 PHE   A O   1 
ATOM   1885 C CB  . PHE   A 1 241 ? -5.700  12.764 -10.469 1.00 29.59  ? 281 PHE   A CB  1 
ATOM   1886 C CG  . PHE   A 1 241 ? -6.345  12.226 -9.228  1.00 31.28  ? 281 PHE   A CG  1 
ATOM   1887 C CD1 . PHE   A 1 241 ? -6.299  10.871 -8.928  1.00 27.65  ? 281 PHE   A CD1 1 
ATOM   1888 C CD2 . PHE   A 1 241 ? -7.013  13.078 -8.363  1.00 31.50  ? 281 PHE   A CD2 1 
ATOM   1889 C CE1 . PHE   A 1 241 ? -6.902  10.383 -7.783  1.00 30.34  ? 281 PHE   A CE1 1 
ATOM   1890 C CE2 . PHE   A 1 241 ? -7.622  12.594 -7.215  1.00 33.50  ? 281 PHE   A CE2 1 
ATOM   1891 C CZ  . PHE   A 1 241 ? -7.561  11.247 -6.925  1.00 31.89  ? 281 PHE   A CZ  1 
ATOM   1892 N N   . LYS   A 1 242 ? -3.674  13.318 -12.826 1.00 28.56  ? 282 LYS   A N   1 
ATOM   1893 C CA  . LYS   A 1 242 ? -3.353  13.238 -14.249 1.00 30.95  ? 282 LYS   A CA  1 
ATOM   1894 C C   . LYS   A 1 242 ? -2.058  12.465 -14.486 1.00 31.99  ? 282 LYS   A C   1 
ATOM   1895 O O   . LYS   A 1 242 ? -1.953  11.685 -15.442 1.00 29.35  ? 282 LYS   A O   1 
ATOM   1896 C CB  . LYS   A 1 242 ? -3.266  14.644 -14.847 1.00 26.92  ? 282 LYS   A CB  1 
ATOM   1897 C CG  . LYS   A 1 242 ? -4.631  15.340 -14.983 1.00 28.48  ? 282 LYS   A CG  1 
ATOM   1898 C CD  . LYS   A 1 242 ? -4.537  16.634 -15.769 1.00 33.82  ? 282 LYS   A CD  1 
ATOM   1899 C CE  . LYS   A 1 242 ? -3.805  17.700 -14.984 1.00 34.05  ? 282 LYS   A CE  1 
ATOM   1900 N NZ  . LYS   A 1 242 ? -3.631  18.933 -15.782 1.00 34.85  ? 282 LYS   A NZ  1 
ATOM   1901 N N   . ASN   A 1 243 ? -1.057  12.674 -13.630 1.00 31.64  ? 283 ASN   A N   1 
ATOM   1902 C CA  . ASN   A 1 243 ? 0.193   11.935 -13.764 1.00 34.04  ? 283 ASN   A CA  1 
ATOM   1903 C C   . ASN   A 1 243 ? 0.004   10.461 -13.447 1.00 33.46  ? 283 ASN   A C   1 
ATOM   1904 O O   . ASN   A 1 243 ? 0.548   9.594  -14.147 1.00 31.90  ? 283 ASN   A O   1 
ATOM   1905 C CB  . ASN   A 1 243 ? 1.254   12.531 -12.849 1.00 35.85  ? 283 ASN   A CB  1 
ATOM   1906 C CG  . ASN   A 1 243 ? 1.860   13.782 -13.418 1.00 38.65  ? 283 ASN   A CG  1 
ATOM   1907 O OD1 . ASN   A 1 243 ? 2.811   13.716 -14.191 1.00 37.29  ? 283 ASN   A OD1 1 
ATOM   1908 N ND2 . ASN   A 1 243 ? 1.308   14.934 -13.052 1.00 37.03  ? 283 ASN   A ND2 1 
ATOM   1909 N N   . ALA   A 1 244 ? -0.751  10.161 -12.387 1.00 31.23  ? 284 ALA   A N   1 
ATOM   1910 C CA  . ALA   A 1 244 ? -0.989  8.769  -12.021 1.00 30.48  ? 284 ALA   A CA  1 
ATOM   1911 C C   . ALA   A 1 244 ? -1.765  8.046  -13.112 1.00 29.79  ? 284 ALA   A C   1 
ATOM   1912 O O   . ALA   A 1 244 ? -1.468  6.889  -13.436 1.00 31.05  ? 284 ALA   A O   1 
ATOM   1913 C CB  . ALA   A 1 244 ? -1.736  8.702  -10.691 1.00 27.29  ? 284 ALA   A CB  1 
ATOM   1914 N N   . MET   A 1 245 ? -2.760  8.718  -13.694 1.00 29.90  ? 285 MET   A N   1 
ATOM   1915 C CA  . MET   A 1 245 ? -3.580  8.102  -14.730 1.00 30.55  ? 285 MET   A CA  1 
ATOM   1916 C C   . MET   A 1 245 ? -2.782  7.860  -15.996 1.00 28.35  ? 285 MET   A C   1 
ATOM   1917 O O   . MET   A 1 245 ? -2.891  6.791  -16.608 1.00 31.23  ? 285 MET   A O   1 
ATOM   1918 C CB  . MET   A 1 245 ? -4.788  8.986  -15.034 1.00 30.12  ? 285 MET   A CB  1 
ATOM   1919 C CG  . MET   A 1 245 ? -5.849  8.937  -13.955 1.00 30.21  ? 285 MET   A CG  1 
ATOM   1920 S SD  . MET   A 1 245 ? -7.128  10.149 -14.214 1.00 34.54  ? 285 MET   A SD  1 
ATOM   1921 C CE  . MET   A 1 245 ? -8.158  9.848  -12.788 1.00 31.38  ? 285 MET   A CE  1 
ATOM   1922 N N   . ARG   A 1 246 ? -2.002  8.854  -16.420 1.00 28.61  ? 286 ARG   A N   1 
ATOM   1923 C CA  . ARG   A 1 246 ? -1.153  8.689  -17.593 1.00 34.67  ? 286 ARG   A CA  1 
ATOM   1924 C C   . ARG   A 1 246 ? -0.259  7.467  -17.448 1.00 35.08  ? 286 ARG   A C   1 
ATOM   1925 O O   . ARG   A 1 246 ? -0.196  6.618  -18.344 1.00 35.40  ? 286 ARG   A O   1 
ATOM   1926 C CB  . ARG   A 1 246 ? -0.313  9.946  -17.808 1.00 49.26  ? 286 ARG   A CB  1 
ATOM   1927 C CG  . ARG   A 1 246 ? 0.907   9.722  -18.668 1.00 52.91  ? 286 ARG   A CG  1 
ATOM   1928 C CD  . ARG   A 1 246 ? 1.091   10.850 -19.634 1.00 57.55  ? 286 ARG   A CD  1 
ATOM   1929 N NE  . ARG   A 1 246 ? 2.494   11.089 -19.938 1.00 70.60  ? 286 ARG   A NE  1 
ATOM   1930 C CZ  . ARG   A 1 246 ? 2.930   11.568 -21.099 1.00 78.35  ? 286 ARG   A CZ  1 
ATOM   1931 N NH1 . ARG   A 1 246 ? 4.227   11.766 -21.285 1.00 77.52  ? 286 ARG   A NH1 1 
ATOM   1932 N NH2 . ARG   A 1 246 ? 2.069   11.835 -22.078 1.00 81.67  ? 286 ARG   A NH2 1 
ATOM   1933 N N   . ALA   A 1 247 ? 0.423   7.352  -16.306 1.00 33.03  ? 287 ALA   A N   1 
ATOM   1934 C CA  . ALA   A 1 247 ? 1.314   6.216  -16.093 1.00 31.18  ? 287 ALA   A CA  1 
ATOM   1935 C C   . ALA   A 1 247 ? 0.545   4.901  -16.120 1.00 30.13  ? 287 ALA   A C   1 
ATOM   1936 O O   . ALA   A 1 247 ? 0.981   3.931  -16.751 1.00 32.28  ? 287 ALA   A O   1 
ATOM   1937 C CB  . ALA   A 1 247 ? 2.059   6.378  -14.768 1.00 30.90  ? 287 ALA   A CB  1 
ATOM   1938 N N   . THR   A 1 248 ? -0.608  4.858  -15.449 1.00 28.79  ? 288 THR   A N   1 
ATOM   1939 C CA  . THR   A 1 248 ? -1.412  3.638  -15.407 1.00 31.73  ? 288 THR   A CA  1 
ATOM   1940 C C   . THR   A 1 248 ? -1.878  3.240  -16.801 1.00 32.84  ? 288 THR   A C   1 
ATOM   1941 O O   . THR   A 1 248 ? -1.766  2.072  -17.200 1.00 32.60  ? 288 THR   A O   1 
ATOM   1942 C CB  . THR   A 1 248 ? -2.616  3.839  -14.482 1.00 32.98  ? 288 THR   A CB  1 
ATOM   1943 O OG1 . THR   A 1 248 ? -2.165  4.191  -13.170 1.00 34.89  ? 288 THR   A OG1 1 
ATOM   1944 C CG2 . THR   A 1 248 ? -3.461  2.567  -14.401 1.00 34.18  ? 288 THR   A CG2 1 
ATOM   1945 N N   . MET   A 1 249 ? -2.402  4.200  -17.569 1.00 28.71  ? 289 MET   A N   1 
ATOM   1946 C CA  . MET   A 1 249 ? -2.969  3.856  -18.869 1.00 32.59  ? 289 MET   A CA  1 
ATOM   1947 C C   . MET   A 1 249 ? -1.892  3.400  -19.844 1.00 32.81  ? 289 MET   A C   1 
ATOM   1948 O O   . MET   A 1 249 ? -2.120  2.489  -20.648 1.00 33.92  ? 289 MET   A O   1 
ATOM   1949 C CB  . MET   A 1 249 ? -3.742  5.041  -19.453 1.00 32.80  ? 289 MET   A CB  1 
ATOM   1950 C CG  . MET   A 1 249 ? -4.923  5.505  -18.599 1.00 35.03  ? 289 MET   A CG  1 
ATOM   1951 S SD  . MET   A 1 249 ? -5.977  4.167  -17.987 1.00 36.19  ? 289 MET   A SD  1 
ATOM   1952 C CE  . MET   A 1 249 ? -6.664  3.534  -19.518 1.00 35.92  ? 289 MET   A CE  1 
ATOM   1953 N N   . GLU   A 1 250 ? -0.712  4.016  -19.795 1.00 32.76  ? 290 GLU   A N   1 
ATOM   1954 C CA  . GLU   A 1 250 ? 0.322   3.633  -20.747 1.00 41.24  ? 290 GLU   A CA  1 
ATOM   1955 C C   . GLU   A 1 250 ? 0.998   2.331  -20.347 1.00 40.52  ? 290 GLU   A C   1 
ATOM   1956 O O   . GLU   A 1 250 ? 1.315   1.510  -21.218 1.00 37.45  ? 290 GLU   A O   1 
ATOM   1957 C CB  . GLU   A 1 250 ? 1.330   4.773  -20.902 1.00 42.20  ? 290 GLU   A CB  1 
ATOM   1958 C CG  . GLU   A 1 250 ? 0.643   6.002  -21.475 1.00 48.32  ? 290 GLU   A CG  1 
ATOM   1959 C CD  . GLU   A 1 250 ? 1.582   7.092  -21.946 1.00 57.07  ? 290 GLU   A CD  1 
ATOM   1960 O OE1 . GLU   A 1 250 ? 2.739   7.146  -21.475 1.00 62.16  ? 290 GLU   A OE1 1 
ATOM   1961 O OE2 . GLU   A 1 250 ? 1.139   7.908  -22.790 1.00 56.99  ? 290 GLU   A OE2 1 
ATOM   1962 N N   . HIS   A 1 251 ? 1.175   2.097  -19.047 1.00 38.56  ? 291 HIS   A N   1 
ATOM   1963 C CA  . HIS   A 1 251 ? 1.869   0.889  -18.620 1.00 38.45  ? 291 HIS   A CA  1 
ATOM   1964 C C   . HIS   A 1 251 ? 1.028   -0.358 -18.873 1.00 43.94  ? 291 HIS   A C   1 
ATOM   1965 O O   . HIS   A 1 251 ? 1.564   -1.406 -19.241 1.00 42.93  ? 291 HIS   A O   1 
ATOM   1966 C CB  . HIS   A 1 251 ? 2.259   0.987  -17.146 1.00 33.33  ? 291 HIS   A CB  1 
ATOM   1967 C CG  . HIS   A 1 251 ? 3.188   -0.101 -16.709 1.00 42.53  ? 291 HIS   A CG  1 
ATOM   1968 N ND1 . HIS   A 1 251 ? 2.848   -1.035 -15.753 1.00 44.93  ? 291 HIS   A ND1 1 
ATOM   1969 C CD2 . HIS   A 1 251 ? 4.432   -0.427 -17.128 1.00 40.64  ? 291 HIS   A CD2 1 
ATOM   1970 C CE1 . HIS   A 1 251 ? 3.849   -1.881 -15.591 1.00 41.10  ? 291 HIS   A CE1 1 
ATOM   1971 N NE2 . HIS   A 1 251 ? 4.822   -1.533 -16.413 1.00 44.05  ? 291 HIS   A NE2 1 
ATOM   1972 N N   . HIS   A 1 252 ? -0.289  -0.267 -18.705 1.00 47.69  ? 292 HIS   A N   1 
ATOM   1973 C CA  . HIS   A 1 252 ? -1.153  -1.436 -18.821 1.00 46.16  ? 292 HIS   A CA  1 
ATOM   1974 C C   . HIS   A 1 252 ? -1.900  -1.503 -20.149 1.00 48.33  ? 292 HIS   A C   1 
ATOM   1975 O O   . HIS   A 1 252 ? -2.797  -2.341 -20.300 1.00 48.03  ? 292 HIS   A O   1 
ATOM   1976 C CB  . HIS   A 1 252 ? -2.142  -1.473 -17.656 1.00 41.09  ? 292 HIS   A CB  1 
ATOM   1977 C CG  . HIS   A 1 252 ? -1.486  -1.688 -16.329 1.00 43.30  ? 292 HIS   A CG  1 
ATOM   1978 N ND1 . HIS   A 1 252 ? -1.150  -2.941 -15.861 1.00 45.10  ? 292 HIS   A ND1 1 
ATOM   1979 C CD2 . HIS   A 1 252 ? -1.077  -0.810 -15.383 1.00 42.78  ? 292 HIS   A CD2 1 
ATOM   1980 C CE1 . HIS   A 1 252 ? -0.575  -2.827 -14.677 1.00 46.73  ? 292 HIS   A CE1 1 
ATOM   1981 N NE2 . HIS   A 1 252 ? -0.519  -1.544 -14.363 1.00 44.66  ? 292 HIS   A NE2 1 
ATOM   1982 N N   . ALA   A 1 253 ? -1.536  -0.654 -21.118 1.00 44.62  ? 293 ALA   A N   1 
ATOM   1983 C CA  . ALA   A 1 253 ? -2.234  -0.624 -22.399 1.00 50.77  ? 293 ALA   A CA  1 
ATOM   1984 C C   . ALA   A 1 253 ? -2.300  -2.000 -23.051 1.00 59.36  ? 293 ALA   A C   1 
ATOM   1985 O O   . ALA   A 1 253 ? -3.291  -2.322 -23.715 1.00 60.51  ? 293 ALA   A O   1 
ATOM   1986 C CB  . ALA   A 1 253 ? -1.556  0.374  -23.337 1.00 45.52  ? 293 ALA   A CB  1 
ATOM   1987 N N   . ASN   A 1 254 ? -1.269  -2.829 -22.871 1.00 67.97  ? 294 ASN   A N   1 
ATOM   1988 C CA  . ASN   A 1 254 ? -1.301  -4.166 -23.460 1.00 79.88  ? 294 ASN   A CA  1 
ATOM   1989 C C   . ASN   A 1 254 ? -2.353  -5.041 -22.792 1.00 77.89  ? 294 ASN   A C   1 
ATOM   1990 O O   . ASN   A 1 254 ? -3.098  -5.753 -23.475 1.00 77.98  ? 294 ASN   A O   1 
ATOM   1991 C CB  . ASN   A 1 254 ? 0.073   -4.826 -23.361 1.00 92.50  ? 294 ASN   A CB  1 
ATOM   1992 C CG  . ASN   A 1 254 ? 1.101   -4.173 -24.258 1.00 100.87 ? 294 ASN   A CG  1 
ATOM   1993 O OD1 . ASN   A 1 254 ? 0.758   -3.451 -25.197 1.00 102.01 ? 294 ASN   A OD1 1 
ATOM   1994 N ND2 . ASN   A 1 254 ? 2.375   -4.430 -23.980 1.00 105.33 ? 294 ASN   A ND2 1 
ATOM   1995 N N   . ARG   A 1 255 ? -2.428  -4.998 -21.459 1.00 77.32  ? 295 ARG   A N   1 
ATOM   1996 C CA  . ARG   A 1 255 ? -3.365  -5.852 -20.737 1.00 76.58  ? 295 ARG   A CA  1 
ATOM   1997 C C   . ARG   A 1 255 ? -4.811  -5.462 -21.019 1.00 71.22  ? 295 ARG   A C   1 
ATOM   1998 O O   . ARG   A 1 255 ? -5.679  -6.333 -21.150 1.00 76.46  ? 295 ARG   A O   1 
ATOM   1999 C CB  . ARG   A 1 255 ? -3.091  -5.793 -19.232 1.00 77.11  ? 295 ARG   A CB  1 
ATOM   2000 C CG  . ARG   A 1 255 ? -1.759  -6.378 -18.787 1.00 81.45  ? 295 ARG   A CG  1 
ATOM   2001 C CD  . ARG   A 1 255 ? -0.650  -5.338 -18.821 1.00 82.21  ? 295 ARG   A CD  1 
ATOM   2002 N NE  . ARG   A 1 255 ? 0.243   -5.452 -17.671 1.00 80.72  ? 295 ARG   A NE  1 
ATOM   2003 C CZ  . ARG   A 1 255 ? 1.392   -4.795 -17.551 1.00 81.50  ? 295 ARG   A CZ  1 
ATOM   2004 N NH1 . ARG   A 1 255 ? 1.794   -3.981 -18.518 1.00 84.90  ? 295 ARG   A NH1 1 
ATOM   2005 N NH2 . ARG   A 1 255 ? 2.142   -4.956 -16.470 1.00 80.61  ? 295 ARG   A NH2 1 
ATOM   2006 N N   . GLY   A 1 256 ? -5.095  -4.165 -21.110 1.00 63.47  ? 296 GLY   A N   1 
ATOM   2007 C CA  . GLY   A 1 256 ? -6.464  -3.710 -21.206 1.00 63.27  ? 296 GLY   A CA  1 
ATOM   2008 C C   . GLY   A 1 256 ? -7.223  -3.699 -19.896 1.00 65.09  ? 296 GLY   A C   1 
ATOM   2009 O O   . GLY   A 1 256 ? -8.409  -3.341 -19.888 1.00 66.07  ? 296 GLY   A O   1 
ATOM   2010 N N   . VAL   A 1 257 ? -6.587  -4.096 -18.796 1.00 61.43  ? 297 VAL   A N   1 
ATOM   2011 C CA  . VAL   A 1 257 ? -7.150  -3.998 -17.454 1.00 59.39  ? 297 VAL   A CA  1 
ATOM   2012 C C   . VAL   A 1 257 ? -6.326  -2.975 -16.688 1.00 59.61  ? 297 VAL   A C   1 
ATOM   2013 O O   . VAL   A 1 257 ? -5.093  -3.069 -16.652 1.00 65.30  ? 297 VAL   A O   1 
ATOM   2014 C CB  . VAL   A 1 257 ? -7.138  -5.355 -16.733 1.00 60.83  ? 297 VAL   A CB  1 
ATOM   2015 C CG1 . VAL   A 1 257 ? -7.776  -5.224 -15.355 1.00 63.43  ? 297 VAL   A CG1 1 
ATOM   2016 C CG2 . VAL   A 1 257 ? -7.835  -6.416 -17.574 1.00 60.56  ? 297 VAL   A CG2 1 
ATOM   2017 N N   . TYR   A 1 258 ? -6.997  -2.005 -16.073 1.00 55.01  ? 298 TYR   A N   1 
ATOM   2018 C CA  . TYR   A 1 258 ? -6.305  -0.858 -15.496 1.00 45.47  ? 298 TYR   A CA  1 
ATOM   2019 C C   . TYR   A 1 258 ? -6.505  -0.810 -13.990 1.00 41.55  ? 298 TYR   A C   1 
ATOM   2020 O O   . TYR   A 1 258 ? -7.650  -0.673 -13.523 1.00 44.41  ? 298 TYR   A O   1 
ATOM   2021 C CB  . TYR   A 1 258 ? -6.780  0.432  -16.160 1.00 39.74  ? 298 TYR   A CB  1 
ATOM   2022 C CG  . TYR   A 1 258 ? -6.502  0.369  -17.634 1.00 38.18  ? 298 TYR   A CG  1 
ATOM   2023 C CD1 . TYR   A 1 258 ? -5.231  0.634  -18.126 1.00 37.59  ? 298 TYR   A CD1 1 
ATOM   2024 C CD2 . TYR   A 1 258 ? -7.486  -0.034 -18.529 1.00 44.28  ? 298 TYR   A CD2 1 
ATOM   2025 C CE1 . TYR   A 1 258 ? -4.954  0.544  -19.468 1.00 42.62  ? 298 TYR   A CE1 1 
ATOM   2026 C CE2 . TYR   A 1 258 ? -7.221  -0.126 -19.882 1.00 47.21  ? 298 TYR   A CE2 1 
ATOM   2027 C CZ  . TYR   A 1 258 ? -5.952  0.165  -20.345 1.00 49.07  ? 298 TYR   A CZ  1 
ATOM   2028 O OH  . TYR   A 1 258 ? -5.675  0.081  -21.689 1.00 51.49  ? 298 TYR   A OH  1 
ATOM   2029 N N   . PRO   A 1 259 ? -5.434  -0.926 -13.204 1.00 39.22  ? 299 PRO   A N   1 
ATOM   2030 C CA  . PRO   A 1 259 ? -5.595  -0.930 -11.756 1.00 40.47  ? 299 PRO   A CA  1 
ATOM   2031 C C   . PRO   A 1 259 ? -6.072  0.425  -11.272 1.00 37.98  ? 299 PRO   A C   1 
ATOM   2032 O O   . PRO   A 1 259 ? -5.784  1.462  -11.896 1.00 40.35  ? 299 PRO   A O   1 
ATOM   2033 C CB  . PRO   A 1 259 ? -4.177  -1.240 -11.242 1.00 38.52  ? 299 PRO   A CB  1 
ATOM   2034 C CG  . PRO   A 1 259 ? -3.391  -1.668 -12.446 1.00 41.70  ? 299 PRO   A CG  1 
ATOM   2035 C CD  . PRO   A 1 259 ? -4.022  -0.998 -13.608 1.00 38.09  ? 299 PRO   A CD  1 
ATOM   2036 N N   . PRO   A 1 260 ? -6.808  0.468  -10.170 1.00 35.43  ? 300 PRO   A N   1 
ATOM   2037 C CA  . PRO   A 1 260 ? -7.312  1.749  -9.668  1.00 36.98  ? 300 PRO   A CA  1 
ATOM   2038 C C   . PRO   A 1 260 ? -6.178  2.626  -9.169  1.00 38.06  ? 300 PRO   A C   1 
ATOM   2039 O O   . PRO   A 1 260 ? -5.046  2.193  -8.952  1.00 38.67  ? 300 PRO   A O   1 
ATOM   2040 C CB  . PRO   A 1 260 ? -8.244  1.338  -8.522  1.00 38.45  ? 300 PRO   A CB  1 
ATOM   2041 C CG  . PRO   A 1 260 ? -7.756  -0.015 -8.103  1.00 40.74  ? 300 PRO   A CG  1 
ATOM   2042 C CD  . PRO   A 1 260 ? -7.228  -0.673 -9.337  1.00 36.45  ? 300 PRO   A CD  1 
ATOM   2043 N N   . ILE   A 1 261 ? -6.501  3.891  -8.981  1.00 33.65  ? 301 ILE   A N   1 
ATOM   2044 C CA  . ILE   A 1 261 ? -5.631  4.801  -8.259  1.00 31.85  ? 301 ILE   A CA  1 
ATOM   2045 C C   . ILE   A 1 261 ? -6.110  4.838  -6.818  1.00 36.43  ? 301 ILE   A C   1 
ATOM   2046 O O   . ILE   A 1 261 ? -7.305  5.020  -6.556  1.00 34.10  ? 301 ILE   A O   1 
ATOM   2047 C CB  . ILE   A 1 261 ? -5.629  6.187  -8.911  1.00 34.94  ? 301 ILE   A CB  1 
ATOM   2048 C CG1 . ILE   A 1 261 ? -5.027  6.040  -10.312 1.00 39.08  ? 301 ILE   A CG1 1 
ATOM   2049 C CG2 . ILE   A 1 261 ? -4.866  7.178  -8.060  1.00 32.13  ? 301 ILE   A CG2 1 
ATOM   2050 C CD1 . ILE   A 1 261 ? -5.082  7.272  -11.106 1.00 42.84  ? 301 ILE   A CD1 1 
ATOM   2051 N N   . GLN   A 1 262 ? -5.199  4.587  -5.886  1.00 33.88  ? 302 GLN   A N   1 
ATOM   2052 C CA  . GLN   A 1 262 ? -5.536  4.532  -4.471  1.00 31.64  ? 302 GLN   A CA  1 
ATOM   2053 C C   . GLN   A 1 262 ? -5.127  5.834  -3.805  1.00 37.28  ? 302 GLN   A C   1 
ATOM   2054 O O   . GLN   A 1 262 ? -4.026  6.342  -4.047  1.00 40.53  ? 302 GLN   A O   1 
ATOM   2055 C CB  . GLN   A 1 262 ? -4.848  3.344  -3.800  1.00 34.28  ? 302 GLN   A CB  1 
ATOM   2056 C CG  . GLN   A 1 262 ? -5.254  2.022  -4.428  1.00 43.73  ? 302 GLN   A CG  1 
ATOM   2057 C CD  . GLN   A 1 262 ? -4.501  0.843  -3.868  1.00 53.62  ? 302 GLN   A CD  1 
ATOM   2058 O OE1 . GLN   A 1 262 ? -3.271  0.853  -3.797  1.00 56.97  ? 302 GLN   A OE1 1 
ATOM   2059 N NE2 . GLN   A 1 262 ? -5.235  -0.188 -3.468  1.00 58.82  ? 302 GLN   A NE2 1 
ATOM   2060 N N   . VAL   A 1 263 ? -6.020  6.383  -2.985  1.00 32.90  ? 303 VAL   A N   1 
ATOM   2061 C CA  . VAL   A 1 263 ? -5.750  7.603  -2.237  1.00 31.23  ? 303 VAL   A CA  1 
ATOM   2062 C C   . VAL   A 1 263 ? -6.056  7.330  -0.776  1.00 35.39  ? 303 VAL   A C   1 
ATOM   2063 O O   . VAL   A 1 263 ? -7.134  6.825  -0.447  1.00 34.72  ? 303 VAL   A O   1 
ATOM   2064 C CB  . VAL   A 1 263 ? -6.573  8.801  -2.748  1.00 29.08  ? 303 VAL   A CB  1 
ATOM   2065 C CG1 . VAL   A 1 263 ? -6.352  10.016 -1.855  1.00 28.82  ? 303 VAL   A CG1 1 
ATOM   2066 C CG2 . VAL   A 1 263 ? -6.180  9.141  -4.188  1.00 30.59  ? 303 VAL   A CG2 1 
ATOM   2067 N N   . HIS   A 1 264 ? -5.102  7.635  0.096   1.00 31.03  ? 304 HIS   A N   1 
ATOM   2068 C CA  A HIS   A 1 264 ? -5.286  7.521  1.536   0.51 33.57  ? 304 HIS   A CA  1 
ATOM   2069 C CA  B HIS   A 1 264 ? -5.285  7.519  1.537   0.49 33.59  ? 304 HIS   A CA  1 
ATOM   2070 C C   . HIS   A 1 264 ? -5.100  8.900  2.145   1.00 33.67  ? 304 HIS   A C   1 
ATOM   2071 O O   . HIS   A 1 264 ? -4.053  9.529  1.952   1.00 31.37  ? 304 HIS   A O   1 
ATOM   2072 C CB  A HIS   A 1 264 ? -4.301  6.522  2.143   0.51 35.25  ? 304 HIS   A CB  1 
ATOM   2073 C CB  B HIS   A 1 264 ? -4.300  6.514  2.143   0.49 35.26  ? 304 HIS   A CB  1 
ATOM   2074 C CG  A HIS   A 1 264 ? -4.683  6.053  3.511   0.51 35.28  ? 304 HIS   A CG  1 
ATOM   2075 C CG  B HIS   A 1 264 ? -4.367  5.147  1.529   0.49 40.09  ? 304 HIS   A CG  1 
ATOM   2076 N ND1 A HIS   A 1 264 ? -5.429  6.820  4.381   0.51 39.33  ? 304 HIS   A ND1 1 
ATOM   2077 N ND1 B HIS   A 1 264 ? -3.514  4.736  0.526   0.49 41.25  ? 304 HIS   A ND1 1 
ATOM   2078 C CD2 A HIS   A 1 264 ? -4.436  4.889  4.154   0.51 38.70  ? 304 HIS   A CD2 1 
ATOM   2079 C CD2 B HIS   A 1 264 ? -5.185  4.096  1.778   0.49 42.96  ? 304 HIS   A CD2 1 
ATOM   2080 C CE1 A HIS   A 1 264 ? -5.618  6.152  5.504   0.51 35.38  ? 304 HIS   A CE1 1 
ATOM   2081 C CE1 B HIS   A 1 264 ? -3.801  3.491  0.187   0.49 40.01  ? 304 HIS   A CE1 1 
ATOM   2082 N NE2 A HIS   A 1 264 ? -5.025  4.977  5.392   0.51 39.34  ? 304 HIS   A NE2 1 
ATOM   2083 N NE2 B HIS   A 1 264 ? -4.816  3.082  0.927   0.49 42.67  ? 304 HIS   A NE2 1 
ATOM   2084 N N   . VAL   A 1 265 ? -6.114  9.372  2.866   1.00 33.53  ? 305 VAL   A N   1 
ATOM   2085 C CA  . VAL   A 1 265 ? -6.098  10.679 3.515   1.00 35.75  ? 305 VAL   A CA  1 
ATOM   2086 C C   . VAL   A 1 265 ? -6.037  10.470 5.021   1.00 36.62  ? 305 VAL   A C   1 
ATOM   2087 O O   . VAL   A 1 265 ? -6.838  9.712  5.586   1.00 33.63  ? 305 VAL   A O   1 
ATOM   2088 C CB  . VAL   A 1 265 ? -7.331  11.518 3.134   1.00 35.81  ? 305 VAL   A CB  1 
ATOM   2089 C CG1 . VAL   A 1 265 ? -7.306  12.873 3.846   1.00 30.75  ? 305 VAL   A CG1 1 
ATOM   2090 C CG2 . VAL   A 1 265 ? -7.390  11.697 1.634   1.00 34.09  ? 305 VAL   A CG2 1 
ATOM   2091 N N   . THR   A 1 266 ? -5.099  11.149 5.674   1.00 32.28  ? 306 THR   A N   1 
ATOM   2092 C CA  . THR   A 1 266 ? -4.922  11.021 7.113   1.00 35.14  ? 306 THR   A CA  1 
ATOM   2093 C C   . THR   A 1 266 ? -4.797  12.399 7.740   1.00 34.46  ? 306 THR   A C   1 
ATOM   2094 O O   . THR   A 1 266 ? -4.023  13.234 7.262   1.00 35.69  ? 306 THR   A O   1 
ATOM   2095 C CB  . THR   A 1 266 ? -3.678  10.188 7.451   1.00 40.43  ? 306 THR   A CB  1 
ATOM   2096 O OG1 . THR   A 1 266 ? -3.763  8.912  6.807   1.00 45.48  ? 306 THR   A OG1 1 
ATOM   2097 C CG2 . THR   A 1 266 ? -3.591  9.969  8.945   1.00 45.87  ? 306 THR   A CG2 1 
ATOM   2098 N N   . LEU   A 1 267 ? -5.544  12.628 8.813   1.00 36.99  ? 307 LEU   A N   1 
ATOM   2099 C CA  . LEU   A 1 267 ? -5.417  13.838 9.618   1.00 37.14  ? 307 LEU   A CA  1 
ATOM   2100 C C   . LEU   A 1 267 ? -4.746  13.453 10.930  1.00 34.53  ? 307 LEU   A C   1 
ATOM   2101 O O   . LEU   A 1 267 ? -5.350  12.783 11.774  1.00 36.78  ? 307 LEU   A O   1 
ATOM   2102 C CB  . LEU   A 1 267 ? -6.775  14.490 9.863   1.00 37.08  ? 307 LEU   A CB  1 
ATOM   2103 C CG  . LEU   A 1 267 ? -6.703  15.824 10.611  1.00 38.75  ? 307 LEU   A CG  1 
ATOM   2104 C CD1 . LEU   A 1 267 ? -5.898  16.829 9.798   1.00 41.72  ? 307 LEU   A CD1 1 
ATOM   2105 C CD2 . LEU   A 1 267 ? -8.090  16.349 10.903  1.00 40.36  ? 307 LEU   A CD2 1 
ATOM   2106 N N   . GLY   A 1 268 ? -3.492  13.866 11.098  1.00 37.11  ? 308 GLY   A N   1 
ATOM   2107 C CA  . GLY   A 1 268 ? -2.768  13.636 12.326  1.00 37.48  ? 308 GLY   A CA  1 
ATOM   2108 C C   . GLY   A 1 268 ? -2.780  14.869 13.213  1.00 39.75  ? 308 GLY   A C   1 
ATOM   2109 O O   . GLY   A 1 268 ? -3.375  15.892 12.895  1.00 41.86  ? 308 GLY   A O   1 
ATOM   2110 N N   . ASN   A 1 269 ? -2.083  14.751 14.345  1.00 42.46  ? 309 ASN   A N   1 
ATOM   2111 C CA  A ASN   A 1 269 ? -2.008  15.861 15.292  0.50 46.12  ? 309 ASN   A CA  1 
ATOM   2112 C CA  B ASN   A 1 269 ? -2.006  15.858 15.292  0.50 46.12  ? 309 ASN   A CA  1 
ATOM   2113 C C   . ASN   A 1 269 ? -1.387  17.099 14.660  1.00 45.22  ? 309 ASN   A C   1 
ATOM   2114 O O   . ASN   A 1 269 ? -1.678  18.224 15.082  1.00 46.11  ? 309 ASN   A O   1 
ATOM   2115 C CB  A ASN   A 1 269 ? -1.200  15.456 16.529  0.50 48.39  ? 309 ASN   A CB  1 
ATOM   2116 C CB  B ASN   A 1 269 ? -1.203  15.426 16.520  0.50 48.40  ? 309 ASN   A CB  1 
ATOM   2117 C CG  A ASN   A 1 269 ? -1.953  14.501 17.443  0.50 52.43  ? 309 ASN   A CG  1 
ATOM   2118 C CG  B ASN   A 1 269 ? -1.077  16.526 17.551  0.50 49.64  ? 309 ASN   A CG  1 
ATOM   2119 O OD1 A ASN   A 1 269 ? -3.177  14.555 17.548  0.50 51.58  ? 309 ASN   A OD1 1 
ATOM   2120 O OD1 B ASN   A 1 269 ? -2.067  16.937 18.157  0.50 52.15  ? 309 ASN   A OD1 1 
ATOM   2121 N ND2 A ASN   A 1 269 ? -1.216  13.625 18.118  0.50 56.27  ? 309 ASN   A ND2 1 
ATOM   2122 N ND2 B ASN   A 1 269 ? 0.148   16.999 17.768  0.50 46.53  ? 309 ASN   A ND2 1 
ATOM   2123 N N   . GLU   A 1 270 ? -0.569  16.920 13.670  1.00 35.89  ? 310 GLU   A N   1 
ATOM   2124 C CA  . GLU   A 1 270 ? 0.218   17.977 13.057  1.00 41.01  ? 310 GLU   A CA  1 
ATOM   2125 C C   . GLU   A 1 270 ? 0.103   18.010 11.538  1.00 39.99  ? 310 GLU   A C   1 
ATOM   2126 O O   . GLU   A 1 270 ? 0.099   19.096 10.945  1.00 37.22  ? 310 GLU   A O   1 
ATOM   2127 C CB  . GLU   A 1 270 ? 1.674   17.747 13.506  1.00 49.88  ? 310 GLU   A CB  1 
ATOM   2128 C CG  . GLU   A 1 270 ? 2.648   18.836 13.193  1.00 55.19  ? 310 GLU   A CG  1 
ATOM   2129 C CD  . GLU   A 1 270 ? 3.987   18.630 13.890  1.00 48.99  ? 310 GLU   A CD  1 
ATOM   2130 O OE1 . GLU   A 1 270 ? 4.031   18.011 14.982  1.00 46.01  ? 310 GLU   A OE1 1 
ATOM   2131 O OE2 . GLU   A 1 270 ? 5.000   19.095 13.339  1.00 45.63  ? 310 GLU   A OE2 1 
ATOM   2132 N N   . ASP   A 1 271 ? -0.003  16.851 10.887  1.00 35.52  ? 311 ASP   A N   1 
ATOM   2133 C CA  . ASP   A 1 271 ? 0.015   16.749 9.436   1.00 37.71  ? 311 ASP   A CA  1 
ATOM   2134 C C   . ASP   A 1 271 ? -1.347  16.318 8.916   1.00 34.90  ? 311 ASP   A C   1 
ATOM   2135 O O   . ASP   A 1 271 ? -1.950  15.378 9.444   1.00 37.83  ? 311 ASP   A O   1 
ATOM   2136 C CB  . ASP   A 1 271 ? 1.055   15.734 8.958   1.00 36.79  ? 311 ASP   A CB  1 
ATOM   2137 C CG  . ASP   A 1 271 ? 2.483   16.153 9.260   1.00 43.76  ? 311 ASP   A CG  1 
ATOM   2138 O OD1 . ASP   A 1 271 ? 2.727   17.352 9.514   1.00 40.69  ? 311 ASP   A OD1 1 
ATOM   2139 O OD2 . ASP   A 1 271 ? 3.369   15.270 9.213   1.00 42.26  ? 311 ASP   A OD2 1 
ATOM   2140 N N   . LEU   A 1 272 ? -1.828  17.014 7.897   1.00 32.60  ? 312 LEU   A N   1 
ATOM   2141 C CA  . LEU   A 1 272 ? -2.778  16.445 6.953   1.00 34.45  ? 312 LEU   A CA  1 
ATOM   2142 C C   . LEU   A 1 272 ? -1.968  15.859 5.806   1.00 34.83  ? 312 LEU   A C   1 
ATOM   2143 O O   . LEU   A 1 272 ? -1.216  16.585 5.141   1.00 35.51  ? 312 LEU   A O   1 
ATOM   2144 C CB  . LEU   A 1 272 ? -3.749  17.504 6.432   1.00 33.80  ? 312 LEU   A CB  1 
ATOM   2145 C CG  . LEU   A 1 272 ? -4.643  17.099 5.253   1.00 38.91  ? 312 LEU   A CG  1 
ATOM   2146 C CD1 . LEU   A 1 272 ? -5.654  16.040 5.669   1.00 39.12  ? 312 LEU   A CD1 1 
ATOM   2147 C CD2 . LEU   A 1 272 ? -5.369  18.324 4.685   1.00 41.15  ? 312 LEU   A CD2 1 
ATOM   2148 N N   . THR   A 1 273 ? -2.102  14.559 5.568   1.00 32.99  ? 313 THR   A N   1 
ATOM   2149 C CA  . THR   A 1 273 ? -1.390  13.931 4.463   1.00 29.77  ? 313 THR   A CA  1 
ATOM   2150 C C   . THR   A 1 273 ? -2.364  13.320 3.469   1.00 31.72  ? 313 THR   A C   1 
ATOM   2151 O O   . THR   A 1 273 ? -3.367  12.713 3.856   1.00 34.16  ? 313 THR   A O   1 
ATOM   2152 C CB  . THR   A 1 273 ? -0.414  12.851 4.942   1.00 38.18  ? 313 THR   A CB  1 
ATOM   2153 O OG1 . THR   A 1 273 ? -1.114  11.878 5.724   1.00 44.43  ? 313 THR   A OG1 1 
ATOM   2154 C CG2 . THR   A 1 273 ? 0.662   13.468 5.780   1.00 41.57  ? 313 THR   A CG2 1 
ATOM   2155 N N   . VAL   A 1 274 ? -2.057  13.486 2.188   1.00 29.83  ? 314 VAL   A N   1 
ATOM   2156 C CA  . VAL   A 1 274 ? -2.779  12.830 1.105   1.00 31.78  ? 314 VAL   A CA  1 
ATOM   2157 C C   . VAL   A 1 274 ? -1.766  11.992 0.340   1.00 31.70  ? 314 VAL   A C   1 
ATOM   2158 O O   . VAL   A 1 274 ? -0.850  12.535 -0.295  1.00 31.28  ? 314 VAL   A O   1 
ATOM   2159 C CB  . VAL   A 1 274 ? -3.480  13.836 0.181   1.00 31.83  ? 314 VAL   A CB  1 
ATOM   2160 C CG1 . VAL   A 1 274 ? -4.238  13.105 -0.927  1.00 27.42  ? 314 VAL   A CG1 1 
ATOM   2161 C CG2 . VAL   A 1 274 ? -4.418  14.734 0.981   1.00 30.49  ? 314 VAL   A CG2 1 
ATOM   2162 N N   . LYS   A 1 275 ? -1.916  10.670 0.398   1.00 31.30  ? 315 LYS   A N   1 
ATOM   2163 C CA  . LYS   A 1 275 ? -1.058  9.759  -0.345  1.00 30.02  ? 315 LYS   A CA  1 
ATOM   2164 C C   . LYS   A 1 275 ? -1.812  9.206  -1.545  1.00 30.80  ? 315 LYS   A C   1 
ATOM   2165 O O   . LYS   A 1 275 ? -2.899  8.643  -1.395  1.00 34.30  ? 315 LYS   A O   1 
ATOM   2166 C CB  . LYS   A 1 275 ? -0.569  8.605  0.530   1.00 31.77  ? 315 LYS   A CB  1 
ATOM   2167 C CG  . LYS   A 1 275 ? 0.189   7.559  -0.279  1.00 37.39  ? 315 LYS   A CG  1 
ATOM   2168 C CD  . LYS   A 1 275 ? 1.046   6.663  0.592   1.00 42.51  ? 315 LYS   A CD  1 
ATOM   2169 C CE  . LYS   A 1 275 ? 0.336   5.382  0.942   1.00 52.33  ? 315 LYS   A CE  1 
ATOM   2170 N NZ  . LYS   A 1 275 ? 1.230   4.516  1.768   1.00 58.15  ? 315 LYS   A NZ  1 
ATOM   2171 N N   . MET   A 1 276 ? -1.226  9.352  -2.727  1.00 30.83  ? 316 MET   A N   1 
ATOM   2172 C CA  . MET   A 1 276 ? -1.808  8.857  -3.967  1.00 27.93  ? 316 MET   A CA  1 
ATOM   2173 C C   . MET   A 1 276 ? -0.868  7.832  -4.578  1.00 31.60  ? 316 MET   A C   1 
ATOM   2174 O O   . MET   A 1 276 ? 0.318   8.115  -4.775  1.00 34.48  ? 316 MET   A O   1 
ATOM   2175 C CB  . MET   A 1 276 ? -2.064  10.005 -4.948  1.00 24.13  ? 316 MET   A CB  1 
ATOM   2176 C CG  . MET   A 1 276 ? -2.655  9.551  -6.288  1.00 27.40  ? 316 MET   A CG  1 
ATOM   2177 S SD  . MET   A 1 276 ? -2.936  10.898 -7.464  1.00 32.00  ? 316 MET   A SD  1 
ATOM   2178 C CE  . MET   A 1 276 ? -3.942  12.002 -6.457  1.00 29.65  ? 316 MET   A CE  1 
ATOM   2179 N N   . SER   A 1 277 ? -1.397  6.644  -4.879  1.00 31.43  ? 317 SER   A N   1 
ATOM   2180 C CA  . SER   A 1 277 ? -0.599  5.511  -5.330  1.00 29.68  ? 317 SER   A CA  1 
ATOM   2181 C C   . SER   A 1 277 ? -1.122  4.992  -6.660  1.00 31.19  ? 317 SER   A C   1 
ATOM   2182 O O   . SER   A 1 277 ? -2.337  4.867  -6.849  1.00 33.88  ? 317 SER   A O   1 
ATOM   2183 C CB  . SER   A 1 277 ? -0.630  4.363  -4.305  1.00 27.67  ? 317 SER   A CB  1 
ATOM   2184 O OG  . SER   A 1 277 ? -0.272  4.806  -3.009  1.00 35.97  ? 317 SER   A OG  1 
ATOM   2185 N N   . ASP   A 1 278 ? -0.205  4.681  -7.578  1.00 30.36  ? 318 ASP   A N   1 
ATOM   2186 C CA  . ASP   A 1 278 ? -0.568  4.056  -8.839  1.00 27.98  ? 318 ASP   A CA  1 
ATOM   2187 C C   . ASP   A 1 278 ? 0.261   2.797  -9.034  1.00 33.06  ? 318 ASP   A C   1 
ATOM   2188 O O   . ASP   A 1 278 ? 1.279   2.582  -8.371  1.00 33.98  ? 318 ASP   A O   1 
ATOM   2189 C CB  . ASP   A 1 278 ? -0.404  5.013  -10.058 1.00 30.64  ? 318 ASP   A CB  1 
ATOM   2190 C CG  . ASP   A 1 278 ? 1.064   5.321  -10.423 1.00 34.62  ? 318 ASP   A CG  1 
ATOM   2191 O OD1 . ASP   A 1 278 ? 1.893   4.395  -10.582 1.00 34.86  ? 318 ASP   A OD1 1 
ATOM   2192 O OD2 . ASP   A 1 278 ? 1.381   6.515  -10.622 1.00 35.07  ? 318 ASP   A OD2 1 
ATOM   2193 N N   . ARG   A 1 279 ? -0.198  1.953  -9.955  1.00 36.25  ? 319 ARG   A N   1 
ATOM   2194 C CA  . ARG   A 1 279 ? 0.599   0.827  -10.418 1.00 33.48  ? 319 ARG   A CA  1 
ATOM   2195 C C   . ARG   A 1 279 ? 0.978   1.069  -11.874 1.00 36.07  ? 319 ARG   A C   1 
ATOM   2196 O O   . ARG   A 1 279 ? 0.757   0.209  -12.732 1.00 38.96  ? 319 ARG   A O   1 
ATOM   2197 C CB  . ARG   A 1 279 ? -0.164  -0.488 -10.259 1.00 36.57  ? 319 ARG   A CB  1 
ATOM   2198 C CG  . ARG   A 1 279 ? -0.331  -0.952 -8.829  1.00 46.02  ? 319 ARG   A CG  1 
ATOM   2199 C CD  . ARG   A 1 279 ? -1.126  -2.244 -8.799  1.00 68.95  ? 319 ARG   A CD  1 
ATOM   2200 N NE  . ARG   A 1 279 ? -1.704  -2.508 -7.486  1.00 87.97  ? 319 ARG   A NE  1 
ATOM   2201 C CZ  . ARG   A 1 279 ? -1.249  -3.421 -6.634  1.00 95.46  ? 319 ARG   A CZ  1 
ATOM   2202 N NH1 . ARG   A 1 279 ? -0.202  -4.170 -6.960  1.00 98.30  ? 319 ARG   A NH1 1 
ATOM   2203 N NH2 . ARG   A 1 279 ? -1.846  -3.588 -5.459  1.00 95.89  ? 319 ARG   A NH2 1 
ATOM   2204 N N   . GLY   A 1 280 ? 1.552   2.241  -12.153 1.00 32.73  ? 320 GLY   A N   1 
ATOM   2205 C CA  . GLY   A 1 280 ? 1.855   2.653  -13.514 1.00 35.91  ? 320 GLY   A CA  1 
ATOM   2206 C C   . GLY   A 1 280 ? 3.273   2.383  -13.982 1.00 41.50  ? 320 GLY   A C   1 
ATOM   2207 O O   . GLY   A 1 280 ? 3.737   3.007  -14.945 1.00 44.00  ? 320 GLY   A O   1 
ATOM   2208 N N   . GLY   A 1 281 ? 3.985   1.471  -13.314 1.00 34.17  ? 321 GLY   A N   1 
ATOM   2209 C CA  . GLY   A 1 281 ? 5.275   1.025  -13.783 1.00 39.11  ? 321 GLY   A CA  1 
ATOM   2210 C C   . GLY   A 1 281 ? 6.470   1.746  -13.192 1.00 34.79  ? 321 GLY   A C   1 
ATOM   2211 O O   . GLY   A 1 281 ? 7.597   1.275  -13.362 1.00 35.99  ? 321 GLY   A O   1 
ATOM   2212 N N   . GLY   A 1 282 ? 6.265   2.871  -12.527 1.00 35.86  ? 322 GLY   A N   1 
ATOM   2213 C CA  . GLY   A 1 282 ? 7.336   3.497  -11.784 1.00 32.55  ? 322 GLY   A CA  1 
ATOM   2214 C C   . GLY   A 1 282 ? 8.334   4.249  -12.649 1.00 35.49  ? 322 GLY   A C   1 
ATOM   2215 O O   . GLY   A 1 282 ? 8.215   4.349  -13.870 1.00 36.11  ? 322 GLY   A O   1 
ATOM   2216 N N   . VAL   A 1 283 ? 9.327   4.817  -11.964 1.00 36.98  ? 323 VAL   A N   1 
ATOM   2217 C CA  . VAL   A 1 283 ? 10.390  5.665  -12.512 1.00 38.21  ? 323 VAL   A CA  1 
ATOM   2218 C C   . VAL   A 1 283 ? 11.658  5.369  -11.721 1.00 33.59  ? 323 VAL   A C   1 
ATOM   2219 O O   . VAL   A 1 283 ? 11.617  5.393  -10.485 1.00 32.86  ? 323 VAL   A O   1 
ATOM   2220 C CB  . VAL   A 1 283 ? 10.078  7.171  -12.394 1.00 46.31  ? 323 VAL   A CB  1 
ATOM   2221 C CG1 . VAL   A 1 283 ? 10.698  7.964  -13.546 1.00 47.10  ? 323 VAL   A CG1 1 
ATOM   2222 C CG2 . VAL   A 1 283 ? 8.598   7.443  -12.255 1.00 49.12  ? 323 VAL   A CG2 1 
ATOM   2223 N N   . PRO   A 1 284 ? 12.804  5.142  -12.355 1.00 37.09  ? 324 PRO   A N   1 
ATOM   2224 C CA  . PRO   A 1 284 ? 14.032  4.975  -11.572 1.00 38.72  ? 324 PRO   A CA  1 
ATOM   2225 C C   . PRO   A 1 284 ? 14.360  6.239  -10.786 1.00 38.42  ? 324 PRO   A C   1 
ATOM   2226 O O   . PRO   A 1 284 ? 14.024  7.359  -11.184 1.00 36.58  ? 324 PRO   A O   1 
ATOM   2227 C CB  . PRO   A 1 284 ? 15.093  4.668  -12.631 1.00 40.01  ? 324 PRO   A CB  1 
ATOM   2228 C CG  . PRO   A 1 284 ? 14.552  5.270  -13.884 1.00 40.20  ? 324 PRO   A CG  1 
ATOM   2229 C CD  . PRO   A 1 284 ? 13.062  5.113  -13.804 1.00 38.07  ? 324 PRO   A CD  1 
ATOM   2230 N N   . LEU   A 1 285 ? 15.024  6.041  -9.644  1.00 34.53  ? 325 LEU   A N   1 
ATOM   2231 C CA  . LEU   A 1 285 ? 15.311  7.148  -8.734  1.00 38.13  ? 325 LEU   A CA  1 
ATOM   2232 C C   . LEU   A 1 285 ? 16.112  8.250  -9.425  1.00 45.02  ? 325 LEU   A C   1 
ATOM   2233 O O   . LEU   A 1 285 ? 15.895  9.445  -9.169  1.00 38.92  ? 325 LEU   A O   1 
ATOM   2234 C CB  . LEU   A 1 285 ? 16.069  6.624  -7.515  1.00 32.26  ? 325 LEU   A CB  1 
ATOM   2235 C CG  . LEU   A 1 285 ? 16.420  7.651  -6.443  1.00 32.73  ? 325 LEU   A CG  1 
ATOM   2236 C CD1 . LEU   A 1 285 ? 15.161  8.299  -5.883  1.00 33.56  ? 325 LEU   A CD1 1 
ATOM   2237 C CD2 . LEU   A 1 285 ? 17.226  6.973  -5.350  1.00 34.82  ? 325 LEU   A CD2 1 
ATOM   2238 N N   . ARG   A 1 286 ? 17.036  7.862  -10.309 1.00 39.54  ? 326 ARG   A N   1 
ATOM   2239 C CA  . ARG   A 1 286 ? 17.865  8.821  -11.032 1.00 42.11  ? 326 ARG   A CA  1 
ATOM   2240 C C   . ARG   A 1 286 ? 17.028  9.804  -11.845 1.00 39.13  ? 326 ARG   A C   1 
ATOM   2241 O O   . ARG   A 1 286 ? 17.458  10.939 -12.073 1.00 43.22  ? 326 ARG   A O   1 
ATOM   2242 C CB  . ARG   A 1 286 ? 18.843  8.057  -11.934 1.00 41.80  ? 326 ARG   A CB  1 
ATOM   2243 C CG  . ARG   A 1 286 ? 19.718  8.909  -12.840 1.00 42.50  ? 326 ARG   A CG  1 
ATOM   2244 C CD  . ARG   A 1 286 ? 20.640  8.043  -13.695 1.00 45.61  ? 326 ARG   A CD  1 
ATOM   2245 N NE  . ARG   A 1 286 ? 19.904  7.094  -14.531 1.00 46.39  ? 326 ARG   A NE  1 
ATOM   2246 C CZ  . ARG   A 1 286 ? 19.488  7.349  -15.767 1.00 52.63  ? 326 ARG   A CZ  1 
ATOM   2247 N NH1 . ARG   A 1 286 ? 19.736  8.529  -16.320 1.00 54.55  ? 326 ARG   A NH1 1 
ATOM   2248 N NH2 . ARG   A 1 286 ? 18.822  6.426  -16.451 1.00 52.49  ? 326 ARG   A NH2 1 
ATOM   2249 N N   . LYS   A 1 287 ? 15.830  9.405  -12.267 1.00 35.39  ? 327 LYS   A N   1 
ATOM   2250 C CA  . LYS   A 1 287 ? 15.017  10.204 -13.171 1.00 34.38  ? 327 LYS   A CA  1 
ATOM   2251 C C   . LYS   A 1 287 ? 13.859  10.910 -12.480 1.00 35.58  ? 327 LYS   A C   1 
ATOM   2252 O O   . LYS   A 1 287 ? 13.036  11.513 -13.166 1.00 40.76  ? 327 LYS   A O   1 
ATOM   2253 C CB  . LYS   A 1 287 ? 14.468  9.332  -14.302 1.00 35.54  ? 327 LYS   A CB  1 
ATOM   2254 C CG  . LYS   A 1 287 ? 15.506  8.787  -15.276 1.00 41.27  ? 327 LYS   A CG  1 
ATOM   2255 C CD  . LYS   A 1 287 ? 14.803  8.030  -16.406 1.00 44.73  ? 327 LYS   A CD  1 
ATOM   2256 C CE  . LYS   A 1 287 ? 15.779  7.448  -17.408 1.00 54.99  ? 327 LYS   A CE  1 
ATOM   2257 N NZ  . LYS   A 1 287 ? 15.111  6.521  -18.370 1.00 55.77  ? 327 LYS   A NZ  1 
ATOM   2258 N N   . ILE   A 1 288 ? 13.763  10.840 -11.152 1.00 34.98  ? 328 ILE   A N   1 
ATOM   2259 C CA  . ILE   A 1 288 ? 12.634  11.451 -10.451 1.00 37.97  ? 328 ILE   A CA  1 
ATOM   2260 C C   . ILE   A 1 288 ? 12.717  12.971 -10.511 1.00 37.76  ? 328 ILE   A C   1 
ATOM   2261 O O   . ILE   A 1 288 ? 11.720  13.655 -10.770 1.00 36.24  ? 328 ILE   A O   1 
ATOM   2262 C CB  . ILE   A 1 288 ? 12.578  10.973 -8.990  1.00 45.31  ? 328 ILE   A CB  1 
ATOM   2263 C CG1 . ILE   A 1 288 ? 12.177  9.511  -8.914  1.00 45.92  ? 328 ILE   A CG1 1 
ATOM   2264 C CG2 . ILE   A 1 288 ? 11.562  11.794 -8.220  1.00 53.43  ? 328 ILE   A CG2 1 
ATOM   2265 C CD1 . ILE   A 1 288 ? 10.719  9.308  -9.212  1.00 49.78  ? 328 ILE   A CD1 1 
ATOM   2266 N N   . ASP   A 1 289 ? 13.901  13.528 -10.242 1.00 39.39  ? 329 ASP   A N   1 
ATOM   2267 C CA  . ASP   A 1 289 ? 13.995  14.966 -10.012 1.00 46.47  ? 329 ASP   A CA  1 
ATOM   2268 C C   . ASP   A 1 289 ? 13.705  15.777 -11.264 1.00 42.25  ? 329 ASP   A C   1 
ATOM   2269 O O   . ASP   A 1 289 ? 13.214  16.908 -11.158 1.00 40.68  ? 329 ASP   A O   1 
ATOM   2270 C CB  . ASP   A 1 289 ? 15.365  15.318 -9.446  1.00 55.04  ? 329 ASP   A CB  1 
ATOM   2271 C CG  . ASP   A 1 289 ? 15.381  15.279 -7.933  1.00 69.91  ? 329 ASP   A CG  1 
ATOM   2272 O OD1 . ASP   A 1 289 ? 14.330  15.597 -7.326  1.00 73.87  ? 329 ASP   A OD1 1 
ATOM   2273 O OD2 . ASP   A 1 289 ? 16.427  14.925 -7.351  1.00 77.08  ? 329 ASP   A OD2 1 
ATOM   2274 N N   . ARG   A 1 290 ? 13.972  15.226 -12.449 1.00 38.53  ? 330 ARG   A N   1 
ATOM   2275 C CA  . ARG   A 1 290 ? 13.661  15.962 -13.668 1.00 37.05  ? 330 ARG   A CA  1 
ATOM   2276 C C   . ARG   A 1 290 ? 12.168  16.236 -13.800 1.00 33.65  ? 330 ARG   A C   1 
ATOM   2277 O O   . ARG   A 1 290 ? 11.778  17.128 -14.560 1.00 38.35  ? 330 ARG   A O   1 
ATOM   2278 C CB  . ARG   A 1 290 ? 14.185  15.212 -14.902 1.00 42.32  ? 330 ARG   A CB  1 
ATOM   2279 C CG  . ARG   A 1 290 ? 13.496  13.900 -15.200 1.00 45.98  ? 330 ARG   A CG  1 
ATOM   2280 C CD  . ARG   A 1 290 ? 14.199  13.115 -16.316 1.00 48.86  ? 330 ARG   A CD  1 
ATOM   2281 N NE  . ARG   A 1 290 ? 15.633  12.932 -16.083 1.00 57.27  ? 330 ARG   A NE  1 
ATOM   2282 C CZ  . ARG   A 1 290 ? 16.429  12.196 -16.858 1.00 58.51  ? 330 ARG   A CZ  1 
ATOM   2283 N NH1 . ARG   A 1 290 ? 15.931  11.565 -17.915 1.00 48.67  ? 330 ARG   A NH1 1 
ATOM   2284 N NH2 . ARG   A 1 290 ? 17.721  12.084 -16.576 1.00 59.19  ? 330 ARG   A NH2 1 
ATOM   2285 N N   . LEU   A 1 291 ? 11.324  15.505 -13.068 1.00 32.66  ? 331 LEU   A N   1 
ATOM   2286 C CA  . LEU   A 1 291 ? 9.898   15.809 -13.069 1.00 33.18  ? 331 LEU   A CA  1 
ATOM   2287 C C   . LEU   A 1 291 ? 9.594   17.168 -12.454 1.00 35.83  ? 331 LEU   A C   1 
ATOM   2288 O O   . LEU   A 1 291 ? 8.521   17.721 -12.719 1.00 35.09  ? 331 LEU   A O   1 
ATOM   2289 C CB  . LEU   A 1 291 ? 9.119   14.729 -12.325 1.00 33.08  ? 331 LEU   A CB  1 
ATOM   2290 C CG  . LEU   A 1 291 ? 9.144   13.326 -12.941 1.00 37.74  ? 331 LEU   A CG  1 
ATOM   2291 C CD1 . LEU   A 1 291 ? 8.460   12.335 -12.004 1.00 38.39  ? 331 LEU   A CD1 1 
ATOM   2292 C CD2 . LEU   A 1 291 ? 8.471   13.324 -14.301 1.00 39.02  ? 331 LEU   A CD2 1 
ATOM   2293 N N   . PHE   A 1 292 ? 10.505  17.715 -11.642 1.00 33.26  ? 332 PHE   A N   1 
ATOM   2294 C CA  . PHE   A 1 292 ? 10.334  19.028 -11.027 1.00 35.65  ? 332 PHE   A CA  1 
ATOM   2295 C C   . PHE   A 1 292 ? 11.185  20.098 -11.699 1.00 36.23  ? 332 PHE   A C   1 
ATOM   2296 O O   . PHE   A 1 292 ? 11.223  21.244 -11.229 1.00 33.21  ? 332 PHE   A O   1 
ATOM   2297 C CB  . PHE   A 1 292 ? 10.662  18.964 -9.533  1.00 32.74  ? 332 PHE   A CB  1 
ATOM   2298 C CG  . PHE   A 1 292 ? 9.714   18.111 -8.739  1.00 34.43  ? 332 PHE   A CG  1 
ATOM   2299 C CD1 . PHE   A 1 292 ? 8.458   18.579 -8.397  1.00 35.74  ? 332 PHE   A CD1 1 
ATOM   2300 C CD2 . PHE   A 1 292 ? 10.082  16.834 -8.331  1.00 42.62  ? 332 PHE   A CD2 1 
ATOM   2301 C CE1 . PHE   A 1 292 ? 7.577   17.788 -7.668  1.00 36.75  ? 332 PHE   A CE1 1 
ATOM   2302 C CE2 . PHE   A 1 292 ? 9.208   16.044 -7.593  1.00 43.86  ? 332 PHE   A CE2 1 
ATOM   2303 C CZ  . PHE   A 1 292 ? 7.955   16.523 -7.264  1.00 39.10  ? 332 PHE   A CZ  1 
ATOM   2304 N N   . ASN   A 1 293 ? 11.856  19.749 -12.788 1.00 32.75  ? 333 ASN   A N   1 
ATOM   2305 C CA  . ASN   A 1 293 ? 12.774  20.641 -13.473 1.00 31.35  ? 333 ASN   A CA  1 
ATOM   2306 C C   . ASN   A 1 293 ? 12.036  21.337 -14.610 1.00 36.79  ? 333 ASN   A C   1 
ATOM   2307 O O   . ASN   A 1 293 ? 11.505  20.675 -15.508 1.00 34.90  ? 333 ASN   A O   1 
ATOM   2308 C CB  . ASN   A 1 293 ? 13.966  19.844 -13.996 1.00 32.85  ? 333 ASN   A CB  1 
ATOM   2309 C CG  . ASN   A 1 293 ? 14.982  20.709 -14.688 1.00 34.39  ? 333 ASN   A CG  1 
ATOM   2310 O OD1 . ASN   A 1 293 ? 14.834  21.044 -15.865 1.00 34.99  ? 333 ASN   A OD1 1 
ATOM   2311 N ND2 . ASN   A 1 293 ? 16.033  21.076 -13.963 1.00 38.54  ? 333 ASN   A ND2 1 
ATOM   2312 N N   . TYR   A 1 294 ? 12.018  22.673 -14.580 1.00 32.97  ? 334 TYR   A N   1 
ATOM   2313 C CA  . TYR   A 1 294 ? 11.253  23.425 -15.572 1.00 32.92  ? 334 TYR   A CA  1 
ATOM   2314 C C   . TYR   A 1 294 ? 11.808  23.242 -16.977 1.00 36.17  ? 334 TYR   A C   1 
ATOM   2315 O O   . TYR   A 1 294 ? 11.041  23.091 -17.933 1.00 38.16  ? 334 TYR   A O   1 
ATOM   2316 C CB  . TYR   A 1 294 ? 11.231  24.903 -15.198 1.00 33.31  ? 334 TYR   A CB  1 
ATOM   2317 C CG  . TYR   A 1 294 ? 10.566  25.152 -13.864 1.00 31.71  ? 334 TYR   A CG  1 
ATOM   2318 C CD1 . TYR   A 1 294 ? 9.187   25.259 -13.771 1.00 30.17  ? 334 TYR   A CD1 1 
ATOM   2319 C CD2 . TYR   A 1 294 ? 11.315  25.256 -12.696 1.00 32.87  ? 334 TYR   A CD2 1 
ATOM   2320 C CE1 . TYR   A 1 294 ? 8.562   25.473 -12.551 1.00 32.69  ? 334 TYR   A CE1 1 
ATOM   2321 C CE2 . TYR   A 1 294 ? 10.700  25.463 -11.467 1.00 34.19  ? 334 TYR   A CE2 1 
ATOM   2322 C CZ  . TYR   A 1 294 ? 9.322   25.577 -11.405 1.00 35.23  ? 334 TYR   A CZ  1 
ATOM   2323 O OH  . TYR   A 1 294 ? 8.689   25.792 -10.194 1.00 34.06  ? 334 TYR   A OH  1 
ATOM   2324 N N   . MET   A 1 295 ? 13.134  23.265 -17.130 1.00 37.79  ? 335 MET   A N   1 
ATOM   2325 C CA  . MET   A 1 295 ? 13.712  23.179 -18.467 1.00 42.90  ? 335 MET   A CA  1 
ATOM   2326 C C   . MET   A 1 295 ? 13.432  21.824 -19.103 1.00 45.12  ? 335 MET   A C   1 
ATOM   2327 O O   . MET   A 1 295 ? 13.130  21.741 -20.299 1.00 47.69  ? 335 MET   A O   1 
ATOM   2328 C CB  . MET   A 1 295 ? 15.217  23.448 -18.417 1.00 42.88  ? 335 MET   A CB  1 
ATOM   2329 C CG  . MET   A 1 295 ? 15.590  24.899 -18.144 1.00 49.05  ? 335 MET   A CG  1 
ATOM   2330 S SD  . MET   A 1 295 ? 15.117  26.031 -19.467 1.00 52.00  ? 335 MET   A SD  1 
ATOM   2331 C CE  . MET   A 1 295 ? 16.144  25.449 -20.813 1.00 49.34  ? 335 MET   A CE  1 
ATOM   2332 N N   . TYR   A 1 296 ? 13.526  20.751 -18.321 1.00 43.42  ? 336 TYR   A N   1 
ATOM   2333 C CA  . TYR   A 1 296 ? 13.195  19.433 -18.845 1.00 46.33  ? 336 TYR   A CA  1 
ATOM   2334 C C   . TYR   A 1 296 ? 11.716  19.331 -19.195 1.00 48.47  ? 336 TYR   A C   1 
ATOM   2335 O O   . TYR   A 1 296 ? 11.352  18.652 -20.160 1.00 51.44  ? 336 TYR   A O   1 
ATOM   2336 C CB  . TYR   A 1 296 ? 13.585  18.360 -17.828 1.00 46.74  ? 336 TYR   A CB  1 
ATOM   2337 C CG  . TYR   A 1 296 ? 13.540  16.945 -18.361 1.00 60.52  ? 336 TYR   A CG  1 
ATOM   2338 C CD1 . TYR   A 1 296 ? 12.368  16.192 -18.303 1.00 65.84  ? 336 TYR   A CD1 1 
ATOM   2339 C CD2 . TYR   A 1 296 ? 14.672  16.354 -18.910 1.00 68.09  ? 336 TYR   A CD2 1 
ATOM   2340 C CE1 . TYR   A 1 296 ? 12.324  14.889 -18.788 1.00 69.91  ? 336 TYR   A CE1 1 
ATOM   2341 C CE2 . TYR   A 1 296 ? 14.639  15.052 -19.397 1.00 74.45  ? 336 TYR   A CE2 1 
ATOM   2342 C CZ  . TYR   A 1 296 ? 13.462  14.327 -19.336 1.00 77.90  ? 336 TYR   A CZ  1 
ATOM   2343 O OH  . TYR   A 1 296 ? 13.426  13.033 -19.813 1.00 84.79  ? 336 TYR   A OH  1 
ATOM   2344 N N   . SER   A 1 297 ? 10.851  20.004 -18.436 1.00 46.60  ? 337 SER   A N   1 
ATOM   2345 C CA  . SER   A 1 297 ? 9.410   19.931 -18.647 1.00 46.97  ? 337 SER   A CA  1 
ATOM   2346 C C   . SER   A 1 297 ? 8.909   20.891 -19.718 1.00 51.08  ? 337 SER   A C   1 
ATOM   2347 O O   . SER   A 1 297 ? 7.704   20.909 -19.994 1.00 56.92  ? 337 SER   A O   1 
ATOM   2348 C CB  . SER   A 1 297 ? 8.668   20.215 -17.335 1.00 50.17  ? 337 SER   A CB  1 
ATOM   2349 O OG  . SER   A 1 297 ? 9.118   19.373 -16.287 1.00 57.96  ? 337 SER   A OG  1 
ATOM   2350 N N   . THR   A 1 298 ? 9.790   21.683 -20.324 1.00 56.44  ? 338 THR   A N   1 
ATOM   2351 C CA  . THR   A 1 298 ? 9.388   22.740 -21.245 1.00 62.91  ? 338 THR   A CA  1 
ATOM   2352 C C   . THR   A 1 298 ? 9.285   22.190 -22.664 1.00 73.58  ? 338 THR   A C   1 
ATOM   2353 O O   . THR   A 1 298 ? 10.289  21.763 -23.248 1.00 71.16  ? 338 THR   A O   1 
ATOM   2354 C CB  . THR   A 1 298 ? 10.379  23.902 -21.190 1.00 56.84  ? 338 THR   A CB  1 
ATOM   2355 O OG1 . THR   A 1 298 ? 10.371  24.478 -19.873 1.00 53.29  ? 338 THR   A OG1 1 
ATOM   2356 C CG2 . THR   A 1 298 ? 10.013  24.971 -22.217 1.00 48.82  ? 338 THR   A CG2 1 
ATOM   2357 N N   . ALA   A 1 299 ? 8.074   22.207 -23.212 1.00 84.62  ? 339 ALA   A N   1 
ATOM   2358 C CA  . ALA   A 1 299 ? 7.785   21.819 -24.584 1.00 89.64  ? 339 ALA   A CA  1 
ATOM   2359 C C   . ALA   A 1 299 ? 6.770   22.799 -25.150 1.00 91.37  ? 339 ALA   A C   1 
ATOM   2360 O O   . ALA   A 1 299 ? 5.964   23.358 -24.395 1.00 91.87  ? 339 ALA   A O   1 
ATOM   2361 C CB  . ALA   A 1 299 ? 7.226   20.389 -24.673 1.00 87.75  ? 339 ALA   A CB  1 
ATOM   2362 N N   . PRO   A 1 300 ? 6.799   23.048 -26.461 1.00 90.16  ? 340 PRO   A N   1 
ATOM   2363 C CA  . PRO   A 1 300 ? 5.749   23.872 -27.073 1.00 84.90  ? 340 PRO   A CA  1 
ATOM   2364 C C   . PRO   A 1 300 ? 4.363   23.331 -26.739 1.00 78.43  ? 340 PRO   A C   1 
ATOM   2365 O O   . PRO   A 1 300 ? 4.149   22.117 -26.649 1.00 71.90  ? 340 PRO   A O   1 
ATOM   2366 C CB  . PRO   A 1 300 ? 6.059   23.784 -28.570 1.00 83.75  ? 340 PRO   A CB  1 
ATOM   2367 C CG  . PRO   A 1 300 ? 7.537   23.579 -28.619 1.00 84.12  ? 340 PRO   A CG  1 
ATOM   2368 C CD  . PRO   A 1 300 ? 7.864   22.712 -27.424 1.00 85.99  ? 340 PRO   A CD  1 
ATOM   2369 N N   . ARG   A 1 301 ? 3.424   24.250 -26.537 1.00 76.90  ? 341 ARG   A N   1 
ATOM   2370 C CA  . ARG   A 1 301 ? 2.115   23.924 -25.997 1.00 75.81  ? 341 ARG   A CA  1 
ATOM   2371 C C   . ARG   A 1 301 ? 1.202   23.327 -27.067 1.00 72.52  ? 341 ARG   A C   1 
ATOM   2372 O O   . ARG   A 1 301 ? 1.429   23.508 -28.268 1.00 66.52  ? 341 ARG   A O   1 
ATOM   2373 C CB  . ARG   A 1 301 ? 1.479   25.175 -25.398 1.00 78.46  ? 341 ARG   A CB  1 
ATOM   2374 C CG  . ARG   A 1 301 ? 1.231   26.306 -26.386 1.00 80.99  ? 341 ARG   A CG  1 
ATOM   2375 C CD  . ARG   A 1 301 ? 0.535   27.466 -25.689 1.00 82.34  ? 341 ARG   A CD  1 
ATOM   2376 N NE  . ARG   A 1 301 ? 1.316   27.940 -24.551 1.00 85.54  ? 341 ARG   A NE  1 
ATOM   2377 C CZ  . ARG   A 1 301 ? 0.817   28.618 -23.523 1.00 90.95  ? 341 ARG   A CZ  1 
ATOM   2378 N NH1 . ARG   A 1 301 ? -0.478  28.906 -23.474 1.00 89.28  ? 341 ARG   A NH1 1 
ATOM   2379 N NH2 . ARG   A 1 301 ? 1.616   29.002 -22.535 1.00 93.84  ? 341 ARG   A NH2 1 
ATOM   2380 N N   . PRO   A 1 302 ? 0.164   22.594 -26.654 1.00 70.90  ? 342 PRO   A N   1 
ATOM   2381 C CA  . PRO   A 1 302 ? -0.778  22.036 -27.634 1.00 67.85  ? 342 PRO   A CA  1 
ATOM   2382 C C   . PRO   A 1 302 ? -1.431  23.127 -28.471 1.00 65.37  ? 342 PRO   A C   1 
ATOM   2383 O O   . PRO   A 1 302 ? -1.820  24.184 -27.967 1.00 62.92  ? 342 PRO   A O   1 
ATOM   2384 C CB  . PRO   A 1 302 ? -1.806  21.296 -26.766 1.00 68.40  ? 342 PRO   A CB  1 
ATOM   2385 C CG  . PRO   A 1 302 ? -1.601  21.818 -25.368 1.00 72.80  ? 342 PRO   A CG  1 
ATOM   2386 C CD  . PRO   A 1 302 ? -0.147  22.155 -25.282 1.00 73.27  ? 342 PRO   A CD  1 
ATOM   2387 N N   . ARG   A 1 303 ? -1.542  22.855 -29.767 1.00 65.16  ? 343 ARG   A N   1 
ATOM   2388 C CA  . ARG   A 1 303 ? -2.101  23.822 -30.696 1.00 65.51  ? 343 ARG   A CA  1 
ATOM   2389 C C   . ARG   A 1 303 ? -3.608  23.968 -30.495 1.00 56.06  ? 343 ARG   A C   1 
ATOM   2390 O O   . ARG   A 1 303 ? -4.301  23.046 -30.053 1.00 47.93  ? 343 ARG   A O   1 
ATOM   2391 C CB  . ARG   A 1 303 ? -1.788  23.409 -32.131 1.00 70.56  ? 343 ARG   A CB  1 
ATOM   2392 C CG  . ARG   A 1 303 ? -0.301  23.269 -32.389 1.00 79.92  ? 343 ARG   A CG  1 
ATOM   2393 C CD  . ARG   A 1 303 ? 0.009   23.118 -33.868 1.00 91.65  ? 343 ARG   A CD  1 
ATOM   2394 N NE  . ARG   A 1 303 ? 1.448   23.130 -34.124 1.00 100.48 ? 343 ARG   A NE  1 
ATOM   2395 C CZ  . ARG   A 1 303 ? 2.147   24.221 -34.427 1.00 106.51 ? 343 ARG   A CZ  1 
ATOM   2396 N NH1 . ARG   A 1 303 ? 3.454   24.134 -34.644 1.00 108.12 ? 343 ARG   A NH1 1 
ATOM   2397 N NH2 . ARG   A 1 303 ? 1.541   25.399 -34.517 1.00 107.21 ? 343 ARG   A NH2 1 
ATOM   2398 N N   . VAL   A 1 304 ? -4.113  25.161 -30.807 1.00 53.94  ? 344 VAL   A N   1 
ATOM   2399 C CA  . VAL   A 1 304 ? -5.544  25.412 -30.686 1.00 48.82  ? 344 VAL   A CA  1 
ATOM   2400 C C   . VAL   A 1 304 ? -6.310  24.671 -31.774 1.00 45.04  ? 344 VAL   A C   1 
ATOM   2401 O O   . VAL   A 1 304 ? -7.374  24.095 -31.521 1.00 46.59  ? 344 VAL   A O   1 
ATOM   2402 C CB  . VAL   A 1 304 ? -5.808  26.930 -30.725 1.00 51.24  ? 344 VAL   A CB  1 
ATOM   2403 C CG1 . VAL   A 1 304 ? -7.288  27.219 -30.898 1.00 51.36  ? 344 VAL   A CG1 1 
ATOM   2404 C CG2 . VAL   A 1 304 ? -5.275  27.585 -29.461 1.00 48.56  ? 344 VAL   A CG2 1 
ATOM   2405 N N   . GLU   A 1 305 ? -5.758  24.636 -32.984 1.00 42.27  ? 345 GLU   A N   1 
ATOM   2406 C CA  . GLU   A 1 305 ? -6.480  24.207 -34.182 1.00 45.03  ? 345 GLU   A CA  1 
ATOM   2407 C C   . GLU   A 1 305 ? -6.452  22.682 -34.339 1.00 47.50  ? 345 GLU   A C   1 
ATOM   2408 O O   . GLU   A 1 305 ? -5.933  22.135 -35.312 1.00 48.46  ? 345 GLU   A O   1 
ATOM   2409 C CB  . GLU   A 1 305 ? -5.900  24.896 -35.411 1.00 48.65  ? 345 GLU   A CB  1 
ATOM   2410 C CG  . GLU   A 1 305 ? -6.003  26.426 -35.412 1.00 51.21  ? 345 GLU   A CG  1 
ATOM   2411 C CD  . GLU   A 1 305 ? -4.991  27.115 -34.498 1.00 51.83  ? 345 GLU   A CD  1 
ATOM   2412 O OE1 . GLU   A 1 305 ? -4.023  26.462 -34.057 1.00 53.88  ? 345 GLU   A OE1 1 
ATOM   2413 O OE2 . GLU   A 1 305 ? -5.169  28.317 -34.212 1.00 54.42  ? 345 GLU   A OE2 1 
ATOM   2414 N N   . THR   A 1 306 ? -7.040  21.989 -33.366 1.00 45.23  ? 346 THR   A N   1 
ATOM   2415 C CA  . THR   A 1 306 ? -7.196  20.544 -33.481 1.00 48.14  ? 346 THR   A CA  1 
ATOM   2416 C C   . THR   A 1 306 ? -8.336  20.082 -32.586 1.00 45.64  ? 346 THR   A C   1 
ATOM   2417 O O   . THR   A 1 306 ? -8.636  20.706 -31.567 1.00 42.38  ? 346 THR   A O   1 
ATOM   2418 C CB  . THR   A 1 306 ? -5.905  19.790 -33.116 1.00 47.25  ? 346 THR   A CB  1 
