data_9FKU
# 
_entry.id   9FKU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9FKU         pdb_00009fku 10.2210/pdb9fku/pdb 
WWPDB D_1292139137 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_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                        9FKU 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              amarina@ibv.csic.es 
_pdbx_contact_author.name_first         Alberto 
_pdbx_contact_author.name_last          Marina 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1334-5273 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gallego del Sol, F.' 1 ? 
'Marina, A.'          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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal Structure of AimR from Katmira phage' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gallego del Sol, F.' 1 ? 
primary 'Marina, A.'          2 ? 
# 
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 'Arbitrium receptor'            45261.781 2   ? ? ? ? 
2 polymer     syn GLY-VAL-VAL-ARG-GLY-ALA         558.652   2   ? ? ? ? 
3 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL' 118.174   3   ? ? ? ? 
4 non-polymer syn 'ACETATE ION'                   59.044    3   ? ? ? ? 
5 water       nat water                           18.015    396 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MELIRIAMKKDLENDNSLMNKWATVAGLKNPNPLYDFLNHDGKTFNEFSSIVNIVKSQYPDREYELMKDYCLNLDVKTKA
ARSALEYADANMFFEIEDALIDSMISCSNMKSKEYGKVYKIHRELSKGEIDVFEASANIGKQRIKTAEMNIFSKMLLMYD
CLNKGNFAPMMLLFQQIDLSEIKENRYLKNSFETRINVLLSNIYLNENNLELCREYAQKAISSTDTQRFLVFSYLTIGTS
YIFSDFNLSKQNYLIGLKFAKGNPGFEEFFKRNLSFLNNFWNKENEWINYDSDAVTDMQEVIFELINHKELSKALQLLNK
LEERDQNENELGFHYYLKGLITNEKEAFFKSVEYFKASQDKLSIKMPLIQLEKMGENPRLLKIITM
;
;MELIRIAMKKDLENDNSLMNKWATVAGLKNPNPLYDFLNHDGKTFNEFSSIVNIVKSQYPDREYELMKDYCLNLDVKTKA
ARSALEYADANMFFEIEDALIDSMISCSNMKSKEYGKVYKIHRELSKGEIDVFEASANIGKQRIKTAEMNIFSKMLLMYD
CLNKGNFAPMMLLFQQIDLSEIKENRYLKNSFETRINVLLSNIYLNENNLELCREYAQKAISSTDTQRFLVFSYLTIGTS
YIFSDFNLSKQNYLIGLKFAKGNPGFEEFFKRNLSFLNNFWNKENEWINYDSDAVTDMQEVIFELINHKELSKALQLLNK
LEERDQNENELGFHYYLKGLITNEKEAFFKSVEYFKASQDKLSIKMPLIQLEKMGENPRLLKIITM
;
A,B ? 
2 'polypeptide(L)' no no GVVRGA GVVRGA C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '(4S)-2-METHYL-2,4-PENTANEDIOL' MPD 
4 'ACETATE ION'                   ACT 
5 water                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   LEU n 
1 4   ILE n 
1 5   ARG n 
1 6   ILE n 
1 7   ALA n 
1 8   MET n 
1 9   LYS n 
1 10  LYS n 
1 11  ASP n 
1 12  LEU n 
1 13  GLU n 
1 14  ASN n 
1 15  ASP n 
1 16  ASN n 
1 17  SER n 
1 18  LEU n 
1 19  MET n 
1 20  ASN n 
1 21  LYS n 
1 22  TRP n 
1 23  ALA n 
1 24  THR n 
1 25  VAL n 
1 26  ALA n 
1 27  GLY n 
1 28  LEU n 
1 29  LYS n 
1 30  ASN n 
1 31  PRO n 
1 32  ASN n 
1 33  PRO n 
1 34  LEU n 
1 35  TYR n 
1 36  ASP n 
1 37  PHE n 
1 38  LEU n 
1 39  ASN n 
1 40  HIS n 
1 41  ASP n 
1 42  GLY n 
1 43  LYS n 
1 44  THR n 
1 45  PHE n 
1 46  ASN n 
1 47  GLU n 
1 48  PHE n 
1 49  SER n 
1 50  SER n 
1 51  ILE n 
1 52  VAL n 
1 53  ASN n 
1 54  ILE n 
1 55  VAL n 
1 56  LYS n 
1 57  SER n 
1 58  GLN n 
1 59  TYR n 
1 60  PRO n 
1 61  ASP n 
1 62  ARG n 
1 63  GLU n 
1 64  TYR n 
1 65  GLU n 
1 66  LEU n 
1 67  MET n 
1 68  LYS n 
1 69  ASP n 
1 70  TYR n 
1 71  CYS n 
1 72  LEU n 
1 73  ASN n 
1 74  LEU n 
1 75  ASP n 
1 76  VAL n 
1 77  LYS n 
1 78  THR n 
1 79  LYS n 
1 80  ALA n 
1 81  ALA n 
1 82  ARG n 
1 83  SER n 
1 84  ALA n 
1 85  LEU n 
1 86  GLU n 
1 87  TYR n 
1 88  ALA n 
1 89  ASP n 
1 90  ALA n 
1 91  ASN n 
1 92  MET n 
1 93  PHE n 
1 94  PHE n 
1 95  GLU n 
1 96  ILE n 
1 97  GLU n 
1 98  ASP n 
1 99  ALA n 
1 100 LEU n 
1 101 ILE n 
1 102 ASP n 
1 103 SER n 
1 104 MET n 
1 105 ILE n 
1 106 SER n 
1 107 CYS n 
1 108 SER n 
1 109 ASN n 
1 110 MET n 
1 111 LYS n 
1 112 SER n 
1 113 LYS n 
1 114 GLU n 
1 115 TYR n 
1 116 GLY n 
1 117 LYS n 
1 118 VAL n 
1 119 TYR n 
1 120 LYS n 
1 121 ILE n 
1 122 HIS n 
1 123 ARG n 
1 124 GLU n 
1 125 LEU n 
1 126 SER n 
1 127 LYS n 
1 128 GLY n 
1 129 GLU n 
1 130 ILE n 
1 131 ASP n 
1 132 VAL n 
1 133 PHE n 
1 134 GLU n 
1 135 ALA n 
1 136 SER n 
1 137 ALA n 
1 138 ASN n 
1 139 ILE n 
1 140 GLY n 
1 141 LYS n 
1 142 GLN n 
1 143 ARG n 
1 144 ILE n 
1 145 LYS n 
1 146 THR n 
1 147 ALA n 
1 148 GLU n 
1 149 MET n 
1 150 ASN n 
1 151 ILE n 
1 152 PHE n 
1 153 SER n 
1 154 LYS n 
1 155 MET n 
1 156 LEU n 
1 157 LEU n 
1 158 MET n 
1 159 TYR n 
1 160 ASP n 
1 161 CYS n 
1 162 LEU n 
1 163 ASN n 
1 164 LYS n 
1 165 GLY n 
1 166 ASN n 
1 167 PHE n 
1 168 ALA n 
1 169 PRO n 
1 170 MET n 
1 171 MET n 
1 172 LEU n 
1 173 LEU n 
1 174 PHE n 
1 175 GLN n 
1 176 GLN n 
1 177 ILE n 
1 178 ASP n 
1 179 LEU n 
1 180 SER n 
1 181 GLU n 
1 182 ILE n 
1 183 LYS n 
1 184 GLU n 
1 185 ASN n 
1 186 ARG n 
1 187 TYR n 
1 188 LEU n 
1 189 LYS n 
1 190 ASN n 
1 191 SER n 
1 192 PHE n 
1 193 GLU n 
1 194 THR n 
1 195 ARG n 
1 196 ILE n 
1 197 ASN n 
1 198 VAL n 
1 199 LEU n 
1 200 LEU n 
1 201 SER n 
1 202 ASN n 
1 203 ILE n 
1 204 TYR n 
1 205 LEU n 
1 206 ASN n 
1 207 GLU n 
1 208 ASN n 
1 209 ASN n 
1 210 LEU n 
1 211 GLU n 
1 212 LEU n 
1 213 CYS n 
1 214 ARG n 
1 215 GLU n 
1 216 TYR n 
1 217 ALA n 
1 218 GLN n 
1 219 LYS n 
1 220 ALA n 
1 221 ILE n 
1 222 SER n 
1 223 SER n 
1 224 THR n 
1 225 ASP n 
1 226 THR n 
1 227 GLN n 
1 228 ARG n 
1 229 PHE n 
1 230 LEU n 
1 231 VAL n 
1 232 PHE n 
1 233 SER n 
1 234 TYR n 
1 235 LEU n 
1 236 THR n 
1 237 ILE n 
1 238 GLY n 
1 239 THR n 
1 240 SER n 
1 241 TYR n 
1 242 ILE n 
1 243 PHE n 
1 244 SER n 
1 245 ASP n 
1 246 PHE n 
1 247 ASN n 
1 248 LEU n 
1 249 SER n 
1 250 LYS n 
1 251 GLN n 
1 252 ASN n 
1 253 TYR n 
1 254 LEU n 
1 255 ILE n 
1 256 GLY n 
1 257 LEU n 
1 258 LYS n 
1 259 PHE n 
1 260 ALA n 
1 261 LYS n 
1 262 GLY n 
1 263 ASN n 
1 264 PRO n 
1 265 GLY n 
1 266 PHE n 
1 267 GLU n 
1 268 GLU n 
1 269 PHE n 
1 270 PHE n 
1 271 LYS n 
1 272 ARG n 
1 273 ASN n 
1 274 LEU n 
1 275 SER n 
1 276 PHE n 
1 277 LEU n 
1 278 ASN n 
1 279 ASN n 
1 280 PHE n 
1 281 TRP n 
1 282 ASN n 
1 283 LYS n 
1 284 GLU n 
1 285 ASN n 
1 286 GLU n 
1 287 TRP n 
1 288 ILE n 
1 289 ASN n 
1 290 TYR n 
1 291 ASP n 
1 292 SER n 
1 293 ASP n 
1 294 ALA n 
1 295 VAL n 
1 296 THR n 
1 297 ASP n 
1 298 MET n 
1 299 GLN n 
1 300 GLU n 
1 301 VAL n 
1 302 ILE n 
1 303 PHE n 
1 304 GLU n 
1 305 LEU n 
1 306 ILE n 
1 307 ASN n 
1 308 HIS n 
1 309 LYS n 
1 310 GLU n 
1 311 LEU n 
1 312 SER n 
1 313 LYS n 
1 314 ALA n 
1 315 LEU n 
1 316 GLN n 
1 317 LEU n 
1 318 LEU n 
1 319 ASN n 
1 320 LYS n 
1 321 LEU n 
1 322 GLU n 
1 323 GLU n 
1 324 ARG n 
1 325 ASP n 
1 326 GLN n 
1 327 ASN n 
1 328 GLU n 
1 329 ASN n 
1 330 GLU n 
1 331 LEU n 
1 332 GLY n 
1 333 PHE n 
1 334 HIS n 
1 335 TYR n 
1 336 TYR n 
1 337 LEU n 
1 338 LYS n 
1 339 GLY n 
1 340 LEU n 
1 341 ILE n 
1 342 THR n 
1 343 ASN n 
1 344 GLU n 
1 345 LYS n 
1 346 GLU n 
1 347 ALA n 
1 348 PHE n 
1 349 PHE n 
1 350 LYS n 
1 351 SER n 
1 352 VAL n 
1 353 GLU n 
1 354 TYR n 
1 355 PHE n 
1 356 LYS n 
1 357 ALA n 
1 358 SER n 
1 359 GLN n 
1 360 ASP n 
1 361 LYS n 
1 362 LEU n 
1 363 SER n 
1 364 ILE n 
1 365 LYS n 
1 366 MET n 
1 367 PRO n 
1 368 LEU n 
1 369 ILE n 
1 370 GLN n 
1 371 LEU n 
1 372 GLU n 
1 373 LYS n 
1 374 MET n 
1 375 GLY n 
1 376 GLU n 
1 377 ASN n 
1 378 PRO n 
1 379 ARG n 
1 380 LEU n 
1 381 LEU n 
1 382 LYS n 
1 383 ILE n 
1 384 ILE n 
1 385 THR n 
1 386 MET n 
2 1   GLY n 
2 2   VAL n 
2 3   VAL n 
2 4   ARG n 
2 5   GLY n 
2 6   ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   386 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Bacillus subtilis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1423 
_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-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       6 
_pdbx_entity_src_syn.organism_scientific    'Bacillus subtilis' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       1423 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'                   ? 'C2 H3 O2 -1'    59.044  
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  
HIS 'L-peptide linking' y HISTIDINE                       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                      ? 'C5 H11 N O2 S'  149.211 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL' ? 'C6 H14 O2'      118.174 
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   MET 1   1   1   MET MET A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   MET 8   8   8   MET MET A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  MET 19  19  19  MET MET A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  TRP 22  22  22  TRP TRP A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  ASN 39  39  39  ASN ASN A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  MET 67  67  67  MET MET A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  CYS 71  71  71  CYS CYS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  THR 78  78  78  THR THR A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  MET 92  92  92  MET MET A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 MET 104 104 104 MET MET A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 CYS 107 107 107 CYS CYS A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 GLU 124 124 124 GLU GLU A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 GLN 142 142 142 GLN GLN A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 MET 149 149 149 MET MET A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 MET 155 155 155 MET MET A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 MET 158 158 158 MET MET A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 CYS 161 161 161 CYS CYS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ASN 163 163 163 ASN ASN A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 MET 170 170 170 MET MET A . n 
A 1 171 MET 171 171 171 MET MET A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 LYS 183 183 183 LYS LYS A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ARG 195 195 195 ARG ARG A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 CYS 213 213 213 CYS CYS A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 LYS 219 219 219 LYS LYS A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 PHE 229 229 229 PHE PHE A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 PHE 232 232 232 PHE PHE A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 TYR 234 234 234 TYR TYR A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 ILE 237 237 237 ILE ILE A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ASN 247 247 247 ASN ASN A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 TYR 253 253 253 TYR TYR A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 GLU 268 268 268 GLU GLU A . n 
A 1 269 PHE 269 269 269 PHE PHE A . n 
A 1 270 PHE 270 270 270 PHE PHE A . n 
A 1 271 LYS 271 271 271 LYS LYS A . n 
A 1 272 ARG 272 272 272 ARG ARG A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 ASN 278 278 278 ASN ASN A . n 
A 1 279 ASN 279 279 279 ASN ASN A . n 
A 1 280 PHE 280 280 280 PHE PHE A . n 
A 1 281 TRP 281 281 281 TRP TRP A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 ASN 285 285 285 ASN ASN A . n 
A 1 286 GLU 286 286 286 GLU GLU A . n 
A 1 287 TRP 287 287 287 TRP TRP A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 SER 292 292 292 SER SER A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 THR 296 296 296 THR THR A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 MET 298 298 298 MET MET A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 PHE 303 303 303 PHE PHE A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 ASN 307 307 307 ASN ASN A . n 
A 1 308 HIS 308 308 308 HIS HIS A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 GLU 310 310 310 GLU GLU A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 SER 312 312 312 SER SER A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 GLN 316 316 316 GLN GLN A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 ASN 319 319 319 ASN ASN A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 ARG 324 324 324 ARG ARG A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 GLN 326 326 326 GLN GLN A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 GLU 328 328 328 GLU GLU A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 PHE 333 333 333 PHE PHE A . n 
A 1 334 HIS 334 334 334 HIS HIS A . n 
A 1 335 TYR 335 335 335 TYR TYR A . n 
A 1 336 TYR 336 336 336 TYR TYR A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 GLY 339 339 339 GLY GLY A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 THR 342 342 342 THR THR A . n 
A 1 343 ASN 343 343 343 ASN ASN A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 GLU 346 346 346 GLU GLU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 LYS 350 350 350 LYS LYS A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 TYR 354 354 354 TYR TYR A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 SER 358 358 358 SER SER A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 ASP 360 360 360 ASP ASP A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 SER 363 363 363 SER SER A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 LYS 365 365 365 LYS LYS A . n 
A 1 366 MET 366 366 366 MET MET A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 GLN 370 370 370 GLN GLN A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 LYS 373 373 373 LYS LYS A . n 
A 1 374 MET 374 374 374 MET MET A . n 
A 1 375 GLY 375 375 375 GLY GLY A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 PRO 378 378 378 PRO PRO A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 LYS 382 382 382 LYS LYS A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 ILE 384 384 384 ILE ILE A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 MET 386 386 386 MET MET A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   GLU 2   2   2   GLU GLU B . n 
B 1 3   LEU 3   3   3   LEU LEU B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   ARG 5   5   5   ARG ARG B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   MET 8   8   8   MET MET B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  LYS 10  10  10  LYS LYS B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  ASP 15  15  15  ASP ASP B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  SER 17  17  17  SER SER B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  MET 19  19  19  MET MET B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  TRP 22  22  22  TRP TRP B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  ALA 26  26  26  ALA ALA B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  LEU 28  28  28  LEU LEU B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  ASN 32  32  32  ASN ASN B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  TYR 35  35  35  TYR TYR B . n 
B 1 36  ASP 36  36  36  ASP ASP B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  ASN 39  39  39  ASN ASN B . n 
B 1 40  HIS 40  40  40  HIS HIS B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  GLY 42  42  42  GLY GLY B . n 
B 1 43  LYS 43  43  43  LYS LYS B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  ASN 46  46  46  ASN ASN B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  SER 49  49  49  SER SER B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  ILE 54  54  54  ILE ILE B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  LYS 56  56  56  LYS LYS B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  TYR 59  59  59  TYR TYR B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  ARG 62  62  62  ARG ARG B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  MET 67  67  67  MET MET B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  TYR 70  70  70  TYR TYR B . n 
B 1 71  CYS 71  71  71  CYS CYS B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  ASN 73  73  73  ASN ASN B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  VAL 76  76  76  VAL VAL B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  THR 78  78  78  THR THR B . n 
B 1 79  LYS 79  79  79  LYS LYS B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  TYR 87  87  87  TYR TYR B . n 
B 1 88  ALA 88  88  88  ALA ALA B . n 
B 1 89  ASP 89  89  89  ASP ASP B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  ASN 91  91  91  ASN ASN B . n 
B 1 92  MET 92  92  92  MET MET B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 ILE 101 101 101 ILE ILE B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 MET 104 104 104 MET MET B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 CYS 107 107 107 CYS CYS B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 MET 110 110 110 MET MET B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 TYR 115 115 115 TYR TYR B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 LYS 117 117 117 LYS LYS B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 TYR 119 119 119 TYR TYR B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 ARG 123 123 123 ARG ARG B . n 
B 1 124 GLU 124 124 124 GLU GLU B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 GLU 134 134 134 GLU GLU B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 ASN 138 138 138 ASN ASN B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 LYS 141 141 141 LYS LYS B . n 
B 1 142 GLN 142 142 142 GLN GLN B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 MET 149 149 149 MET MET B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 PHE 152 152 152 PHE PHE B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 LYS 154 154 154 LYS LYS B . n 
B 1 155 MET 155 155 155 MET MET B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 MET 158 158 158 MET MET B . n 
B 1 159 TYR 159 159 159 TYR TYR B . n 
B 1 160 ASP 160 160 160 ASP ASP B . n 
B 1 161 CYS 161 161 161 CYS CYS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 ASN 163 163 163 ASN ASN B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 ASN 166 166 166 ASN ASN B . n 
B 1 167 PHE 167 167 167 PHE PHE B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 PRO 169 169 169 PRO PRO B . n 
B 1 170 MET 170 170 170 MET MET B . n 
B 1 171 MET 171 171 171 MET MET B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 PHE 174 174 174 PHE PHE B . n 
B 1 175 GLN 175 175 175 GLN GLN B . n 
B 1 176 GLN 176 176 176 GLN GLN B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 ASP 178 178 178 ASP ASP B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 LYS 183 183 183 LYS LYS B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 ASN 185 185 185 ASN ASN B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 TYR 187 187 187 TYR TYR B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 LYS 189 189 189 LYS LYS B . n 
B 1 190 ASN 190 190 190 ASN ASN B . n 
B 1 191 SER 191 191 191 SER SER B . n 
B 1 192 PHE 192 192 192 PHE PHE B . n 
B 1 193 GLU 193 193 193 GLU GLU B . n 
B 1 194 THR 194 194 194 THR THR B . n 
B 1 195 ARG 195 195 195 ARG ARG B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 ASN 197 197 197 ASN ASN B . n 
B 1 198 VAL 198 198 198 VAL VAL B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 SER 201 201 201 SER SER B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 TYR 204 204 204 TYR TYR B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 ASN 209 209 209 ASN ASN B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 CYS 213 213 213 CYS CYS B . n 
B 1 214 ARG 214 214 214 ARG ARG B . n 
B 1 215 GLU 215 215 215 GLU GLU B . n 
B 1 216 TYR 216 216 216 TYR TYR B . n 
B 1 217 ALA 217 217 217 ALA ALA B . n 
B 1 218 GLN 218 218 218 GLN GLN B . n 
B 1 219 LYS 219 219 219 LYS LYS B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 ASP 225 225 225 ASP ASP B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 ARG 228 228 228 ARG ARG B . n 
B 1 229 PHE 229 229 229 PHE PHE B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 VAL 231 231 231 VAL VAL B . n 
B 1 232 PHE 232 232 232 PHE PHE B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 TYR 234 234 234 TYR TYR B . n 
B 1 235 LEU 235 235 235 LEU LEU B . n 
B 1 236 THR 236 236 236 THR THR B . n 
B 1 237 ILE 237 237 237 ILE ILE B . n 
B 1 238 GLY 238 238 238 GLY GLY B . n 
B 1 239 THR 239 239 239 THR THR B . n 
B 1 240 SER 240 240 240 SER SER B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 ILE 242 242 242 ILE ILE B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ASN 247 247 247 ASN ASN B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 SER 249 249 249 SER SER B . n 
B 1 250 LYS 250 250 250 LYS LYS B . n 
B 1 251 GLN 251 251 251 GLN GLN B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 TYR 253 253 253 TYR TYR B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 ILE 255 255 255 ILE ILE B . n 
B 1 256 GLY 256 256 256 GLY GLY B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 LYS 258 258 258 LYS LYS B . n 
B 1 259 PHE 259 259 259 PHE PHE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 LYS 261 261 261 LYS LYS B . n 
B 1 262 GLY 262 262 262 GLY GLY B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 PRO 264 264 264 PRO PRO B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 GLU 268 268 268 GLU GLU B . n 
B 1 269 PHE 269 269 269 PHE PHE B . n 
B 1 270 PHE 270 270 270 PHE PHE B . n 
B 1 271 LYS 271 271 271 LYS LYS B . n 
B 1 272 ARG 272 272 272 ARG ARG B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 LEU 274 274 274 LEU LEU B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 PHE 276 276 276 PHE PHE B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 ASN 278 278 278 ASN ASN B . n 
B 1 279 ASN 279 279 279 ASN ASN B . n 
B 1 280 PHE 280 280 280 PHE PHE B . n 
B 1 281 TRP 281 281 281 TRP TRP B . n 
B 1 282 ASN 282 282 282 ASN ASN B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 GLU 284 284 284 GLU GLU B . n 
B 1 285 ASN 285 285 285 ASN ASN B . n 
B 1 286 GLU 286 286 286 GLU GLU B . n 
B 1 287 TRP 287 287 287 TRP TRP B . n 
B 1 288 ILE 288 288 288 ILE ILE B . n 
B 1 289 ASN 289 289 289 ASN ASN B . n 
B 1 290 TYR 290 290 290 TYR TYR B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 SER 292 292 292 SER SER B . n 
B 1 293 ASP 293 293 293 ASP ASP B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 VAL 295 295 295 VAL VAL B . n 
B 1 296 THR 296 296 296 THR THR B . n 
B 1 297 ASP 297 297 297 ASP ASP B . n 
B 1 298 MET 298 298 298 MET MET B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 GLU 300 300 300 GLU GLU B . n 
B 1 301 VAL 301 301 301 VAL VAL B . n 
B 1 302 ILE 302 302 302 ILE ILE B . n 
B 1 303 PHE 303 303 303 PHE PHE B . n 
B 1 304 GLU 304 304 304 GLU GLU B . n 
B 1 305 LEU 305 305 305 LEU LEU B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 ASN 307 307 307 ASN ASN B . n 
B 1 308 HIS 308 308 308 HIS HIS B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 GLU 310 310 310 GLU GLU B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 SER 312 312 312 SER SER B . n 
B 1 313 LYS 313 313 313 LYS LYS B . n 
B 1 314 ALA 314 314 314 ALA ALA B . n 
B 1 315 LEU 315 315 315 LEU LEU B . n 
B 1 316 GLN 316 316 316 GLN GLN B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 ASN 319 319 319 ASN ASN B . n 
B 1 320 LYS 320 320 320 LYS LYS B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 GLU 322 322 322 GLU GLU B . n 
B 1 323 GLU 323 323 323 GLU GLU B . n 
B 1 324 ARG 324 324 324 ARG ARG B . n 
B 1 325 ASP 325 325 325 ASP ASP B . n 
B 1 326 GLN 326 326 326 GLN GLN B . n 
B 1 327 ASN 327 327 327 ASN ASN B . n 
B 1 328 GLU 328 328 328 GLU GLU B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 GLU 330 330 330 GLU GLU B . n 
B 1 331 LEU 331 331 331 LEU LEU B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 PHE 333 333 333 PHE PHE B . n 
B 1 334 HIS 334 334 334 HIS HIS B . n 
B 1 335 TYR 335 335 335 TYR TYR B . n 
B 1 336 TYR 336 336 336 TYR TYR B . n 
B 1 337 LEU 337 337 337 LEU LEU B . n 
B 1 338 LYS 338 338 338 LYS LYS B . n 
B 1 339 GLY 339 339 339 GLY GLY B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 ILE 341 341 341 ILE ILE B . n 
B 1 342 THR 342 342 342 THR THR B . n 
B 1 343 ASN 343 343 343 ASN ASN B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 LYS 345 345 345 LYS LYS B . n 
B 1 346 GLU 346 346 346 GLU GLU B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 PHE 348 348 348 PHE PHE B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 LYS 350 350 350 LYS LYS B . n 
B 1 351 SER 351 351 351 SER SER B . n 
B 1 352 VAL 352 352 352 VAL VAL B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 TYR 354 354 354 TYR TYR B . n 
B 1 355 PHE 355 355 355 PHE PHE B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 ALA 357 357 357 ALA ALA B . n 
B 1 358 SER 358 358 358 SER SER B . n 
B 1 359 GLN 359 359 359 GLN GLN B . n 
B 1 360 ASP 360 360 360 ASP ASP B . n 
B 1 361 LYS 361 361 361 LYS LYS B . n 
B 1 362 LEU 362 362 362 LEU LEU B . n 
B 1 363 SER 363 363 363 SER SER B . n 
B 1 364 ILE 364 364 364 ILE ILE B . n 
B 1 365 LYS 365 365 365 LYS LYS B . n 
B 1 366 MET 366 366 366 MET MET B . n 
B 1 367 PRO 367 367 367 PRO PRO B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 ILE 369 369 369 ILE ILE B . n 
B 1 370 GLN 370 370 370 GLN GLN B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 LYS 373 373 373 LYS LYS B . n 
B 1 374 MET 374 374 374 MET MET B . n 
B 1 375 GLY 375 375 375 GLY GLY B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 ASN 377 377 377 ASN ASN B . n 
B 1 378 PRO 378 378 378 PRO PRO B . n 
B 1 379 ARG 379 379 379 ARG ARG B . n 
B 1 380 LEU 380 380 380 LEU LEU B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 LYS 382 382 382 LYS LYS B . n 
B 1 383 ILE 383 383 383 ILE ILE B . n 
B 1 384 ILE 384 384 384 ILE ILE B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 MET 386 386 386 MET MET B . n 
C 2 1   GLY 1   1   1   GLY GLY C . n 
C 2 2   VAL 2   2   2   VAL VAL C . n 
C 2 3   VAL 3   3   3   VAL VAL C . n 
C 2 4   ARG 4   4   4   ARG ARG C . n 
C 2 5   GLY 5   5   5   GLY GLY C . n 
C 2 6   ALA 6   6   6   ALA ALA C . n 
D 2 1   GLY 1   1   1   GLY GLY D . n 
D 2 2   VAL 2   2   2   VAL VAL D . n 
D 2 3   VAL 3   3   3   VAL VAL D . n 
D 2 4   ARG 4   4   4   ARG ARG D . n 
D 2 5   GLY 5   5   5   GLY GLY D . n 
D 2 6   ALA 6   6   6   ALA ALA D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 MPD 1   401 2   MPD MPD A . 
F 4 ACT 1   402 2   ACT ACT A . 
G 4 ACT 1   403 3   ACT ACT A . 
H 3 MPD 1   401 1   MPD MPD B . 
I 3 MPD 1   402 3   MPD MPD B . 
J 4 ACT 1   403 1   ACT ACT B . 
K 5 HOH 1   501 150 HOH HOH A . 
K 5 HOH 2   502 271 HOH HOH A . 
K 5 HOH 3   503 174 HOH HOH A . 
K 5 HOH 4   504 272 HOH HOH A . 
K 5 HOH 5   505 266 HOH HOH A . 
K 5 HOH 6   506 128 HOH HOH A . 
K 5 HOH 7   507 63  HOH HOH A . 
K 5 HOH 8   508 91  HOH HOH A . 
K 5 HOH 9   509 277 HOH HOH A . 
K 5 HOH 10  510 18  HOH HOH A . 
K 5 HOH 11  511 141 HOH HOH A . 
K 5 HOH 12  512 17  HOH HOH A . 
K 5 HOH 13  513 357 HOH HOH A . 
K 5 HOH 14  514 259 HOH HOH A . 
K 5 HOH 15  515 119 HOH HOH A . 
K 5 HOH 16  516 250 HOH HOH A . 
K 5 HOH 17  517 51  HOH HOH A . 
K 5 HOH 18  518 177 HOH HOH A . 
K 5 HOH 19  519 260 HOH HOH A . 
K 5 HOH 20  520 380 HOH HOH A . 
K 5 HOH 21  521 274 HOH HOH A . 
K 5 HOH 22  522 247 HOH HOH A . 
K 5 HOH 23  523 154 HOH HOH A . 
K 5 HOH 24  524 281 HOH HOH A . 
K 5 HOH 25  525 121 HOH HOH A . 
K 5 HOH 26  526 255 HOH HOH A . 
K 5 HOH 27  527 246 HOH HOH A . 
K 5 HOH 28  528 19  HOH HOH A . 
K 5 HOH 29  529 140 HOH HOH A . 
K 5 HOH 30  530 118 HOH HOH A . 
K 5 HOH 31  531 6   HOH HOH A . 
K 5 HOH 32  532 142 HOH HOH A . 
K 5 HOH 33  533 83  HOH HOH A . 
K 5 HOH 34  534 240 HOH HOH A . 
K 5 HOH 35  535 1   HOH HOH A . 
K 5 HOH 36  536 178 HOH HOH A . 
K 5 HOH 37  537 109 HOH HOH A . 
K 5 HOH 38  538 267 HOH HOH A . 
K 5 HOH 39  539 71  HOH HOH A . 
K 5 HOH 40  540 249 HOH HOH A . 
K 5 HOH 41  541 87  HOH HOH A . 
K 5 HOH 42  542 152 HOH HOH A . 
K 5 HOH 43  543 161 HOH HOH A . 
K 5 HOH 44  544 268 HOH HOH A . 
K 5 HOH 45  545 5   HOH HOH A . 
K 5 HOH 46  546 270 HOH HOH A . 
K 5 HOH 47  547 276 HOH HOH A . 
K 5 HOH 48  548 375 HOH HOH A . 
K 5 HOH 49  549 24  HOH HOH A . 
K 5 HOH 50  550 167 HOH HOH A . 
K 5 HOH 51  551 73  HOH HOH A . 
K 5 HOH 52  552 57  HOH HOH A . 
K 5 HOH 53  553 68  HOH HOH A . 
K 5 HOH 54  554 35  HOH HOH A . 
K 5 HOH 55  555 138 HOH HOH A . 
K 5 HOH 56  556 123 HOH HOH A . 
K 5 HOH 57  557 86  HOH HOH A . 
K 5 HOH 58  558 50  HOH HOH A . 
K 5 HOH 59  559 34  HOH HOH A . 
K 5 HOH 60  560 378 HOH HOH A . 
K 5 HOH 61  561 69  HOH HOH A . 
K 5 HOH 62  562 2   HOH HOH A . 
K 5 HOH 63  563 49  HOH HOH A . 
K 5 HOH 64  564 32  HOH HOH A . 
K 5 HOH 65  565 96  HOH HOH A . 
K 5 HOH 66  566 284 HOH HOH A . 
K 5 HOH 67  567 180 HOH HOH A . 
K 5 HOH 68  568 179 HOH HOH A . 
K 5 HOH 69  569 242 HOH HOH A . 
K 5 HOH 70  570 151 HOH HOH A . 
K 5 HOH 71  571 100 HOH HOH A . 
K 5 HOH 72  572 61  HOH HOH A . 
K 5 HOH 73  573 39  HOH HOH A . 
K 5 HOH 74  574 241 HOH HOH A . 
K 5 HOH 75  575 72  HOH HOH A . 
K 5 HOH 76  576 273 HOH HOH A . 
K 5 HOH 77  577 269 HOH HOH A . 
K 5 HOH 78  578 102 HOH HOH A . 
K 5 HOH 79  579 27  HOH HOH A . 
K 5 HOH 80  580 245 HOH HOH A . 
K 5 HOH 81  581 172 HOH HOH A . 
K 5 HOH 82  582 117 HOH HOH A . 
K 5 HOH 83  583 147 HOH HOH A . 
K 5 HOH 84  584 256 HOH HOH A . 
K 5 HOH 85  585 103 HOH HOH A . 
K 5 HOH 86  586 129 HOH HOH A . 
K 5 HOH 87  587 160 HOH HOH A . 
K 5 HOH 88  588 84  HOH HOH A . 
K 5 HOH 89  589 139 HOH HOH A . 
K 5 HOH 90  590 8   HOH HOH A . 
K 5 HOH 91  591 143 HOH HOH A . 
K 5 HOH 92  592 60  HOH HOH A . 
K 5 HOH 93  593 3   HOH HOH A . 
K 5 HOH 94  594 113 HOH HOH A . 
K 5 HOH 95  595 248 HOH HOH A . 
K 5 HOH 96  596 78  HOH HOH A . 
K 5 HOH 97  597 81  HOH HOH A . 
K 5 HOH 98  598 254 HOH HOH A . 
K 5 HOH 99  599 75  HOH HOH A . 
K 5 HOH 100 600 280 HOH HOH A . 
K 5 HOH 101 601 170 HOH HOH A . 
K 5 HOH 102 602 149 HOH HOH A . 
K 5 HOH 103 603 382 HOH HOH A . 
K 5 HOH 104 604 62  HOH HOH A . 
K 5 HOH 105 605 22  HOH HOH A . 
K 5 HOH 106 606 146 HOH HOH A . 
K 5 HOH 107 607 391 HOH HOH A . 
K 5 HOH 108 608 14  HOH HOH A . 
K 5 HOH 109 609 261 HOH HOH A . 
K 5 HOH 110 610 392 HOH HOH A . 
K 5 HOH 111 611 7   HOH HOH A . 
K 5 HOH 112 612 171 HOH HOH A . 
K 5 HOH 113 613 92  HOH HOH A . 
K 5 HOH 114 614 163 HOH HOH A . 
K 5 HOH 115 615 53  HOH HOH A . 
K 5 HOH 116 616 253 HOH HOH A . 
K 5 HOH 117 617 168 HOH HOH A . 
K 5 HOH 118 618 108 HOH HOH A . 
K 5 HOH 119 619 156 HOH HOH A . 
K 5 HOH 120 620 363 HOH HOH A . 
K 5 HOH 121 621 257 HOH HOH A . 
K 5 HOH 122 622 275 HOH HOH A . 
K 5 HOH 123 623 89  HOH HOH A . 
K 5 HOH 124 624 28  HOH HOH A . 
K 5 HOH 125 625 93  HOH HOH A . 
K 5 HOH 126 626 173 HOH HOH A . 
K 5 HOH 127 627 243 HOH HOH A . 
K 5 HOH 128 628 279 HOH HOH A . 
K 5 HOH 129 629 126 HOH HOH A . 
K 5 HOH 130 630 159 HOH HOH A . 
K 5 HOH 131 631 11  HOH HOH A . 
K 5 HOH 132 632 169 HOH HOH A . 
K 5 HOH 133 633 144 HOH HOH A . 
K 5 HOH 134 634 145 HOH HOH A . 
K 5 HOH 135 635 389 HOH HOH A . 
K 5 HOH 136 636 153 HOH HOH A . 
K 5 HOH 137 637 9   HOH HOH A . 
K 5 HOH 138 638 371 HOH HOH A . 
K 5 HOH 139 639 40  HOH HOH A . 
K 5 HOH 140 640 43  HOH HOH A . 
K 5 HOH 141 641 134 HOH HOH A . 
K 5 HOH 142 642 158 HOH HOH A . 
K 5 HOH 143 643 26  HOH HOH A . 
K 5 HOH 144 644 396 HOH HOH A . 
K 5 HOH 145 645 376 HOH HOH A . 
K 5 HOH 146 646 157 HOH HOH A . 
K 5 HOH 147 647 258 HOH HOH A . 
K 5 HOH 148 648 283 HOH HOH A . 
K 5 HOH 149 649 54  HOH HOH A . 
K 5 HOH 150 650 360 HOH HOH A . 
K 5 HOH 151 651 110 HOH HOH A . 
K 5 HOH 152 652 166 HOH HOH A . 
K 5 HOH 153 653 264 HOH HOH A . 
K 5 HOH 154 654 366 HOH HOH A . 
K 5 HOH 155 655 137 HOH HOH A . 
K 5 HOH 156 656 135 HOH HOH A . 
K 5 HOH 157 657 358 HOH HOH A . 
K 5 HOH 158 658 131 HOH HOH A . 
K 5 HOH 159 659 379 HOH HOH A . 
K 5 HOH 160 660 239 HOH HOH A . 
K 5 HOH 161 661 390 HOH HOH A . 
K 5 HOH 162 662 362 HOH HOH A . 
K 5 HOH 163 663 369 HOH HOH A . 