ATOM   2419 O OG1 . THR   A 1 306 ? -6.083  18.392 -33.374 1.00 48.85  ? 346 THR   A OG1 1 
ATOM   2420 C CG2 . THR   A 1 306 ? -5.563  19.974 -31.659 1.00 42.63  ? 346 THR   A CG2 1 
ATOM   2421 N N   . SER   A 1 307 ? -8.967  18.980 -32.983 1.00 47.58  ? 347 SER   A N   1 
ATOM   2422 C CA  . SER   A 1 307 ? -9.921  18.295 -32.124 1.00 49.16  ? 347 SER   A CA  1 
ATOM   2423 C C   . SER   A 1 307 ? -9.288  17.170 -31.324 1.00 45.60  ? 347 SER   A C   1 
ATOM   2424 O O   . SER   A 1 307 ? -9.965  16.580 -30.474 1.00 45.55  ? 347 SER   A O   1 
ATOM   2425 C CB  . SER   A 1 307 ? -11.071 17.729 -32.956 1.00 61.15  ? 347 SER   A CB  1 
ATOM   2426 O OG  . SER   A 1 307 ? -11.753 18.772 -33.625 1.00 77.44  ? 347 SER   A OG  1 
ATOM   2427 N N   . ARG   A 1 308 ? -8.016  16.864 -31.569 1.00 39.53  ? 348 ARG   A N   1 
ATOM   2428 C CA  . ARG   A 1 308 ? -7.354  15.775 -30.861 1.00 41.91  ? 348 ARG   A CA  1 
ATOM   2429 C C   . ARG   A 1 308 ? -7.241  16.080 -29.374 1.00 43.54  ? 348 ARG   A C   1 
ATOM   2430 O O   . ARG   A 1 308 ? -6.960  17.211 -28.973 1.00 42.29  ? 348 ARG   A O   1 
ATOM   2431 C CB  . ARG   A 1 308 ? -5.974  15.520 -31.466 1.00 39.23  ? 348 ARG   A CB  1 
ATOM   2432 C CG  . ARG   A 1 308 ? -6.072  14.985 -32.883 1.00 43.18  ? 348 ARG   A CG  1 
ATOM   2433 C CD  . ARG   A 1 308 ? -4.737  14.906 -33.587 1.00 46.20  ? 348 ARG   A CD  1 
ATOM   2434 N NE  . ARG   A 1 308 ? -4.900  14.432 -34.956 1.00 52.41  ? 348 ARG   A NE  1 
ATOM   2435 C CZ  . ARG   A 1 308 ? -3.924  14.408 -35.854 1.00 52.93  ? 348 ARG   A CZ  1 
ATOM   2436 N NH1 . ARG   A 1 308 ? -2.714  14.830 -35.517 1.00 55.53  ? 348 ARG   A NH1 1 
ATOM   2437 N NH2 . ARG   A 1 308 ? -4.155  13.963 -37.079 1.00 57.13  ? 348 ARG   A NH2 1 
ATOM   2438 N N   . ALA   A 1 309 ? -7.473  15.053 -28.560 1.00 40.29  ? 349 ALA   A N   1 
ATOM   2439 C CA  . ALA   A 1 309 ? -7.483  15.211 -27.113 1.00 37.41  ? 349 ALA   A CA  1 
ATOM   2440 C C   . ALA   A 1 309 ? -6.123  15.685 -26.613 1.00 39.34  ? 349 ALA   A C   1 
ATOM   2441 O O   . ALA   A 1 309 ? -5.079  15.369 -27.190 1.00 40.06  ? 349 ALA   A O   1 
ATOM   2442 C CB  . ALA   A 1 309 ? -7.853  13.891 -26.440 1.00 37.63  ? 349 ALA   A CB  1 
ATOM   2443 N N   . VAL   A 1 310 ? -6.148  16.451 -25.529 1.00 36.85  ? 350 VAL   A N   1 
ATOM   2444 C CA  . VAL   A 1 310 ? -4.946  17.011 -24.926 1.00 37.91  ? 350 VAL   A CA  1 
ATOM   2445 C C   . VAL   A 1 310 ? -4.285  15.932 -24.079 1.00 38.66  ? 350 VAL   A C   1 
ATOM   2446 O O   . VAL   A 1 310 ? -4.983  15.232 -23.337 1.00 41.77  ? 350 VAL   A O   1 
ATOM   2447 C CB  . VAL   A 1 310 ? -5.285  18.247 -24.086 1.00 43.89  ? 350 VAL   A CB  1 
ATOM   2448 C CG1 . VAL   A 1 310 ? -4.040  18.828 -23.433 1.00 38.60  ? 350 VAL   A CG1 1 
ATOM   2449 C CG2 . VAL   A 1 310 ? -5.978  19.280 -24.947 1.00 48.69  ? 350 VAL   A CG2 1 
ATOM   2450 N N   . PRO   A 1 311 ? -2.959  15.759 -24.161 1.00 37.66  ? 351 PRO   A N   1 
ATOM   2451 C CA  . PRO   A 1 311 ? -2.280  14.759 -23.323 1.00 37.98  ? 351 PRO   A CA  1 
ATOM   2452 C C   . PRO   A 1 311 ? -2.421  15.105 -21.848 1.00 34.84  ? 351 PRO   A C   1 
ATOM   2453 O O   . PRO   A 1 311 ? -2.547  16.272 -21.480 1.00 36.08  ? 351 PRO   A O   1 
ATOM   2454 C CB  . PRO   A 1 311 ? -0.819  14.835 -23.789 1.00 37.23  ? 351 PRO   A CB  1 
ATOM   2455 C CG  . PRO   A 1 311 ? -0.866  15.479 -25.130 1.00 41.96  ? 351 PRO   A CG  1 
ATOM   2456 C CD  . PRO   A 1 311 ? -2.036  16.418 -25.099 1.00 40.17  ? 351 PRO   A CD  1 
ATOM   2457 N N   . LEU   A 1 312 ? -2.409  14.070 -20.997 1.00 36.05  ? 352 LEU   A N   1 
ATOM   2458 C CA  . LEU   A 1 312 ? -2.669  14.253 -19.567 1.00 40.67  ? 352 LEU   A CA  1 
ATOM   2459 C C   . LEU   A 1 312 ? -1.502  14.898 -18.826 1.00 47.13  ? 352 LEU   A C   1 
ATOM   2460 O O   . LEU   A 1 312 ? -1.712  15.766 -17.973 1.00 62.67  ? 352 LEU   A O   1 
ATOM   2461 C CB  . LEU   A 1 312 ? -2.994  12.915 -18.908 1.00 42.18  ? 352 LEU   A CB  1 
ATOM   2462 C CG  . LEU   A 1 312 ? -4.381  12.328 -19.094 1.00 46.23  ? 352 LEU   A CG  1 
ATOM   2463 C CD1 . LEU   A 1 312 ? -4.825  11.664 -17.822 1.00 41.13  ? 352 LEU   A CD1 1 
ATOM   2464 C CD2 . LEU   A 1 312 ? -5.339  13.407 -19.497 1.00 51.35  ? 352 LEU   A CD2 1 
ATOM   2465 N N   . ALA   A 1 313 ? -0.275  14.468 -19.088 1.00 46.03  ? 353 ALA   A N   1 
ATOM   2466 C CA  . ALA   A 1 313 ? 0.843   14.972 -18.305 1.00 62.18  ? 353 ALA   A CA  1 
ATOM   2467 C C   . ALA   A 1 313 ? 2.086   15.004 -19.177 1.00 80.15  ? 353 ALA   A C   1 
ATOM   2468 O O   . ALA   A 1 313 ? 2.106   14.470 -20.289 1.00 78.50  ? 353 ALA   A O   1 
ATOM   2469 C CB  . ALA   A 1 313 ? 1.070   14.132 -17.042 1.00 59.83  ? 353 ALA   A CB  1 
ATOM   2470 N N   . GLY   A 1 314 ? 3.126   15.650 -18.652 1.00 98.19  ? 354 GLY   A N   1 
ATOM   2471 C CA  . GLY   A 1 314 ? 4.353   15.864 -19.392 1.00 110.60 ? 354 GLY   A CA  1 
ATOM   2472 C C   . GLY   A 1 314 ? 4.360   17.073 -20.301 1.00 120.47 ? 354 GLY   A C   1 
ATOM   2473 O O   . GLY   A 1 314 ? 5.338   17.273 -21.027 1.00 126.07 ? 354 GLY   A O   1 
ATOM   2474 N N   . PHE   A 1 315 ? 3.310   17.898 -20.276 1.00 122.06 ? 355 PHE   A N   1 
ATOM   2475 C CA  . PHE   A 1 315 ? 3.171   19.022 -21.196 1.00 121.51 ? 355 PHE   A CA  1 
ATOM   2476 C C   . PHE   A 1 315 ? 3.063   20.360 -20.466 1.00 109.09 ? 355 PHE   A C   1 
ATOM   2477 O O   . PHE   A 1 315 ? 2.355   21.259 -20.929 1.00 113.67 ? 355 PHE   A O   1 
ATOM   2478 C CB  . PHE   A 1 315 ? 1.956   18.819 -22.107 1.00 132.44 ? 355 PHE   A CB  1 
ATOM   2479 C CG  . PHE   A 1 315 ? 2.274   18.191 -23.449 1.00 140.86 ? 355 PHE   A CG  1 
ATOM   2480 C CD1 . PHE   A 1 315 ? 1.920   18.836 -24.631 1.00 143.15 ? 355 PHE   A CD1 1 
ATOM   2481 C CD2 . PHE   A 1 315 ? 2.910   16.957 -23.533 1.00 142.44 ? 355 PHE   A CD2 1 
ATOM   2482 C CE1 . PHE   A 1 315 ? 2.198   18.270 -25.869 1.00 143.35 ? 355 PHE   A CE1 1 
ATOM   2483 C CE2 . PHE   A 1 315 ? 3.193   16.383 -24.770 1.00 143.23 ? 355 PHE   A CE2 1 
ATOM   2484 C CZ  . PHE   A 1 315 ? 2.836   17.043 -25.940 1.00 144.00 ? 355 PHE   A CZ  1 
ATOM   2485 N N   . GLY   A 1 316 ? 3.753   20.524 -19.340 1.00 86.75  ? 356 GLY   A N   1 
ATOM   2486 C CA  . GLY   A 1 316 ? 3.714   21.806 -18.653 1.00 73.62  ? 356 GLY   A CA  1 
ATOM   2487 C C   . GLY   A 1 316 ? 4.383   21.755 -17.288 1.00 54.29  ? 356 GLY   A C   1 
ATOM   2488 O O   . GLY   A 1 316 ? 5.191   20.867 -17.012 1.00 46.71  ? 356 GLY   A O   1 
ATOM   2489 N N   . TYR   A 1 317 ? 4.027   22.736 -16.442 1.00 35.50  ? 357 TYR   A N   1 
ATOM   2490 C CA  . TYR   A 1 317 ? 4.613   22.893 -15.115 1.00 30.90  ? 357 TYR   A CA  1 
ATOM   2491 C C   . TYR   A 1 317 ? 3.653   22.504 -13.992 1.00 30.90  ? 357 TYR   A C   1 
ATOM   2492 O O   . TYR   A 1 317 ? 3.851   22.926 -12.842 1.00 29.31  ? 357 TYR   A O   1 
ATOM   2493 C CB  . TYR   A 1 317 ? 5.092   24.332 -14.909 1.00 34.96  ? 357 TYR   A CB  1 
ATOM   2494 C CG  . TYR   A 1 317 ? 6.181   24.802 -15.862 1.00 40.77  ? 357 TYR   A CG  1 
ATOM   2495 C CD1 . TYR   A 1 317 ? 7.009   23.891 -16.516 1.00 39.41  ? 357 TYR   A CD1 1 
ATOM   2496 C CD2 . TYR   A 1 317 ? 6.388   26.155 -16.098 1.00 36.17  ? 357 TYR   A CD2 1 
ATOM   2497 C CE1 . TYR   A 1 317 ? 7.999   24.316 -17.376 1.00 36.51  ? 357 TYR   A CE1 1 
ATOM   2498 C CE2 . TYR   A 1 317 ? 7.384   26.592 -16.965 1.00 39.86  ? 357 TYR   A CE2 1 
ATOM   2499 C CZ  . TYR   A 1 317 ? 8.180   25.662 -17.605 1.00 40.45  ? 357 TYR   A CZ  1 
ATOM   2500 O OH  . TYR   A 1 317 ? 9.168   26.081 -18.469 1.00 43.74  ? 357 TYR   A OH  1 
ATOM   2501 N N   . GLY   A 1 318 ? 2.626   21.706 -14.291 1.00 31.80  ? 358 GLY   A N   1 
ATOM   2502 C CA  . GLY   A 1 318 ? 1.671   21.313 -13.262 1.00 31.92  ? 358 GLY   A CA  1 
ATOM   2503 C C   . GLY   A 1 318 ? 2.315   20.732 -12.019 1.00 34.30  ? 358 GLY   A C   1 
ATOM   2504 O O   . GLY   A 1 318 ? 1.905   21.039 -10.898 1.00 32.27  ? 358 GLY   A O   1 
ATOM   2505 N N   . LEU   A 1 319 ? 3.341   19.910 -12.194 1.00 30.17  ? 359 LEU   A N   1 
ATOM   2506 C CA  . LEU   A 1 319 ? 3.912   19.217 -11.046 1.00 34.32  ? 359 LEU   A CA  1 
ATOM   2507 C C   . LEU   A 1 319 ? 4.794   20.121 -10.178 1.00 31.21  ? 359 LEU   A C   1 
ATOM   2508 O O   . LEU   A 1 319 ? 4.574   20.182 -8.959  1.00 30.46  ? 359 LEU   A O   1 
ATOM   2509 C CB  . LEU   A 1 319 ? 4.684   17.986 -11.516 1.00 35.15  ? 359 LEU   A CB  1 
ATOM   2510 C CG  . LEU   A 1 319 ? 4.375   16.670 -10.818 1.00 48.21  ? 359 LEU   A CG  1 
ATOM   2511 C CD1 . LEU   A 1 319 ? 5.273   15.575 -11.386 1.00 51.35  ? 359 LEU   A CD1 1 
ATOM   2512 C CD2 . LEU   A 1 319 ? 4.552   16.785 -9.306  1.00 47.39  ? 359 LEU   A CD2 1 
ATOM   2513 N N   . PRO   A 1 320 ? 5.805   20.817 -10.719 1.00 27.97  ? 360 PRO   A N   1 
ATOM   2514 C CA  . PRO   A 1 320 ? 6.582   21.714 -9.842  1.00 31.17  ? 360 PRO   A CA  1 
ATOM   2515 C C   . PRO   A 1 320 ? 5.742   22.822 -9.227  1.00 30.68  ? 360 PRO   A C   1 
ATOM   2516 O O   . PRO   A 1 320 ? 5.989   23.210 -8.077  1.00 30.93  ? 360 PRO   A O   1 
ATOM   2517 C CB  . PRO   A 1 320 ? 7.672   22.274 -10.769 1.00 27.71  ? 360 PRO   A CB  1 
ATOM   2518 C CG  . PRO   A 1 320 ? 7.144   22.079 -12.149 1.00 29.92  ? 360 PRO   A CG  1 
ATOM   2519 C CD  . PRO   A 1 320 ? 6.363   20.796 -12.084 1.00 28.34  ? 360 PRO   A CD  1 
ATOM   2520 N N   . ILE   A 1 321 ? 4.737   23.326 -9.938  1.00 29.00  ? 361 ILE   A N   1 
ATOM   2521 C CA  . ILE   A 1 321 ? 3.901   24.367 -9.353  1.00 32.15  ? 361 ILE   A CA  1 
ATOM   2522 C C   . ILE   A 1 321 ? 3.016   23.787 -8.253  1.00 32.94  ? 361 ILE   A C   1 
ATOM   2523 O O   . ILE   A 1 321 ? 2.772   24.440 -7.227  1.00 30.68  ? 361 ILE   A O   1 
ATOM   2524 C CB  . ILE   A 1 321 ? 3.093   25.080 -10.452 1.00 31.51  ? 361 ILE   A CB  1 
ATOM   2525 C CG1 . ILE   A 1 321 ? 4.027   25.978 -11.272 1.00 34.33  ? 361 ILE   A CG1 1 
ATOM   2526 C CG2 . ILE   A 1 321 ? 1.944   25.881 -9.859  1.00 29.07  ? 361 ILE   A CG2 1 
ATOM   2527 C CD1 . ILE   A 1 321 ? 3.355   26.675 -12.432 1.00 35.26  ? 361 ILE   A CD1 1 
ATOM   2528 N N   . SER   A 1 322 ? 2.555   22.540 -8.423  1.00 29.80  ? 362 SER   A N   1 
ATOM   2529 C CA  . SER   A 1 322 ? 1.840   21.863 -7.339  1.00 31.60  ? 362 SER   A CA  1 
ATOM   2530 C C   . SER   A 1 322 ? 2.686   21.786 -6.076  1.00 29.81  ? 362 SER   A C   1 
ATOM   2531 O O   . SER   A 1 322 ? 2.189   22.031 -4.971  1.00 30.34  ? 362 SER   A O   1 
ATOM   2532 C CB  . SER   A 1 322 ? 1.424   20.454 -7.761  1.00 31.60  ? 362 SER   A CB  1 
ATOM   2533 O OG  . SER   A 1 322 ? 0.278   20.481 -8.589  1.00 32.80  ? 362 SER   A OG  1 
ATOM   2534 N N   . ARG   A 1 323 ? 3.965   21.425 -6.215  1.00 30.04  ? 363 ARG   A N   1 
ATOM   2535 C CA  . ARG   A 1 323 ? 4.817   21.345 -5.037  1.00 29.14  ? 363 ARG   A CA  1 
ATOM   2536 C C   . ARG   A 1 323 ? 5.026   22.719 -4.412  1.00 31.05  ? 363 ARG   A C   1 
ATOM   2537 O O   . ARG   A 1 323 ? 5.116   22.836 -3.181  1.00 30.74  ? 363 ARG   A O   1 
ATOM   2538 C CB  . ARG   A 1 323 ? 6.156   20.692 -5.390  1.00 25.15  ? 363 ARG   A CB  1 
ATOM   2539 C CG  . ARG   A 1 323 ? 7.091   20.602 -4.199  1.00 26.61  ? 363 ARG   A CG  1 
ATOM   2540 C CD  . ARG   A 1 323 ? 8.292   19.699 -4.455  1.00 30.61  ? 363 ARG   A CD  1 
ATOM   2541 N NE  . ARG   A 1 323 ? 9.243   20.315 -5.368  1.00 31.19  ? 363 ARG   A NE  1 
ATOM   2542 C CZ  . ARG   A 1 323 ? 10.438  19.814 -5.666  1.00 34.61  ? 363 ARG   A CZ  1 
ATOM   2543 N NH1 . ARG   A 1 323 ? 10.847  18.665 -5.127  1.00 31.84  ? 363 ARG   A NH1 1 
ATOM   2544 N NH2 . ARG   A 1 323 ? 11.227  20.470 -6.503  1.00 29.51  ? 363 ARG   A NH2 1 
ATOM   2545 N N   . LEU   A 1 324 ? 5.080   23.772 -5.231  1.00 31.35  ? 364 LEU   A N   1 
ATOM   2546 C CA  . LEU   A 1 324 ? 5.192   25.119 -4.680  1.00 30.01  ? 364 LEU   A CA  1 
ATOM   2547 C C   . LEU   A 1 324 ? 3.950   25.489 -3.880  1.00 32.09  ? 364 LEU   A C   1 
ATOM   2548 O O   . LEU   A 1 324 ? 4.056   26.116 -2.817  1.00 32.40  ? 364 LEU   A O   1 
ATOM   2549 C CB  . LEU   A 1 324 ? 5.433   26.131 -5.800  1.00 28.05  ? 364 LEU   A CB  1 
ATOM   2550 C CG  . LEU   A 1 324 ? 6.787   26.039 -6.518  1.00 31.62  ? 364 LEU   A CG  1 
ATOM   2551 C CD1 . LEU   A 1 324 ? 6.889   27.102 -7.584  1.00 29.83  ? 364 LEU   A CD1 1 
ATOM   2552 C CD2 . LEU   A 1 324 ? 7.937   26.193 -5.531  1.00 33.44  ? 364 LEU   A CD2 1 
ATOM   2553 N N   . TYR   A 1 325 ? 2.760   25.108 -4.366  1.00 29.18  ? 365 TYR   A N   1 
ATOM   2554 C CA  . TYR   A 1 325 ? 1.543   25.334 -3.585  1.00 31.10  ? 365 TYR   A CA  1 
ATOM   2555 C C   . TYR   A 1 325 ? 1.648   24.676 -2.216  1.00 30.19  ? 365 TYR   A C   1 
ATOM   2556 O O   . TYR   A 1 325 ? 1.341   25.296 -1.193  1.00 29.58  ? 365 TYR   A O   1 
ATOM   2557 C CB  . TYR   A 1 325 ? 0.308   24.813 -4.328  1.00 28.44  ? 365 TYR   A CB  1 
ATOM   2558 C CG  . TYR   A 1 325 ? -0.270  25.763 -5.361  1.00 29.61  ? 365 TYR   A CG  1 
ATOM   2559 C CD1 . TYR   A 1 325 ? -0.695  27.041 -5.014  1.00 36.16  ? 365 TYR   A CD1 1 
ATOM   2560 C CD2 . TYR   A 1 325 ? -0.419  25.367 -6.673  1.00 37.50  ? 365 TYR   A CD2 1 
ATOM   2561 C CE1 . TYR   A 1 325 ? -1.234  27.907 -5.970  1.00 44.91  ? 365 TYR   A CE1 1 
ATOM   2562 C CE2 . TYR   A 1 325 ? -0.959  26.215 -7.629  1.00 43.64  ? 365 TYR   A CE2 1 
ATOM   2563 C CZ  . TYR   A 1 325 ? -1.359  27.476 -7.278  1.00 43.05  ? 365 TYR   A CZ  1 
ATOM   2564 O OH  . TYR   A 1 325 ? -1.887  28.287 -8.253  1.00 46.07  ? 365 TYR   A OH  1 
ATOM   2565 N N   . ALA   A 1 326 ? 2.082   23.414 -2.175  1.00 33.34  ? 366 ALA   A N   1 
ATOM   2566 C CA  . ALA   A 1 326 ? 2.213   22.725 -0.894  1.00 35.13  ? 366 ALA   A CA  1 
ATOM   2567 C C   . ALA   A 1 326 ? 3.196   23.449 0.017   1.00 32.48  ? 366 ALA   A C   1 
ATOM   2568 O O   . ALA   A 1 326 ? 2.913   23.686 1.198   1.00 32.32  ? 366 ALA   A O   1 
ATOM   2569 C CB  . ALA   A 1 326 ? 2.653   21.279 -1.118  1.00 35.73  ? 366 ALA   A CB  1 
ATOM   2570 N N   . GLN   A 1 327 ? 4.353   23.832 -0.529  1.00 30.04  ? 367 GLN   A N   1 
ATOM   2571 C CA  . GLN   A 1 327 ? 5.396   24.456 0.271   1.00 30.88  ? 367 GLN   A CA  1 
ATOM   2572 C C   . GLN   A 1 327 ? 5.064   25.892 0.647   1.00 32.05  ? 367 GLN   A C   1 
ATOM   2573 O O   . GLN   A 1 327 ? 5.637   26.411 1.609   1.00 33.66  ? 367 GLN   A O   1 
ATOM   2574 C CB  . GLN   A 1 327 ? 6.727   24.400 -0.480  1.00 30.20  ? 367 GLN   A CB  1 
ATOM   2575 C CG  . GLN   A 1 327 ? 7.300   22.985 -0.619  1.00 31.47  ? 367 GLN   A CG  1 
ATOM   2576 C CD  . GLN   A 1 327 ? 8.516   22.930 -1.530  1.00 35.43  ? 367 GLN   A CD  1 
ATOM   2577 O OE1 . GLN   A 1 327 ? 8.859   23.913 -2.180  1.00 36.45  ? 367 GLN   A OE1 1 
ATOM   2578 N NE2 . GLN   A 1 327 ? 9.168   21.777 -1.582  1.00 31.87  ? 367 GLN   A NE2 1 
ATOM   2579 N N   . TYR   A 1 328 ? 4.136   26.533 -0.070  1.00 29.00  ? 368 TYR   A N   1 
ATOM   2580 C CA  . TYR   A 1 328 ? 3.815   27.933 0.194   1.00 29.48  ? 368 TYR   A CA  1 
ATOM   2581 C C   . TYR   A 1 328 ? 3.344   28.150 1.632   1.00 33.68  ? 368 TYR   A C   1 
ATOM   2582 O O   . TYR   A 1 328 ? 3.654   29.181 2.243   1.00 33.26  ? 368 TYR   A O   1 
ATOM   2583 C CB  . TYR   A 1 328 ? 2.761   28.402 -0.809  1.00 26.97  ? 368 TYR   A CB  1 
ATOM   2584 C CG  . TYR   A 1 328 ? 2.176   29.774 -0.555  1.00 30.68  ? 368 TYR   A CG  1 
ATOM   2585 C CD1 . TYR   A 1 328 ? 2.989   30.896 -0.414  1.00 29.73  ? 368 TYR   A CD1 1 
ATOM   2586 C CD2 . TYR   A 1 328 ? 0.803   29.952 -0.497  1.00 27.99  ? 368 TYR   A CD2 1 
ATOM   2587 C CE1 . TYR   A 1 328 ? 2.443   32.152 -0.196  1.00 30.95  ? 368 TYR   A CE1 1 
ATOM   2588 C CE2 . TYR   A 1 328 ? 0.250   31.201 -0.290  1.00 30.01  ? 368 TYR   A CE2 1 
ATOM   2589 C CZ  . TYR   A 1 328 ? 1.070   32.295 -0.137  1.00 34.58  ? 368 TYR   A CZ  1 
ATOM   2590 O OH  . TYR   A 1 328 ? 0.514   33.540 0.075   1.00 33.58  ? 368 TYR   A OH  1 
ATOM   2591 N N   . PHE   A 1 329 ? 2.603   27.195 2.199   1.00 33.99  ? 369 PHE   A N   1 
ATOM   2592 C CA  . PHE   A 1 329 ? 2.143   27.284 3.584   1.00 32.96  ? 369 PHE   A CA  1 
ATOM   2593 C C   . PHE   A 1 329 ? 2.811   26.233 4.462   1.00 35.65  ? 369 PHE   A C   1 
ATOM   2594 O O   . PHE   A 1 329 ? 2.177   25.653 5.351   1.00 37.44  ? 369 PHE   A O   1 
ATOM   2595 C CB  . PHE   A 1 329 ? 0.623   27.159 3.679   1.00 32.94  ? 369 PHE   A CB  1 
ATOM   2596 C CG  . PHE   A 1 329 ? -0.114  28.441 3.424   1.00 35.33  ? 369 PHE   A CG  1 
ATOM   2597 C CD1 . PHE   A 1 329 ? 0.123   29.563 4.211   1.00 40.04  ? 369 PHE   A CD1 1 
ATOM   2598 C CD2 . PHE   A 1 329 ? -1.052  28.524 2.411   1.00 38.70  ? 369 PHE   A CD2 1 
ATOM   2599 C CE1 . PHE   A 1 329 ? -0.565  30.744 3.987   1.00 43.31  ? 369 PHE   A CE1 1 
ATOM   2600 C CE2 . PHE   A 1 329 ? -1.748  29.705 2.182   1.00 40.70  ? 369 PHE   A CE2 1 
ATOM   2601 C CZ  . PHE   A 1 329 ? -1.500  30.814 2.966   1.00 41.84  ? 369 PHE   A CZ  1 
ATOM   2602 N N   . GLN   A 1 330 ? 4.100   25.985 4.214   1.00 31.87  ? 370 GLN   A N   1 
ATOM   2603 C CA  . GLN   A 1 330 ? 4.960   25.130 5.030   1.00 32.27  ? 370 GLN   A CA  1 
ATOM   2604 C C   . GLN   A 1 330 ? 4.603   23.653 4.926   1.00 33.82  ? 370 GLN   A C   1 
ATOM   2605 O O   . GLN   A 1 330 ? 4.964   22.865 5.808   1.00 35.82  ? 370 GLN   A O   1 
ATOM   2606 C CB  . GLN   A 1 330 ? 4.957   25.564 6.505   1.00 35.48  ? 370 GLN   A CB  1 
ATOM   2607 C CG  . GLN   A 1 330 ? 5.278   27.034 6.727   1.00 36.50  ? 370 GLN   A CG  1 
ATOM   2608 C CD  . GLN   A 1 330 ? 6.659   27.414 6.236   1.00 42.11  ? 370 GLN   A CD  1 
ATOM   2609 O OE1 . GLN   A 1 330 ? 7.593   26.619 6.304   1.00 50.42  ? 370 GLN   A OE1 1 
ATOM   2610 N NE2 . GLN   A 1 330 ? 6.797   28.637 5.746   1.00 50.41  ? 370 GLN   A NE2 1 
ATOM   2611 N N   . GLY   A 1 331 ? 3.890   23.256 3.879   1.00 31.91  ? 371 GLY   A N   1 
ATOM   2612 C CA  . GLY   A 1 331 ? 3.699   21.857 3.556   1.00 30.79  ? 371 GLY   A CA  1 
ATOM   2613 C C   . GLY   A 1 331 ? 4.762   21.383 2.587   1.00 31.73  ? 371 GLY   A C   1 
ATOM   2614 O O   . GLY   A 1 331 ? 5.824   21.995 2.445   1.00 30.61  ? 371 GLY   A O   1 
ATOM   2615 N N   . ASP   A 1 332 ? 4.470   20.281 1.900   1.00 28.72  ? 372 ASP   A N   1 
ATOM   2616 C CA  . ASP   A 1 332 ? 5.433   19.724 0.964   1.00 30.74  ? 372 ASP   A CA  1 
ATOM   2617 C C   . ASP   A 1 332 ? 4.705   18.752 0.047   1.00 29.50  ? 372 ASP   A C   1 
ATOM   2618 O O   . ASP   A 1 332 ? 3.540   18.405 0.268   1.00 31.54  ? 372 ASP   A O   1 
ATOM   2619 C CB  . ASP   A 1 332 ? 6.596   19.048 1.705   1.00 35.17  ? 372 ASP   A CB  1 
ATOM   2620 C CG  . ASP   A 1 332 ? 7.897   19.056 0.900   1.00 34.58  ? 372 ASP   A CG  1 
ATOM   2621 O OD1 . ASP   A 1 332 ? 7.875   19.399 -0.302  1.00 35.67  ? 372 ASP   A OD1 1 
ATOM   2622 O OD2 . ASP   A 1 332 ? 8.951   18.723 1.476   1.00 39.32  ? 372 ASP   A OD2 1 
ATOM   2623 N N   . LEU   A 1 333 ? 5.401   18.339 -1.007  1.00 28.13  ? 373 LEU   A N   1 
ATOM   2624 C CA  . LEU   A 1 333 ? 4.878   17.356 -1.949  1.00 27.77  ? 373 LEU   A CA  1 
ATOM   2625 C C   . LEU   A 1 333 ? 6.056   16.501 -2.374  1.00 30.19  ? 373 LEU   A C   1 
ATOM   2626 O O   . LEU   A 1 333 ? 7.029   17.020 -2.930  1.00 31.61  ? 373 LEU   A O   1 
ATOM   2627 C CB  . LEU   A 1 333 ? 4.209   18.019 -3.161  1.00 29.48  ? 373 LEU   A CB  1 
ATOM   2628 C CG  . LEU   A 1 333 ? 3.275   17.162 -4.044  1.00 32.64  ? 373 LEU   A CG  1 
ATOM   2629 C CD1 . LEU   A 1 333 ? 2.465   18.028 -4.986  1.00 28.41  ? 373 LEU   A CD1 1 
ATOM   2630 C CD2 . LEU   A 1 333 ? 4.023   16.104 -4.850  1.00 31.00  ? 373 LEU   A CD2 1 
ATOM   2631 N N   . LYS   A 1 334 ? 5.979   15.203 -2.104  1.00 30.43  ? 374 LYS   A N   1 
ATOM   2632 C CA  . LYS   A 1 334 ? 7.101   14.309 -2.327  1.00 31.90  ? 374 LYS   A CA  1 
ATOM   2633 C C   . LYS   A 1 334 ? 6.663   13.152 -3.206  1.00 33.06  ? 374 LYS   A C   1 
ATOM   2634 O O   . LYS   A 1 334 ? 5.510   12.709 -3.149  1.00 34.21  ? 374 LYS   A O   1 
ATOM   2635 C CB  . LYS   A 1 334 ? 7.666   13.802 -0.999  1.00 32.75  ? 374 LYS   A CB  1 
ATOM   2636 C CG  . LYS   A 1 334 ? 8.202   14.933 -0.130  1.00 39.44  ? 374 LYS   A CG  1 
ATOM   2637 C CD  . LYS   A 1 334 ? 8.851   14.448 1.151   1.00 44.19  ? 374 LYS   A CD  1 
ATOM   2638 C CE  . LYS   A 1 334 ? 9.794   15.517 1.683   1.00 48.96  ? 374 LYS   A CE  1 
ATOM   2639 N NZ  . LYS   A 1 334 ? 10.763  14.986 2.671   1.00 63.91  ? 374 LYS   A NZ  1 
ATOM   2640 N N   . LEU   A 1 335 ? 7.597   12.678 -4.026  1.00 29.62  ? 375 LEU   A N   1 
ATOM   2641 C CA  . LEU   A 1 335 ? 7.384   11.541 -4.912  1.00 28.18  ? 375 LEU   A CA  1 
ATOM   2642 C C   . LEU   A 1 335 ? 8.336   10.425 -4.536  1.00 31.77  ? 375 LEU   A C   1 
ATOM   2643 O O   . LEU   A 1 335 ? 9.527   10.666 -4.322  1.00 35.23  ? 375 LEU   A O   1 
ATOM   2644 C CB  . LEU   A 1 335 ? 7.635   11.898 -6.378  1.00 34.24  ? 375 LEU   A CB  1 
ATOM   2645 C CG  . LEU   A 1 335 ? 6.759   12.937 -7.058  1.00 41.73  ? 375 LEU   A CG  1 
ATOM   2646 C CD1 . LEU   A 1 335 ? 7.137   12.999 -8.544  1.00 42.01  ? 375 LEU   A CD1 1 
ATOM   2647 C CD2 . LEU   A 1 335 ? 5.295   12.598 -6.875  1.00 39.86  ? 375 LEU   A CD2 1 
ATOM   2648 N N   A TYR   A 1 336 ? 7.830   9.199  -4.452  0.51 31.02  ? 376 TYR   A N   1 
ATOM   2649 N N   B TYR   A 1 336 ? 7.800   9.207  -4.483  0.49 30.96  ? 376 TYR   A N   1 
ATOM   2650 C CA  A TYR   A 1 336 ? 8.756   8.079  -4.361  0.51 32.48  ? 376 TYR   A CA  1 
ATOM   2651 C CA  B TYR   A 1 336 ? 8.569   7.994  -4.242  0.49 32.76  ? 376 TYR   A CA  1 
ATOM   2652 C C   A TYR   A 1 336 ? 8.190   6.885  -5.107  0.51 33.40  ? 376 TYR   A C   1 
ATOM   2653 C C   B TYR   A 1 336 ? 8.097   6.947  -5.239  0.49 33.38  ? 376 TYR   A C   1 
ATOM   2654 O O   A TYR   A 1 336 ? 7.038   6.486  -4.904  0.51 31.37  ? 376 TYR   A O   1 
ATOM   2655 O O   B TYR   A 1 336 ? 6.889   6.719  -5.364  0.49 31.79  ? 376 TYR   A O   1 
ATOM   2656 C CB  A TYR   A 1 336 ? 9.090   7.710  -2.914  0.51 31.55  ? 376 TYR   A CB  1 
ATOM   2657 C CB  B TYR   A 1 336 ? 8.376   7.491  -2.803  0.49 30.87  ? 376 TYR   A CB  1 
ATOM   2658 C CG  A TYR   A 1 336 ? 7.939   7.293  -2.038  0.51 28.97  ? 376 TYR   A CG  1 
ATOM   2659 C CG  B TYR   A 1 336 ? 8.673   8.531  -1.739  0.49 30.98  ? 376 TYR   A CG  1 
ATOM   2660 C CD1 A TYR   A 1 336 ? 7.131   8.239  -1.428  0.51 29.00  ? 376 TYR   A CD1 1 
ATOM   2661 C CD1 B TYR   A 1 336 ? 9.955   8.676  -1.224  0.49 35.20  ? 376 TYR   A CD1 1 
ATOM   2662 C CD2 A TYR   A 1 336 ? 7.704   5.952  -1.767  0.51 32.64  ? 376 TYR   A CD2 1 
ATOM   2663 C CD2 B TYR   A 1 336 ? 7.675   9.368  -1.255  0.49 29.89  ? 376 TYR   A CD2 1 
ATOM   2664 C CE1 A TYR   A 1 336 ? 6.093   7.858  -0.593  0.51 26.86  ? 376 TYR   A CE1 1 
ATOM   2665 C CE1 B TYR   A 1 336 ? 10.236  9.622  -0.258  0.49 35.96  ? 376 TYR   A CE1 1 
ATOM   2666 C CE2 A TYR   A 1 336 ? 6.674   5.565  -0.936  0.51 28.60  ? 376 TYR   A CE2 1 
ATOM   2667 C CE2 B TYR   A 1 336 ? 7.946   10.316 -0.284  0.49 33.71  ? 376 TYR   A CE2 1 
ATOM   2668 C CZ  A TYR   A 1 336 ? 5.872   6.520  -0.356  0.51 26.92  ? 376 TYR   A CZ  1 
ATOM   2669 C CZ  B TYR   A 1 336 ? 9.232   10.437 0.208   0.49 36.23  ? 376 TYR   A CZ  1 
ATOM   2670 O OH  A TYR   A 1 336 ? 4.845   6.131  0.464   0.51 31.65  ? 376 TYR   A OH  1 
ATOM   2671 O OH  B TYR   A 1 336 ? 9.519   11.374 1.170   0.49 38.19  ? 376 TYR   A OH  1 
ATOM   2672 N N   . SER   A 1 337 ? 9.029   6.320  -5.958  1.00 32.31  ? 377 SER   A N   1 
ATOM   2673 C CA  . SER   A 1 337 ? 8.640   5.350  -6.963  1.00 34.23  ? 377 SER   A CA  1 
ATOM   2674 C C   . SER   A 1 337 ? 9.442   4.072  -6.814  1.00 35.98  ? 377 SER   A C   1 
ATOM   2675 O O   . SER   A 1 337 ? 10.607  4.092  -6.406  1.00 38.56  ? 377 SER   A O   1 
ATOM   2676 C CB  . SER   A 1 337 ? 8.839   5.923  -8.370  1.00 35.27  ? 377 SER   A CB  1 
ATOM   2677 O OG  . SER   A 1 337 ? 8.283   5.053  -9.326  1.00 39.55  ? 377 SER   A OG  1 
ATOM   2678 N N   . LEU   A 1 338 ? 8.796   2.959  -7.139  1.00 34.07  ? 378 LEU   A N   1 
ATOM   2679 C CA  . LEU   A 1 338 ? 9.448   1.663  -7.260  1.00 36.50  ? 378 LEU   A CA  1 
ATOM   2680 C C   . LEU   A 1 338 ? 9.491   1.343  -8.750  1.00 36.98  ? 378 LEU   A C   1 
ATOM   2681 O O   . LEU   A 1 338 ? 8.454   1.029  -9.346  1.00 33.97  ? 378 LEU   A O   1 
ATOM   2682 C CB  . LEU   A 1 338 ? 8.689   0.588  -6.486  1.00 37.27  ? 378 LEU   A CB  1 
ATOM   2683 C CG  . LEU   A 1 338 ? 8.190   0.963  -5.083  1.00 48.61  ? 378 LEU   A CG  1 
ATOM   2684 C CD1 . LEU   A 1 338 ? 7.533   -0.237 -4.400  1.00 53.00  ? 378 LEU   A CD1 1 
ATOM   2685 C CD2 . LEU   A 1 338 ? 9.322   1.523  -4.236  1.00 41.89  ? 378 LEU   A CD2 1 
ATOM   2686 N N   . GLU   A 1 339 ? 10.680  1.436  -9.352  1.00 32.29  ? 379 GLU   A N   1 
ATOM   2687 C CA  . GLU   A 1 339 ? 10.797  1.243  -10.793 1.00 33.58  ? 379 GLU   A CA  1 
ATOM   2688 C C   . GLU   A 1 339 ? 10.335  -0.155 -11.175 1.00 37.55  ? 379 GLU   A C   1 
ATOM   2689 O O   . GLU   A 1 339 ? 10.816  -1.149 -10.628 1.00 35.06  ? 379 GLU   A O   1 
ATOM   2690 C CB  . GLU   A 1 339 ? 12.241  1.453  -11.255 1.00 35.79  ? 379 GLU   A CB  1 
ATOM   2691 C CG  . GLU   A 1 339 ? 12.404  1.257  -12.760 1.00 37.38  ? 379 GLU   A CG  1 
ATOM   2692 C CD  . GLU   A 1 339 ? 13.850  1.099  -13.196 1.00 48.99  ? 379 GLU   A CD  1 
ATOM   2693 O OE1 . GLU   A 1 339 ? 14.681  0.635  -12.386 1.00 50.00  ? 379 GLU   A OE1 1 
ATOM   2694 O OE2 . GLU   A 1 339 ? 14.153  1.430  -14.363 1.00 51.87  ? 379 GLU   A OE2 1 
ATOM   2695 N N   . GLY   A 1 340 ? 9.411   -0.229 -12.127 1.00 37.69  ? 380 GLY   A N   1 
ATOM   2696 C CA  . GLY   A 1 340 ? 8.843   -1.489 -12.559 1.00 37.47  ? 380 GLY   A CA  1 
ATOM   2697 C C   . GLY   A 1 340 ? 7.495   -1.804 -11.945 1.00 38.24  ? 380 GLY   A C   1 
ATOM   2698 O O   . GLY   A 1 340 ? 6.799   -2.702 -12.434 1.00 39.52  ? 380 GLY   A O   1 
ATOM   2699 N N   . TYR   A 1 341 ? 7.105   -1.088 -10.892 1.00 36.32  ? 381 TYR   A N   1 
ATOM   2700 C CA  . TYR   A 1 341 ? 5.862   -1.378 -10.182 1.00 36.87  ? 381 TYR   A CA  1 
ATOM   2701 C C   . TYR   A 1 341 ? 4.932   -0.172 -10.197 1.00 35.30  ? 381 TYR   A C   1 
ATOM   2702 O O   . TYR   A 1 341 ? 3.869   -0.238 -10.819 1.00 37.43  ? 381 TYR   A O   1 
ATOM   2703 C CB  . TYR   A 1 341 ? 6.166   -1.838 -8.756  1.00 35.53  ? 381 TYR   A CB  1 
ATOM   2704 C CG  . TYR   A 1 341 ? 4.934   -2.087 -7.926  1.00 43.65  ? 381 TYR   A CG  1 
ATOM   2705 C CD1 . TYR   A 1 341 ? 4.127   -3.198 -8.155  1.00 50.71  ? 381 TYR   A CD1 1 
ATOM   2706 C CD2 . TYR   A 1 341 ? 4.577   -1.215 -6.910  1.00 45.05  ? 381 TYR   A CD2 1 
ATOM   2707 C CE1 . TYR   A 1 341 ? 2.995   -3.424 -7.392  1.00 57.38  ? 381 TYR   A CE1 1 
ATOM   2708 C CE2 . TYR   A 1 341 ? 3.449   -1.431 -6.144  1.00 51.23  ? 381 TYR   A CE2 1 
ATOM   2709 C CZ  . TYR   A 1 341 ? 2.663   -2.534 -6.386  1.00 61.58  ? 381 TYR   A CZ  1 
ATOM   2710 O OH  . TYR   A 1 341 ? 1.542   -2.735 -5.612  1.00 70.76  ? 381 TYR   A OH  1 
ATOM   2711 N N   . GLY   A 1 342 ? 5.292   0.927  -9.545  1.00 34.43  ? 382 GLY   A N   1 
ATOM   2712 C CA  . GLY   A 1 342 ? 4.403   2.067  -9.477  1.00 36.07  ? 382 GLY   A CA  1 
ATOM   2713 C C   . GLY   A 1 342 ? 4.990   3.151  -8.593  1.00 34.98  ? 382 GLY   A C   1 
ATOM   2714 O O   . GLY   A 1 342 ? 6.138   3.065  -8.153  1.00 34.71  ? 382 GLY   A O   1 
ATOM   2715 N N   . THR   A 1 343 ? 4.165   4.159  -8.319  1.00 33.13  ? 383 THR   A N   1 
ATOM   2716 C CA  . THR   A 1 343 ? 4.639   5.409  -7.744  1.00 34.22  ? 383 THR   A CA  1 
ATOM   2717 C C   . THR   A 1 343 ? 3.665   5.911  -6.685  1.00 33.67  ? 383 THR   A C   1 
ATOM   2718 O O   . THR   A 1 343 ? 2.447   5.782  -6.842  1.00 31.14  ? 383 THR   A O   1 
ATOM   2719 C CB  . THR   A 1 343 ? 4.816   6.462  -8.855  1.00 33.06  ? 383 THR   A CB  1 
ATOM   2720 O OG1 . THR   A 1 343 ? 5.751   5.977  -9.824  1.00 31.90  ? 383 THR   A OG1 1 
ATOM   2721 C CG2 . THR   A 1 343 ? 5.310   7.793  -8.297  1.00 34.31  ? 383 THR   A CG2 1 
ATOM   2722 N N   . ASP   A 1 344 ? 4.212   6.466  -5.600  1.00 31.06  ? 384 ASP   A N   1 
ATOM   2723 C CA  . ASP   A 1 344 ? 3.446   7.184  -4.589  1.00 30.19  ? 384 ASP   A CA  1 
ATOM   2724 C C   . ASP   A 1 344 ? 3.778   8.665  -4.655  1.00 31.53  ? 384 ASP   A C   1 
ATOM   2725 O O   . ASP   A 1 344 ? 4.943   9.040  -4.818  1.00 33.41  ? 384 ASP   A O   1 
ATOM   2726 C CB  . ASP   A 1 344 ? 3.753   6.701  -3.163  1.00 33.28  ? 384 ASP   A CB  1 
ATOM   2727 C CG  . ASP   A 1 344 ? 3.260   5.302  -2.889  1.00 42.19  ? 384 ASP   A CG  1 
ATOM   2728 O OD1 . ASP   A 1 344 ? 2.356   4.824  -3.599  1.00 41.95  ? 384 ASP   A OD1 1 
ATOM   2729 O OD2 . ASP   A 1 344 ? 3.779   4.682  -1.941  1.00 48.56  ? 384 ASP   A OD2 1 
ATOM   2730 N N   . ALA   A 1 345 ? 2.754   9.499  -4.514  1.00 28.97  ? 385 ALA   A N   1 
ATOM   2731 C CA  . ALA   A 1 345 ? 2.920   10.922 -4.258  1.00 30.36  ? 385 ALA   A CA  1 
ATOM   2732 C C   . ALA   A 1 345 ? 2.269   11.231 -2.917  1.00 37.16  ? 385 ALA   A C   1 
ATOM   2733 O O   . ALA   A 1 345 ? 1.188   10.710 -2.613  1.00 33.86  ? 385 ALA   A O   1 
ATOM   2734 C CB  . ALA   A 1 345 ? 2.289   11.775 -5.357  1.00 29.84  ? 385 ALA   A CB  1 
ATOM   2735 N N   . VAL   A 1 346 ? 2.919   12.067 -2.109  1.00 32.67  ? 386 VAL   A N   1 
ATOM   2736 C CA  . VAL   A 1 346 ? 2.392   12.431 -0.800  1.00 32.01  ? 386 VAL   A CA  1 
ATOM   2737 C C   . VAL   A 1 346 ? 2.357   13.946 -0.688  1.00 31.59  ? 386 VAL   A C   1 
ATOM   2738 O O   . VAL   A 1 346 ? 3.390   14.612 -0.836  1.00 31.16  ? 386 VAL   A O   1 
ATOM   2739 C CB  . VAL   A 1 346 ? 3.204   11.820 0.353   1.00 34.48  ? 386 VAL   A CB  1 
ATOM   2740 C CG1 . VAL   A 1 346 ? 2.553   12.180 1.684   1.00 33.17  ? 386 VAL   A CG1 1 
ATOM   2741 C CG2 . VAL   A 1 346 ? 3.288   10.303 0.206   1.00 33.79  ? 386 VAL   A CG2 1 
ATOM   2742 N N   . ILE   A 1 347 ? 1.168   14.485 -0.464  1.00 29.10  ? 387 ILE   A N   1 
ATOM   2743 C CA  . ILE   A 1 347 ? 0.985   15.885 -0.108  1.00 27.78  ? 387 ILE   A CA  1 
ATOM   2744 C C   . ILE   A 1 347 ? 1.000   15.990 1.408   1.00 29.95  ? 387 ILE   A C   1 
ATOM   2745 O O   . ILE   A 1 347 ? 0.256   15.277 2.095   1.00 32.10  ? 387 ILE   A O   1 
ATOM   2746 C CB  . ILE   A 1 347 ? -0.342  16.428 -0.659  1.00 28.06  ? 387 ILE   A CB  1 
ATOM   2747 C CG1 . ILE   A 1 347 ? -0.408  16.339 -2.185  1.00 34.26  ? 387 ILE   A CG1 1 
ATOM   2748 C CG2 . ILE   A 1 347 ? -0.578  17.865 -0.163  1.00 26.56  ? 387 ILE   A CG2 1 
ATOM   2749 C CD1 . ILE   A 1 347 ? -1.808  16.598 -2.727  1.00 31.81  ? 387 ILE   A CD1 1 
ATOM   2750 N N   . TYR   A 1 348 ? 1.830   16.884 1.936   1.00 29.92  ? 388 TYR   A N   1 
ATOM   2751 C CA  . TYR   A 1 348 ? 1.817   17.229 3.352   1.00 29.12  ? 388 TYR   A CA  1 
ATOM   2752 C C   . TYR   A 1 348 ? 1.291   18.645 3.509   1.00 32.61  ? 388 TYR   A C   1 
ATOM   2753 O O   . TYR   A 1 348 ? 1.791   19.567 2.858   1.00 35.32  ? 388 TYR   A O   1 
ATOM   2754 C CB  . TYR   A 1 348 ? 3.210   17.144 3.970   1.00 31.16  ? 388 TYR   A CB  1 
ATOM   2755 C CG  . TYR   A 1 348 ? 3.894   15.808 3.828   1.00 32.90  ? 388 TYR   A CG  1 
ATOM   2756 C CD1 . TYR   A 1 348 ? 4.576   15.473 2.666   1.00 35.61  ? 388 TYR   A CD1 1 
ATOM   2757 C CD2 . TYR   A 1 348 ? 3.873   14.888 4.867   1.00 36.47  ? 388 TYR   A CD2 1 
ATOM   2758 C CE1 . TYR   A 1 348 ? 5.219   14.254 2.546   1.00 37.29  ? 388 TYR   A CE1 1 
ATOM   2759 C CE2 . TYR   A 1 348 ? 4.511   13.664 4.754   1.00 41.05  ? 388 TYR   A CE2 1 
ATOM   2760 C CZ  . TYR   A 1 348 ? 5.181   13.356 3.592   1.00 43.09  ? 388 TYR   A CZ  1 
ATOM   2761 O OH  . TYR   A 1 348 ? 5.820   12.143 3.481   1.00 45.02  ? 388 TYR   A OH  1 
ATOM   2762 N N   . ILE   A 1 349 ? 0.293   18.810 4.374   1.00 28.56  ? 389 ILE   A N   1 
ATOM   2763 C CA  . ILE   A 1 349 ? -0.285  20.109 4.697   1.00 32.12  ? 389 ILE   A CA  1 
ATOM   2764 C C   . ILE   A 1 349 ? -0.311  20.254 6.212   1.00 34.42  ? 389 ILE   A C   1 
ATOM   2765 O O   . ILE   A 1 349 ? -0.551  19.277 6.932   1.00 35.29  ? 389 ILE   A O   1 
ATOM   2766 C CB  . ILE   A 1 349 ? -1.701  20.254 4.094   1.00 31.71  ? 389 ILE   A CB  1 
ATOM   2767 C CG1 . ILE   A 1 349 ? -1.608  20.427 2.575   1.00 33.50  ? 389 ILE   A CG1 1 
ATOM   2768 C CG2 . ILE   A 1 349 ? -2.488  21.391 4.755   1.00 30.36  ? 389 ILE   A CG2 1 
ATOM   2769 C CD1 . ILE   A 1 349 ? -2.930  20.266 1.871   1.00 32.76  ? 389 ILE   A CD1 1 
ATOM   2770 N N   . LYS   A 1 350 ? -0.044  21.466 6.703   1.00 37.05  ? 390 LYS   A N   1 
ATOM   2771 C CA  . LYS   A 1 350 ? -0.136  21.720 8.137   1.00 36.32  ? 390 LYS   A CA  1 
ATOM   2772 C C   . LYS   A 1 350 ? -1.589  21.641 8.590   1.00 36.81  ? 390 LYS   A C   1 
ATOM   2773 O O   . LYS   A 1 350 ? -2.455  22.340 8.056   1.00 37.02  ? 390 LYS   A O   1 
ATOM   2774 C CB  . LYS   A 1 350 ? 0.442   23.088 8.482   1.00 33.27  ? 390 LYS   A CB  1 
ATOM   2775 C CG  . LYS   A 1 350 ? 1.924   23.212 8.219   1.00 38.10  ? 390 LYS   A CG  1 
ATOM   2776 C CD  . LYS   A 1 350 ? 2.725   22.363 9.178   1.00 39.20  ? 390 LYS   A CD  1 
ATOM   2777 C CE  . LYS   A 1 350 ? 4.186   22.756 9.143   1.00 44.20  ? 390 LYS   A CE  1 
ATOM   2778 N NZ  . LYS   A 1 350 ? 4.994   21.964 10.105  1.00 46.55  ? 390 LYS   A NZ  1 
ATOM   2779 N N   . ALA   A 1 351 ? -1.854  20.793 9.584   1.00 35.99  ? 391 ALA   A N   1 
ATOM   2780 C CA  . ALA   A 1 351 ? -3.212  20.657 10.090  1.00 40.08  ? 391 ALA   A CA  1 
ATOM   2781 C C   . ALA   A 1 351 ? -3.672  21.880 10.873  1.00 42.24  ? 391 ALA   A C   1 
ATOM   2782 O O   . ALA   A 1 351 ? -4.883  22.081 11.023  1.00 43.45  ? 391 ALA   A O   1 
ATOM   2783 C CB  . ALA   A 1 351 ? -3.327  19.414 10.974  1.00 37.90  ? 391 ALA   A CB  1 
ATOM   2784 N N   . LEU   A 1 352 ? -2.745  22.689 11.377  1.00 40.42  ? 392 LEU   A N   1 
ATOM   2785 C CA  . LEU   A 1 352 ? -3.066  23.828 12.228  1.00 43.74  ? 392 LEU   A CA  1 
ATOM   2786 C C   . LEU   A 1 352 ? -2.823  25.127 11.473  1.00 40.99  ? 392 LEU   A C   1 
ATOM   2787 O O   . LEU   A 1 352 ? -1.756  25.312 10.872  1.00 37.62  ? 392 LEU   A O   1 
ATOM   2788 C CB  . LEU   A 1 352 ? -2.232  23.802 13.509  1.00 47.14  ? 392 LEU   A CB  1 
ATOM   2789 C CG  . LEU   A 1 352 ? -2.322  22.508 14.317  1.00 48.79  ? 392 LEU   A CG  1 
ATOM   2790 C CD1 . LEU   A 1 352 ? -1.586  22.655 15.634  1.00 54.53  ? 392 LEU   A CD1 1 
ATOM   2791 C CD2 . LEU   A 1 352 ? -3.773  22.116 14.544  1.00 50.61  ? 392 LEU   A CD2 1 
ATOM   2792 N N   . SER   A 1 353 ? -3.813  26.024 11.511  1.00 40.74  ? 393 SER   A N   1 
ATOM   2793 C CA  . SER   A 1 353 ? -3.702  27.283 10.779  1.00 45.15  ? 393 SER   A CA  1 
ATOM   2794 C C   . SER   A 1 353 ? -2.558  28.142 11.307  1.00 41.65  ? 393 SER   A C   1 
ATOM   2795 O O   . SER   A 1 353 ? -1.966  28.921 10.551  1.00 45.41  ? 393 SER   A O   1 
ATOM   2796 C CB  . SER   A 1 353 ? -5.024  28.051 10.856  1.00 46.33  ? 393 SER   A CB  1 
ATOM   2797 O OG  . SER   A 1 353 ? -5.417  28.239 12.204  1.00 50.89  ? 393 SER   A OG  1 
ATOM   2798 N N   . THR   A 1 354 ? -2.228  28.011 12.592  1.00 40.65  ? 394 THR   A N   1 
ATOM   2799 C CA  . THR   A 1 354 ? -1.147  28.806 13.160  1.00 46.91  ? 394 THR   A CA  1 
ATOM   2800 C C   . THR   A 1 354 ? 0.223   28.341 12.687  1.00 50.75  ? 394 THR   A C   1 
ATOM   2801 O O   . THR   A 1 354 ? 1.176   29.127 12.734  1.00 54.41  ? 394 THR   A O   1 
ATOM   2802 C CB  . THR   A 1 354 ? -1.220  28.772 14.686  1.00 50.48  ? 394 THR   A CB  1 
ATOM   2803 O OG1 . THR   A 1 354 ? -0.953  27.441 15.148  1.00 55.72  ? 394 THR   A OG1 1 
ATOM   2804 C CG2 . THR   A 1 354 ? -2.607  29.188 15.144  1.00 52.56  ? 394 THR   A CG2 1 
ATOM   2805 N N   . ASP   A 1 355 ? 0.344   27.094 12.222  1.00 45.62  ? 395 ASP   A N   1 
ATOM   2806 C CA  . ASP   A 1 355 ? 1.580   26.611 11.619  1.00 43.06  ? 395 ASP   A CA  1 
ATOM   2807 C C   . ASP   A 1 355 ? 1.683   26.925 10.130  1.00 42.07  ? 395 ASP   A C   1 
ATOM   2808 O O   . ASP   A 1 355 ? 2.744   26.696 9.539   1.00 41.14  ? 395 ASP   A O   1 
ATOM   2809 C CB  . ASP   A 1 355 ? 1.719   25.090 11.802  1.00 44.89  ? 395 ASP   A CB  1 
ATOM   2810 C CG  . ASP   A 1 355 ? 1.922   24.677 13.252  1.00 53.87  ? 395 ASP   A CG  1 
ATOM   2811 O OD1 . ASP   A 1 355 ? 2.292   25.534 14.084  1.00 54.22  ? 395 ASP   A OD1 1 
ATOM   2812 O OD2 . ASP   A 1 355 ? 1.721   23.478 13.552  1.00 54.32  ? 395 ASP   A OD2 1 
ATOM   2813 N N   . SER   A 1 356 ? 0.613   27.416 9.505   1.00 43.53  ? 396 SER   A N   1 
ATOM   2814 C CA  . SER   A 1 356 ? 0.598   27.637 8.057   1.00 44.88  ? 396 SER   A CA  1 
ATOM   2815 C C   . SER   A 1 356 ? 1.027   29.069 7.772   1.00 46.71  ? 396 SER   A C   1 
ATOM   2816 O O   . SER   A 1 356 ? 0.208   29.984 7.709   1.00 54.85  ? 396 SER   A O   1 
ATOM   2817 C CB  . SER   A 1 356 ? -0.784  27.357 7.484   1.00 47.52  ? 396 SER   A CB  1 
ATOM   2818 O OG  . SER   A 1 356 ? -1.285  26.120 7.952   1.00 51.21  ? 396 SER   A OG  1 
ATOM   2819 N N   . ILE   A 1 357 ? 2.327   29.266 7.580   1.00 43.94  ? 397 ILE   A N   1 
ATOM   2820 C CA  . ILE   A 1 357 ? 2.910   30.585 7.362   1.00 40.62  ? 397 ILE   A CA  1 
ATOM   2821 C C   . ILE   A 1 357 ? 3.449   30.653 5.939   1.00 37.50  ? 397 ILE   A C   1 
ATOM   2822 O O   . ILE   A 1 357 ? 4.058   29.692 5.453   1.00 39.35  ? 397 ILE   A O   1 
ATOM   2823 C CB  . ILE   A 1 357 ? 4.019   30.867 8.396   1.00 44.50  ? 397 ILE   A CB  1 
ATOM   2824 C CG1 . ILE   A 1 357 ? 3.444   30.799 9.811   1.00 55.33  ? 397 ILE   A CG1 1 
ATOM   2825 C CG2 . ILE   A 1 357 ? 4.681   32.212 8.140   1.00 41.15  ? 397 ILE   A CG2 1 
ATOM   2826 C CD1 . ILE   A 1 357 ? 4.496   30.694 10.888  1.00 58.48  ? 397 ILE   A CD1 1 
ATOM   2827 N N   . GLU   A 1 358 ? 3.203   31.780 5.266   1.00 35.75  ? 398 GLU   A N   1 
ATOM   2828 C CA  . GLU   A 1 358 ? 3.733   31.992 3.922   1.00 36.64  ? 398 GLU   A CA  1 
ATOM   2829 C C   . GLU   A 1 358 ? 5.232   31.723 3.872   1.00 33.66  ? 398 GLU   A C   1 
ATOM   2830 O O   . GLU   A 1 358 ? 5.983   32.141 4.757   1.00 37.77  ? 398 GLU   A O   1 
ATOM   2831 C CB  . GLU   A 1 358 ? 3.489   33.430 3.467   1.00 35.36  ? 398 GLU   A CB  1 
ATOM   2832 C CG  . GLU   A 1 358 ? 2.076   33.809 3.103   1.00 36.61  ? 398 GLU   A CG  1 
ATOM   2833 C CD  . GLU   A 1 358 ? 2.037   35.228 2.557   1.00 37.90  ? 398 GLU   A CD  1 
ATOM   2834 O OE1 . GLU   A 1 358 ? 2.317   36.170 3.333   1.00 37.03  ? 398 GLU   A OE1 1 
ATOM   2835 O OE2 . GLU   A 1 358 ? 1.774   35.397 1.346   1.00 39.03  ? 398 GLU   A OE2 1 
ATOM   2836 N N   . ARG   A 1 359 ? 5.665   31.045 2.814   1.00 33.56  ? 399 ARG   A N   1 
ATOM   2837 C CA  . ARG   A 1 359 ? 7.080   30.820 2.538   1.00 33.52  ? 399 ARG   A CA  1 
ATOM   2838 C C   . ARG   A 1 359 ? 7.449   31.693 1.342   1.00 32.56  ? 399 ARG   A C   1 
ATOM   2839 O O   . ARG   A 1 359 ? 6.996   31.436 0.223   1.00 34.91  ? 399 ARG   A O   1 
ATOM   2840 C CB  . ARG   A 1 359 ? 7.345   29.340 2.273   1.00 33.49  ? 399 ARG   A CB  1 
ATOM   2841 C CG  . ARG   A 1 359 ? 8.711   29.031 1.699   1.00 43.09  ? 399 ARG   A CG  1 
ATOM   2842 C CD  . ARG   A 1 359 ? 8.999   27.538 1.750   1.00 51.35  ? 399 ARG   A CD  1 
ATOM   2843 N NE  . ARG   A 1 359 ? 10.199  27.190 0.994   1.00 59.73  ? 399 ARG   A NE  1 
ATOM   2844 C CZ  . ARG   A 1 359 ? 11.441  27.344 1.446   1.00 65.87  ? 399 ARG   A CZ  1 
ATOM   2845 N NH1 . ARG   A 1 359 ? 11.655  27.849 2.656   1.00 65.96  ? 399 ARG   A NH1 1 
ATOM   2846 N NH2 . ARG   A 1 359 ? 12.474  26.998 0.685   1.00 60.35  ? 399 ARG   A NH2 1 
ATOM   2847 N N   . LEU   A 1 360 ? 8.251   32.737 1.581   1.00 31.38  ? 400 LEU   A N   1 
ATOM   2848 C CA  . LEU   A 1 360 ? 8.463   33.762 0.565   1.00 32.08  ? 400 LEU   A CA  1 
ATOM   2849 C C   . LEU   A 1 360 ? 9.939   33.925 0.238   1.00 32.75  ? 400 LEU   A C   1 
ATOM   2850 O O   . LEU   A 1 360 ? 10.773  33.945 1.148   1.00 35.75  ? 400 LEU   A O   1 
ATOM   2851 C CB  . LEU   A 1 360 ? 7.919   35.121 1.029   1.00 32.09  ? 400 LEU   A CB  1 
ATOM   2852 C CG  . LEU   A 1 360 ? 6.489   35.153 1.555   1.00 34.63  ? 400 LEU   A CG  1 
ATOM   2853 C CD1 . LEU   A 1 360 ? 6.130   36.554 2.046   1.00 37.95  ? 400 LEU   A CD1 1 
ATOM   2854 C CD2 . LEU   A 1 360 ? 5.550   34.701 0.472   1.00 30.77  ? 400 LEU   A CD2 1 
ATOM   2855 N N   . PRO   A 1 361 ? 10.287  34.078 -1.035  1.00 36.25  ? 401 PRO   A N   1 
ATOM   2856 C CA  . PRO   A 1 361 ? 11.671  34.399 -1.389  1.00 32.00  ? 401 PRO   A CA  1 
ATOM   2857 C C   . PRO   A 1 361 ? 11.973  35.863 -1.113  1.00 36.30  ? 401 PRO   A C   1 
ATOM   2858 O O   . PRO   A 1 361 ? 11.095  36.727 -1.144  1.00 34.95  ? 401 PRO   A O   1 
ATOM   2859 C CB  . PRO   A 1 361 ? 11.732  34.084 -2.890  1.00 35.31  ? 401 PRO   A CB  1 
ATOM   2860 C CG  . PRO   A 1 361 ? 10.332  34.329 -3.373  1.00 37.81  ? 401 PRO   A CG  1 
ATOM   2861 C CD  . PRO   A 1 361 ? 9.406   33.984 -2.213  1.00 35.86  ? 401 PRO   A CD  1 
ATOM   2862 N N   . VAL   A 1 362 ? 13.237  36.143 -0.814  1.00 32.27  ? 402 VAL   A N   1 
ATOM   2863 C CA  . VAL   A 1 362 ? 13.660  37.503 -0.505  1.00 32.18  ? 402 VAL   A CA  1 
ATOM   2864 C C   . VAL   A 1 362 ? 14.928  37.797 -1.289  1.00 37.73  ? 402 VAL   A C   1 
ATOM   2865 O O   . VAL   A 1 362 ? 15.829  36.949 -1.363  1.00 35.05  ? 402 VAL   A O   1 
ATOM   2866 C CB  . VAL   A 1 362 ? 13.879  37.707 1.009   1.00 35.53  ? 402 VAL   A CB  1 
ATOM   2867 C CG1 . VAL   A 1 362 ? 14.724  36.590 1.585   1.00 41.17  ? 402 VAL   A CG1 1 
ATOM   2868 C CG2 . VAL   A 1 362 ? 14.516  39.073 1.298   1.00 32.80  ? 402 VAL   A CG2 1 
ATOM   2869 N N   . TYR   A 1 363 ? 14.989  38.984 -1.892  1.00 36.96  ? 403 TYR   A N   1 
ATOM   2870 C CA  . TYR   A 1 363 ? 16.171  39.377 -2.649  1.00 38.08  ? 403 TYR   A CA  1 
ATOM   2871 C C   . TYR   A 1 363 ? 17.192  40.005 -1.711  1.00 37.96  ? 403 TYR   A C   1 
ATOM   2872 O O   . TYR   A 1 363 ? 16.886  40.977 -1.012  1.00 36.20  ? 403 TYR   A O   1 
ATOM   2873 C CB  . TYR   A 1 363 ? 15.816  40.351 -3.767  1.00 35.79  ? 403 TYR   A CB  1 
ATOM   2874 C CG  . TYR   A 1 363 ? 17.042  40.756 -4.550  1.00 37.50  ? 403 TYR   A CG  1 
ATOM   2875 C CD1 . TYR   A 1 363 ? 17.644  39.859 -5.426  1.00 35.19  ? 403 TYR   A CD1 1 
ATOM   2876 C CD2 . TYR   A 1 363 ? 17.629  42.010 -4.381  1.00 36.92  ? 403 TYR   A CD2 1 
ATOM   2877 C CE1 . TYR   A 1 363 ? 18.774  40.201 -6.137  1.00 39.72  ? 403 TYR   A CE1 1 
ATOM   2878 C CE2 . TYR   A 1 363 ? 18.769  42.368 -5.095  1.00 36.96  ? 403 TYR   A CE2 1 
ATOM   2879 C CZ  . TYR   A 1 363 ? 19.332  41.453 -5.971  1.00 39.40  ? 403 TYR   A CZ  1 
ATOM   2880 O OH  . TYR   A 1 363 ? 20.459  41.762 -6.693  1.00 42.31  ? 403 TYR   A OH  1 
ATOM   2881 N N   . ASN   A 1 364 ? 18.400  39.454 -1.687  1.00 34.92  ? 404 ASN   A N   1 
ATOM   2882 C CA  . ASN   A 1 364 ? 19.483  40.000 -0.880  1.00 34.01  ? 404 ASN   A CA  1 
ATOM   2883 C C   . ASN   A 1 364 ? 20.790  39.455 -1.441  1.00 36.38  ? 404 ASN   A C   1 
ATOM   2884 O O   . ASN   A 1 364 ? 20.802  38.764 -2.465  1.00 38.69  ? 404 ASN   A O   1 
ATOM   2885 C CB  . ASN   A 1 364 ? 19.299  39.652 0.602   1.00 34.15  ? 404 ASN   A CB  1 
ATOM   2886 C CG  . ASN   A 1 364 ? 19.098  38.164 0.828   1.00 38.71  ? 404 ASN   A CG  1 
ATOM   2887 O OD1 . ASN   A 1 364 ? 19.519  37.342 0.019   1.00 38.75  ? 404 ASN   A OD1 1 
ATOM   2888 N ND2 . ASN   A 1 364 ? 18.445  37.813 1.927   1.00 33.79  ? 404 ASN   A ND2 1 
ATOM   2889 N N   . LYS   A 1 365 ? 21.892  39.759 -0.752  1.00 34.66  ? 405 LYS   A N   1 
ATOM   2890 C CA  . LYS   A 1 365 ? 23.205  39.270 -1.161  1.00 38.56  ? 405 LYS   A CA  1 
ATOM   2891 C C   . LYS   A 1 365 ? 23.203  37.761 -1.370  1.00 37.26  ? 405 LYS   A C   1 
ATOM   2892 O O   . LYS   A 1 365 ? 23.780  37.259 -2.344  1.00 37.83  ? 405 LYS   A O   1 
ATOM   2893 C CB  . LYS   A 1 365 ? 24.245  39.662 -0.112  1.00 42.58  ? 405 LYS   A CB  1 
ATOM   2894 C CG  . LYS   A 1 365 ? 25.624  39.070 -0.346  1.00 53.62  ? 405 LYS   A CG  1 
ATOM   2895 C CD  . LYS   A 1 365 ? 26.453  39.943 -1.270  1.00 54.15  ? 405 LYS   A CD  1 
ATOM   2896 C CE  . LYS   A 1 365 ? 26.880  41.219 -0.566  1.00 51.86  ? 405 LYS   A CE  1 
ATOM   2897 N NZ  . LYS   A 1 365 ? 27.638  42.107 -1.474  1.00 55.35  ? 405 LYS   A NZ  1 
ATOM   2898 N N   . ALA   A 1 366 ? 22.554  37.018 -0.470  1.00 36.23  ? 406 ALA   A N   1 
ATOM   2899 C CA  . ALA   A 1 366 ? 22.504  35.565 -0.610  1.00 39.64  ? 406 ALA   A CA  1 
ATOM   2900 C C   . ALA   A 1 366 ? 21.837  35.162 -1.921  1.00 40.99  ? 406 ALA   A C   1 
ATOM   2901 O O   . ALA   A 1 366 ? 22.343  34.298 -2.652  1.00 38.02  ? 406 ALA   A O   1 
ATOM   2902 C CB  . ALA   A 1 366 ? 21.773  34.946 0.584   1.00 35.44  ? 406 ALA   A CB  1 
ATOM   2903 N N   . ALA   A 1 367 ? 20.702  35.789 -2.246  1.00 38.19  ? 407 ALA   A N   1 
ATOM   2904 C CA  . ALA   A 1 367 ? 20.020  35.479 -3.500  1.00 37.22  ? 407 ALA   A CA  1 
ATOM   2905 C C   . ALA   A 1 367 ? 20.899  35.817 -4.698  1.00 36.53  ? 407 ALA   A C   1 
ATOM   2906 O O   . ALA   A 1 367 ? 21.032  35.020 -5.635  1.00 36.07  ? 407 ALA   A O   1 
ATOM   2907 C CB  . ALA   A 1 367 ? 18.690  36.233 -3.579  1.00 38.85  ? 407 ALA   A CB  1 
ATOM   2908 N N   . TRP   A 1 368 ? 21.503  37.006 -4.686  1.00 37.00  ? 408 TRP   A N   1 
ATOM   2909 C CA  . TRP   A 1 368 ? 22.371  37.410 -5.784  1.00 36.78  ? 408 TRP   A CA  1 
ATOM   2910 C C   . TRP   A 1 368 ? 23.529  36.431 -5.953  1.00 43.65  ? 408 TRP   A C   1 
ATOM   2911 O O   . TRP   A 1 368 ? 23.883  36.062 -7.081  1.00 41.63  ? 408 TRP   A O   1 
ATOM   2912 C CB  . TRP   A 1 368 ? 22.881  38.835 -5.538  1.00 35.30  ? 408 TRP   A CB  1 
ATOM   2913 C CG  . TRP   A 1 368 ? 23.720  39.352 -6.655  1.00 36.72  ? 408 TRP   A CG  1 
ATOM   2914 C CD1 . TRP   A 1 368 ? 23.289  40.003 -7.775  1.00 36.89  ? 408 TRP   A CD1 1 
ATOM   2915 C CD2 . TRP   A 1 368 ? 25.140  39.241 -6.775  1.00 39.65  ? 408 TRP   A CD2 1 
ATOM   2916 N NE1 . TRP   A 1 368 ? 24.357  40.306 -8.584  1.00 39.24  ? 408 TRP   A NE1 1 
ATOM   2917 C CE2 . TRP   A 1 368 ? 25.505  39.848 -7.991  1.00 38.44  ? 408 TRP   A CE2 1 
ATOM   2918 C CE3 . TRP   A 1 368 ? 26.141  38.688 -5.966  1.00 39.02  ? 408 TRP   A CE3 1 
ATOM   2919 C CZ2 . TRP   A 1 368 ? 26.830  39.919 -8.421  1.00 40.90  ? 408 TRP   A CZ2 1 
ATOM   2920 C CZ3 . TRP   A 1 368 ? 27.454  38.759 -6.392  1.00 37.72  ? 408 TRP   A CZ3 1 
ATOM   2921 C CH2 . TRP   A 1 368 ? 27.788  39.368 -7.611  1.00 39.33  ? 408 TRP   A CH2 1 
ATOM   2922 N N   . LYS   A 1 369 ? 24.109  35.974 -4.838  1.00 46.39  ? 409 LYS   A N   1 
ATOM   2923 C CA  . LYS   A 1 369 ? 25.226  35.035 -4.901  1.00 46.51  ? 409 LYS   A CA  1 
ATOM   2924 C C   . LYS   A 1 369 ? 24.838  33.747 -5.616  1.00 48.69  ? 409 LYS   A C   1 
ATOM   2925 O O   . LYS   A 1 369 ? 25.662  33.152 -6.321  1.00 47.50  ? 409 LYS   A O   1 
ATOM   2926 C CB  . LYS   A 1 369 ? 25.737  34.718 -3.493  1.00 46.74  ? 409 LYS   A CB  1 
ATOM   2927 C CG  . LYS   A 1 369 ? 26.774  35.675 -2.931  1.00 55.56  ? 409 LYS   A CG  1 
ATOM   2928 C CD  . LYS   A 1 369 ? 27.434  35.051 -1.691  1.00 69.01  ? 409 LYS   A CD  1 
ATOM   2929 C CE  . LYS   A 1 369 ? 28.151  36.075 -0.815  1.00 77.07  ? 409 LYS   A CE  1 
ATOM   2930 N NZ  . LYS   A 1 369 ? 29.440  36.569 -1.380  1.00 77.15  ? 409 LYS   A NZ  1 
ATOM   2931 N N   . HIS   A 1 370 ? 23.590  33.293 -5.443  1.00 50.81  ? 410 HIS   A N   1 
ATOM   2932 C CA  . HIS   A 1 370 ? 23.148  32.070 -6.112  1.00 51.64  ? 410 HIS   A CA  1 
ATOM   2933 C C   . HIS   A 1 370 ? 23.263  32.188 -7.627  1.00 47.24  ? 410 HIS   A C   1 
ATOM   2934 O O   . HIS   A 1 370 ? 23.615  31.216 -8.306  1.00 48.28  ? 410 HIS   A O   1 
ATOM   2935 C CB  . HIS   A 1 370 ? 21.708  31.738 -5.726  1.00 51.10  ? 410 HIS   A CB  1 
ATOM   2936 C CG  . HIS   A 1 370 ? 21.595  30.695 -4.663  1.00 53.49  ? 410 HIS   A CG  1 
ATOM   2937 N ND1 . HIS   A 1 370 ? 21.619  29.346 -4.943  1.00 55.28  ? 410 HIS   A ND1 1 
ATOM   2938 C CD2 . HIS   A 1 370 ? 21.446  30.801 -3.321  1.00 58.76  ? 410 HIS   A CD2 1 
ATOM   2939 C CE1 . HIS   A 1 370 ? 21.500  28.665 -3.816  1.00 59.60  ? 410 HIS   A CE1 1 
ATOM   2940 N NE2 . HIS   A 1 370 ? 21.393  29.525 -2.816  1.00 59.82  ? 410 HIS   A NE2 1 
ATOM   2941 N N   . TYR   A 1 371 ? 22.969  33.367 -8.178  1.00 40.52  ? 411 TYR   A N   1 
ATOM   2942 C CA  . TYR   A 1 371 ? 23.047  33.551 -9.622  1.00 40.68  ? 411 TYR   A CA  1 
ATOM   2943 C C   . TYR   A 1 371 ? 24.480  33.666 -10.128 1.00 50.89  ? 411 TYR   A C   1 
ATOM   2944 O O   . TYR   A 1 371 ? 24.706  33.532 -11.336 1.00 52.77  ? 411 TYR   A O   1 
ATOM   2945 C CB  . TYR   A 1 371 ? 22.263  34.795 -10.037 1.00 38.41  ? 411 TYR   A CB  1 
ATOM   2946 C CG  . TYR   A 1 371 ? 20.763  34.667 -9.869  1.00 41.76  ? 411 TYR   A CG  1 
ATOM   2947 C CD1 . TYR   A 1 371 ? 19.973  34.152 -10.891 1.00 40.52  ? 411 TYR   A CD1 1 
ATOM   2948 C CD2 . TYR   A 1 371 ? 20.138  35.062 -8.692  1.00 42.06  ? 411 TYR   A CD2 1 
ATOM   2949 C CE1 . TYR   A 1 371 ? 18.603  34.035 -10.746 1.00 40.59  ? 411 TYR   A CE1 1 
ATOM   2950 C CE2 . TYR   A 1 371 ? 18.757  34.956 -8.537  1.00 34.93  ? 411 TYR   A CE2 1 
ATOM   2951 C CZ  . TYR   A 1 371 ? 18.001  34.434 -9.567  1.00 37.90  ? 411 TYR   A CZ  1 