K 5 HOH 164 664 114 HOH HOH A . 
K 5 HOH 165 665 381 HOH HOH A . 
K 5 HOH 166 666 393 HOH HOH A . 
K 5 HOH 167 667 164 HOH HOH A . 
K 5 HOH 168 668 352 HOH HOH A . 
K 5 HOH 169 669 104 HOH HOH A . 
K 5 HOH 170 670 162 HOH HOH A . 
K 5 HOH 171 671 252 HOH HOH A . 
K 5 HOH 172 672 23  HOH HOH A . 
K 5 HOH 173 673 359 HOH HOH A . 
K 5 HOH 174 674 262 HOH HOH A . 
K 5 HOH 175 675 148 HOH HOH A . 
K 5 HOH 176 676 55  HOH HOH A . 
K 5 HOH 177 677 368 HOH HOH A . 
K 5 HOH 178 678 370 HOH HOH A . 
K 5 HOH 179 679 133 HOH HOH A . 
K 5 HOH 180 680 136 HOH HOH A . 
K 5 HOH 181 681 165 HOH HOH A . 
K 5 HOH 182 682 64  HOH HOH A . 
K 5 HOH 183 683 282 HOH HOH A . 
K 5 HOH 184 684 263 HOH HOH A . 
K 5 HOH 185 685 244 HOH HOH A . 
K 5 HOH 186 686 265 HOH HOH A . 
K 5 HOH 187 687 361 HOH HOH A . 
K 5 HOH 188 688 365 HOH HOH A . 
K 5 HOH 189 689 237 HOH HOH A . 
K 5 HOH 190 690 278 HOH HOH A . 
K 5 HOH 191 691 346 HOH HOH A . 
L 5 HOH 1   501 324 HOH HOH B . 
L 5 HOH 2   502 203 HOH HOH B . 
L 5 HOH 3   503 329 HOH HOH B . 
L 5 HOH 4   504 328 HOH HOH B . 
L 5 HOH 5   505 298 HOH HOH B . 
L 5 HOH 6   506 322 HOH HOH B . 
L 5 HOH 7   507 349 HOH HOH B . 
L 5 HOH 8   508 321 HOH HOH B . 
L 5 HOH 9   509 290 HOH HOH B . 
L 5 HOH 10  510 326 HOH HOH B . 
L 5 HOH 11  511 309 HOH HOH B . 
L 5 HOH 12  512 194 HOH HOH B . 
L 5 HOH 13  513 201 HOH HOH B . 
L 5 HOH 14  514 41  HOH HOH B . 
L 5 HOH 15  515 308 HOH HOH B . 
L 5 HOH 16  516 238 HOH HOH B . 
L 5 HOH 17  517 189 HOH HOH B . 
L 5 HOH 18  518 354 HOH HOH B . 
L 5 HOH 19  519 182 HOH HOH B . 
L 5 HOH 20  520 181 HOH HOH B . 
L 5 HOH 21  521 74  HOH HOH B . 
L 5 HOH 22  522 230 HOH HOH B . 
L 5 HOH 23  523 213 HOH HOH B . 
L 5 HOH 24  524 234 HOH HOH B . 
L 5 HOH 25  525 45  HOH HOH B . 
L 5 HOH 26  526 191 HOH HOH B . 
L 5 HOH 27  527 305 HOH HOH B . 
L 5 HOH 28  528 337 HOH HOH B . 
L 5 HOH 29  529 286 HOH HOH B . 
L 5 HOH 30  530 317 HOH HOH B . 
L 5 HOH 31  531 186 HOH HOH B . 
L 5 HOH 32  532 294 HOH HOH B . 
L 5 HOH 33  533 211 HOH HOH B . 
L 5 HOH 34  534 218 HOH HOH B . 
L 5 HOH 35  535 332 HOH HOH B . 
L 5 HOH 36  536 44  HOH HOH B . 
L 5 HOH 37  537 21  HOH HOH B . 
L 5 HOH 38  538 199 HOH HOH B . 
L 5 HOH 39  539 331 HOH HOH B . 
L 5 HOH 40  540 377 HOH HOH B . 
L 5 HOH 41  541 333 HOH HOH B . 
L 5 HOH 42  542 225 HOH HOH B . 
L 5 HOH 43  543 209 HOH HOH B . 
L 5 HOH 44  544 47  HOH HOH B . 
L 5 HOH 45  545 219 HOH HOH B . 
L 5 HOH 46  546 394 HOH HOH B . 
L 5 HOH 47  547 299 HOH HOH B . 
L 5 HOH 48  548 198 HOH HOH B . 
L 5 HOH 49  549 46  HOH HOH B . 
L 5 HOH 50  550 12  HOH HOH B . 
L 5 HOH 51  551 196 HOH HOH B . 
L 5 HOH 52  552 190 HOH HOH B . 
L 5 HOH 53  553 323 HOH HOH B . 
L 5 HOH 54  554 372 HOH HOH B . 
L 5 HOH 55  555 16  HOH HOH B . 
L 5 HOH 56  556 347 HOH HOH B . 
L 5 HOH 57  557 48  HOH HOH B . 
L 5 HOH 58  558 13  HOH HOH B . 
L 5 HOH 59  559 288 HOH HOH B . 
L 5 HOH 60  560 338 HOH HOH B . 
L 5 HOH 61  561 76  HOH HOH B . 
L 5 HOH 62  562 184 HOH HOH B . 
L 5 HOH 63  563 193 HOH HOH B . 
L 5 HOH 64  564 205 HOH HOH B . 
L 5 HOH 65  565 195 HOH HOH B . 
L 5 HOH 66  566 232 HOH HOH B . 
L 5 HOH 67  567 316 HOH HOH B . 
L 5 HOH 68  568 350 HOH HOH B . 
L 5 HOH 69  569 112 HOH HOH B . 
L 5 HOH 70  570 310 HOH HOH B . 
L 5 HOH 71  571 90  HOH HOH B . 
L 5 HOH 72  572 29  HOH HOH B . 
L 5 HOH 73  573 120 HOH HOH B . 
L 5 HOH 74  574 125 HOH HOH B . 
L 5 HOH 75  575 98  HOH HOH B . 
L 5 HOH 76  576 187 HOH HOH B . 
L 5 HOH 77  577 52  HOH HOH B . 
L 5 HOH 78  578 116 HOH HOH B . 
L 5 HOH 79  579 15  HOH HOH B . 
L 5 HOH 80  580 339 HOH HOH B . 
L 5 HOH 81  581 348 HOH HOH B . 
L 5 HOH 82  582 30  HOH HOH B . 
L 5 HOH 83  583 59  HOH HOH B . 
L 5 HOH 84  584 224 HOH HOH B . 
L 5 HOH 85  585 185 HOH HOH B . 
L 5 HOH 86  586 313 HOH HOH B . 
L 5 HOH 87  587 70  HOH HOH B . 
L 5 HOH 88  588 220 HOH HOH B . 
L 5 HOH 89  589 101 HOH HOH B . 
L 5 HOH 90  590 364 HOH HOH B . 
L 5 HOH 91  591 314 HOH HOH B . 
L 5 HOH 92  592 200 HOH HOH B . 
L 5 HOH 93  593 88  HOH HOH B . 
L 5 HOH 94  594 95  HOH HOH B . 
L 5 HOH 95  595 320 HOH HOH B . 
L 5 HOH 96  596 351 HOH HOH B . 
L 5 HOH 97  597 99  HOH HOH B . 
L 5 HOH 98  598 227 HOH HOH B . 
L 5 HOH 99  599 58  HOH HOH B . 
L 5 HOH 100 600 343 HOH HOH B . 
L 5 HOH 101 601 285 HOH HOH B . 
L 5 HOH 102 602 183 HOH HOH B . 
L 5 HOH 103 603 115 HOH HOH B . 
L 5 HOH 104 604 356 HOH HOH B . 
L 5 HOH 105 605 292 HOH HOH B . 
L 5 HOH 106 606 223 HOH HOH B . 
L 5 HOH 107 607 36  HOH HOH B . 
L 5 HOH 108 608 386 HOH HOH B . 
L 5 HOH 109 609 297 HOH HOH B . 
L 5 HOH 110 610 94  HOH HOH B . 
L 5 HOH 111 611 221 HOH HOH B . 
L 5 HOH 112 612 105 HOH HOH B . 
L 5 HOH 113 613 38  HOH HOH B . 
L 5 HOH 114 614 42  HOH HOH B . 
L 5 HOH 115 615 122 HOH HOH B . 
L 5 HOH 116 616 97  HOH HOH B . 
L 5 HOH 117 617 66  HOH HOH B . 
L 5 HOH 118 618 37  HOH HOH B . 
L 5 HOH 119 619 384 HOH HOH B . 
L 5 HOH 120 620 79  HOH HOH B . 
L 5 HOH 121 621 330 HOH HOH B . 
L 5 HOH 122 622 124 HOH HOH B . 
L 5 HOH 123 623 208 HOH HOH B . 
L 5 HOH 124 624 334 HOH HOH B . 
L 5 HOH 125 625 25  HOH HOH B . 
L 5 HOH 126 626 207 HOH HOH B . 
L 5 HOH 127 627 296 HOH HOH B . 
L 5 HOH 128 628 65  HOH HOH B . 
L 5 HOH 129 629 107 HOH HOH B . 
L 5 HOH 130 630 206 HOH HOH B . 
L 5 HOH 131 631 231 HOH HOH B . 
L 5 HOH 132 632 335 HOH HOH B . 
L 5 HOH 133 633 106 HOH HOH B . 
L 5 HOH 134 634 188 HOH HOH B . 
L 5 HOH 135 635 301 HOH HOH B . 
L 5 HOH 136 636 217 HOH HOH B . 
L 5 HOH 137 637 192 HOH HOH B . 
L 5 HOH 138 638 56  HOH HOH B . 
L 5 HOH 139 639 33  HOH HOH B . 
L 5 HOH 140 640 202 HOH HOH B . 
L 5 HOH 141 641 216 HOH HOH B . 
L 5 HOH 142 642 130 HOH HOH B . 
L 5 HOH 143 643 325 HOH HOH B . 
L 5 HOH 144 644 226 HOH HOH B . 
L 5 HOH 145 645 312 HOH HOH B . 
L 5 HOH 146 646 82  HOH HOH B . 
L 5 HOH 147 647 80  HOH HOH B . 
L 5 HOH 148 648 67  HOH HOH B . 
L 5 HOH 149 649 132 HOH HOH B . 
L 5 HOH 150 650 289 HOH HOH B . 
L 5 HOH 151 651 293 HOH HOH B . 
L 5 HOH 152 652 336 HOH HOH B . 
L 5 HOH 153 653 295 HOH HOH B . 
L 5 HOH 154 654 175 HOH HOH B . 
L 5 HOH 155 655 307 HOH HOH B . 
L 5 HOH 156 656 385 HOH HOH B . 
L 5 HOH 157 657 236 HOH HOH B . 
L 5 HOH 158 658 315 HOH HOH B . 
L 5 HOH 159 659 228 HOH HOH B . 
L 5 HOH 160 660 291 HOH HOH B . 
L 5 HOH 161 661 197 HOH HOH B . 
L 5 HOH 162 662 229 HOH HOH B . 
L 5 HOH 163 663 373 HOH HOH B . 
L 5 HOH 164 664 342 HOH HOH B . 
L 5 HOH 165 665 77  HOH HOH B . 
L 5 HOH 166 666 287 HOH HOH B . 
L 5 HOH 167 667 327 HOH HOH B . 
L 5 HOH 168 668 367 HOH HOH B . 
L 5 HOH 169 669 215 HOH HOH B . 
L 5 HOH 170 670 214 HOH HOH B . 
L 5 HOH 171 671 233 HOH HOH B . 
L 5 HOH 172 672 319 HOH HOH B . 
L 5 HOH 173 673 395 HOH HOH B . 
L 5 HOH 174 674 204 HOH HOH B . 
L 5 HOH 175 675 383 HOH HOH B . 
L 5 HOH 176 676 210 HOH HOH B . 
L 5 HOH 177 677 374 HOH HOH B . 
L 5 HOH 178 678 306 HOH HOH B . 
L 5 HOH 179 679 344 HOH HOH B . 
L 5 HOH 180 680 176 HOH HOH B . 
L 5 HOH 181 681 155 HOH HOH B . 
L 5 HOH 182 682 302 HOH HOH B . 
L 5 HOH 183 683 318 HOH HOH B . 
L 5 HOH 184 684 127 HOH HOH B . 
L 5 HOH 185 685 111 HOH HOH B . 
L 5 HOH 186 686 355 HOH HOH B . 
L 5 HOH 187 687 212 HOH HOH B . 
L 5 HOH 188 688 222 HOH HOH B . 
L 5 HOH 189 689 388 HOH HOH B . 
L 5 HOH 190 690 353 HOH HOH B . 
L 5 HOH 191 691 311 HOH HOH B . 
L 5 HOH 192 692 85  HOH HOH B . 
L 5 HOH 193 693 340 HOH HOH B . 
L 5 HOH 194 694 235 HOH HOH B . 
L 5 HOH 195 695 300 HOH HOH B . 
L 5 HOH 196 696 387 HOH HOH B . 
M 5 HOH 1   101 341 HOH HOH C . 
M 5 HOH 2   102 251 HOH HOH C . 
M 5 HOH 3   103 20  HOH HOH C . 
M 5 HOH 4   104 31  HOH HOH C . 
M 5 HOH 5   105 10  HOH HOH C . 
N 5 HOH 1   101 304 HOH HOH D . 
N 5 HOH 2   102 4   HOH HOH D . 
N 5 HOH 3   103 345 HOH HOH D . 
N 5 HOH 4   104 303 HOH HOH D . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .        4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FKU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.765 
_cell.length_a_esd                 ? 
_cell.length_b                     203.582 
_cell.length_b_esd                 ? 
_cell.length_c                     143.069 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9FKU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FKU 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.62 
_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    '15% pentaeritritol ethoxilate, 3% jeffamine, 0.2M Potassium Acetate, 0.1M MES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-30 
_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   0.97918 
_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                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FKU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.9 
_reflns.d_resolution_low                               48.64 
_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                                     80454 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.9 
_reflns_shell.d_res_low                                     1.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7816 
_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                               6.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.664 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0 
_refine.aniso_B[1][2]                            -0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -0.12 
_refine.aniso_B[2][3]                            -0 
_refine.aniso_B[3][3]                            0.12 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.967 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_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                                 9FKU 
_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                            1.9 
_refine.ls_d_res_low                             48.69 
_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                     76351 
_refine.ls_number_reflns_R_free                  4067 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17999 
_refine.ls_R_factor_R_free                       0.21206 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17829 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_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                            ? 
_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                       1.9 
_refine_hist.d_res_low                        48.69 
_refine_hist.number_atoms_solvent             396 
_refine_hist.number_atoms_total               6864 
_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        6432 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.9 
_refine_ls_shell.d_res_low                        1.949 
_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               99.98 
_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                  0.321 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.326 
# 
_struct.entry_id                     9FKU 
_struct.title                        'Crystal Structure of AimR from Katmira phage' 
_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        9FKU 
_struct_keywords.text            'Arbitrium receptor, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A8I3AZZ2_BACIU A0A8I3AZZ2 ? 1 
;MELIRIAMKKDLENDNSLMNKWATVAGLKNPNPLYDFLNHDGKTFNEFSSIVNIVKSQYPDREYELMKDYCLNLDVKTKA
ARSALEYADANMFFEIEDALIDSMISCSNMKSKEYGKVYKIHRELSKGEIDVFEASANIGKQRIKTAEMNIFSKMLLMYD
CLNKGNFAPMMLLFQQIDLSEIKENRYLKNSFETRINVLLSNIYLNENNLELCREYAQKAISSTDTQRFLVFSYLTIGTS
YIFSDFNLSKQNYLIGLKFAKGNPGFEEFFKRNLSFLNNFWNKENEWINYDSDAVTDMQEVIFELINHKELSKALQLLNK
LEERDQNENELGFHYYLKGLITNEKEAFFKSVEYFKASQDKLSIKMPLIQLEKMGENPRLLKIITM
;
2 
2 PDB 9FKU             9FKU       ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FKU A 1 ? 386 ? A0A8I3AZZ2 2 ? 387 ? 1 386 
2 1 9FKU B 1 ? 386 ? A0A8I3AZZ2 2 ? 387 ? 1 386 
3 2 9FKU C 1 ? 6   ? 9FKU       1 ? 6   ? 1 6   
4 2 9FKU D 1 ? 6   ? 9FKU       1 ? 6   ? 1 6   
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 5850  ? 
1 MORE         -44   ? 
1 'SSA (A^2)'  34600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 2   ? ASN A 14  ? GLU A 2   ASN A 14  1 ? 13 
HELX_P HELX_P2  AA2 SER A 17  ? ALA A 26  ? SER A 17  ALA A 26  1 ? 10 
HELX_P HELX_P3  AA3 PRO A 31  ? HIS A 40  ? PRO A 31  HIS A 40  1 ? 10 
HELX_P HELX_P4  AA4 PHE A 48  ? TYR A 59  ? PHE A 48  TYR A 59  1 ? 12 
HELX_P HELX_P5  AA5 ARG A 62  ? ASN A 73  ? ARG A 62  ASN A 73  1 ? 12 
HELX_P HELX_P6  AA6 THR A 78  ? MET A 92  ? THR A 78  MET A 92  1 ? 15 
HELX_P HELX_P7  AA7 PHE A 93  ? SER A 106 ? PHE A 93  SER A 106 1 ? 14 
HELX_P HELX_P8  AA8 ASN A 109 ? LYS A 127 ? ASN A 109 LYS A 127 1 ? 19 
HELX_P HELX_P9  AA9 ASP A 131 ? ARG A 143 ? ASP A 131 ARG A 143 1 ? 13 
HELX_P HELX_P10 AB1 THR A 146 ? LYS A 164 ? THR A 146 LYS A 164 1 ? 19 
HELX_P HELX_P11 AB2 ALA A 168 ? GLN A 176 ? ALA A 168 GLN A 176 1 ? 9  
HELX_P HELX_P12 AB3 ILE A 177 ? ILE A 182 ? ILE A 177 ILE A 182 5 ? 6  
HELX_P HELX_P13 AB4 ASN A 185 ? GLU A 207 ? ASN A 185 GLU A 207 1 ? 23 
HELX_P HELX_P14 AB5 ASN A 209 ? THR A 224 ? ASN A 209 THR A 224 1 ? 16 
HELX_P HELX_P15 AB6 THR A 226 ? TYR A 241 ? THR A 226 TYR A 241 1 ? 16 
HELX_P HELX_P16 AB7 ASP A 245 ? ALA A 260 ? ASP A 245 ALA A 260 1 ? 16 
HELX_P HELX_P17 AB8 ASN A 263 ? TRP A 281 ? ASN A 263 TRP A 281 1 ? 19 
HELX_P HELX_P18 AB9 ALA A 294 ? HIS A 308 ? ALA A 294 HIS A 308 1 ? 15 
HELX_P HELX_P19 AC1 GLU A 310 ? GLU A 322 ? GLU A 310 GLU A 322 1 ? 13 
HELX_P HELX_P20 AC2 ASN A 327 ? ASN A 343 ? ASN A 327 ASN A 343 1 ? 17 
HELX_P HELX_P21 AC3 GLU A 344 ? GLN A 359 ? GLU A 344 GLN A 359 1 ? 16 
HELX_P HELX_P22 AC4 ILE A 364 ? MET A 374 ? ILE A 364 MET A 374 1 ? 11 
HELX_P HELX_P23 AC5 ASN A 377 ? MET A 386 ? ASN A 377 MET A 386 1 ? 10 
HELX_P HELX_P24 AC6 GLU B 2   ? ASP B 15  ? GLU B 2   ASP B 15  1 ? 14 
HELX_P HELX_P25 AC7 SER B 17  ? ALA B 26  ? SER B 17  ALA B 26  1 ? 10 
HELX_P HELX_P26 AC8 PRO B 31  ? HIS B 40  ? PRO B 31  HIS B 40  1 ? 10 
HELX_P HELX_P27 AC9 PHE B 48  ? TYR B 59  ? PHE B 48  TYR B 59  1 ? 12 
HELX_P HELX_P28 AD1 ARG B 62  ? ASN B 73  ? ARG B 62  ASN B 73  1 ? 12 
HELX_P HELX_P29 AD2 THR B 78  ? MET B 92  ? THR B 78  MET B 92  1 ? 15 
HELX_P HELX_P30 AD3 PHE B 93  ? SER B 106 ? PHE B 93  SER B 106 1 ? 14 
HELX_P HELX_P31 AD4 ASN B 109 ? LYS B 127 ? ASN B 109 LYS B 127 1 ? 19 
HELX_P HELX_P32 AD5 ASP B 131 ? ARG B 143 ? ASP B 131 ARG B 143 1 ? 13 
HELX_P HELX_P33 AD6 THR B 146 ? LYS B 164 ? THR B 146 LYS B 164 1 ? 19 
HELX_P HELX_P34 AD7 ALA B 168 ? GLN B 176 ? ALA B 168 GLN B 176 1 ? 9  
HELX_P HELX_P35 AD8 ILE B 177 ? ILE B 182 ? ILE B 177 ILE B 182 5 ? 6  
HELX_P HELX_P36 AD9 ASN B 185 ? GLU B 207 ? ASN B 185 GLU B 207 1 ? 23 
HELX_P HELX_P37 AE1 ASN B 209 ? SER B 223 ? ASN B 209 SER B 223 1 ? 15 
HELX_P HELX_P38 AE2 THR B 226 ? TYR B 241 ? THR B 226 TYR B 241 1 ? 16 
HELX_P HELX_P39 AE3 ASP B 245 ? LYS B 261 ? ASP B 245 LYS B 261 1 ? 17 
HELX_P HELX_P40 AE4 ASN B 263 ? TRP B 281 ? ASN B 263 TRP B 281 1 ? 19 
HELX_P HELX_P41 AE5 ALA B 294 ? HIS B 308 ? ALA B 294 HIS B 308 1 ? 15 
HELX_P HELX_P42 AE6 GLU B 310 ? GLU B 323 ? GLU B 310 GLU B 323 1 ? 14 
HELX_P HELX_P43 AE7 ASN B 327 ? ASN B 343 ? ASN B 327 ASN B 343 1 ? 17 
HELX_P HELX_P44 AE8 GLU B 344 ? GLN B 359 ? GLU B 344 GLN B 359 1 ? 16 
HELX_P HELX_P45 AE9 ILE B 364 ? MET B 374 ? ILE B 364 MET B 374 1 ? 11 
HELX_P HELX_P46 AF1 ASN B 377 ? THR B 385 ? ASN B 377 THR B 385 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9FKU 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 508 ? ? O A HOH 684 ? ? 2.08 
2 1 OE1 B GLU 215 ? ? O B HOH 501 ? ? 2.10 
3 1 OE1 B GLU 134 ? ? O B HOH 502 ? ? 2.14 
4 1 NH2 C ARG 4   ? ? O C HOH 101 ? ? 2.15 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A MET 19 ? ? SD A MET 19 ? ? CE A MET 19 ? ? 87.83  100.20 -12.37 1.60 N 
2 1 CG B MET 1  ? ? SD B MET 1  ? ? CE B MET 1  ? ? 110.20 100.20 10.00  1.60 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 ASP A 15  ? ? -170.65 98.53 
2 1 ASN A 209 ? ? -104.87 73.28 
3 1 ASN A 209 ? ? -101.65 68.45 
4 1 GLU A 310 ? ? -100.86 65.24 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 186 ? ? 0.079 'SIDE CHAIN' 
2 1 ARG A 272 ? ? 0.089 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 620 ? L HOH . 
2 1 B HOH 696 ? L HOH . 
# 
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' ? ? 22.8598 43.4859 10.4793 0.0476 ? 0.0225  ? -0.0249 ? 0.051  ? -0.0301 ? 0.0222 ? 1.0053 ? -0.036  ? 
-0.2172 ? 1.3143 ? 0.253   ? 1.6087 ? -0.0614 ? 0.2249  ? 0.1123 ? 0.2249  ? 0.0859 ? -0.0199 ? 0.1123 ? -0.0199 ? -0.0245 ? 
2 'X-RAY DIFFRACTION' ? ? -9.23   17.394  2.22    0.0978 ? -0.0173 ? -0.013  ? 0.0201 ? 0.0188  ? 0.0702 ? 0.9506 ? 0.0413  ? 
-0.4442 ? 1.029  ? 0.2801  ? 1.6182 ? -0.049  ? 0.0794  ? 0.0872 ? 0.0794  ? 0.0303 ? -0.0397 ? 0.0872 ? -0.0397 ? 0.0187  ? 
3 'X-RAY DIFFRACTION' ? ? 25.5987 41.329  1.4206  0.1296 ? -0.0137 ? 0.0151  ? 0.059  ? -0.029  ? 0.0769 ? 5.621  ? -2.6558 ? 
-6.3037 ? 3.5932 ? 2.4849  ? 7.1835 ? -0.3061 ? -0.0404 ? 0.4182 ? -0.0404 ? 0.1127 ? 0.0843  ? 0.4182 ? 0.0843  ? 0.1934  ? 
4 'X-RAY DIFFRACTION' ? ? -5.8409 17.8081 -6.8504 0.0935 ? -0.0222 ? 0.0118  ? 0.0466 ? -0.0015 ? 0.1108 ? 0.3713 ? 0.1965  ? 
-0.1174 ? 2.5374 ? -2.3095 ? 6.0599 ? 0.0937  ? -0.0426 ? -0.237 ? -0.0426 ? 0.0547 ? 0.16    ? -0.237 ? 0.16    ? -0.1484 ? 
# 
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 ? ? A 1 ? ? ? A 386 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 1 ? ? ? B 386 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? C 1 ? ? ? C 6   ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? D 1 ? ? ? D 6   ? ? ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       696 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.18 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
ACT C    C N N 1   
ACT O    O N N 2   
ACT OXT  O N N 3   
ACT CH3  C N N 4   
ACT H1   H N N 5   
ACT H2   H N N 6   
ACT H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
GLN N    N N N 95  
GLN CA   C N S 96  
GLN C    C N N 97  
GLN O    O N N 98  
GLN CB   C N N 99  
GLN CG   C N N 100 
GLN CD   C N N 101 
GLN OE1  O N N 102 
GLN NE2  N N N 103 
GLN OXT  O N N 104 
GLN H    H N N 105 
GLN H2   H N N 106 
GLN HA   H N N 107 
GLN HB2  H N N 108 
GLN HB3  H N N 109 
GLN HG2  H N N 110 
GLN HG3  H N N 111 
GLN HE21 H N N 112 
GLN HE22 H N N 113 
GLN HXT  H N N 114 
GLU N    N N N 115 
GLU CA   C N S 116 
GLU C    C N N 117 
GLU O    O N N 118 
GLU CB   C N N 119 
GLU CG   C N N 120 
GLU CD   C N N 121 
GLU OE1  O N N 122 
GLU OE2  O N N 123 
GLU OXT  O N N 124 
GLU H    H N N 125 
GLU H2   H N N 126 
GLU HA   H N N 127 
GLU HB2  H N N 128 
GLU HB3  H N N 129 
GLU HG2  H N N 130 
GLU HG3  H N N 131 
GLU HE2  H N N 132 
GLU HXT  H N N 133 
GLY N    N N N 134 
GLY CA   C N N 135 
GLY C    C N N 136 
GLY O    O N N 137 
GLY OXT  O N N 138 
GLY H    H N N 139 
GLY H2   H N N 140 
GLY HA2  H N N 141 
GLY HA3  H N N 142 
GLY HXT  H N N 143 
HIS N    N N N 144 
HIS CA   C N S 145 
HIS C    C N N 146 
HIS O    O N N 147 
HIS CB   C N N 148 
HIS CG   C Y N 149 
HIS ND1  N Y N 150 
HIS CD2  C Y N 151 
HIS CE1  C Y N 152 
HIS NE2  N Y N 153 
HIS OXT  O N N 154 
HIS H    H N N 155 
HIS H2   H N N 156 
HIS HA   H N N 157 
HIS HB2  H N N 158 
HIS HB3  H N N 159 
HIS HD1  H N N 160 
HIS HD2  H N N 161 
HIS HE1  H N N 162 
HIS HE2  H N N 163 
HIS HXT  H N N 164 
HOH O    O N N 165 
HOH H1   H N N 166 
HOH H2   H N N 167 
ILE N    N N N 168 
ILE CA   C N S 169 
ILE C    C N N 170 
ILE O    O N N 171 
ILE CB   C N S 172 
ILE CG1  C N N 173 
ILE CG2  C N N 174 
ILE CD1  C N N 175 
ILE OXT  O N N 176 
ILE H    H N N 177 
ILE H2   H N N 178 
ILE HA   H N N 179 
ILE HB   H N N 180 
ILE HG12 H N N 181 
ILE HG13 H N N 182 
ILE HG21 H N N 183 
ILE HG22 H N N 184 
ILE HG23 H N N 185 
ILE HD11 H N N 186 
ILE HD12 H N N 187 
ILE HD13 H N N 188 
ILE HXT  H N N 189 
LEU N    N N N 190 
LEU CA   C N S 191 
LEU C    C N N 192 
LEU O    O N N 193 
LEU CB   C N N 194 
LEU CG   C N N 195 
LEU CD1  C N N 196 
LEU CD2  C N N 197 
LEU OXT  O N N 198 
LEU H    H N N 199 
LEU H2   H N N 200 
LEU HA   H N N 201 
LEU HB2  H N N 202 
LEU HB3  H N N 203 
LEU HG   H N N 204 
LEU HD11 H N N 205 
LEU HD12 H N N 206 
LEU HD13 H N N 207 
LEU HD21 H N N 208 
LEU HD22 H N N 209 
LEU HD23 H N N 210 
LEU HXT  H N N 211 
LYS N    N N N 212 
LYS CA   C N S 213 
LYS C    C N N 214 
LYS O    O N N 215 
LYS CB   C N N 216 
LYS CG   C N N 217 
LYS CD   C N N 218 
LYS CE   C N N 219 
LYS NZ   N N N 220 
LYS OXT  O N N 221 
LYS H    H N N 222 
LYS H2   H N N 223 
LYS HA   H N N 224 
LYS HB2  H N N 225 
LYS HB3  H N N 226 
LYS HG2  H N N 227 
LYS HG3  H N N 228 
LYS HD2  H N N 229 
LYS HD3  H N N 230 
LYS HE2  H N N 231 
LYS HE3  H N N 232 
LYS HZ1  H N N 233 
LYS HZ2  H N N 234 
LYS HZ3  H N N 235 
LYS HXT  H N N 236 
MET N    N N N 237 
MET CA   C N S 238 
MET C    C N N 239 
MET O    O N N 240 
MET CB   C N N 241 
MET CG   C N N 242 
MET SD   S N N 243 
MET CE   C N N 244 
MET OXT  O N N 245 
MET H    H N N 246 
MET H2   H N N 247 
MET HA   H N N 248 
MET HB2  H N N 249 
MET HB3  H N N 250 
MET HG2  H N N 251 
MET HG3  H N N 252 
MET HE1  H N N 253 
MET HE2  H N N 254 
MET HE3  H N N 255 
MET HXT  H N N 256 
MPD C1   C N N 257 
MPD C2   C N N 258 
MPD O2   O N N 259 
MPD CM   C N N 260 
MPD C3   C N N 261 
MPD C4   C N S 262 
MPD O4   O N N 263 
MPD C5   C N N 264 
MPD H11  H N N 265 
MPD H12  H N N 266 
MPD H13  H N N 267 
MPD HO2  H N N 268 
MPD HM1  H N N 269 
MPD HM2  H N N 270 
MPD HM3  H N N 271 
MPD H31  H N N 272 
MPD H32  H N N 273 
MPD H4   H N N 274 
MPD HO4  H N N 275 
MPD H51  H N N 276 
MPD H52  H N N 277 
MPD H53  H N N 278 
PHE N    N N N 279 
PHE CA   C N S 280 
PHE C    C N N 281 
PHE O    O N N 282 
PHE CB   C N N 283 
PHE CG   C Y N 284 
PHE CD1  C Y N 285 
PHE CD2  C Y N 286 
PHE CE1  C Y N 287 
PHE CE2  C Y N 288 
PHE CZ   C Y N 289 
PHE OXT  O N N 290 
PHE H    H N N 291 
PHE H2   H N N 292 
PHE HA   H N N 293 
PHE HB2  H N N 294 
PHE HB3  H N N 295 
PHE HD1  H N N 296 
PHE HD2  H N N 297 
PHE HE1  H N N 298 
PHE HE2  H N N 299 
PHE HZ   H N N 300 
PHE HXT  H N N 301 
PRO N    N N N 302 
PRO CA   C N S 303 
PRO C    C N N 304 
PRO O    O N N 305 
PRO CB   C N N 306 
PRO CG   C N N 307 
PRO CD   C N N 308 
PRO OXT  O N N 309 
PRO H    H N N 310 
PRO HA   H N N 311 
PRO HB2  H N N 312 
PRO HB3  H N N 313 
PRO HG2  H N N 314 
PRO HG3  H N N 315 
PRO HD2  H N N 316 
PRO HD3  H N N 317 
PRO HXT  H N N 318 
SER N    N N N 319 
SER CA   C N S 320 
SER C    C N N 321 
SER O    O N N 322 
SER CB   C N N 323 
SER OG   O N N 324 
SER OXT  O N N 325 
SER H    H N N 326 
SER H2   H N N 327 
SER HA   H N N 328 
SER HB2  H N N 329 
SER HB3  H N N 330 
SER HG   H N N 331 
SER HXT  H N N 332 
THR N    N N N 333 
THR CA   C N S 334 
THR C    C N N 335 
THR O    O N N 336 
THR CB   C N R 337 
THR OG1  O N N 338 
THR CG2  C N N 339 
THR OXT  O N N 340 
THR H    H N N 341 
THR H2   H N N 342 
THR HA   H N N 343 
THR HB   H N N 344 
THR HG1  H N N 345 
THR HG21 H N N 346 
THR HG22 H N N 347 
THR HG23 H N N 348 
THR HXT  H N N 349 
TRP N    N N N 350 
TRP CA   C N S 351 
TRP C    C N N 352 
TRP O    O N N 353 
TRP CB   C N N 354 
TRP CG   C Y N 355 
TRP CD1  C Y N 356 
TRP CD2  C Y N 357 
TRP NE1  N Y N 358 
TRP CE2  C Y N 359 
TRP CE3  C Y N 360 
TRP CZ2  C Y N 361 
TRP CZ3  C Y N 362 
TRP CH2  C Y N 363 
TRP OXT  O N N 364 
TRP H    H N N 365 
TRP H2   H N N 366 
TRP HA   H N N 367 
TRP HB2  H N N 368 
TRP HB3  H N N 369 
TRP HD1  H N N 370 
TRP HE1  H N N 371 
TRP HE3  H N N 372 
TRP HZ2  H N N 373 
TRP HZ3  H N N 374 
TRP HH2  H N N 375 
TRP HXT  H N N 376 
TYR N    N N N 377 
TYR CA   C N S 378 
TYR C    C N N 379 
TYR O    O N N 380 
TYR CB   C N N 381 
TYR CG   C Y N 382 
TYR CD1  C Y N 383 
TYR CD2  C Y N 384 
TYR CE1  C Y N 385 
TYR CE2  C Y N 386 
TYR CZ   C Y N 387 
TYR OH   O N N 388 
TYR OXT  O N N 389 
TYR H    H N N 390 
TYR H2   H N N 391 
TYR HA   H N N 392 
TYR HB2  H N N 393 
TYR HB3  H N N 394 
TYR HD1  H N N 395 
TYR HD2  H N N 396 
TYR HE1  H N N 397 
TYR HE2  H N N 398 
TYR HH   H N N 399 
TYR HXT  H N N 400 
VAL N    N N N 401 
VAL CA   C N S 402 
VAL C    C N N 403 
VAL O    O N N 404 
VAL CB   C N N 405 
VAL CG1  C N N 406 
VAL CG2  C N N 407 
VAL OXT  O N N 408 
VAL H    H N N 409 
VAL H2   H N N 410 
VAL HA   H N N 411 
VAL HB   H N N 412 
VAL HG11 H N N 413 
VAL HG12 H N N 414 
VAL HG13 H N N 415 
VAL HG21 H N N 416 
VAL HG22 H N N 417 
VAL HG23 H N N 418 
VAL HXT  H N N 419 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
HIS N   CA   sing N N 135 
HIS N   H    sing N N 136 
HIS N   H2   sing N N 137 
HIS CA  C    sing N N 138 
HIS CA  CB   sing N N 139 
HIS CA  HA   sing N N 140 
HIS C   O    doub N N 141 
HIS C   OXT  sing N N 142 
HIS CB  CG   sing N N 143 
HIS CB  HB2  sing N N 144 
HIS CB  HB3  sing N N 145 
HIS CG  ND1  sing Y N 146 
HIS CG  CD2  doub Y N 147 
HIS ND1 CE1  doub Y N 148 
HIS ND1 HD1  sing N N 149 
HIS CD2 NE2  sing Y N 150 
HIS CD2 HD2  sing N N 151 
HIS CE1 NE2  sing Y N 152 
HIS CE1 HE1  sing N N 153 
HIS NE2 HE2  sing N N 154 