ATOM   2952 O OH  . TYR   A 1 371 ? 16.637  34.316 -9.425  1.00 34.09  ? 411 TYR   A OH  1 
ATOM   2953 N N   . ASN   A 1 372 ? 25.451  33.913 -9.244  1.00 60.78  ? 412 ASN   A N   1 
ATOM   2954 C CA  . ASN   A 1 372 ? 26.824  34.198 -9.654  1.00 69.28  ? 412 ASN   A CA  1 
ATOM   2955 C C   . ASN   A 1 372 ? 27.824  33.223 -9.042  1.00 83.20  ? 412 ASN   A C   1 
ATOM   2956 O O   . ASN   A 1 372 ? 28.953  33.604 -8.727  1.00 86.65  ? 412 ASN   A O   1 
ATOM   2957 C CB  . ASN   A 1 372 ? 27.207  35.634 -9.298  1.00 63.96  ? 412 ASN   A CB  1 
ATOM   2958 C CG  . ASN   A 1 372 ? 26.356  36.657 -10.022 1.00 71.30  ? 412 ASN   A CG  1 
ATOM   2959 O OD1 . ASN   A 1 372 ? 25.272  37.025 -9.559  1.00 68.30  ? 412 ASN   A OD1 1 
ATOM   2960 N ND2 . ASN   A 1 372 ? 26.837  37.114 -11.174 1.00 75.46  ? 412 ASN   A ND2 1 
ATOM   2961 N N   . THR   A 1 373 ? 27.431  31.961 -8.870  1.00 92.19  ? 413 THR   A N   1 
ATOM   2962 C CA  . THR   A 1 373 ? 28.321  30.970 -8.283  1.00 103.49 ? 413 THR   A CA  1 
ATOM   2963 C C   . THR   A 1 373 ? 28.018  29.605 -8.883  1.00 110.91 ? 413 THR   A C   1 
ATOM   2964 O O   . THR   A 1 373 ? 26.882  29.321 -9.274  1.00 112.01 ? 413 THR   A O   1 
ATOM   2965 C CB  . THR   A 1 373 ? 28.183  30.912 -6.752  1.00 103.24 ? 413 THR   A CB  1 
ATOM   2966 O OG1 . THR   A 1 373 ? 28.146  32.239 -6.217  1.00 101.71 ? 413 THR   A OG1 1 
ATOM   2967 C CG2 . THR   A 1 373 ? 29.365  30.174 -6.132  1.00 106.79 ? 413 THR   A CG2 1 
ATOM   2968 N N   . ASN   A 1 374 ? 29.051  28.767 -8.961  1.00 115.54 ? 414 ASN   A N   1 
ATOM   2969 C CA  . ASN   A 1 374 ? 28.895  27.365 -9.324  1.00 116.87 ? 414 ASN   A CA  1 
ATOM   2970 C C   . ASN   A 1 374 ? 28.632  26.548 -8.063  1.00 121.81 ? 414 ASN   A C   1 
ATOM   2971 O O   . ASN   A 1 374 ? 29.337  26.696 -7.060  1.00 122.04 ? 414 ASN   A O   1 
ATOM   2972 C CB  . ASN   A 1 374 ? 30.141  26.852 -10.048 1.00 114.68 ? 414 ASN   A CB  1 
ATOM   2973 C CG  . ASN   A 1 374 ? 31.389  26.921 -9.185  1.00 113.58 ? 414 ASN   A CG  1 
ATOM   2974 O OD1 . ASN   A 1 374 ? 31.767  25.942 -8.542  1.00 113.88 ? 414 ASN   A OD1 1 
ATOM   2975 N ND2 . ASN   A 1 374 ? 32.030  28.084 -9.163  1.00 112.79 ? 414 ASN   A ND2 1 
ATOM   2976 N N   . HIS   A 1 375 ? 27.613  25.695 -8.110  1.00 127.54 ? 415 HIS   A N   1 
ATOM   2977 C CA  . HIS   A 1 375 ? 27.195  24.897 -6.958  1.00 135.82 ? 415 HIS   A CA  1 
ATOM   2978 C C   . HIS   A 1 375 ? 27.560  23.436 -7.220  1.00 140.33 ? 415 HIS   A C   1 
ATOM   2979 O O   . HIS   A 1 375 ? 26.891  22.752 -8.000  1.00 142.36 ? 415 HIS   A O   1 
ATOM   2980 C CB  . HIS   A 1 375 ? 25.698  25.063 -6.701  1.00 137.73 ? 415 HIS   A CB  1 
ATOM   2981 C CG  . HIS   A 1 375 ? 25.286  26.470 -6.389  1.00 139.18 ? 415 HIS   A CG  1 
ATOM   2982 N ND1 . HIS   A 1 375 ? 25.225  26.959 -5.101  1.00 138.96 ? 415 HIS   A ND1 1 
ATOM   2983 C CD2 . HIS   A 1 375 ? 24.904  27.489 -7.196  1.00 139.07 ? 415 HIS   A CD2 1 
ATOM   2984 C CE1 . HIS   A 1 375 ? 24.830  28.220 -5.129  1.00 138.27 ? 415 HIS   A CE1 1 
ATOM   2985 N NE2 . HIS   A 1 375 ? 24.629  28.566 -6.388  1.00 138.42 ? 415 HIS   A NE2 1 
ATOM   2986 N N   . GLU   A 1 376 ? 28.622  22.958 -6.565  1.00 139.11 ? 416 GLU   A N   1 
ATOM   2987 C CA  . GLU   A 1 376 ? 29.122  21.603 -6.770  1.00 135.78 ? 416 GLU   A CA  1 
ATOM   2988 C C   . GLU   A 1 376 ? 29.619  21.022 -5.453  1.00 128.85 ? 416 GLU   A C   1 
ATOM   2989 O O   . GLU   A 1 376 ? 30.190  21.733 -4.621  1.00 130.55 ? 416 GLU   A O   1 
ATOM   2990 C CB  . GLU   A 1 376 ? 30.253  21.571 -7.809  1.00 139.45 ? 416 GLU   A CB  1 
ATOM   2991 C CG  . GLU   A 1 376 ? 29.874  22.150 -9.161  1.00 140.12 ? 416 GLU   A CG  1 
ATOM   2992 C CD  . GLU   A 1 376 ? 31.072  22.366 -10.053 1.00 143.19 ? 416 GLU   A CD  1 
ATOM   2993 O OE1 . GLU   A 1 376 ? 31.621  21.367 -10.565 1.00 144.90 ? 416 GLU   A OE1 1 
ATOM   2994 O OE2 . GLU   A 1 376 ? 31.474  23.535 -10.232 1.00 144.09 ? 416 GLU   A OE2 1 
ATOM   2995 N N   . ALA   A 1 377 ? 29.412  19.711 -5.281  1.00 110.98 ? 417 ALA   A N   1 
ATOM   2996 C CA  . ALA   A 1 377 ? 29.739  19.017 -4.030  1.00 92.01  ? 417 ALA   A CA  1 
ATOM   2997 C C   . ALA   A 1 377 ? 31.166  18.478 -4.105  1.00 78.70  ? 417 ALA   A C   1 
ATOM   2998 O O   . ALA   A 1 377 ? 31.411  17.288 -4.323  1.00 72.18  ? 417 ALA   A O   1 
ATOM   2999 C CB  . ALA   A 1 377 ? 28.734  17.906 -3.755  1.00 86.40  ? 417 ALA   A CB  1 
ATOM   3000 N N   . ASP   A 1 378 ? 32.126  19.381 -3.893  1.00 68.42  ? 418 ASP   A N   1 
ATOM   3001 C CA  . ASP   A 1 378 ? 33.539  19.050 -4.018  1.00 59.56  ? 418 ASP   A CA  1 
ATOM   3002 C C   . ASP   A 1 378 ? 34.101  18.322 -2.803  1.00 48.75  ? 418 ASP   A C   1 
ATOM   3003 O O   . ASP   A 1 378 ? 35.271  17.923 -2.838  1.00 45.47  ? 418 ASP   A O   1 
ATOM   3004 C CB  . ASP   A 1 378 ? 34.354  20.323 -4.264  1.00 72.08  ? 418 ASP   A CB  1 
ATOM   3005 C CG  . ASP   A 1 378 ? 33.719  21.228 -5.305  1.00 87.98  ? 418 ASP   A CG  1 
ATOM   3006 O OD1 . ASP   A 1 378 ? 33.025  20.704 -6.204  1.00 93.17  ? 418 ASP   A OD1 1 
ATOM   3007 O OD2 . ASP   A 1 378 ? 33.909  22.463 -5.223  1.00 90.06  ? 418 ASP   A OD2 1 
ATOM   3008 N N   . ASP   A 1 379 ? 33.318  18.147 -1.732  1.00 44.60  ? 419 ASP   A N   1 
ATOM   3009 C CA  . ASP   A 1 379 ? 33.796  17.445 -0.544  1.00 45.54  ? 419 ASP   A CA  1 
ATOM   3010 C C   . ASP   A 1 379 ? 33.514  15.947 -0.595  1.00 49.28  ? 419 ASP   A C   1 
ATOM   3011 O O   . ASP   A 1 379 ? 33.864  15.226 0.350   1.00 44.08  ? 419 ASP   A O   1 
ATOM   3012 C CB  . ASP   A 1 379 ? 33.195  18.063 0.731   1.00 42.58  ? 419 ASP   A CB  1 
ATOM   3013 C CG  . ASP   A 1 379 ? 31.679  18.095 0.722   1.00 44.08  ? 419 ASP   A CG  1 
ATOM   3014 O OD1 . ASP   A 1 379 ? 31.075  17.826 -0.335  1.00 51.25  ? 419 ASP   A OD1 1 
ATOM   3015 O OD2 . ASP   A 1 379 ? 31.086  18.401 1.779   1.00 45.86  ? 419 ASP   A OD2 1 
ATOM   3016 N N   . TRP   A 1 380 ? 32.913  15.468 -1.686  1.00 43.46  ? 420 TRP   A N   1 
ATOM   3017 C CA  . TRP   A 1 380 ? 32.722  14.052 -1.957  1.00 44.82  ? 420 TRP   A CA  1 
ATOM   3018 C C   . TRP   A 1 380 ? 33.282  13.726 -3.334  1.00 47.36  ? 420 TRP   A C   1 
ATOM   3019 O O   . TRP   A 1 380 ? 33.323  14.582 -4.220  1.00 48.33  ? 420 TRP   A O   1 
ATOM   3020 C CB  . TRP   A 1 380 ? 31.244  13.669 -1.910  1.00 42.01  ? 420 TRP   A CB  1 
ATOM   3021 C CG  . TRP   A 1 380 ? 30.653  13.703 -0.539  1.00 43.78  ? 420 TRP   A CG  1 
ATOM   3022 C CD1 . TRP   A 1 380 ? 30.131  14.787 0.107   1.00 46.38  ? 420 TRP   A CD1 1 
ATOM   3023 C CD2 . TRP   A 1 380 ? 30.513  12.595 0.352   1.00 41.31  ? 420 TRP   A CD2 1 
ATOM   3024 N NE1 . TRP   A 1 380 ? 29.676  14.421 1.353   1.00 49.22  ? 420 TRP   A NE1 1 
ATOM   3025 C CE2 . TRP   A 1 380 ? 29.897  13.078 1.526   1.00 49.58  ? 420 TRP   A CE2 1 
ATOM   3026 C CE3 . TRP   A 1 380 ? 30.838  11.239 0.267   1.00 42.11  ? 420 TRP   A CE3 1 
ATOM   3027 C CZ2 . TRP   A 1 380 ? 29.608  12.252 2.610   1.00 51.04  ? 420 TRP   A CZ2 1 
ATOM   3028 C CZ3 . TRP   A 1 380 ? 30.557  10.421 1.342   1.00 45.55  ? 420 TRP   A CZ3 1 
ATOM   3029 C CH2 . TRP   A 1 380 ? 29.948  10.928 2.501   1.00 48.20  ? 420 TRP   A CH2 1 
ATOM   3030 N N   . CYS   A 1 381 ? 33.702  12.476 -3.510  1.00 45.68  ? 421 CYS   A N   1 
ATOM   3031 C CA  . CYS   A 1 381 ? 34.244  12.042 -4.789  1.00 53.45  ? 421 CYS   A CA  1 
ATOM   3032 C C   . CYS   A 1 381 ? 33.172  12.007 -5.871  1.00 65.13  ? 421 CYS   A C   1 
ATOM   3033 O O   . CYS   A 1 381 ? 32.005  11.699 -5.616  1.00 60.97  ? 421 CYS   A O   1 
ATOM   3034 C CB  . CYS   A 1 381 ? 34.880  10.667 -4.651  1.00 49.64  ? 421 CYS   A CB  1 
ATOM   3035 S SG  . CYS   A 1 381 ? 36.375  10.731 -3.674  1.00 52.93  ? 421 CYS   A SG  1 
ATOM   3036 N N   . VAL   A 1 382 ? 33.590  12.312 -7.096  1.00 88.90  ? 422 VAL   A N   1 
ATOM   3037 C CA  . VAL   A 1 382 ? 32.687  12.346 -8.245  1.00 97.51  ? 422 VAL   A CA  1 
ATOM   3038 C C   . VAL   A 1 382 ? 32.211  10.933 -8.569  1.00 106.94 ? 422 VAL   A C   1 
ATOM   3039 O O   . VAL   A 1 382 ? 33.033  10.031 -8.800  1.00 108.44 ? 422 VAL   A O   1 
ATOM   3040 C CB  . VAL   A 1 382 ? 33.357  13.009 -9.457  1.00 97.31  ? 422 VAL   A CB  1 
ATOM   3041 C CG1 . VAL   A 1 382 ? 33.427  14.516 -9.248  1.00 95.16  ? 422 VAL   A CG1 1 
ATOM   3042 C CG2 . VAL   A 1 382 ? 34.750  12.435 -9.685  1.00 98.65  ? 422 VAL   A CG2 1 
ATOM   3043 N N   . PRO   A 1 383 ? 30.892  10.689 -8.576  1.00 110.34 ? 423 PRO   A N   1 
ATOM   3044 C CA  . PRO   A 1 383 ? 30.299  9.377  -8.862  1.00 111.14 ? 423 PRO   A CA  1 
ATOM   3045 C C   . PRO   A 1 383 ? 30.467  8.958  -10.319 1.00 109.63 ? 423 PRO   A C   1 
ATOM   3046 O O   . PRO   A 1 383 ? 29.846  7.976  -10.725 1.00 106.98 ? 423 PRO   A O   1 
ATOM   3047 C CB  . PRO   A 1 383 ? 28.814  9.578  -8.526  1.00 110.40 ? 423 PRO   A CB  1 
ATOM   3048 C CG  . PRO   A 1 383 ? 28.758  10.821 -7.685  1.00 108.47 ? 423 PRO   A CG  1 
ATOM   3049 C CD  . PRO   A 1 383 ? 29.877  11.677 -8.173  1.00 108.15 ? 423 PRO   A CD  1 
HETATM 3050 K K   . K     B 2 .   ? 15.032  42.378 0.112   1.00 44.68  ? 501 K     A K   1 
HETATM 3051 C C10 . A1EMR C 3 .   ? 8.467   8.096  -17.270 1.00 55.82  ? 502 A1EMR A C10 1 
HETATM 3052 C C11 . A1EMR C 3 .   ? 9.603   7.169  -16.906 1.00 57.73  ? 502 A1EMR A C11 1 
HETATM 3053 C C16 . A1EMR C 3 .   ? 9.357   5.861  -16.528 1.00 59.56  ? 502 A1EMR A C16 1 
HETATM 3054 C C18 . A1EMR C 3 .   ? 5.670   7.515  -14.062 1.00 30.56  ? 502 A1EMR A C18 1 
HETATM 3055 C C20 . A1EMR C 3 .   ? 4.341   8.319  -12.422 1.00 30.32  ? 502 A1EMR A C20 1 
HETATM 3056 C C22 . A1EMR C 3 .   ? 3.264   9.542  -10.888 1.00 31.23  ? 502 A1EMR A C22 1 
HETATM 3057 C C23 . A1EMR C 3 .   ? 2.418   10.008 -9.875  1.00 25.89  ? 502 A1EMR A C23 1 
HETATM 3058 C C25 . A1EMR C 3 .   ? 0.963   9.392  -7.978  1.00 32.15  ? 502 A1EMR A C25 1 
HETATM 3059 C C26 . A1EMR C 3 .   ? 2.505   11.339 -9.471  1.00 28.41  ? 502 A1EMR A C26 1 
HETATM 3060 C C12 . A1EMR C 3 .   ? 10.887  7.400  -17.366 1.00 60.57  ? 502 A1EMR A C12 1 
HETATM 3061 C C14 . A1EMR C 3 .   ? 11.462  5.242  -17.050 1.00 62.53  ? 502 A1EMR A C14 1 
HETATM 3062 C C2  . A1EMR C 3 .   ? 3.399   12.164 -10.115 1.00 32.51  ? 502 A1EMR A C2  1 
HETATM 3063 C C3  . A1EMR C 3 .   ? 4.234   11.745 -11.123 1.00 30.28  ? 502 A1EMR A C3  1 
HETATM 3064 C C4  . A1EMR C 3 .   ? 4.171   10.411 -11.519 1.00 33.66  ? 502 A1EMR A C4  1 
HETATM 3065 C C5  . A1EMR C 3 .   ? 4.870   9.614  -12.510 1.00 34.10  ? 502 A1EMR A C5  1 
HETATM 3066 C C6  . A1EMR C 3 .   ? 5.864   9.822  -13.457 1.00 34.44  ? 502 A1EMR A C6  1 
HETATM 3067 C C7  . A1EMR C 3 .   ? 6.271   8.755  -14.257 1.00 38.35  ? 502 A1EMR A C7  1 
HETATM 3068 C C8  . A1EMR C 3 .   ? 7.354   8.947  -15.271 1.00 43.77  ? 502 A1EMR A C8  1 
HETATM 3069 F F1  . A1EMR C 3 .   ? 3.464   13.465 -9.730  1.00 33.47  ? 502 A1EMR A F1  1 
HETATM 3070 N N13 . A1EMR C 3 .   ? 11.832  6.458  -17.446 1.00 60.51  ? 502 A1EMR A N13 1 
HETATM 3071 N N15 . A1EMR C 3 .   ? 10.267  4.884  -16.589 1.00 59.65  ? 502 A1EMR A N15 1 
HETATM 3072 N N19 . A1EMR C 3 .   ? 4.710   7.266  -13.160 1.00 31.13  ? 502 A1EMR A N19 1 
HETATM 3073 N N21 . A1EMR C 3 .   ? 3.376   8.285  -11.448 1.00 28.67  ? 502 A1EMR A N21 1 
HETATM 3074 N N24 . A1EMR C 3 .   ? 1.561   9.130  -9.270  1.00 27.99  ? 502 A1EMR A N24 1 
HETATM 3075 N N9  . A1EMR C 3 .   ? 7.385   8.091  -16.295 1.00 47.58  ? 502 A1EMR A N9  1 
HETATM 3076 O O17 . A1EMR C 3 .   ? 8.190   9.834  -15.135 1.00 47.14  ? 502 A1EMR A O17 1 
HETATM 3077 C C1  . GOL   D 4 .   ? 18.870  7.990  -20.166 1.00 76.67  ? 503 GOL   A C1  1 
HETATM 3078 O O1  . GOL   D 4 .   ? 17.902  7.098  -19.700 1.00 73.10  ? 503 GOL   A O1  1 
HETATM 3079 C C2  . GOL   D 4 .   ? 18.574  9.363  -19.509 1.00 76.25  ? 503 GOL   A C2  1 
HETATM 3080 O O2  . GOL   D 4 .   ? 17.563  10.043 -20.173 1.00 73.69  ? 503 GOL   A O2  1 
HETATM 3081 C C3  . GOL   D 4 .   ? 19.929  10.121 -19.535 1.00 76.41  ? 503 GOL   A C3  1 
HETATM 3082 O O3  . GOL   D 4 .   ? 19.853  11.141 -18.581 1.00 76.34  ? 503 GOL   A O3  1 
HETATM 3083 C C1  . GOL   E 4 .   ? 10.625  26.383 -2.851  1.00 76.47  ? 504 GOL   A C1  1 
HETATM 3084 O O1  . GOL   E 4 .   ? 9.994   26.238 -1.611  1.00 67.92  ? 504 GOL   A O1  1 
HETATM 3085 C C2  . GOL   E 4 .   ? 12.129  26.031 -2.667  1.00 81.42  ? 504 GOL   A C2  1 
HETATM 3086 O O2  . GOL   E 4 .   ? 12.332  25.050 -1.702  1.00 81.59  ? 504 GOL   A O2  1 
HETATM 3087 C C3  . GOL   E 4 .   ? 12.595  25.584 -4.071  1.00 84.75  ? 504 GOL   A C3  1 
HETATM 3088 O O3  . GOL   E 4 .   ? 13.690  24.748 -3.889  1.00 89.27  ? 504 GOL   A O3  1 
HETATM 3089 C C1  . GOL   F 4 .   ? -16.042 21.641 -1.219  1.00 110.90 ? 505 GOL   A C1  1 
HETATM 3090 O O1  . GOL   F 4 .   ? -16.683 20.517 -0.691  1.00 108.67 ? 505 GOL   A O1  1 
HETATM 3091 C C2  . GOL   F 4 .   ? -14.890 22.015 -0.247  1.00 110.78 ? 505 GOL   A C2  1 
HETATM 3092 O O2  . GOL   F 4 .   ? -15.330 22.200 1.060   1.00 107.20 ? 505 GOL   A O2  1 
HETATM 3093 C C3  . GOL   F 4 .   ? -14.267 23.301 -0.838  1.00 108.74 ? 505 GOL   A C3  1 
HETATM 3094 O O3  . GOL   F 4 .   ? -13.499 23.860 0.184   1.00 106.37 ? 505 GOL   A O3  1 
HETATM 3095 O O   . HOH   G 5 .   ? -2.498  5.683  -1.453  1.00 34.24  ? 601 HOH   A O   1 
HETATM 3096 O O   . HOH   G 5 .   ? -2.086  24.569 6.259   1.00 38.00  ? 602 HOH   A O   1 
HETATM 3097 O O   . HOH   G 5 .   ? -2.225  18.161 -17.964 1.00 59.72  ? 603 HOH   A O   1 
HETATM 3098 O O   . HOH   G 5 .   ? 28.821  15.562 3.395   1.00 56.68  ? 604 HOH   A O   1 
HETATM 3099 O O   . HOH   G 5 .   ? 7.681   43.691 4.084   1.00 38.81  ? 605 HOH   A O   1 
HETATM 3100 O O   . HOH   G 5 .   ? 15.028  25.809 -6.546  1.00 47.06  ? 606 HOH   A O   1 
HETATM 3101 O O   . HOH   G 5 .   ? 0.414   23.891 2.153   1.00 32.90  ? 607 HOH   A O   1 
HETATM 3102 O O   . HOH   G 5 .   ? 16.589  13.135 -12.962 1.00 72.97  ? 608 HOH   A O   1 
HETATM 3103 O O   . HOH   G 5 .   ? 28.042  44.357 -0.395  1.00 42.52  ? 609 HOH   A O   1 
HETATM 3104 O O   . HOH   G 5 .   ? 1.294   17.693 -14.060 1.00 51.28  ? 610 HOH   A O   1 
HETATM 3105 O O   . HOH   G 5 .   ? -1.902  27.761 -10.755 1.00 59.34  ? 611 HOH   A O   1 
HETATM 3106 O O   . HOH   G 5 .   ? -6.441  61.230 -3.215  1.00 69.08  ? 612 HOH   A O   1 
HETATM 3107 O O   . HOH   G 5 .   ? -3.875  0.243  -7.762  1.00 47.04  ? 613 HOH   A O   1 
HETATM 3108 O O   . HOH   G 5 .   ? -13.193 10.528 8.809   1.00 45.70  ? 614 HOH   A O   1 
HETATM 3109 O O   . HOH   G 5 .   ? 14.797  24.470 -15.014 1.00 38.64  ? 615 HOH   A O   1 
HETATM 3110 O O   . HOH   G 5 .   ? 21.278  40.364 -19.260 1.00 58.43  ? 616 HOH   A O   1 
HETATM 3111 O O   . HOH   G 5 .   ? 6.081   32.461 -28.257 1.00 61.67  ? 617 HOH   A O   1 
HETATM 3112 O O   . HOH   G 5 .   ? 6.389   4.027  -15.702 1.00 40.80  ? 618 HOH   A O   1 
HETATM 3113 O O   . HOH   G 5 .   ? 24.906  30.009 -10.831 1.00 55.44  ? 619 HOH   A O   1 
HETATM 3114 O O   . HOH   G 5 .   ? -5.412  17.759 13.827  1.00 53.97  ? 620 HOH   A O   1 
HETATM 3115 O O   . HOH   G 5 .   ? 9.611   16.795 -3.317  1.00 33.41  ? 621 HOH   A O   1 
HETATM 3116 O O   . HOH   G 5 .   ? -9.104  20.114 11.559  1.00 55.94  ? 622 HOH   A O   1 
HETATM 3117 O O   . HOH   G 5 .   ? 0.321   23.802 4.984   1.00 32.85  ? 623 HOH   A O   1 
HETATM 3118 O O   . HOH   G 5 .   ? -13.833 13.535 5.700   1.00 45.16  ? 624 HOH   A O   1 
HETATM 3119 O O   . HOH   G 5 .   ? -8.802  17.815 -35.359 1.00 53.17  ? 625 HOH   A O   1 
HETATM 3120 O O   . HOH   G 5 .   ? 20.294  49.078 -9.373  1.00 65.05  ? 626 HOH   A O   1 
HETATM 3121 O O   . HOH   G 5 .   ? 1.543   1.910  -23.834 1.00 60.83  ? 627 HOH   A O   1 
HETATM 3122 O O   . HOH   G 5 .   ? -2.924  15.405 -28.743 1.00 50.77  ? 628 HOH   A O   1 
HETATM 3123 O O   . HOH   G 5 .   ? -15.491 6.581  -17.247 1.00 55.40  ? 629 HOH   A O   1 
HETATM 3124 O O   . HOH   G 5 .   ? 13.050  37.853 -4.688  1.00 39.08  ? 630 HOH   A O   1 
HETATM 3125 O O   . HOH   G 5 .   ? 1.568   -1.941 -21.855 1.00 65.68  ? 631 HOH   A O   1 
HETATM 3126 O O   . HOH   G 5 .   ? 5.062   56.236 3.791   1.00 62.35  ? 632 HOH   A O   1 
HETATM 3127 O O   . HOH   G 5 .   ? -1.320  33.280 -11.198 1.00 50.35  ? 633 HOH   A O   1 
HETATM 3128 O O   . HOH   G 5 .   ? -7.785  29.474 12.390  1.00 60.96  ? 634 HOH   A O   1 
HETATM 3129 O O   . HOH   G 5 .   ? 14.074  22.981 -7.679  1.00 45.69  ? 635 HOH   A O   1 
HETATM 3130 O O   . HOH   G 5 .   ? 2.522   18.892 7.331   1.00 41.41  ? 636 HOH   A O   1 
HETATM 3131 O O   . HOH   G 5 .   ? -1.028  13.359 -28.273 1.00 54.99  ? 637 HOH   A O   1 
HETATM 3132 O O   . HOH   G 5 .   ? 7.233   11.656 5.709   1.00 32.73  ? 638 HOH   A O   1 
HETATM 3133 O O   . HOH   G 5 .   ? 8.224   38.462 -4.264  1.00 33.07  ? 639 HOH   A O   1 
HETATM 3134 O O   . HOH   G 5 .   ? -9.538  0.730  -12.219 1.00 34.90  ? 640 HOH   A O   1 
HETATM 3135 O O   . HOH   G 5 .   ? -1.088  26.282 -0.591  1.00 37.99  ? 641 HOH   A O   1 
HETATM 3136 O O   . HOH   G 5 .   ? -15.257 17.250 11.154  1.00 64.35  ? 642 HOH   A O   1 
HETATM 3137 O O   . HOH   G 5 .   ? 5.250   26.460 10.511  1.00 48.35  ? 643 HOH   A O   1 
HETATM 3138 O O   . HOH   G 5 .   ? 30.011  40.954 -0.904  1.00 48.76  ? 644 HOH   A O   1 
HETATM 3139 O O   . HOH   G 5 .   ? 2.668   16.022 16.196  1.00 43.66  ? 645 HOH   A O   1 
HETATM 3140 O O   . HOH   G 5 .   ? -3.934  22.574 -12.645 1.00 61.13  ? 646 HOH   A O   1 
HETATM 3141 O O   . HOH   G 5 .   ? -4.096  2.580  -22.487 1.00 38.95  ? 647 HOH   A O   1 
HETATM 3142 O O   . HOH   G 5 .   ? 6.288   36.847 -8.980  1.00 34.63  ? 648 HOH   A O   1 
HETATM 3143 O O   . HOH   G 5 .   ? 12.086  9.852  -4.658  1.00 34.48  ? 649 HOH   A O   1 
HETATM 3144 O O   . HOH   G 5 .   ? -1.594  32.963 -13.955 1.00 63.13  ? 650 HOH   A O   1 
HETATM 3145 O O   . HOH   G 5 .   ? 5.122   18.101 10.543  1.00 36.74  ? 651 HOH   A O   1 
HETATM 3146 O O   . HOH   G 5 .   ? 8.449   22.719 -7.041  1.00 32.80  ? 652 HOH   A O   1 
HETATM 3147 O O   . HOH   G 5 .   ? -1.358  11.616 -21.910 1.00 43.99  ? 653 HOH   A O   1 
HETATM 3148 O O   . HOH   G 5 .   ? -5.861  17.814 -36.021 1.00 50.66  ? 654 HOH   A O   1 
HETATM 3149 O O   . HOH   G 5 .   ? 4.306   4.882  -11.853 1.00 30.52  ? 655 HOH   A O   1 
HETATM 3150 O O   . HOH   G 5 .   ? 12.223  1.904  -16.222 1.00 54.10  ? 656 HOH   A O   1 
HETATM 3151 O O   . HOH   G 5 .   ? 2.176   2.170  -3.017  1.00 51.99  ? 657 HOH   A O   1 
HETATM 3152 O O   . HOH   G 5 .   ? -11.223 23.285 9.630   1.00 51.15  ? 658 HOH   A O   1 
HETATM 3153 O O   . HOH   G 5 .   ? -3.129  29.512 -32.839 1.00 56.86  ? 659 HOH   A O   1 
HETATM 3154 O O   . HOH   G 5 .   ? 1.790   38.699 -9.969  1.00 47.87  ? 660 HOH   A O   1 
HETATM 3155 O O   . HOH   G 5 .   ? -15.407 12.055 -14.585 1.00 47.21  ? 661 HOH   A O   1 
HETATM 3156 O O   . HOH   G 5 .   ? 4.832   20.258 6.631   1.00 49.34  ? 662 HOH   A O   1 
HETATM 3157 O O   . HOH   G 5 .   ? 12.800  2.592  -8.057  1.00 32.55  ? 663 HOH   A O   1 
HETATM 3158 O O   . HOH   G 5 .   ? 8.315   32.276 6.193   1.00 48.28  ? 664 HOH   A O   1 
HETATM 3159 O O   . HOH   G 5 .   ? 16.322  12.155 -9.108  1.00 44.13  ? 665 HOH   A O   1 
HETATM 3160 O O   . HOH   G 5 .   ? 23.672  32.213 -1.455  1.00 53.66  ? 666 HOH   A O   1 
HETATM 3161 O O   . HOH   G 5 .   ? 10.622  37.770 -3.641  1.00 36.75  ? 667 HOH   A O   1 
HETATM 3162 O O   . HOH   G 5 .   ? 35.315  15.942 -5.535  1.00 59.64  ? 668 HOH   A O   1 
HETATM 3163 O O   . HOH   G 5 .   ? -13.044 15.369 4.086   1.00 37.00  ? 669 HOH   A O   1 
HETATM 3164 O O   . HOH   G 5 .   ? 7.380   59.399 0.939   1.00 52.60  ? 670 HOH   A O   1 
HETATM 3165 O O   . HOH   G 5 .   ? 15.088  51.332 0.881   1.00 37.98  ? 671 HOH   A O   1 
HETATM 3166 O O   . HOH   G 5 .   ? -6.388  20.178 12.325  1.00 49.58  ? 672 HOH   A O   1 
HETATM 3167 O O   . HOH   G 5 .   ? 2.595   24.634 -17.849 1.00 59.11  ? 673 HOH   A O   1 
HETATM 3168 O O   . HOH   G 5 .   ? -11.852 6.025  9.055   1.00 61.76  ? 674 HOH   A O   1 
HETATM 3169 O O   . HOH   G 5 .   ? 15.796  44.119 -16.163 1.00 49.56  ? 675 HOH   A O   1 
HETATM 3170 O O   . HOH   G 5 .   ? 1.858   31.592 13.789  1.00 62.52  ? 676 HOH   A O   1 
HETATM 3171 O O   . HOH   G 5 .   ? 10.133  44.647 -20.092 1.00 46.00  ? 677 HOH   A O   1 
HETATM 3172 O O   . HOH   G 5 .   ? 12.367  5.766  -7.840  1.00 40.01  ? 678 HOH   A O   1 
HETATM 3173 O O   . HOH   G 5 .   ? 6.633   -3.930 -14.917 1.00 56.11  ? 679 HOH   A O   1 
HETATM 3174 O O   . HOH   G 5 .   ? 6.605   17.299 -14.684 1.00 40.07  ? 680 HOH   A O   1 
HETATM 3175 O O   . HOH   G 5 .   ? 21.385  33.938 -14.985 1.00 43.43  ? 681 HOH   A O   1 
HETATM 3176 O O   . HOH   G 5 .   ? -6.629  23.936 9.797   1.00 50.25  ? 682 HOH   A O   1 
HETATM 3177 O O   . HOH   G 5 .   ? -2.239  32.277 -4.990  1.00 49.50  ? 683 HOH   A O   1 
HETATM 3178 O O   . HOH   G 5 .   ? 4.336   45.337 4.839   1.00 52.69  ? 684 HOH   A O   1 
HETATM 3179 O O   . HOH   G 5 .   ? 18.972  25.368 -9.379  1.00 58.65  ? 685 HOH   A O   1 
HETATM 3180 O O   . HOH   G 5 .   ? 4.018   21.768 12.713  1.00 49.76  ? 686 HOH   A O   1 
HETATM 3181 O O   . HOH   G 5 .   ? 17.700  23.498 -15.562 1.00 62.56  ? 687 HOH   A O   1 
HETATM 3182 O O   . HOH   G 5 .   ? -1.411  12.125 15.028  1.00 42.34  ? 688 HOH   A O   1 
HETATM 3183 O O   . HOH   G 5 .   ? -7.661  14.683 -22.729 1.00 33.85  ? 689 HOH   A O   1 
HETATM 3184 O O   . HOH   G 5 .   ? 4.443   15.520 -15.581 1.00 63.36  ? 690 HOH   A O   1 
HETATM 3185 O O   . HOH   G 5 .   ? 12.587  43.536 -13.372 1.00 40.29  ? 691 HOH   A O   1 
HETATM 3186 O O   . HOH   G 5 .   ? -11.633 11.648 -27.565 0.50 48.11  ? 692 HOH   A O   1 
HETATM 3187 O O   . HOH   G 5 .   ? 10.721  22.729 -8.677  1.00 33.01  ? 693 HOH   A O   1 
HETATM 3188 O O   . HOH   G 5 .   ? 19.564  42.296 -9.525  1.00 44.39  ? 694 HOH   A O   1 
HETATM 3189 O O   . HOH   G 5 .   ? 16.383  20.356 -11.257 1.00 49.21  ? 695 HOH   A O   1 
HETATM 3190 O O   . HOH   G 5 .   ? -2.796  2.583  -10.865 1.00 33.57  ? 696 HOH   A O   1 
HETATM 3191 O O   . HOH   G 5 .   ? 5.713   6.082  -17.366 1.00 50.99  ? 697 HOH   A O   1 
HETATM 3192 O O   . HOH   G 5 .   ? 1.625   20.376 -16.575 1.00 51.60  ? 698 HOH   A O   1 
HETATM 3193 O O   . HOH   G 5 .   ? 11.442  17.342 4.077   1.00 66.34  ? 699 HOH   A O   1 
HETATM 3194 O O   . HOH   G 5 .   ? -1.294  12.643 8.440   1.00 36.05  ? 700 HOH   A O   1 
HETATM 3195 O O   . HOH   G 5 .   ? -2.533  9.661  4.369   1.00 47.36  ? 701 HOH   A O   1 
HETATM 3196 O O   . HOH   G 5 .   ? 4.758   52.684 1.649   1.00 60.27  ? 702 HOH   A O   1 
HETATM 3197 O O   . HOH   G 5 .   ? 9.471   18.624 -22.291 1.00 64.28  ? 703 HOH   A O   1 
HETATM 3198 O O   . HOH   G 5 .   ? 2.452   5.004  4.289   1.00 56.02  ? 704 HOH   A O   1 
HETATM 3199 O O   . HOH   G 5 .   ? 0.133   7.484  -25.417 1.00 65.47  ? 705 HOH   A O   1 
HETATM 3200 O O   . HOH   G 5 .   ? 23.168  37.072 -13.734 1.00 58.19  ? 706 HOH   A O   1 
HETATM 3201 O O   . HOH   G 5 .   ? -14.605 12.305 -20.706 1.00 41.09  ? 707 HOH   A O   1 
HETATM 3202 O O   . HOH   G 5 .   ? 11.778  20.985 -2.418  1.00 51.87  ? 708 HOH   A O   1 
HETATM 3203 O O   . HOH   G 5 .   ? -9.252  13.213 -29.825 1.00 38.69  ? 709 HOH   A O   1 
HETATM 3204 O O   . HOH   G 5 .   ? 2.278   2.361  -5.705  1.00 41.93  ? 710 HOH   A O   1 
HETATM 3205 O O   . HOH   G 5 .   ? -9.533  21.577 -13.835 1.00 51.99  ? 711 HOH   A O   1 
HETATM 3206 O O   . HOH   G 5 .   ? -16.274 8.443  -12.112 1.00 55.54  ? 712 HOH   A O   1 
HETATM 3207 O O   . HOH   G 5 .   ? -6.545  25.467 12.160  1.00 50.92  ? 713 HOH   A O   1 
HETATM 3208 O O   . HOH   G 5 .   ? 0.078   21.956 11.766  1.00 37.27  ? 714 HOH   A O   1 
HETATM 3209 O O   . HOH   G 5 .   ? 7.796   23.893 3.292   1.00 55.24  ? 715 HOH   A O   1 
HETATM 3210 O O   . HOH   G 5 .   ? 4.413   18.976 -14.685 1.00 38.02  ? 716 HOH   A O   1 
HETATM 3211 O O   . HOH   G 5 .   ? -11.831 8.522  10.365  1.00 51.88  ? 717 HOH   A O   1 
HETATM 3212 O O   . HOH   G 5 .   ? 6.148   19.694 8.773   1.00 45.89  ? 718 HOH   A O   1 
HETATM 3213 O O   . HOH   G 5 .   ? -8.637  16.649 -24.102 1.00 39.14  ? 719 HOH   A O   1 
HETATM 3214 O O   . HOH   G 5 .   ? 6.040   22.992 -21.074 1.00 68.87  ? 720 HOH   A O   1 
HETATM 3215 O O   . HOH   G 5 .   ? -10.163 20.518 -16.467 1.00 59.12  ? 721 HOH   A O   1 
HETATM 3216 O O   . HOH   G 5 .   ? 3.323   35.059 -24.523 1.00 64.22  ? 722 HOH   A O   1 
HETATM 3217 O O   . HOH   G 5 .   ? -14.109 5.310  -9.160  1.00 43.45  ? 723 HOH   A O   1 
HETATM 3218 O O   . HOH   G 5 .   ? 28.214  18.090 1.778   1.00 54.29  ? 724 HOH   A O   1 
HETATM 3219 O O   . HOH   G 5 .   ? 12.671  44.465 5.883   1.00 46.54  ? 725 HOH   A O   1 
HETATM 3220 O O   . HOH   G 5 .   ? -14.852 21.087 -11.009 1.00 69.26  ? 726 HOH   A O   1 
HETATM 3221 O O   . HOH   G 5 .   ? 10.139  14.069 -4.139  1.00 35.12  ? 727 HOH   A O   1 
HETATM 3222 O O   . HOH   G 5 .   ? -9.370  3.930  7.116   1.00 62.89  ? 728 HOH   A O   1 
HETATM 3223 O O   . HOH   G 5 .   ? 21.977  41.779 1.343   1.00 45.95  ? 729 HOH   A O   1 
HETATM 3224 O O   . HOH   G 5 .   ? -2.102  47.282 8.231   1.00 57.77  ? 730 HOH   A O   1 
HETATM 3225 O O   . HOH   G 5 .   ? 21.927  34.384 -22.440 1.00 51.86  ? 731 HOH   A O   1 
HETATM 3226 O O   . HOH   G 5 .   ? -13.363 1.776  -6.865  1.00 49.72  ? 732 HOH   A O   1 
HETATM 3227 O O   . HOH   G 5 .   ? -4.019  33.277 -12.528 1.00 57.95  ? 733 HOH   A O   1 
HETATM 3228 O O   . HOH   G 5 .   ? 17.189  20.667 -17.553 1.00 62.38  ? 734 HOH   A O   1 
HETATM 3229 O O   . HOH   G 5 .   ? -16.726 16.186 -4.820  1.00 50.70  ? 735 HOH   A O   1 
HETATM 3230 O O   . HOH   G 5 .   ? 14.390  19.387 -10.146 1.00 46.74  ? 736 HOH   A O   1 
HETATM 3231 O O   . HOH   G 5 .   ? -12.803 21.961 -5.674  1.00 55.54  ? 737 HOH   A O   1 
HETATM 3232 O O   . HOH   G 5 .   ? -1.987  1.552  -6.342  1.00 47.03  ? 738 HOH   A O   1 
HETATM 3233 O O   . HOH   G 5 .   ? 4.539   12.057 -15.890 1.00 65.23  ? 739 HOH   A O   1 
HETATM 3234 O O   . HOH   G 5 .   ? -5.656  20.303 -17.410 1.00 43.70  ? 740 HOH   A O   1 
HETATM 3235 O O   . HOH   G 5 .   ? -4.960  17.224 -20.091 1.00 52.79  ? 741 HOH   A O   1 
HETATM 3236 O O   . HOH   G 5 .   ? 0.134   20.082 16.473  1.00 57.38  ? 742 HOH   A O   1 
HETATM 3237 O O   . HOH   G 5 .   ? 18.305  44.245 2.917   1.00 59.56  ? 743 HOH   A O   1 
HETATM 3238 O O   . HOH   G 5 .   ? -9.935  -1.731 -16.269 1.00 58.13  ? 744 HOH   A O   1 
HETATM 3239 O O   . HOH   G 5 .   ? 10.143  23.614 -4.834  1.00 41.07  ? 745 HOH   A O   1 
HETATM 3240 O O   . HOH   G 5 .   ? 3.002   10.144 -15.718 1.00 43.47  ? 746 HOH   A O   1 
HETATM 3241 O O   . HOH   G 5 .   ? 11.856  13.849 5.183   1.00 54.19  ? 747 HOH   A O   1 
HETATM 3242 O O   . HOH   G 5 .   ? 30.373  38.838 0.294   1.00 62.79  ? 748 HOH   A O   1 
HETATM 3243 O O   . HOH   G 5 .   ? 2.550   -2.685 -11.880 1.00 54.40  ? 749 HOH   A O   1 
HETATM 3244 O O   . HOH   G 5 .   ? 18.181  43.660 -1.146  1.00 45.91  ? 750 HOH   A O   1 
HETATM 3245 O O   . HOH   G 5 .   ? -16.973 23.541 3.248   1.00 67.57  ? 751 HOH   A O   1 
HETATM 3246 O O   . HOH   G 5 .   ? -2.716  26.934 -23.675 1.00 69.54  ? 752 HOH   A O   1 
HETATM 3247 O O   . HOH   G 5 .   ? -11.690 -0.119 -7.709  1.00 57.70  ? 753 HOH   A O   1 
HETATM 3248 O O   . HOH   G 5 .   ? 8.123   46.606 4.589   1.00 42.53  ? 754 HOH   A O   1 
HETATM 3249 O O   . HOH   G 5 .   ? 6.784   37.206 -1.956  1.00 44.50  ? 755 HOH   A O   1 
HETATM 3250 O O   . HOH   G 5 .   ? -7.228  3.395  -0.834  1.00 55.83  ? 756 HOH   A O   1 
HETATM 3251 O O   . HOH   G 5 .   ? -11.472 17.571 11.095  1.00 51.40  ? 757 HOH   A O   1 
HETATM 3252 O O   . HOH   G 5 .   ? 3.705   4.235  -17.996 1.00 55.72  ? 758 HOH   A O   1 
HETATM 3253 O O   . HOH   G 5 .   ? 10.551  18.062 -0.987  1.00 42.25  ? 759 HOH   A O   1 
HETATM 3254 O O   . HOH   G 5 .   ? -12.205 5.154  4.813   1.00 51.27  ? 760 HOH   A O   1 
HETATM 3255 O O   . HOH   G 5 .   ? 14.701  28.316 -5.903  1.00 56.45  ? 761 HOH   A O   1 
HETATM 3256 O O   . HOH   G 5 .   ? -4.343  18.568 -28.289 1.00 59.22  ? 762 HOH   A O   1 
HETATM 3257 O O   . HOH   G 5 .   ? -9.786  28.693 -3.333  1.00 52.02  ? 763 HOH   A O   1 
HETATM 3258 O O   . HOH   G 5 .   ? 15.005  43.931 -19.683 1.00 47.80  ? 764 HOH   A O   1 
HETATM 3259 O O   . HOH   G 5 .   ? -2.115  46.405 -18.908 1.00 64.29  ? 765 HOH   A O   1 
HETATM 3260 O O   . HOH   G 5 .   ? 15.191  45.383 -11.368 1.00 61.50  ? 766 HOH   A O   1 
HETATM 3261 O O   . HOH   G 5 .   ? -10.990 -2.470 -18.517 1.00 64.39  ? 767 HOH   A O   1 
HETATM 3262 O O   . HOH   G 5 .   ? 17.189  40.010 3.635   1.00 49.76  ? 768 HOH   A O   1 
HETATM 3263 O O   . HOH   G 5 .   ? -11.228 0.697  -15.262 1.00 60.76  ? 769 HOH   A O   1 
HETATM 3264 O O   . HOH   G 5 .   ? -2.351  31.291 -7.876  1.00 53.42  ? 770 HOH   A O   1 
HETATM 3265 O O   . HOH   G 5 .   ? 14.019  19.910 -7.678  1.00 51.03  ? 771 HOH   A O   1 
HETATM 3266 O O   . HOH   G 5 .   ? -7.177  -2.569 -5.374  1.00 61.36  ? 772 HOH   A O   1 
HETATM 3267 O O   . HOH   G 5 .   ? 9.717   29.060 4.785   1.00 63.69  ? 773 HOH   A O   1 
HETATM 3268 O O   . HOH   G 5 .   ? 11.040  11.103 -15.532 1.00 44.80  ? 774 HOH   A O   1 
HETATM 3269 O O   . HOH   G 5 .   ? 2.738   21.889 16.051  1.00 65.46  ? 775 HOH   A O   1 
HETATM 3270 O O   . HOH   G 5 .   ? 2.037   24.239 -21.853 1.00 65.59  ? 776 HOH   A O   1 
HETATM 3271 O O   . HOH   G 5 .   ? 24.583  41.512 -11.474 1.00 58.87  ? 777 HOH   A O   1 
HETATM 3272 O O   . HOH   G 5 .   ? 32.565  36.475 -1.674  1.00 70.56  ? 778 HOH   A O   1 
HETATM 3273 O O   . HOH   G 5 .   ? -15.775 10.308 -6.850  1.00 61.59  ? 779 HOH   A O   1 
HETATM 3274 O O   . HOH   G 5 .   ? -4.343  6.892  -26.857 1.00 59.02  ? 780 HOH   A O   1 
HETATM 3275 O O   . HOH   G 5 .   ? -2.747  22.137 -35.195 1.00 64.64  ? 781 HOH   A O   1 
HETATM 3276 O O   . HOH   G 5 .   ? -13.843 54.113 0.476   1.00 66.22  ? 782 HOH   A O   1 
HETATM 3277 O O   . HOH   G 5 .   ? 12.414  14.236 -5.161  1.00 58.26  ? 783 HOH   A O   1 
HETATM 3278 O O   . HOH   G 5 .   ? 21.895  37.821 2.561   1.00 52.86  ? 784 HOH   A O   1 
HETATM 3279 O O   . HOH   G 5 .   ? -5.077  32.116 -4.140  1.00 65.25  ? 785 HOH   A O   1 
HETATM 3280 O O   . HOH   G 5 .   ? -3.117  30.891 -21.102 1.00 59.59  ? 786 HOH   A O   1 
HETATM 3281 O O   . HOH   G 5 .   ? 12.573  11.208 2.193   1.00 42.57  ? 787 HOH   A O   1 
HETATM 3282 O O   . HOH   G 5 .   ? 0.161   14.347 -36.912 1.00 67.42  ? 788 HOH   A O   1 
HETATM 3283 O O   . HOH   G 5 .   ? -13.752 4.490  -3.024  1.00 54.81  ? 789 HOH   A O   1 
HETATM 3284 O O   . HOH   G 5 .   ? 4.645   27.334 -27.827 1.00 59.51  ? 790 HOH   A O   1 
HETATM 3285 O O   . HOH   G 5 .   ? -9.388  -3.303 -12.696 1.00 63.81  ? 791 HOH   A O   1 
HETATM 3286 O O   . HOH   G 5 .   ? -11.104 14.725 -28.020 1.00 59.90  ? 792 HOH   A O   1 
HETATM 3287 O O   . HOH   G 5 .   ? 3.564   -4.362 -13.557 1.00 64.69  ? 793 HOH   A O   1 
HETATM 3288 O O   . HOH   G 5 .   ? -15.682 10.774 -17.048 1.00 60.73  ? 794 HOH   A O   1 
HETATM 3289 O O   . HOH   G 5 .   ? 15.662  41.902 2.615   1.00 48.90  ? 795 HOH   A O   1 
HETATM 3290 O O   . HOH   G 5 .   ? -6.274  25.377 -9.432  1.00 52.56  ? 796 HOH   A O   1 
HETATM 3291 O O   . HOH   G 5 .   ? 11.467  23.458 1.105   1.00 69.74  ? 797 HOH   A O   1 
HETATM 3292 O O   . HOH   G 5 .   ? -16.741 10.435 7.793   1.00 64.02  ? 798 HOH   A O   1 
HETATM 3293 O O   . HOH   G 5 .   ? -6.551  32.995 -13.811 1.00 68.89  ? 799 HOH   A O   1 
HETATM 3294 O O   . HOH   G 5 .   ? -1.578  15.932 -38.536 1.00 67.07  ? 800 HOH   A O   1 
HETATM 3295 O O   . HOH   G 5 .   ? -4.745  40.979 1.600   1.00 63.59  ? 801 HOH   A O   1 
HETATM 3296 O O   . HOH   G 5 .   ? 2.566   51.676 5.904   1.00 65.44  ? 802 HOH   A O   1 
HETATM 3297 O O   . HOH   G 5 .   ? 8.884   16.260 -20.836 1.00 67.41  ? 803 HOH   A O   1 
HETATM 3298 O O   . HOH   G 5 .   ? -15.591 7.443  -8.493  1.00 60.79  ? 804 HOH   A O   1 
HETATM 3299 O O   . HOH   G 5 .   ? -12.600 22.917 -10.062 1.00 67.21  ? 805 HOH   A O   1 
HETATM 3300 O O   . HOH   G 5 .   ? 0.509   0.709  -5.072  1.00 54.97  ? 806 HOH   A O   1 
HETATM 3301 O O   . HOH   G 5 .   ? 3.964   8.256  -17.525 1.00 52.77  ? 807 HOH   A O   1 
HETATM 3302 O O   . HOH   G 5 .   ? -17.129 7.749  -15.509 1.00 70.30  ? 808 HOH   A O   1 
HETATM 3303 O O   . HOH   G 5 .   ? -10.820 17.194 13.406  1.00 62.39  ? 809 HOH   A O   1 
HETATM 3304 O O   . HOH   G 5 .   ? 10.305  18.314 -24.548 1.00 68.25  ? 810 HOH   A O   1 
HETATM 3305 O O   . HOH   G 5 .   ? 18.033  45.868 -3.130  1.00 55.58  ? 811 HOH   A O   1 
HETATM 3306 O O   . HOH   G 5 .   ? 9.844   55.837 -2.822  1.00 64.50  ? 812 HOH   A O   1 
HETATM 3307 O O   . HOH   G 5 .   ? -14.368 16.123 -33.639 1.00 48.96  ? 813 HOH   A O   1 
HETATM 3308 O O   . HOH   G 5 .   ? 10.302  12.385 -17.797 1.00 80.40  ? 814 HOH   A O   1 
HETATM 3309 O O   . HOH   G 5 .   ? 25.582  35.759 1.413   1.00 63.31  ? 815 HOH   A O   1 
HETATM 3310 O O   . HOH   G 5 .   ? 2.989   32.306 -28.508 1.00 51.75  ? 816 HOH   A O   1 
HETATM 3311 O O   . HOH   G 5 .   ? -17.149 14.836 -7.148  1.00 68.05  ? 817 HOH   A O   1 
HETATM 3312 O O   . HOH   G 5 .   ? 0.735   57.120 8.020   1.00 56.85  ? 818 HOH   A O   1 
HETATM 3313 O O   . HOH   G 5 .   ? 26.847  43.706 2.067   1.00 57.09  ? 819 HOH   A O   1 
HETATM 3314 O O   . HOH   G 5 .   ? -12.324 27.318 -4.692  1.00 67.60  ? 820 HOH   A O   1 
HETATM 3315 O O   . HOH   G 5 .   ? 7.610   2.160  -17.776 1.00 60.61  ? 821 HOH   A O   1 
HETATM 3316 O O   . HOH   G 5 .   ? 5.180   2.289  -19.245 1.00 63.24  ? 822 HOH   A O   1 
HETATM 3317 O O   . HOH   G 5 .   ? 5.253   0.769  -22.019 1.00 71.51  ? 823 HOH   A O   1 
HETATM 3318 O O   . HOH   G 5 .   ? -11.789 24.354 -6.076  1.00 60.82  ? 824 HOH   A O   1 
HETATM 3319 O O   . HOH   G 5 .   ? 11.273  55.635 -5.215  1.00 71.48  ? 825 HOH   A O   1 
HETATM 3320 O O   . HOH   G 5 .   ? -10.766 -0.763 -10.365 1.00 52.81  ? 826 HOH   A O   1 
HETATM 3321 O O   . HOH   G 5 .   ? 32.503  34.786 -3.545  1.00 62.31  ? 827 HOH   A O   1 
HETATM 3322 O O   . HOH   G 5 .   ? 17.374  25.065 -7.414  1.00 55.84  ? 828 HOH   A O   1 
HETATM 3323 O O   . HOH   G 5 .   ? 13.218  46.254 -13.127 1.00 58.87  ? 829 HOH   A O   1 
HETATM 3324 O O   . HOH   G 5 .   ? 20.798  43.685 -11.163 1.00 60.32  ? 830 HOH   A O   1 
HETATM 3325 O O   . HOH   G 5 .   ? -10.755 16.463 -26.167 1.00 43.85  ? 831 HOH   A O   1 
HETATM 3326 O O   . HOH   G 5 .   ? -7.086  6.297  15.245  1.00 55.61  ? 832 HOH   A O   1 
HETATM 3327 O O   . HOH   G 5 .   ? -14.048 0.833  -4.477  1.00 62.92  ? 833 HOH   A O   1 
HETATM 3328 O O   . HOH   G 5 .   ? -3.724  39.478 -20.906 1.00 65.43  ? 834 HOH   A O   1 
HETATM 3329 O O   . HOH   G 5 .   ? 1.632   26.845 -17.191 1.00 56.22  ? 835 HOH   A O   1 
HETATM 3330 O O   . HOH   G 5 .   ? -6.040  25.344 -26.647 1.00 61.75  ? 836 HOH   A O   1 
HETATM 3331 O O   . HOH   G 5 .   ? 19.125  22.838 -10.745 1.00 62.71  ? 837 HOH   A O   1 
HETATM 3332 O O   . HOH   G 5 .   ? 19.810  43.809 1.014   1.00 52.50  ? 838 HOH   A O   1 
HETATM 3333 O O   . HOH   G 5 .   ? -5.525  19.605 -19.950 1.00 52.38  ? 839 HOH   A O   1 
HETATM 3334 O O   . HOH   G 5 .   ? 25.353  32.878 0.638   1.00 59.29  ? 840 HOH   A O   1 
HETATM 3335 O O   . HOH   G 5 .   ? -9.298  19.141 -23.005 1.00 47.73  ? 841 HOH   A O   1 
HETATM 3336 O O   . HOH   G 5 .   ? -7.357  20.418 -21.315 1.00 49.90  ? 842 HOH   A O   1 
HETATM 3337 O O   . HOH   G 5 .   ? -5.191  22.368 -22.670 1.00 60.26  ? 843 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   . GLY A 1   ? 1.0234 0.8371 0.9409 -0.1473 -0.0610 0.0052  41  GLY A N   
2    C CA  . GLY A 1   ? 1.0770 0.8598 0.9836 -0.1275 -0.0692 0.0066  41  GLY A CA  
3    C C   . GLY A 1   ? 1.0931 0.8999 1.0171 -0.0989 -0.0610 -0.0081 41  GLY A C   
4    O O   . GLY A 1   ? 1.0969 0.9018 1.0352 -0.0829 -0.0615 -0.0219 41  GLY A O   
5    N N   . VAL A 2   ? 1.1028 0.9294 1.0217 -0.0946 -0.0540 -0.0049 42  VAL A N   
6    C CA  . VAL A 2   ? 1.0427 0.8937 0.9762 -0.0710 -0.0462 -0.0175 42  VAL A CA  
7    C C   . VAL A 2   ? 0.9429 0.8358 0.8973 -0.0690 -0.0318 -0.0306 42  VAL A C   
8    O O   . VAL A 2   ? 0.8803 0.7810 0.8509 -0.0498 -0.0308 -0.0433 42  VAL A O   
9    C CB  . VAL A 2   ? 1.0380 0.8956 0.9553 -0.0711 -0.0438 -0.0105 42  VAL A CB  
10   C CG1 . VAL A 2   ? 0.9554 0.8416 0.8867 -0.0511 -0.0341 -0.0240 42  VAL A CG1 
11   C CG2 . VAL A 2   ? 1.0647 0.8818 0.9686 -0.0684 -0.0628 0.0032  42  VAL A CG2 
12   N N   . PRO A 3   ? 0.9400 0.8616 0.8970 -0.0878 -0.0204 -0.0273 43  PRO A N   
13   C CA  . PRO A 3   ? 0.9525 0.9136 0.9373 -0.0848 -0.0102 -0.0378 43  PRO A CA  
14   C C   . PRO A 3   ? 0.8807 0.8287 0.8773 -0.0825 -0.0218 -0.0440 43  PRO A C   
15   O O   . PRO A 3   ? 0.7632 0.7342 0.7800 -0.0714 -0.0190 -0.0545 43  PRO A O   
16   C CB  . PRO A 3   ? 1.0133 1.0033 1.0013 -0.1087 0.0025  -0.0292 43  PRO A CB  
17   C CG  . PRO A 3   ? 1.0322 1.0074 0.9893 -0.1175 0.0064  -0.0194 43  PRO A CG  
18   C CD  . PRO A 3   ? 1.0017 0.9268 0.9386 -0.1113 -0.0140 -0.0138 43  PRO A CD  
19   N N   . GLY A 4   ? 0.8550 0.7628 0.8362 -0.0934 -0.0354 -0.0378 44  GLY A N   
20   C CA  . GLY A 4   ? 0.7617 0.6484 0.7453 -0.0920 -0.0461 -0.0456 44  GLY A CA  
21   C C   . GLY A 4   ? 0.7195 0.5897 0.7028 -0.0652 -0.0477 -0.0587 44  GLY A C   
22   O O   . GLY A 4   ? 0.6939 0.5685 0.6840 -0.0592 -0.0491 -0.0695 44  GLY A O   
23   N N   . GLN A 5   ? 0.7355 0.5875 0.7112 -0.0503 -0.0480 -0.0567 45  GLN A N   
24   C CA  . GLN A 5   ? 0.7600 0.6019 0.7404 -0.0250 -0.0472 -0.0676 45  GLN A CA  
25   C C   . GLN A 5   ? 0.6815 0.5644 0.6781 -0.0135 -0.0373 -0.0766 45  GLN A C   
26   O O   . GLN A 5   ? 0.6419 0.5243 0.6429 -0.0020 -0.0364 -0.0879 45  GLN A O   
27   C CB  . GLN A 5   ? 0.8684 0.6890 0.8443 -0.0133 -0.0513 -0.0600 45  GLN A CB  
28   C CG  . GLN A 5   ? 1.0332 0.8038 0.9973 -0.0157 -0.0629 -0.0540 45  GLN A CG  
29   C CD  . GLN A 5   ? 1.1375 0.8914 1.0995 -0.0105 -0.0709 -0.0401 45  GLN A CD  
30   O OE1 . GLN A 5   ? 1.1646 0.9376 1.1206 -0.0204 -0.0707 -0.0294 45  GLN A OE1 
31   N NE2 . GLN A 5   ? 1.1701 0.8871 1.1368 0.0050  -0.0782 -0.0399 45  GLN A NE2 
32   N N   . VAL A 6   ? 0.6023 0.5179 0.6049 -0.0172 -0.0294 -0.0720 46  VAL A N   
33   C CA  . VAL A 6   ? 0.5535 0.5047 0.5717 -0.0062 -0.0204 -0.0802 46  VAL A CA  
34   C C   . VAL A 6   ? 0.5512 0.5201 0.5832 -0.0111 -0.0211 -0.0864 46  VAL A C   
35   O O   . VAL A 6   ? 0.5128 0.4914 0.5533 0.0015  -0.0206 -0.0952 46  VAL A O   
36   C CB  . VAL A 6   ? 0.5677 0.5453 0.5859 -0.0110 -0.0099 -0.0753 46  VAL A CB  
37   C CG1 . VAL A 6   ? 0.5594 0.5699 0.5948 0.0005  -0.0007 -0.0844 46  VAL A CG1 
38   C CG2 . VAL A 6   ? 0.5729 0.5314 0.5737 -0.0067 -0.0128 -0.0688 46  VAL A CG2 
39   N N   . ASP A 7   ? 0.5389 0.5120 0.5735 -0.0313 -0.0242 -0.0803 47  ASP A N   
40   C CA  . ASP A 7   ? 0.5762 0.5689 0.6271 -0.0389 -0.0285 -0.0834 47  ASP A CA  
41   C C   . ASP A 7   ? 0.5490 0.5102 0.5861 -0.0344 -0.0394 -0.0919 47  ASP A C   
42   O O   . ASP A 7   ? 0.5433 0.5188 0.5895 -0.0313 -0.0430 -0.0976 47  ASP A O   
43   C CB  . ASP A 7   ? 0.6721 0.6762 0.7303 -0.0644 -0.0309 -0.0729 47  ASP A CB  
44   C CG  . ASP A 7   ? 0.8696 0.9141 0.9456 -0.0696 -0.0156 -0.0663 47  ASP A CG  
45   O OD1 . ASP A 7   ? 0.9218 0.9926 1.0114 -0.0535 -0.0047 -0.0721 47  ASP A OD1 
46   O OD2 . ASP A 7   ? 0.9456 0.9933 1.0196 -0.0903 -0.0135 -0.0557 47  ASP A OD2 
47   N N   . PHE A 8   ? 0.5180 0.4343 0.5316 -0.0340 -0.0445 -0.0930 48  PHE A N   
48   C CA  . PHE A 8   ? 0.5998 0.4814 0.5953 -0.0290 -0.0508 -0.1035 48  PHE A CA  
49   C C   . PHE A 8   ? 0.5857 0.4773 0.5848 -0.0078 -0.0443 -0.1133 48  PHE A C   
50   O O   . PHE A 8   ? 0.5156 0.4065 0.5091 -0.0082 -0.0481 -0.1207 48  PHE A O   
51   C CB  . PHE A 8   ? 0.5908 0.4217 0.5645 -0.0275 -0.0540 -0.1038 48  PHE A CB  
52   C CG  . PHE A 8   ? 0.6992 0.4888 0.6501 -0.0217 -0.0565 -0.1169 48  PHE A CG  
53   C CD1 . PHE A 8   ? 0.7595 0.5207 0.6898 -0.0409 -0.0673 -0.1198 48  PHE A CD1 
54   C CD2 . PHE A 8   ? 0.6889 0.4667 0.6373 0.0015  -0.0474 -0.1265 48  PHE A CD2 
55   C CE1 . PHE A 8   ? 0.7490 0.4664 0.6507 -0.0367 -0.0679 -0.1339 48  PHE A CE1 
56   C CE2 . PHE A 8   ? 0.6809 0.4199 0.6056 0.0068  -0.0455 -0.1402 48  PHE A CE2 
57   C CZ  . PHE A 8   ? 0.7070 0.4132 0.6052 -0.0122 -0.0553 -0.1448 48  PHE A CZ  
58   N N   . TYR A 9   ? 0.5670 0.4672 0.5737 0.0086  -0.0359 -0.1122 49  TYR A N   
59   C CA  . TYR A 9   ? 0.5092 0.4157 0.5186 0.0272  -0.0301 -0.1203 49  TYR A CA  
60   C C   . TYR A 9   ? 0.4458 0.3922 0.4723 0.0293  -0.0280 -0.1205 49  TYR A C   
61   O O   . TYR A 9   ? 0.4860 0.4360 0.5113 0.0383  -0.0271 -0.1271 49  TYR A O   
62   C CB  . TYR A 9   ? 0.5094 0.4073 0.5217 0.0426  -0.0247 -0.1178 49  TYR A CB  
63   C CG  . TYR A 9   ? 0.6307 0.4864 0.6303 0.0465  -0.0263 -0.1201 49  TYR A CG  
64   C CD1 . TYR A 9   ? 0.6460 0.4799 0.6356 0.0566  -0.0215 -0.1318 49  TYR A CD1 
65   C CD2 . TYR A 9   ? 0.6801 0.5147 0.6756 0.0394  -0.0318 -0.1110 49  TYR A CD2 
66   C CE1 . TYR A 9   ? 0.6849 0.4774 0.6636 0.0624  -0.0202 -0.1360 49  TYR A CE1 
67   C CE2 . TYR A 9   ? 0.6672 0.4590 0.6528 0.0447  -0.0339 -0.1134 49  TYR A CE2 
68   C CZ  . TYR A 9   ? 0.7327 0.5038 0.7114 0.0575  -0.0271 -0.1268 49  TYR A CZ  
69   O OH  . TYR A 9   ? 0.8767 0.6030 0.8467 0.0654  -0.0263 -0.1311 49  TYR A OH  
70   N N   . ALA A 10  ? 0.4270 0.4021 0.4692 0.0210  -0.0265 -0.1134 50  ALA A N   
71   C CA  . ALA A 10  ? 0.4015 0.4127 0.4639 0.0249  -0.0241 -0.1141 50  ALA A CA  
72   C C   . ALA A 10  ? 0.4334 0.4517 0.5014 0.0161  -0.0341 -0.1156 50  ALA A C   
73   O O   . ALA A 10  ? 0.4260 0.4690 0.5108 0.0218  -0.0353 -0.1163 50  ALA A O   
74   C CB  . ALA A 10  ? 0.3925 0.4323 0.4713 0.0195  -0.0162 -0.1076 50  ALA A CB  
75   N N   . ARG A 11  ? 0.4623 0.4571 0.5155 0.0014  -0.0433 -0.1153 51  ARG A N   
76   C CA  . ARG A 11  ? 0.4488 0.4445 0.5006 -0.0092 -0.0564 -0.1163 51  ARG A CA  
77   C C   . ARG A 11  ? 0.4721 0.4533 0.5068 0.0023  -0.0577 -0.1248 51  ARG A C   
78   O O   . ARG A 11  ? 0.4992 0.4932 0.5392 -0.0014 -0.0677 -0.1238 51  ARG A O   
79   C CB  . ARG A 11  ? 0.4872 0.4518 0.5183 -0.0292 -0.0669 -0.1153 51  ARG A CB  
80   C CG  . ARG A 11  ? 0.6301 0.5967 0.6591 -0.0460 -0.0844 -0.1137 51  ARG A CG  
81   C CD  . ARG A 11  ? 0.7649 0.6919 0.7656 -0.0678 -0.0963 -0.1141 51  ARG A CD  
82   N NE  . ARG A 11  ? 0.7896 0.6620 0.7465 -0.0613 -0.0930 -0.1272 51  ARG A NE  
83   C CZ  . ARG A 11  ? 0.7688 0.6177 0.6968 -0.0608 -0.0976 -0.1366 51  ARG A CZ  
84   N NH1 . ARG A 11  ? 0.6882 0.4881 0.5780 -0.0536 -0.0896 -0.1497 51  ARG A NH1 
85   N NH2 . ARG A 11  ? 0.7693 0.6429 0.7064 -0.0671 -0.1096 -0.1327 51  ARG A NH2 
86   N N   . PHE A 12  ? 0.4551 0.4117 0.4714 0.0157  -0.0481 -0.1317 52  PHE A N   
87   C CA  . PHE A 12  ? 0.4701 0.4126 0.4683 0.0245  -0.0466 -0.1396 52  PHE A CA  
88   C C   . PHE A 12  ? 0.4587 0.4310 0.4762 0.0375  -0.0429 -0.1375 52  PHE A C   
89   O O   . PHE A 12  ? 0.4017 0.3987 0.4424 0.0442  -0.0375 -0.1328 52  PHE A O   
90   C CB  . PHE A 12  ? 0.4743 0.3827 0.4515 0.0346  -0.0357 -0.1473 52  PHE A CB  
91   C CG  . PHE A 12  ? 0.5162 0.3858 0.4688 0.0235  -0.0393 -0.1518 52  PHE A CG  
92   C CD1 . PHE A 12  ? 0.5534 0.3948 0.4741 0.0131  -0.0451 -0.1598 52  PHE A CD1 
93   C CD2 . PHE A 12  ? 0.5621 0.4196 0.5194 0.0212  -0.0383 -0.1476 52  PHE A CD2 
94   C CE1 . PHE A 12  ? 0.6712 0.4708 0.5645 0.0017  -0.0490 -0.1654 52  PHE A CE1 
95   C CE2 . PHE A 12  ? 0.5882 0.4045 0.5211 0.0104  -0.0430 -0.1516 52  PHE A CE2 
96   C CZ  . PHE A 12  ? 0.6597 0.4463 0.5605 0.0010  -0.0479 -0.1614 52  PHE A CZ  
97   N N   . SER A 13  ? 0.4909 0.4571 0.4943 0.0396  -0.0460 -0.1413 53  SER A N   
98   C CA  . SER A 13  ? 0.4875 0.4752 0.5057 0.0519  -0.0430 -0.1393 53  SER A CA  
99   C C   . SER A 13  ? 0.4736 0.4486 0.4818 0.0649  -0.0298 -0.1441 53  SER A C   
100  O O   . SER A 13  ? 0.5175 0.4657 0.5027 0.0646  -0.0240 -0.1507 53  SER A O   
101  C CB  . SER A 13  ? 0.5788 0.5695 0.5901 0.0463  -0.0554 -0.1376 53  SER A CB  
102  O OG  . SER A 13  ? 0.6808 0.6843 0.7009 0.0581  -0.0526 -0.1360 53  SER A OG  
103  N N   . PRO A 14  ? 0.4688 0.4619 0.4945 0.0761  -0.0245 -0.1411 54  PRO A N   
104  C CA  . PRO A 14  ? 0.5027 0.4889 0.5231 0.0864  -0.0150 -0.1434 54  PRO A CA  
105  C C   . PRO A 14  ? 0.5341 0.5083 0.5332 0.0839  -0.0149 -0.1473 54  PRO A C   
106  O O   . PRO A 14  ? 0.5479 0.5244 0.5398 0.0762  -0.0256 -0.1457 54  PRO A O   
107  C CB  . PRO A 14  ? 0.4419 0.4496 0.4815 0.0939  -0.0149 -0.1385 54  PRO A CB  
108  C CG  . PRO A 14  ? 0.4489 0.4702 0.5029 0.0901  -0.0177 -0.1354 54  PRO A CG  
109  C CD  . PRO A 14  ? 0.4162 0.4352 0.4665 0.0790  -0.0257 -0.1359 54  PRO A CD  
110  N N   . SER A 15  ? 0.4964 0.4577 0.4857 0.0898  -0.0028 -0.1516 55  SER A N   
111  C CA  A SER A 15  ? 0.5210 0.4693 0.4855 0.0866  0.0020  -0.1560 55  SER A CA  
112  C CA  B SER A 15  ? 0.5181 0.4666 0.4827 0.0866  0.0019  -0.1559 55  SER A CA  
113  C C   . SER A 15  ? 0.5433 0.5071 0.5188 0.0937  0.0075  -0.1515 55  SER A C   
114  O O   . SER A 15  ? 0.5455 0.5129 0.5342 0.1028  0.0195  -0.1515 55  SER A O   
115  C CB  A SER A 15  ? 0.5486 0.4694 0.4925 0.0875  0.0156  -0.1658 55  SER A CB  
116  C CB  B SER A 15  ? 0.5518 0.4726 0.4952 0.0872  0.0153  -0.1658 55  SER A CB  
117  O OG  A SER A 15  ? 0.5400 0.4460 0.4539 0.0828  0.0236  -0.1715 55  SER A OG  
118  O OG  B SER A 15  ? 0.5640 0.4650 0.4910 0.0771  0.0074  -0.1698 55  SER A OG  
119  N N   . PRO A 16  ? 0.5001 0.4728 0.4729 0.0895  -0.0022 -0.1464 56  PRO A N   
120  C CA  . PRO A 16  ? 0.4966 0.4813 0.4787 0.0940  0.0011  -0.1411 56  PRO A CA  
121  C C   . PRO A 16  ? 0.5462 0.5222 0.5115 0.0927  0.0163  -0.1442 56  PRO A C   
122  O O   . PRO A 16  ? 0.5512 0.5085 0.4864 0.0851  0.0206  -0.1503 56  PRO A O   
123  C CB  . PRO A 16  ? 0.4972 0.4862 0.4760 0.0886  -0.0148 -0.1352 56  PRO A CB  
124  C CG  . PRO A 16  ? 0.5447 0.5297 0.5194 0.0824  -0.0266 -0.1364 56  PRO A CG  
125  C CD  . PRO A 16  ? 0.4994 0.4685 0.4589 0.0790  -0.0180 -0.1442 56  PRO A CD  
126  N N   . LEU A 17  ? 0.5056 0.4955 0.4897 0.0990  0.0247  -0.1399 57  LEU A N   
127  C CA  . LEU A 17  ? 0.5197 0.5092 0.4961 0.0982  0.0416  -0.1410 57  LEU A CA  
128  C C   . LEU A 17  ? 0.5444 0.5434 0.5185 0.0914  0.0359  -0.1319 57  LEU A C   
129  O O   . LEU A 17  ? 0.5299 0.5385 0.5196 0.0925  0.0218  -0.1248 57  LEU A O   
130  C CB  . LEU A 17  ? 0.5412 0.5427 0.5479 0.1100  0.0562  -0.1409 57  LEU A CB  
131  C CG  . LEU A 17  ? 0.5991 0.5876 0.6099 0.1180  0.0629  -0.1489 57  LEU A CG  
132  C CD1 . LEU A 17  ? 0.6589 0.6622 0.7075 0.1307  0.0722  -0.1446 57  LEU A CD1 
133  C CD2 . LEU A 17  ? 0.5919 0.5548 0.5683 0.1141  0.0768  -0.1610 57  LEU A CD2 
134  N N   . SER A 18  ? 0.5402 0.5333 0.4918 0.0836  0.0475  -0.1325 58  SER A N   
135  C CA  . SER A 18  ? 0.5547 0.5568 0.5059 0.0759  0.0437  -0.1222 58  SER A CA  
136  C C   . SER A 18  ? 0.5774 0.6029 0.5624 0.0817  0.0566  -0.1168 58  SER A C   
137  O O   . SER A 18  ? 0.5451 0.5787 0.5500 0.0916  0.0726  -0.1216 58  SER A O   
138  C CB  . SER A 18  ? 0.5676 0.5542 0.4776 0.0616  0.0503  -0.1227 58  SER A CB  
139  O OG  . SER A 18  ? 0.6546 0.6430 0.5602 0.0633  0.0780  -0.1296 58  SER A OG  
140  N N   . MET A 19  ? 0.6203 0.6559 0.6135 0.0751  0.0476  -0.1055 59  MET A N   
141  C CA  . MET A 19  ? 0.5932 0.6528 0.6179 0.0761  0.0574  -0.0975 59  MET A CA  
142  C C   . MET A 19  ? 0.5859 0.6540 0.6090 0.0749  0.0853  -0.1009 59  MET A C   
143  O O   . MET A 19  ? 0.6127 0.7029 0.6721 0.0834  0.0999  -0.0991 59  MET A O   
144  C CB  . MET A 19  ? 0.6467 0.7091 0.6707 0.0646  0.0423  -0.0849 59  MET A CB  
145  C CG  . MET A 19  ? 0.6124 0.7009 0.6705 0.0621  0.0478  -0.0741 59  MET A CG  
146  S SD  . MET A 19  ? 0.6767 0.7711 0.7642 0.0684  0.0267  -0.0689 59  MET A SD  
147  C CE  . MET A 19  ? 0.6230 0.6901 0.6798 0.0601  0.0021  -0.0668 59  MET A CE  
148  N N   . LYS A 20  ? 0.6403 0.6903 0.6215 0.0644  0.0933  -0.1055 60  LYS A N   
149  C CA  . LYS A 20  ? 0.7241 0.7776 0.6955 0.0626  0.1240  -0.1114 60  LYS A CA  
150  C C   . LYS A 20  ? 0.6843 0.7349 0.6694 0.0795  0.1417  -0.1251 60  LYS A C   
151  O O   . LYS A 20  ? 0.6716 0.7397 0.6826 0.0879  0.1675  -0.1275 60  LYS A O   
152  C CB  . LYS A 20  ? 0.8422 0.8689 0.7546 0.0456  0.1261  -0.1146 60  LYS A CB  
153  C CG  . LYS A 20  ? 0.8578 0.8814 0.7479 0.0419  0.1611  -0.1236 60  LYS A CG  
154  C CD  . LYS A 20  ? 0.9257 0.9709 0.8211 0.0289  0.1755  -0.1117 60  LYS A CD  
155  C CE  . LYS A 20  ? 1.0294 1.0731 0.9024 0.0257  0.2154  -0.1220 60  LYS A CE  
156  N NZ  . LYS A 20  ? 1.0498 1.0503 0.8576 0.0192  0.2191  -0.1375 60  LYS A NZ  
157  N N   . GLN A 21  ? 0.6728 0.7016 0.6437 0.0849  0.1281  -0.1335 61  GLN A N   
158  C CA  . GLN A 21  ? 0.6001 0.6203 0.5815 0.0998  0.1417  -0.1458 61  GLN A CA  
159  C C   . GLN A 21  ? 0.5873 0.6351 0.6275 0.1155  0.1440  -0.1392 61  GLN A C   
160  O O   . GLN A 21  ? 0.6345 0.6889 0.6981 0.1283  0.1665  -0.1446 61  GLN A O   