HIS OXT HXT  sing N N 155 
HOH O   H1   sing N N 156 
HOH O   H2   sing N N 157 
ILE N   CA   sing N N 158 
ILE N   H    sing N N 159 
ILE N   H2   sing N N 160 
ILE CA  C    sing N N 161 
ILE CA  CB   sing N N 162 
ILE CA  HA   sing N N 163 
ILE C   O    doub N N 164 
ILE C   OXT  sing N N 165 
ILE CB  CG1  sing N N 166 
ILE CB  CG2  sing N N 167 
ILE CB  HB   sing N N 168 
ILE CG1 CD1  sing N N 169 
ILE CG1 HG12 sing N N 170 
ILE CG1 HG13 sing N N 171 
ILE CG2 HG21 sing N N 172 
ILE CG2 HG22 sing N N 173 
ILE CG2 HG23 sing N N 174 
ILE CD1 HD11 sing N N 175 
ILE CD1 HD12 sing N N 176 
ILE CD1 HD13 sing N N 177 
ILE OXT HXT  sing N N 178 
LEU N   CA   sing N N 179 
LEU N   H    sing N N 180 
LEU N   H2   sing N N 181 
LEU CA  C    sing N N 182 
LEU CA  CB   sing N N 183 
LEU CA  HA   sing N N 184 
LEU C   O    doub N N 185 
LEU C   OXT  sing N N 186 
LEU CB  CG   sing N N 187 
LEU CB  HB2  sing N N 188 
LEU CB  HB3  sing N N 189 
LEU CG  CD1  sing N N 190 
LEU CG  CD2  sing N N 191 
LEU CG  HG   sing N N 192 
LEU CD1 HD11 sing N N 193 
LEU CD1 HD12 sing N N 194 
LEU CD1 HD13 sing N N 195 
LEU CD2 HD21 sing N N 196 
LEU CD2 HD22 sing N N 197 
LEU CD2 HD23 sing N N 198 
LEU OXT HXT  sing N N 199 
LYS N   CA   sing N N 200 
LYS N   H    sing N N 201 
LYS N   H2   sing N N 202 
LYS CA  C    sing N N 203 
LYS CA  CB   sing N N 204 
LYS CA  HA   sing N N 205 
LYS C   O    doub N N 206 
LYS C   OXT  sing N N 207 
LYS CB  CG   sing N N 208 
LYS CB  HB2  sing N N 209 
LYS CB  HB3  sing N N 210 
LYS CG  CD   sing N N 211 
LYS CG  HG2  sing N N 212 
LYS CG  HG3  sing N N 213 
LYS CD  CE   sing N N 214 
LYS CD  HD2  sing N N 215 
LYS CD  HD3  sing N N 216 
LYS CE  NZ   sing N N 217 
LYS CE  HE2  sing N N 218 
LYS CE  HE3  sing N N 219 
LYS NZ  HZ1  sing N N 220 
LYS NZ  HZ2  sing N N 221 
LYS NZ  HZ3  sing N N 222 
LYS OXT HXT  sing N N 223 
MET N   CA   sing N N 224 
MET N   H    sing N N 225 
MET N   H2   sing N N 226 
MET CA  C    sing N N 227 
MET CA  CB   sing N N 228 
MET CA  HA   sing N N 229 
MET C   O    doub N N 230 
MET C   OXT  sing N N 231 
MET CB  CG   sing N N 232 
MET CB  HB2  sing N N 233 
MET CB  HB3  sing N N 234 
MET CG  SD   sing N N 235 
MET CG  HG2  sing N N 236 
MET CG  HG3  sing N N 237 
MET SD  CE   sing N N 238 
MET CE  HE1  sing N N 239 
MET CE  HE2  sing N N 240 
MET CE  HE3  sing N N 241 
MET OXT HXT  sing N N 242 
MPD C1  C2   sing N N 243 
MPD C1  H11  sing N N 244 
MPD C1  H12  sing N N 245 
MPD C1  H13  sing N N 246 
MPD C2  O2   sing N N 247 
MPD C2  CM   sing N N 248 
MPD C2  C3   sing N N 249 
MPD O2  HO2  sing N N 250 
MPD CM  HM1  sing N N 251 
MPD CM  HM2  sing N N 252 
MPD CM  HM3  sing N N 253 
MPD C3  C4   sing N N 254 
MPD C3  H31  sing N N 255 
MPD C3  H32  sing N N 256 
MPD C4  O4   sing N N 257 
MPD C4  C5   sing N N 258 
MPD C4  H4   sing N N 259 
MPD O4  HO4  sing N N 260 
MPD C5  H51  sing N N 261 
MPD C5  H52  sing N N 262 
MPD C5  H53  sing N N 263 
PHE N   CA   sing N N 264 
PHE N   H    sing N N 265 
PHE N   H2   sing N N 266 
PHE CA  C    sing N N 267 
PHE CA  CB   sing N N 268 
PHE CA  HA   sing N N 269 
PHE C   O    doub N N 270 
PHE C   OXT  sing N N 271 
PHE CB  CG   sing N N 272 
PHE CB  HB2  sing N N 273 
PHE CB  HB3  sing N N 274 
PHE CG  CD1  doub Y N 275 
PHE CG  CD2  sing Y N 276 
PHE CD1 CE1  sing Y N 277 
PHE CD1 HD1  sing N N 278 
PHE CD2 CE2  doub Y N 279 
PHE CD2 HD2  sing N N 280 
PHE CE1 CZ   doub Y N 281 
PHE CE1 HE1  sing N N 282 
PHE CE2 CZ   sing Y N 283 
PHE CE2 HE2  sing N N 284 
PHE CZ  HZ   sing N N 285 
PHE OXT HXT  sing N N 286 
PRO N   CA   sing N N 287 
PRO N   CD   sing N N 288 
PRO N   H    sing N N 289 
PRO CA  C    sing N N 290 
PRO CA  CB   sing N N 291 
PRO CA  HA   sing N N 292 
PRO C   O    doub N N 293 
PRO C   OXT  sing N N 294 
PRO CB  CG   sing N N 295 
PRO CB  HB2  sing N N 296 
PRO CB  HB3  sing N N 297 
PRO CG  CD   sing N N 298 
PRO CG  HG2  sing N N 299 
PRO CG  HG3  sing N N 300 
PRO CD  HD2  sing N N 301 
PRO CD  HD3  sing N N 302 
PRO OXT HXT  sing N N 303 
SER N   CA   sing N N 304 
SER N   H    sing N N 305 
SER N   H2   sing N N 306 
SER CA  C    sing N N 307 
SER CA  CB   sing N N 308 
SER CA  HA   sing N N 309 
SER C   O    doub N N 310 
SER C   OXT  sing N N 311 
SER CB  OG   sing N N 312 
SER CB  HB2  sing N N 313 
SER CB  HB3  sing N N 314 
SER OG  HG   sing N N 315 
SER OXT HXT  sing N N 316 
THR N   CA   sing N N 317 
THR N   H    sing N N 318 
THR N   H2   sing N N 319 
THR CA  C    sing N N 320 
THR CA  CB   sing N N 321 
THR CA  HA   sing N N 322 
THR C   O    doub N N 323 
THR C   OXT  sing N N 324 
THR CB  OG1  sing N N 325 
THR CB  CG2  sing N N 326 
THR CB  HB   sing N N 327 
THR OG1 HG1  sing N N 328 
THR CG2 HG21 sing N N 329 
THR CG2 HG22 sing N N 330 
THR CG2 HG23 sing N N 331 
THR OXT HXT  sing N N 332 
TRP N   CA   sing N N 333 
TRP N   H    sing N N 334 
TRP N   H2   sing N N 335 
TRP CA  C    sing N N 336 
TRP CA  CB   sing N N 337 
TRP CA  HA   sing N N 338 
TRP C   O    doub N N 339 
TRP C   OXT  sing N N 340 
TRP CB  CG   sing N N 341 
TRP CB  HB2  sing N N 342 
TRP CB  HB3  sing N N 343 
TRP CG  CD1  doub Y N 344 
TRP CG  CD2  sing Y N 345 
TRP CD1 NE1  sing Y N 346 
TRP CD1 HD1  sing N N 347 
TRP CD2 CE2  doub Y N 348 
TRP CD2 CE3  sing Y N 349 
TRP NE1 CE2  sing Y N 350 
TRP NE1 HE1  sing N N 351 
TRP CE2 CZ2  sing Y N 352 
TRP CE3 CZ3  doub Y N 353 
TRP CE3 HE3  sing N N 354 
TRP CZ2 CH2  doub Y N 355 
TRP CZ2 HZ2  sing N N 356 
TRP CZ3 CH2  sing Y N 357 
TRP CZ3 HZ3  sing N N 358 
TRP CH2 HH2  sing N N 359 
TRP OXT HXT  sing N N 360 
TYR N   CA   sing N N 361 
TYR N   H    sing N N 362 
TYR N   H2   sing N N 363 
TYR CA  C    sing N N 364 
TYR CA  CB   sing N N 365 
TYR CA  HA   sing N N 366 
TYR C   O    doub N N 367 
TYR C   OXT  sing N N 368 
TYR CB  CG   sing N N 369 
TYR CB  HB2  sing N N 370 
TYR CB  HB3  sing N N 371 
TYR CG  CD1  doub Y N 372 
TYR CG  CD2  sing Y N 373 
TYR CD1 CE1  sing Y N 374 
TYR CD1 HD1  sing N N 375 
TYR CD2 CE2  doub Y N 376 
TYR CD2 HD2  sing N N 377 
TYR CE1 CZ   doub Y N 378 
TYR CE1 HE1  sing N N 379 
TYR CE2 CZ   sing Y N 380 
TYR CE2 HE2  sing N N 381 
TYR CZ  OH   sing N N 382 
TYR OH  HH   sing N N 383 
TYR OXT HXT  sing N N 384 
VAL N   CA   sing N N 385 
VAL N   H    sing N N 386 
VAL N   H2   sing N N 387 
VAL CA  C    sing N N 388 
VAL CA  CB   sing N N 389 
VAL CA  HA   sing N N 390 
VAL C   O    doub N N 391 
VAL C   OXT  sing N N 392 
VAL CB  CG1  sing N N 393 
VAL CB  CG2  sing N N 394 
VAL CB  HB   sing N N 395 
VAL CG1 HG11 sing N N 396 
VAL CG1 HG12 sing N N 397 
VAL CG1 HG13 sing N N 398 
VAL CG2 HG21 sing N N 399 
VAL CG2 HG22 sing N N 400 
VAL CG2 HG23 sing N N 401 
VAL OXT HXT  sing N N 402 
# 
_pdbx_audit_support.funding_organization   'Ministerio de Ciencia e Innovacion (MCIN)' 
_pdbx_audit_support.country                Spain 
_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   6S7I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FKU 
_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]   0.014334 
_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]   0.004912 
_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]   0.006990 
_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 
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   . MET A 1 1   ? 28.64   53.687  42.645  1   81.32  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 27.925  54.874  42.101  1   78.05  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 28.215  55.018  40.605  1   70.1   ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 29.362  55.203  40.211  1   67.1   ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 28.367  56.145  42.836  1   83     ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 27.805  57.45   42.277  1   84.35  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 26.02   57.628  42.481  1   87.6   ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 25.915  59.415  42.689  1   79.09  ? 1   MET A CE  1 
ATOM   9    N N   . GLU A 1 2   ? 27.17   55.052  39.771  1   61.84  ? 2   GLU A N   1 
ATOM   10   C CA  . GLU A 1 2   ? 27.404  54.986  38.339  1   61.37  ? 2   GLU A CA  1 
ATOM   11   C C   . GLU A 1 2   ? 27.712  56.39   37.805  1   57.87  ? 2   GLU A C   1 
ATOM   12   O O   . GLU A 1 2   ? 27.222  57.404  38.328  1   60.05  ? 2   GLU A O   1 
ATOM   13   C CB  . GLU A 1 2   ? 26.349  54.258  37.496  1   62.61  ? 2   GLU A CB  1 
ATOM   14   C CG  . GLU A 1 2   ? 24.943  54.264  38.076  1   65.51  ? 2   GLU A CG  1 
ATOM   15   C CD  . GLU A 1 2   ? 24.696  53.299  39.207  1   64.31  ? 2   GLU A CD  1 
ATOM   16   O OE1 . GLU A 1 2   ? 25.149  52.19   38.958  1   60.3   ? 2   GLU A OE1 1 
ATOM   17   O OE2 . GLU A 1 2   ? 24.153  53.626  40.286  1   68.29  ? 2   GLU A OE2 1 
ATOM   18   N N   . LEU A 1 3   ? 28.518  56.41   36.739  1   55.2   ? 3   LEU A N   1 
ATOM   19   C CA  . LEU A 1 3   ? 29      57.623  36.114  1   58.69  ? 3   LEU A CA  1 
ATOM   20   C C   . LEU A 1 3   ? 27.838  58.488  35.614  1   62.42  ? 3   LEU A C   1 
ATOM   21   O O   . LEU A 1 3   ? 27.931  59.719  35.691  1   58.28  ? 3   LEU A O   1 
ATOM   22   C CB  . LEU A 1 3   ? 29.958  57.306  34.974  1   55.58  ? 3   LEU A CB  1 
ATOM   23   C CG  . LEU A 1 3   ? 31.406  56.957  35.339  1   66.35  ? 3   LEU A CG  1 
ATOM   24   C CD1 . LEU A 1 3   ? 31.694  55.711  36.161  1   72.78  ? 3   LEU A CD1 1 
ATOM   25   C CD2 . LEU A 1 3   ? 32.22   56.884  34.053  1   63.43  ? 3   LEU A CD2 1 
ATOM   26   N N   . ILE A 1 4   ? 26.786  57.853  35.056  1   59.62  ? 4   ILE A N   1 
ATOM   27   C CA  . ILE A 1 4   ? 25.667  58.596  34.49   1   57.74  ? 4   ILE A CA  1 
ATOM   28   C C   . ILE A 1 4   ? 25.004  59.463  35.566  1   58.92  ? 4   ILE A C   1 
ATOM   29   O O   . ILE A 1 4   ? 24.749  60.651  35.298  1   57.44  ? 4   ILE A O   1 
ATOM   30   C CB  . ILE A 1 4   ? 24.658  57.696  33.737  1   54.72  ? 4   ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 4   ? 23.582  58.543  32.993  1   54.61  ? 4   ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 4   ? 23.985  56.672  34.666  1   51.48  ? 4   ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 4   ? 24.114  59.689  32.139  1   54.91  ? 4   ILE A CD1 1 
ATOM   34   N N   . ARG A 1 5   ? 24.783  58.896  36.779  1   56.03  ? 5   ARG A N   1 
ATOM   35   C CA  . ARG A 1 5   ? 24.182  59.618  37.877  1   59.3   ? 5   ARG A CA  1 
ATOM   36   C C   . ARG A 1 5   ? 25.034  60.84   38.27   1   59.41  ? 5   ARG A C   1 
ATOM   37   O O   . ARG A 1 5   ? 24.478  61.914  38.504  1   53.17  ? 5   ARG A O   1 
ATOM   38   C CB  . ARG A 1 5   ? 23.898  58.68   39.058  1   65.65  ? 5   ARG A CB  1 
ATOM   39   C CG  . ARG A 1 5   ? 22.802  57.659  38.795  1   64.22  ? 5   ARG A CG  1 
ATOM   40   C CD  . ARG A 1 5   ? 22.797  56.543  39.821  1   66.2   ? 5   ARG A CD  1 
ATOM   41   N NE  . ARG A 1 5   ? 22.253  56.953  41.117  1   70.53  ? 5   ARG A NE  1 
ATOM   42   C CZ  . ARG A 1 5   ? 22.382  56.274  42.263  1   70.52  ? 5   ARG A CZ  1 
ATOM   43   N NH1 . ARG A 1 5   ? 21.925  56.791  43.376  1   71.86  ? 5   ARG A NH1 1 
ATOM   44   N NH2 . ARG A 1 5   ? 22.964  55.089  42.31   1   67.77  ? 5   ARG A NH2 1 
ATOM   45   N N   . ILE A 1 6   ? 26.367  60.679  38.282  1   60.21  ? 6   ILE A N   1 
ATOM   46   C CA  . ILE A 1 6   ? 27.29   61.74   38.659  1   68.92  ? 6   ILE A CA  1 
ATOM   47   C C   . ILE A 1 6   ? 27.246  62.871  37.623  1   66.64  ? 6   ILE A C   1 
ATOM   48   O O   . ILE A 1 6   ? 27.198  64.038  38.001  1   61.15  ? 6   ILE A O   1 
ATOM   49   C CB  . ILE A 1 6   ? 28.717  61.177  38.88   1   73.39  ? 6   ILE A CB  1 
ATOM   50   C CG1 . ILE A 1 6   ? 28.764  60.3    40.174  1   73.68  ? 6   ILE A CG1 1 
ATOM   51   C CG2 . ILE A 1 6   ? 29.779  62.29   38.912  1   76.6   ? 6   ILE A CG2 1 
ATOM   52   C CD1 . ILE A 1 6   ? 30.005  59.434  40.316  1   72.29  ? 6   ILE A CD1 1 
ATOM   53   N N   . ALA A 1 7   ? 27.295  62.538  36.331  1   63.77  ? 7   ALA A N   1 
ATOM   54   C CA  . ALA A 1 7   ? 27.325  63.542  35.262  1   64.36  ? 7   ALA A CA  1 
ATOM   55   C C   . ALA A 1 7   ? 26.07   64.423  35.261  1   63.36  ? 7   ALA A C   1 
ATOM   56   O O   . ALA A 1 7   ? 26.15   65.659  35.116  1   60.63  ? 7   ALA A O   1 
ATOM   57   C CB  . ALA A 1 7   ? 27.506  62.878  33.937  1   61.6   ? 7   ALA A CB  1 
ATOM   58   N N   . MET A 1 8   ? 24.958  63.774  35.495  1   62.19  ? 8   MET A N   1 
ATOM   59   C CA  . MET A 1 8   ? 23.714  64.443  35.524  1   63.36  ? 8   MET A CA  1 
ATOM   60   C C   . MET A 1 8   ? 23.759  65.506  36.623  1   63.61  ? 8   MET A C   1 
ATOM   61   O O   . MET A 1 8   ? 23.566  66.669  36.361  1   60.91  ? 8   MET A O   1 
ATOM   62   C CB  . MET A 1 8   ? 22.575  63.431  35.685  1   60.08  ? 8   MET A CB  1 
ATOM   63   C CG  . MET A 1 8   ? 22.618  62.304  34.64   1   59.33  ? 8   MET A CG  1 
ATOM   64   S SD  . MET A 1 8   ? 21.141  61.475  34.054  1   55.27  ? 8   MET A SD  1 
ATOM   65   C CE  . MET A 1 8   ? 20.615  60.364  35.315  1   64.09  ? 8   MET A CE  1 
ATOM   66   N N   . LYS A 1 9   ? 24.03   65.094  37.857  1   67.96  ? 9   LYS A N   1 
ATOM   67   C CA  . LYS A 1 9   ? 24.111  66.041  38.974  1   62.22  ? 9   LYS A CA  1 
ATOM   68   C C   . LYS A 1 9   ? 25.025  67.236  38.677  1   60.65  ? 9   LYS A C   1 
ATOM   69   O O   . LYS A 1 9   ? 24.636  68.366  38.928  1   61.3   ? 9   LYS A O   1 
ATOM   70   C CB  . LYS A 1 9   ? 24.572  65.249  40.202  1   69.83  ? 9   LYS A CB  1 
ATOM   71   C CG  . LYS A 1 9   ? 23.46   64.699  41.074  1   73.52  ? 9   LYS A CG  1 
ATOM   72   C CD  . LYS A 1 9   ? 23.681  63.251  41.48   1   75.77  ? 9   LYS A CD  1 
ATOM   73   C CE  . LYS A 1 9   ? 22.814  62.895  42.629  1   79.6   ? 9   LYS A CE  1 
ATOM   74   N NZ  . LYS A 1 9   ? 23.122  61.526  43.035  1   79.42  ? 9   LYS A NZ  1 
ATOM   75   N N   . LYS A 1 10  ? 26.215  66.999  38.151  1   63.21  ? 10  LYS A N   1 
ATOM   76   C CA  . LYS A 1 10  ? 27.151  68.054  37.795  1   68.18  ? 10  LYS A CA  1 
ATOM   77   C C   . LYS A 1 10  ? 26.545  69.028  36.803  1   69.58  ? 10  LYS A C   1 
ATOM   78   O O   . LYS A 1 10  ? 26.716  70.211  36.946  1   71.96  ? 10  LYS A O   1 
ATOM   79   C CB  . LYS A 1 10  ? 28.44   67.497  37.225  1   75.42  ? 10  LYS A CB  1 
ATOM   80   C CG  . LYS A 1 10  ? 29.502  68.553  37.014  1   79.89  ? 10  LYS A CG  1 
ATOM   81   C CD  . LYS A 1 10  ? 30.734  68.029  36.287  1   87.68  ? 10  LYS A CD  1 
ATOM   82   C CE  . LYS A 1 10  ? 31.626  67.088  37.116  1   89.55  ? 10  LYS A CE  1 
ATOM   83   N NZ  . LYS A 1 10  ? 32.761  67.743  37.853  1   95.16  ? 10  LYS A NZ  1 
ATOM   84   N N   . ASP A 1 11  ? 25.845  68.516  35.793  1   66.38  ? 11  ASP A N   1 
ATOM   85   C CA  . ASP A 1 11  ? 25.168  69.348  34.803  1   65.25  ? 11  ASP A CA  1 
ATOM   86   C C   . ASP A 1 11  ? 23.957  70.068  35.406  1   67.37  ? 11  ASP A C   1 
ATOM   87   O O   . ASP A 1 11  ? 23.779  71.261  35.152  1   69.55  ? 11  ASP A O   1 
ATOM   88   C CB  . ASP A 1 11  ? 24.815  68.544  33.551  1   63.43  ? 11  ASP A CB  1 
ATOM   89   C CG  . ASP A 1 11  ? 25.97   68.243  32.608  1   64.21  ? 11  ASP A CG  1 
ATOM   90   O OD1 . ASP A 1 11  ? 26.943  69.028  32.6    1   65.65  ? 11  ASP A OD1 1 
ATOM   91   O OD2 . ASP A 1 11  ? 25.907  67.237  31.891  1   60.61  ? 11  ASP A OD2 1 
ATOM   92   N N   . LEU A 1 12  ? 23.147  69.369  36.154  1   68.69  ? 12  LEU A N   1 
ATOM   93   C CA  . LEU A 1 12  ? 22.006  69.947  36.803  1   72.49  ? 12  LEU A CA  1 
ATOM   94   C C   . LEU A 1 12  ? 22.449  71.067  37.786  1   78.27  ? 12  LEU A C   1 
ATOM   95   O O   . LEU A 1 12  ? 21.707  71.986  38.101  1   73.65  ? 12  LEU A O   1 
ATOM   96   C CB  . LEU A 1 12  ? 21.302  68.845  37.553  1   75.64  ? 12  LEU A CB  1 
ATOM   97   C CG  . LEU A 1 12  ? 19.87   69.081  37.938  1   82.99  ? 12  LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 12  ? 19.06   69.212  36.683  1   80.89  ? 12  LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 12  ? 19.376  67.914  38.761  1   82.13  ? 12  LEU A CD2 1 
ATOM   100  N N   . GLU A 1 13  ? 23.708  71.008  38.209  1   80.69  ? 13  GLU A N   1 
ATOM   101  C CA  . GLU A 1 13  ? 24.307  71.996  39.108  1   82.02  ? 13  GLU A CA  1 
ATOM   102  C C   . GLU A 1 13  ? 24.137  73.374  38.478  1   84.52  ? 13  GLU A C   1 
ATOM   103  O O   . GLU A 1 13  ? 23.672  74.303  39.115  1   82.25  ? 13  GLU A O   1 
ATOM   104  C CB  . GLU A 1 13  ? 25.785  71.66   39.329  1   79.49  ? 13  GLU A CB  1 
ATOM   105  C CG  . GLU A 1 13  ? 26.531  72.344  40.46   1   82.24  ? 13  GLU A CG  1 
ATOM   106  C CD  . GLU A 1 13  ? 27.803  71.599  40.855  1   81.46  ? 13  GLU A CD  1 
ATOM   107  O OE1 . GLU A 1 13  ? 27.736  70.375  41.031  1   74.41  ? 13  GLU A OE1 1 
ATOM   108  O OE2 . GLU A 1 13  ? 28.876  72.231  41.013  1   78.28  ? 13  GLU A OE2 1 
ATOM   109  N N   . ASN A 1 14  ? 24.472  73.492  37.209  1   83.09  ? 14  ASN A N   1 
ATOM   110  C CA  . ASN A 1 14  ? 24.291  74.732  36.544  1   86.36  ? 14  ASN A CA  1 
ATOM   111  C C   . ASN A 1 14  ? 22.972  74.964  35.735  1   80.16  ? 14  ASN A C   1 
ATOM   112  O O   . ASN A 1 14  ? 22.911  75.979  35.086  1   79.27  ? 14  ASN A O   1 
ATOM   113  C CB  . ASN A 1 14  ? 25.536  74.966  35.687  1   86.69  ? 14  ASN A CB  1 
ATOM   114  C CG  . ASN A 1 14  ? 26.82   74.529  36.382  1   85.78  ? 14  ASN A CG  1 
ATOM   115  O OD1 . ASN A 1 14  ? 27.285  75.164  37.324  1   86.29  ? 14  ASN A OD1 1 
ATOM   116  N ND2 . ASN A 1 14  ? 27.397  73.439  35.917  1   82.29  ? 14  ASN A ND2 1 
ATOM   117  N N   . ASP A 1 15  ? 21.925  74.123  35.821  1   75.68  ? 15  ASP A N   1 
ATOM   118  C CA  . ASP A 1 15  ? 20.727  74.307  35      1   71.21  ? 15  ASP A CA  1 
ATOM   119  C C   . ASP A 1 15  ? 19.605  73.358  35.458  1   69.09  ? 15  ASP A C   1 
ATOM   120  O O   . ASP A 1 15  ? 19.532  72.214  35.01   1   65.02  ? 15  ASP A O   1 
ATOM   121  C CB  . ASP A 1 15  ? 21.09   74.157  33.518  1   66.52  ? 15  ASP A CB  1 
ATOM   122  C CG  . ASP A 1 15  ? 20.013  74.442  32.47   1   63.63  ? 15  ASP A CG  1 
ATOM   123  O OD1 . ASP A 1 15  ? 18.91   74.881  32.87   1   63.38  ? 15  ASP A OD1 1 
ATOM   124  O OD2 . ASP A 1 15  ? 20.323  74.227  31.245  1   59.89  ? 15  ASP A OD2 1 
ATOM   125  N N   . ASN A 1 16  ? 18.661  73.865  36.267  1   71.72  ? 16  ASN A N   1 
ATOM   126  C CA  . ASN A 1 16  ? 17.557  73.072  36.814  1   73.95  ? 16  ASN A CA  1 
ATOM   127  C C   . ASN A 1 16  ? 16.435  72.827  35.787  1   73.46  ? 16  ASN A C   1 
ATOM   128  O O   . ASN A 1 16  ? 15.541  71.999  36.024  1   69.98  ? 16  ASN A O   1 
ATOM   129  C CB  . ASN A 1 16  ? 17.027  73.677  38.113  1   80.97  ? 16  ASN A CB  1 
ATOM   130  C CG  . ASN A 1 16  ? 16.672  72.575  39.081  1   82.04  ? 16  ASN A CG  1 
ATOM   131  O OD1 . ASN A 1 16  ? 15.959  71.636  38.711  1   83.84  ? 16  ASN A OD1 1 
ATOM   132  N ND2 . ASN A 1 16  ? 17.232  72.602  40.275  1   82.76  ? 16  ASN A ND2 1 
ATOM   133  N N   . SER A 1 17  ? 16.471  73.532  34.638  1   67.83  ? 17  SER A N   1 
ATOM   134  C CA  . SER A 1 17  ? 15.571  73.257  33.526  1   64.26  ? 17  SER A CA  1 
ATOM   135  C C   . SER A 1 17  ? 15.845  71.863  32.935  1   60.18  ? 17  SER A C   1 
ATOM   136  O O   . SER A 1 17  ? 14.929  71.271  32.373  1   59.46  ? 17  SER A O   1 
ATOM   137  C CB  . SER A 1 17  ? 15.619  74.358  32.466  1   60.48  ? 17  SER A CB  1 
ATOM   138  O OG  . SER A 1 17  ? 16.768  74.267  31.64   1   58.19  ? 17  SER A OG  1 
ATOM   139  N N   . LEU A 1 18  ? 17.091  71.352  33.049  1   59.61  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 17.483  70.033  32.533  1   59.27  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 16.585  68.909  33.061  1   58.6   ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 16.311  67.941  32.356  1   61.12  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 18.955  69.712  32.802  1   58.82  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 19.989  70.486  31.974  1   62.38  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 21.403  70.262  32.52   1   64.11  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 19.906  70.126  30.473  1   59.74  ? 18  LEU A CD2 1 
ATOM   147  N N   . MET A 1 19  ? 16.145  69.031  34.311  1   62.29  ? 19  MET A N   1 
ATOM   148  C CA  . MET A 1 19  ? 15.295  68.05   34.961  1   65.86  ? 19  MET A CA  1 
ATOM   149  C C   . MET A 1 19  ? 14.017  67.741  34.153  1   65.84  ? 19  MET A C   1 
ATOM   150  O O   . MET A 1 19  ? 13.743  66.573  33.817  1   58.53  ? 19  MET A O   1 
ATOM   151  C CB  . MET A 1 19  ? 15.041  68.543  36.394  1   70.64  ? 19  MET A CB  1 
ATOM   152  C CG  . MET A 1 19  ? 14.306  67.569  37.251  1   74.59  ? 19  MET A CG  1 
ATOM   153  S SD  . MET A 1 19  ? 15.06   65.925  37.222  1   76.48  ? 19  MET A SD  1 
ATOM   154  C CE  . MET A 1 19  ? 13.398  65.237  37.259  1   75.65  ? 19  MET A CE  1 
ATOM   155  N N   . ASN A 1 20  ? 13.25   68.786  33.806  1   66.07  ? 20  ASN A N   1 
ATOM   156  C CA  . ASN A 1 20  ? 12.034  68.632  33.002  1   66.03  ? 20  ASN A CA  1 
ATOM   157  C C   . ASN A 1 20  ? 12.281  68.07   31.596  1   57.38  ? 20  ASN A C   1 
ATOM   158  O O   . ASN A 1 20  ? 11.459  67.307  31.091  1   53.15  ? 20  ASN A O   1 
ATOM   159  C CB  . ASN A 1 20  ? 11.247  69.94   32.894  1   72.75  ? 20  ASN A CB  1 
ATOM   160  C CG  . ASN A 1 20  ? 10.068  69.931  33.828  1   76.69  ? 20  ASN A CG  1 
ATOM   161  O OD1 . ASN A 1 20  ? 9.258   69.004  33.731  1   81.25  ? 20  ASN A OD1 1 
ATOM   162  N ND2 . ASN A 1 20  ? 9.961   70.907  34.719  1   79.17  ? 20  ASN A ND2 1 
ATOM   163  N N   . LYS A 1 21  ? 13.394  68.467  30.97   1   56.38  ? 21  LYS A N   1 
ATOM   164  C CA  . LYS A 1 21  ? 13.766  68.012  29.643  1   57.57  ? 21  LYS A CA  1 
ATOM   165  C C   . LYS A 1 21  ? 13.973  66.493  29.683  1   54.54  ? 21  LYS A C   1 
ATOM   166  O O   . LYS A 1 21  ? 13.452  65.782  28.826  1   47.62  ? 21  LYS A O   1 
ATOM   167  C CB  . LYS A 1 21  ? 14.965  68.824  29.122  1   59.59  ? 21  LYS A CB  1 
ATOM   168  C CG  . LYS A 1 21  ? 15.497  68.435  27.745  1   64.77  ? 21  LYS A CG  1 
ATOM   169  C CD  . LYS A 1 21  ? 16.556  69.398  27.209  1   72.92  ? 21  LYS A CD  1 
ATOM   170  C CE  . LYS A 1 21  ? 17.959  69.144  27.699  1   77.1   ? 21  LYS A CE  1 
ATOM   171  N NZ  . LYS A 1 21  ? 18.701  68.27   26.789  1   77.17  ? 21  LYS A NZ  1 
ATOM   172  N N   . TRP A 1 22  ? 14.662  66.014  30.742  1   54.23  ? 22  TRP A N   1 
ATOM   173  C CA  . TRP A 1 22  ? 14.997  64.598  30.907  1   53.31  ? 22  TRP A CA  1 
ATOM   174  C C   . TRP A 1 22  ? 13.739  63.751  31.138  1   50.59  ? 22  TRP A C   1 
ATOM   175  O O   . TRP A 1 22  ? 13.622  62.675  30.539  1   47.83  ? 22  TRP A O   1 
ATOM   176  C CB  . TRP A 1 22  ? 16.015  64.429  32.055  1   54.06  ? 22  TRP A CB  1 
ATOM   177  C CG  . TRP A 1 22  ? 17.396  64.981  31.79   1   50.32  ? 22  TRP A CG  1 
ATOM   178  C CD1 . TRP A 1 22  ? 17.986  65.23   30.581  1   49.71  ? 22  TRP A CD1 1 
ATOM   179  C CD2 . TRP A 1 22  ? 18.383  65.315  32.79   1   49.45  ? 22  TRP A CD2 1 
ATOM   180  N NE1 . TRP A 1 22  ? 19.248  65.73   30.76   1   48.96  ? 22  TRP A NE1 1 
ATOM   181  C CE2 . TRP A 1 22  ? 19.529  65.782  32.094  1   48.84  ? 22  TRP A CE2 1 
ATOM   182  C CE3 . TRP A 1 22  ? 18.407  65.263  34.199  1   50.6   ? 22  TRP A CE3 1 
ATOM   183  C CZ2 . TRP A 1 22  ? 20.679  66.207  32.754  1   50.14  ? 22  TRP A CZ2 1 
ATOM   184  C CZ3 . TRP A 1 22  ? 19.544  65.687  34.859  1   50.41  ? 22  TRP A CZ3 1 
ATOM   185  C CH2 . TRP A 1 22  ? 20.659  66.152  34.144  1   50.36  ? 22  TRP A CH2 1 
ATOM   186  N N   . ALA A 1 23  ? 12.823  64.24   31.997  1   51.03  ? 23  ALA A N   1 
ATOM   187  C CA  . ALA A 1 23  ? 11.557  63.572  32.267  1   53.01  ? 23  ALA A CA  1 
ATOM   188  C C   . ALA A 1 23  ? 10.76   63.357  30.979  1   56.95  ? 23  ALA A C   1 
ATOM   189  O O   . ALA A 1 23  ? 10.327  62.232  30.705  1   60.18  ? 23  ALA A O   1 
ATOM   190  C CB  . ALA A 1 23  ? 10.769  64.346  33.276  1   58.42  ? 23  ALA A CB  1 
ATOM   191  N N   . THR A 1 24  ? 10.657  64.39   30.127  1   57.44  ? 24  THR A N   1 
ATOM   192  C CA  . THR A 1 24  ? 9.905   64.253  28.88   1   58.32  ? 24  THR A CA  1 
ATOM   193  C C   . THR A 1 24  ? 10.625  63.281  27.953  1   51.19  ? 24  THR A C   1 
ATOM   194  O O   . THR A 1 24  ? 9.959   62.411  27.423  1   50.41  ? 24  THR A O   1 
ATOM   195  C CB  . THR A 1 24  ? 9.623   65.574  28.163  1   62.05  ? 24  THR A CB  1 
ATOM   196  O OG1 . THR A 1 24  ? 10.895  66.08   27.793  1   73.84  ? 24  THR A OG1 1 
ATOM   197  C CG2 . THR A 1 24  ? 8.859   66.577  29.007  1   60.52  ? 24  THR A CG2 1 
ATOM   198  N N   . VAL A 1 25  ? 11.943  63.476  27.739  1   50.99  ? 25  VAL A N   1 
ATOM   199  C CA  . VAL A 1 25  ? 12.804  62.608  26.923  1   49.54  ? 25  VAL A CA  1 
ATOM   200  C C   . VAL A 1 25  ? 12.676  61.139  27.331  1   45.37  ? 25  VAL A C   1 