161  C CB  . GLN A 21  ? 0.6278 0.6215 0.5849 0.0990  0.1227  -0.1528 61  GLN A CB  
162  C CG  . GLN A 21  ? 0.7641 0.7275 0.6636 0.0837  0.1199  -0.1599 61  GLN A CG  
163  C CD  . GLN A 21  ? 0.8349 0.7787 0.7192 0.0814  0.0980  -0.1636 61  GLN A CD  
164  O OE1 . GLN A 21  ? 0.7669 0.7209 0.6670 0.0806  0.0749  -0.1549 61  GLN A OE1 
165  N NE2 . GLN A 21  ? 0.8775 0.7925 0.7313 0.0799  0.1060  -0.1769 61  GLN A NE2 
166  N N   . PHE A 22  ? 0.5325 0.5946 0.5964 0.1148  0.1202  -0.1274 62  PHE A N   
167  C CA  . PHE A 22  ? 0.5138 0.6022 0.6300 0.1251  0.1174  -0.1177 62  PHE A CA  
168  C C   . PHE A 22  ? 0.5753 0.6921 0.7233 0.1270  0.1391  -0.1115 62  PHE A C   
169  O O   . PHE A 22  ? 0.6298 0.7629 0.8193 0.1412  0.1517  -0.1103 62  PHE A O   
170  C CB  . PHE A 22  ? 0.4342 0.5304 0.5585 0.1181  0.0900  -0.1058 62  PHE A CB  
171  C CG  . PHE A 22  ? 0.4595 0.5398 0.5761 0.1218  0.0713  -0.1090 62  PHE A CG  
172  C CD1 . PHE A 22  ? 0.4887 0.5703 0.6297 0.1332  0.0700  -0.1091 62  PHE A CD1 
173  C CD2 . PHE A 22  ? 0.4603 0.5261 0.5485 0.1135  0.0545  -0.1102 62  PHE A CD2 
174  C CE1 . PHE A 22  ? 0.4614 0.5295 0.5933 0.1341  0.0541  -0.1109 62  PHE A CE1 
175  C CE2 . PHE A 22  ? 0.4740 0.5296 0.5586 0.1165  0.0403  -0.1128 62  PHE A CE2 
176  C CZ  . PHE A 22  ? 0.5035 0.5604 0.6079 0.1256  0.0409  -0.1133 62  PHE A CZ  
177  N N   . LEU A 23  ? 0.5824 0.7064 0.7136 0.1123  0.1435  -0.1062 63  LEU A N   
178  C CA  . LEU A 23  ? 0.6571 0.8133 0.8205 0.1102  0.1636  -0.0976 63  LEU A CA  
179  C C   . LEU A 23  ? 0.7945 0.9492 0.9564 0.1200  0.2002  -0.1107 63  LEU A C   
180  O O   . LEU A 23  ? 0.8060 0.9889 1.0184 0.1328  0.2192  -0.1075 63  LEU A O   
181  C CB  . LEU A 23  ? 0.6327 0.7914 0.7711 0.0889  0.1568  -0.0880 63  LEU A CB  
182  C CG  . LEU A 23  ? 0.6753 0.8707 0.8482 0.0797  0.1675  -0.0729 63  LEU A CG  
183  C CD1 . LEU A 23  ? 0.6421 0.8640 0.8684 0.0833  0.1476  -0.0580 63  LEU A CD1 
184  C CD2 . LEU A 23  ? 0.7354 0.9197 0.8677 0.0567  0.1592  -0.0656 63  LEU A CD2 
185  N N   . ASP A 24  ? 0.8742 0.9949 0.9783 0.1141  0.2105  -0.1255 64  ASP A N   
186  C CA  . ASP A 24  ? 0.9215 1.0326 1.0124 0.1217  0.2472  -0.1409 64  ASP A CA  
187  C C   . ASP A 24  ? 0.9752 1.0851 1.1035 0.1462  0.2576  -0.1493 64  ASP A C   
188  O O   . ASP A 24  ? 1.0987 1.2173 1.2478 0.1589  0.2903  -0.1569 64  ASP A O   
189  C CB  . ASP A 24  ? 0.9543 1.0209 0.9686 0.1087  0.2494  -0.1552 64  ASP A CB  
190  C CG  . ASP A 24  ? 1.0277 1.0939 1.0024 0.0850  0.2505  -0.1481 64  ASP A CG  
191  O OD1 . ASP A 24  ? 1.0057 1.1056 1.0124 0.0783  0.2499  -0.1322 64  ASP A OD1 
192  O OD2 . ASP A 24  ? 1.0753 1.1057 0.9854 0.0713  0.2502  -0.1571 64  ASP A OD2 
193  N N   . PHE A 25  ? 0.9785 1.0770 1.1163 0.1531  0.2304  -0.1476 65  PHE A N   
194  C CA  . PHE A 25  ? 1.0740 1.1661 1.2436 0.1747  0.2361  -0.1537 65  PHE A CA  
195  C C   . PHE A 25  ? 1.1516 1.2863 1.3898 0.1871  0.2402  -0.1383 65  PHE A C   
196  O O   . PHE A 25  ? 1.2527 1.3925 1.5046 0.1985  0.2577  -0.1413 65  PHE A O   
197  C CB  . PHE A 25  ? 1.0902 1.1631 1.2526 0.1751  0.2039  -0.1518 65  PHE A CB  
198  C CG  . PHE A 25  ? 1.2308 1.2953 1.4167 0.1919  0.1981  -0.1504 65  PHE A CG  
199  C CD1 . PHE A 25  ? 1.3748 1.4104 1.5339 0.1992  0.2106  -0.1629 65  PHE A CD1 
200  C CD2 . PHE A 25  ? 1.2421 1.3250 1.4727 0.1984  0.1775  -0.1356 65  PHE A CD2 
201  C CE1 . PHE A 25  ? 1.3986 1.4239 1.5777 0.2138  0.2035  -0.1613 65  PHE A CE1 
202  C CE2 . PHE A 25  ? 1.3049 1.3771 1.5521 0.2117  0.1702  -0.1323 65  PHE A CE2 
203  C CZ  . PHE A 25  ? 1.3569 1.4003 1.5797 0.2200  0.1836  -0.1453 65  PHE A CZ  
204  N N   . GLY A 26  ? 1.0841 1.2494 1.3649 0.1837  0.2212  -0.1214 66  GLY A N   
205  C CA  . GLY A 26  ? 1.0682 1.2737 1.4177 0.1938  0.2191  -0.1046 66  GLY A CA  
206  C C   . GLY A 26  ? 1.0895 1.3352 1.4720 0.1903  0.2426  -0.0966 66  GLY A C   
207  O O   . GLY A 26  ? 1.0654 1.3484 1.5073 0.1959  0.2370  -0.0804 66  GLY A O   
208  N N   . SER A 27  ? 1.1580 1.3977 1.5029 0.1793  0.2682  -0.1066 67  SER A N   
209  C CA  . SER A 27  ? 1.2193 1.5000 1.5944 0.1723  0.2916  -0.0972 67  SER A CA  
210  C C   . SER A 27  ? 1.3698 1.6598 1.7611 0.1869  0.3153  -0.1032 67  SER A C   
211  O O   . SER A 27  ? 1.3638 1.6945 1.8182 0.1948  0.3158  -0.0895 67  SER A O   
212  C CB  . SER A 27  ? 1.1824 1.4483 1.4957 0.1484  0.3002  -0.1015 67  SER A CB  
213  O OG  . SER A 27  ? 1.1035 1.3674 1.4000 0.1292  0.2628  -0.0873 67  SER A OG  
214  N N   . VAL A 28  ? 1.4962 1.7483 1.8317 0.1901  0.3343  -0.1236 68  VAL A N   
215  C CA  . VAL A 28  ? 1.6418 1.8998 1.9878 0.2034  0.3612  -0.1322 68  VAL A CA  
216  C C   . VAL A 28  ? 1.7474 1.9743 2.0917 0.2237  0.3513  -0.1426 68  VAL A C   
217  O O   . VAL A 28  ? 1.6791 1.9281 2.0796 0.2407  0.3478  -0.1351 68  VAL A O   
218  C CB  . VAL A 28  ? 1.6608 1.8984 1.9448 0.1911  0.3924  -0.1475 68  VAL A CB  
219  C CG1 . VAL A 28  ? 1.6763 1.9181 1.9710 0.2065  0.4218  -0.1584 68  VAL A CG1 
220  C CG2 . VAL A 28  ? 1.6294 1.8974 1.9138 0.1687  0.4032  -0.1353 68  VAL A CG2 
221  N N   . ASN A 29  ? 1.9026 2.0775 2.1822 0.2206  0.3459  -0.1590 69  ASN A N   
222  C CA  . ASN A 29  ? 1.9654 2.1055 2.2360 0.2368  0.3375  -0.1697 69  ASN A CA  
223  C C   . ASN A 29  ? 1.8920 2.0465 2.2154 0.2483  0.3089  -0.1543 69  ASN A C   
224  O O   . ASN A 29  ? 1.9175 2.0852 2.2865 0.2662  0.3111  -0.1505 69  ASN A O   
225  C CB  . ASN A 29  ? 2.0327 2.1183 2.2280 0.2260  0.3290  -0.1854 69  ASN A CB  
226  C CG  . ASN A 29  ? 2.1071 2.1705 2.2430 0.2140  0.3554  -0.2013 69  ASN A CG  
227  O OD1 . ASN A 29  ? 2.1275 2.2186 2.2712 0.2079  0.3787  -0.1981 69  ASN A OD1 
228  N ND2 . ASN A 29  ? 2.1447 2.1575 2.2193 0.2087  0.3513  -0.2175 69  ASN A ND2 
229  N N   . ALA A 30  ? 1.7695 1.9209 2.0864 0.2377  0.2819  -0.1451 70  ALA A N   
230  C CA  . ALA A 30  ? 1.6110 1.7722 1.9685 0.2444  0.2526  -0.1297 70  ALA A CA  
231  C C   . ALA A 30  ? 1.4836 1.6142 1.8399 0.2611  0.2468  -0.1364 70  ALA A C   
232  O O   . ALA A 30  ? 1.5390 1.6866 1.9452 0.2756  0.2418  -0.1263 70  ALA A O   
233  C CB  . ALA A 30  ? 1.6149 1.8298 2.0427 0.2466  0.2496  -0.1091 70  ALA A CB  
234  N N   . CYS A 31  ? 1.2182 1.3020 1.5165 0.2580  0.2470  -0.1531 71  CYS A N   
235  C CA  . CYS A 31  ? 1.0167 1.0648 1.3059 0.2717  0.2433  -0.1618 71  CYS A CA  
236  C C   . CYS A 31  ? 0.8345 0.8681 1.1264 0.2700  0.2122  -0.1513 71  CYS A C   
237  O O   . CYS A 31  ? 0.7593 0.7731 1.0123 0.2560  0.1992  -0.1541 71  CYS A O   
238  C CB  . CYS A 31  ? 1.0554 1.0590 1.2810 0.2669  0.2581  -0.1847 71  CYS A CB  
239  S SG  . CYS A 31  ? 1.1539 1.1123 1.3716 0.2845  0.2574  -0.1972 71  CYS A SG  
240  N N   . GLU A 32  ? 0.7308 0.8974 1.0370 0.2405  0.2297  -0.2100 72  GLU A N   
241  C CA  . GLU A 32  ? 0.6496 0.8034 0.9715 0.2402  0.1952  -0.1970 72  GLU A CA  
242  C C   . GLU A 32  ? 0.7220 0.8072 0.9959 0.2442  0.1809  -0.2040 72  GLU A C   
243  O O   . GLU A 32  ? 0.7073 0.7688 0.9611 0.2300  0.1539  -0.1903 72  GLU A O   
244  C CB  . GLU A 32  ? 0.5822 0.7749 0.9742 0.2624  0.1836  -0.1878 72  GLU A CB  
245  C CG  . GLU A 32  ? 0.5877 0.7761 0.9927 0.2594  0.1465  -0.1668 72  GLU A CG  
246  C CD  . GLU A 32  ? 0.6287 0.8569 1.0993 0.2856  0.1336  -0.1570 72  GLU A CD  
247  O OE1 . GLU A 32  ? 0.6605 0.9150 1.1559 0.3022  0.1512  -0.1615 72  GLU A OE1 
248  O OE2 . GLU A 32  ? 0.6338 0.8631 1.1153 0.2858  0.1034  -0.1383 72  GLU A OE2 
249  N N   . LYS A 33  ? 0.6919 0.7447 0.9443 0.2608  0.1985  -0.2244 73  LYS A N   
250  C CA  . LYS A 33  ? 0.7422 0.7296 0.9481 0.2605  0.1875  -0.2363 73  LYS A CA  
251  C C   . LYS A 33  ? 0.7865 0.7550 0.9330 0.2328  0.1803  -0.2376 73  LYS A C   
252  O O   . LYS A 33  ? 0.7835 0.7182 0.9064 0.2204  0.1559  -0.2324 73  LYS A O   
253  C CB  . LYS A 33  ? 0.7523 0.7096 0.9328 0.2780  0.2062  -0.2542 73  LYS A CB  
254  C CG  . LYS A 33  ? 0.8486 0.8090 1.0739 0.3078  0.2082  -0.2507 73  LYS A CG  
255  C CD  . LYS A 33  ? 0.9732 0.8948 1.1640 0.3239  0.2254  -0.2725 73  LYS A CD  
256  C CE  . LYS A 33  ? 1.1154 1.0575 1.3507 0.3564  0.2369  -0.2716 73  LYS A CE  
257  N NZ  . LYS A 33  ? 1.1754 1.0859 1.4379 0.3763  0.2184  -0.2608 73  LYS A NZ  
258  N N   . THR A 34  ? 0.7976 0.7879 0.9175 0.2226  0.2013  -0.2421 74  THR A N   
259  C CA  . THR A 34  ? 0.7982 0.7729 0.8581 0.1995  0.1938  -0.2393 74  THR A CA  
260  C C   . THR A 34  ? 0.7695 0.7547 0.8385 0.1802  0.1661  -0.2142 74  THR A C   
261  O O   . THR A 34  ? 0.7187 0.6773 0.7507 0.1664  0.1460  -0.2123 74  THR A O   
262  C CB  . THR A 34  ? 0.8120 0.8093 0.8454 0.1944  0.2238  -0.2426 74  THR A CB  
263  O OG1 . THR A 34  ? 0.9054 0.8933 0.9229 0.2113  0.2457  -0.2601 74  THR A OG1 
264  C CG2 . THR A 34  ? 0.7897 0.7673 0.7564 0.1755  0.2154  -0.2386 74  THR A CG2 
265  N N   . SER A 35  ? 0.6944 0.7216 0.8135 0.1786  0.1648  -0.1967 75  SER A N   
266  C CA  . SER A 35  ? 0.6315 0.6692 0.7590 0.1609  0.1397  -0.1749 75  SER A CA  
267  C C   . SER A 35  ? 0.5972 0.6039 0.7277 0.1632  0.1120  -0.1702 75  SER A C   
268  O O   . SER A 35  ? 0.5511 0.5432 0.6578 0.1464  0.0924  -0.1609 75  SER A O   
269  C CB  . SER A 35  ? 0.6557 0.7458 0.8387 0.1597  0.1430  -0.1614 75  SER A CB  
270  O OG  . SER A 35  ? 0.6267 0.7266 0.8116 0.1410  0.1214  -0.1431 75  SER A OG  
271  N N   . PHE A 36  ? 0.6375 0.6324 0.7975 0.1844  0.1120  -0.1762 76  PHE A N   
272  C CA  . PHE A 36  ? 0.6384 0.5945 0.7986 0.1876  0.0906  -0.1719 76  PHE A CA  
273  C C   . PHE A 36  ? 0.6597 0.5712 0.7677 0.1729  0.0836  -0.1846 76  PHE A C   
274  O O   . PHE A 36  ? 0.6837 0.5815 0.7795 0.1566  0.0630  -0.1736 76  PHE A O   
275  C CB  . PHE A 36  ? 0.6561 0.5981 0.8496 0.2167  0.0985  -0.1800 76  PHE A CB  
276  C CG  . PHE A 36  ? 0.7311 0.6200 0.9192 0.2213  0.0823  -0.1778 76  PHE A CG  
277  C CD1 . PHE A 36  ? 0.7237 0.6113 0.9265 0.2159  0.0590  -0.1531 76  PHE A CD1 
278  C CD2 . PHE A 36  ? 0.7973 0.6353 0.9641 0.2301  0.0922  -0.2011 76  PHE A CD2 
279  C CE1 . PHE A 36  ? 0.7937 0.6284 0.9898 0.2185  0.0476  -0.1490 76  PHE A CE1 
280  C CE2 . PHE A 36  ? 0.8897 0.6737 1.0529 0.2318  0.0800  -0.1995 76  PHE A CE2 
281  C CZ  . PHE A 36  ? 0.8703 0.6518 1.0482 0.2257  0.0585  -0.1720 76  PHE A CZ  
282  N N   . MET A 37  ? 0.6920 0.5839 0.7689 0.1782  0.1008  -0.2091 77  MET A N   
283  C CA  . MET A 37  ? 0.7258 0.5797 0.7543 0.1651  0.0928  -0.2257 77  MET A CA  
284  C C   . MET A 37  ? 0.7000 0.5681 0.7015 0.1419  0.0772  -0.2134 77  MET A C   
285  O O   . MET A 37  ? 0.7700 0.6161 0.7538 0.1277  0.0587  -0.2154 77  MET A O   
286  C CB  . MET A 37  ? 0.8511 0.6924 0.8448 0.1741  0.1148  -0.2540 77  MET A CB  
287  C CG  . MET A 37  ? 1.0341 0.8481 1.0455 0.1972  0.1302  -0.2738 77  MET A CG  
288  S SD  . MET A 37  ? 1.1896 0.9375 1.1813 0.1914  0.1153  -0.2937 77  MET A SD  
289  C CE  . MET A 37  ? 1.1436 0.8809 1.1897 0.1970  0.0982  -0.2660 77  MET A CE  
290  N N   . PHE A 38  ? 0.6313 0.5358 0.6313 0.1377  0.0857  -0.2013 78  PHE A N   
291  C CA  . PHE A 38  ? 0.6302 0.5459 0.6052 0.1190  0.0728  -0.1888 78  PHE A CA  
292  C C   . PHE A 38  ? 0.6204 0.5437 0.6236 0.1086  0.0516  -0.1680 78  PHE A C   
293  O O   . PHE A 38  ? 0.6441 0.5567 0.6301 0.0947  0.0339  -0.1651 78  PHE A O   
294  C CB  . PHE A 38  ? 0.6089 0.5538 0.5740 0.1175  0.0911  -0.1809 78  PHE A CB  
295  C CG  . PHE A 38  ? 0.5442 0.4969 0.4845 0.1017  0.0801  -0.1666 78  PHE A CG  
296  C CD1 . PHE A 38  ? 0.6767 0.6136 0.5656 0.0974  0.0742  -0.1747 78  PHE A CD1 
297  C CD2 . PHE A 38  ? 0.5159 0.4921 0.4839 0.0925  0.0749  -0.1463 78  PHE A CD2 
298  C CE1 . PHE A 38  ? 0.6456 0.5894 0.5135 0.0869  0.0639  -0.1606 78  PHE A CE1 
299  C CE2 . PHE A 38  ? 0.5706 0.5499 0.5161 0.0800  0.0665  -0.1343 78  PHE A CE2 
300  C CZ  . PHE A 38  ? 0.5930 0.5557 0.4896 0.0785  0.0615  -0.1405 78  PHE A CZ  
301  N N   . LEU A 39  ? 0.5587 0.5032 0.6057 0.1154  0.0529  -0.1540 79  LEU A N   
302  C CA  . LEU A 39  ? 0.5318 0.4893 0.5989 0.1048  0.0343  -0.1331 79  LEU A CA  
303  C C   . LEU A 39  ? 0.5491 0.4758 0.6210 0.1033  0.0173  -0.1304 79  LEU A C   
304  O O   . LEU A 39  ? 0.5566 0.4849 0.6271 0.0895  0.0017  -0.1169 79  LEU A O   
305  C CB  . LEU A 39  ? 0.4825 0.4773 0.5928 0.1121  0.0387  -0.1202 79  LEU A CB  
306  C CG  . LEU A 39  ? 0.4553 0.4836 0.5661 0.1059  0.0550  -0.1189 79  LEU A CG  
307  C CD1 . LEU A 39  ? 0.3890 0.4587 0.5504 0.1122  0.0584  -0.1107 79  LEU A CD1 
308  C CD2 . LEU A 39  ? 0.4568 0.4863 0.5399 0.0861  0.0472  -0.1098 79  LEU A CD2 
309  N N   . ARG A 40  ? 0.5686 0.4645 0.6457 0.1168  0.0221  -0.1430 80  ARG A N   
310  C CA  . ARG A 40  ? 0.5822 0.4429 0.6638 0.1134  0.0085  -0.1382 80  ARG A CA  
311  C C   . ARG A 40  ? 0.6419 0.4843 0.6928 0.0914  -0.0023 -0.1457 80  ARG A C   
312  O O   . ARG A 40  ? 0.5906 0.4117 0.6457 0.0811  -0.0139 -0.1375 80  ARG A O   
313  C CB  . ARG A 40  ? 0.5978 0.4220 0.6905 0.1327  0.0177  -0.1513 80  ARG A CB  
314  C CG  . ARG A 40  ? 0.6279 0.4247 0.6907 0.1326  0.0289  -0.1814 80  ARG A CG  
315  C CD  . ARG A 40  ? 0.7666 0.5142 0.8391 0.1468  0.0342  -0.1933 80  ARG A CD  
316  N NE  . ARG A 40  ? 0.9205 0.6364 0.9617 0.1440  0.0432  -0.2259 80  ARG A NE  
317  C CZ  . ARG A 40  ? 1.0786 0.7449 1.1217 0.1548  0.0510  -0.2438 80  ARG A CZ  
318  N NH1 . ARG A 40  ? 1.0919 0.7336 1.1671 0.1713  0.0512  -0.2288 80  ARG A NH1 
319  N NH2 . ARG A 40  ? 1.1402 0.7801 1.1514 0.1500  0.0583  -0.2769 80  ARG A NH2 
320  N N   . GLN A 41  ? 0.6028 0.4552 0.6236 0.0845  0.0014  -0.1602 81  GLN A N   
321  C CA  . GLN A 41  ? 0.5757 0.4257 0.5714 0.0651  -0.0113 -0.1657 81  GLN A CA  
322  C C   . GLN A 41  ? 0.5643 0.4493 0.5551 0.0558  -0.0175 -0.1491 81  GLN A C   
323  O O   . GLN A 41  ? 0.6115 0.5004 0.6033 0.0412  -0.0307 -0.1410 81  GLN A O   
324  C CB  . GLN A 41  ? 0.6367 0.4743 0.5973 0.0654  -0.0069 -0.1932 81  GLN A CB  
325  C CG  . GLN A 41  ? 0.7177 0.5641 0.6526 0.0482  -0.0222 -0.2003 81  GLN A CG  
326  C CD  . GLN A 41  ? 0.7732 0.5969 0.7181 0.0314  -0.0355 -0.2083 81  GLN A CD  
327  O OE1 . GLN A 41  ? 0.8761 0.6700 0.8427 0.0323  -0.0324 -0.2068 81  GLN A OE1 
328  N NE2 . GLN A 41  ? 0.6682 0.5062 0.5984 0.0164  -0.0497 -0.2165 81  GLN A NE2 
329  N N   . GLU A 42  ? 0.5465 0.4557 0.5338 0.0635  -0.0060 -0.1441 82  GLU A N   
330  C CA  . GLU A 42  ? 0.5002 0.4345 0.4762 0.0548  -0.0092 -0.1318 82  GLU A CA  
331  C C   . GLU A 42  ? 0.4881 0.4379 0.4903 0.0471  -0.0182 -0.1112 82  GLU A C   
332  O O   . GLU A 42  ? 0.4581 0.4177 0.4520 0.0359  -0.0273 -0.1037 82  GLU A O   
333  C CB  . GLU A 42  ? 0.5364 0.4861 0.5005 0.0630  0.0090  -0.1320 82  GLU A CB  
334  C CG  . GLU A 42  ? 0.5540 0.5200 0.5008 0.0552  0.0085  -0.1202 82  GLU A CG  
335  C CD  . GLU A 42  ? 0.6319 0.5900 0.5424 0.0510  -0.0030 -0.1270 82  GLU A CD  
336  O OE1 . GLU A 42  ? 0.6408 0.5837 0.5336 0.0537  -0.0074 -0.1446 82  GLU A OE1 
337  O OE2 . GLU A 42  ? 0.5992 0.5674 0.4999 0.0456  -0.0083 -0.1159 82  GLU A OE2 
338  N N   . LEU A 43  ? 0.4578 0.4119 0.4907 0.0545  -0.0161 -0.1023 83  LEU A N   
339  C CA  . LEU A 43  ? 0.4558 0.4251 0.5080 0.0475  -0.0265 -0.0835 83  LEU A CA  
340  C C   . LEU A 43  ? 0.4841 0.4358 0.5314 0.0358  -0.0402 -0.0791 83  LEU A C   
341  O O   . LEU A 43  ? 0.4594 0.4247 0.5025 0.0238  -0.0473 -0.0697 83  LEU A O   
342  C CB  . LEU A 43  ? 0.4503 0.4315 0.5354 0.0604  -0.0244 -0.0750 83  LEU A CB  
343  C CG  . LEU A 43  ? 0.4939 0.5080 0.5948 0.0656  -0.0121 -0.0751 83  LEU A CG  
344  C CD1 . LEU A 43  ? 0.4716 0.5027 0.6108 0.0808  -0.0130 -0.0689 83  LEU A CD1 
345  C CD2 . LEU A 43  ? 0.4357 0.4730 0.5312 0.0505  -0.0145 -0.0666 83  LEU A CD2 
346  N N   . PRO A 44  ? 0.5006 0.4213 0.5488 0.0373  -0.0424 -0.0862 84  PRO A N   
347  C CA  . PRO A 44  ? 0.4842 0.3891 0.5280 0.0215  -0.0523 -0.0832 84  PRO A CA  
348  C C   . PRO A 44  ? 0.5001 0.4191 0.5255 0.0078  -0.0571 -0.0913 84  PRO A C   
349  O O   . PRO A 44  ? 0.4805 0.4084 0.5079 -0.0053 -0.0641 -0.0825 84  PRO A O   
350  C CB  . PRO A 44  ? 0.5360 0.4009 0.5814 0.0248  -0.0497 -0.0956 84  PRO A CB  
351  C CG  . PRO A 44  ? 0.5272 0.3878 0.5868 0.0466  -0.0410 -0.0947 84  PRO A CG  
352  C CD  . PRO A 44  ? 0.5114 0.4080 0.5678 0.0527  -0.0343 -0.0967 84  PRO A CD  
353  N N   . VAL A 45  ? 0.4602 0.3827 0.4667 0.0123  -0.0533 -0.1077 85  VAL A N   
354  C CA  . VAL A 45  ? 0.4305 0.3683 0.4186 0.0038  -0.0602 -0.1147 85  VAL A CA  
355  C C   . VAL A 45  ? 0.4304 0.3944 0.4193 0.0014  -0.0612 -0.0987 85  VAL A C   
356  O O   . VAL A 45  ? 0.4666 0.4430 0.4559 -0.0087 -0.0690 -0.0957 85  VAL A O   
357  C CB  . VAL A 45  ? 0.4132 0.3490 0.3742 0.0127  -0.0560 -0.1328 85  VAL A CB  
358  C CG1 . VAL A 45  ? 0.4548 0.4116 0.3950 0.0098  -0.0641 -0.1346 85  VAL A CG1 
359  C CG2 . VAL A 45  ? 0.4367 0.3458 0.3931 0.0113  -0.0574 -0.1545 85  VAL A CG2 
360  N N   . ARG A 46  ? 0.4061 0.3796 0.3975 0.0099  -0.0520 -0.0898 86  ARG A N   
361  C CA  . ARG A 46  ? 0.4425 0.4360 0.4334 0.0063  -0.0513 -0.0774 86  ARG A CA  
362  C C   . ARG A 46  ? 0.4524 0.4524 0.4610 -0.0032 -0.0581 -0.0644 86  ARG A C   
363  O O   . ARG A 46  ? 0.4314 0.4439 0.4363 -0.0103 -0.0613 -0.0591 86  ARG A O   
364  C CB  . ARG A 46  ? 0.4085 0.4102 0.4004 0.0140  -0.0384 -0.0735 86  ARG A CB  
365  C CG  . ARG A 46  ? 0.4227 0.4175 0.3899 0.0229  -0.0283 -0.0839 86  ARG A CG  
366  C CD  . ARG A 46  ? 0.4434 0.4475 0.4104 0.0261  -0.0123 -0.0781 86  ARG A CD  
367  N NE  . ARG A 46  ? 0.4428 0.4377 0.3827 0.0350  0.0006  -0.0865 86  ARG A NE  
368  C CZ  . ARG A 46  ? 0.4480 0.4459 0.3785 0.0368  0.0184  -0.0822 86  ARG A CZ  
369  N NH1 . ARG A 46  ? 0.4418 0.4523 0.3916 0.0287  0.0242  -0.0717 86  ARG A NH1 
370  N NH2 . ARG A 46  ? 0.4739 0.4613 0.3740 0.0452  0.0313  -0.0889 86  ARG A NH2 
371  N N   . LEU A 47  ? 0.4390 0.4293 0.4643 -0.0020 -0.0598 -0.0587 87  LEU A N   
372  C CA  . LEU A 47  ? 0.4195 0.4130 0.4543 -0.0104 -0.0662 -0.0448 87  LEU A CA  
373  C C   . LEU A 47  ? 0.4313 0.4193 0.4613 -0.0236 -0.0713 -0.0472 87  LEU A C   
374  O O   . LEU A 47  ? 0.4273 0.4294 0.4561 -0.0326 -0.0733 -0.0400 87  LEU A O   
375  C CB  . LEU A 47  ? 0.3785 0.3586 0.4283 -0.0030 -0.0677 -0.0360 87  LEU A CB  
376  C CG  . LEU A 47  ? 0.4561 0.4545 0.5201 0.0085  -0.0656 -0.0299 87  LEU A CG  
377  C CD1 . LEU A 47  ? 0.5277 0.5120 0.6076 0.0212  -0.0686 -0.0221 87  LEU A CD1 
378  C CD2 . LEU A 47  ? 0.4546 0.4784 0.5188 0.0007  -0.0699 -0.0200 87  LEU A CD2 
379  N N   . ALA A 48  ? 0.4581 0.4279 0.4867 -0.0258 -0.0724 -0.0597 88  ALA A N   
380  C CA  . ALA A 48  ? 0.4644 0.4317 0.4958 -0.0414 -0.0767 -0.0637 88  ALA A CA  
381  C C   . ALA A 48  ? 0.4491 0.4438 0.4743 -0.0456 -0.0801 -0.0706 88  ALA A C   
382  O O   . ALA A 48  ? 0.4268 0.4340 0.4595 -0.0580 -0.0820 -0.0680 88  ALA A O   
383  C CB  . ALA A 48  ? 0.4495 0.3902 0.4829 -0.0448 -0.0773 -0.0790 88  ALA A CB  
384  N N   . ASN A 49  ? 0.4034 0.4071 0.4146 -0.0343 -0.0799 -0.0785 89  ASN A N   
385  C CA  . ASN A 49  ? 0.4238 0.4507 0.4270 -0.0333 -0.0839 -0.0825 89  ASN A CA  
386  C C   . ASN A 49  ? 0.4343 0.4767 0.4421 -0.0363 -0.0808 -0.0690 89  ASN A C   
387  O O   . ASN A 49  ? 0.4475 0.5081 0.4615 -0.0422 -0.0838 -0.0702 89  ASN A O   
388  C CB  . ASN A 49  ? 0.4162 0.4431 0.3970 -0.0184 -0.0820 -0.0886 89  ASN A CB  
389  C CG  . ASN A 49  ? 0.4576 0.4821 0.4265 -0.0163 -0.0895 -0.1071 89  ASN A CG  
390  O OD1 . ASN A 49  ? 0.4136 0.4562 0.3735 -0.0135 -0.0982 -0.1140 89  ASN A OD1 
391  N ND2 . ASN A 49  ? 0.4486 0.4514 0.4170 -0.0164 -0.0870 -0.1163 89  ASN A ND2 
392  N N   . ILE A 50  ? 0.3611 0.3991 0.3678 -0.0326 -0.0746 -0.0579 90  ILE A N   
393  C CA  . ILE A 50  ? 0.4433 0.4943 0.4511 -0.0364 -0.0718 -0.0483 90  ILE A CA  
394  C C   . ILE A 50  ? 0.4229 0.4757 0.4412 -0.0492 -0.0730 -0.0407 90  ILE A C   
395  O O   . ILE A 50  ? 0.4042 0.4711 0.4224 -0.0549 -0.0708 -0.0372 90  ILE A O   
396  C CB  . ILE A 50  ? 0.4297 0.4791 0.4338 -0.0310 -0.0658 -0.0420 90  ILE A CB  
397  C CG1 . ILE A 50  ? 0.4119 0.4725 0.4110 -0.0337 -0.0619 -0.0385 90  ILE A CG1 
398  C CG2 . ILE A 50  ? 0.4093 0.4532 0.4244 -0.0328 -0.0673 -0.0340 90  ILE A CG2 
399  C CD1 . ILE A 50  ? 0.4175 0.4819 0.4062 -0.0272 -0.0606 -0.0442 90  ILE A CD1 
400  N N   . MET A 51  ? 0.3913 0.4273 0.4164 -0.0534 -0.0747 -0.0375 91  MET A N   
401  C CA  . MET A 51  ? 0.4100 0.4421 0.4400 -0.0658 -0.0738 -0.0271 91  MET A CA  
402  C C   . MET A 51  ? 0.4367 0.4816 0.4747 -0.0786 -0.0726 -0.0338 91  MET A C   
403  O O   . MET A 51  ? 0.4590 0.5122 0.4981 -0.0891 -0.0679 -0.0257 91  MET A O   
404  C CB  . MET A 51  ? 0.4139 0.4179 0.4480 -0.0653 -0.0747 -0.0207 91  MET A CB  
405  C CG  . MET A 51  ? 0.4470 0.4468 0.4789 -0.0526 -0.0764 -0.0105 91  MET A CG  
406  S SD  . MET A 51  ? 0.5138 0.4796 0.5533 -0.0427 -0.0773 -0.0076 91  MET A SD  
407  C CE  . MET A 51  ? 0.4376 0.3802 0.4734 -0.0547 -0.0763 0.0107  91  MET A CE  
408  N N   . LYS A 52  ? 0.3824 0.4329 0.4263 -0.0778 -0.0768 -0.0495 92  LYS A N   
409  C CA  . LYS A 52  ? 0.4269 0.4999 0.4847 -0.0891 -0.0775 -0.0584 92  LYS A CA  
410  C C   . LYS A 52  ? 0.4451 0.5460 0.5018 -0.0847 -0.0743 -0.0559 92  LYS A C   
411  O O   . LYS A 52  ? 0.4297 0.5517 0.5005 -0.0953 -0.0703 -0.0575 92  LYS A O   
412  C CB  . LYS A 52  ? 0.3878 0.4677 0.4503 -0.0865 -0.0864 -0.0776 92  LYS A CB  
413  C CG  . LYS A 52  ? 0.4691 0.5204 0.5338 -0.0928 -0.0884 -0.0853 92  LYS A CG  
414  C CD  . LYS A 52  ? 0.5724 0.6128 0.6545 -0.1149 -0.0828 -0.0827 92  LYS A CD  
415  C CE  . LYS A 52  ? 0.6984 0.7721 0.8028 -0.1299 -0.0858 -0.0970 92  LYS A CE  
416  N NZ  . LYS A 52  ? 0.8170 0.8790 0.9400 -0.1553 -0.0764 -0.0939 92  LYS A NZ  
417  N N   . GLU A 53  ? 0.3824 0.4828 0.4240 -0.0699 -0.0741 -0.0531 93  GLU A N   
418  C CA  . GLU A 53  ? 0.3645 0.4844 0.4037 -0.0646 -0.0697 -0.0523 93  GLU A CA  
419  C C   . GLU A 53  ? 0.3949 0.5131 0.4281 -0.0721 -0.0615 -0.0411 93  GLU A C   
420  O O   . GLU A 53  ? 0.4055 0.5412 0.4410 -0.0737 -0.0552 -0.0422 93  GLU A O   
421  C CB  . GLU A 53  ? 0.4049 0.5203 0.4289 -0.0471 -0.0711 -0.0548 93  GLU A CB  
422  C CG  . GLU A 53  ? 0.4055 0.5280 0.4294 -0.0378 -0.0801 -0.0657 93  GLU A CG  
423  C CD  . GLU A 53  ? 0.4547 0.5704 0.4584 -0.0193 -0.0798 -0.0653 93  GLU A CD  
424  O OE1 . GLU A 53  ? 0.4509 0.5592 0.4425 -0.0113 -0.0854 -0.0704 93  GLU A OE1 
425  O OE2 . GLU A 53  ? 0.4225 0.5377 0.4199 -0.0131 -0.0726 -0.0600 93  GLU A OE2 
426  N N   . ILE A 54  ? 0.4044 0.5036 0.4293 -0.0752 -0.0618 -0.0311 94  ILE A N   
427  C CA  . ILE A 54  ? 0.4483 0.5480 0.4641 -0.0832 -0.0566 -0.0201 94  ILE A CA  
428  C C   . ILE A 54  ? 0.4523 0.5622 0.4759 -0.0973 -0.0497 -0.0180 94  ILE A C   
429  O O   . ILE A 54  ? 0.4661 0.5891 0.4828 -0.1023 -0.0416 -0.0155 94  ILE A O   
430  C CB  . ILE A 54  ? 0.4584 0.5390 0.4669 -0.0822 -0.0614 -0.0086 94  ILE A CB  
431  C CG1 . ILE A 54  ? 0.4219 0.4991 0.4279 -0.0699 -0.0654 -0.0123 94  ILE A CG1 
432  C CG2 . ILE A 54  ? 0.4406 0.5231 0.4342 -0.0894 -0.0588 0.0040  94  ILE A CG2 
433  C CD1 . ILE A 54  ? 0.4293 0.4950 0.4354 -0.0657 -0.0710 -0.0029 94  ILE A CD1 
434  N N   . SER A 55  ? 0.4325 0.5374 0.4714 -0.1054 -0.0512 -0.0208 95  SER A N   
435  C CA  . SER A 55  ? 0.4773 0.5912 0.5280 -0.1228 -0.0423 -0.0190 95  SER A CA  
436  C C   . SER A 55  ? 0.4995 0.6497 0.5663 -0.1238 -0.0366 -0.0307 95  SER A C   
437  O O   . SER A 55  ? 0.4751 0.6400 0.5529 -0.1387 -0.0253 -0.0292 95  SER A O   
438  C CB  . SER A 55  ? 0.5048 0.6025 0.5712 -0.1332 -0.0451 -0.0229 95  SER A CB  
439  O OG  . SER A 55  ? 0.5659 0.6279 0.6194 -0.1291 -0.0492 -0.0122 95  SER A OG  
440  N N   . LEU A 56  ? 0.4286 0.5934 0.4975 -0.1075 -0.0426 -0.0414 96  LEU A N   
441  C CA  . LEU A 56  ? 0.4388 0.6383 0.5247 -0.1031 -0.0385 -0.0520 96  LEU A CA  
442  C C   . LEU A 56  ? 0.4605 0.6654 0.5313 -0.0956 -0.0287 -0.0494 96  LEU A C   
443  O O   . LEU A 56  ? 0.4764 0.7081 0.5606 -0.0887 -0.0231 -0.0579 96  LEU A O   
444  C CB  . LEU A 56  ? 0.4189 0.6296 0.5138 -0.0870 -0.0513 -0.0643 96  LEU A CB  
445  C CG  . LEU A 56  ? 0.4042 0.6136 0.5136 -0.0950 -0.0619 -0.0724 96  LEU A CG  
446  C CD1 . LEU A 56  ? 0.3985 0.6144 0.5046 -0.0765 -0.0761 -0.0829 96  LEU A CD1 
447  C CD2 . LEU A 56  ? 0.4015 0.6395 0.5432 -0.1146 -0.0572 -0.0799 96  LEU A CD2 
448  N N   . LEU A 57  ? 0.4164 0.5978 0.4610 -0.0962 -0.0270 -0.0394 97  LEU A N   
449  C CA  . LEU A 57  ? 0.4079 0.5912 0.4349 -0.0917 -0.0183 -0.0399 97  LEU A CA  
450  C C   . LEU A 57  ? 0.4084 0.6134 0.4398 -0.1024 -0.0029 -0.0406 97  LEU A C   
451  O O   . LEU A 57  ? 0.4348 0.6452 0.4757 -0.1180 0.0021  -0.0347 97  LEU A O   
452  C CB  . LEU A 57  ? 0.4308 0.5904 0.4314 -0.0941 -0.0221 -0.0302 97  LEU A CB  
453  C CG  . LEU A 57  ? 0.4564 0.5986 0.4529 -0.0828 -0.0326 -0.0315 97  LEU A CG  
454  C CD1 . LEU A 57  ? 0.4311 0.5596 0.4095 -0.0866 -0.0372 -0.0230 97  LEU A CD1 
455  C CD2 . LEU A 57  ? 0.4641 0.6082 0.4596 -0.0694 -0.0293 -0.0420 97  LEU A CD2 
456  N N   . PRO A 58  ? 0.4584 0.6736 0.4823 -0.0952 0.0073  -0.0481 98  PRO A N   
457  C CA  . PRO A 58  ? 0.4860 0.7202 0.5079 -0.1056 0.0251  -0.0488 98  PRO A CA  
458  C C   . PRO A 58  ? 0.4995 0.7175 0.4947 -0.1225 0.0279  -0.0335 98  PRO A C   
459  O O   . PRO A 58  ? 0.5340 0.7285 0.5048 -0.1211 0.0176  -0.0260 98  PRO A O   
460  C CB  . PRO A 58  ? 0.5061 0.7407 0.5136 -0.0928 0.0335  -0.0600 98  PRO A CB  
461  C CG  . PRO A 58  ? 0.5136 0.7347 0.5262 -0.0748 0.0215  -0.0655 98  PRO A CG  
462  C CD  . PRO A 58  ? 0.4512 0.6548 0.4632 -0.0787 0.0053  -0.0558 98  PRO A CD  
463  N N   . ASP A 59  ? 0.4783 0.7103 0.4792 -0.1380 0.0423  -0.0281 99  ASP A N   
464  C CA  . ASP A 59  ? 0.5469 0.7587 0.5212 -0.1533 0.0449  -0.0092 99  ASP A CA  
465  C C   . ASP A 59  ? 0.5592 0.7574 0.4892 -0.1503 0.0438  -0.0042 99  ASP A C   
466  O O   . ASP A 59  ? 0.5567 0.7321 0.4625 -0.1523 0.0328  0.0108  99  ASP A O   
467  C CB  . ASP A 59  ? 0.5605 0.7888 0.5453 -0.1719 0.0658  -0.0041 99  ASP A CB  
468  C CG  . ASP A 59  ? 0.7473 0.9467 0.7111 -0.1876 0.0673  0.0187  99  ASP A CG  
469  O OD1 . ASP A 59  ? 0.7771 0.9588 0.7586 -0.1910 0.0567  0.0237  99  ASP A OD1 
470  O OD2 . ASP A 59  ? 0.8563 1.0475 0.7826 -0.1950 0.0789  0.0317  99  ASP A OD2 
471  N N   . ASN A 60  ? 0.5615 0.7742 0.4810 -0.1445 0.0541  -0.0182 100 ASN A N   
472  C CA  . ASN A 60  ? 0.6029 0.8054 0.4794 -0.1439 0.0526  -0.0180 100 ASN A CA  
473  C C   . ASN A 60  ? 0.5935 0.7782 0.4635 -0.1343 0.0312  -0.0199 100 ASN A C   
474  O O   . ASN A 60  ? 0.5965 0.7732 0.4335 -0.1365 0.0237  -0.0163 100 ASN A O   
475  C CB  . ASN A 60  ? 0.6256 0.8448 0.4938 -0.1402 0.0705  -0.0366 100 ASN A CB  
476  C CG  . ASN A 60  ? 0.7209 0.9603 0.5873 -0.1518 0.0950  -0.0338 100 ASN A CG  
477  O OD1 . ASN A 60  ? 0.6597 0.8940 0.5139 -0.1659 0.0992  -0.0149 100 ASN A OD1 
478  N ND2 . ASN A 60  ? 0.7781 1.0393 0.6570 -0.1454 0.1132  -0.0521 100 ASN A ND2 
479  N N   . LEU A 61  ? 0.5128 0.6939 0.4131 -0.1242 0.0216  -0.0259 101 LEU A N   
480  C CA  . LEU A 61  ? 0.5320 0.6971 0.4298 -0.1172 0.0040  -0.0259 101 LEU A CA  
481  C C   . LEU A 61  ? 0.5145 0.6672 0.4159 -0.1199 -0.0093 -0.0083 101 LEU A C   
482  O O   . LEU A 61  ? 0.4815 0.6259 0.3668 -0.1191 -0.0216 -0.0012 101 LEU A O   
483  C CB  . LEU A 61  ? 0.4830 0.6461 0.4053 -0.1042 0.0022  -0.0389 101 LEU A CB  
484  C CG  . LEU A 61  ? 0.4550 0.6022 0.3796 -0.0980 -0.0120 -0.0389 101 LEU A CG  
485  C CD1 . LEU A 61  ? 0.4934 0.6363 0.3933 -0.1031 -0.0166 -0.0420 101 LEU A CD1 
486  C CD2 . LEU A 61  ? 0.4612 0.6028 0.4022 -0.0848 -0.0100 -0.0497 101 LEU A CD2 
487  N N   . LEU A 62  ? 0.4912 0.6436 0.4150 -0.1230 -0.0068 -0.0024 102 LEU A N   
488  C CA  . LEU A 62  ? 0.4850 0.6196 0.4127 -0.1252 -0.0167 0.0129  102 LEU A CA  
489  C C   . LEU A 62  ? 0.5587 0.6828 0.4547 -0.1314 -0.0183 0.0314  102 LEU A C   
490  O O   . LEU A 62  ? 0.5693 0.6784 0.4591 -0.1259 -0.0319 0.0429  102 LEU A O   
491  C CB  . LEU A 62  ? 0.5273 0.6634 0.4818 -0.1324 -0.0103 0.0132  102 LEU A CB  
492  C CG  . LEU A 62  ? 0.5078 0.6198 0.4696 -0.1359 -0.0175 0.0256  102 LEU A CG  
493  C CD1 . LEU A 62  ? 0.4948 0.5945 0.4614 -0.1217 -0.0334 0.0228  102 LEU A CD1 
494  C CD2 . LEU A 62  ? 0.4569 0.5748 0.4486 -0.1460 -0.0107 0.0190  102 LEU A CD2 
495  N N   . ARG A 63  ? 0.5193 0.6519 0.3935 -0.1411 -0.0042 0.0349  103 ARG A N   
496  C CA  . ARG A 63  ? 0.5686 0.6899 0.4060 -0.1470 -0.0037 0.0555  103 ARG A CA  
497  C C   . ARG A 63  ? 0.5403 0.6660 0.3454 -0.1404 -0.0171 0.0553  103 ARG A C   
498  O O   . ARG A 63  ? 0.5989 0.7172 0.3690 -0.1422 -0.0207 0.0734  103 ARG A O   
499  C CB  . ARG A 63  ? 0.6917 0.8216 0.5142 -0.1612 0.0195  0.0593  103 ARG A CB  
500  C CG  . ARG A 63  ? 0.8505 0.9776 0.7037 -0.1730 0.0336  0.0630  103 ARG A CG  
501  C CD  . ARG A 63  ? 1.0614 1.1552 0.9047 -0.1791 0.0311  0.0884  103 ARG A CD  
502  N NE  . ARG A 63  ? 1.2140 1.3044 1.0832 -0.1965 0.0488  0.0908  103 ARG A NE  
503  C CZ  . ARG A 63  ? 1.3129 1.4023 1.1663 -0.2138 0.0717  0.1028  103 ARG A CZ  
504  N NH1 . ARG A 63  ? 1.3420 1.4311 1.2265 -0.2322 0.0879  0.1021  103 ARG A NH1 
505  N NH2 . ARG A 63  ? 1.3191 1.4088 1.1248 -0.2141 0.0791  0.1146  103 ARG A NH2 
506  N N   . THR A 64  ? 0.5294 0.6669 0.3441 -0.1335 -0.0246 0.0357  104 THR A N   
507  C CA  . THR A 64  ? 0.5959 0.7412 0.3836 -0.1307 -0.0379 0.0323  104 THR A CA  
508  C C   . THR A 64  ? 0.5832 0.7207 0.3702 -0.1227 -0.0588 0.0497  104 THR A C   
509  O O   . THR A 64  ? 0.5910 0.7158 0.4064 -0.1165 -0.0634 0.0563  104 THR A O   
510  C CB  . THR A 64  ? 0.5509 0.7056 0.3534 -0.1275 -0.0399 0.0071  104 THR A CB  
511  O OG1 . THR A 64  ? 0.5267 0.6745 0.3655 -0.1195 -0.0471 0.0047  104 THR A OG1 
512  C CG2 . THR A 64  ? 0.5673 0.7278 0.3705 -0.1310 -0.0195 -0.0101 104 THR A CG2 
513  N N   . PRO A 65  ? 0.5950 0.7412 0.3492 -0.1212 -0.0721 0.0567  105 PRO A N   
514  C CA  . PRO A 65  ? 0.6267 0.7702 0.3837 -0.1095 -0.0936 0.0736  105 PRO A CA  
515  C C   . PRO A 65  ? 0.5978 0.7475 0.3972 -0.1012 -0.1045 0.0615  105 PRO A C   
516  O O   . PRO A 65  ? 0.6044 0.7441 0.4222 -0.0902 -0.1140 0.0749  105 PRO A O   
517  C CB  . PRO A 65  ? 0.6798 0.8422 0.3947 -0.1095 -0.1079 0.0763  105 PRO A CB  
518  C CG  . PRO A 65  ? 0.7089 0.8828 0.4064 -0.1215 -0.0937 0.0529  105 PRO A CG  
519  C CD  . PRO A 65  ? 0.6790 0.8391 0.3904 -0.1286 -0.0686 0.0500  105 PRO A CD  
520  N N   . SER A 66  ? 0.5105 0.6733 0.3249 -0.1059 -0.1008 0.0367  106 SER A N   
521  C CA  . SER A 66  ? 0.5103 0.6786 0.3614 -0.0997 -0.1082 0.0260  106 SER A CA  
522  C C   . SER A 66  ? 0.5100 0.6586 0.3905 -0.0948 -0.0984 0.0278  106 SER A C   
523  O O   . SER A 66  ? 0.5080 0.6540 0.4133 -0.0854 -0.1058 0.0311  106 SER A O   
524  C CB  . SER A 66  ? 0.4562 0.6381 0.3109 -0.1079 -0.1049 0.0005  106 SER A CB  
525  O OG  . SER A 66  ? 0.5140 0.7124 0.3480 -0.1109 -0.1146 -0.0049 106 SER A OG  
526  N N   . VAL A 67  ? 0.4973 0.6352 0.3768 -0.1004 -0.0820 0.0239  107 VAL A N   
527  C CA  . VAL A 67  ? 0.4867 0.6097 0.3922 -0.0964 -0.0756 0.0242  107 VAL A CA  
528  C C   . VAL A 67  ? 0.4888 0.5946 0.3957 -0.0927 -0.0799 0.0440  107 VAL A C   
529  O O   . VAL A 67  ? 0.4949 0.5887 0.4238 -0.0854 -0.0829 0.0449  107 VAL A O   
530  C CB  . VAL A 67  ? 0.4738 0.5967 0.3818 -0.1023 -0.0594 0.0140  107 VAL A CB  
531  C CG1 . VAL A 67  ? 0.4728 0.5847 0.4056 -0.0993 -0.0559 0.0144  107 VAL A CG1 
532  C CG2 . VAL A 67  ? 0.4590 0.5902 0.3685 -0.1017 -0.0545 -0.0052 107 VAL A CG2 
533  N N   . GLN A 68  ? 0.4957 0.5964 0.3761 -0.0974 -0.0792 0.0603  108 GLN A N   
534  C CA  . GLN A 68  ? 0.5659 0.6426 0.4438 -0.0936 -0.0820 0.0818  108 GLN A CA  
535  C C   . GLN A 68  ? 0.6193 0.6942 0.5087 -0.0775 -0.0992 0.0887  108 GLN A C   
536  O O   . GLN A 68  ? 0.5844 0.6363 0.4892 -0.0699 -0.1005 0.0971  108 GLN A O   
537  C CB  . GLN A 68  ? 0.5829 0.6529 0.4231 -0.1007 -0.0772 0.1008  108 GLN A CB  
538  C CG  . GLN A 68  ? 0.6391 0.7069 0.4751 -0.1168 -0.0559 0.0975  108 GLN A CG  
539  C CD  . GLN A 68  ? 0.6328 0.6788 0.4960 -0.1221 -0.0468 0.0993  108 GLN A CD  
540  O OE1 . GLN A 68  ? 0.6709 0.6878 0.5312 -0.1200 -0.0486 0.1175  108 GLN A OE1 
541  N NE2 . GLN A 68  ? 0.5797 0.6389 0.4691 -0.1282 -0.0377 0.0797  108 GLN A NE2 
542  N N   . LEU A 69  ? 0.5709 0.6715 0.4556 -0.0725 -0.1121 0.0832  109 LEU A N   
543  C CA  . LEU A 69  ? 0.5502 0.6588 0.4529 -0.0566 -0.1285 0.0876  109 LEU A CA  
544  C C   . LEU A 69  ? 0.5325 0.6392 0.4726 -0.0515 -0.1245 0.0725  109 LEU A C   
545  O O   . LEU A 69  ? 0.5309 0.6251 0.4893 -0.0381 -0.1289 0.0795  109 LEU A O   
546  C CB  . LEU A 69  ? 0.5170 0.6607 0.4096 -0.0559 -0.1436 0.0818  109 LEU A CB  
547  C CG  . LEU A 69  ? 0.5694 0.7330 0.4814 -0.0390 -0.1635 0.0874  109 LEU A CG  
548  C CD1 . LEU A 69  ? 0.6503 0.7917 0.5502 -0.0227 -0.1721 0.1158  109 LEU A CD1 
549  C CD2 . LEU A 69  ? 0.5820 0.7855 0.4836 -0.0436 -0.1785 0.0774  109 LEU A CD2 
550  N N   . VAL A 70  ? 0.4498 0.5659 0.3988 -0.0605 -0.1149 0.0525  110 VAL A N   
551  C CA  . VAL A 70  ? 0.4435 0.5555 0.4203 -0.0556 -0.1094 0.0398  110 VAL A CA  
552  C C   . VAL A 70  ? 0.4929 0.5759 0.4767 -0.0523 -0.1030 0.0453  110 VAL A C   
553  O O   . VAL A 70  ? 0.4854 0.5591 0.4880 -0.0415 -0.1044 0.0440  110 VAL A O   
554  C CB  . VAL A 70  ? 0.4219 0.5421 0.3997 -0.0648 -0.0991 0.0211  110 VAL A CB  
555  C CG1 . VAL A 70  ? 0.4240 0.5335 0.4211 -0.0595 -0.0913 0.0114  110 VAL A CG1 
556  C CG2 . VAL A 70  ? 0.3716 0.5166 0.3486 -0.0692 -0.1046 0.0116  110 VAL A CG2 
557  N N   . GLN A 71  ? 0.4969 0.5663 0.4666 -0.0626 -0.0950 0.0497  111 GLN A N   
558  C CA  . GLN A 71  ? 0.5037 0.5465 0.4817 -0.0637 -0.0889 0.0521  111 GLN A CA  
559  C C   . GLN A 71  ? 0.5463 0.5656 0.5256 -0.0530 -0.0953 0.0687  111 GLN A C   
560  O O   . GLN A 71  ? 0.5119 0.5096 0.5062 -0.0473 -0.0933 0.0652  111 GLN A O   
561  C CB  . GLN A 71  ? 0.5539 0.5921 0.5207 -0.0793 -0.0782 0.0540  111 GLN A CB  
562  C CG  . GLN A 71  ? 0.5762 0.5916 0.5563 -0.0852 -0.0716 0.0516  111 GLN A CG  
563  C CD  . GLN A 71  ? 0.5654 0.5818 0.5402 -0.1028 -0.0598 0.0537  111 GLN A CD  
564  O OE1 . GLN A 71  ? 0.5669 0.5773 0.5218 -0.1096 -0.0554 0.0700  111 GLN A OE1 
565  N NE2 . GLN A 71  ? 0.5261 0.5530 0.5185 -0.1099 -0.0544 0.0372  111 GLN A NE2 
566  N N   . SER A 72  ? 0.5154 0.5371 0.4771 -0.0485 -0.1035 0.0866  112 SER A N   
567  C CA  . SER A 72  ? 0.5471 0.5436 0.5091 -0.0340 -0.1103 0.1051  112 SER A CA  
568  C C   . SER A 72  ? 0.5589 0.5660 0.5475 -0.0151 -0.1189 0.0978  112 SER A C   
569  O O   . SER A 72  ? 0.5903 0.5704 0.5906 -0.0020 -0.1191 0.1037  112 SER A O   
570  C CB  . SER A 72  ? 0.6724 0.6701 0.6044 -0.0310 -0.1187 0.1284  112 SER A CB  
571  O OG  . SER A 72  ? 0.8432 0.8792 0.7757 -0.0221 -0.1339 0.1254  112 SER A OG  
572  N N   . TRP A 73  ? 0.5038 0.5484 0.5036 -0.0141 -0.1239 0.0840  113 TRP A N   
573  C CA  . TRP A 73  ? 0.5140 0.5729 0.5435 0.0008  -0.1275 0.0743  113 TRP A CA  
574  C C   . TRP A 73  ? 0.5129 0.5489 0.5566 0.0013  -0.1151 0.0606  113 TRP A C   
575  O O   . TRP A 73  ? 0.4847 0.5081 0.5460 0.0168  -0.1149 0.0601  113 TRP A O   
576  C CB  . TRP A 73  ? 0.4111 0.5122 0.4503 -0.0044 -0.1310 0.0601  113 TRP A CB  
577  C CG  . TRP A 73  ? 0.4832 0.6138 0.5141 -0.0020 -0.1469 0.0692  113 TRP A CG  
578  C CD1 . TRP A 73  ? 0.5125 0.6402 0.5334 0.0115  -0.1608 0.0900  113 TRP A CD1 
579  C CD2 . TRP A 73  ? 0.4785 0.6451 0.5079 -0.0135 -0.1515 0.0569  113 TRP A CD2 
580  N NE1 . TRP A 73  ? 0.5678 0.7327 0.5802 0.0099  -0.1761 0.0910  113 TRP A NE1 
581  C CE2 . TRP A 73  ? 0.5387 0.7277 0.5571 -0.0070 -0.1702 0.0691  113 TRP A CE2 
582  C CE3 . TRP A 73  ? 0.4911 0.6703 0.5257 -0.0282 -0.1414 0.0366  113 TRP A CE3 
583  C CZ2 . TRP A 73  ? 0.5727 0.7994 0.5865 -0.0172 -0.1800 0.0583  113 TRP A CZ2 
584  C CZ3 . TRP A 73  ? 0.4852 0.6957 0.5162 -0.0386 -0.1486 0.0270  113 TRP A CZ3 
585  C CH2 . TRP A 73  ? 0.5337 0.7693 0.5551 -0.0342 -0.1681 0.0361  113 TRP A CH2 
586  N N   . TYR A 74  ? 0.4497 0.4816 0.4853 -0.0142 -0.1052 0.0485  114 TYR A N   
587  C CA  . TYR A 74  ? 0.4834 0.4978 0.5280 -0.0141 -0.0960 0.0339  114 TYR A CA  
588  C C   . TYR A 74  ? 0.5306 0.5060 0.5749 -0.0112 -0.0938 0.0401  114 TYR A C   
589  O O   . TYR A 74  ? 0.5434 0.5019 0.5996 -0.0012 -0.0904 0.0313  114 TYR A O   
590  C CB  . TYR A 74  ? 0.3662 0.3881 0.4016 -0.0289 -0.0890 0.0215  114 TYR A CB  
591  C CG  . TYR A 74  ? 0.4235 0.4702 0.4627 -0.0283 -0.0861 0.0095  114 TYR A CG  
592  C CD1 . TYR A 74  ? 0.4493 0.5203 0.4932 -0.0264 -0.0908 0.0123  114 TYR A CD1 
593  C CD2 . TYR A 74  ? 0.4396 0.4845 0.4768 -0.0301 -0.0788 -0.0044 114 TYR A CD2 
594  C CE1 . TYR A 74  ? 0.4631 0.5517 0.5116 -0.0289 -0.0854 0.0010  114 TYR A CE1 
595  C CE2 . TYR A 74  ? 0.3982 0.4583 0.4354 -0.0294 -0.0736 -0.0125 114 TYR A CE2 
596  C CZ  . TYR A 74  ? 0.4091 0.4888 0.4529 -0.0302 -0.0755 -0.0099 114 TYR A CZ  
597  O OH  . TYR A 74  ? 0.4010 0.4910 0.4457 -0.0326 -0.0677 -0.0183 114 TYR A OH  
598  N N   . ILE A 75  ? 0.5052 0.4633 0.5345 -0.0207 -0.0940 0.0549  115 ILE A N   
599  C CA  . ILE A 75  ? 0.5315 0.4461 0.5595 -0.0214 -0.0897 0.0621  115 ILE A CA  
600  C C   . ILE A 75  ? 0.6050 0.5005 0.6431 0.0017  -0.0946 0.0714  115 ILE A C   
601  O O   . ILE A 75  ? 0.5936 0.4554 0.6406 0.0077  -0.0892 0.0646  115 ILE A O   
602  C CB  . ILE A 75  ? 0.5935 0.4945 0.6013 -0.0364 -0.0865 0.0802  115 ILE A CB  
603  C CG1 . ILE A 75  ? 0.6012 0.5203 0.6062 -0.0582 -0.0788 0.0675  115 ILE A CG1 
604  C CG2 . ILE A 75  ? 0.6438 0.4930 0.6488 -0.0363 -0.0811 0.0928  115 ILE A CG2 
605  C CD1 . ILE A 75  ? 0.6728 0.5858 0.6592 -0.0744 -0.0721 0.0834  115 ILE A CD1 
606  N N   . GLN A 76  ? 0.6295 0.5480 0.6678 0.0158  -0.1054 0.0852  116 GLN A N   
607  C CA  . GLN A 76  ? 0.6395 0.5458 0.6910 0.0415  -0.1119 0.0959  116 GLN A CA  
608  C C   . GLN A 76  ? 0.6074 0.5254 0.6861 0.0549  -0.1079 0.0754  116 GLN A C   
609  O O   . GLN A 76  ? 0.6266 0.5160 0.7177 0.0723  -0.1047 0.0750  116 GLN A O   
610  C CB  . GLN A 76  ? 0.6437 0.5815 0.6901 0.0531  -0.1275 0.1143  116 GLN A CB  
611  C CG  . GLN A 76  ? 0.7696 0.7038 0.8336 0.0836  -0.1371 0.1265  116 GLN A CG  
612  C CD  . GLN A 76  ? 0.9049 0.8600 0.9546 0.0950  -0.1552 0.1506  116 GLN A CD  
613  O OE1 . GLN A 76  ? 0.9608 0.9567 1.0001 0.0832  -0.1632 0.1485  116 GLN A OE1 
614  N NE2 . GLN A 76  ? 0.9419 0.8671 0.9882 0.1190  -0.1621 0.1735  116 GLN A NE2 
615  N N   . SER A 77  ? 0.5082 0.4650 0.5946 0.0473  -0.1059 0.0584  117 SER A N   
616  C CA  . SER A 77  ? 0.4909 0.4587 0.5988 0.0579  -0.0986 0.0395  117 SER A CA  
617  C C   . SER A 77  ? 0.5606 0.4903 0.6633 0.0538  -0.0869 0.0241  117 SER A C   
618  O O   . SER A 77  ? 0.5404 0.4558 0.6568 0.0696  -0.0807 0.0145  117 SER A O   
619  C CB  . SER A 77  ? 0.5099 0.5207 0.6220 0.0478  -0.0965 0.0270  117 SER A CB  
620  O OG  . SER A 77  ? 0.5947 0.6421 0.7143 0.0503  -0.1080 0.0371  117 SER A OG  
621  N N   . LEU A 78  ? 0.5386 0.4541 0.6227 0.0328  -0.0840 0.0198  118 LEU A N   
622  C CA  . LEU A 78  ? 0.5298 0.4133 0.6089 0.0261  -0.0758 0.0029  118 LEU A CA  
623  C C   . LEU A 78  ? 0.5813 0.4173 0.6649 0.0369  -0.0733 0.0081  118 LEU A C   
624  O O   . LEU A 78  ? 0.5800 0.3945 0.6694 0.0459  -0.0662 -0.0086 118 LEU A O   
625  C CB  . LEU A 78  ? 0.5071 0.3901 0.5715 0.0016  -0.0755 -0.0004 118 LEU A CB  
626  C CG  . LEU A 78  ? 0.5606 0.4156 0.6217 -0.0092 -0.0701 -0.0193 118 LEU A CG  
627  C CD1 . LEU A 78  ? 0.5223 0.3874 0.5834 -0.0005 -0.0664 -0.0416 118 LEU A CD1 
628  C CD2 . LEU A 78  ? 0.5573 0.4219 0.6112 -0.0329 -0.0709 -0.0219 118 LEU A CD2 
629  N N   . GLN A 79  ? 0.6415 0.4574 0.7195 0.0371  -0.0779 0.0315  119 GLN A N   
630  C CA  . GLN A 79  ? 0.7076 0.4695 0.7869 0.0480  -0.0742 0.0400  119 GLN A CA  
631  C C   . GLN A 79  ? 0.6666 0.4275 0.7655 0.0793  -0.0745 0.0388  119 GLN A C   
632  O O   . GLN A 79  ? 0.7020 0.4197 0.8065 0.0902  -0.0666 0.0299  119 GLN A O   
633  C CB  . GLN A 79  ? 0.8316 0.5729 0.8958 0.0440  -0.0785 0.0700  119 GLN A CB  
634  C CG  . GLN A 79  ? 0.9691 0.6973 1.0171 0.0126  -0.0726 0.0707  119 GLN A CG  
635  C CD  . GLN A 79  ? 1.0835 0.7912 1.1118 0.0086  -0.0737 0.1024  119 GLN A CD  
636  O OE1 . GLN A 79  ? 1.1389 0.8124 1.1566 -0.0125 -0.0639 0.1077  119 GLN A OE1 
637  N NE2 . GLN A 79  ? 1.0892 0.8196 1.1118 0.0279  -0.0853 0.1233  119 GLN A NE2 
638  N N   . GLU A 80  ? 0.6267 0.4360 0.7388 0.0938  -0.0828 0.0457  120 GLU A N   
639  C CA  . GLU A 80  ? 0.6723 0.4910 0.8103 0.1241  -0.0824 0.0432  120 GLU A CA  
640  C C   . GLU A 80  ? 0.6680 0.4879 0.8155 0.1263  -0.0688 0.0134  120 GLU A C   
641  O O   . GLU A 80  ? 0.7072 0.5075 0.8705 0.1488  -0.0614 0.0056  120 GLU A O   
642  C CB  . GLU A 80  ? 0.6829 0.5614 0.8370 0.1346  -0.0949 0.0542  120 GLU A CB  
643  C CG  . GLU A 80  ? 0.7927 0.6700 0.9361 0.1409  -0.1104 0.0844  120 GLU A CG  
644  C CD  . GLU A 80  ? 0.8205 0.7623 0.9778 0.1465  -0.1252 0.0910  120 GLU A CD  
645  O OE1 . GLU A 80  ? 0.8280 0.8135 1.0019 0.1391  -0.1212 0.0722  120 GLU A OE1 
646  O OE2 . GLU A 80  ? 0.8840 0.8315 1.0338 0.1576  -0.1406 0.1149  120 GLU A OE2 
647  N N   . LEU A 81  ? 0.6457 0.4873 0.7814 0.1049  -0.0646 -0.0032 121 LEU A N   
648  C CA  . LEU A 81  ? 0.6141 0.4558 0.7502 0.1066  -0.0517 -0.0302 121 LEU A CA  
649  C C   . LEU A 81  ? 0.6059 0.3916 0.7289 0.1026  -0.0441 -0.0455 121 LEU A C   
650  O O   . LEU A 81  ? 0.6785 0.4478 0.8062 0.1165  -0.0331 -0.0644 121 LEU A O   
651  C CB  . LEU A 81  ? 0.5939 0.4710 0.7163 0.0871  -0.0506 -0.0404 121 LEU A CB  
652  C CG  . LEU A 81  ? 0.5740 0.5040 0.7114 0.0902  -0.0538 -0.0320 121 LEU A CG  
653  C CD1 . LEU A 81  ? 0.5982 0.5510 0.7175 0.0686  -0.0546 -0.0354 121 LEU A CD1 
654  C CD2 . LEU A 81  ? 0.4973 0.4489 0.6570 0.1089  -0.0421 -0.0437 121 LEU A CD2 
655  N N   . LEU A 82  ? 0.6423 0.3982 0.7500 0.0826  -0.0485 -0.0391 122 LEU A N   
656  C CA  . LEU A 82  ? 0.7708 0.4754 0.8680 0.0727  -0.0416 -0.0568 122 LEU A CA  
657  C C   . LEU A 82  ? 0.8705 0.5238 0.9781 0.0947  -0.0347 -0.0554 122 LEU A C   
658  O O   . LEU A 82  ? 0.9788 0.5873 1.0795 0.0898  -0.0262 -0.0765 122 LEU A O   
659  C CB  . LEU A 82  ? 0.8191 0.5075 0.9035 0.0442  -0.0463 -0.0491 122 LEU A CB  
660  C CG  . LEU A 82  ? 0.8301 0.5650 0.9050 0.0238  -0.0518 -0.0556 122 LEU A CG  
661  C CD1 . LEU A 82  ? 0.8161 0.5374 0.8836 -0.0050 -0.0535 -0.0557 122 LEU A CD1 
662  C CD2 . LEU A 82  ? 0.8485 0.6025 0.9170 0.0272  -0.0479 -0.0829 122 LEU A CD2 
663  N N   . ASP A 83  ? 0.8801 0.5384 1.0042 0.1196  -0.0386 -0.0322 123 ASP A N   
664  C CA  . ASP A 83  ? 1.0027 0.6116 1.1383 0.1460  -0.0319 -0.0294 123 ASP A CA  
665  C C   . ASP A 83  ? 0.9622 0.5705 1.1089 0.1649  -0.0188 -0.0581 123 ASP A C   
666  O O   . ASP A 83  ? 1.0721 0.6307 1.2259 0.1849  -0.0097 -0.0638 123 ASP A O   
667  C CB  . ASP A 83  ? 1.1417 0.7648 1.2935 0.1721  -0.0423 0.0033  123 ASP A CB  
668  C CG  . ASP A 83  ? 1.2723 0.8736 1.4062 0.1584  -0.0517 0.0337  123 ASP A CG  
669  O OD1 . ASP A 83  ? 1.3290 0.8842 1.4442 0.1337  -0.0456 0.0301  123 ASP A OD1 
670  O OD2 . ASP A 83  ? 1.3070 0.9388 1.4453 0.1714  -0.0648 0.0603  123 ASP A OD2 
671  N N   . PHE A 84  ? 0.8720 0.5304 1.0181 0.1598  -0.0157 -0.0759 124 PHE A N   
672  C CA  . PHE A 84  ? 0.9423 0.6049 1.0943 0.1764  -0.0006 -0.1030 124 PHE A CA  
673  C C   . PHE A 84  ? 1.0341 0.6711 1.1574 0.1563  0.0074  -0.1352 124 PHE A C   
674  O O   . PHE A 84  ? 1.0126 0.6506 1.1322 0.1677  0.0212  -0.1605 124 PHE A O   
675  C CB  . PHE A 84  ? 0.8341 0.5668 1.0015 0.1842  0.0010  -0.1019 124 PHE A CB  
676  C CG  . PHE A 84  ? 0.7787 0.5462 0.9792 0.2055  -0.0078 -0.0759 124 PHE A CG  
677  C CD1 . PHE A 84  ? 0.7462 0.5405 0.9459 0.1929  -0.0249 -0.0508 124 PHE A CD1 
678  C CD2 . PHE A 84  ? 0.7728 0.5502 1.0057 0.2388  0.0007  -0.0785 124 PHE A CD2 
679  C CE1 . PHE A 84  ? 0.7010 0.5314 0.9288 0.2119  -0.0358 -0.0290 124 PHE A CE1 
680  C CE2 . PHE A 84  ? 0.7734 0.5904 1.0399 0.2593  -0.0105 -0.0559 124 PHE A CE2 
681  C CZ  . PHE A 84  ? 0.7653 0.6090 1.0278 0.2452  -0.0299 -0.0314 124 PHE A CZ  
682  N N   . LYS A 85  ? 1.0484 0.6656 1.1519 0.1268  -0.0010 -0.1358 125 LYS A N   
683  C CA  . LYS A 85  ? 1.0567 0.6623 1.1341 0.1050  0.0015  -0.1665 125 LYS A CA  
684  C C   . LYS A 85  ? 1.1667 0.7224 1.2379 0.1164  0.0155  -0.1965 125 LYS A C   
685  O O   . LYS A 85  ? 1.1510 0.7140 1.2014 0.1130  0.0216  -0.2260 125 LYS A O   
686  C CB  . LYS A 85  ? 1.0908 0.6809 1.1585 0.0733  -0.0095 -0.1610 125 LYS A CB  
687  C CG  . LYS A 85  ? 1.2303 0.7925 1.2784 0.0507  -0.0086 -0.1943 125 LYS A CG  
688  C CD  . LYS A 85  ? 1.2236 0.8361 1.2523 0.0349  -0.0168 -0.2085 125 LYS A CD  
689  C CE  . LYS A 85  ? 1.2333 0.8285 1.2474 0.0070  -0.0228 -0.2369 125 LYS A CE  
690  N NZ  . LYS A 85  ? 1.1868 0.7499 1.1834 0.0121  -0.0146 -0.2741 125 LYS A NZ  
691  N N   . ASP A 86  ? 1.2266 0.7288 1.3125 0.1313  0.0211  -0.1893 126 ASP A N   
692  C CA  . ASP A 86  ? 1.3386 0.7869 1.4150 0.1409  0.0357  -0.2161 126 ASP A CA  
693  C C   . ASP A 86  ? 1.3153 0.7660 1.4070 0.1798  0.0492  -0.2122 126 ASP A C   
694  O O   . ASP A 86  ? 1.3752 0.7851 1.4512 0.1905  0.0614  -0.2278 126 ASP A O   
695  C CB  . ASP A 86  ? 1.5095 0.8922 1.5767 0.1250  0.0349  -0.2089 126 ASP A CB  
696  C CG  . ASP A 86  ? 1.5885 0.9654 1.6341 0.0842  0.0274  -0.2270 126 ASP A CG  
697  O OD1 . ASP A 86  ? 1.5546 0.9768 1.5884 0.0713  0.0218  -0.2458 126 ASP A OD1 
698  O OD2 . ASP A 86  ? 1.6640 0.9932 1.7035 0.0655  0.0267  -0.2217 126 ASP A OD2 
699  N N   . LYS A 87  ? 1.2113 0.7112 1.3341 0.2011  0.0462  -0.1929 127 LYS A N   
700  C CA  . LYS A 87  ? 1.1777 0.6888 1.3203 0.2377  0.0587  -0.1889 127 LYS A CA  
701  C C   . LYS A 87  ? 1.1600 0.7060 1.2912 0.2434  0.0748  -0.2164 127 LYS A C   
702  O O   . LYS A 87  ? 1.1389 0.7154 1.2525 0.2234  0.0733  -0.2309 127 LYS A O   
703  C CB  . LYS A 87  ? 1.0724 0.6260 1.2553 0.2578  0.0473  -0.1557 127 LYS A CB  
704  C CG  . LYS A 87  ? 1.1619 0.6699 1.3492 0.2650  0.0372  -0.1257 127 LYS A CG  
705  C CD  . LYS A 87  ? 1.1874 0.7396 1.4067 0.2817  0.0208  -0.0908 127 LYS A CD  
706  C CE  . LYS A 87  ? 1.3070 0.8075 1.5196 0.2923  0.0132  -0.0599 127 LYS A CE  
707  N NZ  . LYS A 87  ? 1.3274 0.8694 1.5602 0.3035  -0.0070 -0.0237 127 LYS A NZ  
708  N N   . SER A 88  ? 1.2109 0.7501 1.3484 0.2722  0.0905  -0.2228 128 SER A N   
709  C CA  . SER A 88  ? 1.1435 0.7023 1.2625 0.2784  0.1094  -0.2496 128 SER A CA  
710  C C   . SER A 88  ? 1.0999 0.7330 1.2483 0.2911  0.1168  -0.2424 128 SER A C   
711  O O   . SER A 88  ? 1.0577 0.7224 1.2492 0.3117  0.1129  -0.2199 128 SER A O   
712  C CB  . SER A 88  ? 1.1461 0.6615 1.2567 0.3037  0.1231  -0.2628 128 SER A CB  
713  O OG  . SER A 88  ? 1.1342 0.6814 1.2375 0.3174  0.1424  -0.2822 128 SER A OG  
714  N N   . ALA A 89  ? 1.0902 0.7518 1.2128 0.2782  0.1277  -0.2613 129 ALA A N   
715  C CA  . ALA A 89  ? 1.0880 0.8169 1.2332 0.2864  0.1394  -0.2570 129 ALA A CA  
716  C C   . ALA A 89  ? 1.1681 0.9138 1.3397 0.3187  0.1579  -0.2580 129 ALA A C   
717  O O   . ALA A 89  ? 1.0992 0.9052 1.3072 0.3285  0.1652  -0.2478 129 ALA A O   
718  C CB  . ALA A 89  ? 1.0723 0.8174 1.1733 0.2664  0.1492  -0.2758 129 ALA A CB  
719  N N   . GLU A 90  ? 1.2455 0.9412 1.4007 0.3349  0.1652  -0.2714 130 GLU A N   
720  C CA  . GLU A 90  ? 1.2878 0.9976 1.4690 0.3690  0.1809  -0.2737 130 GLU A CA  
721  C C   . GLU A 90  ? 1.2773 0.9895 1.5058 0.3937  0.1680  -0.2479 130 GLU A C   
722  O O   . GLU A 90  ? 1.2934 1.0414 1.5577 0.4227  0.1771  -0.2433 130 GLU A O   
723  C CB  . GLU A 90  ? 1.3943 1.0494 1.5350 0.3780  0.1932  -0.3019 130 GLU A CB  
724  C CG  . GLU A 90  ? 1.4433 1.0984 1.5317 0.3567  0.2042  -0.3267 130 GLU A CG  
725  C CD  . GLU A 90  ? 1.4830 1.2027 1.5805 0.3628  0.2246  -0.3291 130 GLU A CD  
726  O OE1 . GLU A 90  ? 1.5732 1.2994 1.6713 0.3856  0.2437  -0.3440 130 GLU A OE1 
727  O OE2 . GLU A 90  ? 1.4241 1.1882 1.5292 0.3447  0.2222  -0.3164 130 GLU A OE2 
728  N N   . ASP A 91  ? 1.2156 0.8919 1.4430 0.3832  0.1467  -0.2305 131 ASP A N   
729  C CA  . ASP A 91  ? 1.1374 0.8179 1.4028 0.4045  0.1307  -0.2008 131 ASP A CA  
730  C C   . ASP A 91  ? 1.0240 0.7898 1.3364 0.4083  0.1258  -0.1823 131 ASP A C   
731  O O   . ASP A 91  ? 1.0214 0.8145 1.3378 0.3839  0.1128  -0.1723 131 ASP A O   
732  C CB  . ASP A 91  ? 1.1717 0.7983 1.4190 0.3858  0.1102  -0.1852 131 ASP A CB  
733  C CG  . ASP A 91  ? 1.2371 0.8638 1.5137 0.4074  0.0922  -0.1509 131 ASP A CG  
734  O OD1 . ASP A 91  ? 1.2817 0.9437 1.5911 0.4405  0.0942  -0.1416 131 ASP A OD1 
735  O OD2 . ASP A 91  ? 1.2574 0.8505 1.5220 0.3912  0.0755  -0.1327 131 ASP A OD2 
736  N N   . ALA A 92  ? 0.9935 0.8033 1.3424 0.4383  0.1353  -0.1795 132 ALA A N   
737  C CA  . ALA A 92  ? 0.9056 0.8025 1.3015 0.4392  0.1325  -0.1661 132 ALA A CA  
738  C C   . ALA A 92  ? 0.8751 0.7912 1.2949 0.4362  0.1033  -0.1350 132 ALA A C   