ATOM   201  O O   . VAL A 1 25  ? 12.673  60.244  26.476  1   39.58  ? 25  VAL A O   1 
ATOM   202  C CB  . VAL A 1 25  ? 14.26   63.122  27.017  1   55.34  ? 25  VAL A CB  1 
ATOM   203  C CG1 . VAL A 1 25  ? 15.331  62.091  26.762  1   57.95  ? 25  VAL A CG1 1 
ATOM   204  C CG2 . VAL A 1 25  ? 14.495  64.317  26.098  1   62.39  ? 25  VAL A CG2 1 
ATOM   205  N N   . ALA A 1 26  ? 12.622  60.89   28.653  1   48.65  ? 26  ALA A N   1 
ATOM   206  C CA  . ALA A 1 26  ? 12.543  59.533  29.186  1   47.49  ? 26  ALA A CA  1 
ATOM   207  C C   . ALA A 1 26  ? 11.135  58.946  29.142  1   50.86  ? 26  ALA A C   1 
ATOM   208  O O   . ALA A 1 26  ? 10.944  57.815  29.577  1   52.17  ? 26  ALA A O   1 
ATOM   209  C CB  . ALA A 1 26  ? 13.069  59.544  30.604  1   47.14  ? 26  ALA A CB  1 
ATOM   210  N N   . GLY A 1 27  ? 10.133  59.732  28.716  1   55.59  ? 27  GLY A N   1 
ATOM   211  C CA  . GLY A 1 27  ? 8.766   59.265  28.564  1   53.9   ? 27  GLY A CA  1 
ATOM   212  C C   . GLY A 1 27  ? 8.078   59.116  29.914  1   54.55  ? 27  GLY A C   1 
ATOM   213  O O   . GLY A 1 27  ? 7.176   58.318  30.043  1   54.55  ? 27  GLY A O   1 
ATOM   214  N N   . LEU A 1 28  ? 8.507   59.892  30.912  1   58.35  ? 28  LEU A N   1 
ATOM   215  C CA  . LEU A 1 28  ? 7.954   59.817  32.249  1   60.85  ? 28  LEU A CA  1 
ATOM   216  C C   . LEU A 1 28  ? 6.729   60.73   32.327  1   65.51  ? 28  LEU A C   1 
ATOM   217  O O   . LEU A 1 28  ? 6.678   61.755  31.655  1   64.35  ? 28  LEU A O   1 
ATOM   218  C CB  . LEU A 1 28  ? 9.038   60.243  33.241  1   57.69  ? 28  LEU A CB  1 
ATOM   219  C CG  . LEU A 1 28  ? 10.342  59.44   33.218  1   54.16  ? 28  LEU A CG  1 
ATOM   220  C CD1 . LEU A 1 28  ? 11.274  59.939  34.338  1   54.74  ? 28  LEU A CD1 1 
ATOM   221  C CD2 . LEU A 1 28  ? 10.128  57.934  33.312  1   51.28  ? 28  LEU A CD2 1 
ATOM   222  N N   . LYS A 1 29  ? 5.765   60.352  33.177  1   69.17  ? 29  LYS A N   1 
ATOM   223  C CA  . LYS A 1 29  ? 4.574   61.15   33.423  1   77.12  ? 29  LYS A CA  1 
ATOM   224  C C   . LYS A 1 29  ? 4.956   62.378  34.255  1   82.86  ? 29  LYS A C   1 
ATOM   225  O O   . LYS A 1 29  ? 4.528   63.488  33.952  1   87.69  ? 29  LYS A O   1 
ATOM   226  C CB  . LYS A 1 29  ? 3.508   60.368  34.2    1   85.01  ? 29  LYS A CB  1 
ATOM   227  C CG  . LYS A 1 29  ? 3.095   58.973  33.712  1   86.68  ? 29  LYS A CG  1 
ATOM   228  C CD  . LYS A 1 29  ? 2.124   58.309  34.698  1   93.94  ? 29  LYS A CD  1 
ATOM   229  C CE  . LYS A 1 29  ? 2.262   56.814  34.867  1   96.81  ? 29  LYS A CE  1 
ATOM   230  N NZ  . LYS A 1 29  ? 1.922   56.036  33.669  1   92.78  ? 29  LYS A NZ  1 
ATOM   231  N N   . ASN A 1 30  ? 5.748   62.147  35.315  1   81.58  ? 30  ASN A N   1 
ATOM   232  C CA  . ASN A 1 30  ? 6.211   63.168  36.241  1   83.79  ? 30  ASN A CA  1 
ATOM   233  C C   . ASN A 1 30  ? 7.715   62.978  36.461  1   80.31  ? 30  ASN A C   1 
ATOM   234  O O   . ASN A 1 30  ? 8.286   61.965  36.043  1   76.05  ? 30  ASN A O   1 
ATOM   235  C CB  . ASN A 1 30  ? 5.37    63.123  37.52   1   83.97  ? 30  ASN A CB  1 
ATOM   236  C CG  . ASN A 1 30  ? 5.508   61.819  38.277  1   83.37  ? 30  ASN A CG  1 
ATOM   237  O OD1 . ASN A 1 30  ? 5.652   60.749  37.686  1   87.38  ? 30  ASN A OD1 1 
ATOM   238  N ND2 . ASN A 1 30  ? 5.481   61.869  39.592  1   91.24  ? 30  ASN A ND2 1 
ATOM   239  N N   . PRO A 1 31  ? 8.427   63.955  37.073  1   79.4   ? 31  PRO A N   1 
ATOM   240  C CA  . PRO A 1 31  ? 9.818   63.741  37.49   1   75.82  ? 31  PRO A CA  1 
ATOM   241  C C   . PRO A 1 31  ? 10.209  62.736  38.584  1   71.21  ? 31  PRO A C   1 
ATOM   242  O O   . PRO A 1 31  ? 11.406  62.541  38.762  1   68.49  ? 31  PRO A O   1 
ATOM   243  C CB  . PRO A 1 31  ? 10.22   65.179  37.894  1   79.45  ? 31  PRO A CB  1 
ATOM   244  C CG  . PRO A 1 31  ? 8.934   65.823  38.328  1   85.62  ? 31  PRO A CG  1 
ATOM   245  C CD  . PRO A 1 31  ? 8.005   65.359  37.237  1   84.2   ? 31  PRO A CD  1 
ATOM   246  N N   . ASN A 1 32  ? 9.258   62.084  39.279  1   70.9   ? 32  ASN A N   1 
ATOM   247  C CA  . ASN A 1 32  ? 9.564   61.324  40.499  1   72.81  ? 32  ASN A CA  1 
ATOM   248  C C   . ASN A 1 32  ? 10.504  60.139  40.26   1   69.26  ? 32  ASN A C   1 
ATOM   249  O O   . ASN A 1 32  ? 11.465  60.008  41.014  1   64.81  ? 32  ASN A O   1 
ATOM   250  C CB  . ASN A 1 32  ? 8.323   60.827  41.235  1   74.56  ? 32  ASN A CB  1 
ATOM   251  C CG  . ASN A 1 32  ? 7.712   61.908  42.086  1   82.03  ? 32  ASN A CG  1 
ATOM   252  O OD1 . ASN A 1 32  ? 7.028   62.786  41.557  1   85.17  ? 32  ASN A OD1 1 
ATOM   253  N ND2 . ASN A 1 32  ? 7.962   61.888  43.39   1   85.57  ? 32  ASN A ND2 1 
ATOM   254  N N   . PRO A 1 33  ? 10.285  59.25   39.251  1   68.37  ? 33  PRO A N   1 
ATOM   255  C CA  . PRO A 1 33  ? 11.269  58.21   38.906  1   69.49  ? 33  PRO A CA  1 
ATOM   256  C C   . PRO A 1 33  ? 12.705  58.703  38.711  1   66.03  ? 33  PRO A C   1 
ATOM   257  O O   . PRO A 1 33  ? 13.637  58.009  39.064  1   63.09  ? 33  PRO A O   1 
ATOM   258  C CB  . PRO A 1 33  ? 10.736  57.537  37.591  1   66.28  ? 33  PRO A CB  1 
ATOM   259  C CG  . PRO A 1 33  ? 9.304   57.997  37.432  1   67.55  ? 33  PRO A CG  1 
ATOM   260  C CD  . PRO A 1 33  ? 9.084   59.173  38.392  1   67.86  ? 33  PRO A CD  1 
ATOM   261  N N   . LEU A 1 34  ? 12.864  59.915  38.161  1   65.66  ? 34  LEU A N   1 
ATOM   262  C CA  . LEU A 1 34  ? 14.157  60.516  37.874  1   63.39  ? 34  LEU A CA  1 
ATOM   263  C C   . LEU A 1 34  ? 14.841  61.018  39.154  1   63.14  ? 34  LEU A C   1 
ATOM   264  O O   . LEU A 1 34  ? 16.052  60.89   39.282  1   59.87  ? 34  LEU A O   1 
ATOM   265  C CB  . LEU A 1 34  ? 13.88   61.62   36.854  1   67.68  ? 34  LEU A CB  1 
ATOM   266  C CG  . LEU A 1 34  ? 15.041  62.208  36.044  1   73.87  ? 34  LEU A CG  1 
ATOM   267  C CD1 . LEU A 1 34  ? 15.953  61.185  35.397  1   68.95  ? 34  LEU A CD1 1 
ATOM   268  C CD2 . LEU A 1 34  ? 14.478  63.094  34.926  1   75.11  ? 34  LEU A CD2 1 
ATOM   269  N N   . TYR A 1 35  ? 14.082  61.616  40.08   1   64.96  ? 35  TYR A N   1 
ATOM   270  C CA  . TYR A 1 35  ? 14.581  61.958  41.411  1   69.84  ? 35  TYR A CA  1 
ATOM   271  C C   . TYR A 1 35  ? 15.078  60.699  42.134  1   73.12  ? 35  TYR A C   1 
ATOM   272  O O   . TYR A 1 35  ? 16.21   60.686  42.645  1   69.57  ? 35  TYR A O   1 
ATOM   273  C CB  . TYR A 1 35  ? 13.54   62.681  42.27   1   69.16  ? 35  TYR A CB  1 
ATOM   274  C CG  . TYR A 1 35  ? 13.09   64.071  41.827  1   66.63  ? 35  TYR A CG  1 
ATOM   275  C CD1 . TYR A 1 35  ? 13.939  64.97   41.178  1   66.15  ? 35  TYR A CD1 1 
ATOM   276  C CD2 . TYR A 1 35  ? 11.778  64.479  42.047  1   68.55  ? 35  TYR A CD2 1 
ATOM   277  C CE1 . TYR A 1 35  ? 13.502  66.226  40.785  1   68.34  ? 35  TYR A CE1 1 
ATOM   278  C CE2 . TYR A 1 35  ? 11.329  65.74   41.669  1   70.57  ? 35  TYR A CE2 1 
ATOM   279  C CZ  . TYR A 1 35  ? 12.189  66.609  41.015  1   68.3   ? 35  TYR A CZ  1 
ATOM   280  O OH  . TYR A 1 35  ? 11.738  67.839  40.65   1   68.3   ? 35  TYR A OH  1 
ATOM   281  N N   . ASP A 1 36  ? 14.246  59.643  42.099  1   69.13  ? 36  ASP A N   1 
ATOM   282  C CA  . ASP A 1 36  ? 14.558  58.351  42.692  1   69.33  ? 36  ASP A CA  1 
ATOM   283  C C   . ASP A 1 36  ? 15.826  57.759  42.061  1   60.76  ? 36  ASP A C   1 
ATOM   284  O O   . ASP A 1 36  ? 16.724  57.252  42.731  1   55.58  ? 36  ASP A O   1 
ATOM   285  C CB  . ASP A 1 36  ? 13.36   57.422  42.536  1   72.07  ? 36  ASP A CB  1 
ATOM   286  C CG  . ASP A 1 36  ? 13.107  56.432  43.659  1   77.12  ? 36  ASP A CG  1 
ATOM   287  O OD1 . ASP A 1 36  ? 13.911  56.383  44.605  1   74.3   ? 36  ASP A OD1 1 
ATOM   288  O OD2 . ASP A 1 36  ? 12.094  55.717  43.562  1   82.59  ? 36  ASP A OD2 1 
ATOM   289  N N   . PHE A 1 37  ? 15.899  57.814  40.73   1   60.53  ? 37  PHE A N   1 
ATOM   290  C CA  . PHE A 1 37  ? 17.034  57.279  39.996  1   56.02  ? 37  PHE A CA  1 
ATOM   291  C C   . PHE A 1 37  ? 18.333  57.989  40.394  1   56.88  ? 37  PHE A C   1 
ATOM   292  O O   . PHE A 1 37  ? 19.372  57.34   40.472  1   62.15  ? 37  PHE A O   1 
ATOM   293  C CB  . PHE A 1 37  ? 16.809  57.429  38.488  1   53.9   ? 37  PHE A CB  1 
ATOM   294  C CG  . PHE A 1 37  ? 18.018  57.029  37.671  1   51.57  ? 37  PHE A CG  1 
ATOM   295  C CD1 . PHE A 1 37  ? 18.301  55.677  37.496  1   54.45  ? 37  PHE A CD1 1 
ATOM   296  C CD2 . PHE A 1 37  ? 18.865  57.968  37.073  1   50.09  ? 37  PHE A CD2 1 
ATOM   297  C CE1 . PHE A 1 37  ? 19.39   55.272  36.752  1   52.05  ? 37  PHE A CE1 1 
ATOM   298  C CE2 . PHE A 1 37  ? 19.968  57.544  36.34   1   50.14  ? 37  PHE A CE2 1 
ATOM   299  C CZ  . PHE A 1 37  ? 20.204  56.198  36.147  1   51.2   ? 37  PHE A CZ  1 
ATOM   300  N N   . LEU A 1 38  ? 18.3    59.324  40.534  1   56.04  ? 38  LEU A N   1 
ATOM   301  C CA  . LEU A 1 38  ? 19.504  60.106  40.79   1   57.08  ? 38  LEU A CA  1 
ATOM   302  C C   . LEU A 1 38  ? 20.018  59.869  42.207  1   58.27  ? 38  LEU A C   1 
ATOM   303  O O   . LEU A 1 38  ? 21.233  59.809  42.402  1   58.71  ? 38  LEU A O   1 
ATOM   304  C CB  . LEU A 1 38  ? 19.279  61.6    40.538  1   59.46  ? 38  LEU A CB  1 
ATOM   305  C CG  . LEU A 1 38  ? 19.284  62.027  39.06   1   59.12  ? 38  LEU A CG  1 
ATOM   306  C CD1 . LEU A 1 38  ? 18.916  63.501  38.888  1   61.74  ? 38  LEU A CD1 1 
ATOM   307  C CD2 . LEU A 1 38  ? 20.645  61.745  38.429  1   59.44  ? 38  LEU A CD2 1 
ATOM   308  N N   . ASN A 1 39  ? 19.1    59.711  43.158  1   59.6   ? 39  ASN A N   1 
ATOM   309  C CA  . ASN A 1 39  ? 19.421  59.838  44.569  1   65.52  ? 39  ASN A CA  1 
ATOM   310  C C   . ASN A 1 39  ? 19.574  58.484  45.282  1   69.47  ? 39  ASN A C   1 
ATOM   311  O O   . ASN A 1 39  ? 20.125  58.478  46.392  1   72.03  ? 39  ASN A O   1 
ATOM   312  C CB  . ASN A 1 39  ? 18.375  60.726  45.246  1   68.73  ? 39  ASN A CB  1 
ATOM   313  C CG  . ASN A 1 39  ? 18.42   62.178  44.792  1   69.54  ? 39  ASN A CG  1 
ATOM   314  O OD1 . ASN A 1 39  ? 19.438  62.653  44.237  1   72.86  ? 39  ASN A OD1 1 
ATOM   315  N ND2 . ASN A 1 39  ? 17.337  62.904  45.043  1   68.92  ? 39  ASN A ND2 1 
ATOM   316  N N   . HIS A 1 40  ? 19.032  57.377  44.739  1   63.09  ? 40  HIS A N   1 
ATOM   317  C CA  . HIS A 1 40  ? 18.964  56.109  45.46   1   68.09  ? 40  HIS A CA  1 
ATOM   318  C C   . HIS A 1 40  ? 19.531  54.99   44.594  1   66.63  ? 40  HIS A C   1 
ATOM   319  O O   . HIS A 1 40  ? 19.048  54.784  43.471  1   59.48  ? 40  HIS A O   1 
ATOM   320  C CB  . HIS A 1 40  ? 17.524  55.745  45.838  1   69.81  ? 40  HIS A CB  1 
ATOM   321  C CG  . HIS A 1 40  ? 16.859  56.773  46.664  1   72.43  ? 40  HIS A CG  1 
ATOM   322  N ND1 . HIS A 1 40  ? 15.498  56.968  46.611  1   76.88  ? 40  HIS A ND1 1 
ATOM   323  C CD2 . HIS A 1 40  ? 17.328  57.683  47.509  1   74.92  ? 40  HIS A CD2 1 
ATOM   324  C CE1 . HIS A 1 40  ? 15.174  57.965  47.416  1   79.71  ? 40  HIS A CE1 1 
ATOM   325  N NE2 . HIS A 1 40  ? 16.278  58.416  47.97   1   79.6   ? 40  HIS A NE2 1 
ATOM   326  N N   . ASP A 1 41  ? 20.521  54.267  45.155  1   69.58  ? 41  ASP A N   1 
ATOM   327  C CA  . ASP A 1 41  ? 21.21   53.155  44.5    1   71.83  ? 41  ASP A CA  1 
ATOM   328  C C   . ASP A 1 41  ? 20.227  52.062  44.101  1   66.78  ? 41  ASP A C   1 
ATOM   329  O O   . ASP A 1 41  ? 19.281  51.774  44.831  1   63.88  ? 41  ASP A O   1 
ATOM   330  C CB  . ASP A 1 41  ? 22.288  52.543  45.384  1   78.64  ? 41  ASP A CB  1 
ATOM   331  C CG  . ASP A 1 41  ? 23.375  53.499  45.848  1   79.88  ? 41  ASP A CG  1 
ATOM   332  O OD1 . ASP A 1 41  ? 23.868  54.285  45.004  1   78.91  ? 41  ASP A OD1 1 
ATOM   333  O OD2 . ASP A 1 41  ? 23.685  53.477  47.052  1   94.44  ? 41  ASP A OD2 1 
ATOM   334  N N   . GLY A 1 42  ? 20.43   51.517  42.899  1   69.1   ? 42  GLY A N   1 
ATOM   335  C CA  . GLY A 1 42  ? 19.652  50.389  42.422  1   70.92  ? 42  GLY A CA  1 
ATOM   336  C C   . GLY A 1 42  ? 18.252  50.769  41.943  1   68.01  ? 42  GLY A C   1 
ATOM   337  O O   . GLY A 1 42  ? 17.477  49.883  41.613  1   63.15  ? 42  GLY A O   1 
ATOM   338  N N   . LYS A 1 43  ? 17.901  52.062  41.891  1   66.17  ? 43  LYS A N   1 
ATOM   339  C CA  . LYS A 1 43  ? 16.59   52.415  41.391  1   68.25  ? 43  LYS A CA  1 
ATOM   340  C C   . LYS A 1 43  ? 16.704  52.431  39.867  1   64.16  ? 43  LYS A C   1 
ATOM   341  O O   . LYS A 1 43  ? 17.489  53.197  39.307  1   61.15  ? 43  LYS A O   1 
ATOM   342  C CB  . LYS A 1 43  ? 16.025  53.708  41.977  1   78.31  ? 43  LYS A CB  1 
ATOM   343  C CG  . LYS A 1 43  ? 14.639  54.051  41.43   1   91.31  ? 43  LYS A CG  1 
ATOM   344  C CD  . LYS A 1 43  ? 13.565  52.965  41.313  1   96.83  ? 43  LYS A CD  1 
ATOM   345  C CE  . LYS A 1 43  ? 12.272  53.543  40.789  1   96.5   ? 43  LYS A CE  1 
ATOM   346  N NZ  . LYS A 1 43  ? 11.186  52.563  40.804  1   94.08  ? 43  LYS A NZ  1 
ATOM   347  N N   . THR A 1 44  ? 15.987  51.515  39.213  1   59.06  ? 44  THR A N   1 
ATOM   348  C CA  . THR A 1 44  ? 15.948  51.436  37.757  1   54.37  ? 44  THR A CA  1 
ATOM   349  C C   . THR A 1 44  ? 14.622  52.049  37.309  1   51.82  ? 44  THR A C   1 
ATOM   350  O O   . THR A 1 44  ? 13.634  51.996  38.051  1   51.43  ? 44  THR A O   1 
ATOM   351  C CB  . THR A 1 44  ? 16.101  49.98   37.304  1   53.84  ? 44  THR A CB  1 
ATOM   352  O OG1 . THR A 1 44  ? 15.042  49.233  37.893  1   55.71  ? 44  THR A OG1 1 
ATOM   353  C CG2 . THR A 1 44  ? 17.406  49.357  37.762  1   53.49  ? 44  THR A CG2 1 
ATOM   354  N N   . PHE A 1 45  ? 14.624  52.638  36.1    1   47.51  ? 45  PHE A N   1 
ATOM   355  C CA  . PHE A 1 45  ? 13.376  52.987  35.438  1   47.78  ? 45  PHE A CA  1 
ATOM   356  C C   . PHE A 1 45  ? 12.617  51.708  35.077  1   45.28  ? 45  PHE A C   1 
ATOM   357  O O   . PHE A 1 45  ? 13.224  50.677  34.851  1   46.78  ? 45  PHE A O   1 
ATOM   358  C CB  . PHE A 1 45  ? 13.66   53.829  34.181  1   48.68  ? 45  PHE A CB  1 
ATOM   359  C CG  . PHE A 1 45  ? 14.357  55.153  34.479  1   49.13  ? 45  PHE A CG  1 
ATOM   360  C CD1 . PHE A 1 45  ? 13.65   56.215  35.054  1   52.34  ? 45  PHE A CD1 1 
ATOM   361  C CD2 . PHE A 1 45  ? 15.719  55.322  34.207  1   48.43  ? 45  PHE A CD2 1 
ATOM   362  C CE1 . PHE A 1 45  ? 14.284  57.423  35.337  1   53.07  ? 45  PHE A CE1 1 
ATOM   363  C CE2 . PHE A 1 45  ? 16.357  56.524  34.501  1   50.52  ? 45  PHE A CE2 1 
ATOM   364  C CZ  . PHE A 1 45  ? 15.637  57.569  35.043  1   52.22  ? 45  PHE A CZ  1 
ATOM   365  N N   . ASN A 1 46  ? 11.29   51.806  34.947  1   48.21  ? 46  ASN A N   1 
ATOM   366  C CA  . ASN A 1 46  ? 10.413  50.709  34.552  1   52.33  ? 46  ASN A CA  1 
ATOM   367  C C   . ASN A 1 46  ? 10.776  50.205  33.157  1   47.1   ? 46  ASN A C   1 
ATOM   368  O O   . ASN A 1 46  ? 10.686  48.998  32.917  1   50.17  ? 46  ASN A O   1 
ATOM   369  C CB  . ASN A 1 46  ? 8.931   51.085  34.544  1   56.6   ? 46  ASN A CB  1 
ATOM   370  C CG  . ASN A 1 46  ? 8.359   51.278  35.936  1   67.32  ? 46  ASN A CG  1 
ATOM   371  O OD1 . ASN A 1 46  ? 8.988   50.926  36.944  1   72.25  ? 46  ASN A OD1 1 
ATOM   372  N ND2 . ASN A 1 46  ? 7.157   51.834  36.024  1   71.67  ? 46  ASN A ND2 1 
ATOM   373  N N   . GLU A 1 47  ? 11.187  51.127  32.271  1   45.9   ? 47  GLU A N   1 
ATOM   374  C CA  . GLU A 1 47  ? 11.594  50.774  30.915  1   48.08  ? 47  GLU A CA  1 
ATOM   375  C C   . GLU A 1 47  ? 12.984  51.364  30.651  1   43.68  ? 47  GLU A C   1 
ATOM   376  O O   . GLU A 1 47  ? 13.274  52.544  30.917  1   40.16  ? 47  GLU A O   1 
ATOM   377  C CB  . GLU A 1 47  ? 10.49   51.194  29.938  1   47.73  ? 47  GLU A CB  1 
ATOM   378  C CG  . GLU A 1 47  ? 9.272   50.264  29.905  1   51.38  ? 47  GLU A CG  1 
ATOM   379  C CD  . GLU A 1 47  ? 9.484   48.831  29.391  1   54.17  ? 47  GLU A CD  1 
ATOM   380  O OE1 . GLU A 1 47  ? 10.554  48.544  28.76   1   47.54  ? 47  GLU A OE1 1 
ATOM   381  O OE2 . GLU A 1 47  ? 8.588   47.964  29.659  1   53.12  ? 47  GLU A OE2 1 
ATOM   382  N N   . PHE A 1 48  ? 13.826  50.533  30.037  1   40.56  ? 48  PHE A N   1 
ATOM   383  C CA  . PHE A 1 48  ? 15.217  50.851  29.805  1   38.93  ? 48  PHE A CA  1 
ATOM   384  C C   . PHE A 1 48  ? 15.407  51.989  28.801  1   40.6   ? 48  PHE A C   1 
ATOM   385  O O   . PHE A 1 48  ? 16.438  52.661  28.853  1   42.68  ? 48  PHE A O   1 
ATOM   386  C CB  . PHE A 1 48  ? 15.868  49.567  29.313  1   40.17  ? 48  PHE A CB  1 
ATOM   387  C CG  . PHE A 1 48  ? 17.375  49.584  29.405  1   37.78  ? 48  PHE A CG  1 
ATOM   388  C CD1 . PHE A 1 48  ? 17.986  49.416  30.649  1   39.48  ? 48  PHE A CD1 1 
ATOM   389  C CD2 . PHE A 1 48  ? 18.165  49.795  28.291  1   36.17  ? 48  PHE A CD2 1 
ATOM   390  C CE1 . PHE A 1 48  ? 19.367  49.417  30.75   1   38.47  ? 48  PHE A CE1 1 
ATOM   391  C CE2 . PHE A 1 48  ? 19.547  49.783  28.408  1   38.25  ? 48  PHE A CE2 1 
ATOM   392  C CZ  . PHE A 1 48  ? 20.144  49.58   29.642  1   39.12  ? 48  PHE A CZ  1 
ATOM   393  N N   . SER A 1 49  ? 14.403  52.199  27.93   1   37.31  ? 49  SER A N   1 
ATOM   394  C CA  . SER A 1 49  ? 14.284  53.349  27.03   1   40.09  ? 49  SER A CA  1 
ATOM   395  C C   . SER A 1 49  ? 14.548  54.685  27.757  1   40.68  ? 49  SER A C   1 
ATOM   396  O O   . SER A 1 49  ? 15.121  55.602  27.169  1   43.65  ? 49  SER A O   1 
ATOM   397  C CB  . SER A 1 49  ? 12.884  53.327  26.363  1   37.75  ? 49  SER A CB  1 
ATOM   398  O OG  . SER A 1 49  ? 11.892  53.172  27.387  1   39.14  ? 49  SER A OG  1 
ATOM   399  N N   . SER A 1 50  ? 14.159  54.776  29.023  1   39.86  ? 50  SER A N   1 
ATOM   400  C CA  . SER A 1 50  ? 14.316  55.999  29.822  1   44.63  ? 50  SER A CA  1 
ATOM   401  C C   . SER A 1 50  ? 15.782  56.425  29.928  1   45.44  ? 50  SER A C   1 
ATOM   402  O O   . SER A 1 50  ? 16.111  57.571  29.631  1   46.27  ? 50  SER A O   1 
ATOM   403  C CB  . SER A 1 50  ? 13.742  55.844  31.2    1   45.38  ? 50  SER A CB  1 
ATOM   404  O OG  . SER A 1 50  ? 12.326  55.838  31.133  1   47.33  ? 50  SER A OG  1 
ATOM   405  N N   . ILE A 1 51  ? 16.666  55.508  30.344  1   44.22  ? 51  ILE A N   1 
ATOM   406  C CA  . ILE A 1 51  ? 18.072  55.841  30.494  1   42.71  ? 51  ILE A CA  1 
ATOM   407  C C   . ILE A 1 51  ? 18.73   55.995  29.123  1   41.83  ? 51  ILE A C   1 
ATOM   408  O O   . ILE A 1 51  ? 19.549  56.891  28.966  1   39.9   ? 51  ILE A O   1 
ATOM   409  C CB  . ILE A 1 51  ? 18.797  54.861  31.435  1   46.68  ? 51  ILE A CB  1 
ATOM   410  C CG1 . ILE A 1 51  ? 20.211  55.362  31.766  1   48.96  ? 51  ILE A CG1 1 
ATOM   411  C CG2 . ILE A 1 51  ? 18.847  53.437  30.881  1   45.74  ? 51  ILE A CG2 1 
ATOM   412  C CD1 . ILE A 1 51  ? 20.279  56.745  32.382  1   50.59  ? 51  ILE A CD1 1 
ATOM   413  N N   . VAL A 1 52  ? 18.372  55.163  28.131  1   38.36  ? 52  VAL A N   1 
ATOM   414  C CA  . VAL A 1 52  ? 18.971  55.275  26.803  1   38.62  ? 52  VAL A CA  1 
ATOM   415  C C   . VAL A 1 52  ? 18.651  56.641  26.189  1   38.28  ? 52  VAL A C   1 
ATOM   416  O O   . VAL A 1 52  ? 19.533  57.273  25.614  1   41.21  ? 52  VAL A O   1 
ATOM   417  C CB  . VAL A 1 52  ? 18.519  54.148  25.847  1   37.84  ? 52  VAL A CB  1 
ATOM   418  C CG1 . VAL A 1 52  ? 19.015  54.349  24.418  1   37.71  ? 52  VAL A CG1 1 
ATOM   419  C CG2 . VAL A 1 52  ? 18.919  52.749  26.351  1   39.38  ? 52  VAL A CG2 1 
ATOM   420  N N   . ASN A 1 53  ? 17.386  57.074  26.302  1   39.88  ? 53  ASN A N   1 
ATOM   421  C CA  . ASN A 1 53  ? 16.951  58.324  25.691  1   38.87  ? 53  ASN A CA  1 
ATOM   422  C C   . ASN A 1 53  ? 17.648  59.503  26.345  1   39.19  ? 53  ASN A C   1 
ATOM   423  O O   . ASN A 1 53  ? 17.985  60.46   25.642  1   41.27  ? 53  ASN A O   1 
ATOM   424  C CB  . ASN A 1 53  ? 15.443  58.507  25.735  1   38.44  ? 53  ASN A CB  1 
ATOM   425  C CG  . ASN A 1 53  ? 14.688  57.535  24.847  1   38.69  ? 53  ASN A CG  1 
ATOM   426  O OD1 . ASN A 1 53  ? 15.272  56.812  24.049  1   37.52  ? 53  ASN A OD1 1 
ATOM   427  N ND2 . ASN A 1 53  ? 13.384  57.46   25.047  1   43     ? 53  ASN A ND2 1 
ATOM   428  N N   . ILE A 1 54  ? 17.872  59.432  27.67   1   35.08  ? 54  ILE A N   1 
ATOM   429  C CA  . ILE A 1 54  ? 18.589  60.5    28.361  1   39.14  ? 54  ILE A CA  1 
ATOM   430  C C   . ILE A 1 54  ? 20.028  60.599  27.858  1   38.4   ? 54  ILE A C   1 
ATOM   431  O O   . ILE A 1 54  ? 20.527  61.728  27.675  1   40.43  ? 54  ILE A O   1 
ATOM   432  C CB  . ILE A 1 54  ? 18.553  60.314  29.895  1   39.7   ? 54  ILE A CB  1 
ATOM   433  C CG1 . ILE A 1 54  ? 17.119  60.518  30.426  1   42.07  ? 54  ILE A CG1 1 
ATOM   434  C CG2 . ILE A 1 54  ? 19.541  61.278  30.559  1   42     ? 54  ILE A CG2 1 
ATOM   435  C CD1 . ILE A 1 54  ? 16.876  60.04   31.865  1   45.28  ? 54  ILE A CD1 1 
ATOM   436  N N   . VAL A 1 55  ? 20.708  59.431  27.759  1   37.98  ? 55  VAL A N   1 
ATOM   437  C CA  . VAL A 1 55  ? 22.121  59.39   27.476  1   39.08  ? 55  VAL A CA  1 
ATOM   438  C C   . VAL A 1 55  ? 22.311  59.922  26.057  1   42.22  ? 55  VAL A C   1 
ATOM   439  O O   . VAL A 1 55  ? 23.193  60.75   25.833  1   42.85  ? 55  VAL A O   1 
ATOM   440  C CB  . VAL A 1 55  ? 22.715  57.975  27.685  1   43.25  ? 55  VAL A CB  1 
ATOM   441  C CG1 . VAL A 1 55  ? 24.106  57.838  27.092  1   46.88  ? 55  VAL A CG1 1 
ATOM   442  C CG2 . VAL A 1 55  ? 22.772  57.612  29.171  1   43.6   ? 55  VAL A CG2 1 
ATOM   443  N N   . LYS A 1 56  ? 21.452  59.472  25.131  1   39.71  ? 56  LYS A N   1 
ATOM   444  C CA  . LYS A 1 56  ? 21.525  59.895  23.733  1   43.27  ? 56  LYS A CA  1 
ATOM   445  C C   . LYS A 1 56  ? 21.227  61.382  23.55   1   43.11  ? 56  LYS A C   1 
ATOM   446  O O   . LYS A 1 56  ? 21.823  61.992  22.672  1   47.12  ? 56  LYS A O   1 
ATOM   447  C CB  . LYS A 1 56  ? 20.568  59.08   22.86   1   43.82  ? 56  LYS A CB  1 
ATOM   448  C CG  . LYS A 1 56  ? 21.082  57.686  22.573  1   45.95  ? 56  LYS A CG  1 
ATOM   449  C CD  . LYS A 1 56  ? 20.148  56.934  21.62   1   46.6   ? 56  LYS A CD  1 
ATOM   450  C CE  . LYS A 1 56  ? 20.757  55.683  21.076  1   47.04  ? 56  LYS A CE  1 
ATOM   451  N NZ  . LYS A 1 56  ? 21.76   55.966  20.034  1   44.72  ? 56  LYS A NZ  1 
ATOM   452  N N   . SER A 1 57  ? 20.31   61.935  24.348  1   41.04  ? 57  SER A N   1 
ATOM   453  C CA  . SER A 1 57  ? 19.902  63.321  24.25   1   45.17  ? 57  SER A CA  1 
ATOM   454  C C   . SER A 1 57  ? 20.974  64.23   24.862  1   50.13  ? 57  SER A C   1 
ATOM   455  O O   . SER A 1 57  ? 21.368  65.244  24.27   1   47.86  ? 57  SER A O   1 
ATOM   456  C CB  . SER A 1 57  ? 18.56   63.539  24.938  1   43.01  ? 57  SER A CB  1 
ATOM   457  O OG  . SER A 1 57  ? 18.393  64.864  25.438  1   51.94  ? 57  SER A OG  1 
ATOM   458  N N   . GLN A 1 58  ? 21.346  63.923  26.116  1   50.85  ? 58  GLN A N   1 
ATOM   459  C CA  . GLN A 1 58  ? 22.233  64.776  26.89   1   48.92  ? 58  GLN A CA  1 
ATOM   460  C C   . GLN A 1 58  ? 23.72   64.504  26.609  1   48.78  ? 58  GLN A C   1 
ATOM   461  O O   . GLN A 1 58  ? 24.537  65.434  26.717  1   47.96  ? 58  GLN A O   1 
ATOM   462  C CB  . GLN A 1 58  ? 21.922  64.581  28.374  1   52.2   ? 58  GLN A CB  1 
ATOM   463  C CG  . GLN A 1 58  ? 22.601  65.593  29.292  1   55.15  ? 58  GLN A CG  1 
ATOM   464  C CD  . GLN A 1 58  ? 22.144  67.028  29.062  1   58.69  ? 58  GLN A CD  1 
ATOM   465  O OE1 . GLN A 1 58  ? 20.949  67.3    28.883  1   52.09  ? 58  GLN A OE1 1 
ATOM   466  N NE2 . GLN A 1 58  ? 23.069  67.977  29.142  1   61.64  ? 58  GLN A NE2 1 
ATOM   467  N N   . TYR A 1 59  ? 24.091  63.237  26.355  1   47.78  ? 59  TYR A N   1 
ATOM   468  C CA  . TYR A 1 59  ? 25.493  62.841  26.341  1   48.71  ? 59  TYR A CA  1 
ATOM   469  C C   . TYR A 1 59  ? 25.803  62.017  25.105  1   47.69  ? 59  TYR A C   1 
ATOM   470  O O   . TYR A 1 59  ? 26.459  61      25.223  1   47.42  ? 59  TYR A O   1 
ATOM   471  C CB  . TYR A 1 59  ? 25.88   62.016  27.581  1   50.32  ? 59  TYR A CB  1 
ATOM   472  C CG  . TYR A 1 59  ? 25.608  62.73   28.871  1   48.48  ? 59  TYR A CG  1 
ATOM   473  C CD1 . TYR A 1 59  ? 26.405  63.811  29.254  1   52.1   ? 59  TYR A CD1 1 
ATOM   474  C CD2 . TYR A 1 59  ? 24.545  62.366  29.681  1   51.59  ? 59  TYR A CD2 1 
ATOM   475  C CE1 . TYR A 1 59  ? 26.153  64.496  30.427  1   51.45  ? 59  TYR A CE1 1 
ATOM   476  C CE2 . TYR A 1 59  ? 24.277  63.056  30.856  1   51.47  ? 59  TYR A CE2 1 
ATOM   477  C CZ  . TYR A 1 59  ? 25.086  64.117  31.223  1   52.24  ? 59  TYR A CZ  1 
ATOM   478  O OH  . TYR A 1 59  ? 24.794  64.79   32.356  1   53.12  ? 59  TYR A OH  1 
ATOM   479  N N   . PRO A 1 60  ? 25.423  62.443  23.88   1   49.62  ? 60  PRO A N   1 
ATOM   480  C CA  . PRO A 1 60  ? 25.572  61.565  22.713  1   52.04  ? 60  PRO A CA  1 
ATOM   481  C C   . PRO A 1 60  ? 27.022  61.106  22.498  1   54.57  ? 60  PRO A C   1 
ATOM   482  O O   . PRO A 1 60  ? 27.277  59.971  22.134  1   48.5   ? 60  PRO A O   1 
ATOM   483  C CB  . PRO A 1 60  ? 24.999  62.428  21.557  1   49.76  ? 60  PRO A CB  1 
ATOM   484  C CG  . PRO A 1 60  ? 25.227  63.857  22.024  1   50     ? 60  PRO A CG  1 
ATOM   485  C CD  . PRO A 1 60  ? 24.918  63.788  23.538  1   49.98  ? 60  PRO A CD  1 
ATOM   486  N N   . ASP A 1 61  ? 27.978  61.991  22.799  1   56.42  ? 61  ASP A N   1 
ATOM   487  C CA  . ASP A 1 61  ? 29.4    61.714  22.678  1   56.37  ? 61  ASP A CA  1 
ATOM   488  C C   . ASP A 1 61  ? 29.92   60.736  23.754  1   49.05  ? 61  ASP A C   1 
ATOM   489  O O   . ASP A 1 61  ? 30.953  60.154  23.509  1   52.39  ? 61  ASP A O   1 
ATOM   490  C CB  . ASP A 1 61  ? 30.17   63.035  22.626  1   66.32  ? 61  ASP A CB  1 
ATOM   491  C CG  . ASP A 1 61  ? 29.94   63.994  23.791  1   73.41  ? 61  ASP A CG  1 
ATOM   492  O OD1 . ASP A 1 61  ? 28.758  64.292  24.087  1   76.02  ? 61  ASP A OD1 1 
ATOM   493  O OD2 . ASP A 1 61  ? 30.935  64.457  24.402  1   95.39  ? 61  ASP A OD2 1 
ATOM   494  N N   . ARG A 1 62  ? 29.26   60.546  24.909  1   47.07  ? 62  ARG A N   1 
ATOM   495  C CA  . ARG A 1 62  ? 29.727  59.68   25.996  1   51.69  ? 62  ARG A CA  1 
ATOM   496  C C   . ARG A 1 62  ? 28.907  58.364  26.097  1   50.05  ? 62  ARG A C   1 
ATOM   497  O O   . ARG A 1 62  ? 28.954  57.694  27.131  1   51.63  ? 62  ARG A O   1 
ATOM   498  C CB  . ARG A 1 62  ? 29.749  60.395  27.366  1   55.45  ? 62  ARG A CB  1 
ATOM   499  C CG  . ARG A 1 62  ? 30.603  61.639  27.64   1   58.1   ? 62  ARG A CG  1 
ATOM   500  C CD  . ARG A 1 62  ? 30.385  62.298  29.004  1   60.91  ? 62  ARG A CD  1 
ATOM   501  N NE  . ARG A 1 62  ? 30.855  61.573  30.199  1   59.46  ? 62  ARG A NE  1 
ATOM   502  C CZ  . ARG A 1 62  ? 30.584  61.844  31.479  1   67.6   ? 62  ARG A CZ  1 
ATOM   503  N NH1 . ARG A 1 62  ? 29.923  62.941  31.826  1   73.19  ? 62  ARG A NH1 1 
ATOM   504  N NH2 . ARG A 1 62  ? 30.98   61.027  32.456  1   68.4   ? 62  ARG A NH2 1 
ATOM   505  N N   . GLU A 1 63  ? 28.167  57.947  25.042  1   44.52  ? 63  GLU A N   1 
ATOM   506  C CA  . GLU A 1 63  ? 27.167  56.88   25.191  1   44.63  ? 63  GLU A CA  1 
ATOM   507  C C   . GLU A 1 63  ? 27.811  55.583  25.719  1   39.79  ? 63  GLU A C   1 
ATOM   508  O O   . GLU A 1 63  ? 27.416  55.082  26.769  1   40.57  ? 63  GLU A O   1 
ATOM   509  C CB  . GLU A 1 63  ? 26.344  56.662  23.922  1   39.58  ? 63  GLU A CB  1 
ATOM   510  C CG  . GLU A 1 63  ? 25.234  55.62   24.094  1   42.09  ? 63  GLU A CG  1 
ATOM   511  C CD  . GLU A 1 63  ? 24.361  55.367  22.874  1   45.39  ? 63  GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 63  ? 24.412  56.165  21.906  1   45.12  ? 63  GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 63  ? 23.619  54.352  22.9    1   42.25  ? 63  GLU A OE2 1 
ATOM   514  N N   . TYR A 1 64  ? 28.84   55.098  25.021  1   45.9   ? 64  TYR A N   1 
ATOM   515  C CA  . TYR A 1 64  ? 29.463  53.815  25.354  1   46.33  ? 64  TYR A CA  1 
ATOM   516  C C   . TYR A 1 64  ? 29.972  53.81   26.785  1   50.87  ? 64  TYR A C   1 
ATOM   517  O O   . TYR A 1 64  ? 29.576  52.935  27.574  1   45.96  ? 64  TYR A O   1 
ATOM   518  C CB  . TYR A 1 64  ? 30.503  53.426  24.298  1   49.12  ? 64  TYR A CB  1 
ATOM   519  C CG  . TYR A 1 64  ? 31.102  52.063  24.615  1   49.17  ? 64  TYR A CG  1 
ATOM   520  C CD1 . TYR A 1 64  ? 30.482  50.905  24.164  1   50.06  ? 64  TYR A CD1 1 
ATOM   521  C CD2 . TYR A 1 64  ? 32.238  51.93   25.416  1   52     ? 64  TYR A CD2 1 
ATOM   522  C CE1 . TYR A 1 64  ? 31.005  49.651  24.452  1   51.2   ? 64  TYR A CE1 1 
ATOM   523  C CE2 . TYR A 1 64  ? 32.749  50.687  25.753  1   53.39  ? 64  TYR A CE2 1 
ATOM   524  C CZ  . TYR A 1 64  ? 32.125  49.545  25.271  1   53.91  ? 64  TYR A CZ  1 
ATOM   525  O OH  . TYR A 1 64  ? 32.67   48.336  25.562  1   55.56  ? 64  TYR A OH  1 
ATOM   526  N N   . GLU A 1 65  ? 30.789  54.837  27.135  1   53.05  ? 65  GLU A N   1 
ATOM   527  C CA  . GLU A 1 65  ? 31.389  54.974  28.443  1   48.88  ? 65  GLU A CA  1 
ATOM   528  C C   . GLU A 1 65  ? 30.315  54.868  29.512  1   50.84  ? 65  GLU A C   1 
ATOM   529  O O   . GLU A 1 65  ? 30.467  54.121  30.48   1   47.61  ? 65  GLU A O   1 
ATOM   530  C CB  . GLU A 1 65  ? 32.109  56.333  28.546  1   55.06  ? 65  GLU A CB  1 
ATOM   531  C CG  . GLU A 1 65  ? 32.638  56.731  29.931  1   60.89  ? 65  GLU A CG  1 
ATOM   532  C CD  . GLU A 1 65  ? 32.549  58.196  30.362  1   60.16  ? 65  GLU A CD  1 
ATOM   533  O OE1 . GLU A 1 65  ? 32.429  59.07   29.488  1   64.18  ? 65  GLU A OE1 1 
ATOM   534  O OE2 . GLU A 1 65  ? 32.6    58.476  31.564  1   62.65  ? 65  GLU A OE2 1 
ATOM   535  N N   . LEU A 1 66  ? 29.252  55.685  29.377  1   47.58  ? 66  LEU A N   1 
ATOM   536  C CA  . LEU A 1 66  ? 28.279  55.778  30.444  1   47.45  ? 66  LEU A CA  1 
ATOM   537  C C   . LEU A 1 66  ? 27.48   54.485  30.542  1   42.89  ? 66  LEU A C   1 
ATOM   538  O O   . LEU A 1 66  ? 27.199  54.046  31.657  1   44.74  ? 66  LEU A O   1 
ATOM   539  C CB  . LEU A 1 66  ? 27.4    57.009  30.236  1   50.07  ? 66  LEU A CB  1 
ATOM   540  C CG  . LEU A 1 66  ? 28.14   58.349  30.348  1   54.4   ? 66  LEU A CG  1 
ATOM   541  C CD1 . LEU A 1 66  ? 27.354  59.546  29.796  1   53.71  ? 66  LEU A CD1 1 
ATOM   542  C CD2 . LEU A 1 66  ? 28.574  58.575  31.793  1   55.33  ? 66  LEU A CD2 1 
ATOM   543  N N   . MET A 1 67  ? 27.084  53.93   29.381  1   45.1   ? 67  MET A N   1 
ATOM   544  C CA  . MET A 1 67  ? 26.249  52.736  29.359  1   43.87  ? 67  MET A CA  1 
ATOM   545  C C   . MET A 1 67  ? 27.026  51.494  29.812  1   44.77  ? 67  MET A C   1 
ATOM   546  O O   . MET A 1 67  ? 26.467  50.66   30.523  1   41.44  ? 67  MET A O   1 
ATOM   547  C CB  . MET A 1 67  ? 25.604  52.558  27.975  1   40.74  ? 67  MET A CB  1 
ATOM   548  C CG  . MET A 1 67  ? 24.576  53.652  27.67   1   40.47  ? 67  MET A CG  1 
ATOM   549  S SD  . MET A 1 67  ? 23.26   53.756  28.891  1   42.92  ? 67  MET A SD  1 
ATOM   550  C CE  . MET A 1 67  ? 22.435  52.187  28.607  1   46.31  ? 67  MET A CE  1 
ATOM   551  N N   . LYS A 1 68  ? 28.306  51.37   29.427  1   48.3   ? 68  LYS A N   1 
ATOM   552  C CA  . LYS A 1 68  ? 29.207  50.341  29.964  1   45.12  ? 68  LYS A CA  1 
ATOM   553  C C   . LYS A 1 68  ? 29.199  50.312  31.48   1   46.66  ? 68  LYS A C   1 
ATOM   554  O O   . LYS A 1 68  ? 28.942  49.276  32.092  1   44.44  ? 68  LYS A O   1 
ATOM   555  C CB  . LYS A 1 68  ? 30.611  50.527  29.387  1   50.28  ? 68  LYS A CB  1 
ATOM   556  C CG  . LYS A 1 68  ? 31.662  49.671  30.067  1   56.25  ? 68  LYS A CG  1 
ATOM   557  C CD  . LYS A 1 68  ? 32.791  49.207  29.166  1   61.03  ? 68  LYS A CD  1 
ATOM   558  C CE  . LYS A 1 68  ? 33.686  48.363  30.029  1   61.4   ? 68  LYS A CE  1 
ATOM   559  N NZ  . LYS A 1 68  ? 35.081  48.563  29.674  1   63.79  ? 68  LYS A NZ  1 
ATOM   560  N N   . ASP A 1 69  ? 29.473  51.472  32.09   1   46.25  ? 69  ASP A N   1 
ATOM   561  C CA  . ASP A 1 69  ? 29.509  51.563  33.528  1   47.86  ? 69  ASP A CA  1 
ATOM   562  C C   . ASP A 1 69  ? 28.124  51.295  34.114  1   48.55  ? 69  ASP A C   1 
ATOM   563  O O   . ASP A 1 69  ? 28.013  50.63   35.135  1   47.79  ? 69  ASP A O   1 
ATOM   564  C CB  . ASP A 1 69  ? 30.035  52.924  33.943  1   51.57  ? 69  ASP A CB  1 
ATOM   565  C CG  . ASP A 1 69  ? 29.9    53.193  35.43   1   56.46  ? 69  ASP A CG  1 
ATOM   566  O OD1 . ASP A 1 69  ? 30.743  52.687  36.204  1   58.31  ? 69  ASP A OD1 1 
ATOM   567  O OD2 . ASP A 1 69  ? 28.915  53.867  35.8    1   59.98  ? 69  ASP A OD2 1 
ATOM   568  N N   . TYR A 1 70  ? 27.067  51.848  33.495  1   47.41  ? 70  TYR A N   1 
ATOM   569  C CA  . TYR A 1 70  ? 25.717  51.66   34.006  1   47.95  ? 70  TYR A CA  1 
ATOM   570  C C   . TYR A 1 70  ? 25.345  50.177  33.96   1   44.46  ? 70  TYR A C   1 
ATOM   571  O O   . TYR A 1 70  ? 24.897  49.638  34.955  1   44.8   ? 70  TYR A O   1 
ATOM   572  C CB  . TYR A 1 70  ? 24.694  52.506  33.224  1   48.93  ? 70  TYR A CB  1 
ATOM   573  C CG  . TYR A 1 70  ? 23.282  52.355  33.771  1   49.68  ? 70  TYR A CG  1 
ATOM   574  C CD1 . TYR A 1 70  ? 22.951  52.865  35.018  1   49.56  ? 70  TYR A CD1 1 
ATOM   575  C CD2 . TYR A 1 70  ? 22.293  51.694  33.049  1   48.4   ? 70  TYR A CD2 1 
ATOM   576  C CE1 . TYR A 1 70  ? 21.692  52.689  35.567  1   53.61  ? 70  TYR A CE1 1 
ATOM   577  C CE2 . TYR A 1 70  ? 21.018  51.529  33.58   1   51.36  ? 70  TYR A CE2 1 
ATOM   578  C CZ  . TYR A 1 70  ? 20.712  52.036  34.831  1   51.74  ? 70  TYR A CZ  1 
ATOM   579  O OH  . TYR A 1 70  ? 19.464  51.88   35.356  1   54.14  ? 70  TYR A OH  1 
ATOM   580  N N   . CYS A 1 71  ? 25.525  49.543  32.792  1   48.23  ? 71  CYS A N   1 
ATOM   581  C CA  . CYS A 1 71  ? 25.073  48.167  32.553  1   50.21  ? 71  CYS A CA  1 
ATOM   582  C C   . CYS A 1 71  ? 25.816  47.168  33.436  1   49.91  ? 71  CYS A C   1 
ATOM   583  O O   . CYS A 1 71  ? 25.171  46.288  33.996  1   53.04  ? 71  CYS A O   1 
ATOM   584  C CB  . CYS A 1 71  ? 25.215  47.726  31.092  1   48.98  ? 71  CYS A CB  1 
ATOM   585  S SG  . CYS A 1 71  ? 24.245  48.661  29.873  1   49.89  ? 71  CYS A SG  1 
ATOM   586  N N   . LEU A 1 72  ? 27.138  47.362  33.615  1   55.22  ? 72  LEU A N   1 
ATOM   587  C CA  . LEU A 1 72  ? 27.991  46.501  34.434  1   59.7   ? 72  LEU A CA  1 
ATOM   588  C C   . LEU A 1 72  ? 27.681  46.626  35.927  1   58.85  ? 72  LEU A C   1 
ATOM   589  O O   . LEU A 1 72  ? 28.067  45.738  36.682  1   58.54  ? 72  LEU A O   1 
ATOM   590  C CB  . LEU A 1 72  ? 29.475  46.821  34.227  1   72.45  ? 72  LEU A CB  1 
ATOM   591  C CG  . LEU A 1 72  ? 30.286  45.971  33.236  1   81.96  ? 72  LEU A CG  1 
ATOM   592  C CD1 . LEU A 1 72  ? 29.888  46.009  31.757  1   77.28  ? 72  LEU A CD1 1 
ATOM   593  C CD2 . LEU A 1 72  ? 31.75   46.405  33.442  1   93.13  ? 72  LEU A CD2 1 
ATOM   594  N N   . ASN A 1 73  ? 27.018  47.716  36.351  1   54.53  ? 73  ASN A N   1 
ATOM   595  C CA  . ASN A 1 73  ? 26.562  47.88   37.727  1   53.8   ? 73  ASN A CA  1 
ATOM   596  C C   . ASN A 1 73  ? 25.121  47.429  37.975  1   53.25  ? 73  ASN A C   1 
ATOM   597  O O   . ASN A 1 73  ? 24.683  47.461  39.125  1   48.76  ? 73  ASN A O   1 
ATOM   598  C CB  . ASN A 1 73  ? 26.762  49.313  38.199  1   56.13  ? 73  ASN A CB  1 
ATOM   599  C CG  . ASN A 1 73  ? 28.051  49.394  38.975  1   59.86  ? 73  ASN A CG  1 
ATOM   600  O OD1 . ASN A 1 73  ? 28.117  48.938  40.123  1   57.25  ? 73  ASN A OD1 1 
ATOM   601  N ND2 . ASN A 1 73  ? 29.089  49.888  38.325  1   61.99  ? 73  ASN A ND2 1 
ATOM   602  N N   . LEU A 1 74  ? 24.42   46.93   36.941  1   49.18  ? 74  LEU A N   1 
ATOM   603  C CA  . LEU A 1 74  ? 23.058  46.447  37.134  1   50.95  ? 74  LEU A CA  1 
ATOM   604  C C   . LEU A 1 74  ? 23.088  45.127  37.9    1   51.62  ? 74  LEU A C   1 
ATOM   605  O O   . LEU A 1 74  ? 24.012  44.339  37.721  1   52.12  ? 74  LEU A O   1 
ATOM   606  C CB  . LEU A 1 74  ? 22.3    46.319  35.811  1   44.83  ? 74  LEU A CB  1 
ATOM   607  C CG  . LEU A 1 74  ? 21.938  47.64   35.119  1   45.83  ? 74  LEU A CG  1 
ATOM   608  C CD1 . LEU A 1 74  ? 21.486  47.357  33.71   1   42.52  ? 74  LEU A CD1 1 
ATOM   609  C CD2 . LEU A 1 74  ? 20.896  48.516  35.863  1   48.51  ? 74  LEU A CD2 1 
ATOM   610  N N   . ASP A 1 75  ? 22.088  44.932  38.779  1   54.51  ? 75  ASP A N   1 
ATOM   611  C CA  . ASP A 1 75  ? 21.742  43.633  39.329  1   56.03  ? 75  ASP A CA  1 
ATOM   612  C C   . ASP A 1 75  ? 21.257  42.762  38.17   1   56.71  ? 75  ASP A C   1 
ATOM   613  O O   . ASP A 1 75  ? 20.236  43.068  37.555  1   50.56  ? 75  ASP A O   1 
ATOM   614  C CB  . ASP A 1 75  ? 20.698  43.791  40.42   1   58.84  ? 75  ASP A CB  1 
ATOM   615  C CG  . ASP A 1 75  ? 20.16   42.515  41.057  1   61.14  ? 75  ASP A CG  1 
ATOM   616  O OD1 . ASP A 1 75  ? 20.459  41.407  40.55   1   59.27  ? 75  ASP A OD1 1 
ATOM   617  O OD2 . ASP A 1 75  ? 19.395  42.64   42.026  1   62.5   ? 75  ASP A OD2 1 
ATOM   618  N N   . VAL A 1 76  ? 21.973  41.658  37.902  1   56.44  ? 76  VAL A N   1 
ATOM   619  C CA  . VAL A 1 76  ? 21.784  40.898  36.667  1   55.98  ? 76  VAL A CA  1 
ATOM   620  C C   . VAL A 1 76  ? 20.488  40.084  36.702  1   55.99  ? 76  VAL A C   1 
ATOM   621  O O   . VAL A 1 76  ? 20.059  39.591  35.67   1   59.95  ? 76  VAL A O   1 
ATOM   622  C CB  . VAL A 1 76  ? 23.015  40.036  36.33   1   56.18  ? 76  VAL A CB  1 
ATOM   623  C CG1 . VAL A 1 76  ? 24.234  40.927  36.106  1   55.9   ? 76  VAL A CG1 1 
ATOM   624  C CG2 . VAL A 1 76  ? 23.323  38.953  37.363  1   59.73  ? 76  VAL A CG2 1 
ATOM   625  N N   . LYS A 1 77  ? 19.819  40.022  37.861  1   57.19  ? 77  LYS A N   1 
ATOM   626  C CA  . LYS A 1 77  ? 18.544  39.339  38.017  1   57.68  ? 77  LYS A CA  1 
ATOM   627  C C   . LYS A 1 77  ? 17.373  40.214  37.589  1   51.5   ? 77  LYS A C   1 
ATOM   628  O O   . LYS A 1 77  ? 16.265  39.698  37.567  1   54.98  ? 77  LYS A O   1 
ATOM   629  C CB  . LYS A 1 77  ? 18.393  38.902  39.489  1   65.05  ? 77  LYS A CB  1 
ATOM   630  C CG  . LYS A 1 77  ? 19.476  37.931  39.978  1   69.26  ? 77  LYS A CG  1 
ATOM   631  C CD  . LYS A 1 77  ? 19.302  37.392  41.39   1   73.72  ? 77  LYS A CD  1 
ATOM   632  C CE  . LYS A 1 77  ? 19.58   38.434  42.401  1   75.26  ? 77  LYS A CE  1 
ATOM   633  N NZ  . LYS A 1 77  ? 19.572  37.776  43.705  1   83.3   ? 77  LYS A NZ  1 
ATOM   634  N N   . THR A 1 78  ? 17.599  41.491  37.218  1   49.18  ? 78  THR A N   1 
ATOM   635  C CA  . THR A 1 78  ? 16.527  42.442  36.957  1   47.25  ? 78  THR A CA  1 
ATOM   636  C C   . THR A 1 78  ? 16.15   42.513  35.465  1   44.96  ? 78  THR A C   1 
ATOM   637  O O   . THR A 1 78  ? 16.938  42.219  34.56   1   43.98  ? 78  THR A O   1 
ATOM   638  C CB  . THR A 1 78  ? 16.903  43.846  37.443  1   47.08  ? 78  THR A CB  1 
ATOM   639  O OG1 . THR A 1 78  ? 17.981  44.303  36.619  1   43.54  ? 78  THR A OG1 1 
ATOM   640  C CG2 . THR A 1 78  ? 17.21   43.901  38.933  1   49.93  ? 78  THR A CG2 1 
ATOM   641  N N   . LYS A 1 79  ? 14.932  43.006  35.239  1   43.29  ? 79  LYS A N   1 
ATOM   642  C CA  . LYS A 1 79  ? 14.447  43.444  33.943  1   44.66  ? 79  LYS A CA  1 
ATOM   643  C C   . LYS A 1 79  ? 15.41   44.441  33.292  1   44.24  ? 79  LYS A C   1 
ATOM   644  O O   . LYS A 1 79  ? 15.644  44.402  32.061  1   41.14  ? 79  LYS A O   1 
ATOM   645  C CB  . LYS A 1 79  ? 13.076  44.096  34.14   1   47.86  ? 79  LYS A CB  1 
ATOM   646  C CG  . LYS A 1 79  ? 12.382  44.461  32.826  1   46.71  ? 79  LYS A CG  1 
ATOM   647  C CD  . LYS A 1 79  ? 11.072  45.2    33.033  1   50.8   ? 79  LYS A CD  1 
ATOM   648  C CE  . LYS A 1 79  ? 10.566  45.693  31.732  1   50.51  ? 79  LYS A CE  1 
ATOM   649  N NZ  . LYS A 1 79  ? 9.272   46.338  31.892  1   55.05  ? 79  LYS A NZ  1 
ATOM   650  N N   . ALA A 1 80  ? 15.956  45.354  34.11   1   41.08  ? 80  ALA A N   1 
ATOM   651  C CA  . ALA A 1 80  ? 16.909  46.323  33.601  1   40.7   ? 80  ALA A CA  1 
ATOM   652  C C   . ALA A 1 80  ? 18.097  45.625  32.931  1   40.73  ? 80  ALA A C   1 
ATOM   653  O O   . ALA A 1 80  ? 18.49   46.049  31.847  1   38.63  ? 80  ALA A O   1 
ATOM   654  C CB  . ALA A 1 80  ? 17.331  47.265  34.699  1   44.07  ? 80  ALA A CB  1 
ATOM   655  N N   . ALA A 1 81  ? 18.645  44.575  33.57   1   43.63  ? 81  ALA A N   1 
ATOM   656  C CA  . ALA A 1 81  ? 19.806  43.85   33.062  1   41.53  ? 81  ALA A CA  1 
ATOM   657  C C   . ALA A 1 81  ? 19.479  43.077  31.793  1   39.78  ? 81  ALA A C   1 
ATOM   658  O O   . ALA A 1 81  ? 20.286  43.047  30.859  1   38.15  ? 81  ALA A O   1 
ATOM   659  C CB  . ALA A 1 81  ? 20.354  42.896  34.11   1   42.18  ? 81  ALA A CB  1 
ATOM   660  N N   . ARG A 1 82  ? 18.297  42.447  31.768  1   41.08  ? 82  ARG A N   1 
ATOM   661  C CA  . ARG A 1 82  ? 17.817  41.79   30.545  1   39.11  ? 82  ARG A CA  1 
ATOM   662  C C   . ARG A 1 82  ? 17.675  42.76   29.373  1   36.6   ? 82  ARG A C   1 
ATOM   663  O O   . ARG A 1 82  ? 18.1    42.435  28.246  1   35.34  ? 82  ARG A O   1 
ATOM   664  C CB  . ARG A 1 82  ? 16.521  41.042  30.861  1   40.88  ? 82  ARG A CB  1 
ATOM   665  C CG  . ARG A 1 82  ? 16.835  39.847  31.749  1   41.81  ? 82  ARG A CG  1 
ATOM   666  C CD  . ARG A 1 82  ? 15.606  38.966  31.906  1   45.77  ? 82  ARG A CD  1 
ATOM   667  N NE  . ARG A 1 82  ? 14.483  39.585  32.621  1   47.49  ? 82  ARG A NE  1 
ATOM   668  C CZ  . ARG A 1 82  ? 14.348  39.63   33.941  1   51.04  ? 82  ARG A CZ  1 
ATOM   669  N NH1 . ARG A 1 82  ? 13.252  40.133  34.457  1   53.02  ? 82  ARG A NH1 1 
ATOM   670  N NH2 . ARG A 1 82  ? 15.278  39.166  34.752  1   52.18  ? 82  ARG A NH2 1 
ATOM   671  N N   . SER A 1 83  ? 17.129  43.953  29.642  1   37.33  ? 83  SER A N   1 
ATOM   672  C CA  . SER A 1 83  ? 17.026  45.01   28.64   1   38.18  ? 83  SER A CA  1 
ATOM   673  C C   . SER A 1 83  ? 18.41   45.486  28.178  1   35.18  ? 83  SER A C   1 
ATOM   674  O O   . SER A 1 83  ? 18.613  45.734  26.994  1   33.77  ? 83  SER A O   1 
ATOM   675  C CB  . SER A 1 83  ? 16.192  46.163  29.146  1   40.27  ? 83  SER A CB  1 
ATOM   676  O OG  . SER A 1 83  ? 14.924  45.729  29.623  1   41.72  ? 83  SER A OG  1 
ATOM   677  N N   . ALA A 1 84  ? 19.35   45.615  29.126  1   35.56  ? 84  ALA A N   1 
ATOM   678  C CA  . ALA A 1 84  ? 20.729  46.012  28.87   1   34.91  ? 84  ALA A CA  1 
ATOM   679  C C   . ALA A 1 84  ? 21.449  45.02   27.955  1   34.24  ? 84  ALA A C   1 
ATOM   680  O O   . ALA A 1 84  ? 22.215  45.424  27.08   1   32.91  ? 84  ALA A O   1 
ATOM   681  C CB  . ALA A 1 84  ? 21.445  46.168  30.216  1   37.91  ? 84  ALA A CB  1 
ATOM   682  N N   . LEU A 1 85  ? 21.15   43.722  28.096  1   33.19  ? 85  LEU A N   1 
ATOM   683  C CA  . LEU A 1 85  ? 21.737  42.711  27.231  1   33.96  ? 85  LEU A CA  1 
ATOM   684  C C   . LEU A 1 85  ? 21.253  42.883  25.792  1   32.39  ? 85  LEU A C   1 
ATOM   685  O O   . LEU A 1 85  ? 22.075  42.862  24.867  1   31.34  ? 85  LEU A O   1 
ATOM   686  C CB  . LEU A 1 85  ? 21.42   41.321  27.784  1   35.58  ? 85  LEU A CB  1 
ATOM   687  C CG  . LEU A 1 85  ? 21.875  40.116  26.953  1   37.73  ? 85  LEU A CG  1 
ATOM   688  C CD1 . LEU A 1 85  ? 23.339  40.23   26.636  1   39.32  ? 85  LEU A CD1 1 
ATOM   689  C CD2 . LEU A 1 85  ? 21.608  38.836  27.723  1   40.04  ? 85  LEU A CD2 1 
ATOM   690  N N   . GLU A 1 86  ? 19.937  43.13   25.615  1   32.64  ? 86  GLU A N   1 
ATOM   691  C CA  . GLU A 1 86  ? 19.409  43.44   24.301  1   30.97  ? 86  GLU A CA  1 
ATOM   692  C C   . GLU A 1 86  ? 20.059  44.704  23.725  1   31.94  ? 86  GLU A C   1 
ATOM   693  O O   . GLU A 1 86  ? 20.422  44.731  22.557  1   33.02  ? 86  GLU A O   1 
ATOM   694  C CB  . GLU A 1 86  ? 17.886  43.487  24.317  1   31.41  ? 86  GLU A CB  1 
ATOM   695  C CG  . GLU A 1 86  ? 17.269  44.011  23.025  1   28.85  ? 86  GLU A CG  1 
ATOM   696  C CD  . GLU A 1 86  ? 17.603  43.239  21.761  1   28.33  ? 86  GLU A CD  1 
ATOM   697  O OE1 . GLU A 1 86  ? 18.187  42.154  21.861  1   27.75  ? 86  GLU A OE1 1 
ATOM   698  O OE2 . GLU A 1 86  ? 17.236  43.738  20.685  1   30.07  ? 86  GLU A OE2 1 
ATOM   699  N N   . TYR A 1 87  ? 20.157  45.765  24.538  1   32.96  ? 87  TYR A N   1 
ATOM   700  C CA  . TYR A 1 87  ? 20.816  46.998  24.129  1   32.33  ? 87  TYR A CA  1 
ATOM   701  C C   . TYR A 1 87  ? 22.219  46.681  23.61   1   31.05  ? 87  TYR A C   1 
ATOM   702  O O   . TYR A 1 87  ? 22.575  47.113  22.5    1   30.21  ? 87  TYR A O   1 
ATOM   703  C CB  . TYR A 1 87  ? 20.797  47.991  25.31   1   32.94  ? 87  TYR A CB  1 
ATOM   704  C CG  . TYR A 1 87  ? 21.718  49.178  25.124  1   34.34  ? 87  TYR A CG  1 
ATOM   705  C CD1 . TYR A 1 87  ? 21.324  50.284  24.361  1   35.77  ? 87  TYR A CD1 1 
ATOM   706  C CD2 . TYR A 1 87  ? 22.984  49.194  25.71   1   35.45  ? 87  TYR A CD2 1 
ATOM   707  C CE1 . TYR A 1 87  ? 22.186  51.354  24.151  1   37.34  ? 87  TYR A CE1 1 
ATOM   708  C CE2 . TYR A 1 87  ? 23.849  50.263  25.519  1   35.09  ? 87  TYR A CE2 1 
ATOM   709  C CZ  . TYR A 1 87  ? 23.445  51.346  24.749  1   38.32  ? 87  TYR A CZ  1 
ATOM   710  O OH  . TYR A 1 87  ? 24.266  52.414  24.579  1   39.43  ? 87  TYR A OH  1 
ATOM   711  N N   . ALA A 1 88  ? 23.003  45.965  24.431  1   33.69  ? 88  ALA A N   1 
ATOM   712  C CA  . ALA A 1 88  ? 24.39   45.682  24.119  1   33.31  ? 88  ALA A CA  1 
ATOM   713  C C   . ALA A 1 88  ? 24.454  44.845  22.836  1   31.67  ? 88  ALA A C   1 
ATOM   714  O O   . ALA A 1 88  ? 25.225  45.156  21.947  1   32.87  ? 88  ALA A O   1 
ATOM   715  C CB  . ALA A 1 88  ? 25.058  45.009  25.307  1   33.78  ? 88  ALA A CB  1 
ATOM   716  N N   . ASP A 1 89  ? 23.599  43.816  22.696  1   30.98  ? 89  ASP A N   1 
ATOM   717  C CA  . ASP A 1 89  ? 23.653  42.992  21.484  1   30.63  ? 89  ASP A CA  1 
ATOM   718  C C   . ASP A 1 89  ? 23.218  43.744  20.233  1   29.99  ? 89  ASP A C   1 
ATOM   719  O O   . ASP A 1 89  ? 23.846  43.608  19.192  1   30.8   ? 89  ASP A O   1 
ATOM   720  C CB  . ASP A 1 89  ? 22.85   41.722  21.67   1   32.87  ? 89  ASP A CB  1 
ATOM   721  C CG  . ASP A 1 89  ? 23.021  40.749  20.525  1   34.2   ? 89  ASP A CG  1 
ATOM   722  O OD1 . ASP A 1 89  ? 22.288  40.938  19.524  1   29.96  ? 89  ASP A OD1 1 
ATOM   723  O OD2 . ASP A 1 89  ? 23.914  39.86   20.664  1   35.89  ? 89  ASP A OD2 1 
ATOM   724  N N   . ALA A 1 90  ? 22.14   44.544  20.328  1   29.12  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 90  ? 21.628  45.316  19.21   1   27.48  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 90  ? 22.708  46.28   18.703  1   29.17  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 90  ? 22.86   46.47   17.502  1   28.46  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 90  ? 20.395  46.07   19.647  1   30.32  ? 90  ALA A CB  1 
ATOM   729  N N   . ASN A 1 91  ? 23.45   46.891  19.645  1   28.65  ? 91  ASN A N   1 
ATOM   730  C CA  . ASN A 1 91  ? 24.502  47.842  19.289  1   32.91  ? 91  ASN A CA  1 
ATOM   731  C C   . ASN A 1 91  ? 25.831  47.158  18.935  1   34.22  ? 91  ASN A C   1 
ATOM   732  O O   . ASN A 1 91  ? 26.775  47.861  18.574  1   38.68  ? 91  ASN A O   1 
ATOM   733  C CB  . ASN A 1 91  ? 24.726  48.865  20.404  1   31.34  ? 91  ASN A CB  1 
ATOM   734  C CG  . ASN A 1 91  ? 23.625  49.912  20.409  1   31.83  ? 91  ASN A CG  1 
ATOM   735  O OD1 . ASN A 1 91  ? 23.712  50.9    19.692  1   31.98  ? 91  ASN A OD1 1 
ATOM   736  N ND2 . ASN A 1 91  ? 22.619  49.767  21.247  1   31.71  ? 91  ASN A ND2 1 
ATOM   737  N N   . MET A 1 92  ? 25.938  45.833  19.104  1   33.73  ? 92  MET A N   1 
ATOM   738  C CA  . MET A 1 92  ? 27.172  45.075  18.957  1   34.4   ? 92  MET A CA  1 
ATOM   739  C C   . MET A 1 92  ? 28.258  45.616  19.878  1   37.97  ? 92  MET A C   1 
ATOM   740  O O   . MET A 1 92  ? 29.416  45.68   19.493  1   39.89  ? 92  MET A O   1 
ATOM   741  C CB  . MET A 1 92  ? 27.585  45.024  17.484  1   34.48  ? 92  MET A CB  1 
ATOM   742  C CG  . MET A 1 92  ? 26.553  44.329  16.592  1   34.46  ? 92  MET A CG  1 
ATOM   743  S SD  . MET A 1 92  ? 27.093  44.223  14.881  1   37.52  ? 92  MET A SD  1 
ATOM   744  C CE  . MET A 1 92  ? 25.762  43.219  14.209  1   42.68  ? 92  MET A CE  1 
ATOM   745  N N   . PHE A 1 93  ? 27.881  45.945  21.129  1   35.49  ? 93  PHE A N   1 
ATOM   746  C CA  . PHE A 1 93  ? 28.821  46.26   22.183  1   38.57  ? 93  PHE A CA  1 
ATOM   747  C C   . PHE A 1 93  ? 29.2    44.952  22.861  1   36.52  ? 93  PHE A C   1 
ATOM   748  O O   . PHE A 1 93  ? 28.73   44.654  23.958  1   40.94  ? 93  PHE A O   1 
ATOM   749  C CB  . PHE A 1 93  ? 28.171  47.282  23.135  1   40.08  ? 93  PHE A CB  1 
ATOM   750  C CG  . PHE A 1 93  ? 27.847  48.663  22.566  1   36.28  ? 93  PHE A CG  1 
ATOM   751  C CD1 . PHE A 1 93  ? 28.473  49.168  21.425  1   37.81  ? 93  PHE A CD1 1 
ATOM   752  C CD2 . PHE A 1 93  ? 26.962  49.498  23.238  1   39.57  ? 93  PHE A CD2 1 
ATOM   753  C CE1 . PHE A 1 93  ? 28.184  50.435  20.943  1   38.15  ? 93  PHE A CE1 1 
ATOM   754  C CE2 . PHE A 1 93  ? 26.678  50.761  22.754  1   37.25  ? 93  PHE A CE2 1 
ATOM   755  C CZ  . PHE A 1 93  ? 27.288  51.231  21.622  1   41.8   ? 93  PHE A CZ  1 
ATOM   756  N N   . PHE A 1 94  ? 30.061  44.18   22.191  1   39     ? 94  PHE A N   1 
ATOM   757  C CA  . PHE A 1 94  ? 30.389  42.814  22.583  1   39.56  ? 94  PHE A CA  1 
ATOM   758  C C   . PHE A 1 94  ? 31.012  42.709  23.975  1   41.96  ? 94  PHE A C   1 
ATOM   759  O O   . PHE A 1 94  ? 30.709  41.754  24.693  1   42.73  ? 94  PHE A O   1 
ATOM   760  C CB  . PHE A 1 94  ? 31.312  42.192  21.527  1   42.81  ? 94  PHE A CB  1 
ATOM   761  C CG  . PHE A 1 94  ? 30.767  42.109  20.111  1   43.39  ? 94  PHE A CG  1 
ATOM   762  C CD1 . PHE A 1 94  ? 29.429  41.772  19.846  1   45.12  ? 94  PHE A CD1 1 
ATOM   763  C CD2 . PHE A 1 94  ? 31.592  42.412  19.022  1   49.59  ? 94  PHE A CD2 1 
ATOM   764  C CE1 . PHE A 1 94  ? 28.959  41.686  18.544  1   40.94  ? 94  PHE A CE1 1 
ATOM   765  C CE2 . PHE A 1 94  ? 31.095  42.36   17.719  1   50.04  ? 94  PHE A CE2 1 
ATOM   766  C CZ  . PHE A 1 94  ? 29.79   41.977  17.488  1   44.41  ? 94  PHE A CZ  1 