739  O O   . ALA A 92  ? 0.8456 0.8206 1.2873 0.4184  0.0944  -0.1271 132 ALA A O   
740  C CB  . ALA A 92  ? 0.9019 0.8418 1.3348 0.4730  0.1477  -0.1692 132 ALA A CB  
741  N N   . LYS A 93  ? 0.9248 0.7908 1.3369 0.4533  0.0879  -0.1170 133 LYS A N   
742  C CA  . LYS A 93  ? 0.9010 0.7808 1.3260 0.4500  0.0596  -0.0858 133 LYS A CA  
743  C C   . LYS A 93  ? 0.8217 0.6864 1.2212 0.4113  0.0481  -0.0856 133 LYS A C   
744  O O   . LYS A 93  ? 0.7854 0.6934 1.2007 0.3991  0.0282  -0.0682 133 LYS A O   
745  C CB  . LYS A 93  ? 1.0024 0.8228 1.4143 0.4763  0.0478  -0.0653 133 LYS A CB  
746  C CG  . LYS A 93  ? 1.0514 0.8855 1.4687 0.4735  0.0190  -0.0306 133 LYS A CG  
747  C CD  . LYS A 93  ? 1.1847 0.9461 1.5741 0.4937  0.0074  -0.0096 133 LYS A CD  
748  C CE  . LYS A 93  ? 1.2252 1.0031 1.6118 0.4874  -0.0201 0.0255  133 LYS A CE  
749  N NZ  . LYS A 93  ? 1.3657 1.0771 1.7223 0.5049  -0.0347 0.0467  133 LYS A NZ  
750  N N   . ALA A 94  ? 0.8376 0.6429 1.1962 0.3918  0.0591  -0.1061 134 ALA A N   
751  C CA  . ALA A 94  ? 0.7944 0.5881 1.1290 0.3561  0.0489  -0.1088 134 ALA A CA  
752  C C   . ALA A 94  ? 0.7729 0.6381 1.1241 0.3395  0.0509  -0.1171 134 ALA A C   
753  O O   . ALA A 94  ? 0.7134 0.6035 1.0537 0.3150  0.0337  -0.1005 134 ALA A O   
754  C CB  . ALA A 94  ? 0.8485 0.5738 1.1372 0.3385  0.0614  -0.1333 134 ALA A CB  
755  N N   . ILE A 95  ? 0.8416 0.7401 1.2007 0.3454  0.0741  -0.1370 135 ILE A N   
756  C CA  . ILE A 95  ? 0.7990 0.7647 1.1739 0.3297  0.0804  -0.1433 135 ILE A CA  
757  C C   . ILE A 95  ? 0.7536 0.7825 1.1718 0.3337  0.0613  -0.1189 135 ILE A C   
758  O O   . ILE A 95  ? 0.6751 0.7369 1.0838 0.3064  0.0504  -0.1088 135 ILE A O   
759  C CB  . ILE A 95  ? 0.8226 0.8115 1.1987 0.3376  0.1113  -0.1643 135 ILE A CB  
760  C CG1 . ILE A 95  ? 0.8581 0.7852 1.1812 0.3320  0.1279  -0.1886 135 ILE A CG1 
761  C CG2 . ILE A 95  ? 0.7527 0.8063 1.1424 0.3187  0.1211  -0.1682 135 ILE A CG2 
762  C CD1 . ILE A 95  ? 0.8409 0.7554 1.1218 0.3006  0.1271  -0.2008 135 ILE A CD1 
763  N N   . TYR A 96  ? 0.7936 0.8388 1.2453 0.3631  0.0566  -0.1056 136 TYR A N   
764  C CA  . TYR A 96  ? 0.7849 0.8947 1.2774 0.3688  0.0365  -0.0840 136 TYR A CA  
765  C C   . TYR A 96  ? 0.6890 0.7828 1.1665 0.3560  0.0058  -0.0622 136 TYR A C   
766  O O   . TYR A 96  ? 0.6580 0.8031 1.1460 0.3381  -0.0091 -0.0526 136 TYR A O   
767  C CB  . TYR A 96  ? 0.9042 1.0281 1.4272 0.4056  0.0370  -0.0728 136 TYR A CB  
768  C CG  . TYR A 96  ? 0.9332 1.1333 1.5007 0.4123  0.0180  -0.0535 136 TYR A CG  
769  C CD1 . TYR A 96  ? 0.9802 1.1746 1.5467 0.4237  -0.0108 -0.0251 136 TYR A CD1 
770  C CD2 . TYR A 96  ? 0.9673 1.2448 1.5749 0.4050  0.0295  -0.0633 136 TYR A CD2 
771  C CE1 . TYR A 96  ? 1.0325 1.2988 1.6367 0.4282  -0.0296 -0.0081 136 TYR A CE1 
772  C CE2 . TYR A 96  ? 1.0169 1.3657 1.6663 0.4073  0.0113  -0.0476 136 TYR A CE2 
773  C CZ  . TYR A 96  ? 1.0529 1.3970 1.7004 0.4191  -0.0193 -0.0206 136 TYR A CZ  
774  O OH  . TYR A 96  ? 1.0750 1.4907 1.7622 0.4196  -0.0391 -0.0057 136 TYR A OH  
775  N N   . ASP A 97  ? 0.7481 0.7681 1.1932 0.3610  -0.0021 -0.0529 137 ASP A N   
776  C CA  . ASP A 97  ? 0.7552 0.7539 1.1704 0.3430  -0.0267 -0.0283 137 ASP A CA  
777  C C   . ASP A 97  ? 0.7002 0.7055 1.0782 0.2999  -0.0260 -0.0343 137 ASP A C   
778  O O   . ASP A 97  ? 0.6828 0.7059 1.0484 0.2819  -0.0449 -0.0166 137 ASP A O   
779  C CB  . ASP A 97  ? 0.8316 0.7442 1.2175 0.3529  -0.0293 -0.0184 137 ASP A CB  
780  C CG  . ASP A 97  ? 0.9219 0.8222 1.3258 0.3919  -0.0308 -0.0029 137 ASP A CG  
781  O OD1 . ASP A 97  ? 0.9658 0.9266 1.4067 0.4124  -0.0279 -0.0032 137 ASP A OD1 
782  O OD2 . ASP A 97  ? 0.9994 0.8294 1.3754 0.3996  -0.0329 0.0106  137 ASP A OD2 
783  N N   . PHE A 98  ? 0.7230 0.7137 1.0806 0.2847  -0.0047 -0.0590 138 PHE A N   
784  C CA  . PHE A 98  ? 0.7043 0.7002 1.0263 0.2477  -0.0043 -0.0639 138 PHE A CA  
785  C C   . PHE A 98  ? 0.6215 0.6885 0.9660 0.2355  -0.0061 -0.0615 138 PHE A C   
786  O O   . PHE A 98  ? 0.5662 0.6470 0.8940 0.2119  -0.0194 -0.0505 138 PHE A O   
787  C CB  . PHE A 98  ? 0.6904 0.6538 0.9819 0.2379  0.0171  -0.0901 138 PHE A CB  
788  C CG  . PHE A 98  ? 0.6300 0.5962 0.8836 0.2045  0.0163  -0.0940 138 PHE A CG  
789  C CD1 . PHE A 98  ? 0.6672 0.5931 0.8857 0.1851  0.0043  -0.0888 138 PHE A CD1 
790  C CD2 . PHE A 98  ? 0.5901 0.5992 0.8448 0.1929  0.0284  -0.1020 138 PHE A CD2 
791  C CE1 . PHE A 98  ? 0.6152 0.5473 0.8025 0.1581  0.0026  -0.0922 138 PHE A CE1 
792  C CE2 . PHE A 98  ? 0.5342 0.5421 0.7529 0.1660  0.0273  -0.1036 138 PHE A CE2 
793  C CZ  . PHE A 98  ? 0.5377 0.5091 0.7239 0.1502  0.0134  -0.0989 138 PHE A CZ  
794  N N   . THR A 99  ? 0.5945 0.7067 0.9780 0.2501  0.0092  -0.0733 139 THR A N   
795  C CA  . THR A 99  ? 0.5359 0.7167 0.9478 0.2370  0.0089  -0.0723 139 THR A CA  
796  C C   . THR A 99  ? 0.5381 0.7511 0.9696 0.2381  -0.0199 -0.0507 139 THR A C   
797  O O   . THR A 99  ? 0.5061 0.7519 0.9345 0.2140  -0.0284 -0.0464 139 THR A O   
798  C CB  . THR A 99  ? 0.5522 0.7789 1.0117 0.2551  0.0308  -0.0879 139 THR A CB  
799  O OG1 . THR A 99  ? 0.5634 0.7620 0.9952 0.2502  0.0592  -0.1084 139 THR A OG1 
800  C CG2 . THR A 99  ? 0.5094 0.8099 1.0059 0.2397  0.0302  -0.0873 139 THR A CG2 
801  N N   . ASP A 100 ? 0.5722 0.7722 1.0196 0.2665  -0.0353 -0.0367 140 ASP A N   
802  C CA  . ASP A 100 ? 0.6052 0.8295 1.0606 0.2696  -0.0649 -0.0138 140 ASP A CA  
803  C C   . ASP A 100 ? 0.5518 0.7413 0.9549 0.2406  -0.0772 -0.0020 140 ASP A C   
804  O O   . ASP A 100 ? 0.5204 0.7447 0.9220 0.2259  -0.0947 0.0081  140 ASP A O   
805  C CB  . ASP A 100 ? 0.7921 0.9965 1.2656 0.3088  -0.0774 0.0018  140 ASP A CB  
806  C CG  . ASP A 100 ? 0.9395 1.1893 1.4333 0.3205  -0.1079 0.0238  140 ASP A CG  
807  O OD1 . ASP A 100 ? 0.9561 1.2586 1.4554 0.2973  -0.1182 0.0226  140 ASP A OD1 
808  O OD2 . ASP A 100 ? 1.0717 1.3003 1.5641 0.3485  -0.1177 0.0438  140 ASP A OD2 
809  N N   . THR A 101 ? 0.5474 0.6708 0.9086 0.2314  -0.0678 -0.0050 141 THR A N   
810  C CA  . THR A 101 ? 0.5395 0.6322 0.8555 0.2048  -0.0775 0.0052  141 THR A CA  
811  C C   . THR A 101 ? 0.5263 0.6491 0.8302 0.1738  -0.0718 -0.0055 141 THR A C   
812  O O   . THR A 101 ? 0.5082 0.6395 0.7929 0.1549  -0.0849 0.0047  141 THR A O   
813  C CB  . THR A 101 ? 0.5642 0.5845 0.8460 0.2017  -0.0683 0.0014  141 THR A CB  
814  O OG1 . THR A 101 ? 0.6668 0.6512 0.9580 0.2300  -0.0729 0.0135  141 THR A OG1 
815  C CG2 . THR A 101 ? 0.5641 0.5593 0.8054 0.1736  -0.0764 0.0105  141 THR A CG2 
816  N N   . VAL A 102 ? 0.5575 0.6933 0.8695 0.1692  -0.0510 -0.0256 142 VAL A N   
817  C CA  . VAL A 102 ? 0.5467 0.7069 0.8472 0.1424  -0.0433 -0.0340 142 VAL A CA  
818  C C   . VAL A 102 ? 0.4936 0.7104 0.8208 0.1349  -0.0566 -0.0271 142 VAL A C   
819  O O   . VAL A 102 ? 0.4574 0.6807 0.7647 0.1118  -0.0630 -0.0241 142 VAL A O   
820  C CB  . VAL A 102 ? 0.5075 0.6727 0.8129 0.1426  -0.0168 -0.0540 142 VAL A CB  
821  C CG1 . VAL A 102 ? 0.4332 0.6273 0.7337 0.1182  -0.0074 -0.0594 142 VAL A CG1 
822  C CG2 . VAL A 102 ? 0.5130 0.6221 0.7806 0.1432  -0.0064 -0.0636 142 VAL A CG2 
823  N N   . ILE A 103 ? 0.5021 0.7619 0.8759 0.1551  -0.0617 -0.0260 143 ILE A N   
824  C CA  . ILE A 103 ? 0.5045 0.8250 0.9084 0.1481  -0.0769 -0.0226 143 ILE A CA  
825  C C   . ILE A 103 ? 0.5379 0.8494 0.9160 0.1434  -0.1038 -0.0040 143 ILE A C   
826  O O   . ILE A 103 ? 0.5168 0.8547 0.8882 0.1219  -0.1132 -0.0043 143 ILE A O   
827  C CB  . ILE A 103 ? 0.4697 0.8426 0.9337 0.1744  -0.0786 -0.0259 143 ILE A CB  
828  C CG1 . ILE A 103 ? 0.4476 0.8377 0.9371 0.1730  -0.0477 -0.0462 143 ILE A CG1 
829  C CG2 . ILE A 103 ? 0.4318 0.8707 0.9284 0.1704  -0.1018 -0.0214 143 ILE A CG2 
830  C CD1 . ILE A 103 ? 0.4628 0.8911 1.0091 0.2050  -0.0427 -0.0514 143 ILE A CD1 
831  N N   . ARG A 104 ? 0.5408 0.8114 0.9011 0.1626  -0.1144 0.0120  144 ARG A N   
832  C CA  . ARG A 104 ? 0.5534 0.8098 0.8830 0.1586  -0.1366 0.0320  144 ARG A CA  
833  C C   . ARG A 104 ? 0.5262 0.7583 0.8125 0.1267  -0.1318 0.0293  144 ARG A C   
834  O O   . ARG A 104 ? 0.4991 0.7517 0.7710 0.1116  -0.1455 0.0347  144 ARG A O   
835  C CB  . ARG A 104 ? 0.6604 0.8649 0.9749 0.1829  -0.1423 0.0501  144 ARG A CB  
836  C CG  . ARG A 104 ? 0.7732 0.9593 1.0531 0.1813  -0.1630 0.0746  144 ARG A CG  
837  C CD  . ARG A 104 ? 0.8625 0.9872 1.1253 0.2033  -0.1641 0.0938  144 ARG A CD  
838  N NE  . ARG A 104 ? 0.9359 1.0546 1.2346 0.2341  -0.1562 0.0883  144 ARG A NE  
839  C CZ  . ARG A 104 ? 0.9888 1.0543 1.2821 0.2383  -0.1366 0.0784  144 ARG A CZ  
840  N NH1 . ARG A 104 ? 0.9912 1.0086 1.2472 0.2131  -0.1253 0.0733  144 ARG A NH1 
841  N NH2 . ARG A 104 ? 1.0022 1.0646 1.3287 0.2682  -0.1286 0.0718  144 ARG A NH2 
842  N N   . ILE A 105 ? 0.5231 0.7133 0.7881 0.1171  -0.1129 0.0195  145 ILE A N   
843  C CA  . ILE A 105 ? 0.4898 0.6589 0.7176 0.0904  -0.1081 0.0163  145 ILE A CA  
844  C C   . ILE A 105 ? 0.4897 0.6992 0.7252 0.0705  -0.1045 0.0048  145 ILE A C   
845  O O   . ILE A 105 ? 0.4994 0.7110 0.7121 0.0522  -0.1109 0.0074  145 ILE A O   
846  C CB  . ILE A 105 ? 0.4406 0.5641 0.6485 0.0870  -0.0906 0.0062  145 ILE A CB  
847  C CG1 . ILE A 105 ? 0.4514 0.5276 0.6468 0.1000  -0.0946 0.0171  145 ILE A CG1 
848  C CG2 . ILE A 105 ? 0.3855 0.4981 0.5625 0.0621  -0.0851 0.0003  145 ILE A CG2 
849  C CD1 . ILE A 105 ? 0.4721 0.5069 0.6543 0.0992  -0.0792 0.0031  145 ILE A CD1 
850  N N   . ARG A 106 ? 0.4560 0.6961 0.7239 0.0732  -0.0923 -0.0086 146 ARG A N   
851  C CA  . ARG A 106 ? 0.4396 0.7134 0.7170 0.0522  -0.0858 -0.0199 146 ARG A CA  
852  C C   . ARG A 106 ? 0.4713 0.7816 0.7551 0.0439  -0.1071 -0.0147 146 ARG A C   
853  O O   . ARG A 106 ? 0.4921 0.8038 0.7566 0.0218  -0.1073 -0.0191 146 ARG A O   
854  C CB  . ARG A 106 ? 0.3978 0.7038 0.7154 0.0570  -0.0686 -0.0333 146 ARG A CB  
855  C CG  . ARG A 106 ? 0.4530 0.7883 0.7809 0.0322  -0.0587 -0.0449 146 ARG A CG  
856  C CD  . ARG A 106 ? 0.5008 0.8642 0.8652 0.0323  -0.0358 -0.0580 146 ARG A CD  
857  N NE  . ARG A 106 ? 0.6197 1.0433 1.0402 0.0429  -0.0456 -0.0611 146 ARG A NE  
858  C CZ  . ARG A 106 ? 0.6426 1.1112 1.1073 0.0353  -0.0293 -0.0742 146 ARG A CZ  
859  N NH1 . ARG A 106 ? 0.6398 1.0930 1.0930 0.0163  -0.0009 -0.0832 146 ARG A NH1 
860  N NH2 . ARG A 106 ? 0.6465 1.1764 1.1670 0.0468  -0.0412 -0.0776 146 ARG A NH2 
861  N N   . ASN A 107 ? 0.4461 0.7855 0.7549 0.0630  -0.1258 -0.0056 147 ASN A N   
862  C CA  . ASN A 107 ? 0.4393 0.8170 0.7504 0.0566  -0.1491 -0.0013 147 ASN A CA  
863  C C   . ASN A 107 ? 0.4552 0.7978 0.7153 0.0485  -0.1600 0.0121  147 ASN A C   
864  O O   . ASN A 107 ? 0.4568 0.8156 0.7008 0.0295  -0.1679 0.0078  147 ASN A O   
865  C CB  . ASN A 107 ? 0.4854 0.9050 0.8346 0.0832  -0.1687 0.0069  147 ASN A CB  
866  C CG  . ASN A 107 ? 0.5423 1.0111 0.9498 0.0886  -0.1579 -0.0090 147 ASN A CG  
867  O OD1 . ASN A 107 ? 0.5916 1.0762 1.0120 0.0657  -0.1403 -0.0266 147 ASN A OD1 
868  N ND2 . ASN A 107 ? 0.5994 1.0912 1.0430 0.1195  -0.1667 -0.0024 147 ASN A ND2 
869  N N   . ARG A 108 ? 0.4959 0.7898 0.7304 0.0612  -0.1585 0.0268  148 ARG A N   
870  C CA  . ARG A 108 ? 0.5692 0.8301 0.7574 0.0518  -0.1647 0.0397  148 ARG A CA  
871  C C   . ARG A 108 ? 0.5273 0.7775 0.6918 0.0247  -0.1519 0.0269  148 ARG A C   
872  O O   . ARG A 108 ? 0.5534 0.8021 0.6884 0.0119  -0.1590 0.0309  148 ARG A O   
873  C CB  . ARG A 108 ? 0.6408 0.8478 0.8107 0.0652  -0.1595 0.0540  148 ARG A CB  
874  C CG  . ARG A 108 ? 0.6805 0.8532 0.8058 0.0541  -0.1624 0.0681  148 ARG A CG  
875  C CD  . ARG A 108 ? 0.7101 0.8271 0.8212 0.0618  -0.1538 0.0790  148 ARG A CD  
876  N NE  . ARG A 108 ? 0.7837 0.8888 0.9073 0.0889  -0.1630 0.0953  148 ARG A NE  
877  C CZ  . ARG A 108 ? 0.7975 0.8766 0.9403 0.1051  -0.1538 0.0917  148 ARG A CZ  
878  N NH1 . ARG A 108 ? 0.7158 0.7799 0.8644 0.0958  -0.1361 0.0721  148 ARG A NH1 
879  N NH2 . ARG A 108 ? 0.8092 0.8755 0.9630 0.1323  -0.1624 0.1076  148 ARG A NH2 
880  N N   . HIS A 109 ? 0.5986 0.8787 0.8103 0.1317  -0.0566 -0.0281 149 HIS A N   
881  C CA  . HIS A 109 ? 0.5638 0.8272 0.7372 0.0830  -0.0521 -0.0305 149 HIS A CA  
882  C C   . HIS A 109 ? 0.5008 0.8370 0.7062 0.0558  -0.0576 -0.0423 149 HIS A C   
883  O O   . HIS A 109 ? 0.4389 0.7572 0.6137 0.0187  -0.0511 -0.0439 149 HIS A O   
884  C CB  . HIS A 109 ? 0.4705 0.6867 0.6153 0.0622  -0.0212 -0.0444 149 HIS A CB  
885  C CG  . HIS A 109 ? 0.5336 0.6692 0.6371 0.0722  -0.0147 -0.0377 149 HIS A CG  
886  N ND1 . HIS A 109 ? 0.6216 0.7086 0.6787 0.0424  -0.0044 -0.0429 149 HIS A ND1 
887  C CD2 . HIS A 109 ? 0.6141 0.7072 0.7152 0.1070  -0.0162 -0.0272 149 HIS A CD2 
888  C CE1 . HIS A 109 ? 0.6359 0.6588 0.6687 0.0521  0.0016  -0.0402 149 HIS A CE1 
889  N NE2 . HIS A 109 ? 0.6308 0.6477 0.6856 0.0911  -0.0028 -0.0291 149 HIS A NE2 
890  N N   . ASN A 110 ? 0.4460 0.8637 0.7139 0.0735  -0.0696 -0.0515 150 ASN A N   
891  C CA  A ASN A 110 ? 0.3963 0.8871 0.7022 0.0411  -0.0708 -0.0691 150 ASN A CA  
892  C CA  B ASN A 110 ? 0.3959 0.8820 0.6987 0.0387  -0.0682 -0.0694 150 ASN A CA  
893  C C   . ASN A 110 ? 0.3855 0.8531 0.6468 0.0090  -0.0876 -0.0607 150 ASN A C   
894  O O   . ASN A 110 ? 0.4316 0.9162 0.6971 -0.0305 -0.0761 -0.0742 150 ASN A O   
895  C CB  A ASN A 110 ? 0.4049 0.9964 0.7877 0.0687  -0.0928 -0.0798 150 ASN A CB  
896  C CB  B ASN A 110 ? 0.3983 0.9908 0.7858 0.0609  -0.0818 -0.0853 150 ASN A CB  
897  C CG  A ASN A 110 ? 0.4099 1.0722 0.8676 0.0685  -0.0634 -0.1075 150 ASN A CG  
898  C CG  B ASN A 110 ? 0.4195 1.0339 0.8107 0.1029  -0.1261 -0.0674 150 ASN A CG  
899  O OD1 A ASN A 110 ? 0.3924 1.0449 0.8441 0.0291  -0.0273 -0.1224 150 ASN A OD1 
900  O OD1 B ASN A 110 ? 0.4280 0.9837 0.7555 0.1039  -0.1456 -0.0449 150 ASN A OD1 
901  N ND2 A ASN A 110 ? 0.4711 1.2064 0.9991 0.1146  -0.0776 -0.1138 150 ASN A ND2 
902  N ND2 B ASN A 110 ? 0.4749 1.1776 0.9408 0.1397  -0.1415 -0.0772 150 ASN A ND2 
903  N N   . ASP A 111 ? 0.3915 0.8159 0.6082 0.0254  -0.1110 -0.0392 151 ASP A N   
904  C CA  . ASP A 111 ? 0.3915 0.8012 0.5702 0.0007  -0.1267 -0.0342 151 ASP A CA  
905  C C   . ASP A 111 ? 0.4110 0.7374 0.5280 -0.0125 -0.1153 -0.0202 151 ASP A C   
906  O O   . ASP A 111 ? 0.4056 0.7096 0.4864 -0.0207 -0.1276 -0.0120 151 ASP A O   
907  C CB  . ASP A 111 ? 0.5332 0.9726 0.7076 0.0259  -0.1630 -0.0237 151 ASP A CB  
908  C CG  . ASP A 111 ? 0.6919 1.1660 0.8598 -0.0043 -0.1796 -0.0369 151 ASP A CG  
909  O OD1 . ASP A 111 ? 0.7707 1.2998 0.9834 -0.0323 -0.1724 -0.0621 151 ASP A OD1 
910  O OD2 . ASP A 111 ? 0.7326 1.1754 0.8483 -0.0034 -0.1959 -0.0246 151 ASP A OD2 
911  N N   . VAL A 112 ? 0.4068 0.6935 0.5130 -0.0158 -0.0918 -0.0204 152 VAL A N   
912  C CA  . VAL A 112 ? 0.3998 0.6217 0.4577 -0.0254 -0.0852 -0.0097 152 VAL A CA  
913  C C   . VAL A 112 ? 0.4187 0.6309 0.4555 -0.0536 -0.0848 -0.0116 152 VAL A C   
914  O O   . VAL A 112 ? 0.4392 0.6219 0.4466 -0.0563 -0.0913 -0.0026 152 VAL A O   
915  C CB  . VAL A 112 ? 0.4345 0.6261 0.4849 -0.0255 -0.0639 -0.0150 152 VAL A CB  
916  C CG1 . VAL A 112 ? 0.4575 0.6063 0.4682 -0.0447 -0.0595 -0.0111 152 VAL A CG1 
917  C CG2 . VAL A 112 ? 0.5290 0.6967 0.5817 0.0035  -0.0626 -0.0100 152 VAL A CG2 
918  N N   . ILE A 113 ? 0.4364 0.6686 0.4875 -0.0750 -0.0730 -0.0238 153 ILE A N   
919  C CA  . ILE A 113 ? 0.4348 0.6406 0.4605 -0.0986 -0.0683 -0.0240 153 ILE A CA  
920  C C   . ILE A 113 ? 0.4177 0.6307 0.4372 -0.1028 -0.0844 -0.0258 153 ILE A C   
921  O O   . ILE A 113 ? 0.4240 0.6001 0.4133 -0.1041 -0.0855 -0.0190 153 ILE A O   
922  C CB  . ILE A 113 ? 0.4097 0.6220 0.4441 -0.1231 -0.0469 -0.0346 153 ILE A CB  
923  C CG1 . ILE A 113 ? 0.4311 0.6165 0.4448 -0.1211 -0.0291 -0.0299 153 ILE A CG1 
924  C CG2 . ILE A 113 ? 0.4259 0.6046 0.4354 -0.1453 -0.0418 -0.0349 153 ILE A CG2 
925  C CD1 . ILE A 113 ? 0.4746 0.6462 0.4746 -0.1472 -0.0031 -0.0338 153 ILE A CD1 
926  N N   . PRO A 114 ? 0.4487 0.7121 0.4949 -0.1043 -0.0979 -0.0369 154 PRO A N   
927  C CA  . PRO A 114 ? 0.4588 0.7251 0.4856 -0.1101 -0.1141 -0.0410 154 PRO A CA  
928  C C   . PRO A 114 ? 0.4499 0.6941 0.4446 -0.0866 -0.1273 -0.0236 154 PRO A C   
929  O O   . PRO A 114 ? 0.4468 0.6703 0.4090 -0.0934 -0.1301 -0.0244 154 PRO A O   
930  C CB  . PRO A 114 ? 0.4671 0.8054 0.5334 -0.1178 -0.1295 -0.0598 154 PRO A CB  
931  C CG  . PRO A 114 ? 0.5375 0.9149 0.6485 -0.1010 -0.1259 -0.0591 154 PRO A CG  
932  C CD  . PRO A 114 ? 0.4630 0.7899 0.5602 -0.1044 -0.0982 -0.0508 154 PRO A CD  
933  N N   . THR A 115 ? 0.4648 0.7057 0.4640 -0.0610 -0.1305 -0.0089 155 THR A N   
934  C CA  . THR A 115 ? 0.5227 0.7298 0.4849 -0.0441 -0.1363 0.0094  155 THR A CA  
935  C C   . THR A 115 ? 0.4463 0.6049 0.3848 -0.0551 -0.1185 0.0139  155 THR A C   
936  O O   . THR A 115 ? 0.4861 0.6232 0.3932 -0.0573 -0.1172 0.0195  155 THR A O   
937  C CB  . THR A 115 ? 0.5325 0.7354 0.5031 -0.0142 -0.1406 0.0238  155 THR A CB  
938  O OG1 . THR A 115 ? 0.4861 0.7471 0.4891 0.0026  -0.1604 0.0188  155 THR A OG1 
939  C CG2 . THR A 115 ? 0.5128 0.6699 0.4367 -0.0006 -0.1425 0.0452  155 THR A CG2 
940  N N   . MET A 116 ? 0.4065 0.5528 0.3596 -0.0617 -0.1049 0.0104  156 MET A N   
941  C CA  . MET A 116 ? 0.4603 0.5765 0.3999 -0.0702 -0.0939 0.0118  156 MET A CA  
942  C C   . MET A 116 ? 0.4716 0.5840 0.4004 -0.0821 -0.0920 0.0042  156 MET A C   
943  O O   . MET A 116 ? 0.4706 0.5670 0.3856 -0.0823 -0.0864 0.0058  156 MET A O   
944  C CB  . MET A 116 ? 0.4447 0.5541 0.3945 -0.0736 -0.0855 0.0090  156 MET A CB  
945  C CG  . MET A 116 ? 0.4612 0.5519 0.4018 -0.0780 -0.0813 0.0101  156 MET A CG  
946  S SD  . MET A 116 ? 0.4883 0.5683 0.4253 -0.0761 -0.0788 0.0143  156 MET A SD  
947  C CE  . MET A 116 ? 0.4955 0.5634 0.4351 -0.0744 -0.0752 0.0133  156 MET A CE  
948  N N   . ALA A 117 ? 0.4405 0.5663 0.3774 -0.0937 -0.0929 -0.0069 157 ALA A N   
949  C CA  . ALA A 117 ? 0.4819 0.5935 0.4049 -0.1064 -0.0881 -0.0178 157 ALA A CA  
950  C C   . ALA A 117 ? 0.5068 0.6234 0.4067 -0.1050 -0.0949 -0.0212 157 ALA A C   
951  O O   . ALA A 117 ? 0.5201 0.6148 0.4018 -0.1093 -0.0854 -0.0285 157 ALA A O   
952  C CB  . ALA A 117 ? 0.5345 0.6568 0.4699 -0.1262 -0.0850 -0.0324 157 ALA A CB  
953  N N   . GLN A 118 ? 0.5337 0.6767 0.4299 -0.0965 -0.1105 -0.0157 158 GLN A N   
954  C CA  . GLN A 118 ? 0.5601 0.7024 0.4190 -0.0938 -0.1177 -0.0145 158 GLN A CA  
955  C C   . GLN A 118 ? 0.5615 0.6704 0.3986 -0.0873 -0.1017 -0.0020 158 GLN A C   
956  O O   . GLN A 118 ? 0.5955 0.6917 0.3985 -0.0923 -0.0940 -0.0065 158 GLN A O   
957  C CB  . GLN A 118 ? 0.5109 0.6857 0.3655 -0.0789 -0.1416 -0.0054 158 GLN A CB  
958  C CG  . GLN A 118 ? 0.6418 0.8169 0.4441 -0.0764 -0.1537 -0.0032 158 GLN A CG  
959  C CD  . GLN A 118 ? 0.7449 0.9372 0.5345 -0.0999 -0.1582 -0.0315 158 GLN A CD  
960  O OE1 . GLN A 118 ? 0.7523 0.9822 0.5760 -0.1133 -0.1688 -0.0505 158 GLN A OE1 
961  N NE2 . GLN A 118 ? 0.7724 0.9357 0.5134 -0.1084 -0.1458 -0.0378 158 GLN A NE2 
962  N N   . GLY A 119 ? 0.5669 0.6639 0.4236 -0.0798 -0.0941 0.0101  159 GLY A N   
963  C CA  . GLY A 119 ? 0.6290 0.7036 0.4764 -0.0801 -0.0769 0.0171  159 GLY A CA  
964  C C   . GLY A 119 ? 0.5454 0.6164 0.4035 -0.0869 -0.0619 0.0039  159 GLY A C   
965  O O   . GLY A 119 ? 0.5364 0.6002 0.3820 -0.0901 -0.0454 0.0019  159 GLY A O   
966  N N   . VAL A 120 ? 0.4676 0.5412 0.3481 -0.0874 -0.0647 -0.0046 160 VAL A N   
967  C CA  . VAL A 120 ? 0.5057 0.5692 0.3950 -0.0858 -0.0522 -0.0151 160 VAL A CA  
968  C C   . VAL A 120 ? 0.5113 0.5645 0.3723 -0.0924 -0.0434 -0.0299 160 VAL A C   
969  O O   . VAL A 120 ? 0.5729 0.6184 0.4343 -0.0886 -0.0257 -0.0392 160 VAL A O   
970  C CB  . VAL A 120 ? 0.5166 0.5699 0.4217 -0.0831 -0.0566 -0.0157 160 VAL A CB  
971  C CG1 . VAL A 120 ? 0.4793 0.5132 0.3912 -0.0729 -0.0450 -0.0226 160 VAL A CG1 
972  C CG2 . VAL A 120 ? 0.5146 0.5784 0.4369 -0.0782 -0.0649 -0.0039 160 VAL A CG2 
973  N N   . ILE A 121 ? 0.5407 0.5987 0.3789 -0.1025 -0.0554 -0.0358 161 ILE A N   
974  C CA  . ILE A 121 ? 0.5713 0.6216 0.3728 -0.1127 -0.0499 -0.0539 161 ILE A CA  
975  C C   . ILE A 121 ? 0.5931 0.6421 0.3623 -0.1100 -0.0386 -0.0479 161 ILE A C   
976  O O   . ILE A 121 ? 0.6052 0.6402 0.3547 -0.1131 -0.0176 -0.0627 161 ILE A O   
977  C CB  . ILE A 121 ? 0.6118 0.6826 0.3993 -0.1259 -0.0716 -0.0633 161 ILE A CB  
978  C CG1 . ILE A 121 ? 0.6325 0.6996 0.4509 -0.1368 -0.0726 -0.0733 161 ILE A CG1 
979  C CG2 . ILE A 121 ? 0.6832 0.7511 0.4223 -0.1388 -0.0709 -0.0841 161 ILE A CG2 
980  C CD1 . ILE A 121 ? 0.6653 0.7679 0.4872 -0.1540 -0.0923 -0.0867 161 ILE A CD1 
981  N N   . GLU A 122 ? 0.6029 0.6604 0.3638 -0.1043 -0.0480 -0.0262 162 GLU A N   
982  C CA  . GLU A 122 ? 0.6422 0.6872 0.3635 -0.1052 -0.0328 -0.0159 162 GLU A CA  
983  C C   . GLU A 122 ? 0.6216 0.6623 0.3698 -0.1066 -0.0020 -0.0214 162 GLU A C   
984  O O   . GLU A 122 ? 0.6776 0.7100 0.3969 -0.1133 0.0228  -0.0294 162 GLU A O   
985  C CB  . GLU A 122 ? 0.6744 0.7145 0.3840 -0.0967 -0.0455 0.0112  162 GLU A CB  
986  C CG  . GLU A 122 ? 0.7287 0.7805 0.4054 -0.0885 -0.0762 0.0192  162 GLU A CG  
987  C CD  . GLU A 122 ? 0.7814 0.8352 0.4796 -0.0715 -0.0929 0.0406  162 GLU A CD  
988  O OE1 . GLU A 122 ? 0.8431 0.9223 0.5392 -0.0596 -0.1212 0.0435  162 GLU A OE1 
989  O OE2 . GLU A 122 ? 0.7415 0.7749 0.4620 -0.0700 -0.0776 0.0511  162 GLU A OE2 
990  N N   . TYR A 123 ? 0.5704 0.6226 0.3744 -0.1005 -0.0034 -0.0190 163 TYR A N   
991  C CA  . TYR A 123 ? 0.5828 0.6484 0.4279 -0.0986 0.0185  -0.0268 163 TYR A CA  
992  C C   . TYR A 123 ? 0.5561 0.6202 0.4059 -0.0931 0.0354  -0.0490 163 TYR A C   
993  O O   . TYR A 123 ? 0.5874 0.6595 0.4406 -0.0952 0.0638  -0.0600 163 TYR A O   
994  C CB  . TYR A 123 ? 0.4778 0.5597 0.3738 -0.0906 0.0033  -0.0214 163 TYR A CB  
995  C CG  . TYR A 123 ? 0.4856 0.5960 0.4342 -0.0834 0.0145  -0.0308 163 TYR A CG  
996  C CD1 . TYR A 123 ? 0.5525 0.6844 0.5200 -0.0939 0.0380  -0.0359 163 TYR A CD1 
997  C CD2 . TYR A 123 ? 0.4664 0.5850 0.4470 -0.0660 0.0009  -0.0339 163 TYR A CD2 
998  C CE1 . TYR A 123 ? 0.5280 0.7035 0.5569 -0.0865 0.0449  -0.0481 163 TYR A CE1 
999  C CE2 . TYR A 123 ? 0.4290 0.5831 0.4609 -0.0530 0.0040  -0.0412 163 TYR A CE2 
1000 C CZ  . TYR A 123 ? 0.4784 0.6682 0.5404 -0.0630 0.0244  -0.0503 163 TYR A CZ  
1001 O OH  . TYR A 123 ? 0.5655 0.8071 0.6907 -0.0493 0.0246  -0.0612 163 TYR A OH  
1002 N N   . LYS A 124 ? 0.5695 0.6193 0.4195 -0.0870 0.0225  -0.0575 164 LYS A N   
1003 C CA  . LYS A 124 ? 0.7260 0.7591 0.5775 -0.0796 0.0404  -0.0797 164 LYS A CA  
1004 C C   . LYS A 124 ? 0.8478 0.8674 0.6458 -0.0925 0.0602  -0.0970 164 LYS A C   
1005 O O   . LYS A 124 ? 0.8061 0.8187 0.6079 -0.0861 0.0885  -0.1174 164 LYS A O   
1006 C CB  . LYS A 124 ? 0.7037 0.7100 0.5560 -0.0771 0.0252  -0.0835 164 LYS A CB  
1007 C CG  . LYS A 124 ? 0.7386 0.7159 0.6093 -0.0594 0.0417  -0.0982 164 LYS A CG  
1008 C CD  . LYS A 124 ? 0.7031 0.6453 0.5734 -0.0591 0.0284  -0.0931 164 LYS A CD  
1009 C CE  . LYS A 124 ? 0.7773 0.6640 0.6382 -0.0497 0.0492  -0.1126 164 LYS A CE  
1010 N NZ  . LYS A 124 ? 0.8014 0.6395 0.6465 -0.0611 0.0436  -0.1106 164 LYS A NZ  
1011 N N   . GLU A 125 ? 0.9357 0.9528 0.6812 -0.1079 0.0455  -0.0897 165 GLU A N   
1012 C CA  . GLU A 125 ? 1.0005 1.0043 0.6793 -0.1210 0.0590  -0.1052 165 GLU A CA  
1013 C C   . GLU A 125 ? 1.0092 1.0169 0.6758 -0.1229 0.0947  -0.1050 165 GLU A C   
1014 O O   . GLU A 125 ? 1.1096 1.1046 0.7437 -0.1279 0.1235  -0.1288 165 GLU A O   
1015 C CB  . GLU A 125 ? 1.0617 1.0702 0.6876 -0.1311 0.0283  -0.0920 165 GLU A CB  
1016 C CG  . GLU A 125 ? 1.1896 1.2005 0.8089 -0.1401 0.0017  -0.1085 165 GLU A CG  
1017 C CD  . GLU A 125 ? 1.2865 1.3208 0.8690 -0.1438 -0.0340 -0.0948 165 GLU A CD  
1018 O OE1 . GLU A 125 ? 1.2788 1.3157 0.8405 -0.1340 -0.0388 -0.0664 165 GLU A OE1 
1019 O OE2 . GLU A 125 ? 1.3184 1.3686 0.8950 -0.1559 -0.0569 -0.1130 165 GLU A OE2 
1020 N N   . SER A 126 ? 0.9722 0.9952 0.6630 -0.1224 0.0976  -0.0817 166 SER A N   
1021 C CA  . SER A 126 ? 1.0938 1.1169 0.7607 -0.1337 0.1330  -0.0780 166 SER A CA  
1022 C C   . SER A 126 ? 1.0794 1.1346 0.8221 -0.1291 0.1645  -0.0902 166 SER A C   
1023 O O   . SER A 126 ? 1.1462 1.2082 0.8792 -0.1426 0.2027  -0.0939 166 SER A O   
1024 C CB  . SER A 126 ? 1.2004 1.2102 0.8340 -0.1419 0.1211  -0.0448 166 SER A CB  
1025 O OG  . SER A 126 ? 1.2401 1.2371 0.8319 -0.1364 0.0813  -0.0319 166 SER A OG  
1026 N N   . PHE A 127 ? 1.0285 1.1067 0.8453 -0.1103 0.1496  -0.0964 167 PHE A N   
1027 C CA  . PHE A 127 ? 1.0709 1.1944 0.9688 -0.1010 0.1702  -0.1072 167 PHE A CA  
1028 C C   . PHE A 127 ? 1.1794 1.3132 1.1309 -0.0707 0.1644  -0.1240 167 PHE A C   
1029 O O   . PHE A 127 ? 1.1482 1.3271 1.1703 -0.0554 0.1807  -0.1364 167 PHE A O   
1030 C CB  . PHE A 127 ? 0.9997 1.1501 0.9415 -0.1080 0.1531  -0.0882 167 PHE A CB  
1031 C CG  . PHE A 127 ? 0.9986 1.1199 0.8832 -0.1326 0.1543  -0.0662 167 PHE A CG  
1032 C CD1 . PHE A 127 ? 1.0815 1.2041 0.9514 -0.1564 0.1932  -0.0658 167 PHE A CD1 
1033 C CD2 . PHE A 127 ? 0.9543 1.0436 0.7990 -0.1306 0.1196  -0.0452 167 PHE A CD2 
1034 C CE1 . PHE A 127 ? 1.1222 1.2019 0.9296 -0.1758 0.1963  -0.0408 167 PHE A CE1 
1035 C CE2 . PHE A 127 ? 1.0245 1.0810 0.8160 -0.1449 0.1198  -0.0224 167 PHE A CE2 
1036 C CZ  . PHE A 127 ? 1.0998 1.1449 0.8678 -0.1665 0.1576  -0.0181 167 PHE A CZ  
1037 N N   . GLY A 128 ? 1.3244 1.4183 1.2469 -0.0613 0.1427  -0.1248 168 GLY A N   
1038 C CA  . GLY A 128 ? 1.5051 1.5880 1.4646 -0.0320 0.1411  -0.1372 168 GLY A CA  
1039 C C   . GLY A 128 ? 1.6110 1.7199 1.6307 -0.0108 0.1127  -0.1200 168 GLY A C   
1040 O O   . GLY A 128 ? 1.5067 1.6461 1.5439 -0.0215 0.0945  -0.1028 168 GLY A O   
1041 N N   . VAL A 129 ? 1.8023 1.8918 1.8472 0.0208  0.1097  -0.1251 169 VAL A N   
1042 C CA  . VAL A 129 ? 1.7423 1.8530 1.8346 0.0468  0.0814  -0.1076 169 VAL A CA  
1043 C C   . VAL A 129 ? 1.6256 1.8156 1.7953 0.0632  0.0882  -0.1147 169 VAL A C   
1044 O O   . VAL A 129 ? 1.6742 1.8876 1.8778 0.0779  0.1191  -0.1365 169 VAL A O   
1045 C CB  . VAL A 129 ? 1.8388 1.8902 1.9216 0.0778  0.0767  -0.1057 169 VAL A CB  
1046 C CG1 . VAL A 129 ? 1.8986 1.9375 2.0034 0.1062  0.1102  -0.1307 169 VAL A CG1 
1047 C CG2 . VAL A 129 ? 1.8299 1.8953 1.9425 0.1052  0.0436  -0.0816 169 VAL A CG2 
1048 N N   . ASP A 130 ? 1.4738 1.7101 1.6738 0.0572  0.0616  -0.1003 170 ASP A N   
1049 C CA  . ASP A 130 ? 1.3282 1.6518 1.6100 0.0684  0.0607  -0.1096 170 ASP A CA  
1050 C C   . ASP A 130 ? 1.3858 1.7286 1.6999 0.1056  0.0213  -0.0953 170 ASP A C   
1051 O O   . ASP A 130 ? 1.3379 1.6686 1.6243 0.0945  -0.0096 -0.0768 170 ASP A O   
1052 C CB  . ASP A 130 ? 1.1688 1.5306 1.4557 0.0254  0.0632  -0.1092 170 ASP A CB  
1053 C CG  . ASP A 130 ? 1.0932 1.5529 1.4705 0.0257  0.0661  -0.1256 170 ASP A CG  
1054 O OD1 . ASP A 130 ? 1.0686 1.5792 1.5112 0.0652  0.0584  -0.1352 170 ASP A OD1 
1055 O OD2 . ASP A 130 ? 1.0620 1.5482 1.4468 -0.0140 0.0764  -0.1296 170 ASP A OD2 
1056 N N   . PRO A 131 ? 1.2876 1.4299 1.5832 -0.0675 0.1610  -0.2059 171 PRO A N   
1057 C CA  . PRO A 131 ? 1.2881 1.4598 1.6272 -0.0440 0.1379  -0.1991 171 PRO A CA  
1058 C C   . PRO A 131 ? 1.2685 1.4582 1.6232 -0.0384 0.1197  -0.1965 171 PRO A C   
1059 O O   . PRO A 131 ? 1.2540 1.4569 1.6189 -0.0205 0.0949  -0.1846 171 PRO A O   
1060 C CB  . PRO A 131 ? 1.3137 1.5053 1.7131 -0.0416 0.1529  -0.2156 171 PRO A CB  
1061 C CG  . PRO A 131 ? 1.3298 1.5115 1.7284 -0.0654 0.1847  -0.2349 171 PRO A CG  
1062 C CD  . PRO A 131 ? 1.3294 1.4732 1.6532 -0.0813 0.1910  -0.2265 171 PRO A CD  
1063 N N   . VAL A 132 ? 1.2733 1.4620 1.6274 -0.0543 0.1314  -0.2073 172 VAL A N   
1064 C CA  . VAL A 132 ? 1.2802 1.4839 1.6461 -0.0504 0.1143  -0.2051 172 VAL A CA  
1065 C C   . VAL A 132 ? 1.2790 1.4640 1.5901 -0.0463 0.0956  -0.1870 172 VAL A C   
1066 O O   . VAL A 132 ? 1.2966 1.4933 1.6127 -0.0315 0.0719  -0.1766 172 VAL A O   
1067 C CB  . VAL A 132 ? 1.2873 1.4943 1.6685 -0.0701 0.1337  -0.2227 172 VAL A CB  
1068 C CG1 . VAL A 132 ? 1.2658 1.4941 1.6724 -0.0648 0.1154  -0.2227 172 VAL A CG1 
1069 C CG2 . VAL A 132 ? 1.2801 1.5009 1.7112 -0.0772 0.1587  -0.2427 172 VAL A CG2 
1070 N N   . THR A 133 ? 1.2559 1.4098 1.5137 -0.0597 0.1058  -0.1834 173 THR A N   
1071 C CA  . THR A 133 ? 1.1599 1.2952 1.3696 -0.0565 0.0892  -0.1680 173 THR A CA  
1072 C C   . THR A 133 ? 1.0466 1.1795 1.2426 -0.0393 0.0731  -0.1524 173 THR A C   
1073 O O   . THR A 133 ? 1.0437 1.1737 1.2193 -0.0300 0.0547  -0.1404 173 THR A O   
1074 C CB  . THR A 133 ? 1.1483 1.2487 1.3070 -0.0766 0.1027  -0.1688 173 THR A CB  
1075 O OG1 . THR A 133 ? 1.1663 1.2480 1.3046 -0.0815 0.1145  -0.1676 173 THR A OG1 
1076 C CG2 . THR A 133 ? 1.1077 1.2078 1.2771 -0.0964 0.1219  -0.1852 173 THR A CG2 
1077 N N   . SER A 134 ? 0.9516 1.0853 1.1591 -0.0355 0.0807  -0.1533 174 SER A N   
1078 C CA  . SER A 134 ? 0.9013 1.0283 1.0903 -0.0223 0.0684  -0.1389 174 SER A CA  
1079 C C   . SER A 134 ? 0.7840 0.9305 0.9904 -0.0033 0.0454  -0.1291 174 SER A C   
1080 O O   . SER A 134 ? 0.6747 0.8133 0.8566 0.0059  0.0327  -0.1159 174 SER A O   
1081 C CB  . SER A 134 ? 0.9459 1.0717 1.1488 -0.0222 0.0816  -0.1433 174 SER A CB  
1082 O OG  . SER A 134 ? 0.9749 1.1264 1.2328 -0.0168 0.0861  -0.1545 174 SER A OG  
1083 N N   . GLN A 135 ? 0.7194 0.8903 0.9676 0.0019  0.0396  -0.1358 175 GLN A N   
1084 C CA  . GLN A 135 ? 0.6703 0.8548 0.9271 0.0169  0.0164  -0.1264 175 GLN A CA  
1085 C C   . GLN A 135 ? 0.5540 0.7277 0.7752 0.0147  0.0067  -0.1196 175 GLN A C   
1086 O O   . GLN A 135 ? 0.4722 0.6440 0.6763 0.0251  -0.0088 -0.1080 175 GLN A O   
1087 C CB  . GLN A 135 ? 0.7608 0.9713 1.0695 0.0213  0.0100  -0.1353 175 GLN A CB  
1088 C CG  . GLN A 135 ? 0.8920 1.1155 1.2438 0.0272  0.0154  -0.1416 175 GLN A CG  
1089 C CD  . GLN A 135 ? 0.9897 1.2389 1.3988 0.0295  0.0102  -0.1529 175 GLN A CD  
1090 O OE1 . GLN A 135 ? 1.0041 1.2637 1.4530 0.0248  0.0260  -0.1672 175 GLN A OE1 
1091 N NE2 . GLN A 135 ? 1.0023 1.2613 1.4167 0.0363  -0.0121 -0.1474 175 GLN A NE2 
1092 N N   . ASN A 136 ? 0.4400 0.6053 0.6496 0.0005  0.0167  -0.1272 176 ASN A N   
1093 C CA  . ASN A 136 ? 0.4207 0.5732 0.5966 -0.0020 0.0083  -0.1215 176 ASN A CA  
1094 C C   . ASN A 136 ? 0.4004 0.5295 0.5344 -0.0008 0.0070  -0.1106 176 ASN A C   
1095 O O   . ASN A 136 ? 0.4277 0.5508 0.5406 0.0053  -0.0054 -0.1023 176 ASN A O   
1096 C CB  . ASN A 136 ? 0.4008 0.5475 0.5739 -0.0186 0.0195  -0.1324 176 ASN A CB  
1097 C CG  . ASN A 136 ? 0.4718 0.6427 0.6849 -0.0186 0.0154  -0.1418 176 ASN A CG  
1098 O OD1 . ASN A 136 ? 0.5291 0.7202 0.7729 -0.0062 0.0030  -0.1400 176 ASN A OD1 
1099 N ND2 . ASN A 136 ? 0.4766 0.6442 0.6896 -0.0332 0.0248  -0.1516 176 ASN A ND2 
1100 N N   . VAL A 137 ? 0.3503 0.4654 0.4727 -0.0071 0.0195  -0.1111 177 VAL A N   
1101 C CA  . VAL A 137 ? 0.3672 0.4601 0.4527 -0.0062 0.0162  -0.1007 177 VAL A CA  
1102 C C   . VAL A 137 ? 0.2995 0.4016 0.3885 0.0107  0.0026  -0.0899 177 VAL A C   
1103 O O   . VAL A 137 ? 0.3303 0.4228 0.3966 0.0157  -0.0070 -0.0813 177 VAL A O   
1104 C CB  . VAL A 137 ? 0.4804 0.5549 0.5514 -0.0179 0.0316  -0.1038 177 VAL A CB  
1105 C CG1 . VAL A 137 ? 0.4186 0.4724 0.4568 -0.0152 0.0247  -0.0922 177 VAL A CG1 
1106 C CG2 . VAL A 137 ? 0.4726 0.5314 0.5298 -0.0374 0.0455  -0.1138 177 VAL A CG2 
1107 N N   . GLN A 138 ? 0.3418 0.4616 0.4599 0.0192  0.0018  -0.0906 178 GLN A N   
1108 C CA  . GLN A 138 ? 0.3408 0.4678 0.4607 0.0338  -0.0109 -0.0805 178 GLN A CA  
1109 C C   . GLN A 138 ? 0.3535 0.4869 0.4683 0.0403  -0.0252 -0.0763 178 GLN A C   
1110 O O   . GLN A 138 ? 0.3398 0.4673 0.4357 0.0470  -0.0330 -0.0676 178 GLN A O   
1111 C CB  . GLN A 138 ? 0.3139 0.4573 0.4677 0.0408  -0.0106 -0.0827 178 GLN A CB  
1112 C CG  . GLN A 138 ? 0.3681 0.5161 0.5214 0.0544  -0.0235 -0.0719 178 GLN A CG  
1113 C CD  . GLN A 138 ? 0.4058 0.5393 0.5366 0.0555  -0.0198 -0.0643 178 GLN A CD  
1114 O OE1 . GLN A 138 ? 0.3597 0.4808 0.4804 0.0468  -0.0078 -0.0676 178 GLN A OE1 
1115 N NE2 . GLN A 138 ? 0.3690 0.5027 0.4904 0.0649  -0.0299 -0.0544 178 GLN A NE2 
1116 N N   . TYR A 139 ? 0.2843 0.4292 0.4163 0.0377  -0.0280 -0.0833 179 TYR A N   
1117 C CA  . TYR A 139 ? 0.2758 0.4245 0.4005 0.0419  -0.0412 -0.0805 179 TYR A CA  
1118 C C   . TYR A 139 ? 0.3105 0.4416 0.4020 0.0382  -0.0410 -0.0775 179 TYR A C   
1119 O O   . TYR A 139 ? 0.3180 0.4458 0.3940 0.0449  -0.0496 -0.0712 179 TYR A O   
1120 C CB  . TYR A 139 ? 0.3086 0.4716 0.4588 0.0375  -0.0436 -0.0898 179 TYR A CB  
1121 C CG  . TYR A 139 ? 0.3416 0.5081 0.4851 0.0400  -0.0576 -0.0884 179 TYR A CG  
1122 C CD1 . TYR A 139 ? 0.3272 0.5022 0.4769 0.0495  -0.0729 -0.0828 179 TYR A CD1 
1123 C CD2 . TYR A 139 ? 0.3286 0.4877 0.4579 0.0315  -0.0558 -0.0932 179 TYR A CD2 
1124 C CE1 . TYR A 139 ? 0.3361 0.5116 0.4759 0.0500  -0.0854 -0.0820 179 TYR A CE1 
1125 C CE2 . TYR A 139 ? 0.3391 0.5001 0.4612 0.0329  -0.0678 -0.0928 179 TYR A CE2 
1126 C CZ  . TYR A 139 ? 0.3244 0.4935 0.4510 0.0418  -0.0824 -0.0874 179 TYR A CZ  
1127 O OH  . TYR A 139 ? 0.3697 0.5378 0.4849 0.0415  -0.0942 -0.0874 179 TYR A OH  
1128 N N   . PHE A 140 ? 0.3055 0.4231 0.3854 0.0270  -0.0310 -0.0822 180 PHE A N   
1129 C CA  . PHE A 140 ? 0.3408 0.4394 0.3913 0.0236  -0.0329 -0.0794 180 PHE A CA  
1130 C C   . PHE A 140 ? 0.3464 0.4348 0.3802 0.0309  -0.0363 -0.0701 180 PHE A C   
1131 O O   . PHE A 140 ? 0.3744 0.4571 0.3948 0.0357  -0.0432 -0.0663 180 PHE A O   
1132 C CB  . PHE A 140 ? 0.3473 0.4293 0.3856 0.0087  -0.0226 -0.0853 180 PHE A CB  
1133 C CG  . PHE A 140 ? 0.3950 0.4527 0.4024 0.0053  -0.0260 -0.0809 180 PHE A CG  
1134 C CD1 . PHE A 140 ? 0.4109 0.4632 0.4086 0.0043  -0.0322 -0.0824 180 PHE A CD1 
1135 C CD2 . PHE A 140 ? 0.4240 0.4633 0.4133 0.0033  -0.0244 -0.0753 180 PHE A CD2 
1136 C CE1 . PHE A 140 ? 0.4349 0.4642 0.4079 0.0022  -0.0368 -0.0787 180 PHE A CE1 
1137 C CE2 . PHE A 140 ? 0.4114 0.4277 0.3760 0.0009  -0.0306 -0.0710 180 PHE A CE2 
1138 C CZ  . PHE A 140 ? 0.4117 0.4230 0.3693 0.0007  -0.0367 -0.0728 180 PHE A CZ  
1139 N N   . LEU A 141 ? 0.3621 0.4478 0.3978 0.0311  -0.0308 -0.0672 181 LEU A N   
1140 C CA  . LEU A 141 ? 0.3390 0.4130 0.3589 0.0357  -0.0337 -0.0591 181 LEU A CA  
1141 C C   . LEU A 141 ? 0.3153 0.4004 0.3398 0.0483  -0.0415 -0.0532 181 LEU A C   
1142 O O   . LEU A 141 ? 0.3898 0.4671 0.4025 0.0525  -0.0455 -0.0485 181 LEU A O   
1143 C CB  . LEU A 141 ? 0.3251 0.3922 0.3444 0.0317  -0.0260 -0.0578 181 LEU A CB  
1144 C CG  . LEU A 141 ? 0.3941 0.4404 0.3962 0.0168  -0.0180 -0.0620 181 LEU A CG  
1145 C CD1 . LEU A 141 ? 0.4007 0.4398 0.4011 0.0120  -0.0093 -0.0617 181 LEU A CD1 
1146 C CD2 . LEU A 141 ? 0.3952 0.4196 0.3718 0.0137  -0.0253 -0.0576 181 LEU A CD2 
1147 N N   . ASP A 142 ? 0.3115 0.4135 0.3533 0.0538  -0.0438 -0.0535 182 ASP A N   
1148 C CA  . ASP A 142 ? 0.3381 0.4469 0.3782 0.0632  -0.0514 -0.0482 182 ASP A CA  
1149 C C   . ASP A 142 ? 0.3875 0.4917 0.4141 0.0633  -0.0559 -0.0498 182 ASP A C   
1150 O O   . ASP A 142 ? 0.3863 0.4858 0.4021 0.0680  -0.0575 -0.0462 182 ASP A O   
1151 C CB  . ASP A 142 ? 0.3895 0.5135 0.4477 0.0674  -0.0565 -0.0485 182 ASP A CB  
1152 C CG  . ASP A 142 ? 0.4641 0.5920 0.5341 0.0715  -0.0543 -0.0445 182 ASP A CG  
1153 O OD1 . ASP A 142 ? 0.4241 0.5437 0.4849 0.0721  -0.0496 -0.0402 182 ASP A OD1 
1154 O OD2 . ASP A 142 ? 0.4731 0.6119 0.5631 0.0742  -0.0583 -0.0458 182 ASP A OD2 
1155 N N   . ARG A 143 ? 0.3467 0.4517 0.3750 0.0576  -0.0568 -0.0562 183 ARG A N   
1156 C CA  . ARG A 143 ? 0.3869 0.4871 0.4028 0.0573  -0.0610 -0.0586 183 ARG A CA  
1157 C C   . ARG A 143 ? 0.3008 0.3842 0.3022 0.0551  -0.0586 -0.0585 183 ARG A C   
1158 O O   . ARG A 143 ? 0.3512 0.4295 0.3435 0.0592  -0.0609 -0.0580 183 ARG A O   
1159 C CB  . ARG A 143 ? 0.3142 0.4205 0.3378 0.0512  -0.0634 -0.0656 183 ARG A CB  
1160 C CG  . ARG A 143 ? 0.3217 0.4443 0.3626 0.0545  -0.0698 -0.0655 183 ARG A CG  
1161 C CD  . ARG A 143 ? 0.3089 0.4404 0.3672 0.0476  -0.0710 -0.0733 183 ARG A CD  
1162 N NE  . ARG A 143 ? 0.3503 0.4771 0.3970 0.0433  -0.0753 -0.0777 183 ARG A NE  
1163 C CZ  . ARG A 143 ? 0.3852 0.5149 0.4257 0.0461  -0.0856 -0.0771 183 ARG A CZ  
1164 N NH1 . ARG A 143 ? 0.3737 0.5097 0.4167 0.0528  -0.0935 -0.0715 183 ARG A NH1 
1165 N NH2 . ARG A 143 ? 0.4025 0.5263 0.4316 0.0411  -0.0884 -0.0819 183 ARG A NH2 
1166 N N   . PHE A 144 ? 0.3276 0.4005 0.3266 0.0483  -0.0543 -0.0592 184 PHE A N   
1167 C CA  . PHE A 144 ? 0.3510 0.4047 0.3358 0.0460  -0.0553 -0.0579 184 PHE A CA  
1168 C C   . PHE A 144 ? 0.4016 0.4534 0.3861 0.0543  -0.0573 -0.0519 184 PHE A C   
1169 O O   . PHE A 144 ? 0.4191 0.4621 0.3988 0.0576  -0.0608 -0.0518 184 PHE A O   
1170 C CB  . PHE A 144 ? 0.4006 0.4396 0.3779 0.0352  -0.0511 -0.0587 184 PHE A CB  
1171 C CG  . PHE A 144 ? 0.4111 0.4266 0.3720 0.0324  -0.0557 -0.0557 184 PHE A CG  
1172 C CD1 . PHE A 144 ? 0.4524 0.4536 0.4023 0.0282  -0.0598 -0.0589 184 PHE A CD1 
1173 C CD2 . PHE A 144 ? 0.4550 0.4619 0.4127 0.0344  -0.0577 -0.0496 184 PHE A CD2 
1174 C CE1 . PHE A 144 ? 0.4627 0.4403 0.3993 0.0264  -0.0668 -0.0557 184 PHE A CE1 
1175 C CE2 . PHE A 144 ? 0.4663 0.4505 0.4112 0.0322  -0.0653 -0.0464 184 PHE A CE2 
1176 C CZ  . PHE A 144 ? 0.4321 0.4014 0.3670 0.0286  -0.0704 -0.0493 184 PHE A CZ  
1177 N N   . TYR A 145 ? 0.3637 0.4240 0.3558 0.0577  -0.0549 -0.0475 185 TYR A N   
1178 C CA  . TYR A 145 ? 0.3526 0.4115 0.3459 0.0644  -0.0560 -0.0422 185 TYR A CA  
1179 C C   . TYR A 145 ? 0.3631 0.4317 0.3589 0.0720  -0.0566 -0.0425 185 TYR A C   
1180 O O   . TYR A 145 ? 0.3968 0.4616 0.3934 0.0764  -0.0569 -0.0417 185 TYR A O   
1181 C CB  . TYR A 145 ? 0.3437 0.4064 0.3423 0.0645  -0.0528 -0.0376 185 TYR A CB  
1182 C CG  . TYR A 145 ? 0.3614 0.4084 0.3523 0.0563  -0.0517 -0.0366 185 TYR A CG  
1183 C CD1 . TYR A 145 ? 0.3898 0.4180 0.3698 0.0528  -0.0570 -0.0356 185 TYR A CD1 
1184 C CD2 . TYR A 145 ? 0.3980 0.4467 0.3916 0.0514  -0.0458 -0.0368 185 TYR A CD2 
1185 C CE1 . TYR A 145 ? 0.3540 0.3632 0.3210 0.0434  -0.0575 -0.0339 185 TYR A CE1 
1186 C CE2 . TYR A 145 ? 0.3819 0.4128 0.3634 0.0419  -0.0434 -0.0365 185 TYR A CE2 
1187 C CZ  . TYR A 145 ? 0.3910 0.4012 0.3568 0.0373  -0.0498 -0.0345 185 TYR A CZ  
1188 O OH  . TYR A 145 ? 0.4918 0.4803 0.4401 0.0260  -0.0489 -0.0335 185 TYR A OH  
1189 N N   . MET A 146 ? 0.3541 0.4339 0.3509 0.0729  -0.0567 -0.0441 186 MET A N   
1190 C CA  . MET A 146 ? 0.3885 0.4726 0.3805 0.0774  -0.0570 -0.0451 186 MET A CA  
1191 C C   . MET A 146 ? 0.4192 0.4947 0.4047 0.0766  -0.0575 -0.0509 186 MET A C   
1192 O O   . MET A 146 ? 0.3898 0.4628 0.3736 0.0804  -0.0547 -0.0525 186 MET A O   
1193 C CB  . MET A 146 ? 0.3400 0.4340 0.3313 0.0771  -0.0604 -0.0453 186 MET A CB  
1194 C CG  . MET A 146 ? 0.4223 0.5166 0.4017 0.0795  -0.0607 -0.0456 186 MET A CG  
1195 S SD  . MET A 146 ? 0.4402 0.5360 0.4185 0.0842  -0.0560 -0.0391 186 MET A SD  
1196 C CE  . MET A 146 ? 0.4048 0.5080 0.3850 0.0846  -0.0631 -0.0333 186 MET A CE  
1197 N N   . SER A 147 ? 0.4120 0.4820 0.3948 0.0711  -0.0600 -0.0549 187 SER A N   
1198 C CA  . SER A 147 ? 0.4254 0.4843 0.4021 0.0700  -0.0610 -0.0604 187 SER A CA  
1199 C C   . SER A 147 ? 0.4113 0.4594 0.3922 0.0735  -0.0611 -0.0591 187 SER A C   
1200 O O   . SER A 147 ? 0.4287 0.4728 0.4109 0.0775  -0.0598 -0.0631 187 SER A O   
1201 C CB  . SER A 147 ? 0.3985 0.4512 0.3712 0.0620  -0.0635 -0.0640 187 SER A CB  
1202 O OG  . SER A 147 ? 0.4463 0.4825 0.4134 0.0604  -0.0656 -0.0671 187 SER A OG  
1203 N N   . ARG A 148 ? 0.3856 0.4281 0.3697 0.0717  -0.0629 -0.0542 188 ARG A N   
1204 C CA  . ARG A 148 ? 0.4041 0.4352 0.3939 0.0747  -0.0664 -0.0522 188 ARG A CA  
1205 C C   . ARG A 148 ? 0.3555 0.3960 0.3570 0.0827  -0.0624 -0.0519 188 ARG A C   
1206 O O   . ARG A 148 ? 0.3927 0.4275 0.4037 0.0871  -0.0636 -0.0549 188 ARG A O   
1207 C CB  . ARG A 148 ? 0.3917 0.4140 0.3787 0.0698  -0.0696 -0.0463 188 ARG A CB  
1208 C CG  . ARG A 148 ? 0.4599 0.4738 0.4552 0.0734  -0.0749 -0.0423 188 ARG A CG  
1209 C CD  . ARG A 148 ? 0.5811 0.5788 0.5789 0.0750  -0.0828 -0.0451 188 ARG A CD  
1210 N NE  . ARG A 148 ? 0.6375 0.6263 0.6467 0.0783  -0.0910 -0.0411 188 ARG A NE  
1211 C CZ  . ARG A 148 ? 0.6548 0.6343 0.6774 0.0834  -0.0985 -0.0437 188 ARG A CZ  
1212 N NH1 . ARG A 148 ? 0.6842 0.6564 0.7204 0.0862  -0.1078 -0.0398 188 ARG A NH1 
1213 N NH2 . ARG A 148 ? 0.4559 0.4331 0.4800 0.0858  -0.0971 -0.0507 188 ARG A NH2 
1214 N N   . ILE A 149 ? 0.4012 0.4553 0.4036 0.0843  -0.0575 -0.0488 189 ILE A N   
1215 C CA  . ILE A 149 ? 0.4065 0.4686 0.4169 0.0899  -0.0517 -0.0489 189 ILE A CA  
1216 C C   . ILE A 149 ? 0.4086 0.4703 0.4173 0.0919  -0.0470 -0.0569 189 ILE A C   
1217 O O   . ILE A 149 ? 0.3974 0.4588 0.4182 0.0961  -0.0426 -0.0607 189 ILE A O   
1218 C CB  . ILE A 149 ? 0.3803 0.4538 0.3866 0.0898  -0.0481 -0.0440 189 ILE A CB  
1219 C CG1 . ILE A 149 ? 0.3904 0.4635 0.4023 0.0890  -0.0504 -0.0372 189 ILE A CG1 
1220 C CG2 . ILE A 149 ? 0.3812 0.4609 0.3878 0.0929  -0.0404 -0.0456 189 ILE A CG2 
1221 C CD1 . ILE A 149 ? 0.4026 0.4846 0.4112 0.0885  -0.0486 -0.0326 189 ILE A CD1 
1222 N N   . SER A 150 ? 0.3648 0.4261 0.3599 0.0885  -0.0474 -0.0604 190 SER A N   
1223 C CA  . SER A 150 ? 0.3831 0.4420 0.3723 0.0890  -0.0422 -0.0685 190 SER A CA  
1224 C C   . SER A 150 ? 0.3909 0.4385 0.3895 0.0910  -0.0439 -0.0747 190 SER A C   
1225 O O   . SER A 150 ? 0.4130 0.4586 0.4170 0.0939  -0.0369 -0.0822 190 SER A O   
1226 C CB  . SER A 150 ? 0.3835 0.4437 0.3550 0.0840  -0.0444 -0.0701 190 SER A CB  
1227 O OG  . SER A 150 ? 0.4051 0.4581 0.3746 0.0805  -0.0506 -0.0725 190 SER A OG  
1228 N N   . ILE A 151 ? 0.3737 0.4118 0.3733 0.0889  -0.0526 -0.0723 191 ILE A N   
1229 C CA  . ILE A 151 ? 0.4204 0.4441 0.4280 0.0907  -0.0571 -0.0771 191 ILE A CA  
1230 C C   . ILE A 151 ? 0.4566 0.4794 0.4867 0.0972  -0.0580 -0.0764 191 ILE A C   
1231 O O   . ILE A 151 ? 0.4582 0.4758 0.5033 0.1021  -0.0565 -0.0836 191 ILE A O   
1232 C CB  . ILE A 151 ? 0.4418 0.4520 0.4395 0.0845  -0.0668 -0.0738 191 ILE A CB  
1233 C CG1 . ILE A 151 ? 0.4588 0.4701 0.4396 0.0781  -0.0656 -0.0772 191 ILE A CG1 
1234 C CG2 . ILE A 151 ? 0.4355 0.4268 0.4414 0.0865  -0.0749 -0.0760 191 ILE A CG2 
1235 C CD1 . ILE A 151 ? 0.4763 0.4780 0.4469 0.0696  -0.0717 -0.0739 191 ILE A CD1 
1236 N N   . ARG A 152 ? 0.4298 0.4577 0.4648 0.0974  -0.0604 -0.0685 192 ARG A N   
1237 C CA  . ARG A 152 ? 0.4553 0.4846 0.5135 0.1029  -0.0619 -0.0674 192 ARG A CA  
1238 C C   . ARG A 152 ? 0.4599 0.5008 0.5324 0.1078  -0.0491 -0.0751 192 ARG A C   
1239 O O   . ARG A 152 ? 0.4815 0.5211 0.5793 0.1134  -0.0488 -0.0805 192 ARG A O   
1240 C CB  . ARG A 152 ? 0.4525 0.4868 0.5088 0.1008  -0.0645 -0.0579 192 ARG A CB  
1241 C CG  . ARG A 152 ? 0.6059 0.6378 0.6843 0.1047  -0.0707 -0.0552 192 ARG A CG  
1242 C CD  . ARG A 152 ? 0.8190 0.8312 0.9024 0.1049  -0.0847 -0.0556 192 ARG A CD  
1243 N NE  . ARG A 152 ? 0.9735 0.9807 1.0805 0.1088  -0.0949 -0.0530 192 ARG A NE  
1244 C CZ  . ARG A 152 ? 0.9734 0.9599 1.0843 0.1084  -0.1116 -0.0506 192 ARG A CZ  
1245 N NH1 . ARG A 152 ? 1.0059 0.9883 1.1404 0.1121  -0.1230 -0.0479 192 ARG A NH1 
1246 N NH2 . ARG A 152 ? 0.9186 0.8873 1.0094 0.1037  -0.1179 -0.0508 192 ARG A NH2 
1247 N N   . MET A 153 ? 0.4273 0.4784 0.4841 0.1052  -0.0385 -0.0761 193 MET A N   
1248 C CA  . MET A 153 ? 0.4316 0.4904 0.4940 0.1068  -0.0241 -0.0839 193 MET A CA  
1249 C C   . MET A 153 ? 0.4605 0.5119 0.5316 0.1092  -0.0195 -0.0959 193 MET A C   
1250 O O   . MET A 153 ? 0.4827 0.5372 0.5769 0.1132  -0.0106 -0.1042 193 MET A O   
1251 C CB  . MET A 153 ? 0.4409 0.5055 0.4764 0.1015  -0.0172 -0.0817 193 MET A CB  
1252 C CG  . MET A 153 ? 0.4988 0.5676 0.5312 0.1001  -0.0014 -0.0888 193 MET A CG  
1253 S SD  . MET A 153 ? 0.5726 0.6520 0.6225 0.1018  0.0055  -0.0845 193 MET A SD  
1254 C CE  . MET A 153 ? 0.5414 0.6209 0.5817 0.0971  0.0269  -0.0957 193 MET A CE  
1255 N N   . LEU A 154 ? 0.4682 0.5098 0.5230 0.1064  -0.0247 -0.0980 194 LEU A N   
1256 C CA  . LEU A 154 ? 0.4687 0.5014 0.5300 0.1083  -0.0203 -0.1099 194 LEU A CA  
1257 C C   . LEU A 154 ? 0.4545 0.4798 0.5481 0.1154  -0.0280 -0.1126 194 LEU A C   
1258 O O   . LEU A 154 ? 0.4584 0.4834 0.5748 0.1202  -0.0197 -0.1237 194 LEU A O   
1259 C CB  . LEU A 154 ? 0.4060 0.4288 0.4423 0.1031  -0.0258 -0.1107 194 LEU A CB  
1260 C CG  . LEU A 154 ? 0.4275 0.4554 0.4335 0.0960  -0.0212 -0.1092 194 LEU A CG  
1261 C CD1 . LEU A 154 ? 0.4157 0.4339 0.4034 0.0910  -0.0282 -0.1110 194 LEU A CD1 
1262 C CD2 . LEU A 154 ? 0.5194 0.5505 0.5182 0.0944  -0.0053 -0.1176 194 LEU A CD2 
1263 N N   . LEU A 155 ? 0.4511 0.4692 0.5474 0.1158  -0.0442 -0.1030 195 LEU A N   
1264 C CA  . LEU A 155 ? 0.5096 0.5171 0.6344 0.1219  -0.0560 -0.1038 195 LEU A CA  
1265 C C   . LEU A 155 ? 0.5009 0.5208 0.6605 0.1282  -0.0506 -0.1069 195 LEU A C   
1266 O O   . LEU A 155 ? 0.5175 0.5344 0.7097 0.1351  -0.0512 -0.1155 195 LEU A O   
1267 C CB  . LEU A 155 ? 0.4918 0.4860 0.6049 0.1182  -0.0744 -0.0917 195 LEU A CB  
1268 C CG  . LEU A 155 ? 0.5077 0.4889 0.5889 0.1104  -0.0802 -0.0884 195 LEU A CG  
1269 C CD1 . LEU A 155 ? 0.5393 0.5089 0.6072 0.1046  -0.0939 -0.0768 195 LEU A CD1 
1270 C CD2 . LEU A 155 ? 0.4693 0.4338 0.5530 0.1120  -0.0844 -0.0963 195 LEU A CD2 
1271 N N   . ASN A 156 ? 0.4769 0.5105 0.6323 0.1260  -0.0453 -0.1004 196 ASN A N   
1272 C CA  . ASN A 156 ? 0.5068 0.5529 0.6949 0.1306  -0.0393 -0.1033 196 ASN A CA  
1273 C C   . ASN A 156 ? 0.5351 0.5895 0.7407 0.1331  -0.0196 -0.1185 196 ASN A C   
1274 O O   . ASN A 156 ? 0.5700 0.6281 0.8160 0.1394  -0.0175 -0.1269 196 ASN A O   
1275 C CB  . ASN A 156 ? 0.4443 0.5024 0.6194 0.1264  -0.0354 -0.0939 196 ASN A CB  
1276 C CG  . ASN A 156 ? 0.5438 0.5947 0.7136 0.1248  -0.0533 -0.0809 196 ASN A CG  
1277 O OD1 . ASN A 156 ? 0.6341 0.6711 0.8148 0.1270  -0.0696 -0.0785 196 ASN A OD1 
1278 N ND2 . ASN A 156 ? 0.4766 0.5347 0.6280 0.1203  -0.0505 -0.0725 196 ASN A ND2 
1279 N N   . GLN A 157 ? 0.5080 0.5647 0.6842 0.1274  -0.0048 -0.1227 197 GLN A N   
1280 C CA  . GLN A 157 ? 0.4674 0.5287 0.6526 0.1270  0.0165  -0.1379 197 GLN A CA  
1281 C C   . GLN A 157 ? 0.5236 0.5762 0.7379 0.1335  0.0154  -0.1504 197 GLN A C   
1282 O O   . GLN A 157 ? 0.5795 0.6387 0.8320 0.1383  0.0261  -0.1622 197 GLN A O   
1283 C CB  . GLN A 157 ? 0.5430 0.6018 0.6844 0.1184  0.0280  -0.1392 197 GLN A CB  
1284 C CG  . GLN A 157 ? 0.6511 0.7183 0.7674 0.1121  0.0325  -0.1296 197 GLN A CG  
1285 C CD  . GLN A 157 ? 0.6537 0.7324 0.7918 0.1121  0.0469  -0.1336 197 GLN A CD  
1286 O OE1 . GLN A 157 ? 0.7336 0.8202 0.8846 0.1140  0.0402  -0.1246 197 GLN A OE1 
1287 N NE2 . GLN A 157 ? 0.6270 0.7059 0.7682 0.1088  0.0680  -0.1478 197 GLN A NE2 
1288 N N   . HIS A 158 ? 0.5397 0.5772 0.7386 0.1337  0.0027  -0.1485 198 HIS A N   
1289 C CA  . HIS A 158 ? 0.5699 0.5963 0.7947 0.1400  0.0006  -0.1602 198 HIS A CA  
1290 C C   . HIS A 158 ? 0.5840 0.6103 0.8571 0.1494  -0.0132 -0.1597 198 HIS A C   
1291 O O   . HIS A 158 ? 0.5740 0.6008 0.8873 0.1564  -0.0073 -0.1734 198 HIS A O   
1292 C CB  . HIS A 158 ? 0.5494 0.5575 0.7459 0.1373  -0.0121 -0.1566 198 HIS A CB  
1293 C CG  . HIS A 158 ? 0.5662 0.5602 0.7853 0.1433  -0.0142 -0.1687 198 HIS A CG  
1294 N ND1 . HIS A 158 ? 0.5711 0.5602 0.7804 0.1409  0.0019  -0.1828 198 HIS A ND1 
1295 C CD2 . HIS A 158 ? 0.5510 0.5328 0.8022 0.1513  -0.0314 -0.1689 198 HIS A CD2 
1296 C CE1 . HIS A 158 ? 0.5704 0.5460 0.8066 0.1479  -0.0039 -0.1918 198 HIS A CE1 
1297 N NE2 . HIS A 158 ? 0.5917 0.5624 0.8542 0.1546  -0.0250 -0.1832 198 HIS A NE2 
1298 N N   . SER A 159 ? 0.5571 0.5822 0.8281 0.1495  -0.0320 -0.1447 199 SER A N   
1299 C CA  . SER A 159 ? 0.5568 0.5786 0.8701 0.1573  -0.0496 -0.1425 199 SER A CA  
1300 C C   . SER A 159 ? 0.4907 0.5324 0.8479 0.1619  -0.0363 -0.1513 199 SER A C   
1301 O O   . SER A 159 ? 0.5821 0.6226 0.9751 0.1641  -0.0410 -0.1545 199 SER A O   
1302 C CB  . SER A 159 ? 0.6139 0.6272 0.9074 0.1537  -0.0715 -0.1243 199 SER A CB  
1303 O OG  . SER A 159 ? 0.7188 0.7125 0.9758 0.1487  -0.0831 -0.1176 199 SER A OG  
1304 N N   . LEU A 160 ? 0.4816 0.5397 0.8234 0.1559  -0.0191 -0.1498 200 LEU A N   
1305 C CA  . LEU A 160 ? 0.4884 0.5646 0.8667 0.1570  -0.0046 -0.1571 200 LEU A CA  
1306 C C   . LEU A 160 ? 0.5673 0.6472 0.9612 0.1554  0.0190  -0.1743 200 LEU A C   
1307 O O   . LEU A 160 ? 0.6179 0.7046 1.0485 0.1552  0.0237  -0.1795 200 LEU A O   
1308 C CB  . LEU A 160 ? 0.4094 0.4988 0.7629 0.1502  0.0062  -0.1498 200 LEU A CB  
1309 C CG  . LEU A 160 ? 0.4805 0.5651 0.8186 0.1490  -0.0166 -0.1312 200 LEU A CG  
1310 C CD1 . LEU A 160 ? 0.5076 0.6013 0.8129 0.1411  -0.0073 -0.1222 200 LEU A CD1 
1311 C CD2 . LEU A 160 ? 0.5371 0.6227 0.9186 0.1538  -0.0329 -0.1283 200 LEU A CD2 
1312 N N   . LEU A 161 ? 0.5715 0.6461 0.9372 0.1536  0.0336  -0.1840 201 LEU A N   
1313 C CA  . LEU A 161 ? 0.5585 0.6340 0.9325 0.1499  0.0580  -0.2004 201 LEU A CA  
1314 C C   . LEU A 161 ? 0.5995 0.6644 1.0039 0.1548  0.0489  -0.2060 201 LEU A C   
1315 O O   . LEU A 161 ? 0.6547 0.7244 1.0855 0.1530  0.0646  -0.2177 201 LEU A O   
1316 C CB  . LEU A 161 ? 0.5593 0.6283 0.8858 0.1434  0.0747  -0.2076 201 LEU A CB  