ATOM   767  N N   . GLU A 1 95  ? 31.838  43.682  24.399  1   45.52  ? 95  GLU A N   1 
ATOM   768  C CA  . GLU A 1 95  ? 32.411  43.638  25.743  1   49.87  ? 95  GLU A CA  1 
ATOM   769  C C   . GLU A 1 95  ? 31.333  43.775  26.816  1   46.99  ? 95  GLU A C   1 
ATOM   770  O O   . GLU A 1 95  ? 31.403  43.096  27.819  1   44.32  ? 95  GLU A O   1 
ATOM   771  C CB  . GLU A 1 95  ? 33.416  44.754  26.03   1   58.07  ? 95  GLU A CB  1 
ATOM   772  C CG  . GLU A 1 95  ? 34.543  44.905  25.01   1   63.08  ? 95  GLU A CG  1 
ATOM   773  C CD  . GLU A 1 95  ? 35.77   45.628  25.554  1   67.01  ? 95  GLU A CD  1 
ATOM   774  O OE1 . GLU A 1 95  ? 35.841  46.012  26.749  1   73.15  ? 95  GLU A OE1 1 
ATOM   775  O OE2 . GLU A 1 95  ? 36.688  45.789  24.729  1   68.03  ? 95  GLU A OE2 1 
ATOM   776  N N   . ILE A 1 96  ? 30.331  44.643  26.6    1   44.29  ? 96  ILE A N   1 
ATOM   777  C CA  . ILE A 1 96  ? 29.244  44.782  27.557  1   42.08  ? 96  ILE A CA  1 
ATOM   778  C C   . ILE A 1 96  ? 28.432  43.49   27.56   1   39.89  ? 96  ILE A C   1 
ATOM   779  O O   . ILE A 1 96  ? 28.109  42.955  28.633  1   42.32  ? 96  ILE A O   1 
ATOM   780  C CB  . ILE A 1 96  ? 28.345  46.021  27.316  1   42.84  ? 96  ILE A CB  1 
ATOM   781  C CG1 . ILE A 1 96  ? 29.135  47.349  27.301  1   40.91  ? 96  ILE A CG1 1 
ATOM   782  C CG2 . ILE A 1 96  ? 27.253  46.092  28.401  1   42.77  ? 96  ILE A CG2 1 
ATOM   783  C CD1 . ILE A 1 96  ? 28.334  48.537  26.807  1   42.07  ? 96  ILE A CD1 1 
ATOM   784  N N   . GLU A 1 97  ? 28.048  43.045  26.361  1   37.8   ? 97  GLU A N   1 
ATOM   785  C CA  . GLU A 1 97  ? 27.206  41.872  26.204  1   37.4   ? 97  GLU A CA  1 
ATOM   786  C C   . GLU A 1 97  ? 27.806  40.623  26.838  1   36.36  ? 97  GLU A C   1 
ATOM   787  O O   . GLU A 1 97  ? 27.14   39.926  27.593  1   38.74  ? 97  GLU A O   1 
ATOM   788  C CB  . GLU A 1 97  ? 27.023  41.693  24.706  1   36.73  ? 97  GLU A CB  1 
ATOM   789  C CG  . GLU A 1 97  ? 26.341  40.393  24.367  1   38.12  ? 97  GLU A CG  1 
ATOM   790  C CD  . GLU A 1 97  ? 25.906  40.325  22.927  1   37.06  ? 97  GLU A CD  1 
ATOM   791  O OE1 . GLU A 1 97  ? 26.393  41.051  22.046  1   36.37  ? 97  GLU A OE1 1 
ATOM   792  O OE2 . GLU A 1 97  ? 25.059  39.426  22.779  1   38.09  ? 97  GLU A OE2 1 
ATOM   793  N N   . ASP A 1 98  ? 29.056  40.32   26.515  1   40.26  ? 98  ASP A N   1 
ATOM   794  C CA  . ASP A 1 98  ? 29.718  39.121  27.01   1   42.2   ? 98  ASP A CA  1 
ATOM   795  C C   . ASP A 1 98  ? 29.878  39.13   28.531  1   44.61  ? 98  ASP A C   1 
ATOM   796  O O   . ASP A 1 98  ? 29.754  38.069  29.149  1   44.78  ? 98  ASP A O   1 
ATOM   797  C CB  . ASP A 1 98  ? 31.039  38.904  26.295  1   49.09  ? 98  ASP A CB  1 
ATOM   798  C CG  . ASP A 1 98  ? 30.956  38.609  24.806  1   45.45  ? 98  ASP A CG  1 
ATOM   799  O OD1 . ASP A 1 98  ? 29.863  38.229  24.301  1   44.02  ? 98  ASP A OD1 1 
ATOM   800  O OD2 . ASP A 1 98  ? 31.975  38.791  24.141  1   50.81  ? 98  ASP A OD2 1 
ATOM   801  N N   . ALA A 1 99  ? 30.086  40.312  29.144  1   48.12  ? 99  ALA A N   1 
ATOM   802  C CA  . ALA A 1 99  ? 30.173  40.422  30.605  1   49.34  ? 99  ALA A CA  1 
ATOM   803  C C   . ALA A 1 99  ? 28.807  40.167  31.242  1   48.29  ? 99  ALA A C   1 
ATOM   804  O O   . ALA A 1 99  ? 28.703  39.474  32.243  1   46.38  ? 99  ALA A O   1 
ATOM   805  C CB  . ALA A 1 99  ? 30.679  41.797  31.003  1   52.07  ? 99  ALA A CB  1 
ATOM   806  N N   . LEU A 1 100 ? 27.744  40.724  30.65   1   46.68  ? 100 LEU A N   1 
ATOM   807  C CA  . LEU A 1 100 ? 26.381  40.5    31.113  1   44.83  ? 100 LEU A CA  1 
ATOM   808  C C   . LEU A 1 100 ? 26.023  39.025  30.936  1   43.04  ? 100 LEU A C   1 
ATOM   809  O O   . LEU A 1 100 ? 25.497  38.422  31.861  1   47.59  ? 100 LEU A O   1 
ATOM   810  C CB  . LEU A 1 100 ? 25.376  41.382  30.369  1   43.25  ? 100 LEU A CB  1 
ATOM   811  C CG  . LEU A 1 100 ? 25.308  42.861  30.754  1   46.46  ? 100 LEU A CG  1 
ATOM   812  C CD1 . LEU A 1 100 ? 24.427  43.542  29.713  1   46.85  ? 100 LEU A CD1 1 
ATOM   813  C CD2 . LEU A 1 100 ? 24.82   43.084  32.182  1   48.17  ? 100 LEU A CD2 1 
ATOM   814  N N   . ILE A 1 101 ? 26.302  38.449  29.755  1   43.52  ? 101 ILE A N   1 
ATOM   815  C CA  . ILE A 1 101 ? 26.054  37.025  29.523  1   41.92  ? 101 ILE A CA  1 
ATOM   816  C C   . ILE A 1 101 ? 26.698  36.161  30.615  1   44.73  ? 101 ILE A C   1 
ATOM   817  O O   . ILE A 1 101 ? 26.046  35.322  31.23   1   46.72  ? 101 ILE A O   1 
ATOM   818  C CB  . ILE A 1 101 ? 26.527  36.608  28.12   1   40.11  ? 101 ILE A CB  1 
ATOM   819  C CG1 . ILE A 1 101 ? 25.576  37.152  27.042  1   37.99  ? 101 ILE A CG1 1 
ATOM   820  C CG2 . ILE A 1 101 ? 26.67   35.079  28.034  1   41.58  ? 101 ILE A CG2 1 
ATOM   821  C CD1 . ILE A 1 101 ? 26.095  37.041  25.621  1   38.76  ? 101 ILE A CD1 1 
ATOM   822  N N   . ASP A 1 102 ? 27.992  36.374  30.848  1   50.42  ? 102 ASP A N   1 
ATOM   823  C CA  . ASP A 1 102 ? 28.768  35.55   31.773  1   53.84  ? 102 ASP A CA  1 
ATOM   824  C C   . ASP A 1 102 ? 28.202  35.654  33.194  1   52.51  ? 102 ASP A C   1 
ATOM   825  O O   . ASP A 1 102 ? 28.068  34.646  33.881  1   54.36  ? 102 ASP A O   1 
ATOM   826  C CB  . ASP A 1 102 ? 30.239  35.865  31.567  1   57.41  ? 102 ASP A CB  1 
ATOM   827  C CG  . ASP A 1 102 ? 31.226  34.87   32.143  1   70.61  ? 102 ASP A CG  1 
ATOM   828  O OD1 . ASP A 1 102 ? 31.223  33.709  31.671  1   76.08  ? 102 ASP A OD1 1 
ATOM   829  O OD2 . ASP A 1 102 ? 31.996  35.276  33.048  1   73.31  ? 102 ASP A OD2 1 
ATOM   830  N N   . SER A 1 103 ? 27.78   36.846  33.642  1   54.07  ? 103 SER A N   1 
ATOM   831  C CA  . SER A 1 103 ? 27.202  36.946  34.984  1   56.45  ? 103 SER A CA  1 
ATOM   832  C C   . SER A 1 103 ? 25.717  36.535  35.023  1   54.94  ? 103 SER A C   1 
ATOM   833  O O   . SER A 1 103 ? 25.222  36.134  36.074  1   49.2   ? 103 SER A O   1 
ATOM   834  C CB  . SER A 1 103 ? 27.462  38.285  35.619  1   58.29  ? 103 SER A CB  1 
ATOM   835  O OG  . SER A 1 103 ? 27.105  39.36   34.785  1   63.27  ? 103 SER A OG  1 
ATOM   836  N N   . MET A 1 104 ? 25.004  36.595  33.885  1   50.61  ? 104 MET A N   1 
ATOM   837  C CA  . MET A 1 104 ? 23.603  36.183  33.85   1   52.95  ? 104 MET A CA  1 
ATOM   838  C C   . MET A 1 104 ? 23.479  34.658  33.863  1   52.26  ? 104 MET A C   1 
ATOM   839  O O   . MET A 1 104 ? 22.595  34.118  34.528  1   52.34  ? 104 MET A O   1 
ATOM   840  C CB  . MET A 1 104 ? 22.872  36.846  32.678  1   49.46  ? 104 MET A CB  1 
ATOM   841  C CG  . MET A 1 104 ? 22.606  38.311  32.966  1   54.15  ? 104 MET A CG  1 
ATOM   842  S SD  . MET A 1 104 ? 22.044  39.323  31.573  1   51.64  ? 104 MET A SD  1 
ATOM   843  C CE  . MET A 1 104 ? 20.382  38.657  31.591  1   48.11  ? 104 MET A CE  1 
ATOM   844  N N   . ILE A 1 105 ? 24.378  33.965  33.154  1   54.8   ? 105 ILE A N   1 
ATOM   845  C CA  . ILE A 1 105 ? 24.401  32.508  33.151  1   56.77  ? 105 ILE A CA  1 
ATOM   846  C C   . ILE A 1 105 ? 24.558  31.953  34.572  1   64.72  ? 105 ILE A C   1 
ATOM   847  O O   . ILE A 1 105 ? 23.928  30.947  34.877  1   71.63  ? 105 ILE A O   1 
ATOM   848  C CB  . ILE A 1 105 ? 25.464  32.019  32.157  1   58.9   ? 105 ILE A CB  1 
ATOM   849  C CG1 . ILE A 1 105 ? 24.936  32.211  30.725  1   60.36  ? 105 ILE A CG1 1 
ATOM   850  C CG2 . ILE A 1 105 ? 25.865  30.566  32.414  1   63.18  ? 105 ILE A CG2 1 
ATOM   851  C CD1 . ILE A 1 105 ? 25.992  32.077  29.656  1   61.3   ? 105 ILE A CD1 1 
ATOM   852  N N   . SER A 1 106 ? 25.354  32.617  35.432  1   66.58  ? 106 SER A N   1 
ATOM   853  C CA  . SER A 1 106 ? 25.635  32.167  36.794  1   70.71  ? 106 SER A CA  1 
ATOM   854  C C   . SER A 1 106 ? 24.575  32.566  37.824  1   70.37  ? 106 SER A C   1 
ATOM   855  O O   . SER A 1 106 ? 24.656  32.079  38.933  1   69.63  ? 106 SER A O   1 
ATOM   856  C CB  . SER A 1 106 ? 26.971  32.687  37.266  1   71.41  ? 106 SER A CB  1 
ATOM   857  O OG  . SER A 1 106 ? 28.006  32.13   36.475  1   70.3   ? 106 SER A OG  1 
ATOM   858  N N   . CYS A 1 107 ? 23.642  33.486  37.53   1   67.55  ? 107 CYS A N   1 
ATOM   859  C CA  . CYS A 1 107 ? 22.721  33.967  38.555  1   67.38  ? 107 CYS A CA  1 
ATOM   860  C C   . CYS A 1 107 ? 21.57   32.976  38.736  1   70.75  ? 107 CYS A C   1 
ATOM   861  O O   . CYS A 1 107 ? 21.372  32.084  37.907  1   64.95  ? 107 CYS A O   1 
ATOM   862  C CB  . CYS A 1 107 ? 22.227  35.376  38.257  1   66.5   ? 107 CYS A CB  1 
ATOM   863  S SG  . CYS A 1 107 ? 20.951  35.435  36.972  1   62.97  ? 107 CYS A SG  1 
ATOM   864  N N   . SER A 1 108 ? 20.786  33.192  39.804  1   68.24  ? 108 SER A N   1 
ATOM   865  C CA  . SER A 1 108 ? 19.694  32.316  40.199  1   71.49  ? 108 SER A CA  1 
ATOM   866  C C   . SER A 1 108 ? 18.336  32.785  39.66   1   71.35  ? 108 SER A C   1 
ATOM   867  O O   . SER A 1 108 ? 17.316  32.19   40.007  1   75.01  ? 108 SER A O   1 
ATOM   868  C CB  . SER A 1 108 ? 19.684  32.2    41.713  1   76.7   ? 108 SER A CB  1 
ATOM   869  O OG  . SER A 1 108 ? 19.567  33.493  42.294  1   80.35  ? 108 SER A OG  1 
ATOM   870  N N   . ASN A 1 109 ? 18.286  33.823  38.807  1   65.03  ? 109 ASN A N   1 
ATOM   871  C CA  . ASN A 1 109 ? 17.036  34.246  38.188  1   59.43  ? 109 ASN A CA  1 
ATOM   872  C C   . ASN A 1 109 ? 16.886  33.485  36.876  1   58.85  ? 109 ASN A C   1 
ATOM   873  O O   . ASN A 1 109 ? 17.762  33.607  36.015  1   54.87  ? 109 ASN A O   1 
ATOM   874  C CB  . ASN A 1 109 ? 17.025  35.749  37.95   1   57.21  ? 109 ASN A CB  1 
ATOM   875  C CG  . ASN A 1 109 ? 15.723  36.22   37.35   1   55.92  ? 109 ASN A CG  1 
ATOM   876  O OD1 . ASN A 1 109 ? 15.451  36.065  36.15   1   53.01  ? 109 ASN A OD1 1 
ATOM   877  N ND2 . ASN A 1 109 ? 14.901  36.821  38.181  1   54.64  ? 109 ASN A ND2 1 
ATOM   878  N N   . MET A 1 110 ? 15.779  32.737  36.712  1   59.69  ? 110 MET A N   1 
ATOM   879  C CA  . MET A 1 110 ? 15.632  31.812  35.587  1   61.77  ? 110 MET A CA  1 
ATOM   880  C C   . MET A 1 110 ? 15.486  32.55   34.255  1   55.01  ? 110 MET A C   1 
ATOM   881  O O   . MET A 1 110 ? 16.017  32.057  33.272  1   52.12  ? 110 MET A O   1 
ATOM   882  C CB  . MET A 1 110 ? 14.439  30.857  35.735  1   68.06  ? 110 MET A CB  1 
ATOM   883  C CG  . MET A 1 110 ? 14.633  29.762  36.791  1   78.31  ? 110 MET A CG  1 
ATOM   884  S SD  . MET A 1 110 ? 16.047  28.664  36.52   1   88.43  ? 110 MET A SD  1 
ATOM   885  C CE  . MET A 1 110 ? 17.313  29.321  37.619  1   78.9   ? 110 MET A CE  1 
ATOM   886  N N   . LYS A 1 111 ? 14.807  33.709  34.244  1   53.77  ? 111 LYS A N   1 
ATOM   887  C CA  . LYS A 1 111 ? 14.673  34.516  33.034  1   53.99  ? 111 LYS A CA  1 
ATOM   888  C C   . LYS A 1 111 ? 16.012  35.098  32.603  1   50.93  ? 111 LYS A C   1 
ATOM   889  O O   . LYS A 1 111 ? 16.371  34.999  31.425  1   47.13  ? 111 LYS A O   1 
ATOM   890  C CB  . LYS A 1 111 ? 13.635  35.636  33.146  1   55.9   ? 111 LYS A CB  1 
ATOM   891  C CG  . LYS A 1 111 ? 12.248  35.074  33.463  1   61.01  ? 111 LYS A CG  1 
ATOM   892  C CD  . LYS A 1 111 ? 11.078  35.581  32.623  1   67     ? 111 LYS A CD  1 
ATOM   893  C CE  . LYS A 1 111 ? 10.8    37.051  32.681  1   67.22  ? 111 LYS A CE  1 
ATOM   894  N NZ  . LYS A 1 111 ? 9.971   37.342  33.848  1   70.94  ? 111 LYS A NZ  1 
ATOM   895  N N   . SER A 1 112 ? 16.742  35.714  33.542  1   48.44  ? 112 SER A N   1 
ATOM   896  C CA  . SER A 1 112 ? 18.064  36.243  33.247  1   47.17  ? 112 SER A CA  1 
ATOM   897  C C   . SER A 1 112 ? 19.006  35.129  32.77   1   45.18  ? 112 SER A C   1 
ATOM   898  O O   . SER A 1 112 ? 19.777  35.329  31.84   1   44     ? 112 SER A O   1 
ATOM   899  C CB  . SER A 1 112 ? 18.631  36.993  34.434  1   49.66  ? 112 SER A CB  1 
ATOM   900  O OG  . SER A 1 112 ? 17.923  38.22   34.637  1   53.08  ? 112 SER A OG  1 
ATOM   901  N N   . LYS A 1 113 ? 18.927  33.955  33.392  1   46.6   ? 113 LYS A N   1 
ATOM   902  C CA  . LYS A 1 113 ? 19.742  32.834  32.959  1   51.74  ? 113 LYS A CA  1 
ATOM   903  C C   . LYS A 1 113 ? 19.402  32.448  31.516  1   47.86  ? 113 LYS A C   1 
ATOM   904  O O   . LYS A 1 113 ? 20.313  32.237  30.699  1   46.8   ? 113 LYS A O   1 
ATOM   905  C CB  . LYS A 1 113 ? 19.53   31.658  33.913  1   55.98  ? 113 LYS A CB  1 
ATOM   906  C CG  . LYS A 1 113 ? 20.536  30.521  33.806  1   66.87  ? 113 LYS A CG  1 
ATOM   907  C CD  . LYS A 1 113 ? 20.002  29.2    34.386  1   78.02  ? 113 LYS A CD  1 
ATOM   908  C CE  . LYS A 1 113 ? 20.876  28.492  35.371  1   82.63  ? 113 LYS A CE  1 
ATOM   909  N NZ  . LYS A 1 113 ? 20.714  29.06   36.713  1   87.07  ? 113 LYS A NZ  1 
ATOM   910  N N   . GLU A 1 114 ? 18.097  32.334  31.215  1   47.83  ? 114 GLU A N   1 
ATOM   911  C CA  . GLU A 1 114 ? 17.655  31.968  29.864  1   45.97  ? 114 GLU A CA  1 
ATOM   912  C C   . GLU A 1 114 ? 18.178  32.976  28.844  1   41.09  ? 114 GLU A C   1 
ATOM   913  O O   . GLU A 1 114 ? 18.692  32.589  27.789  1   41.2   ? 114 GLU A O   1 
ATOM   914  C CB  . GLU A 1 114 ? 16.128  31.852  29.849  1   48.34  ? 114 GLU A CB  1 
ATOM   915  C CG  . GLU A 1 114 ? 15.554  31.532  28.47   1   46.6   ? 114 GLU A CG  1 
ATOM   916  C CD  . GLU A 1 114 ? 14.071  31.247  28.491  1   49.53  ? 114 GLU A CD  1 
ATOM   917  O OE1 . GLU A 1 114 ? 13.657  30.296  29.201  1   49.93  ? 114 GLU A OE1 1 
ATOM   918  O OE2 . GLU A 1 114 ? 13.318  31.943  27.766  1   49.05  ? 114 GLU A OE2 1 
ATOM   919  N N   . TYR A 1 115 ? 18.014  34.285  29.135  1   40.45  ? 115 TYR A N   1 
ATOM   920  C CA  . TYR A 1 115 ? 18.496  35.316  28.236  1   38.26  ? 115 TYR A CA  1 
ATOM   921  C C   . TYR A 1 115 ? 20.001  35.148  28.018  1   37.61  ? 115 TYR A C   1 
ATOM   922  O O   . TYR A 1 115 ? 20.481  35.198  26.902  1   33.88  ? 115 TYR A O   1 
ATOM   923  C CB  . TYR A 1 115 ? 18.234  36.742  28.724  1   38.71  ? 115 TYR A CB  1 
ATOM   924  C CG  . TYR A 1 115 ? 16.857  37.353  28.527  1   36.98  ? 115 TYR A CG  1 
ATOM   925  C CD1 . TYR A 1 115 ? 15.685  36.65   28.764  1   39.76  ? 115 TYR A CD1 1 
ATOM   926  C CD2 . TYR A 1 115 ? 16.735  38.672  28.12   1   38.85  ? 115 TYR A CD2 1 
ATOM   927  C CE1 . TYR A 1 115 ? 14.43   37.232  28.627  1   39.3   ? 115 TYR A CE1 1 
ATOM   928  C CE2 . TYR A 1 115 ? 15.498  39.277  27.989  1   39.52  ? 115 TYR A CE2 1 
ATOM   929  C CZ  . TYR A 1 115 ? 14.346  38.568  28.28   1   41.52  ? 115 TYR A CZ  1 
ATOM   930  O OH  . TYR A 1 115 ? 13.153  39.229  28.213  1   43.26  ? 115 TYR A OH  1 
ATOM   931  N N   . GLY A 1 116 ? 20.761  34.949  29.098  1   40.37  ? 116 GLY A N   1 
ATOM   932  C CA  . GLY A 1 116 ? 22.206  34.83   28.969  1   41.4   ? 116 GLY A CA  1 
ATOM   933  C C   . GLY A 1 116 ? 22.625  33.657  28.081  1   39.97  ? 116 GLY A C   1 
ATOM   934  O O   . GLY A 1 116 ? 23.477  33.825  27.24   1   40.58  ? 116 GLY A O   1 
ATOM   935  N N   . LYS A 1 117 ? 21.986  32.507  28.246  1   42.14  ? 117 LYS A N   1 
ATOM   936  C CA  . LYS A 1 117 ? 22.305  31.303  27.502  1   42.16  ? 117 LYS A CA  1 
ATOM   937  C C   . LYS A 1 117 ? 21.969  31.445  26.014  1   38.67  ? 117 LYS A C   1 
ATOM   938  O O   . LYS A 1 117 ? 22.748  31.044  25.156  1   36.98  ? 117 LYS A O   1 
ATOM   939  C CB  . LYS A 1 117 ? 21.492  30.148  28.093  1   46.51  ? 117 LYS A CB  1 
ATOM   940  C CG  . LYS A 1 117 ? 21.94   29.65   29.461  1   55.3   ? 117 LYS A CG  1 
ATOM   941  C CD  . LYS A 1 117 ? 22.961  28.516  29.373  1   61.24  ? 117 LYS A CD  1 
ATOM   942  C CE  . LYS A 1 117 ? 22.64   27.424  30.347  1   69.34  ? 117 LYS A CE  1 
ATOM   943  N NZ  . LYS A 1 117 ? 22.533  27.894  31.737  1   67.9   ? 117 LYS A NZ  1 
ATOM   944  N N   . VAL A 1 118 ? 20.83   32.074  25.704  1   40.01  ? 118 VAL A N   1 
ATOM   945  C CA  . VAL A 1 118 ? 20.372  32.182  24.326  1   36.66  ? 118 VAL A CA  1 
ATOM   946  C C   . VAL A 1 118 ? 21.203  33.217  23.57   1   35.24  ? 118 VAL A C   1 
ATOM   947  O O   . VAL A 1 118 ? 21.561  32.962  22.434  1   33.94  ? 118 VAL A O   1 
ATOM   948  C CB  . VAL A 1 118 ? 18.853  32.415  24.269  1   36.42  ? 118 VAL A CB  1 
ATOM   949  C CG1 . VAL A 1 118 ? 18.394  32.659  22.841  1   33.23  ? 118 VAL A CG1 1 
ATOM   950  C CG2 . VAL A 1 118 ? 18.128  31.194  24.827  1   36.95  ? 118 VAL A CG2 1 
ATOM   951  N N   . TYR A 1 119 ? 21.5    34.374  24.174  1   33.89  ? 119 TYR A N   1 
ATOM   952  C CA  . TYR A 1 119 ? 22.394  35.347  23.558  1   31.67  ? 119 TYR A CA  1 
ATOM   953  C C   . TYR A 1 119 ? 23.793  34.743  23.374  1   33.2   ? 119 TYR A C   1 
ATOM   954  O O   . TYR A 1 119 ? 24.436  35.016  22.356  1   32.58  ? 119 TYR A O   1 
ATOM   955  C CB  . TYR A 1 119 ? 22.44   36.653  24.362  1   34.89  ? 119 TYR A CB  1 
ATOM   956  C CG  . TYR A 1 119 ? 21.286  37.611  24.103  1   31.32  ? 119 TYR A CG  1 
ATOM   957  C CD1 . TYR A 1 119 ? 21.337  38.588  23.116  1   32.61  ? 119 TYR A CD1 1 
ATOM   958  C CD2 . TYR A 1 119 ? 20.13   37.554  24.876  1   33.58  ? 119 TYR A CD2 1 
ATOM   959  C CE1 . TYR A 1 119 ? 20.254  39.426  22.878  1   32.57  ? 119 TYR A CE1 1 
ATOM   960  C CE2 . TYR A 1 119 ? 19.045  38.391  24.643  1   32.4   ? 119 TYR A CE2 1 
ATOM   961  C CZ  . TYR A 1 119 ? 19.109  39.343  23.659  1   31.97  ? 119 TYR A CZ  1 
ATOM   962  O OH  . TYR A 1 119 ? 17.989  40.135  23.503  1   32.39  ? 119 TYR A OH  1 
ATOM   963  N N   . LYS A 1 120 ? 24.21   33.868  24.297  1   35.33  ? 120 LYS A N   1 
ATOM   964  C CA  . LYS A 1 120 ? 25.492  33.174  24.182  1   38.35  ? 120 LYS A CA  1 
ATOM   965  C C   . LYS A 1 120 ? 25.53   32.257  22.959  1   35.63  ? 120 LYS A C   1 
ATOM   966  O O   . LYS A 1 120 ? 26.556  32.213  22.28   1   38.25  ? 120 LYS A O   1 
ATOM   967  C CB  . LYS A 1 120 ? 25.891  32.391  25.439  1   39.52  ? 120 LYS A CB  1 
ATOM   968  C CG  . LYS A 1 120 ? 27.387  32.072  25.433  1   44.15  ? 120 LYS A CG  1 
ATOM   969  C CD  . LYS A 1 120 ? 27.987  31.539  26.736  1   48.36  ? 120 LYS A CD  1 
ATOM   970  C CE  . LYS A 1 120 ? 29.449  31.308  26.526  1   50.57  ? 120 LYS A CE  1 
ATOM   971  N NZ  . LYS A 1 120 ? 30.099  30.837  27.742  1   58.17  ? 120 LYS A NZ  1 
ATOM   972  N N   . ILE A 1 121 ? 24.425  31.572  22.66   1   37.05  ? 121 ILE A N   1 
ATOM   973  C CA  . ILE A 1 121 ? 24.345  30.741  21.457  1   37.92  ? 121 ILE A CA  1 
ATOM   974  C C   . ILE A 1 121 ? 24.576  31.623  20.242  1   34.34  ? 121 ILE A C   1 
ATOM   975  O O   . ILE A 1 121 ? 25.392  31.294  19.371  1   35.23  ? 121 ILE A O   1 
ATOM   976  C CB  . ILE A 1 121 ? 23.039  29.923  21.38   1   38.04  ? 121 ILE A CB  1 
ATOM   977  C CG1 . ILE A 1 121 ? 23.005  28.869  22.496  1   41.86  ? 121 ILE A CG1 1 
ATOM   978  C CG2 . ILE A 1 121 ? 22.858  29.266  19.994  1   36.57  ? 121 ILE A CG2 1 
ATOM   979  C CD1 . ILE A 1 121 ? 21.62   28.307  22.811  1   42.08  ? 121 ILE A CD1 1 
ATOM   980  N N   . HIS A 1 122 ? 23.9    32.784  20.224  1   35.47  ? 122 HIS A N   1 
ATOM   981  C CA  . HIS A 1 122 ? 24.054  33.738  19.143  1   32.69  ? 122 HIS A CA  1 
ATOM   982  C C   . HIS A 1 122 ? 25.516  34.176  18.995  1   33.22  ? 122 HIS A C   1 
ATOM   983  O O   . HIS A 1 122 ? 26.017  34.316  17.867  1   33.09  ? 122 HIS A O   1 
ATOM   984  C CB  . HIS A 1 122 ? 23.083  34.919  19.329  1   33.17  ? 122 HIS A CB  1 
ATOM   985  C CG  . HIS A 1 122 ? 23.361  36.052  18.436  1   32.63  ? 122 HIS A CG  1 
ATOM   986  N ND1 . HIS A 1 122 ? 23.416  35.92   17.075  1   32.69  ? 122 HIS A ND1 1 
ATOM   987  C CD2 . HIS A 1 122 ? 23.612  37.333  18.709  1   38.83  ? 122 HIS A CD2 1 
ATOM   988  C CE1 . HIS A 1 122 ? 23.698  37.106  16.55   1   37.32  ? 122 HIS A CE1 1 
ATOM   989  N NE2 . HIS A 1 122 ? 23.85   37.977  17.523  1   38.07  ? 122 HIS A NE2 1 
ATOM   990  N N   . ARG A 1 123 ? 26.148  34.532  20.118  1   31.69  ? 123 ARG A N   1 
ATOM   991  C CA  . ARG A 1 123 ? 27.527  35.011  20.108  1   32.66  ? 123 ARG A CA  1 
ATOM   992  C C   . ARG A 1 123 ? 28.484  33.917  19.616  1   32.28  ? 123 ARG A C   1 
ATOM   993  O O   . ARG A 1 123 ? 29.327  34.196  18.756  1   33.18  ? 123 ARG A O   1 
ATOM   994  C CB  . ARG A 1 123 ? 27.955  35.493  21.509  1   34.48  ? 123 ARG A CB  1 
ATOM   995  C CG  . ARG A 1 123 ? 27.326  36.851  21.819  1   35.08  ? 123 ARG A CG  1 
ATOM   996  C CD  . ARG A 1 123 ? 27.949  38.001  21.016  1   36.45  ? 123 ARG A CD  1 
ATOM   997  N NE  . ARG A 1 123 ? 29.337  38.268  21.408  1   39.93  ? 123 ARG A NE  1 
ATOM   998  C CZ  . ARG A 1 123 ? 30.41   38.444  20.629  1   41.88  ? 123 ARG A CZ  1 
ATOM   999  N NH1 . ARG A 1 123 ? 30.315  38.524  19.334  1   43.21  ? 123 ARG A NH1 1 
ATOM   1000 N NH2 . ARG A 1 123 ? 31.597  38.581  21.17   1   46.08  ? 123 ARG A NH2 1 
ATOM   1001 N N   . GLU A 1 124 ? 28.303  32.691  20.117  1   32.48  ? 124 GLU A N   1 
ATOM   1002 C CA  . GLU A 1 124 ? 29.12   31.557  19.692  1   35.94  ? 124 GLU A CA  1 
ATOM   1003 C C   . GLU A 1 124 ? 28.954  31.269  18.197  1   36.33  ? 124 GLU A C   1 
ATOM   1004 O O   . GLU A 1 124 ? 29.965  31.076  17.513  1   36.2   ? 124 GLU A O   1 
ATOM   1005 C CB  . GLU A 1 124 ? 28.832  30.337  20.547  1   38.38  ? 124 GLU A CB  1 
ATOM   1006 C CG  . GLU A 1 124 ? 29.409  30.482  21.955  1   44.34  ? 124 GLU A CG  1 
ATOM   1007 C CD  . GLU A 1 124 ? 29.152  29.262  22.814  1   51.67  ? 124 GLU A CD  1 
ATOM   1008 O OE1 . GLU A 1 124 ? 28.453  28.322  22.336  1   56.18  ? 124 GLU A OE1 1 
ATOM   1009 O OE2 . GLU A 1 124 ? 29.672  29.244  23.955  1   54.36  ? 124 GLU A OE2 1 
ATOM   1010 N N   . LEU A 1 125 ? 27.697  31.297  17.697  1   35.4   ? 125 LEU A N   1 
ATOM   1011 C CA  . LEU A 1 125 ? 27.445  31.019  16.284  1   34.51  ? 125 LEU A CA  1 
ATOM   1012 C C   . LEU A 1 125 ? 28.074  32.113  15.423  1   34.14  ? 125 LEU A C   1 
ATOM   1013 O O   . LEU A 1 125 ? 28.725  31.832  14.427  1   36.38  ? 125 LEU A O   1 
ATOM   1014 C CB  . LEU A 1 125 ? 25.949  30.893  15.999  1   32.84  ? 125 LEU A CB  1 
ATOM   1015 C CG  . LEU A 1 125 ? 25.535  30.601  14.545  1   32.24  ? 125 LEU A CG  1 
ATOM   1016 C CD1 . LEU A 1 125 ? 26.234  29.321  14.042  1   32.06  ? 125 LEU A CD1 1 
ATOM   1017 C CD2 . LEU A 1 125 ? 24.027  30.436  14.549  1   32.8   ? 125 LEU A CD2 1 
ATOM   1018 N N   . SER A 1 126 ? 27.867  33.372  15.783  1   33.85  ? 126 SER A N   1 
ATOM   1019 C CA  . SER A 1 126 ? 28.358  34.459  14.973  1   35.62  ? 126 SER A CA  1 
ATOM   1020 C C   . SER A 1 126 ? 29.891  34.486  14.938  1   35.48  ? 126 SER A C   1 
ATOM   1021 O O   . SER A 1 126 ? 30.457  34.845  13.917  1   37.91  ? 126 SER A O   1 
ATOM   1022 C CB  . SER A 1 126 ? 27.76   35.796  15.412  1   36.63  ? 126 SER A CB  1 
ATOM   1023 O OG  . SER A 1 126 ? 28.216  36.138  16.683  1   44.46  ? 126 SER A OG  1 
ATOM   1024 N N   . LYS A 1 127 ? 30.575  34.107  16.022  1   37.54  ? 127 LYS A N   1 
ATOM   1025 C CA  . LYS A 1 127 ? 32.033  34.026  16.043  1   39.74  ? 127 LYS A CA  1 
ATOM   1026 C C   . LYS A 1 127 ? 32.584  32.756  15.392  1   44.37  ? 127 LYS A C   1 
ATOM   1027 O O   . LYS A 1 127 ? 33.789  32.656  15.242  1   47.48  ? 127 LYS A O   1 
ATOM   1028 C CB  . LYS A 1 127 ? 32.57   34.075  17.481  1   42.82  ? 127 LYS A CB  1 
ATOM   1029 C CG  . LYS A 1 127 ? 32.393  35.433  18.153  1   46.13  ? 127 LYS A CG  1 
ATOM   1030 C CD  . LYS A 1 127 ? 32.112  35.318  19.657  1   50.16  ? 127 LYS A CD  1 
ATOM   1031 C CE  . LYS A 1 127 ? 33.27   35.292  20.485  1   50.19  ? 127 LYS A CE  1 
ATOM   1032 N NZ  . LYS A 1 127 ? 32.933  34.656  21.762  1   60.25  ? 127 LYS A NZ  1 
ATOM   1033 N N   . GLY A 1 128 ? 31.745  31.764  15.068  1   45.68  ? 128 GLY A N   1 
ATOM   1034 C CA  . GLY A 1 128 ? 32.204  30.524  14.474  1   44.38  ? 128 GLY A CA  1 
ATOM   1035 C C   . GLY A 1 128 ? 32.817  29.582  15.501  1   47.93  ? 128 GLY A C   1 
ATOM   1036 O O   . GLY A 1 128 ? 33.527  28.68   15.106  1   52.43  ? 128 GLY A O   1 
ATOM   1037 N N   . GLU A 1 129 ? 32.498  29.736  16.794  1   44.83  ? 129 GLU A N   1 
ATOM   1038 C CA  . GLU A 1 129 ? 32.854  28.76   17.815  1   48.38  ? 129 GLU A CA  1 
ATOM   1039 C C   . GLU A 1 129 ? 31.968  27.518  17.744  1   47.68  ? 129 GLU A C   1 
ATOM   1040 O O   . GLU A 1 129 ? 32.38   26.453  18.21   1   48.87  ? 129 GLU A O   1 
ATOM   1041 C CB  . GLU A 1 129 ? 32.809  29.391  19.205  1   45.92  ? 129 GLU A CB  1 
ATOM   1042 C CG  . GLU A 1 129 ? 33.863  30.484  19.359  1   50.12  ? 129 GLU A CG  1 
ATOM   1043 C CD  . GLU A 1 129 ? 33.727  31.339  20.612  1   56.81  ? 129 GLU A CD  1 
ATOM   1044 O OE1 . GLU A 1 129 ? 34.449  32.352  20.716  1   62.87  ? 129 GLU A OE1 1 
ATOM   1045 O OE2 . GLU A 1 129 ? 32.873  31.018  21.458  1   53.37  ? 129 GLU A OE2 1 
ATOM   1046 N N   . ILE A 1 130 ? 30.75   27.656  17.213  1   43.38  ? 130 ILE A N   1 
ATOM   1047 C CA  . ILE A 1 130 ? 29.883  26.527  16.918  1   41.48  ? 130 ILE A CA  1 
ATOM   1048 C C   . ILE A 1 130 ? 29.358  26.712  15.504  1   41     ? 130 ILE A C   1 
ATOM   1049 O O   . ILE A 1 130 ? 29.412  27.823  14.972  1   40.17  ? 130 ILE A O   1 
ATOM   1050 C CB  . ILE A 1 130 ? 28.734  26.403  17.93   1   42.84  ? 130 ILE A CB  1 
ATOM   1051 C CG1 . ILE A 1 130 ? 27.762  27.626  17.866  1   40.21  ? 130 ILE A CG1 1 
ATOM   1052 C CG2 . ILE A 1 130 ? 29.268  26.126  19.341  1   45.59  ? 130 ILE A CG2 1 
ATOM   1053 C CD1 . ILE A 1 130 ? 26.67   27.612  18.923  1   38.57  ? 130 ILE A CD1 1 
ATOM   1054 N N   . ASP A 1 131 ? 28.824  25.623  14.936  1   40.82  ? 131 ASP A N   1 
ATOM   1055 C CA  . ASP A 1 131 ? 28.129  25.677  13.655  1   42.17  ? 131 ASP A CA  1 
ATOM   1056 C C   . ASP A 1 131 ? 26.633  25.731  13.948  1   37.08  ? 131 ASP A C   1 
ATOM   1057 O O   . ASP A 1 131 ? 26.195  25.589  15.089  1   37.78  ? 131 ASP A O   1 
ATOM   1058 C CB  . ASP A 1 131 ? 28.58   24.548  12.718  1   45.48  ? 131 ASP A CB  1 
ATOM   1059 C CG  . ASP A 1 131 ? 28.181  23.117  13.067  1   56.65  ? 131 ASP A CG  1 
ATOM   1060 O OD1 . ASP A 1 131 ? 27.265  22.911  13.898  1   63.32  ? 131 ASP A OD1 1 
ATOM   1061 O OD2 . ASP A 1 131 ? 28.823  22.187  12.521  1   70.29  ? 131 ASP A OD2 1 
ATOM   1062 N N   . VAL A 1 132 ? 25.863  25.859  12.868  1   41.78  ? 132 VAL A N   1 
ATOM   1063 C CA  . VAL A 1 132 ? 24.432  26.073  12.927  1   44.94  ? 132 VAL A CA  1 
ATOM   1064 C C   . VAL A 1 132 ? 23.717  24.837  13.464  1   46     ? 132 VAL A C   1 
ATOM   1065 O O   . VAL A 1 132 ? 22.746  24.983  14.203  1   44.03  ? 132 VAL A O   1 
ATOM   1066 C CB  . VAL A 1 132 ? 23.908  26.536  11.557  1   49.68  ? 132 VAL A CB  1 
ATOM   1067 C CG1 . VAL A 1 132 ? 23.922  25.418  10.508  1   51.16  ? 132 VAL A CG1 1 
ATOM   1068 C CG2 . VAL A 1 132 ? 22.528  27.163  11.681  1   47.12  ? 132 VAL A CG2 1 
ATOM   1069 N N   . PHE A 1 133 ? 24.239  23.63   13.193  1   48.31  ? 133 PHE A N   1 
ATOM   1070 C CA  . PHE A 1 133 ? 23.635  22.407  13.72   1   51.53  ? 133 PHE A CA  1 
ATOM   1071 C C   . PHE A 1 133 ? 23.79   22.337  15.244  1   47.98  ? 133 PHE A C   1 
ATOM   1072 O O   . PHE A 1 133 ? 22.858  21.958  15.945  1   49.33  ? 133 PHE A O   1 
ATOM   1073 C CB  . PHE A 1 133 ? 24.164  21.149  13.002  1   60.71  ? 133 PHE A CB  1 
ATOM   1074 C CG  . PHE A 1 133 ? 23.922  21.195  11.496  1   70.13  ? 133 PHE A CG  1 
ATOM   1075 C CD1 . PHE A 1 133 ? 22.652  20.951  10.964  1   77.22  ? 133 PHE A CD1 1 
ATOM   1076 C CD2 . PHE A 1 133 ? 24.945  21.57   10.613  1   74.88  ? 133 PHE A CD2 1 
ATOM   1077 C CE1 . PHE A 1 133 ? 22.421  21.05   9.591   1   79.04  ? 133 PHE A CE1 1 
ATOM   1078 C CE2 . PHE A 1 133 ? 24.702  21.684  9.246   1   73.72  ? 133 PHE A CE2 1 
ATOM   1079 C CZ  . PHE A 1 133 ? 23.444  21.42   8.737   1   77.05  ? 133 PHE A CZ  1 
ATOM   1080 N N   . GLU A 1 134 ? 24.965  22.688  15.777  1   47.31  ? 134 GLU A N   1 
ATOM   1081 C CA  . GLU A 1 134 ? 25.149  22.756  17.224  1   50.53  ? 134 GLU A CA  1 
ATOM   1082 C C   . GLU A 1 134 ? 24.294  23.875  17.829  1   44.04  ? 134 GLU A C   1 
ATOM   1083 O O   . GLU A 1 134 ? 23.74   23.679  18.904  1   46.11  ? 134 GLU A O   1 
ATOM   1084 C CB  . GLU A 1 134 ? 26.578  23.037  17.691  1   55.59  ? 134 GLU A CB  1 
ATOM   1085 C CG  . GLU A 1 134 ? 27.628  22.036  17.218  1   65.31  ? 134 GLU A CG  1 
ATOM   1086 C CD  . GLU A 1 134 ? 29.026  22.611  17.38   1   66.41  ? 134 GLU A CD  1 
ATOM   1087 O OE1 . GLU A 1 134 ? 29.489  22.538  18.549  1   75.85  ? 134 GLU A OE1 1 
ATOM   1088 O OE2 . GLU A 1 134 ? 29.587  23.185  16.395  1   52.61  ? 134 GLU A OE2 1 
ATOM   1089 N N   . ALA A 1 135 ? 24.224  25.042  17.167  1   42.44  ? 135 ALA A N   1 
ATOM   1090 C CA  . ALA A 1 135 ? 23.364  26.121  17.652  1   39.47  ? 135 ALA A CA  1 
ATOM   1091 C C   . ALA A 1 135 ? 21.915  25.642  17.766  1   40.14  ? 135 ALA A C   1 
ATOM   1092 O O   . ALA A 1 135 ? 21.299  25.822  18.808  1   37.44  ? 135 ALA A O   1 
ATOM   1093 C CB  . ALA A 1 135 ? 23.492  27.314  16.754  1   38.81  ? 135 ALA A CB  1 
ATOM   1094 N N   . SER A 1 136 ? 21.393  24.975  16.721  1   45.78  ? 136 SER A N   1 
ATOM   1095 C CA  . SER A 1 136 ? 20.047  24.405  16.764  1   47.89  ? 136 SER A CA  1 
ATOM   1096 C C   . SER A 1 136 ? 19.868  23.413  17.9    1   44.38  ? 136 SER A C   1 
ATOM   1097 O O   . SER A 1 136 ? 18.868  23.498  18.61   1   42.55  ? 136 SER A O   1 
ATOM   1098 C CB  . SER A 1 136 ? 19.626  23.768  15.464  1   46.46  ? 136 SER A CB  1 
ATOM   1099 O OG  . SER A 1 136 ? 18.978  24.753  14.693  1   47.4   ? 136 SER A OG  1 
ATOM   1100 N N   . ALA A 1 137 ? 20.802  22.457  18.034  1   50.41  ? 137 ALA A N   1 
ATOM   1101 C CA  . ALA A 1 137 ? 20.753  21.496  19.134  1   53.07  ? 137 ALA A CA  1 
ATOM   1102 C C   . ALA A 1 137 ? 20.794  22.196  20.493  1   51.16  ? 137 ALA A C   1 
ATOM   1103 O O   . ALA A 1 137 ? 20.077  21.809  21.414  1   51.1   ? 137 ALA A O   1 
ATOM   1104 C CB  . ALA A 1 137 ? 21.88   20.49   19.03   1   54.48  ? 137 ALA A CB  1 
ATOM   1105 N N   . ASN A 1 138 ? 21.632  23.234  20.612  1   47.63  ? 138 ASN A N   1 
ATOM   1106 C CA  . ASN A 1 138 ? 21.725  23.976  21.86   1   48.38  ? 138 ASN A CA  1 
ATOM   1107 C C   . ASN A 1 138 ? 20.413  24.691  22.179  1   46.12  ? 138 ASN A C   1 
ATOM   1108 O O   . ASN A 1 138 ? 20.052  24.769  23.348  1   46.71  ? 138 ASN A O   1 
ATOM   1109 C CB  . ASN A 1 138 ? 22.9    24.945  21.84   1   52     ? 138 ASN A CB  1 
ATOM   1110 C CG  . ASN A 1 138 ? 24.233  24.242  21.914  1   57.68  ? 138 ASN A CG  1 
ATOM   1111 O OD1 . ASN A 1 138 ? 24.3    23.016  22.023  1   53.21  ? 138 ASN A OD1 1 
ATOM   1112 N ND2 . ASN A 1 138 ? 25.313  25.002  21.823  1   59.39  ? 138 ASN A ND2 1 
ATOM   1113 N N   . ILE A 1 139 ? 19.723  25.241  21.166  1   42.75  ? 139 ILE A N   1 
ATOM   1114 C CA  . ILE A 1 139 ? 18.428  25.864  21.374  1   41.52  ? 139 ILE A CA  1 
ATOM   1115 C C   . ILE A 1 139 ? 17.453  24.823  21.919  1   44.47  ? 139 ILE A C   1 
ATOM   1116 O O   . ILE A 1 139 ? 16.825  25.089  22.939  1   45.52  ? 139 ILE A O   1 
ATOM   1117 C CB  . ILE A 1 139 ? 17.913  26.527  20.083  1   39.75  ? 139 ILE A CB  1 
ATOM   1118 C CG1 . ILE A 1 139 ? 18.759  27.779  19.718  1   38.96  ? 139 ILE A CG1 1 
ATOM   1119 C CG2 . ILE A 1 139 ? 16.415  26.838  20.173  1   39.81  ? 139 ILE A CG2 1 
ATOM   1120 C CD1 . ILE A 1 139 ? 18.594  28.181  18.268  1   37.17  ? 139 ILE A CD1 1 
ATOM   1121 N N   . GLY A 1 140 ? 17.364  23.646  21.264  1   51.2   ? 140 GLY A N   1 
ATOM   1122 C CA  . GLY A 1 140 ? 16.481  22.568  21.712  1   53.01  ? 140 GLY A CA  1 
ATOM   1123 C C   . GLY A 1 140 ? 16.741  22.145  23.158  1   55.28  ? 140 GLY A C   1 
ATOM   1124 O O   . GLY A 1 140 ? 15.815  22.038  23.97   1   58.32  ? 140 GLY A O   1 
ATOM   1125 N N   . LYS A 1 141 ? 18.028  21.945  23.477  1   59.69  ? 141 LYS A N   1 
ATOM   1126 C CA  . LYS A 1 141 ? 18.439  21.574  24.823  1   61.5   ? 141 LYS A CA  1 
ATOM   1127 C C   . LYS A 1 141 ? 18.089  22.629  25.87   1   59.83  ? 141 LYS A C   1 
ATOM   1128 O O   . LYS A 1 141 ? 17.932  22.277  27.023  1   59.88  ? 141 LYS A O   1 
ATOM   1129 C CB  . LYS A 1 141 ? 19.95   21.366  24.927  1   70.02  ? 141 LYS A CB  1 
ATOM   1130 C CG  . LYS A 1 141 ? 20.477  20.08   24.309  1   77.47  ? 141 LYS A CG  1 
ATOM   1131 C CD  . LYS A 1 141 ? 21.995  20.066  24.178  1   82.79  ? 141 LYS A CD  1 
ATOM   1132 C CE  . LYS A 1 141 ? 22.676  20.152  25.508  1   92.43  ? 141 LYS A CE  1 
ATOM   1133 N NZ  . LYS A 1 141 ? 24.118  19.948  25.372  1   100.51 ? 141 LYS A NZ  1 
ATOM   1134 N N   . GLN A 1 142 ? 18.027  23.915  25.502  1   56.54  ? 142 GLN A N   1 
ATOM   1135 C CA  . GLN A 1 142 ? 17.81   24.99   26.459  1   57.3   ? 142 GLN A CA  1 
ATOM   1136 C C   . GLN A 1 142 ? 16.386  24.983  27.029  1   60.23  ? 142 GLN A C   1 
ATOM   1137 O O   . GLN A 1 142 ? 16.202  25.478  28.154  1   55.45  ? 142 GLN A O   1 
ATOM   1138 C CB  . GLN A 1 142 ? 18.163  26.332  25.813  1   57.61  ? 142 GLN A CB  1 
ATOM   1139 C CG  . GLN A 1 142 ? 18.15   27.536  26.754  1   57.62  ? 142 GLN A CG  1 
ATOM   1140 C CD  . GLN A 1 142 ? 19.021  27.361  27.976  1   53.91  ? 142 GLN A CD  1 
ATOM   1141 O OE1 . GLN A 1 142 ? 20.15   26.876  27.918  1   55.45  ? 142 GLN A OE1 1 
ATOM   1142 N NE2 . GLN A 1 142 ? 18.479  27.759  29.102  1   54.13  ? 142 GLN A NE2 1 
ATOM   1143 N N   . ARG A 1 143 ? 15.392  24.465  26.273  1   59.83  ? 143 ARG A N   1 
ATOM   1144 C CA  . ARG A 1 143 ? 14.019  24.389  26.776  1   66.07  ? 143 ARG A CA  1 
ATOM   1145 C C   . ARG A 1 143 ? 13.566  25.795  27.195  1   63.21  ? 143 ARG A C   1 
ATOM   1146 O O   . ARG A 1 143 ? 13.329  26.104  28.358  1   57.72  ? 143 ARG A O   1 
ATOM   1147 C CB  . ARG A 1 143 ? 13.886  23.344  27.899  1   73.96  ? 143 ARG A CB  1 
ATOM   1148 C CG  . ARG A 1 143 ? 14.148  21.896  27.494  1   77.84  ? 143 ARG A CG  1 
ATOM   1149 C CD  . ARG A 1 143 ? 12.894  21.02   27.626  1   86.29  ? 143 ARG A CD  1 
ATOM   1150 N NE  . ARG A 1 143 ? 12.404  20.928  29.016  1   93.04  ? 143 ARG A NE  1 
ATOM   1151 C CZ  . ARG A 1 143 ? 12.01   19.831  29.688  1   103.39 ? 143 ARG A CZ  1 
ATOM   1152 N NH1 . ARG A 1 143 ? 11.69   19.889  30.978  1   101.83 ? 143 ARG A NH1 1 
ATOM   1153 N NH2 . ARG A 1 143 ? 11.948  18.661  29.078  1   110.94 ? 143 ARG A NH2 1 
ATOM   1154 N N   . ILE A 1 144 ? 13.509  26.674  26.198  1   56.41  ? 144 ILE A N   1 
ATOM   1155 C CA  . ILE A 1 144 ? 13.228  28.098  26.371  1   52.87  ? 144 ILE A CA  1 
ATOM   1156 C C   . ILE A 1 144 ? 11.791  28.274  26.859  1   52.54  ? 144 ILE A C   1 
ATOM   1157 O O   . ILE A 1 144 ? 10.905  27.652  26.291  1   55.69  ? 144 ILE A O   1 
ATOM   1158 C CB  . ILE A 1 144 ? 13.469  28.751  24.992  1   49.65  ? 144 ILE A CB  1 
ATOM   1159 C CG1 . ILE A 1 144 ? 14.962  28.707  24.639  1   50.96  ? 144 ILE A CG1 1 
ATOM   1160 C CG2 . ILE A 1 144 ? 12.907  30.161  24.889  1   47.53  ? 144 ILE A CG2 1 
ATOM   1161 C CD1 . ILE A 1 144 ? 15.262  29.139  23.228  1   49.62  ? 144 ILE A CD1 1 
ATOM   1162 N N   . LYS A 1 145 ? 11.546  29.139  27.849  1   53.21  ? 145 LYS A N   1 
ATOM   1163 C CA  . LYS A 1 145 ? 10.204  29.37   28.386  1   57.42  ? 145 LYS A CA  1 
ATOM   1164 C C   . LYS A 1 145 ? 9.629   30.737  28.001  1   52.83  ? 145 LYS A C   1 
ATOM   1165 O O   . LYS A 1 145 ? 8.409   30.874  28.058  1   52.28  ? 145 LYS A O   1 
ATOM   1166 C CB  . LYS A 1 145 ? 10.133  29.283  29.92   1   66.56  ? 145 LYS A CB  1 
ATOM   1167 C CG  . LYS A 1 145 ? 10.695  28.028  30.609  1   75.41  ? 145 LYS A CG  1 
ATOM   1168 C CD  . LYS A 1 145 ? 10.688  28.167  32.138  1   84.81  ? 145 LYS A CD  1 
ATOM   1169 C CE  . LYS A 1 145 ? 11.899  27.648  32.888  1   92.51  ? 145 LYS A CE  1 
ATOM   1170 N NZ  . LYS A 1 145 ? 11.797  26.235  33.26   1   98.18  ? 145 LYS A NZ  1 
ATOM   1171 N N   . THR A 1 146 ? 10.458  31.755  27.705  1   46.95  ? 146 THR A N   1 
ATOM   1172 C CA  . THR A 1 146 ? 9.944   33.082  27.395  1   47.81  ? 146 THR A CA  1 
ATOM   1173 C C   . THR A 1 146 ? 9.626   33.212  25.904  1   43.69  ? 146 THR A C   1 
ATOM   1174 O O   . THR A 1 146 ? 10.353  32.718  25.037  1   41.6   ? 146 THR A O   1 
ATOM   1175 C CB  . THR A 1 146 ? 10.915  34.183  27.836  1   46.95  ? 146 THR A CB  1 
ATOM   1176 O OG1 . THR A 1 146 ? 12.121  34.172  27.075  1   42.08  ? 146 THR A OG1 1 
ATOM   1177 C CG2 . THR A 1 146 ? 11.198  34.098  29.324  1   47.38  ? 146 THR A CG2 1 
ATOM   1178 N N   . ALA A 1 147 ? 8.587   33.994  25.608  1   44.26  ? 147 ALA A N   1 
ATOM   1179 C CA  . ALA A 1 147 ? 8.265   34.32   24.229  1   45.57  ? 147 ALA A CA  1 
ATOM   1180 C C   . ALA A 1 147 ? 9.436   35.049  23.56   1   44.02  ? 147 ALA A C   1 
ATOM   1181 O O   . ALA A 1 147 ? 9.71    34.808  22.402  1   42.54  ? 147 ALA A O   1 
ATOM   1182 C CB  . ALA A 1 147 ? 6.989   35.127  24.177  1   45.86  ? 147 ALA A CB  1 
ATOM   1183 N N   . GLU A 1 148 ? 10.133  35.889  24.305  1   41.48  ? 148 GLU A N   1 
ATOM   1184 C CA  . GLU A 1 148 ? 11.263  36.651  23.818  1   40.57  ? 148 GLU A CA  1 
ATOM   1185 C C   . GLU A 1 148 ? 12.404  35.828  23.295  1   36.16  ? 148 GLU A C   1 
ATOM   1186 O O   . GLU A 1 148 ? 12.892  36.065  22.229  1   31.58  ? 148 GLU A O   1 
ATOM   1187 C CB  . GLU A 1 148 ? 11.87   37.493  24.934  1   49.19  ? 148 GLU A CB  1 
ATOM   1188 C CG  . GLU A 1 148 ? 10.937  38.434  25.608  1   51.84  ? 148 GLU A CG  1 
ATOM   1189 C CD  . GLU A 1 148 ? 10.305  37.817  26.813  1   51.16  ? 148 GLU A CD  1 
ATOM   1190 O OE1 . GLU A 1 148 ? 10.841  37.988  27.91   1   51.23  ? 148 GLU A OE1 1 
ATOM   1191 O OE2 . GLU A 1 148 ? 9.301   37.158  26.652  1   46.89  ? 148 GLU A OE2 1 
ATOM   1192 N N   . MET A 1 149 ? 12.856  34.892  24.099  1   34.89  ? 149 MET A N   1 
ATOM   1193 C CA  . MET A 1 149 ? 14.001  34.081  23.718  1   35.16  ? 149 MET A CA  1 
ATOM   1194 C C   . MET A 1 149 ? 13.609  33.019  22.682  1   34.45  ? 149 MET A C   1 
ATOM   1195 O O   . MET A 1 149 ? 14.443  32.641  21.836  1   33.33  ? 149 MET A O   1 
ATOM   1196 C CB  . MET A 1 149 ? 14.692  33.52   24.961  1   36.13  ? 149 MET A CB  1 
ATOM   1197 C CG  . MET A 1 149 ? 15.366  34.606  25.804  1   37.43  ? 149 MET A CG  1 
ATOM   1198 S SD  . MET A 1 149 ? 16.553  35.613  24.863  1   36.08  ? 149 MET A SD  1 
ATOM   1199 C CE  . MET A 1 149 ? 15.629  37.117  24.51   1   36.13  ? 149 MET A CE  1 
ATOM   1200 N N   . ASN A 1 150 ? 12.34   32.597  22.673  1   36.55  ? 150 ASN A N   1 
ATOM   1201 C CA  . ASN A 1 150 ? 11.829  31.749  21.595  1   36.5   ? 150 ASN A CA  1 
ATOM   1202 C C   . ASN A 1 150 ? 11.998  32.501  20.266  1   33.83  ? 150 ASN A C   1 
ATOM   1203 O O   . ASN A 1 150 ? 12.535  31.945  19.301  1   34.3   ? 150 ASN A O   1 
ATOM   1204 C CB  . ASN A 1 150 ? 10.406  31.291  21.893  1   42.05  ? 150 ASN A CB  1 
ATOM   1205 C CG  . ASN A 1 150 ? 9.825   30.513  20.729  1   49.67  ? 150 ASN A CG  1 
ATOM   1206 O OD1 . ASN A 1 150 ? 10.414  29.525  20.295  1   51.28  ? 150 ASN A OD1 1 
ATOM   1207 N ND2 . ASN A 1 150 ? 8.75    30.989  20.125  1   53.08  ? 150 ASN A ND2 1 
ATOM   1208 N N   . ILE A 1 151 ? 11.589  33.781  20.235  1   32.44  ? 151 ILE A N   1 
ATOM   1209 C CA  . ILE A 1 151 ? 11.757  34.617  19.044  1   31     ? 151 ILE A CA  1 
ATOM   1210 C C   . ILE A 1 151 ? 13.239  34.877  18.733  1   30.07  ? 151 ILE A C   1 
ATOM   1211 O O   . ILE A 1 151 ? 13.644  34.779  17.573  1   26.98  ? 151 ILE A O   1 
ATOM   1212 C CB  . ILE A 1 151 ? 10.954  35.923  19.193  1   29.82  ? 151 ILE A CB  1 
ATOM   1213 C CG1 . ILE A 1 151 ? 9.475   35.622  19.14   1   33.02  ? 151 ILE A CG1 1 
ATOM   1214 C CG2 . ILE A 1 151 ? 11.369  36.991  18.165  1   27.84  ? 151 ILE A CG2 1 
ATOM   1215 C CD1 . ILE A 1 151 ? 8.588   36.705  19.768  1   34.06  ? 151 ILE A CD1 1 
ATOM   1216 N N   . PHE A 1 152 ? 14.042  35.244  19.754  1   29.89  ? 152 PHE A N   1 
ATOM   1217 C CA  . PHE A 1 152 ? 15.462  35.514  19.59   1   29.28  ? 152 PHE A CA  1 
ATOM   1218 C C   . PHE A 1 152 ? 16.179  34.28   19.033  1   27.92  ? 152 PHE A C   1 
ATOM   1219 O O   . PHE A 1 152 ? 17.071  34.413  18.201  1   29.48  ? 152 PHE A O   1 
ATOM   1220 C CB  . PHE A 1 152 ? 16.175  36.044  20.853  1   30.69  ? 152 PHE A CB  1 
ATOM   1221 C CG  . PHE A 1 152 ? 17.507  36.695  20.519  1   31.49  ? 152 PHE A CG  1 
ATOM   1222 C CD1 . PHE A 1 152 ? 17.545  37.932  19.896  1   39.69  ? 152 PHE A CD1 1 
ATOM   1223 C CD2 . PHE A 1 152 ? 18.712  36.043  20.705  1   36.41  ? 152 PHE A CD2 1 
ATOM   1224 C CE1 . PHE A 1 152 ? 18.736  38.52   19.484  1   35.58  ? 152 PHE A CE1 1 
ATOM   1225 C CE2 . PHE A 1 152 ? 19.92   36.647  20.33   1   35.37  ? 152 PHE A CE2 1 
ATOM   1226 C CZ  . PHE A 1 152 ? 19.926  37.88   19.713  1   37.59  ? 152 PHE A CZ  1 
ATOM   1227 N N   . SER A 1 153 ? 15.76   33.081  19.45   1   30.35  ? 153 SER A N   1 
ATOM   1228 C CA  . SER A 1 153 ? 16.363  31.857  18.951  1   30.65  ? 153 SER A CA  1 
ATOM   1229 C C   . SER A 1 153 ? 16.126  31.701  17.434  1   32.29  ? 153 SER A C   1 
ATOM   1230 O O   . SER A 1 153 ? 16.994  31.184  16.729  1   32.46  ? 153 SER A O   1 
ATOM   1231 C CB  . SER A 1 153 ? 15.897  30.649  19.701  1   33.68  ? 153 SER A CB  1 
ATOM   1232 O OG  . SER A 1 153 ? 14.569  30.289  19.333  1   36.97  ? 153 SER A OG  1 
ATOM   1233 N N   . LYS A 1 154 ? 14.994  32.204  16.93   1   30.88  ? 154 LYS A N   1 
ATOM   1234 C CA  . LYS A 1 154 ? 14.721  32.201  15.497  1   29.26  ? 154 LYS A CA  1 
ATOM   1235 C C   . LYS A 1 154 ? 15.551  33.272  14.811  1   28.52  ? 154 LYS A C   1 
ATOM   1236 O O   . LYS A 1 154 ? 16.162  33.018  13.766  1   26.39  ? 154 LYS A O   1 
ATOM   1237 C CB  . LYS A 1 154 ? 13.23   32.343  15.235  1   32.1   ? 154 LYS A CB  1 
ATOM   1238 C CG  . LYS A 1 154 ? 12.474  31.106  15.802  1   37.12  ? 154 LYS A CG  1 
ATOM   1239 C CD  . LYS A 1 154 ? 10.986  31.376  15.89   1   43.49  ? 154 LYS A CD  1 
ATOM   1240 C CE  . LYS A 1 154 ? 10.227  30.407  16.759  1   47.27  ? 154 LYS A CE  1 
ATOM   1241 N NZ  . LYS A 1 154 ? 10.576  29.055  16.332  1   47.02  ? 154 LYS A NZ  1 
ATOM   1242 N N   . MET A 1 155 ? 15.647  34.443  15.44   1   26.22  ? 155 MET A N   1 
ATOM   1243 C CA  . MET A 1 155 ? 16.427  35.518  14.863  1   27.99  ? 155 MET A CA  1 
ATOM   1244 C C   . MET A 1 155 ? 17.903  35.125  14.72   1   26.03  ? 155 MET A C   1 
ATOM   1245 O O   . MET A 1 155 ? 18.491  35.491  13.709  1   24.25  ? 155 MET A O   1 
ATOM   1246 C CB  . MET A 1 155 ? 16.251  36.82   15.652  1   30.7   ? 155 MET A CB  1 
ATOM   1247 C CG  . MET A 1 155 ? 14.857  37.4    15.527  1   33.63  ? 155 MET A CG  1 
ATOM   1248 S SD  . MET A 1 155 ? 14.62   38.974  16.388  1   37.14  ? 155 MET A SD  1 
ATOM   1249 C CE  . MET A 1 155 ? 15.095  38.727  18.066  1   44.5   ? 155 MET A CE  1 
ATOM   1250 N N   . LEU A 1 156 ? 18.505  34.457  15.719  1   27.85  ? 156 LEU A N   1 
ATOM   1251 C CA  . LEU A 1 156 ? 19.938  34.182  15.624  1   27.06  ? 156 LEU A CA  1 
ATOM   1252 C C   . LEU A 1 156 ? 20.233  33.234  14.448  1   27.01  ? 156 LEU A C   1 
ATOM   1253 O O   . LEU A 1 156 ? 21.28   33.357  13.804  1   26.27  ? 156 LEU A O   1 
ATOM   1254 C CB  . LEU A 1 156 ? 20.54   33.73   16.954  1   29.84  ? 156 LEU A CB  1 
ATOM   1255 C CG  . LEU A 1 156 ? 20.169  32.323  17.423  1   30.83  ? 156 LEU A CG  1 
ATOM   1256 C CD1 . LEU A 1 156 ? 21.082  31.231  16.908  1   31.53  ? 156 LEU A CD1 1 
ATOM   1257 C CD2 . LEU A 1 156 ? 20.051  32.309  18.949  1   33.33  ? 156 LEU A CD2 1 
ATOM   1258 N N   . LEU A 1 157 ? 19.3    32.316  14.151  1   27.77  ? 157 LEU A N   1 
ATOM   1259 C CA  . LEU A 1 157 ? 19.404  31.435  12.991  1   28.16  ? 157 LEU A CA  1 
ATOM   1260 C C   . LEU A 1 157 ? 19.275  32.224  11.692  1   24.54  ? 157 LEU A C   1 
ATOM   1261 O O   . LEU A 1 157 ? 20.001  31.955  10.73   1   27.15  ? 157 LEU A O   1 
ATOM   1262 C CB  . LEU A 1 157 ? 18.362  30.328  13.083  1   30.96  ? 157 LEU A CB  1 
ATOM   1263 C CG  . LEU A 1 157 ? 18.524  29.361  14.248  1   34.06  ? 157 LEU A CG  1 
ATOM   1264 C CD1 . LEU A 1 157 ? 17.348  28.408  14.295  1   37.13  ? 157 LEU A CD1 1 
ATOM   1265 C CD2 . LEU A 1 157 ? 19.817  28.569  14.1    1   36.58  ? 157 LEU A CD2 1 
ATOM   1266 N N   . MET A 1 158 ? 18.378  33.211  11.674  1   27.36  ? 158 MET A N   1 
ATOM   1267 C CA  . MET A 1 158 ? 18.166  34.073  10.516  1   26.76  ? 158 MET A CA  1 
ATOM   1268 C C   . MET A 1 158 ? 19.409  34.914  10.231  1   23.51  ? 158 MET A C   1 
ATOM   1269 O O   . MET A 1 158 ? 19.789  34.998  9.056   1   22.95  ? 158 MET A O   1 
ATOM   1270 C CB  . MET A 1 158 ? 16.965  35.013  10.691  1   27.29  ? 158 MET A CB  1 
ATOM   1271 C CG  . MET A 1 158 ? 15.657  34.277  10.808  1   28.84  ? 158 MET A CG  1 
ATOM   1272 S SD  . MET A 1 158 ? 14.273  35.276  11.395  1   31.35  ? 158 MET A SD  1 
ATOM   1273 C CE  . MET A 1 158 ? 14.053  36.288  9.936   1   30.92  ? 158 MET A CE  1 
ATOM   1274 N N   . TYR A 1 159 ? 20.074  35.461  11.278  1   24.21  ? 159 TYR A N   1 
ATOM   1275 C CA  . TYR A 1 159 ? 21.292  36.245  11.085  1   23.95  ? 159 TYR A CA  1 
ATOM   1276 C C   . TYR A 1 159 ? 22.389  35.376  10.445  1   24.56  ? 159 TYR A C   1 
ATOM   1277 O O   . TYR A 1 159 ? 23.067  35.827  9.531   1   24.85  ? 159 TYR A O   1 
ATOM   1278 C CB  . TYR A 1 159 ? 21.783  36.815  12.428  1   26.5   ? 159 TYR A CB  1 
ATOM   1279 C CG  . TYR A 1 159 ? 20.974  37.973  12.985  1   24.1   ? 159 TYR A CG  1 
ATOM   1280 C CD1 . TYR A 1 159 ? 20.745  39.114  12.237  1   25.79  ? 159 TYR A CD1 1 
ATOM   1281 C CD2 . TYR A 1 159 ? 20.462  37.944  14.279  1   28.67  ? 159 TYR A CD2 1 
ATOM   1282 C CE1 . TYR A 1 159 ? 20.008  40.179  12.732  1   26.02  ? 159 TYR A CE1 1 
ATOM   1283 C CE2 . TYR A 1 159 ? 19.747  39.014  14.795  1   28.16  ? 159 TYR A CE2 1 
ATOM   1284 C CZ  . TYR A 1 159 ? 19.517  40.137  14.022  1   26.18  ? 159 TYR A CZ  1 
ATOM   1285 O OH  . TYR A 1 159 ? 18.784  41.17   14.5    1   26.19  ? 159 TYR A OH  1 
ATOM   1286 N N   . ASP A 1 160 ? 22.547  34.154  10.94   1   26.08  ? 160 ASP A N   1 
ATOM   1287 C CA  . ASP A 1 160 ? 23.532  33.208  10.445  1   28.32  ? 160 ASP A CA  1 
ATOM   1288 C C   . ASP A 1 160 ? 23.261  32.824  8.99    1   26.07  ? 160 ASP A C   1 
ATOM   1289 O O   . ASP A 1 160 ? 24.2    32.844  8.179   1   26.01  ? 160 ASP A O   1 
ATOM   1290 C CB  . ASP A 1 160 ? 23.606  31.949  11.29   1   29.16  ? 160 ASP A CB  1 
ATOM   1291 C CG  . ASP A 1 160 ? 24.766  31.025  10.907  1   35.14  ? 160 ASP A CG  1 
ATOM   1292 O OD1 . ASP A 1 160 ? 25.911  31.495  10.962  1   34.44  ? 160 ASP A OD1 1 
ATOM   1293 O OD2 . ASP A 1 160 ? 24.504  29.871  10.517  1   37.03  ? 160 ASP A OD2 1 
ATOM   1294 N N   . CYS A 1 161 ? 22.003  32.489  8.674   1   27.54  ? 161 CYS A N   1 
ATOM   1295 C CA  . CYS A 1 161 ? 21.625  32.199  7.284   1   27.16  ? 161 CYS A CA  1 
ATOM   1296 C C   . CYS A 1 161 ? 22.004  33.338  6.345   1   27.03  ? 161 CYS A C   1 
ATOM   1297 O O   . CYS A 1 161 ? 22.582  33.102  5.289   1   24     ? 161 CYS A O   1 
ATOM   1298 C CB  . CYS A 1 161 ? 20.126  32.045  7.136   1   27.07  ? 161 CYS A CB  1 
ATOM   1299 S SG  . CYS A 1 161 ? 19.541  30.504  7.84    1   31.2   ? 161 CYS A SG  1 
ATOM   1300 N N   . LEU A 1 162 ? 21.718  34.584  6.754   1   24.97  ? 162 LEU A N   1 
ATOM   1301 C CA  . LEU A 1 162 ? 22.044  35.73   5.926   1   25     ? 162 LEU A CA  1 
ATOM   1302 C C   . LEU A 1 162 ? 23.557  35.848  5.732   1   26.37  ? 162 LEU A C   1 
ATOM   1303 O O   . LEU A 1 162 ? 24.02   36.079  4.617   1   24.9   ? 162 LEU A O   1 
ATOM   1304 C CB  . LEU A 1 162 ? 21.437  36.978  6.561   1   25.73  ? 162 LEU A CB  1 
ATOM   1305 C CG  . LEU A 1 162 ? 21.569  38.293  5.805   1   24.74  ? 162 LEU A CG  1 
ATOM   1306 C CD1 . LEU A 1 162 ? 20.939  38.259  4.41    1   24.21  ? 162 LEU A CD1 1 
ATOM   1307 C CD2 . LEU A 1 162 ? 20.951  39.418  6.652   1   27.36  ? 162 LEU A CD2 1 
ATOM   1308 N N   . ASN A 1 163 ? 24.327  35.716  6.815   1   24.25  ? 163 ASN A N   1 
ATOM   1309 C CA  . ASN A 1 163 ? 25.774  35.769  6.747   1   28.75  ? 163 ASN A CA  1 
ATOM   1310 C C   . ASN A 1 163 ? 26.369  34.631  5.909   1   28.84  ? 163 ASN A C   1 
ATOM   1311 O O   . ASN A 1 163 ? 27.412  34.845  5.347   1   27.61  ? 163 ASN A O   1 
ATOM   1312 C CB  . ASN A 1 163 ? 26.478  35.66   8.101   1   32.65  ? 163 ASN A CB  1 
ATOM   1313 C CG  . ASN A 1 163 ? 26.029  36.725  9.068   1   38.42  ? 163 ASN A CG  1 
ATOM   1314 O OD1 . ASN A 1 163 ? 25.444  37.749  8.657   1   47.46  ? 163 ASN A OD1 1 
ATOM   1315 N ND2 . ASN A 1 163 ? 26.226  36.467  10.364  1   41.93  ? 163 ASN A ND2 1 
ATOM   1316 N N   . LYS A 1 164 ? 25.778  33.433  5.878   1   26.82  ? 164 LYS A N   1 
ATOM   1317 C CA  . LYS A 1 164 ? 26.364  32.313  5.154   1   27.18  ? 164 LYS A CA  1 
ATOM   1318 C C   . LYS A 1 164 ? 25.784  32.132  3.747   1   27.47  ? 164 LYS A C   1 
ATOM   1319 O O   . LYS A 1 164 ? 26.032  31.109  3.094   1   27.06  ? 164 LYS A O   1 
ATOM   1320 C CB  . LYS A 1 164 ? 26.217  31.01   5.958   1   30.98  ? 164 LYS A CB  1 
ATOM   1321 C CG  . LYS A 1 164 ? 26.905  30.966  7.331   1   38.66  ? 164 LYS A CG  1 
ATOM   1322 C CD  . LYS A 1 164 ? 28.364  31.417  7.472   1   48.5   ? 164 LYS A CD  1 
ATOM   1323 C CE  . LYS A 1 164 ? 28.812  31.669  8.916   1   48.11  ? 164 LYS A CE  1 
ATOM   1324 N NZ  . LYS A 1 164 ? 28.394  30.555  9.78    1   49.93  ? 164 LYS A NZ  1 
ATOM   1325 N N   . GLY A 1 165 ? 24.966  33.069  3.273   1   26.8   ? 165 GLY A N   1 
ATOM   1326 C CA  . GLY A 1 165 ? 24.456  33.001  1.911   1   29.16  ? 165 GLY A CA  1 
ATOM   1327 C C   . GLY A 1 165 ? 23.425  31.897  1.725   1   29.72  ? 165 GLY A C   1 
ATOM   1328 O O   . GLY A 1 165 ? 23.366  31.302  0.654   1   32.06  ? 165 GLY A O   1 
ATOM   1329 N N   . ASN A 1 166 ? 22.744  31.494  2.802   1   26.86  ? 166 ASN A N   1 
ATOM   1330 C CA  . ASN A 1 166 ? 21.74   30.448  2.75    1   24.44  ? 166 ASN A CA  1 
ATOM   1331 C C   . ASN A 1 166 ? 20.378  31.094  3.024   1   25.14  ? 166 ASN A C   1 
ATOM   1332 O O   . ASN A 1 166 ? 19.897  31.081  4.171   1   25.13  ? 166 ASN A O   1 
ATOM   1333 C CB  . ASN A 1 166 ? 22.096  29.321  3.713   1   27.8   ? 166 ASN A CB  1 