1317 C CG  . LEU A 161 ? 0.5641 0.6400 0.8475 0.1323  0.0869  -0.1997 201 LEU A CG  
1318 C CD1 . LEU A 161 ? 0.5909 0.6545 0.8205 0.1228  0.0967  -0.2020 201 LEU A CD1 
1319 C CD2 . LEU A 161 ? 0.5668 0.6574 0.8754 0.1292  0.1103  -0.2100 201 LEU A CD2 
1320 N N   . PHE A 162 ? 0.6250 0.6745 1.0258 0.1604  0.0237  -0.1980 202 PHE A N   
1321 C CA  . PHE A 162 ? 0.6023 0.6381 1.0246 0.1646  0.0152  -0.2039 202 PHE A CA  
1322 C C   . PHE A 162 ? 0.6540 0.6803 1.0994 0.1694  -0.0159 -0.1917 202 PHE A C   
1323 O O   . PHE A 162 ? 0.6796 0.6920 1.1408 0.1730  -0.0270 -0.1949 202 PHE A O   
1324 C CB  . PHE A 162 ? 0.5571 0.5760 0.9453 0.1644  0.0171  -0.2096 202 PHE A CB  
1325 C CG  . PHE A 162 ? 0.6060 0.6301 0.9622 0.1575  0.0448  -0.2209 202 PHE A CG  
1326 C CD1 . PHE A 162 ? 0.6478 0.6783 1.0158 0.1528  0.0709  -0.2351 202 PHE A CD1 
1327 C CD2 . PHE A 162 ? 0.6215 0.6426 0.9282 0.1519  0.0434  -0.2137 202 PHE A CD2 
1328 C CE1 . PHE A 162 ? 0.6589 0.6899 0.9904 0.1437  0.0958  -0.2445 202 PHE A CE1 
1329 C CE2 . PHE A 162 ? 0.6784 0.7015 0.9467 0.1416  0.0656  -0.2196 202 PHE A CE2 
1330 C CZ  . PHE A 162 ? 0.6692 0.6963 0.9532 0.1395  0.0932  -0.2392 202 PHE A CZ  
1331 N N   . GLY A 163 ? 0.7138 0.7453 1.1594 0.1687  -0.0304 -0.1781 203 GLY A N   
1332 C CA  . GLY A 163 ? 0.7679 0.7878 1.2306 0.1707  -0.0599 -0.1665 203 GLY A CA  
1333 C C   . GLY A 163 ? 0.8055 0.8346 1.3180 0.1718  -0.0612 -0.1719 203 GLY A C   
1334 O O   . GLY A 163 ? 0.8591 0.9068 1.3897 0.1694  -0.0492 -0.1739 203 GLY A O   
1335 N N   . HIS A 175 ? 0.6233 0.7846 0.9617 0.0895  0.1844  -0.1955 215 HIS A N   
1336 C CA  . HIS A 175 ? 0.7925 0.9475 1.1124 0.0983  0.1574  -0.1821 215 HIS A CA  
1337 C C   . HIS A 175 ? 0.8747 1.0184 1.1867 0.1025  0.1548  -0.1899 215 HIS A C   
1338 O O   . HIS A 175 ? 0.9805 1.1251 1.3278 0.1061  0.1588  -0.2013 215 HIS A O   
1339 C CB  . HIS A 175 ? 0.8982 1.0627 1.2596 0.1092  0.1317  -0.1725 215 HIS A CB  
1340 C CG  . HIS A 175 ? 0.9921 1.1573 1.3293 0.1064  0.1181  -0.1537 215 HIS A CG  
1341 N ND1 . HIS A 175 ? 1.0129 1.1680 1.3153 0.1086  0.0958  -0.1371 215 HIS A ND1 
1342 C CD2 . HIS A 175 ? 1.0104 1.1846 1.3549 0.1012  0.1246  -0.1497 215 HIS A CD2 
1343 C CE1 . HIS A 175 ? 0.9875 1.1452 1.2771 0.1054  0.0893  -0.1242 215 HIS A CE1 
1344 N NE2 . HIS A 175 ? 1.0045 1.1733 1.3181 0.1010  0.1058  -0.1309 215 HIS A NE2 
1345 N N   . ILE A 176 ? 0.7652 0.8949 1.0248 0.0997  0.1440  -0.1791 216 ILE A N   
1346 C CA  . ILE A 176 ? 0.6945 0.8117 0.9384 0.1016  0.1415  -0.1853 216 ILE A CA  
1347 C C   . ILE A 176 ? 0.7418 0.8535 0.9746 0.1089  0.1112  -0.1694 216 ILE A C   
1348 O O   . ILE A 176 ? 0.7239 0.8289 0.9123 0.1042  0.1020  -0.1562 216 ILE A O   
1349 C CB  . ILE A 176 ? 0.6492 0.7526 0.8375 0.0888  0.1589  -0.1893 216 ILE A CB  
1350 C CG1 . ILE A 176 ? 0.7078 0.8138 0.8994 0.0784  0.1906  -0.2039 216 ILE A CG1 
1351 C CG2 . ILE A 176 ? 0.6850 0.7757 0.8613 0.0905  0.1577  -0.1979 216 ILE A CG2 
1352 C CD1 . ILE A 176 ? 0.7921 0.9037 1.0331 0.0817  0.2080  -0.2247 216 ILE A CD1 
1353 N N   . GLY A 177 ? 0.7328 0.8462 1.0062 0.1196  0.0956  -0.1709 217 GLY A N   
1354 C CA  . GLY A 177 ? 0.7407 0.8480 1.0053 0.1248  0.0675  -0.1553 217 GLY A CA  
1355 C C   . GLY A 177 ? 0.7332 0.8480 0.9934 0.1232  0.0583  -0.1405 217 GLY A C   
1356 O O   . GLY A 177 ? 0.7837 0.9103 1.0756 0.1241  0.0641  -0.1429 217 GLY A O   
1357 N N   . SER A 178 ? 0.6665 0.7747 0.8889 0.1204  0.0446  -0.1259 218 SER A N   
1358 C CA  . SER A 178 ? 0.6675 0.7810 0.8805 0.1181  0.0374  -0.1122 218 SER A CA  
1359 C C   . SER A 178 ? 0.6320 0.7482 0.8129 0.1093  0.0534  -0.1101 218 SER A C   
1360 O O   . SER A 178 ? 0.6278 0.7467 0.7962 0.1069  0.0481  -0.0986 218 SER A O   
1361 C CB  . SER A 178 ? 0.6842 0.7888 0.8762 0.1191  0.0156  -0.0985 218 SER A CB  
1362 O OG  . SER A 178 ? 0.7485 0.8453 0.9021 0.1149  0.0163  -0.0969 218 SER A OG  
1363 N N   . ILE A 179 ? 0.5816 0.6948 0.7470 0.1039  0.0721  -0.1209 219 ILE A N   
1364 C CA  . ILE A 179 ? 0.5402 0.6511 0.6703 0.0940  0.0865  -0.1190 219 ILE A CA  
1365 C C   . ILE A 179 ? 0.5363 0.6562 0.6904 0.0903  0.1065  -0.1278 219 ILE A C   
1366 O O   . ILE A 179 ? 0.5217 0.6466 0.7100 0.0925  0.1191  -0.1428 219 ILE A O   
1367 C CB  . ILE A 179 ? 0.5207 0.6191 0.6132 0.0875  0.0952  -0.1254 219 ILE A CB  
1368 C CG1 . ILE A 179 ? 0.5863 0.6774 0.6550 0.0899  0.0752  -0.1158 219 ILE A CG1 
1369 C CG2 . ILE A 179 ? 0.4817 0.5738 0.5370 0.0757  0.1106  -0.1246 219 ILE A CG2 
1370 C CD1 . ILE A 179 ? 0.6705 0.7494 0.7076 0.0844  0.0807  -0.1227 219 ILE A CD1 
1371 N N   . ASN A 180 ? 0.4514 0.5733 0.5899 0.0844  0.1098  -0.1192 220 ASN A N   
1372 C CA  . ASN A 180 ? 0.4466 0.5748 0.5991 0.0777  0.1313  -0.1272 220 ASN A CA  
1373 C C   . ASN A 180 ? 0.5419 0.6564 0.6442 0.0644  0.1483  -0.1288 220 ASN A C   
1374 O O   . ASN A 180 ? 0.5588 0.6646 0.6218 0.0601  0.1391  -0.1151 220 ASN A O   
1375 C CB  . ASN A 180 ? 0.4375 0.5752 0.6075 0.0791  0.1235  -0.1166 220 ASN A CB  
1376 C CG  . ASN A 180 ? 0.4691 0.6153 0.6612 0.0721  0.1459  -0.1260 220 ASN A CG  
1377 O OD1 . ASN A 180 ? 0.4397 0.5815 0.6211 0.0633  0.1695  -0.1386 220 ASN A OD1 
1378 N ND2 . ASN A 180 ? 0.4912 0.6486 0.7133 0.0749  0.1392  -0.1205 220 ASN A ND2 
1379 N N   . PRO A 181 ? 0.5500 0.6604 0.6513 0.0569  0.1726  -0.1453 221 PRO A N   
1380 C CA  . PRO A 181 ? 0.5001 0.5928 0.5472 0.0417  0.1888  -0.1466 221 PRO A CA  
1381 C C   . PRO A 181 ? 0.4821 0.5731 0.5138 0.0323  0.1969  -0.1395 221 PRO A C   
1382 O O   . PRO A 181 ? 0.5806 0.6531 0.5600 0.0194  0.2040  -0.1355 221 PRO A O   
1383 C CB  . PRO A 181 ? 0.5721 0.6620 0.6305 0.0357  0.2160  -0.1688 221 PRO A CB  
1384 C CG  . PRO A 181 ? 0.6324 0.7375 0.7485 0.0503  0.2088  -0.1774 221 PRO A CG  
1385 C CD  . PRO A 181 ? 0.5842 0.7043 0.7338 0.0613  0.1868  -0.1641 221 PRO A CD  
1386 N N   . ASN A 182 ? 0.4654 0.5733 0.5397 0.0376  0.1955  -0.1375 222 ASN A N   
1387 C CA  . ASN A 182 ? 0.4934 0.6008 0.5583 0.0286  0.2042  -0.1317 222 ASN A CA  
1388 C C   . ASN A 182 ? 0.4563 0.5749 0.5426 0.0382  0.1816  -0.1164 222 ASN A C   
1389 O O   . ASN A 182 ? 0.5320 0.6637 0.6536 0.0387  0.1863  -0.1178 222 ASN A O   
1390 C CB  . ASN A 182 ? 0.5261 0.6424 0.6240 0.0210  0.2338  -0.1496 222 ASN A CB  
1391 C CG  . ASN A 182 ? 0.6657 0.7671 0.7351 0.0082  0.2602  -0.1656 222 ASN A CG  
1392 O OD1 . ASN A 182 ? 0.7562 0.8374 0.7722 -0.0075 0.2725  -0.1631 222 ASN A OD1 
1393 N ND2 . ASN A 182 ? 0.6365 0.7453 0.7397 0.0140  0.2688  -0.1822 222 ASN A ND2 
1394 N N   . CYS A 183 ? 0.4196 0.5328 0.4847 0.0451  0.1573  -0.1023 223 CYS A N   
1395 C CA  . CYS A 183 ? 0.4317 0.5533 0.5141 0.0535  0.1365  -0.0887 223 CYS A CA  
1396 C C   . CYS A 183 ? 0.4861 0.6037 0.5517 0.0454  0.1409  -0.0798 223 CYS A C   
1397 O O   . CYS A 183 ? 0.5076 0.6089 0.5265 0.0371  0.1423  -0.0727 223 CYS A O   
1398 C CB  . CYS A 183 ? 0.4775 0.5925 0.5377 0.0604  0.1132  -0.0774 223 CYS A CB  
1399 S SG  . CYS A 183 ? 0.4814 0.6036 0.5595 0.0696  0.0891  -0.0624 223 CYS A SG  
1400 N N   . ASN A 184 ? 0.4266 0.5576 0.5303 0.0474  0.1422  -0.0802 224 ASN A N   
1401 C CA  A ASN A 184 ? 0.4520 0.5800 0.5444 0.0401  0.1459  -0.0719 224 ASN A CA  
1402 C CA  B ASN A 184 ? 0.4521 0.5801 0.5448 0.0401  0.1459  -0.0719 224 ASN A CA  
1403 C C   . ASN A 184 ? 0.4547 0.5786 0.5329 0.0467  0.1217  -0.0549 224 ASN A C   
1404 O O   . ASN A 184 ? 0.4291 0.5632 0.5379 0.0552  0.1073  -0.0511 224 ASN A O   
1405 C CB  A ASN A 184 ? 0.4513 0.5959 0.5926 0.0391  0.1568  -0.0801 224 ASN A CB  
1406 C CB  B ASN A 184 ? 0.4509 0.5958 0.5931 0.0393  0.1566  -0.0801 224 ASN A CB  
1407 C CG  A ASN A 184 ? 0.4841 0.6241 0.6116 0.0288  0.1655  -0.0739 224 ASN A CG  
1408 C CG  B ASN A 184 ? 0.5145 0.6646 0.6754 0.0317  0.1842  -0.0992 224 ASN A CG  
1409 O OD1 A ASN A 184 ? 0.3756 0.5057 0.4752 0.0288  0.1519  -0.0591 224 ASN A OD1 
1410 O OD1 B ASN A 184 ? 0.5694 0.7053 0.6924 0.0200  0.2025  -0.1040 224 ASN A OD1 
1411 N ND2 A ASN A 184 ? 0.5149 0.6618 0.6637 0.0195  0.1890  -0.0861 224 ASN A ND2 
1412 N ND2 B ASN A 184 ? 0.5351 0.7042 0.7550 0.0379  0.1872  -0.1106 224 ASN A ND2 
1413 N N   . VAL A 185 ? 0.3995 0.5066 0.4307 0.0420  0.1170  -0.0450 225 VAL A N   
1414 C CA  . VAL A 185 ? 0.3972 0.4998 0.4148 0.0487  0.0949  -0.0308 225 VAL A CA  
1415 C C   . VAL A 185 ? 0.3450 0.4533 0.3819 0.0503  0.0890  -0.0233 225 VAL A C   
1416 O O   . VAL A 185 ? 0.3500 0.4636 0.4026 0.0585  0.0728  -0.0177 225 VAL A O   
1417 C CB  . VAL A 185 ? 0.4219 0.5050 0.3893 0.0428  0.0914  -0.0227 225 VAL A CB  
1418 C CG1 . VAL A 185 ? 0.4040 0.4831 0.3627 0.0491  0.0708  -0.0089 225 VAL A CG1 
1419 C CG2 . VAL A 185 ? 0.4321 0.5095 0.3814 0.0423  0.0925  -0.0293 225 VAL A CG2 
1420 N N   . LEU A 186 ? 0.3732 0.4790 0.4072 0.0411  0.1027  -0.0237 226 LEU A N   
1421 C CA  . LEU A 186 ? 0.3925 0.5014 0.4404 0.0415  0.0966  -0.0159 226 LEU A CA  
1422 C C   . LEU A 186 ? 0.3820 0.5087 0.4788 0.0483  0.0914  -0.0209 226 LEU A C   
1423 O O   . LEU A 186 ? 0.3442 0.4723 0.4513 0.0522  0.0778  -0.0131 226 LEU A O   
1424 C CB  . LEU A 186 ? 0.4606 0.5617 0.4937 0.0289  0.1132  -0.0156 226 LEU A CB  
1425 C CG  . LEU A 186 ? 0.5560 0.6364 0.5446 0.0249  0.1057  -0.0021 226 LEU A CG  
1426 C CD1 . LEU A 186 ? 0.5177 0.5827 0.4661 0.0222  0.1049  -0.0014 226 LEU A CD1 
1427 C CD2 . LEU A 186 ? 0.6476 0.7197 0.6256 0.0129  0.1188  0.0002  226 LEU A CD2 
1428 N N   . GLU A 187 ? 0.3542 0.4927 0.4812 0.0493  0.1010  -0.0339 227 GLU A N   
1429 C CA  . GLU A 187 ? 0.3488 0.5022 0.5238 0.0563  0.0924  -0.0384 227 GLU A CA  
1430 C C   . GLU A 187 ? 0.2776 0.4287 0.4526 0.0663  0.0700  -0.0322 227 GLU A C   
1431 O O   . GLU A 187 ? 0.3047 0.4587 0.4994 0.0701  0.0556  -0.0274 227 GLU A O   
1432 C CB  . GLU A 187 ? 0.4354 0.6012 0.6457 0.0560  0.1072  -0.0547 227 GLU A CB  
1433 C CG  . GLU A 187 ? 0.7630 0.9340 0.9847 0.0450  0.1312  -0.0634 227 GLU A CG  
1434 C CD  . GLU A 187 ? 0.9924 1.1663 1.2250 0.0408  0.1281  -0.0562 227 GLU A CD  
1435 O OE1 . GLU A 187 ? 1.0033 1.1867 1.2709 0.0473  0.1123  -0.0539 227 GLU A OE1 
1436 O OE2 . GLU A 187 ? 1.0763 1.2407 1.2798 0.0302  0.1406  -0.0523 227 GLU A OE2 
1437 N N   . VAL A 188 ? 0.3047 0.4490 0.4560 0.0694  0.0670  -0.0323 228 VAL A N   
1438 C CA  . VAL A 188 ? 0.3132 0.4537 0.4605 0.0770  0.0476  -0.0264 228 VAL A CA  
1439 C C   . VAL A 188 ? 0.3881 0.5209 0.5169 0.0766  0.0364  -0.0138 228 VAL A C   
1440 O O   . VAL A 188 ? 0.3279 0.4594 0.4658 0.0805  0.0217  -0.0093 228 VAL A O   
1441 C CB  . VAL A 188 ? 0.3227 0.4572 0.4464 0.0790  0.0478  -0.0291 228 VAL A CB  
1442 C CG1 . VAL A 188 ? 0.3104 0.4404 0.4287 0.0852  0.0293  -0.0232 228 VAL A CG1 
1443 C CG2 . VAL A 188 ? 0.3341 0.4749 0.4776 0.0796  0.0593  -0.0428 228 VAL A CG2 
1444 N N   . ILE A 189 ? 0.3729 0.4984 0.4742 0.0712  0.0432  -0.0082 229 ILE A N   
1445 C CA  . ILE A 189 ? 0.3516 0.4690 0.4366 0.0712  0.0335  0.0029  229 ILE A CA  
1446 C C   . ILE A 189 ? 0.3363 0.4576 0.4446 0.0702  0.0294  0.0053  229 ILE A C   
1447 O O   . ILE A 189 ? 0.3597 0.4767 0.4681 0.0728  0.0168  0.0111  229 ILE A O   
1448 C CB  . ILE A 189 ? 0.3605 0.4670 0.4128 0.0655  0.0404  0.0084  229 ILE A CB  
1449 C CG1 . ILE A 189 ? 0.3612 0.4607 0.3876 0.0677  0.0364  0.0091  229 ILE A CG1 
1450 C CG2 . ILE A 189 ? 0.3646 0.4637 0.4086 0.0647  0.0334  0.0185  229 ILE A CG2 
1451 C CD1 . ILE A 189 ? 0.3624 0.4490 0.3556 0.0610  0.0427  0.0128  229 ILE A CD1 
1452 N N   . LYS A 190 ? 0.3294 0.4583 0.4578 0.0654  0.0406  0.0002  230 LYS A N   
1453 C CA  . LYS A 190 ? 0.3456 0.4787 0.4985 0.0637  0.0356  0.0021  230 LYS A CA  
1454 C C   . LYS A 190 ? 0.4164 0.5533 0.5941 0.0696  0.0199  0.0004  230 LYS A C   
1455 O O   . LYS A 190 ? 0.3856 0.5183 0.5687 0.0692  0.0080  0.0059  230 LYS A O   
1456 C CB  . LYS A 190 ? 0.3442 0.4870 0.5195 0.0572  0.0513  -0.0051 230 LYS A CB  
1457 C CG  . LYS A 190 ? 0.3993 0.5343 0.5471 0.0484  0.0668  -0.0025 230 LYS A CG  
1458 C CD  . LYS A 190 ? 0.4734 0.6188 0.6453 0.0405  0.0861  -0.0127 230 LYS A CD  
1459 C CE  . LYS A 190 ? 0.6067 0.7403 0.7447 0.0295  0.1034  -0.0110 230 LYS A CE  
1460 N NZ  . LYS A 190 ? 0.6024 0.7452 0.7615 0.0199  0.1261  -0.0231 230 LYS A NZ  
1461 N N   . ASP A 191 ? 0.4034 0.5457 0.5942 0.0743  0.0194  -0.0072 231 ASP A N   
1462 C CA  . ASP A 191 ? 0.3476 0.4895 0.5582 0.0795  0.0029  -0.0082 231 ASP A CA  
1463 C C   . ASP A 191 ? 0.3591 0.4874 0.5428 0.0810  -0.0111 0.0005  231 ASP A C   
1464 O O   . ASP A 191 ? 0.3320 0.4539 0.5220 0.0805  -0.0254 0.0045  231 ASP A O   
1465 C CB  . ASP A 191 ? 0.4568 0.6046 0.6822 0.0843  0.0062  -0.0180 231 ASP A CB  
1466 C CG  . ASP A 191 ? 0.7001 0.8482 0.9554 0.0892  -0.0104 -0.0206 231 ASP A CG  
1467 O OD1 . ASP A 191 ? 0.8150 0.9620 1.0880 0.0878  -0.0222 -0.0169 231 ASP A OD1 
1468 O OD2 . ASP A 191 ? 0.7869 0.9341 1.0466 0.0940  -0.0130 -0.0260 231 ASP A OD2 
1469 N N   . GLY A 192 ? 0.2982 0.4212 0.4520 0.0818  -0.0070 0.0029  232 GLY A N   
1470 C CA  . GLY A 192 ? 0.3756 0.4873 0.5072 0.0825  -0.0172 0.0095  232 GLY A CA  
1471 C C   . GLY A 192 ? 0.4145 0.5193 0.5387 0.0785  -0.0203 0.0167  232 GLY A C   
1472 O O   . GLY A 192 ? 0.3456 0.4408 0.4642 0.0773  -0.0310 0.0202  232 GLY A O   
1473 N N   . TYR A 193 ? 0.3750 0.4827 0.4972 0.0752  -0.0105 0.0186  233 TYR A N   
1474 C CA  . TYR A 193 ? 0.3528 0.4532 0.4687 0.0711  -0.0127 0.0251  233 TYR A CA  
1475 C C   . TYR A 193 ? 0.3206 0.4196 0.4563 0.0686  -0.0231 0.0253  233 TYR A C   
1476 O O   . TYR A 193 ? 0.3541 0.4417 0.4796 0.0660  -0.0315 0.0300  233 TYR A O   
1477 C CB  . TYR A 193 ? 0.3528 0.4554 0.4645 0.0670  -0.0004 0.0268  233 TYR A CB  
1478 C CG  . TYR A 193 ? 0.3715 0.4671 0.4823 0.0624  -0.0032 0.0325  233 TYR A CG  
1479 C CD1 . TYR A 193 ? 0.3766 0.4600 0.4665 0.0626  -0.0073 0.0385  233 TYR A CD1 
1480 C CD2 . TYR A 193 ? 0.3521 0.4533 0.4853 0.0577  -0.0020 0.0310  233 TYR A CD2 
1481 C CE1 . TYR A 193 ? 0.3650 0.4401 0.4528 0.0581  -0.0093 0.0431  233 TYR A CE1 
1482 C CE2 . TYR A 193 ? 0.4069 0.5003 0.5377 0.0528  -0.0053 0.0362  233 TYR A CE2 
1483 C CZ  . TYR A 193 ? 0.4192 0.4988 0.5256 0.0529  -0.0087 0.0423  233 TYR A CZ  
1484 O OH  . TYR A 193 ? 0.4147 0.4848 0.5174 0.0478  -0.0112 0.0467  233 TYR A OH  
1485 N N   . GLU A 194 ? 0.2905 0.4002 0.4553 0.0686  -0.0226 0.0199  234 GLU A N   
1486 C CA  . GLU A 194 ? 0.3674 0.4757 0.5542 0.0658  -0.0347 0.0205  234 GLU A CA  
1487 C C   . GLU A 194 ? 0.3688 0.4648 0.5495 0.0670  -0.0520 0.0223  234 GLU A C   
1488 O O   . GLU A 194 ? 0.3600 0.4446 0.5386 0.0623  -0.0643 0.0266  234 GLU A O   
1489 C CB  . GLU A 194 ? 0.4776 0.6018 0.7034 0.0664  -0.0307 0.0129  234 GLU A CB  
1490 C CG  . GLU A 194 ? 0.6448 0.7789 0.8776 0.0619  -0.0130 0.0106  234 GLU A CG  
1491 C CD  . GLU A 194 ? 0.7591 0.8877 0.9889 0.0552  -0.0154 0.0168  234 GLU A CD  
1492 O OE1 . GLU A 194 ? 0.7356 0.8541 0.9640 0.0537  -0.0315 0.0216  234 GLU A OE1 
1493 O OE2 . GLU A 194 ? 0.7789 0.9109 1.0050 0.0503  -0.0008 0.0168  234 GLU A OE2 
1494 N N   . ASN A 195 ? 0.3275 0.4232 0.5028 0.0718  -0.0533 0.0192  235 ASN A N   
1495 C CA  . ASN A 195 ? 0.3755 0.4564 0.5410 0.0713  -0.0690 0.0210  235 ASN A CA  
1496 C C   . ASN A 195 ? 0.3691 0.4346 0.5003 0.0671  -0.0695 0.0264  235 ASN A C   
1497 O O   . ASN A 195 ? 0.3776 0.4261 0.4969 0.0618  -0.0818 0.0296  235 ASN A O   
1498 C CB  . ASN A 195 ? 0.4222 0.5066 0.5926 0.0770  -0.0698 0.0156  235 ASN A CB  
1499 C CG  . ASN A 195 ? 0.5327 0.6275 0.7411 0.0807  -0.0742 0.0095  235 ASN A CG  
1500 O OD1 . ASN A 195 ? 0.5646 0.6706 0.7858 0.0857  -0.0652 0.0025  235 ASN A OD1 
1501 N ND2 . ASN A 195 ? 0.5916 0.6824 0.8198 0.0780  -0.0881 0.0114  235 ASN A ND2 
1502 N N   . ALA A 196 ? 0.3500 0.4194 0.4651 0.0687  -0.0567 0.0271  236 ALA A N   
1503 C CA  . ALA A 196 ? 0.3643 0.4209 0.4538 0.0652  -0.0557 0.0308  236 ALA A CA  
1504 C C   . ALA A 196 ? 0.3679 0.4160 0.4551 0.0589  -0.0581 0.0351  236 ALA A C   
1505 O O   . ALA A 196 ? 0.3808 0.4123 0.4508 0.0532  -0.0636 0.0372  236 ALA A O   
1506 C CB  . ALA A 196 ? 0.2896 0.3528 0.3678 0.0692  -0.0437 0.0307  236 ALA A CB  
1507 N N   . ARG A 197 ? 0.3619 0.4198 0.4649 0.0588  -0.0534 0.0359  237 ARG A N   
1508 C CA  . ARG A 197 ? 0.4526 0.5026 0.5545 0.0524  -0.0558 0.0398  237 ARG A CA  
1509 C C   . ARG A 197 ? 0.4452 0.4826 0.5504 0.0466  -0.0722 0.0409  237 ARG A C   
1510 O O   . ARG A 197 ? 0.4327 0.4541 0.5225 0.0395  -0.0770 0.0442  237 ARG A O   
1511 C CB  . ARG A 197 ? 0.4549 0.5183 0.5757 0.0522  -0.0476 0.0396  237 ARG A CB  
1512 C CG  . ARG A 197 ? 0.4406 0.4964 0.5631 0.0449  -0.0512 0.0433  237 ARG A CG  
1513 C CD  . ARG A 197 ? 0.4671 0.5344 0.6051 0.0430  -0.0409 0.0432  237 ARG A CD  
1514 N NE  . ARG A 197 ? 0.6581 0.7137 0.7797 0.0376  -0.0378 0.0481  237 ARG A NE  
1515 C CZ  . ARG A 197 ? 0.6134 0.6726 0.7413 0.0335  -0.0298 0.0496  237 ARG A CZ  
1516 N NH1 . ARG A 197 ? 0.4510 0.5261 0.6019 0.0331  -0.0223 0.0458  237 ARG A NH1 
1517 N NH2 . ARG A 197 ? 0.6562 0.7019 0.7671 0.0290  -0.0282 0.0542  237 ARG A NH2 
1518 N N   . ARG A 198 ? 0.4000 0.4423 0.5245 0.0492  -0.0820 0.0381  238 ARG A N   
1519 C CA  A ARG A 198 ? 0.4200 0.4473 0.5467 0.0436  -0.1013 0.0400  238 ARG A CA  
1520 C CA  B ARG A 198 ? 0.4200 0.4472 0.5465 0.0435  -0.1013 0.0401  238 ARG A CA  
1521 C C   . ARG A 198 ? 0.4174 0.4204 0.5084 0.0374  -0.1071 0.0424  238 ARG A C   
1522 O O   . ARG A 198 ? 0.4526 0.4357 0.5280 0.0283  -0.1175 0.0459  238 ARG A O   
1523 C CB  A ARG A 198 ? 0.4165 0.4531 0.5724 0.0490  -0.1110 0.0361  238 ARG A CB  
1524 C CB  B ARG A 198 ? 0.4167 0.4528 0.5729 0.0486  -0.1116 0.0363  238 ARG A CB  
1525 C CG  A ARG A 198 ? 0.4305 0.4493 0.5894 0.0442  -0.1349 0.0386  238 ARG A CG  
1526 C CG  B ARG A 198 ? 0.4075 0.4620 0.6042 0.0505  -0.1115 0.0334  238 ARG A CG  
1527 C CD  A ARG A 198 ? 0.5004 0.5279 0.6880 0.0516  -0.1432 0.0340  238 ARG A CD  
1528 C CD  B ARG A 198 ? 0.4832 0.5456 0.7140 0.0562  -0.1226 0.0285  238 ARG A CD  
1529 N NE  A ARG A 198 ? 0.5692 0.6079 0.7512 0.0588  -0.1277 0.0295  238 ARG A NE  
1530 N NE  B ARG A 198 ? 0.5228 0.6056 0.7976 0.0579  -0.1192 0.0236  238 ARG A NE  
1531 C CZ  A ARG A 198 ? 0.5297 0.5555 0.6862 0.0588  -0.1298 0.0298  238 ARG A CZ  
1532 C CZ  B ARG A 198 ? 0.5352 0.6398 0.8329 0.0633  -0.1012 0.0160  238 ARG A CZ  
1533 N NH1 A ARG A 198 ? 0.4045 0.4419 0.5582 0.0650  -0.1159 0.0254  238 ARG A NH1 
1534 N NH1 B ARG A 198 ? 0.6056 0.7277 0.9442 0.0631  -0.0967 0.0105  238 ARG A NH1 
1535 N NH2 A ARG A 198 ? 0.5909 0.5907 0.7233 0.0512  -0.1458 0.0343  238 ARG A NH2 
1536 N NH2 B ARG A 198 ? 0.5020 0.6099 0.7814 0.0680  -0.0874 0.0135  238 ARG A NH2 
1537 N N   . LEU A 199 ? 0.3753 0.3788 0.4521 0.0412  -0.0997 0.0400  239 LEU A N   
1538 C CA  . LEU A 199 ? 0.4364 0.4180 0.4803 0.0344  -0.1013 0.0405  239 LEU A CA  
1539 C C   . LEU A 199 ? 0.4402 0.4135 0.4648 0.0291  -0.0910 0.0418  239 LEU A C   
1540 O O   . LEU A 199 ? 0.4625 0.4126 0.4616 0.0191  -0.0948 0.0427  239 LEU A O   
1541 C CB  . LEU A 199 ? 0.3946 0.3818 0.4328 0.0398  -0.0945 0.0367  239 LEU A CB  
1542 C CG  . LEU A 199 ? 0.4215 0.4116 0.4735 0.0441  -0.1050 0.0348  239 LEU A CG  
1543 C CD1 . LEU A 199 ? 0.4277 0.4261 0.4748 0.0497  -0.0954 0.0306  239 LEU A CD1 
1544 C CD2 . LEU A 199 ? 0.4482 0.4118 0.4845 0.0351  -0.1236 0.0375  239 LEU A CD2 
1545 N N   . CYS A 200 ? 0.4001 0.3897 0.4352 0.0348  -0.0780 0.0417  240 CYS A N   
1546 C CA  . CYS A 200 ? 0.4327 0.4146 0.4533 0.0311  -0.0686 0.0427  240 CYS A CA  
1547 C C   . CYS A 200 ? 0.4706 0.4372 0.4855 0.0216  -0.0767 0.0460  240 CYS A C   
1548 O O   . CYS A 200 ? 0.4484 0.3952 0.4401 0.0134  -0.0748 0.0457  240 CYS A O   
1549 C CB  . CYS A 200 ? 0.3635 0.3638 0.3967 0.0391  -0.0562 0.0431  240 CYS A CB  
1550 S SG  . CYS A 200 ? 0.3964 0.3876 0.4152 0.0372  -0.0448 0.0440  240 CYS A SG  
1551 N N   . ASP A 201 ? 0.4422 0.4174 0.4790 0.0221  -0.0853 0.0482  241 ASP A N   
1552 C CA  . ASP A 201 ? 0.4684 0.4294 0.5021 0.0126  -0.0957 0.0514  241 ASP A CA  
1553 C C   . ASP A 201 ? 0.4683 0.4018 0.4769 0.0022  -0.1101 0.0523  241 ASP A C   
1554 O O   . ASP A 201 ? 0.5032 0.4152 0.4904 -0.0085 -0.1138 0.0541  241 ASP A O   
1555 C CB  . ASP A 201 ? 0.4586 0.4358 0.5266 0.0150  -0.1039 0.0524  241 ASP A CB  
1556 C CG  . ASP A 201 ? 0.5456 0.5408 0.6302 0.0188  -0.0901 0.0524  241 ASP A CG  
1557 O OD1 . ASP A 201 ? 0.5552 0.5447 0.6225 0.0175  -0.0786 0.0536  241 ASP A OD1 
1558 O OD2 . ASP A 201 ? 0.5705 0.5843 0.6861 0.0224  -0.0905 0.0509  241 ASP A OD2 
1559 N N   . LEU A 202 ? 0.4464 0.3776 0.4545 0.0042  -0.1186 0.0512  242 LEU A N   
1560 C CA  . LEU A 202 ? 0.5041 0.4056 0.4846 -0.0070 -0.1336 0.0528  242 LEU A CA  
1561 C C   . LEU A 202 ? 0.5200 0.3998 0.4617 -0.0159 -0.1219 0.0503  242 LEU A C   
1562 O O   . LEU A 202 ? 0.5401 0.3894 0.4510 -0.0298 -0.1306 0.0517  242 LEU A O   
1563 C CB  . LEU A 202 ? 0.5381 0.4416 0.5269 -0.0022 -0.1444 0.0521  242 LEU A CB  
1564 C CG  . LEU A 202 ? 0.5472 0.4628 0.5723 0.0033  -0.1617 0.0537  242 LEU A CG  
1565 C CD1 . LEU A 202 ? 0.5723 0.4920 0.6068 0.0101  -0.1677 0.0516  242 LEU A CD1 
1566 C CD2 . LEU A 202 ? 0.5754 0.4672 0.5930 -0.0079 -0.1847 0.0588  242 LEU A CD2 
1567 N N   . TYR A 203 ? 0.4879 0.3815 0.4307 -0.0090 -0.1024 0.0460  243 TYR A N   
1568 C CA  . TYR A 203 ? 0.5111 0.3871 0.4243 -0.0166 -0.0893 0.0416  243 TYR A CA  
1569 C C   . TYR A 203 ? 0.5274 0.3986 0.4344 -0.0201 -0.0777 0.0406  243 TYR A C   
1570 O O   . TYR A 203 ? 0.5702 0.4150 0.4479 -0.0329 -0.0748 0.0383  243 TYR A O   
1571 C CB  . TYR A 203 ? 0.5195 0.4118 0.4398 -0.0076 -0.0761 0.0366  243 TYR A CB  
1572 C CG  . TYR A 203 ? 0.5381 0.4118 0.4311 -0.0167 -0.0645 0.0305  243 TYR A CG  
1573 C CD1 . TYR A 203 ? 0.5838 0.4370 0.4529 -0.0263 -0.0706 0.0289  243 TYR A CD1 
1574 C CD2 . TYR A 203 ? 0.5859 0.4613 0.4778 -0.0163 -0.0470 0.0255  243 TYR A CD2 
1575 C CE1 . TYR A 203 ? 0.6267 0.4623 0.4707 -0.0365 -0.0574 0.0220  243 TYR A CE1 
1576 C CE2 . TYR A 203 ? 0.6311 0.4907 0.5026 -0.0251 -0.0341 0.0179  243 TYR A CE2 
1577 C CZ  . TYR A 203 ? 0.6378 0.4779 0.4849 -0.0357 -0.0384 0.0158  243 TYR A CZ  
1578 O OH  . TYR A 203 ? 0.7269 0.5509 0.5535 -0.0463 -0.0233 0.0070  243 TYR A OH  
1579 N N   . TYR A 204 ? 0.4944 0.3883 0.4265 -0.0099 -0.0709 0.0421  244 TYR A N   
1580 C CA  . TYR A 204 ? 0.4773 0.3675 0.4058 -0.0114 -0.0593 0.0411  244 TYR A CA  
1581 C C   . TYR A 204 ? 0.4857 0.3724 0.4197 -0.0158 -0.0677 0.0461  244 TYR A C   
1582 O O   . TYR A 204 ? 0.5472 0.4279 0.4765 -0.0183 -0.0592 0.0457  244 TYR A O   
1583 C CB  . TYR A 204 ? 0.4328 0.3460 0.3810 0.0018  -0.0456 0.0396  244 TYR A CB  
1584 C CG  . TYR A 204 ? 0.4565 0.3738 0.4020 0.0059  -0.0366 0.0340  244 TYR A CG  
1585 C CD1 . TYR A 204 ? 0.4856 0.3876 0.4152 -0.0001 -0.0250 0.0275  244 TYR A CD1 
1586 C CD2 . TYR A 204 ? 0.4418 0.3780 0.4020 0.0151  -0.0389 0.0341  244 TYR A CD2 
1587 C CE1 . TYR A 204 ? 0.4392 0.3465 0.3704 0.0031  -0.0164 0.0213  244 TYR A CE1 
1588 C CE2 . TYR A 204 ? 0.4641 0.4043 0.4229 0.0182  -0.0315 0.0288  244 TYR A CE2 
1589 C CZ  . TYR A 204 ? 0.4554 0.3819 0.4011 0.0122  -0.0205 0.0225  244 TYR A CZ  
1590 O OH  . TYR A 204 ? 0.5003 0.4325 0.4487 0.0149  -0.0128 0.0163  244 TYR A OH  
1591 N N   . ILE A 205 ? 0.4918 0.3591 0.3747 0.0261  -0.0880 -0.0338 245 ILE A N   
1592 C CA  . ILE A 205 ? 0.5035 0.3670 0.3968 0.0190  -0.1010 -0.0360 245 ILE A CA  
1593 C C   . ILE A 205 ? 0.4980 0.3600 0.4107 0.0151  -0.0975 -0.0356 245 ILE A C   
1594 O O   . ILE A 205 ? 0.5712 0.4251 0.4895 0.0084  -0.1065 -0.0391 245 ILE A O   
1595 C CB  . ILE A 205 ? 0.5897 0.4372 0.4583 0.0178  -0.1115 -0.0450 245 ILE A CB  
1596 C CG1 . ILE A 205 ? 0.6393 0.4855 0.4805 0.0233  -0.1096 -0.0457 245 ILE A CG1 
1597 C CG2 . ILE A 205 ? 0.6528 0.5013 0.5321 0.0101  -0.1280 -0.0458 245 ILE A CG2 
1598 C CD1 . ILE A 205 ? 0.6371 0.4958 0.4828 0.0233  -0.1129 -0.0369 245 ILE A CD1 
1599 N N   . ASN A 206 ? 0.5033 0.3727 0.4257 0.0188  -0.0850 -0.0309 246 ASN A N   
1600 C CA  . ASN A 206 ? 0.4853 0.3543 0.4247 0.0157  -0.0800 -0.0284 246 ASN A CA  
1601 C C   . ASN A 206 ? 0.4822 0.3630 0.4283 0.0216  -0.0668 -0.0229 246 ASN A C   
1602 O O   . ASN A 206 ? 0.5243 0.4106 0.4609 0.0275  -0.0620 -0.0225 246 ASN A O   
1603 C CB  . ASN A 206 ? 0.5862 0.4340 0.5126 0.0155  -0.0811 -0.0351 246 ASN A CB  
1604 C CG  . ASN A 206 ? 0.6438 0.4875 0.5882 0.0082  -0.0814 -0.0317 246 ASN A CG  
1605 O OD1 . ASN A 206 ? 0.6972 0.5561 0.6622 0.0055  -0.0761 -0.0239 246 ASN A OD1 
1606 N ND2 . ASN A 206 ? 0.6643 0.4869 0.6002 0.0048  -0.0876 -0.0376 246 ASN A ND2 
1607 N N   . SER A 207 ? 0.4568 0.3414 0.4187 0.0195  -0.0610 -0.0186 247 SER A N   
1608 C CA  . SER A 207 ? 0.5022 0.3989 0.4707 0.0249  -0.0495 -0.0138 247 SER A CA  
1609 C C   . SER A 207 ? 0.4757 0.3700 0.4538 0.0229  -0.0439 -0.0101 247 SER A C   
1610 O O   . SER A 207 ? 0.4843 0.3730 0.4712 0.0150  -0.0489 -0.0089 247 SER A O   
1611 C CB  . SER A 207 ? 0.4991 0.4149 0.4832 0.0248  -0.0492 -0.0089 247 SER A CB  
1612 O OG  . SER A 207 ? 0.5608 0.4839 0.5629 0.0176  -0.0569 -0.0068 247 SER A OG  
1613 N N   . PRO A 208 ? 0.4856 0.3839 0.4618 0.0291  -0.0339 -0.0079 248 PRO A N   
1614 C CA  . PRO A 208 ? 0.4909 0.3866 0.4738 0.0277  -0.0285 -0.0031 248 PRO A CA  
1615 C C   . PRO A 208 ? 0.4704 0.3838 0.4746 0.0224  -0.0255 0.0038  248 PRO A C   
1616 O O   . PRO A 208 ? 0.4390 0.3689 0.4525 0.0238  -0.0246 0.0047  248 PRO A O   
1617 C CB  . PRO A 208 ? 0.4667 0.3637 0.4396 0.0374  -0.0199 -0.0037 248 PRO A CB  
1618 C CG  . PRO A 208 ? 0.4985 0.3981 0.4599 0.0428  -0.0205 -0.0093 248 PRO A CG  
1619 C CD  . PRO A 208 ? 0.4407 0.3459 0.4081 0.0373  -0.0277 -0.0093 248 PRO A CD  
1620 N N   . GLU A 209 ? 0.4757 0.3852 0.4873 0.0166  -0.0235 0.0088  249 GLU A N   
1621 C CA  . GLU A 209 ? 0.4579 0.3860 0.4887 0.0121  -0.0180 0.0157  249 GLU A CA  
1622 C C   . GLU A 209 ? 0.4794 0.4179 0.5075 0.0202  -0.0076 0.0184  249 GLU A C   
1623 O O   . GLU A 209 ? 0.4797 0.4100 0.4926 0.0282  -0.0049 0.0158  249 GLU A O   
1624 C CB  . GLU A 209 ? 0.5045 0.4250 0.5429 0.0018  -0.0185 0.0214  249 GLU A CB  
1625 C CG  . GLU A 209 ? 0.5967 0.5045 0.6377 -0.0075 -0.0298 0.0183  249 GLU A CG  
1626 C CD  . GLU A 209 ? 0.7448 0.6713 0.8042 -0.0128 -0.0358 0.0171  249 GLU A CD  
1627 O OE1 . GLU A 209 ? 0.7746 0.7247 0.8499 -0.0115 -0.0300 0.0206  249 GLU A OE1 
1628 O OE2 . GLU A 209 ? 0.8185 0.7362 0.8764 -0.0174 -0.0470 0.0120  249 GLU A OE2 
1629 N N   . LEU A 210 ? 0.4406 0.3985 0.4843 0.0184  -0.0017 0.0230  250 LEU A N   
1630 C CA  . LEU A 210 ? 0.4224 0.3914 0.4644 0.0252  0.0078  0.0253  250 LEU A CA  
1631 C C   . LEU A 210 ? 0.4236 0.3929 0.4681 0.0204  0.0144  0.0332  250 LEU A C   
1632 O O   . LEU A 210 ? 0.4719 0.4477 0.5307 0.0110  0.0144  0.0378  250 LEU A O   
1633 C CB  . LEU A 210 ? 0.4064 0.3972 0.4621 0.0282  0.0101  0.0236  250 LEU A CB  
1634 C CG  . LEU A 210 ? 0.3907 0.3950 0.4469 0.0343  0.0198  0.0253  250 LEU A CG  
1635 C CD1 . LEU A 210 ? 0.3523 0.3489 0.3915 0.0430  0.0215  0.0217  250 LEU A CD1 
1636 C CD2 . LEU A 210 ? 0.3690 0.3940 0.4418 0.0364  0.0212  0.0233  250 LEU A CD2 
1637 N N   . GLU A 211 ? 0.4273 0.3899 0.4579 0.0264  0.0196  0.0353  251 GLU A N   
1638 C CA  . GLU A 211 ? 0.4359 0.4005 0.4657 0.0235  0.0270  0.0438  251 GLU A CA  
1639 C C   . GLU A 211 ? 0.4579 0.4387 0.4849 0.0320  0.0349  0.0433  251 GLU A C   
1640 O O   . GLU A 211 ? 0.4921 0.4680 0.5061 0.0411  0.0346  0.0393  251 GLU A O   
1641 C CB  . GLU A 211 ? 0.4449 0.3843 0.4585 0.0235  0.0248  0.0475  251 GLU A CB  
1642 C CG  . GLU A 211 ? 0.4994 0.4197 0.5144 0.0149  0.0165  0.0471  251 GLU A CG  
1643 C CD  . GLU A 211 ? 0.6113 0.5044 0.6105 0.0157  0.0140  0.0507  251 GLU A CD  
1644 O OE1 . GLU A 211 ? 0.6524 0.5417 0.6387 0.0244  0.0179  0.0529  251 GLU A OE1 
1645 O OE2 . GLU A 211 ? 0.6737 0.5485 0.6733 0.0079  0.0073  0.0510  251 GLU A OE2 
1646 N N   . LEU A 212 ? 0.4217 0.4227 0.4612 0.0292  0.0417  0.0466  252 LEU A N   
1647 C CA  . LEU A 212 ? 0.4608 0.4792 0.4995 0.0370  0.0487  0.0443  252 LEU A CA  
1648 C C   . LEU A 212 ? 0.5062 0.5296 0.5389 0.0354  0.0577  0.0527  252 LEU A C   
1649 O O   . LEU A 212 ? 0.5887 0.6182 0.6310 0.0261  0.0618  0.0599  252 LEU A O   
1650 C CB  . LEU A 212 ? 0.4483 0.4877 0.5060 0.0372  0.0495  0.0397  252 LEU A CB  
1651 C CG  . LEU A 212 ? 0.5141 0.5620 0.5721 0.0468  0.0488  0.0312  252 LEU A CG  
1652 C CD1 . LEU A 212 ? 0.5220 0.5919 0.5996 0.0470  0.0519  0.0290  252 LEU A CD1 
1653 C CD2 . LEU A 212 ? 0.5034 0.5507 0.5457 0.0551  0.0533  0.0294  252 LEU A CD2 
1654 N N   . GLU A 213 ? 0.4425 0.4643 0.4593 0.0439  0.0607  0.0520  253 GLU A N   
1655 C CA  . GLU A 213 ? 0.4591 0.4854 0.4656 0.0443  0.0689  0.0596  253 GLU A CA  
1656 C C   . GLU A 213 ? 0.4511 0.4951 0.4546 0.0536  0.0739  0.0534  253 GLU A C   
1657 O O   . GLU A 213 ? 0.4614 0.5046 0.4624 0.0612  0.0693  0.0446  253 GLU A O   
1658 C CB  . GLU A 213 ? 0.6368 0.6411 0.6232 0.0471  0.0657  0.0647  253 GLU A CB  
1659 C CG  . GLU A 213 ? 0.9263 0.9177 0.9076 0.0381  0.0678  0.0771  253 GLU A CG  
1660 C CD  . GLU A 213 ? 1.1060 1.0756 1.0656 0.0441  0.0641  0.0815  253 GLU A CD  
1661 O OE1 . GLU A 213 ? 1.1160 1.0911 1.0633 0.0541  0.0655  0.0791  253 GLU A OE1 
1662 O OE2 . GLU A 213 ? 1.1944 1.1413 1.1498 0.0394  0.0590  0.0867  253 GLU A OE2 
1663 N N   . GLU A 214 ? 0.4643 0.5238 0.4671 0.0526  0.0834  0.0579  254 GLU A N   
1664 C CA  . GLU A 214 ? 0.4824 0.5573 0.4802 0.0619  0.0879  0.0509  254 GLU A CA  
1665 C C   . GLU A 214 ? 0.5126 0.5914 0.4929 0.0633  0.0958  0.0584  254 GLU A C   
1666 O O   . GLU A 214 ? 0.4903 0.5679 0.4687 0.0551  0.1013  0.0697  254 GLU A O   
1667 C CB  . GLU A 214 ? 0.4881 0.5847 0.5057 0.0625  0.0917  0.0442  254 GLU A CB  
1668 C CG  . GLU A 214 ? 0.5343 0.6487 0.5625 0.0555  0.1018  0.0510  254 GLU A CG  
1669 C CD  . GLU A 214 ? 0.6878 0.8249 0.7372 0.0583  0.1049  0.0430  254 GLU A CD  
1670 O OE1 . GLU A 214 ? 0.7439 0.8885 0.8140 0.0511  0.1041  0.0450  254 GLU A OE1 
1671 O OE2 . GLU A 214 ? 0.6965 0.8435 0.7422 0.0682  0.1074  0.0342  254 GLU A OE2 
1672 N N   . LEU A 215 ? 0.4410 0.5240 0.4078 0.0732  0.0960  0.0521  255 LEU A N   
1673 C CA  . LEU A 215 ? 0.5312 0.6194 0.4786 0.0762  0.1028  0.0576  255 LEU A CA  
1674 C C   . LEU A 215 ? 0.4948 0.6002 0.4400 0.0855  0.1058  0.0461  255 LEU A C   
1675 O O   . LEU A 215 ? 0.4421 0.5433 0.3847 0.0928  0.0985  0.0362  255 LEU A O   
1676 C CB  . LEU A 215 ? 0.5230 0.5912 0.4492 0.0796  0.0966  0.0632  255 LEU A CB  
1677 C CG  . LEU A 215 ? 0.5744 0.6469 0.4773 0.0841  0.1019  0.0687  255 LEU A CG  
1678 C CD1 . LEU A 215 ? 0.5670 0.6486 0.4683 0.0755  0.1137  0.0805  255 LEU A CD1 
1679 C CD2 . LEU A 215 ? 0.5961 0.6481 0.4796 0.0888  0.0936  0.0741  255 LEU A CD2 
1680 N N   . ASN A 216 ? 0.4547 0.5795 0.4019 0.0849  0.1166  0.0468  256 ASN A N   
1681 C CA  . ASN A 216 ? 0.4983 0.6387 0.4394 0.0945  0.1204  0.0359  256 ASN A CA  
1682 C C   . ASN A 216 ? 0.5095 0.6490 0.4226 0.0979  0.1242  0.0419  256 ASN A C   
1683 O O   . ASN A 216 ? 0.4804 0.6321 0.3858 0.0953  0.1352  0.0490  256 ASN A O   
1684 C CB  . ASN A 216 ? 0.4927 0.6562 0.4518 0.0936  0.1301  0.0320  256 ASN A CB  
1685 C CG  . ASN A 216 ? 0.5685 0.7460 0.5235 0.1047  0.1327  0.0180  256 ASN A CG  
1686 O OD1 . ASN A 216 ? 0.6010 0.7746 0.5347 0.1115  0.1307  0.0140  256 ASN A OD1 
1687 N ND2 . ASN A 216 ? 0.5532 0.7467 0.5288 0.1070  0.1366  0.0099  256 ASN A ND2 
1688 N N   . ALA A 217 ? 0.5183 0.6438 0.4158 0.1039  0.1148  0.0393  257 ALA A N   
1689 C CA  . ALA A 217 ? 0.5614 0.6850 0.4310 0.1082  0.1162  0.0448  257 ALA A CA  
1690 C C   . ALA A 217 ? 0.6704 0.8135 0.5299 0.1152  0.1237  0.0362  257 ALA A C   
1691 O O   . ALA A 217 ? 0.6858 0.8351 0.5248 0.1157  0.1313  0.0436  257 ALA A O   
1692 C CB  . ALA A 217 ? 0.5493 0.6571 0.4076 0.1143  0.1034  0.0419  257 ALA A CB  
1693 N N   . LYS A 218 ? 0.7718 0.9236 0.6446 0.1206  0.1216  0.0207  258 LYS A N   
1694 C CA  . LYS A 218 ? 0.9248 1.0941 0.7899 0.1283  0.1280  0.0097  258 LYS A CA  
1695 C C   . LYS A 218 ? 0.9466 1.1346 0.8128 0.1246  0.1436  0.0163  258 LYS A C   
1696 O O   . LYS A 218 ? 0.9551 1.1537 0.7997 0.1283  0.1515  0.0176  258 LYS A O   
1697 C CB  . LYS A 218 ? 0.9706 1.1423 0.8544 0.1333  0.1224  -0.0071 258 LYS A CB  
1698 C CG  . LYS A 218 ? 1.0538 1.2356 0.9266 0.1436  0.1232  -0.0225 258 LYS A CG  
1699 C CD  . LYS A 218 ? 1.1140 1.2881 0.9608 0.1487  0.1155  -0.0247 258 LYS A CD  
1700 C CE  . LYS A 218 ? 1.1065 1.2856 0.9457 0.1583  0.1117  -0.0431 258 LYS A CE  
1701 N NZ  . LYS A 218 ? 1.0584 1.2270 0.9152 0.1589  0.1002  -0.0547 258 LYS A NZ  
1702 N N   . SER A 219 ? 0.9531 1.1469 0.8444 0.1170  0.1483  0.0207  259 SER A N   
1703 C CA  . SER A 219 ? 0.8794 1.0943 0.7777 0.1121  0.1635  0.0270  259 SER A CA  
1704 C C   . SER A 219 ? 0.7630 0.9721 0.6791 0.0988  0.1643  0.0410  259 SER A C   
1705 O O   . SER A 219 ? 0.7152 0.9287 0.6588 0.0956  0.1624  0.0371  259 SER A O   
1706 C CB  . SER A 219 ? 0.8943 1.1303 0.8111 0.1190  0.1690  0.0121  259 SER A CB  
1707 O OG  . SER A 219 ? 0.9209 1.1543 0.8274 0.1310  0.1626  -0.0041 259 SER A OG  
1708 N N   . PRO A 220 ? 0.7215 0.9197 0.6221 0.0909  0.1664  0.0573  260 PRO A N   
1709 C CA  . PRO A 220 ? 0.7126 0.8981 0.6278 0.0782  0.1637  0.0697  260 PRO A CA  
1710 C C   . PRO A 220 ? 0.7783 0.9841 0.7221 0.0697  0.1726  0.0715  260 PRO A C   
1711 O O   . PRO A 220 ? 0.8310 1.0624 0.7778 0.0700  0.1860  0.0709  260 PRO A O   
1712 C CB  . PRO A 220 ? 0.6916 0.8641 0.5810 0.0724  0.1667  0.0868  260 PRO A CB  
1713 C CG  . PRO A 220 ? 0.7108 0.8794 0.5716 0.0844  0.1632  0.0812  260 PRO A CG  
1714 C CD  . PRO A 220 ? 0.7122 0.9040 0.5790 0.0941  0.1682  0.0644  260 PRO A CD  
1715 N N   . GLY A 221 ? 0.7401 0.9355 0.7055 0.0622  0.1649  0.0733  261 GLY A N   
1716 C CA  . GLY A 221 ? 0.7622 0.9755 0.7577 0.0538  0.1701  0.0744  261 GLY A CA  
1717 C C   . GLY A 221 ? 0.7124 0.9462 0.7298 0.0626  0.1704  0.0587  261 GLY A C   
1718 O O   . GLY A 221 ? 0.7021 0.9491 0.7474 0.0569  0.1713  0.0582  261 GLY A O   
1719 N N   . GLN A 222 ? 0.6374 0.8736 0.6433 0.0763  0.1689  0.0457  262 GLN A N   
1720 C CA  . GLN A 222 ? 0.6213 0.8725 0.6459 0.0860  0.1678  0.0302  262 GLN A CA  
1721 C C   . GLN A 222 ? 0.5578 0.7903 0.5949 0.0875  0.1523  0.0236  262 GLN A C   
1722 O O   . GLN A 222 ? 0.5169 0.7250 0.5406 0.0860  0.1426  0.0265  262 GLN A O   
1723 C CB  . GLN A 222 ? 0.5930 0.8509 0.5988 0.0995  0.1713  0.0186  262 GLN A CB  
1724 C CG  . GLN A 222 ? 0.7278 1.0084 0.7215 0.0998  0.1876  0.0227  262 GLN A CG  
1725 C CD  . GLN A 222 ? 0.7995 1.1101 0.8208 0.0964  0.1993  0.0229  262 GLN A CD  
1726 O OE1 . GLN A 222 ? 0.7616 1.0896 0.7977 0.1066  0.2016  0.0091  262 GLN A OE1 
1727 N NE2 . GLN A 222 ? 0.8003 1.1172 0.8298 0.0821  0.2061  0.0385  262 GLN A NE2 
1728 N N   . PRO A 223 ? 0.5353 0.7792 0.5975 0.0910  0.1499  0.0149  263 PRO A N   
1729 C CA  . PRO A 223 ? 0.4739 0.6998 0.5452 0.0928  0.1355  0.0089  263 PRO A CA  
1730 C C   . PRO A 223 ? 0.4636 0.6719 0.5151 0.1019  0.1280  0.0002  263 PRO A C   
1731 O O   . PRO A 223 ? 0.4873 0.7022 0.5246 0.1102  0.1330  -0.0066 263 PRO A O   
1732 C CB  . PRO A 223 ? 0.5047 0.7494 0.6035 0.0979  0.1358  0.0002  263 PRO A CB  
1733 C CG  . PRO A 223 ? 0.5156 0.7892 0.6260 0.0941  0.1501  0.0053  263 PRO A CG  
1734 C CD  . PRO A 223 ? 0.5641 0.8386 0.6476 0.0938  0.1601  0.0104  263 PRO A CD  
1735 N N   . ILE A 224 ? 0.4300 0.6165 0.4803 0.0997  0.1160  0.0002  264 ILE A N   
1736 C CA  . ILE A 224 ? 0.4221 0.5922 0.4565 0.1061  0.1081  -0.0071 264 ILE A CA  
1737 C C   . ILE A 224 ? 0.4287 0.5977 0.4765 0.1129  0.1015  -0.0190 264 ILE A C   
1738 O O   . ILE A 224 ? 0.4453 0.6075 0.5078 0.1096  0.0943  -0.0183 264 ILE A O   
1739 C CB  . ILE A 224 ? 0.4298 0.5781 0.4545 0.1000  0.0999  -0.0001 264 ILE A CB  
1740 C CG1 . ILE A 224 ? 0.4166 0.5624 0.4238 0.0956  0.1055  0.0109  264 ILE A CG1 
1741 C CG2 . ILE A 224 ? 0.3583 0.4925 0.3738 0.1056  0.0908  -0.0085 264 ILE A CG2 
1742 C CD1 . ILE A 224 ? 0.4307 0.5549 0.4289 0.0909  0.0975  0.0175  264 ILE A CD1 
1743 N N   . GLN A 225 ? 0.4350 0.6094 0.4765 0.1226  0.1033  -0.0299 265 GLN A N   
1744 C CA  . GLN A 225 ? 0.4643 0.6337 0.5153 0.1298  0.0963  -0.0417 265 GLN A CA  
1745 C C   . GLN A 225 ? 0.5254 0.6831 0.5584 0.1354  0.0915  -0.0505 265 GLN A C   
1746 O O   . GLN A 225 ? 0.5831 0.7444 0.5979 0.1372  0.0961  -0.0507 265 GLN A O   
1747 C CB  . GLN A 225 ? 0.4332 0.6224 0.4996 0.1375  0.1028  -0.0491 265 GLN A CB  
1748 C CG  . GLN A 225 ? 0.5111 0.7172 0.5981 0.1322  0.1083  -0.0414 265 GLN A CG  
1749 C CD  . GLN A 225 ? 0.5960 0.8250 0.6995 0.1413  0.1153  -0.0498 265 GLN A CD  
1750 O OE1 . GLN A 225 ? 0.6019 0.8411 0.6953 0.1497  0.1228  -0.0578 265 GLN A OE1 
1751 N NE2 . GLN A 225 ? 0.6120 0.8497 0.7407 0.1406  0.1125  -0.0489 265 GLN A NE2 
1752 N N   . VAL A 226 ? 0.4661 0.6097 0.5044 0.1376  0.0818  -0.0576 266 VAL A N   
1753 C CA  . VAL A 226 ? 0.4588 0.5918 0.4844 0.1424  0.0763  -0.0677 266 VAL A CA  
1754 C C   . VAL A 226 ? 0.4761 0.6014 0.5142 0.1479  0.0698  -0.0777 266 VAL A C   
1755 O O   . VAL A 226 ? 0.4640 0.5894 0.5193 0.1473  0.0677  -0.0752 266 VAL A O   
1756 C CB  . VAL A 226 ? 0.4505 0.5683 0.4651 0.1359  0.0690  -0.0634 266 VAL A CB  
1757 C CG1 . VAL A 226 ? 0.5418 0.6649 0.5405 0.1333  0.0741  -0.0556 266 VAL A CG1 
1758 C CG2 . VAL A 226 ? 0.3694 0.4761 0.3954 0.1288  0.0629  -0.0563 266 VAL A CG2 
1759 N N   . VAL A 227 ? 0.4964 0.6142 0.5254 0.1534  0.0659  -0.0891 267 VAL A N   
1760 C CA  . VAL A 227 ? 0.4739 0.5774 0.5116 0.1572  0.0574  -0.0981 267 VAL A CA  
1761 C C   . VAL A 227 ? 0.4781 0.5633 0.5163 0.1480  0.0481  -0.0920 267 VAL A C   
1762 O O   . VAL A 227 ? 0.5280 0.6076 0.5540 0.1432  0.0455  -0.0911 267 VAL A O   
1763 C CB  . VAL A 227 ? 0.4292 0.5292 0.4561 0.1652  0.0559  -0.1129 267 VAL A CB  
1764 C CG1 . VAL A 227 ? 0.5096 0.5929 0.5464 0.1696  0.0472  -0.1219 267 VAL A CG1 
1765 C CG2 . VAL A 227 ? 0.4334 0.5540 0.4550 0.1741  0.0668  -0.1185 267 VAL A CG2 
1766 N N   . TYR A 228 ? 0.4654 0.5426 0.5174 0.1457  0.0432  -0.0876 268 TYR A N   
1767 C CA  . TYR A 228 ? 0.4787 0.5398 0.5296 0.1367  0.0356  -0.0812 268 TYR A CA  
1768 C C   . TYR A 228 ? 0.4958 0.5450 0.5596 0.1372  0.0286  -0.0801 268 TYR A C   
1769 O O   . TYR A 228 ? 0.4480 0.5030 0.5234 0.1447  0.0295  -0.0834 268 TYR A O   
1770 C CB  . TYR A 228 ? 0.4552 0.5218 0.5025 0.1288  0.0389  -0.0694 268 TYR A CB  
1771 C CG  . TYR A 228 ? 0.4833 0.5379 0.5226 0.1210  0.0336  -0.0661 268 TYR A CG  
1772 C CD1 . TYR A 228 ? 0.4559 0.5098 0.4837 0.1207  0.0329  -0.0711 268 TYR A CD1 
1773 C CD2 . TYR A 228 ? 0.4457 0.4911 0.4890 0.1142  0.0293  -0.0584 268 TYR A CD2 
1774 C CE1 . TYR A 228 ? 0.4364 0.4827 0.4595 0.1138  0.0285  -0.0685 268 TYR A CE1 
1775 C CE2 . TYR A 228 ? 0.4446 0.4816 0.4810 0.1074  0.0258  -0.0557 268 TYR A CE2 
1776 C CZ  . TYR A 228 ? 0.4383 0.4767 0.4660 0.1072  0.0257  -0.0608 268 TYR A CZ  
1777 O OH  . TYR A 228 ? 0.4368 0.4702 0.4603 0.1007  0.0227  -0.0586 268 TYR A OH  
1778 N N   . VAL A 229 ? 0.4950 0.5282 0.5563 0.1295  0.0217  -0.0753 269 VAL A N   
1779 C CA  . VAL A 229 ? 0.5008 0.5211 0.5710 0.1281  0.0144  -0.0711 269 VAL A CA  
1780 C C   . VAL A 229 ? 0.5044 0.5309 0.5779 0.1222  0.0157  -0.0599 269 VAL A C   
1781 O O   . VAL A 229 ? 0.4676 0.4910 0.5326 0.1141  0.0159  -0.0539 269 VAL A O   
1782 C CB  . VAL A 229 ? 0.4997 0.4987 0.5638 0.1220  0.0066  -0.0713 269 VAL A CB  
1783 C CG1 . VAL A 229 ? 0.4604 0.4450 0.5311 0.1208  -0.0011 -0.0655 269 VAL A CG1 
1784 C CG2 . VAL A 229 ? 0.5943 0.5854 0.6552 0.1268  0.0043  -0.0832 269 VAL A CG2 
1785 N N   . PRO A 230 ? 0.4936 0.5295 0.5798 0.1262  0.0163  -0.0576 270 PRO A N   
1786 C CA  . PRO A 230 ? 0.4779 0.5212 0.5672 0.1201  0.0177  -0.0480 270 PRO A CA  
1787 C C   . PRO A 230 ? 0.4568 0.4844 0.5402 0.1121  0.0107  -0.0409 270 PRO A C   
1788 O O   . PRO A 230 ? 0.4364 0.4660 0.5142 0.1053  0.0125  -0.0346 270 PRO A O   
1789 C CB  . PRO A 230 ? 0.4916 0.5476 0.5987 0.1265  0.0177  -0.0487 270 PRO A CB  
1790 C CG  . PRO A 230 ? 0.4891 0.5514 0.6001 0.1370  0.0212  -0.0593 270 PRO A CG  
1791 C CD  . PRO A 230 ? 0.4771 0.5195 0.5764 0.1369  0.0161  -0.0645 270 PRO A CD  
1792 N N   . SER A 231 ? 0.4429 0.4541 0.5262 0.1128  0.0027  -0.0417 271 SER A N   
1793 C CA  . SER A 231 ? 0.4401 0.4373 0.5159 0.1048  -0.0032 -0.0342 271 SER A CA  
1794 C C   . SER A 231 ? 0.4497 0.4430 0.5117 0.0973  0.0001  -0.0331 271 SER A C   
1795 O O   . SER A 231 ? 0.4729 0.4622 0.5276 0.0905  -0.0008 -0.0267 271 SER A O   
1796 C CB  . SER A 231 ? 0.4437 0.4228 0.5209 0.1069  -0.0124 -0.0341 271 SER A CB  
1797 O OG  . SER A 231 ? 0.5091 0.4779 0.5822 0.1082  -0.0130 -0.0405 271 SER A OG  
1798 N N   . HIS A 232 ? 0.4098 0.4053 0.4681 0.0991  0.0038  -0.0397 272 HIS A N   
1799 C CA  . HIS A 232 ? 0.4518 0.4478 0.4995 0.0929  0.0068  -0.0391 272 HIS A CA  
1800 C C   . HIS A 232 ? 0.4393 0.4476 0.4839 0.0914  0.0126  -0.0350 272 HIS A C   
1801 O O   . HIS A 232 ? 0.3988 0.4053 0.4362 0.0856  0.0131  -0.0307 272 HIS A O   
1802 C CB  . HIS A 232 ? 0.4818 0.4792 0.5270 0.0956  0.0083  -0.0478 272 HIS A CB  
1803 C CG  . HIS A 232 ? 0.5456 0.5270 0.5916 0.0947  0.0020  -0.0519 272 HIS A CG  
1804 N ND1 . HIS A 232 ? 0.5575 0.5362 0.6001 0.0941  0.0013  -0.0596 272 HIS A ND1 
1805 C CD2 . HIS A 232 ? 0.5623 0.5281 0.6116 0.0942  -0.0046 -0.0493 272 HIS A CD2 
1806 C CE1 . HIS A 232 ? 0.5781 0.5391 0.6224 0.0925  -0.0052 -0.0616 272 HIS A CE1 
1807 N NE2 . HIS A 232 ? 0.5823 0.5347 0.6302 0.0929  -0.0088 -0.0549 272 HIS A NE2 
1808 N N   . LEU A 233 ? 0.3862 0.4071 0.4361 0.0965  0.0172  -0.0364 273 LEU A N   
1809 C CA  . LEU A 233 ? 0.4002 0.4302 0.4472 0.0945  0.0221  -0.0315 273 LEU A CA  
1810 C C   . LEU A 233 ? 0.3571 0.3827 0.4062 0.0897  0.0189  -0.0245 273 LEU A C   
1811 O O   . LEU A 233 ? 0.3656 0.3901 0.4078 0.0855  0.0201  -0.0204 273 LEU A O   
1812 C CB  . LEU A 233 ? 0.3952 0.4396 0.4477 0.0998  0.0282  -0.0334 273 LEU A CB  
1813 C CG  . LEU A 233 ? 0.3815 0.4341 0.4314 0.0971  0.0335  -0.0273 273 LEU A CG  
1814 C CD1 . LEU A 233 ? 0.3945 0.4443 0.4309 0.0952  0.0352  -0.0263 273 LEU A CD1 
1815 C CD2 . LEU A 233 ? 0.3690 0.4368 0.4249 0.1016  0.0403  -0.0286 273 LEU A CD2 
1816 N N   . TYR A 234 ? 0.3514 0.3741 0.4097 0.0910  0.0139  -0.0236 274 TYR A N   
1817 C CA  . TYR A 234 ? 0.3976 0.4159 0.4570 0.0865  0.0093  -0.0175 274 TYR A CA  
1818 C C   . TYR A 234 ? 0.4092 0.4153 0.4555 0.0807  0.0066  -0.0147 274 TYR A C   
1819 O O   . TYR A 234 ? 0.3973 0.4020 0.4377 0.0765  0.0067  -0.0110 274 TYR A O   
1820 C CB  . TYR A 234 ? 0.3648 0.3813 0.4357 0.0898  0.0026  -0.0174 274 TYR A CB  
1821 C CG  . TYR A 234 ? 0.4215 0.4328 0.4919 0.0852  -0.0038 -0.0115 274 TYR A CG  
1822 C CD1 . TYR A 234 ? 0.4363 0.4581 0.5157 0.0836  -0.0036 -0.0090 274 TYR A CD1 
1823 C CD2 . TYR A 234 ? 0.3888 0.3850 0.4488 0.0816  -0.0102 -0.0085 274 TYR A CD2 
1824 C CE1 . TYR A 234 ? 0.4646 0.4813 0.5428 0.0792  -0.0107 -0.0047 274 TYR A CE1 
1825 C CE2 . TYR A 234 ? 0.4171 0.4085 0.4739 0.0777  -0.0164 -0.0037 274 TYR A CE2 
1826 C CZ  . TYR A 234 ? 0.4629 0.4644 0.5289 0.0767  -0.0172 -0.0024 274 TYR A CZ  
1827 O OH  . TYR A 234 ? 0.4933 0.4895 0.5555 0.0727  -0.0246 0.0014  274 TYR A OH  
1828 N N   . HIS A 235 ? 0.3986 0.3957 0.4403 0.0801  0.0043  -0.0167 275 HIS A N   
1829 C CA  . HIS A 235 ? 0.4345 0.4222 0.4646 0.0739  0.0029  -0.0138 275 HIS A CA  
1830 C C   . HIS A 235 ? 0.3860 0.3798 0.4085 0.0718  0.0085  -0.0139 275 HIS A C   
1831 O O   . HIS A 235 ? 0.3937 0.3840 0.4083 0.0679  0.0082  -0.0107 275 HIS A O   
1832 C CB  . HIS A 235 ? 0.5082 0.4870 0.5361 0.0725  0.0008  -0.0160 275 HIS A CB  
1833 C CG  . HIS A 235 ? 0.6688 0.6397 0.6859 0.0652  0.0001  -0.0122 275 HIS A CG  
1834 N ND1 . HIS A 235 ? 0.7025 0.6796 0.7131 0.0618  0.0053  -0.0129 275 HIS A ND1 
1835 C CD2 . HIS A 235 ? 0.7357 0.6936 0.7471 0.0607  -0.0048 -0.0073 275 HIS A CD2 
1836 C CE1 . HIS A 235 ? 0.7306 0.7010 0.7329 0.0553  0.0046  -0.0092 275 HIS A CE1 
1837 N NE2 . HIS A 235 ? 0.7118 0.6698 0.7133 0.0540  -0.0014 -0.0052 275 HIS A NE2 
1838 N N   . MET A 236 ? 0.3510 0.3535 0.3751 0.0751  0.0133  -0.0179 276 MET A N   
1839 C CA  . MET A 236 ? 0.3738 0.3815 0.3909 0.0745  0.0177  -0.0180 276 MET A CA  
1840 C C   . MET A 236 ? 0.3899 0.3982 0.4053 0.0740  0.0185  -0.0140 276 MET A C   
1841 O O   . MET A 236 ? 0.4164 0.4214 0.4241 0.0718  0.0188  -0.0125 276 MET A O   
1842 C CB  . MET A 236 ? 0.3365 0.3531 0.3546 0.0789  0.0214  -0.0226 276 MET A CB  
1843 C CG  . MET A 236 ? 0.4378 0.4532 0.4567 0.0786  0.0199  -0.0278 276 MET A CG  
1844 S SD  . MET A 236 ? 0.4946 0.5209 0.5118 0.0838  0.0232  -0.0341 276 MET A SD  
1845 C CE  . MET A 236 ? 0.4425 0.4733 0.4655 0.0899  0.0254  -0.0354 276 MET A CE  
1846 N N   . VAL A 237 ? 0.3600 0.3726 0.3830 0.0760  0.0190  -0.0128 277 VAL A N   
1847 C CA  . VAL A 237 ? 0.3983 0.4110 0.4204 0.0743  0.0198  -0.0089 277 VAL A CA  
1848 C C   . VAL A 237 ? 0.3533 0.3574 0.3733 0.0700  0.0143  -0.0062 277 VAL A C   
1849 O O   . VAL A 237 ? 0.3802 0.3793 0.3936 0.0678  0.0139  -0.0046 277 VAL A O   
1850 C CB  . VAL A 237 ? 0.4311 0.4530 0.4630 0.0761  0.0227  -0.0078 277 VAL A CB  
1851 C CG1 . VAL A 237 ? 0.4137 0.4438 0.4434 0.0805  0.0285  -0.0104 277 VAL A CG1 
1852 C CG2 . VAL A 237 ? 0.5488 0.5738 0.5928 0.0771  0.0193  -0.0086 277 VAL A CG2 
1853 N N   . PHE A 238 ? 0.3622 0.3630 0.3864 0.0694  0.0094  -0.0060 278 PHE A N   
1854 C CA  . PHE A 238 ? 0.3877 0.3800 0.4075 0.0657  0.0031  -0.0033 278 PHE A CA  
1855 C C   . PHE A 238 ? 0.3772 0.3623 0.3822 0.0631  0.0039  -0.0035 278 PHE A C   
1856 O O   . PHE A 238 ? 0.3923 0.3720 0.3897 0.0607  0.0019  -0.0025 278 PHE A O   
1857 C CB  . PHE A 238 ? 0.3784 0.3677 0.4044 0.0666  -0.0028 -0.0026 278 PHE A CB  
1858 C CG  . PHE A 238 ? 0.4113 0.3911 0.4305 0.0632  -0.0105 0.0007  278 PHE A CG  
1859 C CD1 . PHE A 238 ? 0.4037 0.3837 0.4247 0.0610  -0.0149 0.0023  278 PHE A CD1 
1860 C CD2 . PHE A 238 ? 0.4311 0.4013 0.4420 0.0619  -0.0138 0.0024  278 PHE A CD2 
1861 C CE1 . PHE A 238 ? 0.4061 0.3773 0.4191 0.0583  -0.0230 0.0049  278 PHE A CE1 
1862 C CE2 . PHE A 238 ? 0.4511 0.4120 0.4530 0.0590  -0.0211 0.0062  278 PHE A CE2 
1863 C CZ  . PHE A 238 ? 0.4322 0.3940 0.4348 0.0576  -0.0260 0.0070  278 PHE A CZ  
1864 N N   . GLU A 239 ? 0.3545 0.3402 0.3556 0.0635  0.0071  -0.0054 279 GLU A N   
1865 C CA  . GLU A 239 ? 0.3851 0.3678 0.3742 0.0611  0.0091  -0.0058 279 GLU A CA  
1866 C C   . GLU A 239 ? 0.4146 0.4002 0.3992 0.0632  0.0130  -0.0076 279 GLU A C   
1867 O O   . GLU A 239 ? 0.3941 0.3754 0.3689 0.0621  0.0130  -0.0079 279 GLU A O   
1868 C CB  . GLU A 239 ? 0.3769 0.3620 0.3657 0.0600  0.0117  -0.0074 279 GLU A CB  
1869 C CG  . GLU A 239 ? 0.5303 0.5075 0.5199 0.0570  0.0070  -0.0048 279 GLU A CG  
1870 C CD  . GLU A 239 ? 0.6080 0.5762 0.5862 0.0526  0.0034  -0.0005 279 GLU A CD  
1871 O OE1 . GLU A 239 ? 0.5214 0.4909 0.4895 0.0509  0.0067  -0.0008 279 GLU A OE1 
1872 O OE2 . GLU A 239 ? 0.4950 0.4547 0.4736 0.0517  -0.0029 0.0031  279 GLU A OE2 
1873 N N   . LEU A 240 ? 0.3799 0.3720 0.3705 0.0668  0.0162  -0.0088 280 LEU A N   
1874 C CA  . LEU A 240 ? 0.3865 0.3790 0.3725 0.0695  0.0190  -0.0095 280 LEU A CA  
1875 C C   . LEU A 240 ? 0.3797 0.3638 0.3631 0.0676  0.0158  -0.0075 280 LEU A C   
1876 O O   . LEU A 240 ? 0.4114 0.3897 0.3861 0.0685  0.0159  -0.0088 280 LEU A O   
1877 C CB  . LEU A 240 ? 0.3723 0.3723 0.3635 0.0734  0.0224  -0.0099 280 LEU A CB  
1878 C CG  . LEU A 240 ? 0.3781 0.3864 0.3701 0.0758  0.0250  -0.0134 280 LEU A CG  
1879 C CD1 . LEU A 240 ? 0.3499 0.3651 0.3445 0.0800  0.0276  -0.0138 280 LEU A CD1 
1880 C CD2 . LEU A 240 ? 0.3956 0.4055 0.3810 0.0767  0.0264  -0.0158 280 LEU A CD2 
1881 N N   . PHE A 241 ? 0.3650 0.3487 0.3566 0.0652  0.0125  -0.0049 281 PHE A N   
1882 C CA  . PHE A 241 ? 0.3816 0.3579 0.3725 0.0620  0.0083  -0.0033 281 PHE A CA  
1883 C C   . PHE A 241 ? 0.4023 0.3694 0.3814 0.0599  0.0041  -0.0049 281 PHE A C   
1884 O O   . PHE A 241 ? 0.4107 0.3693 0.3823 0.0593  0.0023  -0.0062 281 PHE A O   
1885 C CB  . PHE A 241 ? 0.3796 0.3608 0.3840 0.0594  0.0050  -0.0007 281 PHE A CB  
1886 C CG  . PHE A 241 ? 0.3954 0.3836 0.4094 0.0596  0.0089  0.0016  281 PHE A CG  
1887 C CD1 . PHE A 241 ? 0.3527 0.3352 0.3628 0.0581  0.0103  0.0034  281 PHE A CD1 
1888 C CD2 . PHE A 241 ? 0.3901 0.3902 0.4164 0.0614  0.0114  0.0021  281 PHE A CD2 
1889 C CE1 . PHE A 241 ? 0.3821 0.3708 0.3998 0.0572  0.0146  0.0070  281 PHE A CE1 
1890 C CE2 . PHE A 241 ? 0.4101 0.4185 0.4442 0.0613  0.0163  0.0045  281 PHE A CE2 
1891 C CZ  . PHE A 241 ? 0.3932 0.3960 0.4226 0.0586  0.0181  0.0076  281 PHE A CZ  
1892 N N   . LYS A 242 ? 0.3805 0.3481 0.3566 0.0589  0.0025  -0.0048 282 LYS A N   
1893 C CA  . LYS A 242 ? 0.4180 0.3776 0.3804 0.0567  -0.0008 -0.0058 282 LYS A CA  
1894 C C   . LYS A 242 ? 0.4356 0.3936 0.3862 0.0594  0.0040  -0.0096 282 LYS A C   
1895 O O   . LYS A 242 ? 0.4087 0.3588 0.3477 0.0590  0.0018  -0.0120 282 LYS A O   
1896 C CB  . LYS A 242 ? 0.3676 0.3274 0.3278 0.0548  -0.0027 -0.0035 282 LYS A CB  
1897 C CG  . LYS A 242 ? 0.3845 0.3434 0.3543 0.0533  -0.0099 -0.0002 282 LYS A CG  
1898 C CD  . LYS A 242 ? 0.4555 0.4099 0.4197 0.0516  -0.0134 0.0028  282 LYS A CD  
1899 C CE  . LYS A 242 ? 0.4553 0.4139 0.4245 0.0526  -0.0083 0.0029  282 LYS A CE  
1900 N NZ  . LYS A 242 ? 0.4702 0.4213 0.4325 0.0498  -0.0117 0.0068  282 LYS A NZ  
1901 N N   . ASN A 243 ? 0.4274 0.3936 0.3811 0.0626  0.0103  -0.0109 283 ASN A N   
1902 C CA  . ASN A 243 ? 0.4602 0.4278 0.4056 0.0665  0.0149  -0.0150 283 ASN A CA  
1903 C C   . ASN A 243 ? 0.4559 0.4161 0.3994 0.0700  0.0138  -0.0167 283 ASN A C   
1904 O O   . ASN A 243 ? 0.4417 0.3958 0.3747 0.0728  0.0139  -0.0207 283 ASN A O   
1905 C CB  . ASN A 243 ? 0.4771 0.4568 0.4284 0.0691  0.0204  -0.0160 283 ASN A CB  
1906 C CG  . ASN A 243 ? 0.5111 0.4963 0.4610 0.0651  0.0223  -0.0153 283 ASN A CG  
1907 O OD1 . ASN A 243 ? 0.4955 0.4840 0.4375 0.0649  0.0257  -0.0175 283 ASN A OD1 
1908 N ND2 . ASN A 243 ? 0.4879 0.4738 0.4452 0.0619  0.0203  -0.0123 283 ASN A ND2 
1909 N N   . ALA A 244 ? 0.4246 0.3845 0.3775 0.0700  0.0129  -0.0137 284 ALA A N   
1910 C CA  . ALA A 244 ? 0.4188 0.3694 0.3699 0.0720  0.0117  -0.0138 284 ALA A CA  
1911 C C   . ALA A 244 ? 0.4166 0.3539 0.3614 0.0682  0.0055  -0.0150 284 ALA A C   
1912 O O   . ALA A 244 ? 0.4392 0.3650 0.3756 0.0708  0.0040  -0.0182 284 ALA A O   
1913 C CB  . ALA A 244 ? 0.3737 0.3279 0.3355 0.0711  0.0127  -0.0090 284 ALA A CB  
1914 N N   . MET A 245 ? 0.4164 0.3545 0.3651 0.0625  0.0010  -0.0129 285 MET A N   
1915 C CA  . MET A 245 ? 0.4302 0.3569 0.3737 0.0583  -0.0063 -0.0143 285 MET A CA  
1916 C C   . MET A 245 ? 0.4105 0.3303 0.3365 0.0605  -0.0072 -0.0199 285 MET A C   
1917 O O   . MET A 245 ? 0.4542 0.3611 0.3712 0.0606  -0.0113 -0.0241 285 MET A O   
1918 C CB  . MET A 245 ? 0.4200 0.3517 0.3728 0.0529  -0.0117 -0.0108 285 MET A CB  
1919 C CG  . MET A 245 ? 0.4132 0.3513 0.3835 0.0501  -0.0117 -0.0063 285 MET A CG  
1920 S SD  . MET A 245 ? 0.4602 0.4081 0.4442 0.0465  -0.0172 -0.0031 285 MET A SD  
1921 C CE  . MET A 245 ? 0.4099 0.3683 0.4143 0.0443  -0.0140 0.0011  285 MET A CE  
1922 N N   . ARG A 246 ? 0.4127 0.3407 0.3335 0.0618  -0.0033 -0.0203 286 ARG A N   
1923 C CA  . ARG A 246 ? 0.4963 0.4209 0.4000 0.0640  -0.0020 -0.0254 286 ARG A CA  
1924 C C   . ARG A 246 ? 0.5055 0.4249 0.4026 0.0708  0.0013  -0.0314 286 ARG A C   
1925 O O   . ARG A 246 ? 0.5176 0.4259 0.4015 0.0725  -0.0016 -0.0372 286 ARG A O   
1926 C CB  . ARG A 246 ? 0.6778 0.6143 0.5795 0.0636  0.0037  -0.0235 286 ARG A CB  
1927 C CG  . ARG A 246 ? 0.7282 0.6671 0.6150 0.0670  0.0091  -0.0288 286 ARG A CG  
1928 C CD  . ARG A 246 ? 0.7887 0.7316 0.6663 0.0622  0.0101  -0.0257 286 ARG A CD  
1929 N NE  . ARG A 246 ? 0.9523 0.9065 0.8238 0.0643  0.0193  -0.0283 286 ARG A NE  
1930 C CZ  . ARG A 246 ? 1.0548 1.0109 0.9111 0.0613  0.0220  -0.0279 286 ARG A CZ  
1931 N NH1 . ARG A 246 ? 1.0406 1.0103 0.8943 0.0626  0.0315  -0.0302 286 ARG A NH1 
1932 N NH2 . ARG A 246 ? 1.1046 1.0503 0.9483 0.0569  0.0153  -0.0251 286 ARG A NH2 
1933 N N   . ALA A 247 ? 0.4742 0.4009 0.3801 0.0754  0.0067  -0.0306 287 ALA A N   
1934 C CA  . ALA A 247 ? 0.4540 0.3758 0.3548 0.0835  0.0092  -0.0360 287 ALA A CA  
1935 C C   . ALA A 247 ? 0.4482 0.3507 0.3458 0.0833  0.0027  -0.0375 287 ALA A C   
1936 O O   . ALA A 247 ? 0.4831 0.3742 0.3691 0.0884  0.0013  -0.0444 287 ALA A O   
1937 C CB  . ALA A 247 ? 0.4432 0.3763 0.3546 0.0883  0.0144  -0.0338 287 ALA A CB  
1938 N N   . THR A 248 ? 0.4291 0.3277 0.3371 0.0772  -0.0013 -0.0315 288 THR A N   
1939 C CA  . THR A 248 ? 0.4727 0.3531 0.3797 0.0746  -0.0076 -0.0317 288 THR A CA  
1940 C C   . THR A 248 ? 0.4950 0.3629 0.3901 0.0714  -0.0146 -0.0375 288 THR A C   
1941 O O   . THR A 248 ? 0.5008 0.3513 0.3864 0.0741  -0.0185 -0.0432 288 THR A O   
1942 C CB  . THR A 248 ? 0.4824 0.3659 0.4048 0.0670  -0.0094 -0.0234 288 THR A CB  
1943 O OG1 . THR A 248 ? 0.5001 0.3947 0.4308 0.0705  -0.0029 -0.0187 288 THR A OG1 
1944 C CG2 . THR A 248 ? 0.5035 0.3686 0.4266 0.0623  -0.0156 -0.0226 288 THR A CG2 
1945 N N   . MET A 249 ? 0.4404 0.3158 0.3348 0.0661  -0.0170 -0.0364 289 MET A N   
1946 C CA  . MET A 249 ? 0.4973 0.3612 0.3796 0.0626  -0.0251 -0.0414 289 MET A CA  
1947 C C   . MET A 249 ? 0.5088 0.3667 0.3710 0.0699  -0.0229 -0.0507 289 MET A C   
1948 O O   . MET A 249 ? 0.5325 0.3741 0.3823 0.0701  -0.0292 -0.0578 289 MET A O   
1949 C CB  . MET A 249 ? 0.4959 0.3694 0.3809 0.0563  -0.0290 -0.0373 289 MET A CB  
1950 C CG  . MET A 249 ? 0.5148 0.3957 0.4205 0.0498  -0.0317 -0.0294 289 MET A CG  
1951 S SD  . MET A 249 ? 0.5299 0.3984 0.4468 0.0440  -0.0378 -0.0284 289 MET A SD  
1952 C CE  . MET A 249 ? 0.5360 0.3892 0.4396 0.0392  -0.0505 -0.0355 289 MET A CE  
1953 N N   . GLU A 250 ? 0.5047 0.3761 0.3638 0.0758  -0.0138 -0.0515 290 GLU A N   
1954 C CA  . GLU A 250 ? 0.6188 0.4884 0.4599 0.0830  -0.0102 -0.0605 290 GLU A CA  
1955 C C   . GLU A 250 ? 0.6142 0.4726 0.4529 0.0922  -0.0090 -0.0673 290 GLU A C   
1956 O O   . GLU A 250 ? 0.5846 0.4310 0.4075 0.0975  -0.0110 -0.0769 290 GLU A O   
1957 C CB  . GLU A 250 ? 0.6244 0.5145 0.4645 0.0848  -0.0007 -0.0587 290 GLU A CB  
1958 C CG  . GLU A 250 ? 0.7005 0.5965 0.5392 0.0762  -0.0033 -0.0523 290 GLU A CG  
1959 C CD  . GLU A 250 ? 0.8078 0.7197 0.6407 0.0760  0.0051  -0.0505 290 GLU A CD  
1960 O OE1 . GLU A 250 ? 0.8666 0.7909 0.7043 0.0812  0.0140  -0.0522 290 GLU A OE1 
1961 O OE2 . GLU A 250 ? 0.8097 0.7219 0.6337 0.0700  0.0022  -0.0467 290 GLU A OE2 
1962 N N   . HIS A 251 ? 0.5839 0.4443 0.4369 0.0947  -0.0066 -0.0625 291 HIS A N   
1963 C CA  . HIS A 251 ? 0.5873 0.4359 0.4377 0.1046  -0.0062 -0.0679 291 HIS A CA  
1964 C C   . HIS A 251 ? 0.6680 0.4894 0.5122 0.1023  -0.0158 -0.0713 291 HIS A C   
1965 O O   . HIS A 251 ? 0.6640 0.4700 0.4973 0.1108  -0.0176 -0.0802 291 HIS A O   
1966 C CB  . HIS A 251 ? 0.5146 0.3719 0.3799 0.1077  -0.0020 -0.0609 291 HIS A CB  
1967 C CG  . HIS A 251 ? 0.6351 0.4834 0.4975 0.1199  -0.0012 -0.0660 291 HIS A CG  
1968 N ND1 . HIS A 251 ? 0.6697 0.5012 0.5363 0.1211  -0.0055 -0.0617 291 HIS A ND1 
1969 C CD2 . HIS A 251 ? 0.6117 0.4652 0.4672 0.1319  0.0033  -0.0749 291 HIS A CD2 
1970 C CE1 . HIS A 251 ? 0.6250 0.4498 0.4869 0.1340  -0.0048 -0.0676 291 HIS A CE1 
1971 N NE2 . HIS A 251 ? 0.6595 0.4986 0.5156 0.1412  0.0006  -0.0762 291 HIS A NE2 
1972 N N   . HIS A 252 ? 0.7150 0.5302 0.5668 0.0909  -0.0224 -0.0649 292 HIS A N   
1973 C CA  . HIS A 252 ? 0.7049 0.4949 0.5541 0.0864  -0.0320 -0.0670 292 HIS A CA  
1974 C C   . HIS A 252 ? 0.7392 0.5201 0.5769 0.0802  -0.0403 -0.0734 292 HIS A C   
1975 O O   . HIS A 252 ? 0.7418 0.5034 0.5796 0.0736  -0.0497 -0.0747 292 HIS A O   
1976 C CB  . HIS A 252 ? 0.6349 0.4243 0.5019 0.0772  -0.0339 -0.0557 292 HIS A CB  
1977 C CG  . HIS A 252 ? 0.6594 0.4518 0.5339 0.0834  -0.0278 -0.0499 292 HIS A CG  
1978 N ND1 . HIS A 252 ? 0.6908 0.4618 0.5609 0.0889  -0.0302 -0.0512 292 HIS A ND1 
1979 C CD2 . HIS A 252 ? 0.6426 0.4557 0.5273 0.0854  -0.0201 -0.0430 292 HIS A CD2 
1980 C CE1 . HIS A 252 ? 0.7065 0.4858 0.5833 0.0942  -0.0244 -0.0447 292 HIS A CE1 
1981 N NE2 . HIS A 252 ? 0.6686 0.4739 0.5544 0.0921  -0.0182 -0.0401 292 HIS A NE2 
1982 N N   . ALA A 253 ? 0.6913 0.4855 0.5186 0.0818  -0.0375 -0.0771 293 ALA A N   
1983 C CA  . ALA A 253 ? 0.7759 0.5629 0.5901 0.0762  -0.0459 -0.0826 293 ALA A CA  
1984 C C   . ALA A 253 ? 0.8987 0.6589 0.6979 0.0791  -0.0540 -0.0941 293 ALA A C   
1985 O O   . ALA A 253 ? 0.9188 0.6666 0.7135 0.0712  -0.0650 -0.0971 293 ALA A O   
1986 C CB  . ALA A 253 ? 0.7086 0.5119 0.5091 0.0796  -0.0400 -0.0850 293 ALA A CB  
1987 N N   . ASN A 254 ? 1.0132 0.7639 0.8053 0.0908  -0.0496 -0.1013 294 ASN A N   
1988 C CA  . ASN A 254 ? 1.1784 0.9007 0.9559 0.0947  -0.0578 -0.1133 294 ASN A CA  
1989 C C   . ASN A 254 ? 1.1565 0.8571 0.9458 0.0853  -0.0676 -0.1087 294 ASN A C   
1990 O O   . ASN A 254 ? 1.1672 0.8471 0.9485 0.0795  -0.0789 -0.1155 294 ASN A O   
1991 C CB  . ASN A 254 ? 1.3427 1.0605 1.1115 0.1110  -0.0507 -0.1221 294 ASN A CB  
1992 C CG  . ASN A 254 ? 1.4471 1.1842 1.2014 0.1199  -0.0415 -0.1294 294 ASN A CG  
1993 O OD1 . ASN A 254 ? 1.4618 1.2082 1.2059 0.1142  -0.0424 -0.1303 294 ASN A OD1 
1994 N ND2 . ASN A 254 ? 1.5015 1.2456 1.2550 0.1339  -0.0327 -0.1344 294 ASN A ND2 
1995 N N   . ARG A 255 ? 1.1415 0.8469 0.9495 0.0831  -0.0634 -0.0972 295 ARG A N   
1996 C CA  . ARG A 255 ? 1.1348 0.8206 0.9542 0.0736  -0.0710 -0.0913 295 ARG A CA  
1997 C C   . ARG A 255 ? 1.0620 0.7523 0.8917 0.0574  -0.0791 -0.0863 295 ARG A C   
1998 O O   . ARG A 255 ? 1.1348 0.8041 0.9664 0.0482  -0.0895 -0.0879 295 ARG A O   
1999 C CB  . ARG A 255 ? 1.1339 0.8268 0.9689 0.0751  -0.0636 -0.0791 295 ARG A CB  
2000 C CG  . ARG A 255 ? 1.1939 0.8793 1.0215 0.0909  -0.0580 -0.0831 295 ARG A CG  
2001 C CD  . ARG A 255 ? 1.1943 0.9084 1.0210 0.1011  -0.0469 -0.0842 295 ARG A CD  
2002 N NE  . ARG A 255 ? 1.1714 0.8909 1.0047 0.1106  -0.0402 -0.0789 295 ARG A NE  
2003 C CZ  . ARG A 255 ? 1.1737 0.9154 1.0074 0.1211  -0.0312 -0.0807 295 ARG A CZ  
2004 N NH1 . ARG A 255 ? 1.2129 0.9726 1.0402 0.1228  -0.0268 -0.0870 295 ARG A NH1 
2005 N NH2 . ARG A 255 ? 1.1589 0.9049 0.9992 0.1294  -0.0270 -0.0760 295 ARG A NH2 
2006 N N   . GLY A 256 ? 0.9523 0.6696 0.7896 0.0536  -0.0752 -0.0804 296 GLY A N   
2007 C CA  . GLY A 256 ? 0.9424 0.6679 0.7936 0.0396  -0.0823 -0.0743 296 GLY A CA  
2008 C C   . GLY A 256 ? 0.9553 0.6875 0.8305 0.0307  -0.0801 -0.0615 296 GLY A C   
2009 O O   . GLY A 256 ? 0.9595 0.7013 0.8497 0.0191  -0.0855 -0.0563 296 GLY A O   
2010 N N   . VAL A 257 ? 0.9089 0.6372 0.7878 0.0360  -0.0725 -0.0563 297 VAL A N   
2011 C CA  . VAL A 257 ? 0.8735 0.6107 0.7723 0.0291  -0.0679 -0.0433 297 VAL A CA  
2012 C C   . VAL A 257 ? 0.8674 0.6277 0.7699 0.0378  -0.0559 -0.0379 297 VAL A C   
2013 O O   . VAL A 257 ? 0.9442 0.7020 0.8350 0.0500  -0.0506 -0.0422 297 VAL A O   
2014 C CB  . VAL A 257 ? 0.9006 0.6117 0.7990 0.0272  -0.0700 -0.0405 297 VAL A CB  
2015 C CG1 . VAL A 257 ? 0.9236 0.6456 0.8410 0.0190  -0.0644 -0.0262 297 VAL A CG1 
2016 C CG2 . VAL A 257 ? 0.9077 0.5924 0.8007 0.0189  -0.0829 -0.0478 297 VAL A CG2 
2017 N N   . TYR A 258 ? 0.7958 0.5789 0.7152 0.0318  -0.0519 -0.0291 298 TYR A N   
2018 C CA  . TYR A 258 ? 0.6664 0.4720 0.5891 0.0390  -0.0419 -0.0254 298 TYR A CA  
2019 C C   . TYR A 258 ? 0.6094 0.4235 0.5456 0.0370  -0.0351 -0.0149 298 TYR A C   
2020 O O   . TYR A 258 ? 0.6378 0.4599 0.5897 0.0269  -0.0360 -0.0080 298 TYR A O   
2021 C CB  . TYR A 258 ? 0.5856 0.4109 0.5133 0.0361  -0.0430 -0.0257 298 TYR A CB  
2022 C CG  . TYR A 258 ? 0.5745 0.3911 0.4851 0.0386  -0.0492 -0.0356 298 TYR A CG  
2023 C CD1 . TYR A 258 ? 0.5719 0.3897 0.4666 0.0490  -0.0441 -0.0416 298 TYR A CD1 
2024 C CD2 . TYR A 258 ? 0.6553 0.4623 0.5649 0.0304  -0.0603 -0.0393 298 TYR A CD2 
2025 C CE1 . TYR A 258 ? 0.6439 0.4544 0.5209 0.0515  -0.0486 -0.0506 298 TYR A CE1 
2026 C CE2 . TYR A 258 ? 0.7015 0.4997 0.5924 0.0331  -0.0663 -0.0488 298 TYR A CE2 
2027 C CZ  . TYR A 258 ? 0.7303 0.5302 0.6041 0.0438  -0.0598 -0.0543 298 TYR A CZ  
2028 O OH  . TYR A 258 ? 0.7702 0.5627 0.6235 0.0466  -0.0646 -0.0637 298 TYR A OH  
2029 N N   . PRO A 259 ? 0.5819 0.3958 0.5125 0.0465  -0.0283 -0.0134 299 PRO A N   
2030 C CA  . PRO A 259 ? 0.5922 0.4130 0.5324 0.0450  -0.0222 -0.0034 299 PRO A CA  
2031 C C   . PRO A 259 ? 0.5471 0.3951 0.5009 0.0423  -0.0167 0.0013  299 PRO A C   
2032 O O   . PRO A 259 ? 0.5730 0.4341 0.5260 0.0456  -0.0159 -0.0032 299 PRO A O   
2033 C CB  . PRO A 259 ? 0.5731 0.3888 0.5018 0.0580  -0.0177 -0.0050 299 PRO A CB  
2034 C CG  . PRO A 259 ? 0.6224 0.4252 0.5369 0.0653  -0.0219 -0.0162 299 PRO A CG  
2035 C CD  . PRO A 259 ? 0.5738 0.3840 0.4896 0.0592  -0.0258 -0.0210 299 PRO A CD  
2036 N N   . PRO A 260 ? 0.5081 0.3644 0.4738 0.0364  -0.0127 0.0102  300 PRO A N   
2037 C CA  . PRO A 260 ? 0.5147 0.3966 0.4938 0.0349  -0.0075 0.0135  300 PRO A CA  
2038 C C   . PRO A 260 ? 0.5262 0.4200 0.4998 0.0454  -0.0011 0.0118  300 PRO A C   
2039 O O   . PRO A 260 ? 0.5405 0.4261 0.5025 0.0535  0.0005  0.0098  300 PRO A O   
2040 C CB  . PRO A 260 ? 0.5281 0.4142 0.5186 0.0269  -0.0037 0.0232  300 PRO A CB  
2041 C CG  . PRO A 260 ? 0.5687 0.4316 0.5477 0.0277  -0.0046 0.0264  300 PRO A CG  
2042 C CD  . PRO A 260 ? 0.5253 0.3674 0.4922 0.0307  -0.0126 0.0178  300 PRO A CD  
2043 N N   . ILE A 261 ? 0.4605 0.3744 0.4438 0.0453  0.0021  0.0122  301 ILE A N   
2044 C CA  . ILE A 261 ? 0.4339 0.3608 0.4154 0.0531  0.0084  0.0116  301 ILE A CA  
2045 C C   . ILE A 261 ? 0.4863 0.4230 0.4750 0.0516  0.0145  0.0186  301 ILE A C   
2046 O O   . ILE A 261 ? 0.4495 0.3952 0.4510 0.0447  0.0153  0.0225  301 ILE A O   
2047 C CB  . ILE A 261 ? 0.4673 0.4072 0.4531 0.0542  0.0077  0.0074  301 ILE A CB  
2048 C CG1 . ILE A 261 ? 0.5269 0.4564 0.5016 0.0558  0.0027  0.0011  301 ILE A CG1 
2049 C CG2 . ILE A 261 ? 0.4271 0.3805 0.4133 0.0605  0.0137  0.0068  301 ILE A CG2 
2050 C CD1 . ILE A 261 ? 0.5711 0.5093 0.5475 0.0556  0.0011  -0.0016 301 ILE A CD1 
2051 N N   . GLN A 262 ? 0.4572 0.3927 0.4374 0.0581  0.0185  0.0204  302 GLN A N   
2052 C CA  . GLN A 262 ? 0.4254 0.3689 0.4080 0.0575  0.0246  0.0273  302 GLN A CA  
2053 C C   . GLN A 262 ? 0.4898 0.4520 0.4748 0.0633  0.0292  0.0245  302 GLN A C   
2054 O O   . GLN A 262 ? 0.5323 0.4961 0.5114 0.0701  0.0284  0.0189  302 GLN A O   
2055 C CB  . GLN A 262 ? 0.4683 0.3963 0.4380 0.0611  0.0247  0.0319  302 GLN A CB  
2056 C CG  . GLN A 262 ? 0.5962 0.5021 0.5630 0.0552  0.0194  0.0344  302 GLN A CG  
2057 C CD  . GLN A 262 ? 0.7325 0.6193 0.6856 0.0602  0.0182  0.0385  302 GLN A CD  
2058 O OE1 . GLN A 262 ? 0.7787 0.6634 0.7224 0.0709  0.0174  0.0344  302 GLN A OE1 
2059 N NE2 . GLN A 262 ? 0.8033 0.6759 0.7557 0.0524  0.0176  0.0470  302 GLN A NE2 
2060 N N   . VAL A 263 ? 0.4264 0.4031 0.4205 0.0603  0.0342  0.0279  303 VAL A N   
2061 C CA  . VAL A 263 ? 0.3991 0.3923 0.3952 0.0658  0.0385  0.0246  303 VAL A CA  
2062 C C   . VAL A 263 ? 0.4504 0.4507 0.4434 0.0661  0.0452  0.0308  303 VAL A C   
2063 O O   . VAL A 263 ? 0.4389 0.4418 0.4383 0.0593  0.0484  0.0371  303 VAL A O   
2064 C CB  . VAL A 263 ? 0.3630 0.3687 0.3732 0.0637  0.0379  0.0205  303 VAL A CB  
2065 C CG1 . VAL A 263 ? 0.3542 0.3747 0.3659 0.0696  0.0422  0.0167  303 VAL A CG1 
2066 C CG2 . VAL A 263 ? 0.3847 0.3829 0.3946 0.0636  0.0312  0.0152  303 VAL A CG2 
2067 N N   . HIS A 264 ? 0.3974 0.4015 0.3802 0.0736  0.0473  0.0291  304 HIS A N   
2068 C CA  A HIS A 264 ? 0.4291 0.4411 0.4055 0.0752  0.0536  0.0343  304 HIS A CA  
2069 C CA  B HIS A 264 ? 0.4294 0.4413 0.4058 0.0752  0.0536  0.0343  304 HIS A CA  
2070 C C   . HIS A 264 ? 0.4240 0.4527 0.4025 0.0808  0.0564  0.0272  304 HIS A C   
2071 O O   . HIS A 264 ? 0.3961 0.4249 0.3710 0.0865  0.0528  0.0203  304 HIS A O   
2072 C CB  A HIS A 264 ? 0.4601 0.4596 0.4197 0.0798  0.0521  0.0390  304 HIS A CB  
2073 C CB  B HIS A 264 ? 0.4602 0.4596 0.4197 0.0798  0.0521  0.0390  304 HIS A CB  
2074 C CG  A HIS A 264 ? 0.4624 0.4653 0.4128 0.0791  0.0582  0.0476  304 HIS A CG  
2075 C CG  B HIS A 264 ? 0.5294 0.5085 0.4855 0.0754  0.0483  0.0449  304 HIS A CG  
2076 N ND1 A HIS A 264 ? 0.5064 0.5275 0.4604 0.0783  0.0655  0.0475  304 HIS A ND1 
2077 N ND1 B HIS A 264 ? 0.5496 0.5151 0.5026 0.0788  0.0416  0.0404  304 HIS A ND1 
2078 C CD2 A HIS A 264 ? 0.5146 0.5044 0.4512 0.0792  0.0583  0.0569  304 HIS A CD2 
2079 C CD2 B HIS A 264 ? 0.5692 0.5386 0.5243 0.0678  0.0501  0.0546  304 HIS A CD2 
2080 C CE1 A HIS A 264 ? 0.4605 0.4811 0.4025 0.0775  0.0706  0.0566  304 HIS A CE1 
2081 C CE1 B HIS A 264 ? 0.5412 0.4881 0.4908 0.0744  0.0388  0.0461  304 HIS A CE1 
2082 N NE2 A HIS A 264 ? 0.5210 0.5218 0.4520 0.0777  0.0660  0.0631  304 HIS A NE2 
2083 N NE2 B HIS A 264 ? 0.5741 0.5222 0.5252 0.0670  0.0436  0.0551  304 HIS A NE2 
2084 N N   . VAL A 265 ? 0.4153 0.4583 0.4003 0.0791  0.0628  0.0284  305 VAL A N   
2085 C CA  . VAL A 265 ? 0.4378 0.4958 0.4247 0.0848  0.0657  0.0209  305 VAL A CA  
2086 C C   . VAL A 265 ? 0.4507 0.5162 0.4244 0.0882  0.0722  0.0245  305 VAL A C   
2087 O O   . VAL A 265 ? 0.4124 0.4807 0.3846 0.0835  0.0783  0.0331  305 VAL A O   
2088 C CB  . VAL A 265 ? 0.4285 0.4986 0.4336 0.0822  0.0679  0.0176  305 VAL A CB  
2089 C CG1 . VAL A 265 ? 0.3597 0.4428 0.3658 0.0893  0.0705  0.0088  305 VAL A CG1 
2090 C CG2 . VAL A 265 ? 0.4061 0.4677 0.4215 0.0789  0.0606  0.0150  305 VAL A CG2 
2091 N N   . THR A 266 ? 0.3980 0.4670 0.3617 0.0957  0.0707  0.0180  306 THR A N   
2092 C CA  . THR A 266 ? 0.4372 0.5130 0.3851 0.1001  0.0756  0.0203  306 THR A CA  
2093 C C   . THR A 266 ? 0.4243 0.5130 0.3720 0.1065  0.0767  0.0091  306 THR A C   
2094 O O   . THR A 266 ? 0.4394 0.5259 0.3907 0.1096  0.0703  0.0002  306 THR A O   
2095 C CB  . THR A 266 ? 0.5137 0.5780 0.4445 0.1039  0.0705  0.0242  306 THR A CB  
2096 O OG1 . THR A 266 ? 0.5827 0.6318 0.5136 0.0987  0.0685  0.0334  306 THR A OG1 
2097 C CG2 . THR A 266 ? 0.5868 0.6572 0.4990 0.1080  0.0751  0.0282  306 THR A CG2 
2098 N N   . LEU A 267 ? 0.4535 0.5555 0.3965 0.1082  0.0849  0.0096  307 LEU A N   
2099 C CA  . LEU A 267 ? 0.4530 0.5663 0.3918 0.1155  0.0862  -0.0016 307 LEU A CA  
2100 C C   . LEU A 267 ? 0.4273 0.5424 0.3423 0.1204  0.0875  0.0006  307 LEU A C   
2101 O O   . LEU A 267 ? 0.4573 0.5782 0.3620 0.1190  0.0956  0.0091  307 LEU A O   
2102 C CB  . LEU A 267 ? 0.4430 0.5719 0.3938 0.1157  0.0947  -0.0049 307 LEU A CB  
2103 C CG  . LEU A 267 ? 0.4621 0.6008 0.4096 0.1243  0.0955  -0.0185 307 LEU A CG  
2104 C CD1 . LEU A 267 ? 0.5005 0.6292 0.4556 0.1265  0.0852  -0.0288 307 LEU A CD1 
2105 C CD2 . LEU A 267 ? 0.4728 0.6283 0.4323 0.1258  0.1048  -0.0216 307 LEU A CD2 
2106 N N   . GLY A 268 ? 0.4644 0.5750 0.3707 0.1257  0.0794  -0.0064 308 GLY A N   
2107 C CA  . GLY A 268 ? 0.4758 0.5887 0.3595 0.1315  0.0783  -0.0060 308 GLY A CA  
2108 C C   . GLY A 268 ? 0.5027 0.6273 0.3803 0.1380  0.0795  -0.0190 308 GLY A C   
2109 O O   . GLY A 268 ? 0.5231 0.6531 0.4145 0.1385  0.0814  -0.0281 308 GLY A O   
2110 N N   . ASN A 269 ? 0.5434 0.6707 0.3990 0.1437  0.0773  -0.0201 309 ASN A N   
2111 C CA  A ASN A 269 ? 0.5897 0.7269 0.4357 0.1505  0.0774  -0.0334 309 ASN A CA  
2112 C CA  B ASN A 269 ? 0.5897 0.7269 0.4357 0.1505  0.0774  -0.0334 309 ASN A CA  
2113 C C   . ASN A 269 ? 0.5747 0.7088 0.4349 0.1516  0.0687  -0.0480 309 ASN A C   
2114 O O   . ASN A 269 ? 0.5838 0.7236 0.4445 0.1558  0.0696  -0.0607 309 ASN A O   
2115 C CB  A ASN A 269 ? 0.6270 0.7661 0.4456 0.1563  0.0740  -0.0320 309 ASN A CB  
2116 C CB  B ASN A 269 ? 0.6271 0.7660 0.4457 0.1562  0.0740  -0.0316 309 ASN A CB  
2117 C CG  A ASN A 269 ? 0.6828 0.8267 0.4826 0.1559  0.0844  -0.0190 309 ASN A CG  
2118 C CG  B ASN A 269 ? 0.6440 0.7925 0.4497 0.1634  0.0732  -0.0463 309 ASN A CG  
2119 O OD1 A ASN A 269 ? 0.6675 0.8200 0.4724 0.1533  0.0961  -0.0164 309 ASN A OD1 
2120 O OD1 B ASN A 269 ? 0.6739 0.8325 0.4750 0.1658  0.0831  -0.0498 309 ASN A OD1 
2121 N ND2 A ASN A 269 ? 0.7404 0.8792 0.5183 0.1585  0.0800  -0.0103 309 ASN A ND2 
2122 N ND2 B ASN A 269 ? 0.6072 0.7533 0.4073 0.1672  0.0613  -0.0556 309 ASN A ND2 
2123 N N   . GLU A 270 ? 0.4558 0.5805 0.3272 0.1480  0.0606  -0.0466 310 GLU A N   
2124 C CA  . GLU A 270 ? 0.5179 0.6389 0.4015 0.1474  0.0517  -0.0583 310 GLU A CA  
2125 C C   . GLU A 270 ? 0.5005 0.6132 0.4057 0.1408  0.0502  -0.0552 310 GLU A C   
2126 O O   . GLU A 270 ? 0.4621 0.5718 0.3803 0.1392  0.0471  -0.0640 310 GLU A O   
2127 C CB  . GLU A 270 ? 0.6339 0.7549 0.5063 0.1502  0.0420  -0.0604 310 GLU A CB  
2128 C CG  . GLU A 270 ? 0.6985 0.8185 0.5801 0.1493  0.0324  -0.0731 310 GLU A CG  
2129 C CD  . GLU A 270 ? 0.6223 0.7469 0.4922 0.1530  0.0229  -0.0763 310 GLU A CD  
2130 O OE1 . GLU A 270 ? 0.5898 0.7191 0.4392 0.1586  0.0236  -0.0726 310 GLU A OE1 
2131 O OE2 . GLU A 270 ? 0.5760 0.7003 0.4575 0.1500  0.0147  -0.0823 310 GLU A OE2 
2132 N N   . ASP A 271 ? 0.4447 0.5521 0.3528 0.1368  0.0520  -0.0430 311 ASP A N   
2133 C CA  . ASP A 271 ? 0.4695 0.5687 0.3947 0.1309  0.0498  -0.0400 311 ASP A CA  
2134 C C   . ASP A 271 ? 0.4313 0.5293 0.3653 0.1269  0.0572  -0.0324 311 ASP A C   
2135 O O   . ASP A 271 ? 0.4703 0.5705 0.3964 0.1265  0.0632  -0.0235 311 ASP A O   
2136 C CB  . ASP A 271 ? 0.4608 0.5539 0.3834 0.1299  0.0447  -0.0336 311 ASP A CB  
2137 C CG  . ASP A 271 ? 0.5491 0.6455 0.4680 0.1330  0.0363  -0.0412 311 ASP A CG  
2138 O OD1 . ASP A 271 ? 0.5079 0.6083 0.4299 0.1336  0.0332  -0.0520 311 ASP A OD1 
2139 O OD2 . ASP A 271 ? 0.5322 0.6271 0.4463 0.1350  0.0322  -0.0366 311 ASP A OD2 
2140 N N   . LEU A 272 ? 0.3978 0.4927 0.3483 0.1234  0.0563  -0.0357 312 LEU A N   
2141 C CA  . LEU A 272 ? 0.4186 0.5098 0.3806 0.1181  0.0595  -0.0279 312 LEU A CA  
2142 C C   . LEU A 272 ? 0.4259 0.5063 0.3912 0.1139  0.0537  -0.0240 312 LEU A C   
2143 O O   . LEU A 272 ? 0.4340 0.5106 0.4046 0.1131  0.0480  -0.0299 312 LEU A O   
2144 C CB  . LEU A 272 ? 0.4045 0.4981 0.3817 0.1176  0.0605  -0.0335 312 LEU A CB  
2145 C CG  . LEU A 272 ? 0.4658 0.5555 0.4572 0.1118  0.0610  -0.0270 312 LEU A CG  
2146 C CD1 . LEU A 272 ? 0.4661 0.5627 0.4575 0.1093  0.0685  -0.0178 312 LEU A CD1 
2147 C CD2 . LEU A 272 ? 0.4889 0.5795 0.4950 0.1130  0.0592  -0.0337 312 LEU A CD2 
2148 N N   . THR A 273 ? 0.4055 0.4806 0.3674 0.1112  0.0552  -0.0142 313 THR A N   
2149 C CA  . THR A 273 ? 0.3673 0.4321 0.3316 0.1084  0.0502  -0.0113 313 THR A CA  
2150 C C   . THR A 273 ? 0.3913 0.4496 0.3646 0.1023  0.0516  -0.0051 313 THR A C   
2151 O O   . THR A 273 ? 0.4214 0.4817 0.3950 0.0999  0.0566  0.0013  313 THR A O   
2152 C CB  . THR A 273 ? 0.4797 0.5403 0.4307 0.1117  0.0481  -0.0068 313 THR A CB  
2153 O OG1 . THR A 273 ? 0.5621 0.6217 0.5044 0.1114  0.0530  0.0022  313 THR A OG1 
2154 C CG2 . THR A 273 ? 0.5227 0.5906 0.4663 0.1175  0.0446  -0.0138 313 THR A CG2 
2155 N N   . VAL A 274 ? 0.3672 0.4185 0.3476 0.0993  0.0472  -0.0069 314 VAL A N   
2156 C CA  . VAL A 274 ? 0.3924 0.4358 0.3793 0.0937  0.0464  -0.0019 314 VAL A CA  
2157 C C   . VAL A 274 ? 0.3969 0.4297 0.3779 0.0938  0.0424  -0.0006 314 VAL A C   
2158 O O   . VAL A 274 ? 0.3914 0.4238 0.3732 0.0948  0.0390  -0.0058 314 VAL A O   
2159 C CB  . VAL A 274 ? 0.3885 0.4329 0.3881 0.0907  0.0445  -0.0055 314 VAL A CB  
2160 C CG1 . VAL A 274 ? 0.3332 0.3700 0.3386 0.0849  0.0425  -0.0006 314 VAL A CG1 
2161 C CG2 . VAL A 274 ? 0.3655 0.4212 0.3718 0.0928  0.0484  -0.0084 314 VAL A CG2 
2162 N N   . LYS A 275 ? 0.3965 0.4209 0.3718 0.0928  0.0428  0.0061  315 LYS A N   
2163 C CA  . LYS A 275 ? 0.3860 0.3990 0.3556 0.0941  0.0389  0.0068  315 LYS A CA  
2164 C C   . LYS A 275 ? 0.3977 0.4003 0.3723 0.0880  0.0369  0.0090  315 LYS A C   
2165 O O   . LYS A 275 ? 0.4420 0.4414 0.4196 0.0831  0.0386  0.0147  315 LYS A O   
2166 C CB  . LYS A 275 ? 0.4141 0.4209 0.3719 0.0984  0.0391  0.0121  315 LYS A CB  
2167 C CG  . LYS A 275 ? 0.4915 0.4847 0.4443 0.1008  0.0348  0.0124  315 LYS A CG  
2168 C CD  . LYS A 275 ? 0.5620 0.5501 0.5031 0.1082  0.0332  0.0158  315 LYS A CD  
2169 C CE  . LYS A 275 ? 0.6938 0.6665 0.6280 0.1055  0.0336  0.0254  315 LYS A CE  
2170 N NZ  . LYS A 275 ? 0.7742 0.7397 0.6955 0.1138  0.0309  0.0293  315 LYS A NZ  
2171 N N   . MET A 276 ? 0.3994 0.3974 0.3744 0.0879  0.0334  0.0046  316 MET A N   
2172 C CA  . MET A 276 ? 0.3655 0.3531 0.3427 0.0828  0.0303  0.0053  316 MET A CA  
2173 C C   . MET A 276 ? 0.4189 0.3947 0.3870 0.0864  0.0276  0.0038  316 MET A C   
2174 O O   . MET A 276 ? 0.4551 0.4350 0.4199 0.0915  0.0274  -0.0009 316 MET A O   
2175 C CB  . MET A 276 ? 0.3135 0.3057 0.2976 0.0797  0.0285  0.0012  316 MET A CB  
2176 C CG  . MET A 276 ? 0.3583 0.3401 0.3428 0.0747  0.0242  0.0014  316 MET A CG  
2177 S SD  . MET A 276 ? 0.4137 0.3991 0.4032 0.0715  0.0211  -0.0019 316 MET A SD  
2178 C CE  . MET A 276 ? 0.3753 0.3735 0.3777 0.0711  0.0235  -0.0006 316 MET A CE  
2179 N N   . SER A 277 ? 0.4227 0.3841 0.3875 0.0837  0.0254  0.0075  317 SER A N   
2180 C CA  . SER A 277 ? 0.4083 0.3555 0.3637 0.0883  0.0225  0.0059  317 SER A CA  
2181 C C   . SER A 277 ? 0.4322 0.3665 0.3866 0.0836  0.0183  0.0037  317 SER A C   
2182 O O   . SER A 277 ? 0.4654 0.3962 0.4256 0.0757  0.0168  0.0071  317 SER A O   
2183 C CB  . SER A 277 ? 0.3886 0.3252 0.3376 0.0906  0.0226  0.0125  317 SER A CB  
2184 O OG  . SER A 277 ? 0.4902 0.4385 0.4381 0.0947  0.0260  0.0152  317 SER A OG  
2185 N N   . ASP A 278 ? 0.4259 0.3545 0.3732 0.0885  0.0163  -0.0025 318 ASP A N   
2186 C CA  . ASP A 278 ? 0.4019 0.3164 0.3446 0.0854  0.0118  -0.0059 318 ASP A CA  
2187 C C   . ASP A 278 ? 0.4751 0.3738 0.4073 0.0930  0.0095  -0.0092 318 ASP A C   
2188 O O   . ASP A 278 ? 0.4865 0.3885 0.4159 0.1017  0.0114  -0.0098 318 ASP A O   
2189 C CB  . ASP A 278 ? 0.4331 0.3555 0.3754 0.0836  0.0115  -0.0115 318 ASP A CB  
2190 C CG  . ASP A 278 ? 0.4826 0.4132 0.4195 0.0914  0.0146  -0.0176 318 ASP A CG  
2191 O OD1 . ASP A 278 ? 0.4906 0.4136 0.4201 0.0987  0.0142  -0.0216 318 ASP A OD1 
2192 O OD2 . ASP A 278 ? 0.4823 0.4272 0.4229 0.0899  0.0173  -0.0188 318 ASP A OD2 
2193 N N   . ARG A 279 ? 0.5232 0.4043 0.4498 0.0901  0.0045  -0.0119 319 ARG A N   
2194 C CA  . ARG A 279 ? 0.4973 0.3618 0.4129 0.0984  0.0017  -0.0176 319 ARG A CA  
2195 C C   . ARG A 279 ? 0.5320 0.3976 0.4409 0.0999  0.0008  -0.0270 319 ARG A C   
2196 O O   . ARG A 279 ? 0.5774 0.4250 0.4777 0.0998  -0.0042 -0.0320 319 ARG A O   
2197 C CB  . ARG A 279 ? 0.5460 0.3854 0.4581 0.0944  -0.0039 -0.0140 319 ARG A CB  
2198 C CG  . ARG A 279 ? 0.6663 0.5014 0.5808 0.0944  -0.0026 -0.0043 319 ARG A CG  
2199 C CD  . ARG A 279 ? 0.9668 0.7751 0.8777 0.0883  -0.0082 -0.0001 319 ARG A CD  
2200 N NE  . ARG A 279 ? 1.2070 1.0136 1.1218 0.0831  -0.0060 0.0119  319 ARG A NE  
2201 C CZ  . ARG A 279 ? 1.3096 1.1006 1.2166 0.0887  -0.0071 0.0174  319 ARG A CZ  
2202 N NH1 . ARG A 279 ? 1.3542 1.1300 1.2509 0.1008  -0.0110 0.0113  319 ARG A NH1 
2203 N NH2 . ARG A 279 ? 1.3145 1.1054 1.2235 0.0827  -0.0043 0.0292  319 ARG A NH2 
2204 N N   . GLY A 280 ? 0.4819 0.3680 0.3936 0.1010  0.0055  -0.0293 320 GLY A N   
2205 C CA  . GLY A 280 ? 0.5234 0.4132 0.4278 0.1008  0.0059  -0.0363 320 GLY A CA  
2206 C C   . GLY A 280 ? 0.5949 0.4898 0.4921 0.1117  0.0096  -0.0445 320 GLY A C   
2207 O O   . GLY A 280 ? 0.6247 0.5299 0.5171 0.1116  0.0128  -0.0492 320 GLY A O   
2208 N N   . GLY A 281 ? 0.5043 0.3931 0.4008 0.1214  0.0095  -0.0460 321 GLY A N   
2209 C CA  . GLY A 281 ? 0.5675 0.4603 0.4583 0.1333  0.0123  -0.0549 321 GLY A CA  
2210 C C   . GLY A 281 ? 0.5015 0.4193 0.4011 0.1394  0.0185  -0.0553 321 GLY A C   
2211 O O   . GLY A 281 ? 0.5152 0.4388 0.4133 0.1507  0.0206  -0.0623 321 GLY A O   
2212 N N   . GLY A 282 ? 0.5066 0.4400 0.4160 0.1323  0.0210  -0.0488 322 GLY A N   
2213 C CA  . GLY A 282 ? 0.4540 0.4096 0.3730 0.1372  0.0252  -0.0489 322 GLY A CA  
2214 C C   . GLY A 282 ? 0.4839 0.4603 0.4044 0.1379  0.0315  -0.0550 322 GLY A C   
2215 O O   . GLY A 282 ? 0.4951 0.4694 0.4075 0.1349  0.0333  -0.0589 322 GLY A O   
2216 N N   . VAL A 283 ? 0.4919 0.4898 0.4232 0.1414  0.0348  -0.0554 323 VAL A N   
2217 C CA  . VAL A 283 ? 0.4973 0.5199 0.4345 0.1406  0.0415  -0.0598 323 VAL A CA  
2218 C C   . VAL A 283 ? 0.4296 0.4694 0.3772 0.1516  0.0422  -0.0635 323 VAL A C   
2219 O O   . VAL A 283 ? 0.4182 0.4587 0.3718 0.1534  0.0384  -0.0593 323 VAL A O   
2220 C CB  . VAL A 283 ? 0.5939 0.6278 0.5377 0.1279  0.0437  -0.0544 323 VAL A CB  
2221 C CG1 . VAL A 283 ? 0.5992 0.6484 0.5421 0.1225  0.0505  -0.0573 323 VAL A CG1 
2222 C CG2 . VAL A 283 ? 0.6368 0.6529 0.5765 0.1192  0.0393  -0.0475 323 VAL A CG2 
2223 N N   . PRO A 284 ? 0.4676 0.5238 0.4179 0.1591  0.0470  -0.0714 324 PRO A N   
2224 C CA  . PRO A 284 ? 0.4770 0.5537 0.4404 0.1694  0.0471  -0.0750 324 PRO A CA  
2225 C C   . PRO A 284 ? 0.4618 0.5593 0.4388 0.1610  0.0481  -0.0710 324 PRO A C   
2226 O O   . PRO A 284 ? 0.4364 0.5390 0.4144 0.1480  0.0516  -0.0678 324 PRO A O   
2227 C CB  . PRO A 284 ? 0.4874 0.5809 0.4521 0.1769  0.0539  -0.0846 324 PRO A CB  
2228 C CG  . PRO A 284 ? 0.4943 0.5843 0.4488 0.1654  0.0594  -0.0840 324 PRO A CG  
2229 C CD  . PRO A 284 ? 0.4815 0.5413 0.4238 0.1584  0.0531  -0.0774 324 PRO A CD  
2230 N N   . LEU A 285 ? 0.4058 0.5138 0.3925 0.1690  0.0439  -0.0714 325 LEU A N   
2231 C CA  . LEU A 285 ? 0.4415 0.5670 0.4403 0.1620  0.0429  -0.0686 325 LEU A CA  
2232 C C   . LEU A 285 ? 0.5162 0.6680 0.5265 0.1532  0.0502  -0.0718 325 LEU A C   
2233 O O   . LEU A 285 ? 0.4354 0.5928 0.4507 0.1410  0.0507  -0.0682 325 LEU A O   
2234 C CB  . LEU A 285 ? 0.3615 0.4963 0.3679 0.1741  0.0367  -0.0700 325 LEU A CB  
2235 C CG  . LEU A 285 ? 0.3578 0.5101 0.3755 0.1685  0.0339  -0.0683 325 LEU A CG  
2236 C CD1 . LEU A 285 ? 0.3771 0.5116 0.3866 0.1578  0.0318  -0.0610 325 LEU A CD1 
2237 C CD2 . LEU A 285 ? 0.3795 0.5408 0.4027 0.1824  0.0268  -0.0702 325 LEU A CD2 
2238 N N   . ARG A 286 ? 0.4402 0.6079 0.4544 0.1593  0.0560  -0.0786 326 ARG A N   
2239 C CA  . ARG A 286 ? 0.4602 0.6547 0.4853 0.1505  0.0642  -0.0812 326 ARG A CA  
2240 C C   . ARG A 286 ? 0.4291 0.6128 0.4450 0.1342  0.0684  -0.0755 326 ARG A C   
2241 O O   . ARG A 286 ? 0.4723 0.6728 0.4971 0.1224  0.0729  -0.0739 326 ARG A O   
2242 C CB  . ARG A 286 ? 0.4497 0.6609 0.4775 0.1612  0.0708  -0.0898 326 ARG A CB  
2243 C CG  . ARG A 286 ? 0.4455 0.6860 0.4833 0.1521  0.0815  -0.0923 326 ARG A CG  
2244 C CD  . ARG A 286 ? 0.4785 0.7363 0.5183 0.1648  0.0886  -0.1018 326 ARG A CD  
2245 N NE  . ARG A 286 ? 0.5045 0.7356 0.5226 0.1717  0.0890  -0.1041 326 ARG A NE  
2246 C CZ  . ARG A 286 ? 0.5907 0.8150 0.5938 0.1638  0.0961  -0.1034 326 ARG A CZ  
2247 N NH1 . ARG A 286 ? 0.6081 0.8495 0.6151 0.1484  0.1039  -0.0993 326 ARG A NH1 
2248 N NH2 . ARG A 286 ? 0.6039 0.8033 0.5873 0.1708  0.0947  -0.1066 326 ARG A NH2 
2249 N N   . LYS A 287 ? 0.3969 0.5522 0.3955 0.1331  0.0661  -0.0720 327 LYS A N   
2250 C CA  . LYS A 287 ? 0.3913 0.5353 0.3795 0.1198  0.0691  -0.0669 327 LYS A CA  
2251 C C   . LYS A 287 ? 0.4133 0.5395 0.3992 0.1111  0.0630  -0.0594 327 LYS A C   
2252 O O   . LYS A 287 ? 0.4859 0.5997 0.4629 0.1016  0.0636  -0.0547 327 LYS A O   
2253 C CB  . LYS A 287 ? 0.4179 0.5444 0.3883 0.1239  0.0706  -0.0691 327 LYS A CB  
2254 C CG  . LYS A 287 ? 0.4852 0.6286 0.4543 0.1312  0.0785  -0.0772 327 LYS A CG  
2255 C CD  . LYS A 287 ? 0.5429 0.6653 0.4913 0.1339  0.0789  -0.0797 327 LYS A CD  
2256 C CE  . LYS A 287 ? 0.6688 0.8070 0.6135 0.1424  0.0872  -0.0890 327 LYS A CE  
2257 N NZ  . LYS A 287 ? 0.6935 0.8086 0.6168 0.1477  0.0857  -0.0935 327 LYS A NZ  
2258 N N   . ILE A 288 ? 0.4036 0.5288 0.3967 0.1150  0.0570  -0.0582 328 ILE A N   
2259 C CA  . ILE A 288 ? 0.4475 0.5571 0.4383 0.1082  0.0520  -0.0521 328 ILE A CA  
2260 C C   . ILE A 288 ? 0.4397 0.5577 0.4374 0.0954  0.0538  -0.0494 328 ILE A C   
2261 O O   . ILE A 288 ? 0.4271 0.5306 0.4191 0.0872  0.0524  -0.0445 328 ILE A O   
2262 C CB  . ILE A 288 ? 0.5398 0.6474 0.5344 0.1160  0.0459  -0.0518 328 ILE A CB  
2263 C CG1 . ILE A 288 ? 0.5563 0.6474 0.5412 0.1267  0.0429  -0.0519 328 ILE A CG1 
2264 C CG2 . ILE A 288 ? 0.6462 0.7435 0.6403 0.1088  0.0423  -0.0466 328 ILE A CG2 
2265 C CD1 . ILE A 288 ? 0.6170 0.6838 0.5907 0.1219  0.0409  -0.0468 328 ILE A CD1 
2266 N N   . ASP A 289 ? 0.4481 0.5893 0.4592 0.0934  0.0561  -0.0527 329 ASP A N   
2267 C CA  . ASP A 289 ? 0.5332 0.6800 0.5523 0.0812  0.0560  -0.0504 329 ASP A CA  
2268 C C   . ASP A 289 ? 0.4839 0.6249 0.4966 0.0695  0.0607  -0.0460 329 ASP A C   
2269 O O   . ASP A 289 ? 0.4665 0.5992 0.4799 0.0596  0.0586  -0.0419 329 ASP A O   
2270 C CB  . ASP A 289 ? 0.6270 0.8010 0.6633 0.0809  0.0567  -0.0553 329 ASP A CB  
2271 C CG  . ASP A 289 ? 0.8127 0.9884 0.8550 0.0865  0.0492  -0.0574 329 ASP A CG  
2272 O OD1 . ASP A 289 ? 0.8712 1.0286 0.9067 0.0849  0.0447  -0.0542 329 ASP A OD1 
2273 O OD2 . ASP A 289 ? 0.8931 1.0891 0.9466 0.0931  0.0477  -0.0625 329 ASP A OD2 
2274 N N   . ARG A 290 ? 0.4383 0.5822 0.4433 0.0709  0.0667  -0.0468 330 ARG A N   
2275 C CA  . ARG A 290 ? 0.4252 0.5622 0.4206 0.0600  0.0709  -0.0417 330 ARG A CA  
2276 C C   . ARG A 290 ? 0.3952 0.5051 0.3785 0.0569  0.0652  -0.0359 330 ARG A C   
2277 O O   . ARG A 290 ? 0.4597 0.5611 0.4364 0.0469  0.0660  -0.0302 330 ARG A O   
2278 C CB  . ARG A 290 ? 0.4922 0.6372 0.4786 0.0636  0.0785  -0.0446 330 ARG A CB  
2279 C CG  . ARG A 290 ? 0.5484 0.6774 0.5213 0.0749  0.0759  -0.0474 330 ARG A CG  
2280 C CD  . ARG A 290 ? 0.5840 0.7234 0.5489 0.0805  0.0836  -0.0528 330 ARG A CD  
2281 N NE  . ARG A 290 ? 0.6756 0.8445 0.6559 0.0853  0.0897  -0.0590 330 ARG A NE  
2282 C CZ  . ARG A 290 ? 0.6874 0.8708 0.6650 0.0928  0.0970  -0.0657 330 ARG A CZ  
2283 N NH1 . ARG A 290 ? 0.5739 0.7433 0.5320 0.0962  0.0989  -0.0674 330 ARG A NH1 
2284 N NH2 . ARG A 290 ? 0.6804 0.8933 0.6751 0.0975  0.1021  -0.0714 330 ARG A NH2 
2285 N N   . LEU A 291 ? 0.3877 0.4845 0.3687 0.0650  0.0592  -0.0367 331 LEU A N   
2286 C CA  . LEU A 291 ? 0.4041 0.4790 0.3776 0.0621  0.0536  -0.0316 331 LEU A CA  
2287 C C   . LEU A 291 ? 0.4361 0.5081 0.4172 0.0541  0.0504  -0.0283 331 LEU A C   
2288 O O   . LEU A 291 ? 0.4339 0.4898 0.4097 0.0500  0.0466  -0.0236 331 LEU A O   
2289 C CB  . LEU A 291 ? 0.4070 0.4712 0.3785 0.0715  0.0488  -0.0329 331 LEU A CB  
2290 C CG  . LEU A 291 ? 0.4709 0.5304 0.4329 0.0795  0.0499  -0.0361 331 LEU A CG  
2291 C CD1 . LEU A 291 ? 0.4826 0.5314 0.4445 0.0873  0.0450  -0.0362 331 LEU A CD1 
2292 C CD2 . LEU A 291 ? 0.4958 0.5428 0.4440 0.0750  0.0501  -0.0337 331 LEU A CD2 
2293 N N   . PHE A 292 ? 0.3944 0.4812 0.3882 0.0523  0.0511  -0.0312 332 PHE A N   
2294 C CA  . PHE A 292 ? 0.4234 0.5068 0.4244 0.0449  0.0477  -0.0296 332 PHE A CA  
2295 C C   . PHE A 292 ? 0.4267 0.5180 0.4318 0.0330  0.0515  -0.0274 332 PHE A C   
2296 O O   . PHE A 292 ? 0.3872 0.4754 0.3991 0.0257  0.0485  -0.0267 332 PHE A O   
2297 C CB  . PHE A 292 ? 0.3802 0.4724 0.3915 0.0503  0.0441  -0.0347 332 PHE A CB  
2298 C CG  . PHE A 292 ? 0.4062 0.4888 0.4130 0.0600  0.0404  -0.0351 332 PHE A CG  
2299 C CD1 . PHE A 292 ? 0.4291 0.4960 0.4329 0.0592  0.0365  -0.0324 332 PHE A CD1 
2300 C CD2 . PHE A 292 ? 0.5080 0.5974 0.5139 0.0700  0.0409  -0.0379 332 PHE A CD2 
2301 C CE1 . PHE A 292 ? 0.4453 0.5054 0.4457 0.0669  0.0342  -0.0321 332 PHE A CE1 
2302 C CE2 . PHE A 292 ? 0.5287 0.6082 0.5297 0.0774  0.0379  -0.0369 332 PHE A CE2 
2303 C CZ  . PHE A 292 ? 0.4738 0.5396 0.4722 0.0752  0.0351  -0.0338 332 PHE A CZ  
2304 N N   . ASN A 293 ? 0.3811 0.4819 0.3815 0.0307  0.0582  -0.0265 333 ASN A N   
2305 C CA  . ASN A 293 ? 0.3584 0.4701 0.3627 0.0186  0.0637  -0.0238 333 ASN A CA  
2306 C C   . ASN A 293 ? 0.4384 0.5311 0.4282 0.0101  0.0638  -0.0153 333 ASN A C   
2307 O O   . ASN A 293 ? 0.4220 0.5068 0.3973 0.0138  0.0653  -0.0133 333 ASN A O   
2308 C CB  . ASN A 293 ? 0.3682 0.5042 0.3759 0.0217  0.0721  -0.0279 333 ASN A CB  
2309 C CG  . ASN A 293 ? 0.3806 0.5321 0.3940 0.0084  0.0793  -0.0249 333 ASN A CG  
2310 O OD1 . ASN A 293 ? 0.3946 0.5396 0.3953 0.0009  0.0841  -0.0186 333 ASN A OD1 
2311 N ND2 . ASN A 293 ? 0.4198 0.5925 0.4521 0.0048  0.0801  -0.0290 333 ASN A ND2 
2312 N N   . TYR A 294 ? 0.3917 0.4762 0.3849 -0.0014 0.0615  -0.0104 334 TYR A N   
2313 C CA  . TYR A 294 ? 0.4028 0.4663 0.3818 -0.0089 0.0598  -0.0014 334 TYR A CA  
2314 C C   . TYR A 294 ? 0.4456 0.5163 0.4122 -0.0148 0.0684  0.0034  334 TYR A C   
2315 O O   . TYR A 294 ? 0.4817 0.5376 0.4307 -0.0142 0.0673  0.0086  334 TYR A O   
2316 C CB  . TYR A 294 ? 0.4094 0.4612 0.3950 -0.0197 0.0552  0.0026  334 TYR A CB  
2317 C CG  . TYR A 294 ? 0.3889 0.4318 0.3839 -0.0132 0.0468  -0.0027 334 TYR A CG  
2318 C CD1 . TYR A 294 ? 0.3790 0.4006 0.3669 -0.0072 0.0397  -0.0007 334 TYR A CD1 
2319 C CD2 . TYR A 294 ? 0.3935 0.4510 0.4044 -0.0125 0.0459  -0.0102 334 TYR A CD2 
2320 C CE1 . TYR A 294 ? 0.4102 0.4257 0.4063 -0.0007 0.0332  -0.0059 334 TYR A CE1 
2321 C CE2 . TYR A 294 ? 0.4109 0.4606 0.4277 -0.0059 0.0386  -0.0155 334 TYR A CE2 
2322 C CZ  . TYR A 294 ? 0.4334 0.4624 0.4427 0.0000  0.0330  -0.0134 334 TYR A CZ  
2323 O OH  . TYR A 294 ? 0.4188 0.4419 0.4336 0.0068  0.0271  -0.0189 334 TYR A OH  
2324 N N   . MET A 295 ? 0.4553 0.5500 0.4307 -0.0206 0.0770  0.0016  335 MET A N   
2325 C CA  . MET A 295 ? 0.5210 0.6248 0.4843 -0.0271 0.0867  0.0062  335 MET A CA  
2326 C C   . MET A 295 ? 0.5528 0.6592 0.5025 -0.0148 0.0897  0.0019  335 MET A C   
2327 O O   . MET A 295 ? 0.5946 0.6931 0.5245 -0.0173 0.0928  0.0070  335 MET A O   
2328 C CB  . MET A 295 ? 0.5056 0.6389 0.4848 -0.0355 0.0960  0.0042  335 MET A CB  
2329 C CG  . MET A 295 ? 0.5816 0.7110 0.5711 -0.0519 0.0944  0.0103  335 MET A CG  
2330 S SD  . MET A 295 ? 0.6342 0.7394 0.6021 -0.0675 0.0957  0.0258  335 MET A SD  
2331 C CE  . MET A 295 ? 0.5948 0.7269 0.5529 -0.0718 0.1121  0.0279  335 MET A CE  
2332 N N   . TYR A 296 ? 0.5251 0.6410 0.4837 -0.0017 0.0881  -0.0075 336 TYR A N   
2333 C CA  . TYR A 296 ? 0.5668 0.6810 0.5126 0.0104  0.0894  -0.0124 336 TYR A CA  
2334 C C   . TYR A 296 ? 0.6088 0.6946 0.5382 0.0130  0.0809  -0.0082 336 TYR A C   
2335 O O   . TYR A 296 ? 0.6544 0.7338 0.5663 0.0168  0.0822  -0.0086 336 TYR A O   
2336 C CB  . TYR A 296 ? 0.5632 0.6902 0.5226 0.0236  0.0881  -0.0222 336 TYR A CB  
2337 C CG  . TYR A 296 ? 0.7411 0.8689 0.6895 0.0361  0.0904  -0.0286 336 TYR A CG  
2338 C CD1 . TYR A 296 ? 0.8194 0.9253 0.7570 0.0439  0.0829  -0.0294 336 TYR A CD1 
2339 C CD2 . TYR A 296 ? 0.8288 0.9797 0.7787 0.0401  0.1001  -0.0344 336 TYR A CD2 
2340 C CE1 . TYR A 296 ? 0.8751 0.9789 0.8024 0.0548  0.0840  -0.0358 336 TYR A CE1 
2341 C CE2 . TYR A 296 ? 0.9132 1.0629 0.8525 0.0526  0.1017  -0.0415 336 TYR A CE2 
2342 C CZ  . TYR A 296 ? 0.9693 1.0938 0.8967 0.0596  0.0932  -0.0421 336 TYR A CZ  
2343 O OH  . TYR A 296 ? 1.0616 1.1820 0.9782 0.0714  0.0939  -0.0496 336 TYR A OH  
2344 N N   . SER A 297 ? 0.5886 0.6582 0.5238 0.0111  0.0720  -0.0049 337 SER A N   
2345 C CA  . SER A 297 ? 0.6051 0.6508 0.5289 0.0142  0.0633  -0.0015 337 SER A CA  
2346 C C   . SER A 297 ? 0.6673 0.6975 0.5760 0.0045  0.0615  0.0083  337 SER A C   
2347 O O   . SER A 297 ? 0.7507 0.7619 0.6503 0.0068  0.0535  0.0116  337 SER A O   
2348 C CB  . SER A 297 ? 0.6440 0.6810 0.5813 0.0178  0.0552  -0.0028 337 SER A CB  
2349 O OG  . SER A 297 ? 0.7341 0.7842 0.6837 0.0264  0.0562  -0.0106 337 SER A OG  
2350 N N   . THR A 298 ? 0.7335 0.7714 0.6394 -0.0063 0.0684  0.0135  338 THR A N   
2351 C CA  . THR A 298 ? 0.8259 0.8472 0.7172 -0.0167 0.0662  0.0245  338 THR A CA  
2352 C C   . THR A 298 ? 0.9699 0.9891 0.8368 -0.0164 0.0700  0.0272  338 THR A C   
2353 O O   . THR A 298 ? 0.9346 0.9724 0.7966 -0.0180 0.0808  0.0248  338 THR A O   
2354 C CB  . THR A 298 ? 0.7439 0.7726 0.6433 -0.0303 0.0717  0.0301  338 THR A CB  
2355 O OG1 . THR A 298 ? 0.6924 0.7198 0.6125 -0.0304 0.0663  0.0269  338 THR A OG1 
2356 C CG2 . THR A 298 ? 0.6547 0.6641 0.5363 -0.0415 0.0697  0.0430  338 THR A CG2 
2357 N N   . ALA A 299 ? 1.1217 1.1197 0.9736 -0.0139 0.0609  0.0315  339 ALA A N   
2358 C CA  . ALA A 299 ? 1.1962 1.1879 1.0220 -0.0140 0.0616  0.0347  339 ALA A CA  
2359 C C   . ALA A 299 ? 1.2307 1.1978 1.0433 -0.0193 0.0516  0.0459  339 ALA A C   
2360 O O   . ALA A 299 ? 1.2372 1.1913 1.0622 -0.0177 0.0420  0.0476  339 ALA A O   
2361 C CB  . ALA A 299 ? 1.1739 1.1656 0.9945 -0.0016 0.0584  0.0250  339 ALA A CB  
2362 N N   . PRO A 300 ? 1.2259 1.1867 1.0130 -0.0251 0.0535  0.0536  340 PRO A N   
2363 C CA  . PRO A 300 ? 1.1726 1.1085 0.9447 -0.0282 0.0420  0.0644  340 PRO A CA  
2364 C C   . PRO A 300 ? 1.0933 1.0170 0.8698 -0.0174 0.0285  0.0596  340 PRO A C   
2365 O O   . PRO A 300 ? 1.0077 0.9389 0.7854 -0.0088 0.0284  0.0497  340 PRO A O   
2366 C CB  . PRO A 300 ? 1.1687 1.1040 0.9095 -0.0333 0.0473  0.0706  340 PRO A CB  
2367 C CG  . PRO A 300 ? 1.1640 1.1240 0.9082 -0.0387 0.0641  0.0674  340 PRO A CG  
2368 C CD  . PRO A 300 ? 1.1732 1.1501 0.9441 -0.0296 0.0667  0.0537  340 PRO A CD  
2369 N N   . ARG A 301 ? 1.0788 0.9838 0.8592 -0.0181 0.0169  0.0667  341 ARG A N   
2370 C CA  . ARG A 301 ? 1.0640 0.9606 0.8556 -0.0087 0.0045  0.0624  341 ARG A CA  
2371 C C   . ARG A 301 ? 1.0322 0.9199 0.8031 -0.0046 -0.0042 0.0633  341 ARG A C   
2372 O O   . ARG A 301 ? 0.9667 0.8489 0.7118 -0.0096 -0.0031 0.0700  341 ARG A O   
2373 C CB  . ARG A 301 ? 1.0985 0.9798 0.9028 -0.0098 -0.0044 0.0689  341 ARG A CB  
2374 C CG  . ARG A 301 ? 1.1438 1.0049 0.9286 -0.0166 -0.0107 0.0826  341 ARG A CG  
2375 C CD  . ARG A 301 ? 1.1614 1.0061 0.9612 -0.0152 -0.0207 0.0870  341 ARG A CD  
2376 N NE  . ARG A 301 ? 1.1927 1.0443 1.0132 -0.0186 -0.0137 0.0830  341 ARG A NE  
2377 C CZ  . ARG A 301 ? 1.2571 1.1013 1.0973 -0.0145 -0.0199 0.0806  341 ARG A CZ  
2378 N NH1 . ARG A 301 ? 1.2391 1.0701 1.0830 -0.0063 -0.0327 0.0818  341 ARG A NH1 
2379 N NH2 . ARG A 301 ? 1.2859 1.1370 1.1425 -0.0182 -0.0135 0.0762  341 ARG A NH2 
2380 N N   . PRO A 302 ? 1.0085 0.8954 0.7900 0.0040  -0.0129 0.0564  342 PRO A N   
2381 C CA  . PRO A 302 ? 0.9785 0.8570 0.7425 0.0074  -0.0231 0.0565  342 PRO A CA  
2382 C C   . PRO A 302 ? 0.9583 0.8187 0.7068 0.0042  -0.0339 0.0687  342 PRO A C   
2383 O O   . PRO A 302 ? 0.9263 0.7774 0.6872 0.0037  -0.0395 0.0749  342 PRO A O   
2384 C CB  . PRO A 302 ? 0.9771 0.8587 0.7631 0.0154  -0.0307 0.0482  342 PRO A CB  
2385 C CG  . PRO A 302 ? 1.0220 0.9094 0.8348 0.0163  -0.0266 0.0468  342 PRO A CG  
2386 C CD  . PRO A 302 ? 1.0265 0.9216 0.8358 0.0102  -0.0132 0.0480  342 PRO A CD  
2387 N N   . ARG A 303 ? 0.9672 0.8217 0.6870 0.0026  -0.0372 0.0719  343 ARG A N   
2388 C CA  . ARG A 303 ? 0.9841 0.8206 0.6842 -0.0003 -0.0478 0.0845  343 ARG A CA  
2389 C C   . ARG A 303 ? 0.8634 0.6906 0.5760 0.0070  -0.0656 0.0847  343 ARG A C   
2390 O O   . ARG A 303 ? 0.7527 0.5880 0.4805 0.0134  -0.0703 0.0748  343 ARG A O   
2391 C CB  . ARG A 303 ? 1.0610 0.8952 0.7247 -0.0034 -0.0462 0.0870  343 ARG A CB  
2392 C CG  . ARG A 303 ? 1.1794 1.0258 0.8313 -0.0103 -0.0277 0.0866  343 ARG A CG  
2393 C CD  . ARG A 303 ? 1.3423 1.1851 0.9549 -0.0141 -0.0255 0.0914  343 ARG A CD  
2394 N NE  . ARG A 303 ? 1.4528 1.3095 1.0554 -0.0214 -0.0066 0.0922  343 ARG A NE  
2395 C CZ  . ARG A 303 ? 1.5337 1.3865 1.1266 -0.0319 0.0006  0.1055  343 ARG A CZ  
2396 N NH1 . ARG A 303 ? 1.5506 1.4202 1.1373 -0.0386 0.0186  0.1051  343 ARG A NH1 
2397 N NH2 . ARG A 303 ? 1.5504 1.3825 1.1405 -0.0358 -0.0103 0.1192  343 ARG A NH2 
2398 N N   . VAL A 304 ? 0.8439 0.6542 0.5512 0.0060  -0.0757 0.0965  344 VAL A N   
2399 C CA  . VAL A 304 ? 0.7776 0.5802 0.4973 0.0137  -0.0932 0.0973  344 VAL A CA  
2400 C C   . VAL A 304 ? 0.7370 0.5378 0.4367 0.0166  -0.1048 0.0958  344 VAL A C   
2401 O O   . VAL A 304 ? 0.7494 0.5557 0.4651 0.0232  -0.1154 0.0889  344 VAL A O   
2402 C CB  . VAL A 304 ? 0.8149 0.5982 0.5339 0.0129  -0.1013 0.1103  344 VAL A CB  
2403 C CG1 . VAL A 304 ? 0.8166 0.5916 0.5432 0.0218  -0.1210 0.1124  344 VAL A CG1 
2404 C CG2 . VAL A 304 ? 0.7717 0.5572 0.5161 0.0116  -0.0925 0.1086  344 VAL A CG2 
2405 N N   . GLU A 305 ? 0.7156 0.5101 0.3802 0.0113  -0.1025 0.1016  345 GLU A N   
2406 C CA  . GLU A 305 ? 0.7613 0.5494 0.4004 0.0135  -0.1157 0.1025  345 GLU A CA  
2407 C C   . GLU A 305 ? 0.7889 0.5906 0.4253 0.0155  -0.1125 0.0879  345 GLU A C   
2408 O O   . GLU A 305 ? 0.8112 0.6129 0.4172 0.0127  -0.1083 0.0862  345 GLU A O   
2409 C CB  . GLU A 305 ? 0.8250 0.5991 0.4246 0.0068  -0.1144 0.1158  345 GLU A CB  
2410 C CG  . GLU A 305 ? 0.8642 0.6195 0.4622 0.0044  -0.1202 0.1319  345 GLU A CG  
2411 C CD  . GLU A 305 ? 0.8658 0.6229 0.4807 -0.0018 -0.1048 0.1348  345 GLU A CD  
2412 O OE1 . GLU A 305 ? 0.8838 0.6576 0.5056 -0.0054 -0.0882 0.1263  345 GLU A OE1 
2413 O OE2 . GLU A 305 ? 0.9014 0.6429 0.5235 -0.0027 -0.1103 0.1451  345 GLU A OE2 
2414 N N   . THR A 306 ? 0.7459 0.5586 0.4138 0.0205  -0.1147 0.0773  346 THR A N   
2415 C CA  . THR A 306 ? 0.7799 0.6019 0.4473 0.0225  -0.1147 0.0638  346 THR A CA  
2416 C C   . THR A 306 ? 0.7344 0.5637 0.4359 0.0276  -0.1242 0.0568  346 THR A C   
2417 O O   . THR A 306 ? 0.6827 0.5154 0.4123 0.0298  -0.1237 0.0593  346 THR A O   
2418 C CB  . THR A 306 ? 0.7655 0.5981 0.4315 0.0202  -0.0953 0.0557  346 THR A CB  
2419 O OG1 . THR A 306 ? 0.7859 0.6231 0.4472 0.0227  -0.0970 0.0429  346 THR A OG1 
2420 C CG2 . THR A 306 ? 0.6927 0.5348 0.3923 0.0210  -0.0855 0.0535  346 THR A CG2 
2421 N N   . SER A 307 ? 0.7591 0.5911 0.4578 0.0291  -0.1327 0.0476  347 SER A N   
2422 C CA  . SER A 307 ? 0.7650 0.6067 0.4961 0.0320  -0.1389 0.0396  347 SER A CA  
2423 C C   . SER A 307 ? 0.7128 0.5636 0.4563 0.0313  -0.1255 0.0289  347 SER A C   
2424 O O   . SER A 307 ? 0.7002 0.5592 0.4713 0.0326  -0.1280 0.0231  347 SER A O   
2425 C CB  . SER A 307 ? 0.9199 0.7591 0.6445 0.0329  -0.1577 0.0359  347 SER A CB  
2426 O OG  . SER A 307 ? 1.1318 0.9631 0.8476 0.0349  -0.1720 0.0461  347 SER A OG  
2427 N N   . ARG A 308 ? 0.6426 0.4927 0.3667 0.0294  -0.1114 0.0264  348 ARG A N   
2428 C CA  . ARG A 308 ? 0.6669 0.5244 0.4009 0.0301  -0.0994 0.0162  348 ARG A CA  
2429 C C   . ARG A 308 ? 0.6736 0.5405 0.4403 0.0313  -0.0912 0.0173  348 ARG A C   
2430 O O   . ARG A 308 ? 0.6554 0.5230 0.4287 0.0308  -0.0871 0.0254  348 ARG A O   
2431 C CB  . ARG A 308 ? 0.6422 0.4991 0.3494 0.0291  -0.0859 0.0137  348 ARG A CB  
2432 C CG  . ARG A 308 ? 0.7062 0.5547 0.3796 0.0288  -0.0930 0.0097  348 ARG A CG  
2433 C CD  . ARG A 308 ? 0.7536 0.6034 0.3986 0.0280  -0.0790 0.0084  348 ARG A CD  
2434 N NE  . ARG A 308 ? 0.8466 0.6881 0.4569 0.0282  -0.0863 0.0042  348 ARG A NE  
2435 C CZ  . ARG A 308 ? 0.8634 0.7054 0.4424 0.0276  -0.0763 0.0034  348 ARG A CZ  
2436 N NH1 . ARG A 308 ? 0.8923 0.7442 0.4733 0.0261  -0.0586 0.0068  348 ARG A NH1 
2437 N NH2 . ARG A 308 ? 0.9300 0.7642 0.4764 0.0284  -0.0838 -0.0012 348 ARG A NH2 
2438 N N   . ALA A 309 ? 0.6241 0.4968 0.4099 0.0327  -0.0893 0.0091  349 ALA A N   
2439 C CA  . ALA A 309 ? 0.5745 0.4566 0.3903 0.0341  -0.0824 0.0095  349 ALA A CA  
2440 C C   . ALA A 309 ? 0.5983 0.4846 0.4119 0.0342  -0.0670 0.0114  349 ALA A C   
2441 O O   . ALA A 309 ? 0.6145 0.4997 0.4079 0.0335  -0.0588 0.0088  349 ALA A O   
2442 C CB  . ALA A 309 ? 0.5709 0.4567 0.4022 0.0347  -0.0824 0.0010  349 ALA A CB  
2443 N N   . VAL A 310 ? 0.5575 0.4498 0.3927 0.0351  -0.0630 0.0153  350 VAL A N   
2444 C CA  . VAL A 310 ? 0.5686 0.4659 0.4059 0.0345  -0.0500 0.0171  350 VAL A CA  
2445 C C   . VAL A 310 ? 0.5724 0.4778 0.4188 0.0368  -0.0403 0.0091  350 VAL A C   
2446 O O   . VAL A 310 ? 0.6052 0.5135 0.4684 0.0388  -0.0432 0.0053  350 VAL A O   
2447 C CB  . VAL A 310 ? 0.6376 0.5364 0.4937 0.0351  -0.0511 0.0231  350 VAL A CB  
2448 C CG1 . VAL A 310 ? 0.5679 0.4717 0.4270 0.0335  -0.0387 0.0242  350 VAL A CG1 
2449 C CG2 . VAL A 310 ? 0.7049 0.5933 0.5516 0.0340  -0.0621 0.0313  350 VAL A CG2 
2450 N N   . PRO A 311 ? 0.5617 0.4714 0.3980 0.0366  -0.0289 0.0067  351 PRO A N   
2451 C CA  . PRO A 311 ? 0.5602 0.4773 0.4055 0.0402  -0.0206 -0.0006 351 PRO A CA  
2452 C C   . PRO A 311 ? 0.5097 0.4341 0.3799 0.0417  -0.0178 0.0006  351 PRO A C   
2453 O O   . PRO A 311 ? 0.5222 0.4480 0.4007 0.0400  -0.0183 0.0062  351 PRO A O   
2454 C CB  . PRO A 311 ? 0.5536 0.4765 0.3844 0.0396  -0.0094 -0.0020 351 PRO A CB  
2455 C CG  . PRO A 311 ? 0.6232 0.5394 0.4316 0.0354  -0.0126 0.0032  351 PRO A CG  
2456 C CD  . PRO A 311 ? 0.6007 0.5093 0.4162 0.0331  -0.0235 0.0108  351 PRO A CD  
2457 N N   . LEU A 312 ? 0.5204 0.4482 0.4013 0.0452  -0.0153 -0.0048 352 LEU A N   
2458 C CA  . LEU A 312 ? 0.5693 0.5041 0.4720 0.0470  -0.0131 -0.0039 352 LEU A CA  
2459 C C   . LEU A 312 ? 0.6464 0.5903 0.5541 0.0478  -0.0038 -0.0035 352 LEU A C   
2460 O O   . LEU A 312 ? 0.8373 0.7853 0.7584 0.0476  -0.0035 -0.0008 352 LEU A O   
2461 C CB  . LEU A 312 ? 0.5861 0.5203 0.4962 0.0497  -0.0133 -0.0085 352 LEU A CB  
2462 C CG  . LEU A 312 ? 0.6376 0.5659 0.5531 0.0477  -0.0228 -0.0084 352 LEU A CG  
2463 C CD1 . LEU A 312 ? 0.5660 0.4983 0.4985 0.0489  -0.0209 -0.0088 352 LEU A CD1 
2464 C CD2 . LEU A 312 ? 0.7008 0.6292 0.6209 0.0452  -0.0304 -0.0033 352 LEU A CD2 
2465 N N   . ALA A 313 ? 0.6342 0.5824 0.5325 0.0491  0.0036  -0.0072 353 ALA A N   
2466 C CA  . ALA A 313 ? 0.8324 0.7918 0.7384 0.0498  0.0118  -0.0076 353 ALA A CA  
2467 C C   . ALA A 313 ? 1.0626 1.0275 0.9551 0.0484  0.0188  -0.0092 353 ALA A C   
2468 O O   . ALA A 313 ? 1.0489 1.0087 0.9251 0.0485  0.0181  -0.0110 353 ALA A O   
2469 C CB  . ALA A 313 ? 0.7967 0.7620 0.7147 0.0553  0.0148  -0.0118 353 ALA A CB  
2470 N N   . GLY A 314 ? 1.2849 1.2612 1.1846 0.0470  0.0256  -0.0089 354 GLY A N   
2471 C CA  . GLY A 314 ? 1.4420 1.4276 1.3326 0.0444  0.0335  -0.0096 354 GLY A CA  
2472 C C   . GLY A 314 ? 1.5718 1.5532 1.4525 0.0358  0.0334  -0.0022 354 GLY A C   
2473 O O   . GLY A 314 ? 1.6430 1.6326 1.5145 0.0321  0.0408  -0.0016 354 GLY A O   
2474 N N   . PHE A 315 ? 1.5954 1.5645 1.4779 0.0326  0.0254  0.0039  355 PHE A N   
2475 C CA  . PHE A 315 ? 1.5951 1.5557 1.4660 0.0250  0.0232  0.0122  355 PHE A CA  
2476 C C   . PHE A 315 ? 1.4347 1.3917 1.3185 0.0207  0.0209  0.0173  355 PHE A C   
2477 O O   . PHE A 315 ? 1.4990 1.4425 1.3775 0.0171  0.0141  0.0244  355 PHE A O   
2478 C CB  . PHE A 315 ? 1.7429 1.6888 1.6002 0.0258  0.0136  0.0150  355 PHE A CB  
2479 C CG  . PHE A 315 ? 1.8577 1.8026 1.6916 0.0251  0.0160  0.0139  355 PHE A CG  
2480 C CD1 . PHE A 315 ? 1.8969 1.8310 1.7112 0.0201  0.0115  0.0214  355 PHE A CD1 
2481 C CD2 . PHE A 315 ? 1.8762 1.8298 1.7062 0.0303  0.0221  0.0052  355 PHE A CD2 
2482 C CE1 . PHE A 315 ? 1.9077 1.8411 1.6979 0.0197  0.0138  0.0199  355 PHE A CE1 
2483 C CE2 . PHE A 315 ? 1.8941 1.8466 1.7014 0.0306  0.0244  0.0027  355 PHE A CE2 
2484 C CZ  . PHE A 315 ? 1.9139 1.8568 1.7006 0.0251  0.0206  0.0099  355 PHE A CZ  
2485 N N   . GLY A 316 ? 1.1426 1.1105 1.0428 0.0213  0.0255  0.0136  356 GLY A N   
2486 C CA  . GLY A 316 ? 0.9741 0.9375 0.8855 0.0171  0.0231  0.0171  356 GLY A CA  
2487 C C   . GLY A 316 ? 0.7191 0.6954 0.6481 0.0196  0.0270  0.0108  356 GLY A C   
2488 O O   . GLY A 316 ? 0.6173 0.6082 0.5492 0.0229  0.0331  0.0051  356 GLY A O   
2489 N N   . TYR A 317 ? 0.4794 0.4496 0.4197 0.0187  0.0226  0.0114  357 TYR A N   
2490 C CA  . TYR A 317 ? 0.4125 0.3933 0.3682 0.0205  0.0248  0.0055  357 TYR A CA  
2491 C C   . TYR A 317 ? 0.4097 0.3895 0.3749 0.0294  0.0205  0.0010  357 TYR A C   
2492 O O   . TYR A 317 ? 0.3844 0.3685 0.3608 0.0310  0.0202  -0.0033 357 TYR A O   
2493 C CB  . TYR A 317 ? 0.4640 0.4394 0.4248 0.0122  0.0238  0.0082  357 TYR A CB  
2494 C CG  . TYR A 317 ? 0.5388 0.5178 0.4924 0.0013  0.0295  0.0132  357 TYR A CG  
2495 C CD1 . TYR A 317 ? 0.5186 0.5128 0.4658 0.0008  0.0374  0.0121  357 TYR A CD1 
2496 C CD2 . TYR A 317 ? 0.4847 0.4519 0.4379 -0.0086 0.0273  0.0191  357 TYR A CD2 
2497 C CE1 . TYR A 317 ? 0.4818 0.4823 0.4231 -0.0093 0.0441  0.0167  357 TYR A CE1 
2498 C CE2 . TYR A 317 ? 0.5321 0.5034 0.4789 -0.0201 0.0335  0.0249  357 TYR A CE2 
2499 C CZ  . TYR A 317 ? 0.5355 0.5250 0.4764 -0.0205 0.0424  0.0237  357 TYR A CZ  
2500 O OH  . TYR A 317 ? 0.5768 0.5734 0.5117 -0.0321 0.0499  0.0295  357 TYR A OH  
2501 N N   . GLY A 318 ? 0.4241 0.3991 0.3852 0.0346  0.0173  0.0016  358 GLY A N   
2502 C CA  . GLY A 318 ? 0.4221 0.3978 0.3927 0.0419  0.0143  -0.0017 358 GLY A CA  
2503 C C   . GLY A 318 ? 0.4453 0.4341 0.4239 0.0463  0.0187  -0.0078 358 GLY A C   
2504 O O   . GLY A 318 ? 0.4160 0.4064 0.4036 0.0500  0.0173  -0.0106 358 GLY A O   
2505 N N   . LEU A 319 ? 0.3909 0.3894 0.3658 0.0466  0.0239  -0.0099 359 LEU A N   
2506 C CA  . LEU A 319 ? 0.4375 0.4477 0.4188 0.0521  0.0268  -0.0151 359 LEU A CA  
2507 C C   . LEU A 319 ? 0.3926 0.4110 0.3823 0.0499  0.0278  -0.0184 359 LEU A C   
2508 O O   . LEU A 319 ? 0.3799 0.4015 0.3759 0.0542  0.0265  -0.0218 359 LEU A O   
2509 C CB  . LEU A 319 ? 0.4476 0.4649 0.4229 0.0550  0.0310  -0.0170 359 LEU A CB  
2510 C CG  . LEU A 319 ? 0.6127 0.6311 0.5882 0.0629  0.0308  -0.0192 359 LEU A CG  
2511 C CD1 . LEU A 319 ? 0.6527 0.6764 0.6220 0.0664  0.0344  -0.0218 359 LEU A CD1 
2512 C CD2 . LEU A 319 ? 0.5969 0.6227 0.5810 0.0670  0.0307  -0.0219 359 LEU A CD2 
2513 N N   . PRO A 320 ? 0.3500 0.3728 0.3398 0.0428  0.0302  -0.0178 360 PRO A N   
2514 C CA  . PRO A 320 ? 0.3850 0.4149 0.3844 0.0396  0.0298  -0.0215 360 PRO A CA  
2515 C C   . PRO A 320 ? 0.3815 0.3992 0.3849 0.0389  0.0244  -0.0219 360 PRO A C   
2516 O O   . PRO A 320 ? 0.3808 0.4033 0.3912 0.0408  0.0228  -0.0272 360 PRO A O   
2517 C CB  . PRO A 320 ? 0.3396 0.3750 0.3383 0.0299  0.0336  -0.0192 360 PRO A CB  
2518 C CG  . PRO A 320 ? 0.3751 0.4003 0.3616 0.0274  0.0346  -0.0129 360 PRO A CG  
2519 C CD  . PRO A 320 ? 0.3572 0.3805 0.3389 0.0368  0.0338  -0.0142 360 PRO A CD  
2520 N N   . ILE A 321 ? 0.3670 0.3692 0.3658 0.0371  0.0210  -0.0169 361 ILE A N   
2521 C CA  . ILE A 321 ? 0.4091 0.3997 0.4126 0.0383  0.0156  -0.0180 361 ILE A CA  
2522 C C   . ILE A 321 ? 0.4166 0.4110 0.4241 0.0481  0.0148  -0.0222 361 ILE A C   
2523 O O   . ILE A 321 ? 0.3863 0.3797 0.3996 0.0511  0.0126  -0.0272 361 ILE A O   
2524 C CB  . ILE A 321 ? 0.4087 0.3820 0.4066 0.0347  0.0113  -0.0111 361 ILE A CB  
2525 C CG1 . ILE A 321 ? 0.4475 0.4153 0.4416 0.0237  0.0120  -0.0067 361 ILE A CG1 
2526 C CG2 . ILE A 321 ? 0.3797 0.3416 0.3832 0.0399  0.0053  -0.0129 361 ILE A CG2 
2527 C CD1 . ILE A 321 ? 0.4683 0.4177 0.4538 0.0196  0.0075  0.0016  361 ILE A CD1 
2528 N N   . SER A 322 ? 0.3764 0.3753 0.3805 0.0527  0.0170  -0.0205 362 SER A N   
2529 C CA  . SER A 322 ? 0.3962 0.4006 0.4037 0.0605  0.0176  -0.0234 362 SER A CA  
2530 C C   . SER A 322 ? 0.3689 0.3844 0.3792 0.0634  0.0196  -0.0294 362 SER A C   
2531 O O   . SER A 322 ? 0.3739 0.3914 0.3874 0.0682  0.0190  -0.0332 362 SER A O   
2532 C CB  . SER A 322 ? 0.3971 0.4035 0.4001 0.0632  0.0195  -0.0202 362 SER A CB  
2533 O OG  . SER A 322 ? 0.4156 0.4129 0.4178 0.0624  0.0162  -0.0160 362 SER A OG  
2534 N N   . ARG A 323 ? 0.3694 0.3937 0.3784 0.0609  0.0220  -0.0305 363 ARG A N   
2535 C CA  . ARG A 323 ? 0.3531 0.3891 0.3650 0.0639  0.0225  -0.0363 363 ARG A CA  
2536 C C   . ARG A 323 ? 0.3764 0.4099 0.3934 0.0609  0.0190  -0.0413 363 ARG A C   
2537 O O   . ARG A 323 ? 0.3702 0.4093 0.3884 0.0654  0.0178  -0.0470 363 ARG A O   
2538 C CB  . ARG A 323 ? 0.2987 0.3466 0.3104 0.0625  0.0251  -0.0368 363 ARG A CB  
2539 C CG  . ARG A 323 ? 0.3113 0.3728 0.3268 0.0660  0.0242  -0.0427 363 ARG A CG  
2540 C CD  . ARG A 323 ? 0.3570 0.4324 0.3736 0.0678  0.0266  -0.0434 363 ARG A CD  
2541 N NE  . ARG A 323 ? 0.3605 0.4420 0.3825 0.0593  0.0283  -0.0435 363 ARG A NE  
2542 C CZ  . ARG A 323 ? 0.3972 0.4945 0.4236 0.0595  0.0309  -0.0453 363 ARG A CZ  
2543 N NH1 . ARG A 323 ? 0.3592 0.4659 0.3847 0.0689  0.0310  -0.0473 363 ARG A NH1 
2544 N NH2 . ARG A 323 ? 0.3284 0.4324 0.3603 0.0503  0.0336  -0.0447 363 ARG A NH2 
2545 N N   . LEU A 324 ? 0.3829 0.4065 0.4017 0.0533  0.0170  -0.0393 364 LEU A N   
2546 C CA  . LEU A 324 ? 0.3666 0.3836 0.3901 0.0501  0.0128  -0.0443 364 LEU A CA  
2547 C C   . LEU A 324 ? 0.3955 0.4047 0.4192 0.0576  0.0103  -0.0476 364 LEU A C   
2548 O O   . LEU A 324 ? 0.3984 0.4083 0.4242 0.0602  0.0078  -0.0552 364 LEU A O   
2549 C CB  . LEU A 324 ? 0.3457 0.3503 0.3696 0.0400  0.0109  -0.0397 364 LEU A CB  
2550 C CG  . LEU A 324 ? 0.3872 0.4015 0.4125 0.0308  0.0142  -0.0373 364 LEU A CG  
2551 C CD1 . LEU A 324 ? 0.3698 0.3699 0.3937 0.0201  0.0127  -0.0313 364 LEU A CD1 
2552 C CD2 . LEU A 324 ? 0.4030 0.4319 0.4358 0.0292  0.0135  -0.0449 364 LEU A CD2 
2553 N N   . TYR A 325 ? 0.3612 0.3645 0.3831 0.0615  0.0109  -0.0428 365 TYR A N   
2554 C CA  . TYR A 325 ? 0.3856 0.3862 0.4098 0.0694  0.0099  -0.0461 365 TYR A CA  
2555 C C   . TYR A 325 ? 0.3702 0.3841 0.3926 0.0761  0.0129  -0.0514 365 TYR A C   
2556 O O   . TYR A 325 ? 0.3621 0.3762 0.3855 0.0809  0.0117  -0.0584 365 TYR A O   
2557 C CB  . TYR A 325 ? 0.3532 0.3498 0.3777 0.0720  0.0104  -0.0397 365 TYR A CB  
2558 C CG  . TYR A 325 ? 0.3726 0.3537 0.3988 0.0690  0.0053  -0.0359 365 TYR A CG  
2559 C CD1 . TYR A 325 ? 0.4577 0.4279 0.4883 0.0713  0.0007  -0.0403 365 TYR A CD1 
2560 C CD2 . TYR A 325 ? 0.4755 0.4516 0.4978 0.0646  0.0045  -0.0281 365 TYR A CD2 
2561 C CE1 . TYR A 325 ? 0.5737 0.5276 0.6052 0.0694  -0.0050 -0.0359 365 TYR A CE1 
2562 C CE2 . TYR A 325 ? 0.5584 0.5195 0.5803 0.0623  -0.0009 -0.0236 365 TYR A CE2 
2563 C CZ  . TYR A 325 ? 0.5531 0.5029 0.5798 0.0647  -0.0059 -0.0270 365 TYR A CZ  
2564 O OH  . TYR A 325 ? 0.5973 0.5305 0.6227 0.0630  -0.0122 -0.0216 365 TYR A OH  
2565 N N   . ALA A 326 ? 0.4080 0.4322 0.4264 0.0771  0.0166  -0.0482 366 ALA A N   
2566 C CA  . ALA A 326 ? 0.4283 0.4638 0.4428 0.0834  0.0190  -0.0516 366 ALA A CA  
2567 C C   . ALA A 326 ? 0.3933 0.4334 0.4075 0.0831  0.0161  -0.0599 366 ALA A C   
2568 O O   . ALA A 326 ? 0.3910 0.4348 0.4023 0.0888  0.0159  -0.0658 366 ALA A O   
2569 C CB  . ALA A 326 ? 0.4349 0.4775 0.4450 0.0842  0.0222  -0.0463 366 ALA A CB  
2570 N N   . GLN A 327 ? 0.3611 0.4019 0.3785 0.0762  0.0137  -0.0606 367 GLN A N   
2571 C CA  . GLN A 327 ? 0.3691 0.4160 0.3881 0.0745  0.0100  -0.0686 367 GLN A CA  
2572 C C   . GLN A 327 ? 0.3869 0.4224 0.4084 0.0730  0.0055  -0.0756 367 GLN A C   
2573 O O   . GLN A 327 ? 0.4061 0.4455 0.4272 0.0737  0.0017  -0.0842 367 GLN A O   
2574 C CB  . GLN A 327 ? 0.3566 0.4103 0.3806 0.0665  0.0095  -0.0669 367 GLN A CB  
2575 C CG  . GLN A 327 ? 0.3691 0.4359 0.3907 0.0700  0.0129  -0.0628 367 GLN A CG  
2576 C CD  . GLN A 327 ? 0.4144 0.4895 0.4424 0.0628  0.0138  -0.0612 367 GLN A CD  
2577 O OE1 . GLN A 327 ? 0.4270 0.4973 0.4605 0.0535  0.0127  -0.0612 367 GLN A OE1 
2578 N NE2 . GLN A 327 ? 0.3654 0.4530 0.3925 0.0670  0.0161  -0.0595 367 GLN A NE2 
2579 N N   . TYR A 328 ? 0.3524 0.3733 0.3763 0.0717  0.0049  -0.0726 368 TYR A N   
2580 C CA  . TYR A 328 ? 0.3622 0.3690 0.3888 0.0711  -0.0002 -0.0793 368 TYR A CA  
2581 C C   . TYR A 328 ? 0.4155 0.4260 0.4381 0.0805  -0.0008 -0.0892 368 TYR A C   
2582 O O   . TYR A 328 ? 0.4123 0.4160 0.4354 0.0798  -0.0060 -0.0986 368 TYR A O   
2583 C CB  . TYR A 328 ? 0.3347 0.3260 0.3640 0.0707  -0.0009 -0.0734 368 TYR A CB  
2584 C CG  . TYR A 328 ? 0.3865 0.3608 0.4184 0.0729  -0.0064 -0.0799 368 TYR A CG  
2585 C CD1 . TYR A 328 ? 0.3775 0.3409 0.4113 0.0662  -0.0123 -0.0857 368 TYR A CD1 
2586 C CD2 . TYR A 328 ? 0.3538 0.3225 0.3874 0.0817  -0.0062 -0.0803 368 TYR A CD2 
2587 C CE1 . TYR A 328 ? 0.3987 0.3432 0.4343 0.0688  -0.0182 -0.0920 368 TYR A CE1 
2588 C CE2 . TYR A 328 ? 0.3838 0.3362 0.4203 0.0855  -0.0116 -0.0868 368 TYR A CE2 
2589 C CZ  . TYR A 328 ? 0.4462 0.3850 0.4829 0.0793  -0.0178 -0.0927 368 TYR A CZ  
2590 O OH  . TYR A 328 ? 0.4392 0.3587 0.4782 0.0838  -0.0240 -0.0998 368 TYR A OH  
2591 N N   . PHE A 329 ? 0.4176 0.4384 0.4355 0.0888  0.0044  -0.0875 369 PHE A N   
2592 C CA  . PHE A 329 ? 0.4046 0.4314 0.4163 0.0980  0.0055  -0.0960 369 PHE A CA  
2593 C C   . PHE A 329 ? 0.4360 0.4791 0.4393 0.1008  0.0078  -0.0960 369 PHE A C   
2594 O O   . PHE A 329 ? 0.4585 0.5098 0.4542 0.1085  0.0123  -0.0965 369 PHE A O   
2595 C CB  . PHE A 329 ? 0.4041 0.4304 0.4170 0.1058  0.0102  -0.0944 369 PHE A CB  
2596 C CG  . PHE A 329 ? 0.4372 0.4486 0.4564 0.1080  0.0063  -0.0997 369 PHE A CG  
2597 C CD1 . PHE A 329 ? 0.5000 0.5040 0.5172 0.1108  0.0015  -0.1120 369 PHE A CD1 
2598 C CD2 . PHE A 329 ? 0.4799 0.4839 0.5067 0.1080  0.0067  -0.0929 369 PHE A CD2 
2599 C CE1 . PHE A 329 ? 0.5449 0.5328 0.5677 0.1141  -0.0028 -0.1174 369 PHE A CE1 
2600 C CE2 . PHE A 329 ? 0.5081 0.4975 0.5409 0.1115  0.0021  -0.0975 369 PHE A CE2 
2601 C CZ  . PHE A 329 ? 0.5260 0.5066 0.5570 0.1148  -0.0025 -0.1097 369 PHE A CZ  
2602 N N   . GLN A 330 ? 0.3861 0.4343 0.3906 0.0946  0.0048  -0.0949 370 GLN A N   
2603 C CA  . GLN A 330 ? 0.3885 0.4514 0.3860 0.0974  0.0045  -0.0958 370 GLN A CA  
2604 C C   . GLN A 330 ? 0.4075 0.4776 0.3998 0.1015  0.0106  -0.0859 370 GLN A C   
2605 O O   . GLN A 330 ? 0.4325 0.5126 0.4158 0.1066  0.0109  -0.0858 370 GLN A O   
2606 C CB  . GLN A 330 ? 0.4310 0.4981 0.4190 0.1040  0.0018  -0.1065 370 GLN A CB  
2607 C CG  . GLN A 330 ? 0.4457 0.5033 0.4377 0.1005  -0.0052 -0.1181 370 GLN A CG  
2608 C CD  . GLN A 330 ? 0.5133 0.5726 0.5140 0.0904  -0.0114 -0.1196 370 GLN A CD  
2609 O OE1 . GLN A 330 ? 0.6138 0.6870 0.6147 0.0893  -0.0121 -0.1167 370 GLN A OE1 
2610 N NE2 . GLN A 330 ? 0.6203 0.6658 0.6291 0.0830  -0.0161 -0.1241 370 GLN A NE2 
2611 N N   . GLY A 331 ? 0.3838 0.4478 0.3808 0.0993  0.0145  -0.0775 371 GLY A N   
2612 C CA  . GLY A 331 ? 0.3694 0.4375 0.3631 0.1010  0.0190  -0.0681 371 GLY A CA  
2613 C C   . GLY A 331 ? 0.3792 0.4492 0.3772 0.0958  0.0176  -0.0642 371 GLY A C   
2614 O O   . GLY A 331 ? 0.3623 0.4356 0.3652 0.0913  0.0136  -0.0688 371 GLY A O   
2615 N N   . ASP A 332 ? 0.3420 0.4106 0.3388 0.0962  0.0211  -0.0560 372 ASP A N   
2616 C CA  . ASP A 332 ? 0.3656 0.4369 0.3655 0.0928  0.0207  -0.0529 372 ASP A CA  
2617 C C   . ASP A 332 ? 0.3528 0.4172 0.3510 0.0926  0.0243  -0.0449 372 ASP A C   
2618 O O   . ASP A 332 ? 0.3811 0.4407 0.3767 0.0949  0.0267  -0.0414 372 ASP A O   
2619 C CB  . ASP A 332 ? 0.4188 0.5022 0.4153 0.0973  0.0186  -0.0550 372 ASP A CB  
2620 C CG  . ASP A 332 ? 0.4062 0.4974 0.4104 0.0931  0.0171  -0.0563 372 ASP A CG  
2621 O OD1 . ASP A 332 ? 0.4198 0.5060 0.4294 0.0866  0.0189  -0.0540 372 ASP A OD1 
2622 O OD2 . ASP A 332 ? 0.4618 0.5653 0.4667 0.0966  0.0142  -0.0595 372 ASP A OD2 
2623 N N   . LEU A 333 ? 0.3345 0.3993 0.3350 0.0896  0.0246  -0.0426 373 LEU A N   
2624 C CA  . LEU A 333 ? 0.3333 0.3910 0.3310 0.0894  0.0270  -0.0363 373 LEU A CA  
2625 C C   . LEU A 333 ? 0.3621 0.4261 0.3588 0.0914  0.0273  -0.0364 373 LEU A C   
2626 O O   . LEU A 333 ? 0.3762 0.4470 0.3781 0.0875  0.0270  -0.0393 373 LEU A O   
2627 C CB  . LEU A 333 ? 0.3570 0.4052 0.3580 0.0830  0.0271  -0.0340 373 LEU A CB  
2628 C CG  . LEU A 333 ? 0.4010 0.4401 0.3989 0.0825  0.0282  -0.0282 373 LEU A CG  
2629 C CD1 . LEU A 333 ? 0.3494 0.3798 0.3503 0.0772  0.0266  -0.0263 373 LEU A CD1 
2630 C CD2 . LEU A 333 ? 0.3817 0.4211 0.3752 0.0833  0.0294  -0.0267 373 LEU A CD2 
2631 N N   . LYS A 334 ? 0.3678 0.4300 0.3584 0.0974  0.0280  -0.0332 374 LYS A N   
2632 C CA  . LYS A 334 ? 0.3847 0.4529 0.3743 0.1020  0.0276  -0.0341 374 LYS A CA  
2633 C C   . LYS A 334 ? 0.4049 0.4619 0.3892 0.1035  0.0291  -0.0298 374 LYS A C   
2634 O O   . LYS A 334 ? 0.4247 0.4704 0.4047 0.1027  0.0296  -0.0253 374 LYS A O   
2635 C CB  . LYS A 334 ? 0.3943 0.4699 0.3803 0.1098  0.0251  -0.0352 374 LYS A CB  
2636 C CG  . LYS A 334 ? 0.4736 0.5608 0.4642 0.1084  0.0224  -0.0410 374 LYS A CG  
2637 C CD  . LYS A 334 ? 0.5325 0.6282 0.5183 0.1165  0.0187  -0.0425 374 LYS A CD  
2638 C CE  . LYS A 334 ? 0.5857 0.6958 0.5787 0.1144  0.0147  -0.0503 374 LYS A CE  
2639 N NZ  . LYS A 334 ? 0.7719 0.8939 0.7623 0.1226  0.0096  -0.0526 374 LYS A NZ  
2640 N N   . LEU A 335 ? 0.3597 0.4209 0.3449 0.1054  0.0298  -0.0320 375 LEU A N   
2641 C CA  . LEU A 335 ? 0.3471 0.3975 0.3263 0.1079  0.0306  -0.0301 375 LEU A CA  
2642 C C   . LEU A 335 ? 0.3921 0.4461 0.3690 0.1179  0.0292  -0.0318 375 LEU A C   
2643 O O   . LEU A 335 ? 0.4286 0.4984 0.4116 0.1213  0.0289  -0.0363 375 LEU A O   
2644 C CB  . LEU A 335 ? 0.4233 0.4744 0.4035 0.1027  0.0332  -0.0320 375 LEU A CB  
2645 C CG  . LEU A 335 ? 0.5198 0.5651 0.5008 0.0933  0.0337  -0.0298 375 LEU A CG  
2646 C CD1 . LEU A 335 ? 0.5244 0.5694 0.5022 0.0896  0.0362  -0.0309 375 LEU A CD1 
2647 C CD2 . LEU A 335 ? 0.5021 0.5331 0.4794 0.0921  0.0318  -0.0251 375 LEU A CD2 
2648 N N   A TYR A 336 ? 0.3902 0.4294 0.3591 0.1226  0.0278  -0.0282 376 TYR A N   
2649 N N   B TYR A 336 ? 0.3895 0.4284 0.3584 0.1224  0.0279  -0.0281 376 TYR A N   
2650 C CA  A TYR A 336 ? 0.4096 0.4488 0.3757 0.1331  0.0259  -0.0301 376 TYR A CA  
2651 C CA  B TYR A 336 ? 0.4144 0.4510 0.3793 0.1329  0.0256  -0.0290 376 TYR A CA  
2652 C C   A TYR A 336 ? 0.4306 0.4499 0.3884 0.1351  0.0252  -0.0283 376 TYR A C   
2653 C C   B TYR A 336 ? 0.4306 0.4492 0.3883 0.1339  0.0255  -0.0283 376 TYR A C   
2654 O O   A TYR A 336 ? 0.4121 0.4156 0.3644 0.1312  0.0242  -0.0225 376 TYR A O   
2655 O O   B TYR A 336 ? 0.4170 0.4206 0.3703 0.1283  0.0252  -0.0235 376 TYR A O   
2656 C CB  A TYR A 336 ? 0.3976 0.4399 0.3613 0.1404  0.0222  -0.0278 376 TYR A CB  
2657 C CB  B TYR A 336 ? 0.3936 0.4260 0.3531 0.1382  0.0223  -0.0241 376 TYR A CB  
2658 C CG  A TYR A 336 ? 0.3727 0.4002 0.3279 0.1388  0.0212  -0.0201 376 TYR A CG  
2659 C CG  B TYR A 336 ? 0.3884 0.4365 0.3524 0.1370  0.0216  -0.0254 376 TYR A CG  
2660 C CD1 A TYR A 336 ? 0.3714 0.4026 0.3281 0.1318  0.0229  -0.0179 376 TYR A CD1 
2661 C CD1 B TYR A 336 ? 0.4346 0.4994 0.4036 0.1436  0.0188  -0.0301 376 TYR A CD1 
2662 C CD2 A TYR A 336 ? 0.4279 0.4384 0.3738 0.1446  0.0187  -0.0150 376 TYR A CD2 
2663 C CD2 B TYR A 336 ? 0.3749 0.4219 0.3388 0.1296  0.0232  -0.0228 376 TYR A CD2 
2664 C CE1 A TYR A 336 ? 0.3500 0.3711 0.2996 0.1303  0.0234  -0.0108 376 TYR A CE1 
2665 C CE1 B TYR A 336 ? 0.4385 0.5168 0.4109 0.1421  0.0170  -0.0323 376 TYR A CE1 
2666 C CE2 A TYR A 336 ? 0.3833 0.3818 0.3216 0.1418  0.0187  -0.0069 376 TYR A CE2 
2667 C CE2 B TYR A 336 ? 0.4182 0.4779 0.3848 0.1291  0.0222  -0.0254 376 TYR A CE2 
2668 C CZ  A TYR A 336 ? 0.3590 0.3644 0.2996 0.1346  0.0216  -0.0048 376 TYR A CZ  
2669 C CZ  B TYR A 336 ? 0.4439 0.5185 0.4141 0.1349  0.0187  -0.0302 376 TYR A CZ  
2670 O OH  A TYR A 336 ? 0.4242 0.4205 0.3579 0.1316  0.0229  0.0032  376 TYR A OH  
2671 O OH  B TYR A 336 ? 0.4640 0.5506 0.4364 0.1341  0.0165  -0.0337 376 TYR A OH  
2672 N N   . SER A 337 ? 0.4164 0.4374 0.3738 0.1411  0.0258  -0.0337 377 SER A N   
2673 C CA  . SER A 337 ? 0.4493 0.4526 0.3987 0.1425  0.0253  -0.0348 377 SER A CA  
2674 C C   . SER A 337 ? 0.4750 0.4718 0.4203 0.1558  0.0223  -0.0377 377 SER A C   
2675 O O   . SER A 337 ? 0.5003 0.5132 0.4517 0.1643  0.0219  -0.0415 377 SER A O   
2676 C CB  . SER A 337 ? 0.4599 0.4699 0.4102 0.1375  0.0294  -0.0400 377 SER A CB  
2677 O OG  . SER A 337 ? 0.5235 0.5148 0.4643 0.1378  0.0281  -0.0414 377 SER A OG  
2678 N N   . LEU A 338 ? 0.4620 0.4346 0.3979 0.1575  0.0193  -0.0360 378 LEU A N   
2679 C CA  . LEU A 338 ? 0.4986 0.4593 0.4289 0.1704  0.0158  -0.0397 378 LEU A CA  
2680 C C   . LEU A 338 ? 0.5084 0.4628 0.4340 0.1707  0.0178  -0.0475 378 LEU A C   
2681 O O   . LEU A 338 ? 0.4790 0.4145 0.3974 0.1635  0.0163  -0.0458 378 LEU A O   
2682 C CB  . LEU A 338 ? 0.5201 0.4545 0.4416 0.1717  0.0103  -0.0318 378 LEU A CB  
2683 C CG  . LEU A 338 ? 0.6626 0.5995 0.5849 0.1673  0.0095  -0.0221 378 LEU A CG  
2684 C CD1 . LEU A 338 ? 0.7306 0.6404 0.6426 0.1687  0.0046  -0.0136 378 LEU A CD1 
2685 C CD2 . LEU A 338 ? 0.5675 0.5278 0.4965 0.1749  0.0093  -0.0240 378 LEU A CD2 
2686 N N   . GLU A 339 ? 0.4416 0.4136 0.3716 0.1788  0.0212  -0.0562 379 GLU A N   
2687 C CA  . GLU A 339 ? 0.4608 0.4304 0.3848 0.1793  0.0244  -0.0644 379 GLU A CA  
2688 C C   . GLU A 339 ? 0.5254 0.4644 0.4370 0.1854  0.0189  -0.0668 379 GLU A C   
2689 O O   . GLU A 339 ? 0.4978 0.4263 0.4079 0.1977  0.0144  -0.0679 379 GLU A O   
2690 C CB  . GLU A 339 ? 0.4775 0.4733 0.4091 0.1886  0.0297  -0.0734 379 GLU A CB  
2691 C CG  . GLU A 339 ? 0.5006 0.4957 0.4240 0.1896  0.0343  -0.0823 379 GLU A CG  
2692 C CD  . GLU A 339 ? 0.6375 0.6563 0.5677 0.2020  0.0398  -0.0923 379 GLU A CD  
2693 O OE1 . GLU A 339 ? 0.6446 0.6715 0.5835 0.2143  0.0371  -0.0941 379 GLU A OE1 
2694 O OE2 . GLU A 339 ? 0.6715 0.7016 0.5979 0.1998  0.0468  -0.0985 379 GLU A OE2 
2695 N N   . GLY A 340 ? 0.5353 0.4591 0.4378 0.1769  0.0184  -0.0678 380 GLY A N   
2696 C CA  . GLY A 340 ? 0.5467 0.4396 0.4373 0.1801  0.0123  -0.0705 380 GLY A CA  
2697 C C   . GLY A 340 ? 0.5648 0.4351 0.4530 0.1697  0.0066  -0.0605 380 GLY A C   
2698 O O   . GLY A 340 ? 0.5928 0.4368 0.4718 0.1678  0.0012  -0.0621 380 GLY A O   
2699 N N   . TYR A 341 ? 0.5343 0.4148 0.4309 0.1626  0.0077  -0.0507 381 TYR A N   
2700 C CA  . TYR A 341 ? 0.5472 0.4103 0.4432 0.1530  0.0036  -0.0405 381 TYR A CA  
2701 C C   . TYR A 341 ? 0.5206 0.3971 0.4234 0.1389  0.0067  -0.0352 381 TYR A C   
2702 O O   . TYR A 341 ? 0.5522 0.4174 0.4527 0.1293  0.0042  -0.0342 381 TYR A O   
2703 C CB  . TYR A 341 ? 0.5310 0.3905 0.4284 0.1592  0.0016  -0.0330 381 TYR A CB  
2704 C CG  . TYR A 341 ? 0.6389 0.4838 0.5358 0.1488  -0.0008 -0.0215 381 TYR A CG  
2705 C CD1 . TYR A 341 ? 0.7405 0.5560 0.6303 0.1447  -0.0062 -0.0190 381 TYR A CD1 
2706 C CD2 . TYR A 341 ? 0.6489 0.5101 0.5526 0.1426  0.0026  -0.0136 381 TYR A CD2 
2707 C CE1 . TYR A 341 ? 0.8283 0.6329 0.7190 0.1338  -0.0074 -0.0078 381 TYR A CE1 
2708 C CE2 . TYR A 341 ? 0.7307 0.5817 0.6343 0.1332  0.0019  -0.0031 381 TYR A CE2 
2709 C CZ  . TYR A 341 ? 0.8727 0.6965 0.7705 0.1284  -0.0027 0.0002  381 TYR A CZ  
2710 O OH  . TYR A 341 ? 0.9911 0.8073 0.8902 0.1177  -0.0024 0.0112  381 TYR A OH  
2711 N N   . GLY A 342 ? 0.4989 0.3987 0.4105 0.1377  0.0111  -0.0324 382 GLY A N   
2712 C CA  . GLY A 342 ? 0.5138 0.4244 0.4321 0.1258  0.0134  -0.0277 382 GLY A CA  
2713 C C   . GLY A 342 ? 0.4895 0.4232 0.4164 0.1267  0.0175  -0.0257 382 GLY A C   
2714 O O   . GLY A 342 ? 0.4822 0.4260 0.4105 0.1360  0.0184  -0.0286 382 GLY A O   
2715 N N   . THR A 343 ? 0.4613 0.4030 0.3944 0.1174  0.0191  -0.0212 383 THR A N   
2716 C CA  . THR A 343 ? 0.4655 0.4283 0.4065 0.1165  0.0226  -0.0212 383 THR A CA  
2717 C C   . THR A 343 ? 0.4563 0.4212 0.4020 0.1107  0.0229  -0.0143 383 THR A C   
2718 O O   . THR A 343 ? 0.4271 0.3827 0.3734 0.1037  0.0218  -0.0102 383 THR A O   
2719 C CB  . THR A 343 ? 0.4465 0.4198 0.3899 0.1114  0.0251  -0.0254 383 THR A CB  
2720 O OG1 . THR A 343 ? 0.4334 0.4071 0.3716 0.1170  0.0261  -0.0321 383 THR A OG1 
2721 C CG2 . THR A 343 ? 0.4530 0.4456 0.4049 0.1092  0.0280  -0.0256 383 THR A CG2 
2722 N N   . ASP A 344 ? 0.4176 0.3957 0.3668 0.1140  0.0244  -0.0136 384 ASP A N   
2723 C CA  . ASP A 344 ? 0.4031 0.3874 0.3565 0.1096  0.0259  -0.0091 384 ASP A CA  
2724 C C   . ASP A 344 ? 0.4122 0.4128 0.3730 0.1066  0.0278  -0.0131 384 ASP A C   
2725 O O   . ASP A 344 ? 0.4318 0.4431 0.3946 0.1101  0.0282  -0.0181 384 ASP A O   
2726 C CB  . ASP A 344 ? 0.4434 0.4288 0.3924 0.1156  0.0255  -0.0052 384 ASP A CB  
2727 C CG  . ASP A 344 ? 0.5650 0.5319 0.5061 0.1170  0.0235  0.0011  384 ASP A CG  
2728 O OD1 . ASP A 344 ? 0.5662 0.5204 0.5073 0.1110  0.0228  0.0032  384 ASP A OD1 
2729 O OD2 . ASP A 344 ? 0.6486 0.6131 0.5833 0.1238  0.0220  0.0043  384 ASP A OD2 
2730 N N   . ALA A 345 ? 0.3776 0.3801 0.3433 0.1002  0.0288  -0.0110 385 ALA A N   
2731 C CA  . ALA A 345 ? 0.3888 0.4037 0.3610 0.0978  0.0300  -0.0141 385 ALA A CA  
2732 C C   . ALA A 345 ? 0.4732 0.4924 0.4465 0.0984  0.0313  -0.0116 385 ALA A C   
2733 O O   . ALA A 345 ? 0.4337 0.4468 0.4062 0.0964  0.0322  -0.0065 385 ALA A O   
2734 C CB  . ALA A 345 ? 0.3816 0.3942 0.3581 0.0910  0.0296  -0.0148 385 ALA A CB  
2735 N N   . VAL A 346 ? 0.4119 0.4423 0.3869 0.1008  0.0314  -0.0153 386 VAL A N   
2736 C CA  . VAL A 346 ? 0.4023 0.4379 0.3762 0.1023  0.0329  -0.0144 386 VAL A CA  
2737 C C   . VAL A 346 ? 0.3921 0.4353 0.3727 0.0998  0.0327  -0.0199 386 VAL A C   
2738 O O   . VAL A 346 ? 0.3838 0.4330 0.3670 0.0998  0.0308  -0.0251 386 VAL A O   
2739 C CB  . VAL A 346 ? 0.4347 0.4747 0.4006 0.1093  0.0320  -0.0139 386 VAL A CB  
2740 C CG1 . VAL A 346 ? 0.4177 0.4629 0.3796 0.1106  0.0342  -0.0128 386 VAL A CG1 
2741 C CG2 . VAL A 346 ? 0.4321 0.4612 0.3907 0.1124  0.0312  -0.0082 386 VAL A CG2 
2742 N N   . ILE A 347 ? 0.3596 0.4022 0.3440 0.0975  0.0345  -0.0190 387 ILE A N   
2743 C CA  . ILE A 347 ? 0.3394 0.3870 0.3291 0.0969  0.0341  -0.0246 387 ILE A CA  
2744 C C   . ILE A 347 ? 0.3661 0.4216 0.3501 0.1020  0.0357  -0.0268 387 ILE A C   
2745 O O   . ILE A 347 ? 0.3946 0.4509 0.3740 0.1038  0.0392  -0.0221 387 ILE A O   
2746 C CB  . ILE A 347 ? 0.3416 0.3854 0.3391 0.0936  0.0347  -0.0232 387 ILE A CB  
2747 C CG1 . ILE A 347 ? 0.4219 0.4574 0.4226 0.0887  0.0322  -0.0208 387 ILE A CG1 
2748 C CG2 . ILE A 347 ? 0.3199 0.3671 0.3223 0.0948  0.0339  -0.0296 387 ILE A CG2 
2749 C CD1 . ILE A 347 ? 0.3894 0.4215 0.3976 0.0861  0.0316  -0.0182 387 ILE A CD1 
2750 N N   . TYR A 348 ? 0.3641 0.4252 0.3477 0.1036  0.0332  -0.0338 388 TYR A N   
2751 C CA  . TYR A 348 ? 0.3536 0.4220 0.3308 0.1085  0.0338  -0.0380 388 TYR A CA  
2752 C C   . TYR A 348 ? 0.3958 0.4643 0.3789 0.1078  0.0333  -0.0451 388 TYR A C   
2753 O O   . TYR A 348 ? 0.4291 0.4941 0.4189 0.1041  0.0295  -0.0496 388 TYR A O   
2754 C CB  . TYR A 348 ? 0.3792 0.4542 0.3506 0.1116  0.0297  -0.0420 388 TYR A CB  
2755 C CG  . TYR A 348 ? 0.4031 0.4776 0.3692 0.1141  0.0290  -0.0361 388 TYR A CG  
2756 C CD1 . TYR A 348 ? 0.4364 0.5083 0.4085 0.1115  0.0274  -0.0350 388 TYR A CD1 
2757 C CD2 . TYR A 348 ? 0.4519 0.5281 0.4059 0.1198  0.0298  -0.0317 388 TYR A CD2 
2758 C CE1 . TYR A 348 ? 0.4594 0.5304 0.4269 0.1154  0.0263  -0.0308 388 TYR A CE1 
2759 C CE2 . TYR A 348 ? 0.5125 0.5858 0.4613 0.1232  0.0280  -0.0263 388 TYR A CE2 
2760 C CZ  . TYR A 348 ? 0.5368 0.6074 0.4929 0.1215  0.0261  -0.0265 388 TYR A CZ  
2761 O OH  . TYR A 348 ? 0.5640 0.6312 0.5154 0.1264  0.0241  -0.0224 388 TYR A OH  
2762 N N   . ILE A 349 ? 0.3441 0.4164 0.3246 0.1115  0.0373  -0.0461 389 ILE A N   
2763 C CA  . ILE A 349 ? 0.3876 0.4602 0.3728 0.1133  0.0370  -0.0541 389 ILE A CA  
2764 C C   . ILE A 349 ? 0.4174 0.4987 0.3916 0.1197  0.0392  -0.0596 389 ILE A C   
2765 O O   . ILE A 349 ? 0.4297 0.5169 0.3943 0.1223  0.0437  -0.0540 389 ILE A O   
2766 C CB  . ILE A 349 ? 0.3797 0.4501 0.3749 0.1124  0.0403  -0.0509 389 ILE A CB  
2767 C CG1 . ILE A 349 ? 0.4026 0.4630 0.4071 0.1063  0.0363  -0.0475 389 ILE A CG1 
2768 C CG2 . ILE A 349 ? 0.3605 0.4338 0.3592 0.1175  0.0416  -0.0593 389 ILE A CG2 
2769 C CD1 . ILE A 349 ? 0.3907 0.4496 0.4045 0.1050  0.0382  -0.0426 389 ILE A CD1 
2770 N N   . LYS A 350 ? 0.4509 0.5318 0.4249 0.1220  0.0357  -0.0704 390 LYS A N   
2771 C CA  . LYS A 350 ? 0.4431 0.5318 0.4051 0.1288  0.0375  -0.0774 390 LYS A CA  
2772 C C   . LYS A 350 ? 0.4471 0.5420 0.4094 0.1331  0.0459  -0.0760 390 LYS A C   
2773 O O   . LYS A 350 ? 0.4468 0.5386 0.4212 0.1334  0.0469  -0.0785 390 LYS A O   
2774 C CB  . LYS A 350 ? 0.4056 0.4905 0.3681 0.1299  0.0310  -0.0907 390 LYS A CB  
2775 C CG  . LYS A 350 ? 0.4673 0.5501 0.4303 0.1251  0.0230  -0.0930 390 LYS A CG  
2776 C CD  . LYS A 350 ? 0.4826 0.5752 0.4316 0.1286  0.0218  -0.0918 390 LYS A CD  
2777 C CE  . LYS A 350 ? 0.5446 0.6387 0.4959 0.1250  0.0129  -0.0977 390 LYS A CE  
2778 N NZ  . LYS A 350 ? 0.5753 0.6798 0.5134 0.1296  0.0101  -0.0971 390 LYS A NZ  
2779 N N   . ALA A 351 ? 0.4527 0.4687 0.4460 0.0539  0.1053  -0.0392 391 ALA A N   
2780 C CA  . ALA A 351 ? 0.4961 0.5164 0.5103 0.0555  0.1184  -0.0270 391 ALA A CA  
2781 C C   . ALA A 351 ? 0.5229 0.5465 0.5355 0.0641  0.1297  -0.0282 391 ALA A C   
2782 O O   . ALA A 351 ? 0.5281 0.5577 0.5650 0.0647  0.1399  -0.0186 391 ALA A O   
2783 C CB  . ALA A 351 ? 0.4728 0.4881 0.4792 0.0596  0.1279  -0.0178 391 ALA A CB  
2784 N N   . LEU A 352 ? 0.5106 0.5294 0.4956 0.0710  0.1280  -0.0392 392 LEU A N   
2785 C CA  . LEU A 352 ? 0.5564 0.5735 0.5320 0.0806  0.1385  -0.0415 392 LEU A CA  
2786 C C   . LEU A 352 ? 0.5186 0.5397 0.4990 0.0773  0.1280  -0.0514 392 LEU A C   
2787 O O   . LEU A 352 ? 0.4799 0.5000 0.4494 0.0729  0.1135  -0.0610 392 LEU A O   
2788 C CB  . LEU A 352 ? 0.6166 0.6210 0.5534 0.0916  0.1437  -0.0460 392 LEU A CB  
2789 C CG  . LEU A 352 ? 0.6427 0.6412 0.5698 0.0954  0.1533  -0.0369 392 LEU A CG  
2790 C CD1 . LEU A 352 ? 0.7341 0.7172 0.6205 0.1068  0.1581  -0.0414 392 LEU A CD1 
2791 C CD2 . LEU A 352 ? 0.6551 0.6593 0.6086 0.0962  0.1696  -0.0225 392 LEU A CD2 
2792 N N   . SER A 353 ? 0.5082 0.5340 0.5058 0.0796  0.1358  -0.0484 393 SER A N   
2793 C CA  . SER A 353 ? 0.5605 0.5901 0.5649 0.0762  0.1260  -0.0570 393 SER A CA  
2794 C C   . SER A 353 ? 0.5306 0.5511 0.5010 0.0825  0.1203  -0.0695 393 SER A C   
2795 O O   . SER A 353 ? 0.5775 0.6002 0.5479 0.0774  0.1068  -0.0784 393 SER A O   
2796 C CB  . SER A 353 ? 0.5650 0.6006 0.5945 0.0790  0.1371  -0.0503 393 SER A CB  
2797 O OG  . SER A 353 ? 0.6306 0.6590 0.6442 0.0925  0.1558  -0.0464 393 SER A OG  
2798 N N   . THR A 354 ? 0.5315 0.5405 0.4723 0.0934  0.1295  -0.0698 394 THR A N   
2799 C CA  . THR A 354 ? 0.6258 0.6235 0.5332 0.0992  0.1222  -0.0809 394 THR A CA  
2800 C C   . THR A 354 ? 0.6779 0.6758 0.5746 0.0931  0.1057  -0.0873 394 THR A C   
2801 O O   . THR A 354 ? 0.7316 0.7245 0.6111 0.0940  0.0944  -0.0966 394 THR A O   
2802 C CB  . THR A 354 ? 0.6870 0.6685 0.5628 0.1126  0.1360  -0.0788 394 THR A CB  
2803 O OG1 . THR A 354 ? 0.7574 0.7357 0.6242 0.1134  0.1397  -0.0729 394 THR A OG1 
2804 C CG2 . THR A 354 ? 0.7092 0.6907 0.5973 0.1198  0.1552  -0.0710 394 THR A CG2 
2805 N N   . ASP A 355 ? 0.6076 0.6106 0.5150 0.0871  0.1039  -0.0821 395 ASP A N   
2806 C CA  . ASP A 355 ? 0.5766 0.5809 0.4785 0.0813  0.0896  -0.0872 395 ASP A CA  
2807 C C   . ASP A 355 ? 0.5533 0.5675 0.4776 0.0705  0.0782  -0.0906 395 ASP A C   
2808 O O   . ASP A 355 ? 0.5426 0.5579 0.4628 0.0663  0.0671  -0.0952 395 ASP A O   
2809 C CB  . ASP A 355 ? 0.6010 0.6036 0.5010 0.0807  0.0930  -0.0804 395 ASP A CB  
2810 C CG  . ASP A 355 ? 0.7279 0.7185 0.6004 0.0909  0.1017  -0.0778 395 ASP A CG  
2811 O OD1 . ASP A 355 ? 0.7433 0.7244 0.5925 0.0983  0.1015  -0.0832 395 ASP A OD1 
2812 O OD2 . ASP A 355 ? 0.7342 0.7230 0.6068 0.0914  0.1079  -0.0704 395 ASP A OD2 
2813 N N   . SER A 356 ? 0.5618 0.5824 0.5097 0.0662  0.0808  -0.0878 396 SER A N   
2814 C CA  . SER A 356 ? 0.5700 0.5973 0.5380 0.0554  0.0699  -0.0901 396 SER A CA  
2815 C C   . SER A 356 ? 0.5939 0.6225 0.5583 0.0550  0.0618  -0.0992 396 SER A C   
2816 O O   . SER A 356 ? 0.6922 0.7234 0.6683 0.0554  0.0645  -0.0992 396 SER A O   
2817 C CB  . SER A 356 ? 0.5922 0.6245 0.5890 0.0497  0.0745  -0.0814 396 SER A CB  
2818 O OG  . SER A 356 ? 0.6383 0.6688 0.6386 0.0511  0.0833  -0.0718 396 SER A OG  
2819 N N   . ILE A 357 ? 0.5642 0.5913 0.5141 0.0542  0.0515  -0.1064 397 ILE A N   
2820 C CA  . ILE A 357 ? 0.5235 0.5514 0.4686 0.0537  0.0423  -0.1147 397 ILE A CA  
2821 C C   . ILE A 357 ? 0.4783 0.5113 0.4353 0.0438  0.0312  -0.1177 397 ILE A C   
2822 O O   . ILE A 357 ? 0.5021 0.5349 0.4581 0.0406  0.0286  -0.1161 397 ILE A O   
2823 C CB  . ILE A 357 ? 0.5838 0.6046 0.5026 0.0611  0.0388  -0.1195 397 ILE A CB  
2824 C CG1 . ILE A 357 ? 0.7296 0.7411 0.6316 0.0716  0.0506  -0.1165 397 ILE A CG1 
2825 C CG2 . ILE A 357 ? 0.5424 0.5635 0.4574 0.0597  0.0274  -0.1274 397 ILE A CG2 
2826 C CD1 . ILE A 357 ? 0.7826 0.7834 0.6558 0.0786  0.0469  -0.1194 397 ILE A CD1 
2827 N N   . GLU A 358 ? 0.4517 0.4878 0.4188 0.0394  0.0252  -0.1217 398 GLU A N   
2828 C CA  . GLU A 358 ? 0.4592 0.4982 0.4347 0.0305  0.0150  -0.1248 398 GLU A CA  
2829 C C   . GLU A 358 ? 0.4258 0.4647 0.3884 0.0312  0.0089  -0.1281 398 GLU A C   
2830 O O   . GLU A 358 ? 0.4827 0.5205 0.4317 0.0371  0.0067  -0.1311 398 GLU A O   
2831 C CB  . GLU A 358 ? 0.4398 0.4811 0.4228 0.0273  0.0086  -0.1298 398 GLU A CB  
2832 C CG  . GLU A 358 ? 0.4487 0.4916 0.4506 0.0242  0.0118  -0.1265 398 GLU A CG  
2833 C CD  . GLU A 358 ? 0.4625 0.5071 0.4705 0.0206  0.0036  -0.1321 398 GLU A CD  
2834 O OE1 . GLU A 358 ? 0.4555 0.4987 0.4528 0.0267  0.0030  -0.1368 398 GLU A OE1 
2835 O OE2 . GLU A 358 ? 0.4722 0.5175 0.4933 0.0117  -0.0032 -0.1319 398 GLU A OE2 
2836 N N   . ARG A 359 ? 0.4230 0.4618 0.3902 0.0253  0.0058  -0.1269 399 ARG A N   
2837 C CA  . ARG A 359 ? 0.4245 0.4645 0.3845 0.0255  0.0009  -0.1289 399 ARG A CA  
2838 C C   . ARG A 359 ? 0.4091 0.4514 0.3766 0.0186  -0.0068 -0.1325 399 ARG A C   
2839 O O   . ARG A 359 ? 0.4379 0.4764 0.4122 0.0120  -0.0075 -0.1313 399 ARG A O   
2840 C CB  . ARG A 359 ? 0.4266 0.4625 0.3835 0.0256  0.0052  -0.1243 399 ARG A CB  
2841 C CG  . ARG A 359 ? 0.5490 0.5859 0.5025 0.0253  0.0017  -0.1252 399 ARG A CG  
2842 C CD  . ARG A 359 ? 0.6573 0.6891 0.6049 0.0280  0.0071  -0.1207 399 ARG A CD  
2843 N NE  . ARG A 359 ? 0.7639 0.7954 0.7102 0.0278  0.0056  -0.1206 399 ARG A NE  
2844 C CZ  . ARG A 359 ? 0.8400 0.8777 0.7851 0.0323  0.0031  -0.1209 399 ARG A CZ  
2845 N NH1 . ARG A 359 ? 0.8409 0.8830 0.7824 0.0369  0.0000  -0.1219 399 ARG A NH1 
2846 N NH2 . ARG A 359 ? 0.7694 0.8074 0.7164 0.0326  0.0036  -0.1195 399 ARG A NH2 
2847 N N   . LEU A 360 ? 0.3934 0.4400 0.3588 0.0198  -0.0135 -0.1367 400 LEU A N   
2848 C CA  . LEU A 360 ? 0.3988 0.4479 0.3720 0.0133  -0.0206 -0.1400 400 LEU A CA  
2849 C C   . LEU A 360 ? 0.4061 0.4596 0.3787 0.0131  -0.0257 -0.1405 400 LEU A C   
2850 O O   . LEU A 360 ? 0.4450 0.5013 0.4121 0.0184  -0.0281 -0.1403 400 LEU A O   
2851 C CB  . LEU A 360 ? 0.3980 0.4483 0.3730 0.0138  -0.0250 -0.1440 400 LEU A CB  
2852 C CG  . LEU A 360 ? 0.4302 0.4776 0.4080 0.0159  -0.0189 -0.1428 400 LEU A CG  
2853 C CD1 . LEU A 360 ? 0.4725 0.5198 0.4498 0.0179  -0.0228 -0.1473 400 LEU A CD1 
2854 C CD2 . LEU A 360 ? 0.3779 0.4232 0.3680 0.0088  -0.0170 -0.1397 400 LEU A CD2 
2855 N N   . PRO A 361 ? 0.4486 0.5018 0.4268 0.0071  -0.0276 -0.1404 401 PRO A N   
2856 C CA  . PRO A 361 ? 0.3918 0.4507 0.3732 0.0068  -0.0316 -0.1398 401 PRO A CA  
2857 C C   . PRO A 361 ? 0.4428 0.5073 0.4289 0.0053  -0.0411 -0.1433 401 PRO A C   
2858 O O   . PRO A 361 ? 0.4260 0.4886 0.4135 0.0024  -0.0444 -0.1468 401 PRO A O   
2859 C CB  . PRO A 361 ? 0.4350 0.4886 0.4182 0.0012  -0.0286 -0.1384 401 PRO A CB  
2860 C CG  . PRO A 361 ? 0.4689 0.5152 0.4524 -0.0042 -0.0294 -0.1404 401 PRO A CG  
2861 C CD  . PRO A 361 ? 0.4448 0.4912 0.4266 0.0001  -0.0266 -0.1403 401 PRO A CD  
2862 N N   . VAL A 362 ? 0.3886 0.4596 0.3781 0.0073  -0.0462 -0.1417 402 VAL A N   
2863 C CA  . VAL A 362 ? 0.3846 0.4597 0.3784 0.0056  -0.0572 -0.1442 402 VAL A CA  
2864 C C   . VAL A 362 ? 0.4483 0.5311 0.4543 0.0024  -0.0605 -0.1404 402 VAL A C   
2865 O O   . VAL A 362 ? 0.4117 0.4984 0.4217 0.0054  -0.0561 -0.1353 402 VAL A O   
2866 C CB  . VAL A 362 ? 0.4307 0.5041 0.4154 0.0119  -0.0631 -0.1453 402 VAL A CB  
2867 C CG1 . VAL A 362 ? 0.5022 0.5774 0.4848 0.0173  -0.0602 -0.1405 402 VAL A CG1 
2868 C CG2 . VAL A 362 ? 0.3942 0.4697 0.3825 0.0099  -0.0767 -0.1472 402 VAL A CG2 
2869 N N   . TYR A 363 ? 0.4354 0.5204 0.4486 -0.0033 -0.0674 -0.1423 403 TYR A N   
2870 C CA  . TYR A 363 ? 0.4424 0.5353 0.4692 -0.0066 -0.0700 -0.1378 403 TYR A CA  
2871 C C   . TYR A 363 ? 0.4362 0.5359 0.4702 -0.0047 -0.0818 -0.1355 403 TYR A C   
2872 O O   . TYR A 363 ? 0.4165 0.5130 0.4460 -0.0054 -0.0925 -0.1398 403 TYR A O   
2873 C CB  . TYR A 363 ? 0.4124 0.5039 0.4437 -0.0142 -0.0725 -0.1399 403 TYR A CB  
2874 C CG  . TYR A 363 ? 0.4264 0.5260 0.4722 -0.0173 -0.0737 -0.1341 403 TYR A CG  
2875 C CD1 . TYR A 363 ? 0.3962 0.4963 0.4448 -0.0160 -0.0622 -0.1285 403 TYR A CD1 
2876 C CD2 . TYR A 363 ? 0.4133 0.5193 0.4701 -0.0209 -0.0859 -0.1335 403 TYR A CD2 
2877 C CE1 . TYR A 363 ? 0.4461 0.5539 0.5092 -0.0179 -0.0608 -0.1219 403 TYR A CE1 
2878 C CE2 . TYR A 363 ? 0.4055 0.5202 0.4787 -0.0238 -0.0862 -0.1266 403 TYR A CE2 
2879 C CZ  . TYR A 363 ? 0.4347 0.5509 0.5116 -0.0220 -0.0727 -0.1205 403 TYR A CZ  
2880 O OH  . TYR A 363 ? 0.4628 0.5877 0.5570 -0.0238 -0.0704 -0.1125 403 TYR A OH  
2881 N N   . ASN A 364 ? 0.3913 0.4989 0.4364 -0.0022 -0.0805 -0.1285 404 ASN A N   
2882 C CA  . ASN A 364 ? 0.3742 0.4882 0.4297 -0.0013 -0.0935 -0.1245 404 ASN A CA  
2883 C C   . ASN A 364 ? 0.3938 0.5192 0.4692 -0.0004 -0.0886 -0.1147 404 ASN A C   
2884 O O   . ASN A 364 ? 0.4221 0.5483 0.4998 -0.0001 -0.0748 -0.1122 404 ASN A O   
2885 C CB  . ASN A 364 ? 0.3832 0.4903 0.4242 0.0047  -0.0993 -0.1268 404 ASN A CB  
2886 C CG  . ASN A 364 ? 0.4444 0.5491 0.4774 0.0107  -0.0870 -0.1252 404 ASN A CG  
2887 O OD1 . ASN A 364 ? 0.4402 0.5501 0.4820 0.0113  -0.0764 -0.1205 404 ASN A OD1 
2888 N ND2 . ASN A 364 ? 0.3913 0.4866 0.4060 0.0155  -0.0877 -0.1291 404 ASN A ND2 
2889 N N   . LYS A 365 ? 0.3648 0.4976 0.4544 0.0005  -0.1002 -0.1088 405 LYS A N   
2890 C CA  . LYS A 365 ? 0.4021 0.5476 0.5154 0.0021  -0.0961 -0.0978 405 LYS A CA  
2891 C C   . LYS A 365 ? 0.3877 0.5319 0.4960 0.0086  -0.0798 -0.0955 405 LYS A C   
2892 O O   . LYS A 365 ? 0.3889 0.5389 0.5095 0.0098  -0.0673 -0.0891 405 LYS A O   
2893 C CB  . LYS A 365 ? 0.4464 0.5975 0.5738 0.0026  -0.1134 -0.0918 405 LYS A CB  
2894 C CG  . LYS A 365 ? 0.5721 0.7375 0.7277 0.0052  -0.1099 -0.0790 405 LYS A CG  
2895 C CD  . LYS A 365 ? 0.5653 0.7435 0.7487 -0.0003 -0.1114 -0.0709 405 LYS A CD  
2896 C CE  . LYS A 365 ? 0.5326 0.7121 0.7259 -0.0061 -0.1349 -0.0694 405 LYS A CE  
2897 N NZ  . LYS A 365 ? 0.5631 0.7554 0.7845 -0.0122 -0.1366 -0.0610 405 LYS A NZ  
2898 N N   . ALA A 366 ? 0.3841 0.5193 0.4733 0.0132  -0.0792 -0.1003 406 ALA A N   
2899 C CA  . ALA A 366 ? 0.4301 0.5626 0.5133 0.0192  -0.0649 -0.0983 406 ALA A CA  
2900 C C   . ALA A 366 ? 0.4517 0.5785 0.5270 0.0176  -0.0494 -0.1008 406 ALA A C   
2901 O O   . ALA A 366 ? 0.4121 0.5400 0.4926 0.0211  -0.0367 -0.0954 406 ALA A O   
2902 C CB  . ALA A 366 ? 0.3872 0.5098 0.4495 0.0235  -0.0673 -0.1033 406 ALA A CB  
2903 N N   . ALA A 367 ? 0.4234 0.5421 0.4854 0.0127  -0.0507 -0.1086 407 ALA A N   
2904 C CA  . ALA A 367 ? 0.4169 0.5273 0.4699 0.0101  -0.0389 -0.1109 407 ALA A CA  
2905 C C   . ALA A 367 ? 0.4016 0.5174 0.4688 0.0079  -0.0332 -0.1049 407 ALA A C   
2906 O O   . ALA A 367 ? 0.3995 0.5090 0.4620 0.0102  -0.0197 -0.1021 407 ALA A O   
2907 C CB  . ALA A 367 ? 0.4445 0.5466 0.4849 0.0047  -0.0438 -0.1193 407 ALA A CB  
2908 N N   . TRP A 368 ? 0.3988 0.5246 0.4823 0.0037  -0.0431 -0.1024 408 TRP A N   
2909 C CA  . TRP A 368 ? 0.3887 0.5207 0.4879 0.0016  -0.0373 -0.0955 408 TRP A CA  
2910 C C   . TRP A 368 ? 0.4689 0.6078 0.5817 0.0087  -0.0260 -0.0856 408 TRP A C   
2911 O O   . TRP A 368 ? 0.4444 0.5797 0.5575 0.0103  -0.0117 -0.0811 408 TRP A O   
2912 C CB  . TRP A 368 ? 0.3605 0.5033 0.4776 -0.0041 -0.0521 -0.0934 408 TRP A CB  
2913 C CG  . TRP A 368 ? 0.3703 0.5201 0.5048 -0.0070 -0.0462 -0.0856 408 TRP A CG  
2914 C CD1 . TRP A 368 ? 0.3768 0.5200 0.5050 -0.0127 -0.0424 -0.0879 408 TRP A CD1 
2915 C CD2 . TRP A 368 ? 0.3934 0.5577 0.5553 -0.0040 -0.0425 -0.0732 408 TRP A CD2 
2916 N NE1 . TRP A 368 ? 0.3970 0.5490 0.5450 -0.0132 -0.0356 -0.0778 408 TRP A NE1 
2917 C CE2 . TRP A 368 ? 0.3746 0.5407 0.5453 -0.0077 -0.0351 -0.0682 408 TRP A CE2 
2918 C CE3 . TRP A 368 ? 0.3751 0.5511 0.5563 0.0016  -0.0450 -0.0650 408 TRP A CE3 
2919 C CZ2 . TRP A 368 ? 0.3915 0.5716 0.5909 -0.0057 -0.0286 -0.0548 408 TRP A CZ2 
2920 C CZ3 . TRP A 368 ? 0.3437 0.5343 0.5553 0.0033  -0.0399 -0.0516 408 TRP A CZ3 
2921 C CH2 . TRP A 368 ? 0.3600 0.5531 0.5812 -0.0001 -0.0309 -0.0463 408 TRP A CH2 
2922 N N   . LYS A 369 ? 0.4978 0.6445 0.6202 0.0135  -0.0319 -0.0820 409 LYS A N   
2923 C CA  . LYS A 369 ? 0.4916 0.6459 0.6298 0.0207  -0.0221 -0.0719 409 LYS A CA  
2924 C C   . LYS A 369 ? 0.5299 0.6709 0.6494 0.0263  -0.0039 -0.0733 409 LYS A C   
2925 O O   . LYS A 369 ? 0.5109 0.6539 0.6400 0.0316  0.0101  -0.0653 409 LYS A O   
2926 C CB  . LYS A 369 ? 0.4888 0.6506 0.6366 0.0244  -0.0338 -0.0690 409 LYS A CB  
2927 C CG  . LYS A 369 ? 0.5861 0.7629 0.7620 0.0214  -0.0496 -0.0613 409 LYS A CG  
2928 C CD  . LYS A 369 ? 0.7519 0.9335 0.9368 0.0265  -0.0587 -0.0563 409 LYS A CD  
2929 C CE  . LYS A 369 ? 0.8446 1.0348 1.0488 0.0221  -0.0810 -0.0516 409 LYS A CE  
2930 N NZ  . LYS A 369 ? 0.8271 1.0347 1.0695 0.0204  -0.0818 -0.0381 409 LYS A NZ  
2931 N N   . HIS A 370 ? 0.5705 0.6967 0.6634 0.0254  -0.0036 -0.0828 410 HIS A N   
2932 C CA  . HIS A 370 ? 0.5927 0.7034 0.6659 0.0298  0.0113  -0.0843 410 HIS A CA  
2933 C C   . HIS A 370 ? 0.5420 0.6435 0.6095 0.0286  0.0240  -0.0823 410 HIS A C   
2934 O O   . HIS A 370 ? 0.5609 0.6529 0.6208 0.0348  0.0389  -0.0785 410 HIS A O   
2935 C CB  . HIS A 370 ? 0.5985 0.6956 0.6473 0.0272  0.0075  -0.0940 410 HIS A CB  
2936 C CG  . HIS A 370 ? 0.6310 0.7271 0.6743 0.0329  0.0069  -0.0941 410 HIS A CG  
2937 N ND1 . HIS A 370 ? 0.6608 0.7465 0.6931 0.0389  0.0187  -0.0922 410 HIS A ND1 
2938 C CD2 . HIS A 370 ? 0.6952 0.7972 0.7402 0.0337  -0.0041 -0.0959 410 HIS A CD2 
2939 C CE1 . HIS A 370 ? 0.7160 0.8031 0.7457 0.0428  0.0148  -0.0925 410 HIS A CE1 
2940 N NE2 . HIS A 370 ? 0.7133 0.8098 0.7498 0.0398  0.0014  -0.0947 410 HIS A NE2 
2941 N N   . TYR A 371 ? 0.4562 0.5582 0.5251 0.0210  0.0184  -0.0849 411 TYR A N   
2942 C CA  . TYR A 371 ? 0.4648 0.5556 0.5253 0.0194  0.0298  -0.0831 411 TYR A CA  
2943 C C   . TYR A 371 ? 0.5826 0.6851 0.6659 0.0240  0.0401  -0.0715 411 TYR A C   
2944 O O   . TYR A 371 ? 0.6134 0.7042 0.6873 0.0257  0.0542  -0.0683 411 TYR A O   
2945 C CB  . TYR A 371 ? 0.4390 0.5263 0.4940 0.0096  0.0199  -0.0892 411 TYR A CB  
2946 C CG  . TYR A 371 ? 0.4939 0.5666 0.5261 0.0051  0.0131  -0.0995 411 TYR A CG  
2947 C CD1 . TYR A 371 ? 0.4943 0.5440 0.5012 0.0035  0.0202  -0.1032 411 TYR A CD1 
2948 C CD2 . TYR A 371 ? 0.4939 0.5744 0.5298 0.0027  -0.0005 -0.1049 411 TYR A CD2 
2949 C CE1 . TYR A 371 ? 0.5048 0.5423 0.4953 -0.0012 0.0131  -0.1110 411 TYR A CE1 
2950 C CE2 . TYR A 371 ? 0.4132 0.4818 0.4320 -0.0010 -0.0053 -0.1128 411 TYR A CE2 
2951 C CZ  . TYR A 371 ? 0.4644 0.5129 0.4629 -0.0031 0.0012  -0.1153 411 TYR A CZ  
2952 O OH  . TYR A 371 ? 0.4240 0.4617 0.4096 -0.0072 -0.0043 -0.1216 411 TYR A OH  
2953 N N   . ASN A 372 ? 0.6908 0.8150 0.8037 0.0262  0.0333  -0.0643 412 ASN A N   
2954 C CA  . ASN A 372 ? 0.7836 0.9228 0.9258 0.0295  0.0410  -0.0515 412 ASN A CA  
2955 C C   . ASN A 372 ? 0.9499 1.1000 1.1112 0.0390  0.0469  -0.0425 412 ASN A C   
2956 O O   . ASN A 372 ? 0.9756 1.1456 1.1710 0.0403  0.0439  -0.0315 412 ASN A O   
2957 C CB  . ASN A 372 ? 0.7021 0.8589 0.8694 0.0217  0.0251  -0.0486 412 ASN A CB  
2958 C CG  . ASN A 372 ? 0.8034 0.9503 0.9551 0.0128  0.0205  -0.0560 412 ASN A CG  
2959 O OD1 . ASN A 372 ? 0.7734 0.9132 0.9083 0.0073  0.0081  -0.0667 412 ASN A OD1 
2960 N ND2 . ASN A 372 ? 0.8548 1.0006 1.0119 0.0116  0.0313  -0.0497 412 ASN A ND2 
2961 N N   . THR A 373 ? 1.0749 1.2119 1.2159 0.0453  0.0545  -0.0462 413 THR A N   
2962 C CA  . THR A 373 ? 1.2097 1.3554 1.3672 0.0546  0.0600  -0.0381 413 THR A CA  
2963 C C   . THR A 373 ? 1.3194 1.4443 1.4503 0.0627  0.0776  -0.0402 413 THR A C   
2964 O O   . THR A 373 ? 1.3513 1.4553 1.4491 0.0598  0.0787  -0.0503 413 THR A O   
2965 C CB  . THR A 373 ? 1.2009 1.3563 1.3656 0.0532  0.0413  -0.0409 413 THR A CB  
2966 O OG1 . THR A 373 ? 1.1729 1.3401 1.3513 0.0446  0.0228  -0.0423 413 THR A OG1 
2967 C CG2 . THR A 373 ? 1.2324 1.4015 1.4236 0.0616  0.0437  -0.0297 413 THR A CG2 
2968 N N   . ASN A 374 ? 1.3711 1.5012 1.5177 0.0729  0.0909  -0.0300 414 ASN A N   
2969 C CA  . ASN A 374 ? 1.4022 1.5129 1.5255 0.0820  0.1063  -0.0312 414 ASN A CA  
2970 C C   . ASN A 374 ? 1.4645 1.5776 1.5859 0.0841  0.0959  -0.0345 414 ASN A C   
2971 O O   . ASN A 374 ? 1.4512 1.5846 1.6012 0.0850  0.0856  -0.0284 414 ASN A O   
2972 C CB  . ASN A 374 ? 1.3677 1.4813 1.5082 0.0931  0.1274  -0.0183 414 ASN A CB  
2973 C CG  . ASN A 374 ? 1.3291 1.4712 1.5151 0.0972  0.1226  -0.0057 414 ASN A CG  
2974 O OD1 . ASN A 374 ? 1.3299 1.4745 1.5227 0.1047  0.1240  -0.0022 414 ASN A OD1 
2975 N ND2 . ASN A 374 ? 1.3015 1.4645 1.5196 0.0919  0.1155  0.0018  414 ASN A ND2 
2976 N N   . HIS A 375 ? 1.5557 1.6470 1.6433 0.0846  0.0978  -0.0436 415 HIS A N   
2977 C CA  . HIS A 375 ? 1.6629 1.7536 1.7441 0.0860  0.0886  -0.0474 415 HIS A CA  
2978 C C   . HIS A 375 ? 1.7278 1.8052 1.7989 0.0971  0.1040  -0.0436 415 HIS A C   
2979 O O   . HIS A 375 ? 1.7722 1.8247 1.8121 0.0987  0.1136  -0.0488 415 HIS A O   
2980 C CB  . HIS A 375 ? 1.7007 1.7781 1.7543 0.0776  0.0778  -0.0597 415 HIS A CB  
2981 C CG  . HIS A 375 ? 1.7125 1.8013 1.7744 0.0676  0.0629  -0.0638 415 HIS A CG  
2982 N ND1 . HIS A 375 ? 1.7010 1.8039 1.7751 0.0643  0.0465  -0.0652 415 HIS A ND1 
2983 C CD2 . HIS A 375 ? 1.7135 1.7994 1.7712 0.0605  0.0618  -0.0671 415 HIS A CD2 
2984 C CE1 . HIS A 375 ? 1.6894 1.7977 1.7666 0.0560  0.0362  -0.0692 415 HIS A CE1 
2985 N NE2 . HIS A 375 ? 1.6971 1.7963 1.7659 0.0533  0.0451  -0.0703 415 HIS A NE2 
2986 N N   . GLU A 376 ? 1.6986 1.7913 1.7958 0.1046  0.1052  -0.0343 416 GLU A N   
2987 C CA  . GLU A 376 ? 1.6615 1.7438 1.7537 0.1163  0.1201  -0.0294 416 GLU A CA  
2988 C C   . GLU A 376 ? 1.5627 1.6590 1.6739 0.1201  0.1104  -0.0249 416 GLU A C   
2989 O O   . GLU A 376 ? 1.5670 1.6856 1.7076 0.1169  0.0970  -0.0199 416 GLU A O   
2990 C CB  . GLU A 376 ? 1.7019 1.7864 1.8103 0.1251  0.1400  -0.0186 416 GLU A CB  
2991 C CG  . GLU A 376 ? 1.7225 1.7911 1.8105 0.1221  0.1508  -0.0220 416 GLU A CG  
2992 C CD  . GLU A 376 ? 1.7520 1.8273 1.8614 0.1302  0.1697  -0.0097 416 GLU A CD  
2993 O OE1 . GLU A 376 ? 1.7798 1.8426 1.8831 0.1424  0.1886  -0.0042 416 GLU A OE1 
2994 O OE2 . GLU A 376 ? 1.7496 1.8425 1.8828 0.1247  0.1660  -0.0051 416 GLU A OE2 
2995 N N   . ALA A 377 ? 1.3475 1.4286 1.4408 0.1270  0.1166  -0.0263 417 ALA A N   
2996 C CA  . ALA A 377 ? 1.1003 1.1902 1.2055 0.1306  0.1073  -0.0231 417 ALA A CA  
2997 C C   . ALA A 377 ? 0.9177 1.0192 1.0535 0.1420  0.1182  -0.0096 417 ALA A C   
2998 O O   . ALA A 377 ? 0.8421 0.9313 0.9693 0.1518  0.1306  -0.0070 417 ALA A O   
2999 C CB  . ALA A 377 ? 1.0479 1.1159 1.1191 0.1313  0.1072  -0.0312 417 ALA A CB  
3000 N N   . ASP A 378 ? 0.7665 0.8925 0.9406 0.1407  0.1125  -0.0004 418 ASP A N   
3001 C CA  . ASP A 378 ? 0.6370 0.7779 0.8481 0.1508  0.1227  0.0146  418 ASP A CA  
3002 C C   . ASP A 378 ? 0.4907 0.6412 0.7203 0.1553  0.1119  0.0206  418 ASP A C   
3003 O O   . ASP A 378 ? 0.4341 0.5970 0.6965 0.1645  0.1198  0.0338  418 ASP A O   
3004 C CB  . ASP A 378 ? 0.7755 0.9395 1.0239 0.1468  0.1195  0.0238  418 ASP A CB  
3005 C CG  . ASP A 378 ? 0.9858 1.1415 1.2156 0.1401  0.1255  0.0170  418 ASP A CG  
3006 O OD1 . ASP A 378 ? 1.0716 1.2030 1.2655 0.1427  0.1401  0.0095  418 ASP A OD1 
3007 O OD2 . ASP A 378 ? 1.0001 1.1718 1.2502 0.1319  0.1146  0.0192  418 ASP A OD2 
3008 N N   . ASP A 379 ? 0.4463 0.5913 0.6569 0.1494  0.0945  0.0121  419 ASP A N   
3009 C CA  . ASP A 379 ? 0.4518 0.6029 0.6757 0.1531  0.0831  0.0173  419 ASP A CA  
3010 C C   . ASP A 379 ? 0.5135 0.6454 0.7137 0.1619  0.0947  0.0149  419 ASP A C   
3011 O O   . ASP A 379 ? 0.4443 0.5785 0.6522 0.1658  0.0866  0.0190  419 ASP A O   
3012 C CB  . ASP A 379 ? 0.4160 0.5701 0.6317 0.1429  0.0581  0.0107  419 ASP A CB  
3013 C CG  . ASP A 379 ? 0.4558 0.5910 0.6281 0.1360  0.0563  -0.0044 419 ASP A CG  
3014 O OD1 . ASP A 379 ? 0.5588 0.6795 0.7091 0.1371  0.0718  -0.0100 419 ASP A OD1 
3015 O OD2 . ASP A 379 ? 0.4829 0.6165 0.6430 0.1296  0.0392  -0.0101 419 ASP A OD2 
3016 N N   . TRP A 380 ? 0.4562 0.5677 0.6272 0.1651  0.1125  0.0088  420 TRP A N   
3017 C CA  . TRP A 380 ? 0.4881 0.5786 0.6361 0.1743  0.1255  0.0072  420 TRP A CA  
3018 C C   . TRP A 380 ? 0.5234 0.6046 0.6716 0.1844  0.1502  0.0124  420 TRP A C   
3019 O O   . TRP A 380 ? 0.5342 0.6174 0.6847 0.1817  0.1577  0.0125  420 TRP A O   
3020 C CB  . TRP A 380 ? 0.4753 0.5424 0.5786 0.1678  0.1215  -0.0065 420 TRP A CB  
3021 C CG  . TRP A 380 ? 0.4980 0.5695 0.5959 0.1606  0.1012  -0.0111 420 TRP A CG  
3022 C CD1 . TRP A 380 ? 0.5273 0.6087 0.6262 0.1498  0.0847  -0.0161 420 TRP A CD1 
3023 C CD2 . TRP A 380 ? 0.4726 0.5362 0.5608 0.1643  0.0962  -0.0110 420 TRP A CD2 
3024 N NE1 . TRP A 380 ? 0.5672 0.6466 0.6562 0.1471  0.0707  -0.0189 420 TRP A NE1 
3025 C CE2 . TRP A 380 ? 0.5774 0.6464 0.6601 0.1555  0.0772  -0.0158 420 TRP A CE2 
3026 C CE3 . TRP A 380 ? 0.4889 0.5400 0.5709 0.1746  0.1063  -0.0073 420 TRP A CE3 
3027 C CZ2 . TRP A 380 ? 0.6018 0.6644 0.6732 0.1565  0.0685  -0.0165 420 TRP A CZ2 
3028 C CZ3 . TRP A 380 ? 0.5373 0.5832 0.6099 0.1750  0.0965  -0.0082 420 TRP A CZ3 
3029 C CH2 . TRP A 380 ? 0.5708 0.6226 0.6381 0.1659  0.0779  -0.0126 420 TRP A CH2 
3030 N N   . CYS A 381 ? 0.5077 0.5766 0.6512 0.1965  0.1634  0.0167  421 CYS A N   
3031 C CA  . CYS A 381 ? 0.6121 0.6676 0.7512 0.2082  0.1887  0.0218  421 CYS A CA  
3032 C C   . CYS A 381 ? 0.7859 0.8108 0.8778 0.2049  0.1978  0.0102  421 CYS A C   
3033 O O   . CYS A 381 ? 0.7502 0.7578 0.8086 0.1976  0.1877  -0.0011 421 CYS A O   
3034 C CB  . CYS A 381 ? 0.5656 0.6125 0.7079 0.2223  0.1997  0.0284  421 CYS A CB  
3035 S SG  . CYS A 381 ? 0.5751 0.6573 0.7789 0.2283  0.1930  0.0454  421 CYS A SG  
3036 N N   . VAL A 382 ? 1.0902 1.1076 1.1800 0.2107  0.2171  0.0139  422 VAL A N   
3037 C CA  . VAL A 382 ? 1.2247 1.2107 1.2695 0.2081  0.2260  0.0041  422 VAL A CA  
3038 C C   . VAL A 382 ? 1.3694 1.3200 1.3739 0.2158  0.2344  -0.0011 422 VAL A C   
3039 O O   . VAL A 382 ? 1.3891 1.3325 1.3985 0.2303  0.2506  0.0065  422 VAL A O   
3040 C CB  . VAL A 382 ? 1.2200 1.2054 1.2720 0.2134  0.2456  0.0106  422 VAL A CB  
3041 C CG1 . VAL A 382 ? 1.1737 1.1875 1.2543 0.2017  0.2334  0.0121  422 VAL A CG1 
3042 C CG2 . VAL A 382 ? 1.2246 1.2181 1.3057 0.2302  0.2661  0.0253  422 VAL A CG2 
3043 N N   . PRO A 383 ? 1.4331 1.3608 1.3986 0.2066  0.2234  -0.0134 423 PRO A N   
3044 C CA  . PRO A 383 ? 1.4687 1.3604 1.3937 0.2118  0.2278  -0.0189 423 PRO A CA  
3045 C C   . PRO A 383 ? 1.4724 1.3288 1.3643 0.2218  0.2497  -0.0190 423 PRO A C   
3046 O O   . PRO A 383 ? 1.4644 1.2849 1.3157 0.2246  0.2520  -0.0249 423 PRO A O   
3047 C CB  . PRO A 383 ? 1.4712 1.3530 1.3706 0.1965  0.2084  -0.0307 423 PRO A CB  
3048 C CG  . PRO A 383 ? 1.4240 1.3415 1.3559 0.1853  0.1925  -0.0305 423 PRO A CG  
3049 C CD  . PRO A 383 ? 1.4033 1.3406 1.3654 0.1902  0.2039  -0.0219 423 PRO A CD  
# 