ATOM   1334 C CG  . ASN A 1 166 ? 21.088  28.19   3.686   1   29.76  ? 166 ASN A CG  1 
ATOM   1335 O OD1 . ASN A 1 166 ? 20.384  27.986  2.697   1   30.91  ? 166 ASN A OD1 1 
ATOM   1336 N ND2 . ASN A 1 166 ? 20.875  27.543  4.796   1   32.51  ? 166 ASN A ND2 1 
ATOM   1337 N N   . PHE A 1 167 ? 19.75   31.668  1.98    1   25.52  ? 167 PHE A N   1 
ATOM   1338 C CA  . PHE A 1 167 ? 18.61   32.559  2.179   1   25.87  ? 167 PHE A CA  1 
ATOM   1339 C C   . PHE A 1 167 ? 17.268  31.832  2.365   1   28.26  ? 167 PHE A C   1 
ATOM   1340 O O   . PHE A 1 167 ? 16.378  32.371  3.023   1   27.32  ? 167 PHE A O   1 
ATOM   1341 C CB  . PHE A 1 167 ? 18.583  33.659  1.127   1   23.45  ? 167 PHE A CB  1 
ATOM   1342 C CG  . PHE A 1 167 ? 19.882  34.411  0.964   1   25.48  ? 167 PHE A CG  1 
ATOM   1343 C CD1 . PHE A 1 167 ? 20.678  34.761  2.062   1   24.18  ? 167 PHE A CD1 1 
ATOM   1344 C CD2 . PHE A 1 167 ? 20.303  34.818  -0.313  1   23.73  ? 167 PHE A CD2 1 
ATOM   1345 C CE1 . PHE A 1 167 ? 21.879  35.455  1.887   1   22.5   ? 167 PHE A CE1 1 
ATOM   1346 C CE2 . PHE A 1 167 ? 21.494  35.523  -0.474  1   27.23  ? 167 PHE A CE2 1 
ATOM   1347 C CZ  . PHE A 1 167 ? 22.284  35.823  0.621   1   26.28  ? 167 PHE A CZ  1 
ATOM   1348 N N   . ALA A 1 168 ? 17.125  30.597  1.875   1   26.63  ? 168 ALA A N   1 
ATOM   1349 C CA  . ALA A 1 168 ? 15.821  29.945  1.811   1   31.51  ? 168 ALA A CA  1 
ATOM   1350 C C   . ALA A 1 168 ? 15.15   29.802  3.166   1   30.01  ? 168 ALA A C   1 
ATOM   1351 O O   . ALA A 1 168 ? 13.965  30.053  3.261   1   29.04  ? 168 ALA A O   1 
ATOM   1352 C CB  . ALA A 1 168 ? 15.919  28.58   1.142   1   36.94  ? 168 ALA A CB  1 
ATOM   1353 N N   . PRO A 1 169 ? 15.84   29.413  4.265   1   27.8   ? 169 PRO A N   1 
ATOM   1354 C CA  . PRO A 1 169 ? 15.148  29.225  5.541   1   26.69  ? 169 PRO A CA  1 
ATOM   1355 C C   . PRO A 1 169 ? 14.604  30.528  6.158   1   25.65  ? 169 PRO A C   1 
ATOM   1356 O O   . PRO A 1 169 ? 13.764  30.46   7.056   1   25.49  ? 169 PRO A O   1 
ATOM   1357 C CB  . PRO A 1 169 ? 16.174  28.547  6.439   1   29.77  ? 169 PRO A CB  1 
ATOM   1358 C CG  . PRO A 1 169 ? 17.243  28.041  5.506   1   29.95  ? 169 PRO A CG  1 
ATOM   1359 C CD  . PRO A 1 169 ? 17.257  28.998  4.318   1   27.44  ? 169 PRO A CD  1 
ATOM   1360 N N   . MET A 1 170 ? 15.117  31.695  5.721   1   25.87  ? 170 MET A N   1 
ATOM   1361 C CA  . MET A 1 170 ? 14.892  32.928  6.466   1   25.27  ? 170 MET A CA  1 
ATOM   1362 C C   . MET A 1 170 ? 13.41   33.278  6.539   1   24.1   ? 170 MET A C   1 
ATOM   1363 O O   . MET A 1 170 ? 12.947  33.642  7.582   1   25.44  ? 170 MET A O   1 
ATOM   1364 C CB  . MET A 1 170 ? 15.735  34.066  5.89    1   26.11  ? 170 MET A CB  1 
ATOM   1365 C CG  . MET A 1 170 ? 17.229  33.887  6.205   1   27.27  ? 170 MET A CG  1 
ATOM   1366 S SD  . MET A 1 170 ? 18.163  35.291  5.593   1   25.96  ? 170 MET A SD  1 
ATOM   1367 C CE  . MET A 1 170 ? 17.658  36.611  6.726   1   29.25  ? 170 MET A CE  1 
ATOM   1368 N N   . MET A 1 171 ? 12.684  33.243  5.416   1   23.79  ? 171 MET A N   1 
ATOM   1369 C CA  . MET A 1 171 ? 11.26   33.564  5.372   1   25.39  ? 171 MET A CA  1 
ATOM   1370 C C   . MET A 1 171 ? 10.438  32.583  6.215   1   25.9   ? 171 MET A C   1 
ATOM   1371 O O   . MET A 1 171 ? 9.479   32.971  6.892   1   25.63  ? 171 MET A O   1 
ATOM   1372 C CB  . MET A 1 171 ? 10.717  33.601  3.926   1   27.07  ? 171 MET A CB  1 
ATOM   1373 C CG  . MET A 1 171 ? 9.266   34.027  3.84    1   30.26  ? 171 MET A CG  1 
ATOM   1374 S SD  . MET A 1 171 ? 8.797   35.573  4.665   1   32.49  ? 171 MET A SD  1 
ATOM   1375 C CE  . MET A 1 171 ? 8.473   36.654  3.245   1   35.98  ? 171 MET A CE  1 
ATOM   1376 N N   . LEU A 1 172 ? 10.86   31.331  6.263   1   25.45  ? 172 LEU A N   1 
ATOM   1377 C CA  . LEU A 1 172 ? 10.194  30.313  7.044   1   28.85  ? 172 LEU A CA  1 
ATOM   1378 C C   . LEU A 1 172 ? 10.317  30.625  8.532   1   28.52  ? 172 LEU A C   1 
ATOM   1379 O O   . LEU A 1 172 ? 9.305   30.595  9.245   1   28.54  ? 172 LEU A O   1 
ATOM   1380 C CB  . LEU A 1 172 ? 10.734  28.907  6.718   1   34.76  ? 172 LEU A CB  1 
ATOM   1381 C CG  . LEU A 1 172 ? 10.601  28.46   5.251   1   35.83  ? 172 LEU A CG  1 
ATOM   1382 C CD1 . LEU A 1 172 ? 10.99   27.003  5.048   1   38.42  ? 172 LEU A CD1 1 
ATOM   1383 C CD2 . LEU A 1 172 ? 9.2     28.681  4.717   1   40.56  ? 172 LEU A CD2 1 
ATOM   1384 N N   . LEU A 1 173 ? 11.544  30.937  8.961   1   28.31  ? 173 LEU A N   1 
ATOM   1385 C CA  . LEU A 1 173 ? 11.769  31.359  10.337  1   28.44  ? 173 LEU A CA  1 
ATOM   1386 C C   . LEU A 1 173 ? 10.985  32.63   10.683  1   26.75  ? 173 LEU A C   1 
ATOM   1387 O O   . LEU A 1 173 ? 10.417  32.71   11.769  1   25.81  ? 173 LEU A O   1 
ATOM   1388 C CB  . LEU A 1 173 ? 13.269  31.506  10.577  1   29.26  ? 173 LEU A CB  1 
ATOM   1389 C CG  . LEU A 1 173 ? 14.036  30.185  10.65   1   31.52  ? 173 LEU A CG  1 
ATOM   1390 C CD1 . LEU A 1 173 ? 15.484  30.422  10.291  1   33.46  ? 173 LEU A CD1 1 
ATOM   1391 C CD2 . LEU A 1 173 ? 13.881  29.592  12.022  1   33.41  ? 173 LEU A CD2 1 
ATOM   1392 N N   . PHE A 1 174 ? 10.974  33.614  9.785   1   26.35  ? 174 PHE A N   1 
ATOM   1393 C CA  . PHE A 1 174 ? 10.199  34.832  10.012  1   26.25  ? 174 PHE A CA  1 
ATOM   1394 C C   . PHE A 1 174 ? 8.742   34.506  10.331  1   26.73  ? 174 PHE A C   1 
ATOM   1395 O O   . PHE A 1 174 ? 8.147   35.114  11.216  1   25.36  ? 174 PHE A O   1 
ATOM   1396 C CB  . PHE A 1 174 ? 10.294  35.747  8.773   1   28.04  ? 174 PHE A CB  1 
ATOM   1397 C CG  . PHE A 1 174 ? 9.337   36.935  8.831   1   29.1   ? 174 PHE A CG  1 
ATOM   1398 C CD1 . PHE A 1 174 ? 9.633   38.044  9.626   1   31.28  ? 174 PHE A CD1 1 
ATOM   1399 C CD2 . PHE A 1 174 ? 8.127   36.925  8.15    1   29.79  ? 174 PHE A CD2 1 
ATOM   1400 C CE1 . PHE A 1 174 ? 8.765   39.136  9.67    1   33.39  ? 174 PHE A CE1 1 
ATOM   1401 C CE2 . PHE A 1 174 ? 7.221   37.975  8.258   1   34.89  ? 174 PHE A CE2 1 
ATOM   1402 C CZ  . PHE A 1 174 ? 7.535   39.083  9.051   1   35.31  ? 174 PHE A CZ  1 
ATOM   1403 N N   . GLN A 1 175 ? 8.116   33.586  9.56    1   26.7   ? 175 GLN A N   1 
ATOM   1404 C CA  . GLN A 1 175 ? 6.724   33.241  9.747   1   27.79  ? 175 GLN A CA  1 
ATOM   1405 C C   . GLN A 1 175 ? 6.458   32.656  11.129  1   28.52  ? 175 GLN A C   1 
ATOM   1406 O O   . GLN A 1 175 ? 5.343   32.667  11.55   1   29.72  ? 175 GLN A O   1 
ATOM   1407 C CB  . GLN A 1 175 ? 6.222   32.266  8.683   1   28.57  ? 175 GLN A CB  1 
ATOM   1408 C CG  . GLN A 1 175 ? 6.27    32.826  7.273   1   29.06  ? 175 GLN A CG  1 
ATOM   1409 C CD  . GLN A 1 175 ? 5.346   34.009  7.072   1   30.89  ? 175 GLN A CD  1 
ATOM   1410 O OE1 . GLN A 1 175 ? 4.33    34.173  7.741   1   34.93  ? 175 GLN A OE1 1 
ATOM   1411 N NE2 . GLN A 1 175 ? 5.705   34.87   6.143   1   33.23  ? 175 GLN A NE2 1 
ATOM   1412 N N   . GLN A 1 176 ? 7.458   32.105  11.805  1   30.82  ? 176 GLN A N   1 
ATOM   1413 C CA  . GLN A 1 176 ? 7.287   31.552  13.139  1   33.42  ? 176 GLN A CA  1 
ATOM   1414 C C   . GLN A 1 176 ? 7.302   32.618  14.234  1   35.64  ? 176 GLN A C   1 
ATOM   1415 O O   . GLN A 1 176 ? 7.013   32.29   15.375  1   37.56  ? 176 GLN A O   1 
ATOM   1416 C CB  . GLN A 1 176 ? 8.369   30.507  13.408  1   35.73  ? 176 GLN A CB  1 
ATOM   1417 C CG  . GLN A 1 176 ? 8.395   29.353  12.403  1   35.34  ? 176 GLN A CG  1 
ATOM   1418 C CD  . GLN A 1 176 ? 9.643   28.495  12.509  1   39.62  ? 176 GLN A CD  1 
ATOM   1419 O OE1 . GLN A 1 176 ? 10.335  28.492  13.525  1   40.14  ? 176 GLN A OE1 1 
ATOM   1420 N NE2 . GLN A 1 176 ? 9.938   27.718  11.483  1   44.32  ? 176 GLN A NE2 1 
ATOM   1421 N N   . ILE A 1 177 ? 7.62    33.874  13.914  1   33.28  ? 177 ILE A N   1 
ATOM   1422 C CA  . ILE A 1 177 ? 7.734   34.911  14.931  1   33.07  ? 177 ILE A CA  1 
ATOM   1423 C C   . ILE A 1 177 ? 6.408   35.65   15.069  1   37.19  ? 177 ILE A C   1 
ATOM   1424 O O   . ILE A 1 177 ? 5.882   36.125  14.07   1   34.63  ? 177 ILE A O   1 
ATOM   1425 C CB  . ILE A 1 177 ? 8.864   35.889  14.569  1   32.47  ? 177 ILE A CB  1 
ATOM   1426 C CG1 . ILE A 1 177 ? 10.219  35.171  14.614  1   30.58  ? 177 ILE A CG1 1 
ATOM   1427 C CG2 . ILE A 1 177 ? 8.823   37.142  15.459  1   32.13  ? 177 ILE A CG2 1 
ATOM   1428 C CD1 . ILE A 1 177 ? 11.368  35.934  13.994  1   32.42  ? 177 ILE A CD1 1 
ATOM   1429 N N   . ASP A 1 178 ? 5.977   35.873  16.324  1   38.41  ? 178 ASP A N   1 
ATOM   1430 C CA  . ASP A 1 178 ? 4.845   36.727  16.64   1   40.31  ? 178 ASP A CA  1 
ATOM   1431 C C   . ASP A 1 178 ? 5.239   37.652  17.8    1   41.12  ? 178 ASP A C   1 
ATOM   1432 O O   . ASP A 1 178 ? 5.162   37.265  18.984  1   36.61  ? 178 ASP A O   1 
ATOM   1433 C CB  . ASP A 1 178 ? 3.654   35.828  16.919  1   43.73  ? 178 ASP A CB  1 
ATOM   1434 C CG  . ASP A 1 178 ? 2.344   36.5    17.299  1   46.4   ? 178 ASP A CG  1 
ATOM   1435 O OD1 . ASP A 1 178 ? 2.278   37.751  17.246  1   50.17  ? 178 ASP A OD1 1 
ATOM   1436 O OD2 . ASP A 1 178 ? 1.406   35.755  17.644  1   51.32  ? 178 ASP A OD2 1 
ATOM   1437 N N   . LEU A 1 179 ? 5.604   38.901  17.447  1   39.33  ? 179 LEU A N   1 
ATOM   1438 C CA  . LEU A 1 179 ? 6.081   39.891  18.415  1   41.93  ? 179 LEU A CA  1 
ATOM   1439 C C   . LEU A 1 179 ? 5.013   40.253  19.445  1   44.02  ? 179 LEU A C   1 
ATOM   1440 O O   . LEU A 1 179 ? 5.358   40.607  20.581  1   43.95  ? 179 LEU A O   1 
ATOM   1441 C CB  . LEU A 1 179 ? 6.609   41.155  17.731  1   45.02  ? 179 LEU A CB  1 
ATOM   1442 C CG  . LEU A 1 179 ? 7.844   40.979  16.84   1   41.39  ? 179 LEU A CG  1 
ATOM   1443 C CD1 . LEU A 1 179 ? 8.264   42.297  16.192  1   44.43  ? 179 LEU A CD1 1 
ATOM   1444 C CD2 . LEU A 1 179 ? 8.999   40.355  17.62   1   41.44  ? 179 LEU A CD2 1 
ATOM   1445 N N   . SER A 1 180 ? 3.733   40.07   19.095  1   41.31  ? 180 SER A N   1 
ATOM   1446 C CA  . SER A 1 180 ? 2.64    40.332  20.019  1   44.08  ? 180 SER A CA  1 
ATOM   1447 C C   . SER A 1 180 ? 2.689   39.428  21.245  1   46.27  ? 180 SER A C   1 
ATOM   1448 O O   . SER A 1 180 ? 1.998   39.719  22.212  1   49.17  ? 180 SER A O   1 
ATOM   1449 C CB  . SER A 1 180 ? 1.287   40.209  19.323  1   46.09  ? 180 SER A CB  1 
ATOM   1450 O OG  . SER A 1 180 ? 0.863   38.85   19.273  1   48.59  ? 180 SER A OG  1 
ATOM   1451 N N   . GLU A 1 181 ? 3.443   38.321  21.202  1   45.48  ? 181 GLU A N   1 
ATOM   1452 C CA  . GLU A 1 181 ? 3.597   37.445  22.343  1   46.66  ? 181 GLU A CA  1 
ATOM   1453 C C   . GLU A 1 181 ? 4.52    38.027  23.417  1   46.59  ? 181 GLU A C   1 
ATOM   1454 O O   . GLU A 1 181 ? 4.509   37.499  24.514  1   44.6   ? 181 GLU A O   1 
ATOM   1455 C CB  . GLU A 1 181 ? 4.151   36.083  21.936  1   51.11  ? 181 GLU A CB  1 
ATOM   1456 C CG  . GLU A 1 181 ? 3.151   35.251  21.146  1   62.41  ? 181 GLU A CG  1 
ATOM   1457 C CD  . GLU A 1 181 ? 3.732   33.883  20.822  1   77.96  ? 181 GLU A CD  1 
ATOM   1458 O OE1 . GLU A 1 181 ? 3.887   33.577  19.61   1   87.66  ? 181 GLU A OE1 1 
ATOM   1459 O OE2 . GLU A 1 181 ? 4.064   33.136  21.775  1   85.94  ? 181 GLU A OE2 1 
ATOM   1460 N N   . ILE A 1 182 ? 5.325   39.053  23.102  1   43.7   ? 182 ILE A N   1 
ATOM   1461 C CA  . ILE A 1 182 ? 6.207   39.695  24.071  1   45.73  ? 182 ILE A CA  1 
ATOM   1462 C C   . ILE A 1 182 ? 5.375   40.678  24.916  1   47.34  ? 182 ILE A C   1 
ATOM   1463 O O   . ILE A 1 182 ? 4.943   41.695  24.401  1   49.57  ? 182 ILE A O   1 
ATOM   1464 C CB  . ILE A 1 182 ? 7.406   40.391  23.373  1   41.56  ? 182 ILE A CB  1 
ATOM   1465 C CG1 . ILE A 1 182 ? 8.173   39.418  22.458  1   42.7   ? 182 ILE A CG1 1 
ATOM   1466 C CG2 . ILE A 1 182 ? 8.336   41.049  24.409  1   42.23  ? 182 ILE A CG2 1 
ATOM   1467 C CD1 . ILE A 1 182 ? 9.344   40.015  21.695  1   39.2   ? 182 ILE A CD1 1 
ATOM   1468 N N   . LYS A 1 183 ? 5.191   40.401  26.206  1   55.02  ? 183 LYS A N   1 
ATOM   1469 C CA  . LYS A 1 183 ? 4.311   41.202  27.058  1   59.56  ? 183 LYS A CA  1 
ATOM   1470 C C   . LYS A 1 183 ? 5.044   42.01   28.128  1   61.89  ? 183 LYS A C   1 
ATOM   1471 O O   . LYS A 1 183 ? 4.526   43.031  28.576  1   60.85  ? 183 LYS A O   1 
ATOM   1472 C CB  . LYS A 1 183 ? 3.303   40.343  27.836  1   65.17  ? 183 LYS A CB  1 
ATOM   1473 C CG  . LYS A 1 183 ? 2.517   39.282  27.069  1   71.32  ? 183 LYS A CG  1 
ATOM   1474 C CD  . LYS A 1 183 ? 1.627   39.756  25.927  1   68.33  ? 183 LYS A CD  1 
ATOM   1475 C CE  . LYS A 1 183 ? 0.68    38.651  25.568  1   70.68  ? 183 LYS A CE  1 
ATOM   1476 N NZ  . LYS A 1 183 ? -0.115  39.023  24.398  1   71.77  ? 183 LYS A NZ  1 
ATOM   1477 N N   . GLU A 1 184 ? 6.165   41.517  28.652  1   64.25  ? 184 GLU A N   1 
ATOM   1478 C CA  . GLU A 1 184 ? 6.752   42.099  29.86   1   71.35  ? 184 GLU A CA  1 
ATOM   1479 C C   . GLU A 1 184 ? 7.436   43.433  29.513  1   60.96  ? 184 GLU A C   1 
ATOM   1480 O O   . GLU A 1 184 ? 7.274   44.429  30.217  1   63.96  ? 184 GLU A O   1 
ATOM   1481 C CB  . GLU A 1 184 ? 7.605   40.994  30.507  1   79.27  ? 184 GLU A CB  1 
ATOM   1482 C CG  . GLU A 1 184 ? 8.823   41.418  31.338  1   89.9   ? 184 GLU A CG  1 
ATOM   1483 C CD  . GLU A 1 184 ? 10.112  40.581  31.288  1   98.66  ? 184 GLU A CD  1 
ATOM   1484 O OE1 . GLU A 1 184 ? 10.368  39.794  30.336  1   110.35 ? 184 GLU A OE1 1 
ATOM   1485 O OE2 . GLU A 1 184 ? 10.918  40.752  32.24   1   84.4   ? 184 GLU A OE2 1 
ATOM   1486 N N   . ASN A 1 185 ? 8.151   43.464  28.385  1   51.5   ? 185 ASN A N   1 
ATOM   1487 C CA  . ASN A 1 185 ? 9.289   44.347  28.197  1   47.66  ? 185 ASN A CA  1 
ATOM   1488 C C   . ASN A 1 185 ? 9.113   45.14   26.898  1   47.4   ? 185 ASN A C   1 
ATOM   1489 O O   . ASN A 1 185 ? 9.526   44.698  25.827  1   45.73  ? 185 ASN A O   1 
ATOM   1490 C CB  . ASN A 1 185 ? 10.555  43.49   28.286  1   47.43  ? 185 ASN A CB  1 
ATOM   1491 C CG  . ASN A 1 185 ? 11.828  44.299  28.308  1   41.95  ? 185 ASN A CG  1 
ATOM   1492 O OD1 . ASN A 1 185 ? 11.842  45.425  27.796  1   38.85  ? 185 ASN A OD1 1 
ATOM   1493 N ND2 . ASN A 1 185 ? 12.896  43.749  28.88   1   43.05  ? 185 ASN A ND2 1 
ATOM   1494 N N   . ARG A 1 186 ? 8.581   46.35   27.005  1   41.56  ? 186 ARG A N   1 
ATOM   1495 C CA  . ARG A 1 186 ? 8.318   47.195  25.852  1   44.94  ? 186 ARG A CA  1 
ATOM   1496 C C   . ARG A 1 186 ? 9.605   47.617  25.143  1   43.68  ? 186 ARG A C   1 
ATOM   1497 O O   . ARG A 1 186 ? 9.594   47.729  23.903  1   36.46  ? 186 ARG A O   1 
ATOM   1498 C CB  . ARG A 1 186 ? 7.554   48.463  26.246  1   49.5   ? 186 ARG A CB  1 
ATOM   1499 C CG  . ARG A 1 186 ? 6.47    48.937  25.289  1   60.82  ? 186 ARG A CG  1 
ATOM   1500 C CD  . ARG A 1 186 ? 5.121   49.075  26.063  1   70.68  ? 186 ARG A CD  1 
ATOM   1501 N NE  . ARG A 1 186 ? 5.239   49.883  27.291  1   77.57  ? 186 ARG A NE  1 
ATOM   1502 C CZ  . ARG A 1 186 ? 4.545   50.953  27.618  1   84.27  ? 186 ARG A CZ  1 
ATOM   1503 N NH1 . ARG A 1 186 ? 3.374   51.191  27.038  1   87.48  ? 186 ARG A NH1 1 
ATOM   1504 N NH2 . ARG A 1 186 ? 5.001   51.72   28.595  1   82.05  ? 186 ARG A NH2 1 
ATOM   1505 N N   . TYR A 1 187 ? 10.675  47.892  25.935  1   40.52  ? 187 TYR A N   1 
ATOM   1506 C CA  . TYR A 1 187 ? 11.98   48.246  25.386  1   39.5   ? 187 TYR A CA  1 
ATOM   1507 C C   . TYR A 1 187 ? 12.452  47.14   24.441  1   36.75  ? 187 TYR A C   1 
ATOM   1508 O O   . TYR A 1 187 ? 12.869  47.409  23.31   1   32.67  ? 187 TYR A O   1 
ATOM   1509 C CB  . TYR A 1 187 ? 13.08   48.451  26.444  1   39.08  ? 187 TYR A CB  1 
ATOM   1510 C CG  . TYR A 1 187 ? 14.436  48.686  25.806  1   37.18  ? 187 TYR A CG  1 
ATOM   1511 C CD1 . TYR A 1 187 ? 14.733  49.902  25.189  1   36.93  ? 187 TYR A CD1 1 
ATOM   1512 C CD2 . TYR A 1 187 ? 15.373  47.655  25.701  1   37.11  ? 187 TYR A CD2 1 
ATOM   1513 C CE1 . TYR A 1 187 ? 15.933  50.101  24.535  1   35.85  ? 187 TYR A CE1 1 
ATOM   1514 C CE2 . TYR A 1 187 ? 16.589  47.855  25.072  1   35.42  ? 187 TYR A CE2 1 
ATOM   1515 C CZ  . TYR A 1 187 ? 16.877  49.087  24.507  1   35.83  ? 187 TYR A CZ  1 
ATOM   1516 O OH  . TYR A 1 187 ? 18.042  49.297  23.839  1   37.67  ? 187 TYR A OH  1 
ATOM   1517 N N   . LEU A 1 188 ? 12.406  45.901  24.937  1   35.47  ? 188 LEU A N   1 
ATOM   1518 C CA  . LEU A 1 188 ? 12.874  44.78   24.134  1   36.27  ? 188 LEU A CA  1 
ATOM   1519 C C   . LEU A 1 188 ? 11.947  44.535  22.936  1   33.69  ? 188 LEU A C   1 
ATOM   1520 O O   . LEU A 1 188 ? 12.431  44.31   21.823  1   33.63  ? 188 LEU A O   1 
ATOM   1521 C CB  . LEU A 1 188 ? 13.006  43.569  25.048  1   38.58  ? 188 LEU A CB  1 
ATOM   1522 C CG  . LEU A 1 188 ? 13.546  42.313  24.366  1   39.89  ? 188 LEU A CG  1 
ATOM   1523 C CD1 . LEU A 1 188 ? 14.376  41.453  25.291  1   40.65  ? 188 LEU A CD1 1 
ATOM   1524 C CD2 . LEU A 1 188 ? 12.405  41.475  23.803  1   44.99  ? 188 LEU A CD2 1 
ATOM   1525 N N   . LYS A 1 189 ? 10.629  44.617  23.131  1   34.29  ? 189 LYS A N   1 
ATOM   1526 C CA  . LYS A 1 189 ? 9.7     44.41   22.022  1   36     ? 189 LYS A CA  1 
ATOM   1527 C C   . LYS A 1 189 ? 9.999   45.381  20.898  1   34.24  ? 189 LYS A C   1 
ATOM   1528 O O   . LYS A 1 189 ? 10.051  45.003  19.726  1   34.28  ? 189 LYS A O   1 
ATOM   1529 C CB  . LYS A 1 189 ? 8.248   44.608  22.451  1   40.27  ? 189 LYS A CB  1 
ATOM   1530 C CG  . LYS A 1 189 ? 7.212   44.149  21.457  1   41.91  ? 189 LYS A CG  1 
ATOM   1531 C CD  . LYS A 1 189 ? 5.821   44.506  21.936  1   47.01  ? 189 LYS A CD  1 
ATOM   1532 C CE  . LYS A 1 189 ? 4.839   44.057  20.923  1   49.64  ? 189 LYS A CE  1 
ATOM   1533 N NZ  . LYS A 1 189 ? 3.639   44.886  21.049  1   59.67  ? 189 LYS A NZ  1 
ATOM   1534 N N   . ASN A 1 190 ? 10.213  46.633  21.278  1   32.08  ? 190 ASN A N   1 
ATOM   1535 C CA  . ASN A 1 190 ? 10.543  47.698  20.35   1   35.7   ? 190 ASN A CA  1 
ATOM   1536 C C   . ASN A 1 190 ? 11.84   47.453  19.574  1   32.48  ? 190 ASN A C   1 
ATOM   1537 O O   . ASN A 1 190 ? 11.913  47.7    18.365  1   29.11  ? 190 ASN A O   1 
ATOM   1538 C CB  . ASN A 1 190 ? 10.769  48.999  21.107  1   41.61  ? 190 ASN A CB  1 
ATOM   1539 C CG  . ASN A 1 190 ? 9.822   50.023  20.618  1   54.39  ? 190 ASN A CG  1 
ATOM   1540 O OD1 . ASN A 1 190 ? 10.06   50.55   19.519  1   53.27  ? 190 ASN A OD1 1 
ATOM   1541 N ND2 . ASN A 1 190 ? 8.785   50.248  21.426  1   53.77  ? 190 ASN A ND2 1 
ATOM   1542 N N   . SER A 1 191 ? 12.888  47.057  20.302  1   30.77  ? 191 SER A N   1 
ATOM   1543 C CA  . SER A 1 191 ? 14.166  46.72   19.696  1   27.93  ? 191 SER A CA  1 
ATOM   1544 C C   . SER A 1 191 ? 14.017  45.565  18.705  1   28.68  ? 191 SER A C   1 
ATOM   1545 O O   . SER A 1 191 ? 14.597  45.618  17.617  1   26.85  ? 191 SER A O   1 
ATOM   1546 C CB  . SER A 1 191 ? 15.165  46.358  20.791  1   27.07  ? 191 SER A CB  1 
ATOM   1547 O OG  . SER A 1 191 ? 16.451  46.229  20.227  1   28.14  ? 191 SER A OG  1 
ATOM   1548 N N   . PHE A 1 192 ? 13.283  44.508  19.108  1   27.75  ? 192 PHE A N   1 
ATOM   1549 C CA  . PHE A 1 192 ? 12.973  43.404  18.197  1   28.5   ? 192 PHE A CA  1 
ATOM   1550 C C   . PHE A 1 192 ? 12.182  43.84   16.965  1   27.36  ? 192 PHE A C   1 
ATOM   1551 O O   . PHE A 1 192 ? 12.416  43.279  15.876  1   28.58  ? 192 PHE A O   1 
ATOM   1552 C CB  . PHE A 1 192 ? 12.213  42.29   18.92   1   28.14  ? 192 PHE A CB  1 
ATOM   1553 C CG  . PHE A 1 192 ? 13.052  41.396  19.807  1   29.24  ? 192 PHE A CG  1 
ATOM   1554 C CD1 . PHE A 1 192 ? 14.325  41.764  20.271  1   29.07  ? 192 PHE A CD1 1 
ATOM   1555 C CD2 . PHE A 1 192 ? 12.558  40.127  20.122  1   31.46  ? 192 PHE A CD2 1 
ATOM   1556 C CE1 . PHE A 1 192 ? 15.061  40.885  21.071  1   33.44  ? 192 PHE A CE1 1 
ATOM   1557 C CE2 . PHE A 1 192 ? 13.288  39.267  20.945  1   35.88  ? 192 PHE A CE2 1 
ATOM   1558 C CZ  . PHE A 1 192 ? 14.522  39.661  21.45   1   35.68  ? 192 PHE A CZ  1 
ATOM   1559 N N   . GLU A 1 193 ? 11.266  44.805  17.104  1   27.42  ? 193 GLU A N   1 
ATOM   1560 C CA  . GLU A 1 193 ? 10.525  45.297  15.933  1   28.99  ? 193 GLU A CA  1 
ATOM   1561 C C   . GLU A 1 193 ? 11.518  45.883  14.93   1   26.43  ? 193 GLU A C   1 
ATOM   1562 O O   . GLU A 1 193 ? 11.431  45.605  13.721  1   25.2   ? 193 GLU A O   1 
ATOM   1563 C CB  . GLU A 1 193 ? 9.45    46.34   16.303  1   34.31  ? 193 GLU A CB  1 
ATOM   1564 C CG  . GLU A 1 193 ? 8.108   45.762  16.728  1   43.22  ? 193 GLU A CG  1 
ATOM   1565 C CD  . GLU A 1 193 ? 7.157   46.507  17.684  1   53.55  ? 193 GLU A CD  1 
ATOM   1566 O OE1 . GLU A 1 193 ? 7.47    47.56   18.309  1   59.96  ? 193 GLU A OE1 1 
ATOM   1567 O OE2 . GLU A 1 193 ? 6.048   45.934  17.848  1   56.5   ? 193 GLU A OE2 1 
ATOM   1568 N N   . THR A 1 194 ? 12.495  46.691  15.416  1   25.52  ? 194 THR A N   1 
ATOM   1569 C CA  . THR A 1 194 ? 13.517  47.21   14.503  1   24.29  ? 194 THR A CA  1 
ATOM   1570 C C   . THR A 1 194 ? 14.338  46.064  13.89   1   26.2   ? 194 THR A C   1 
ATOM   1571 O O   . THR A 1 194 ? 14.619  46.07   12.708  1   24.34  ? 194 THR A O   1 
ATOM   1572 C CB  . THR A 1 194 ? 14.44   48.209  15.197  1   27.54  ? 194 THR A CB  1 
ATOM   1573 O OG1 . THR A 1 194 ? 13.609  49.208  15.758  1   28.41  ? 194 THR A OG1 1 
ATOM   1574 C CG2 . THR A 1 194 ? 15.316  48.931  14.198  1   28.45  ? 194 THR A CG2 1 
ATOM   1575 N N   . ARG A 1 195 ? 14.801  45.117  14.721  1   27.35  ? 195 ARG A N   1 
ATOM   1576 C CA  . ARG A 1 195 ? 15.545  43.976  14.205  1   26.56  ? 195 ARG A CA  1 
ATOM   1577 C C   . ARG A 1 195 ? 14.806  43.294  13.043  1   23.25  ? 195 ARG A C   1 
ATOM   1578 O O   . ARG A 1 195 ? 15.417  42.921  12.014  1   23.59  ? 195 ARG A O   1 
ATOM   1579 C CB  . ARG A 1 195 ? 15.835  42.88   15.241  1   25.52  ? 195 ARG A CB  1 
ATOM   1580 C CG  . ARG A 1 195 ? 16.837  43.275  16.313  1   27.98  ? 195 ARG A CG  1 
ATOM   1581 C CD  . ARG A 1 195 ? 16.962  42.116  17.267  1   28.31  ? 195 ARG A CD  1 
ATOM   1582 N NE  . ARG A 1 195 ? 17.912  42.39   18.352  1   28.29  ? 195 ARG A NE  1 
ATOM   1583 C CZ  . ARG A 1 195 ? 19.181  41.992  18.346  1   29.38  ? 195 ARG A CZ  1 
ATOM   1584 N NH1 . ARG A 1 195 ? 19.78   41.59   17.224  1   27.96  ? 195 ARG A NH1 1 
ATOM   1585 N NH2 . ARG A 1 195 ? 19.928  42.083  19.432  1   33.14  ? 195 ARG A NH2 1 
ATOM   1586 N N   . ILE A 1 196 ? 13.507  43.097  13.232  1   24.89  ? 196 ILE A N   1 
ATOM   1587 C CA  . ILE A 1 196 ? 12.688  42.367  12.271  1   26.25  ? 196 ILE A CA  1 
ATOM   1588 C C   . ILE A 1 196 ? 12.479  43.187  11.014  1   24.65  ? 196 ILE A C   1 
ATOM   1589 O O   . ILE A 1 196 ? 12.507  42.615  9.922   1   23.16  ? 196 ILE A O   1 
ATOM   1590 C CB  . ILE A 1 196 ? 11.377  41.916  12.931  1   29.83  ? 196 ILE A CB  1 
ATOM   1591 C CG1 . ILE A 1 196 ? 11.667  40.767  13.865  1   34.96  ? 196 ILE A CG1 1 
ATOM   1592 C CG2 . ILE A 1 196 ? 10.273  41.596  11.911  1   34.73  ? 196 ILE A CG2 1 
ATOM   1593 C CD1 . ILE A 1 196 ? 12.043  39.465  13.154  1   41.92  ? 196 ILE A CD1 1 
ATOM   1594 N N   . ASN A 1 197 ? 12.348  44.509  11.132  1   24.45  ? 197 ASN A N   1 
ATOM   1595 C CA  . ASN A 1 197 ? 12.283  45.334  9.937   1   25.51  ? 197 ASN A CA  1 
ATOM   1596 C C   . ASN A 1 197 ? 13.516  45.141  9.045   1   26.45  ? 197 ASN A C   1 
ATOM   1597 O O   . ASN A 1 197 ? 13.384  45.015  7.817   1   24.5   ? 197 ASN A O   1 
ATOM   1598 C CB  . ASN A 1 197 ? 12.056  46.808  10.257  1   28.26  ? 197 ASN A CB  1 
ATOM   1599 C CG  . ASN A 1 197 ? 10.648  47.105  10.742  1   31.45  ? 197 ASN A CG  1 
ATOM   1600 O OD1 . ASN A 1 197 ? 9.688   46.407  10.44   1   29.18  ? 197 ASN A OD1 1 
ATOM   1601 N ND2 . ASN A 1 197 ? 10.49   48.181  11.479  1   31.27  ? 197 ASN A ND2 1 
ATOM   1602 N N   . VAL A 1 198 ? 14.717  45.141  9.656   1   25.65  ? 198 VAL A N   1 
ATOM   1603 C CA  . VAL A 1 198 ? 15.953  45.049  8.916   1   24.69  ? 198 VAL A CA  1 
ATOM   1604 C C   . VAL A 1 198 ? 16.104  43.617  8.36    1   23.26  ? 198 VAL A C   1 
ATOM   1605 O O   . VAL A 1 198 ? 16.482  43.442  7.175   1   21.36  ? 198 VAL A O   1 
ATOM   1606 C CB  . VAL A 1 198 ? 17.15   45.537  9.762   1   25.9   ? 198 VAL A CB  1 
ATOM   1607 C CG1 . VAL A 1 198 ? 18.423  45.522  8.92    1   27.79  ? 198 VAL A CG1 1 
ATOM   1608 C CG2 . VAL A 1 198 ? 16.896  46.959  10.26   1   25.97  ? 198 VAL A CG2 1 
ATOM   1609 N N   . LEU A 1 199 ? 15.779  42.607  9.173   1   21.81  ? 199 LEU A N   1 
ATOM   1610 C CA  . LEU A 1 199 ? 15.769  41.224  8.655   1   23.25  ? 199 LEU A CA  1 
ATOM   1611 C C   . LEU A 1 199 ? 14.787  41.05   7.496   1   22.91  ? 199 LEU A C   1 
ATOM   1612 O O   . LEU A 1 199 ? 15.126  40.449  6.467   1   24.17  ? 199 LEU A O   1 
ATOM   1613 C CB  . LEU A 1 199 ? 15.479  40.216  9.756   1   22.5   ? 199 LEU A CB  1 
ATOM   1614 C CG  . LEU A 1 199 ? 16.664  39.902  10.682  1   22.86  ? 199 LEU A CG  1 
ATOM   1615 C CD1 . LEU A 1 199 ? 16.203  39.342  11.997  1   24.88  ? 199 LEU A CD1 1 
ATOM   1616 C CD2 . LEU A 1 199 ? 17.637  38.976  9.974   1   25.56  ? 199 LEU A CD2 1 
ATOM   1617 N N   . LEU A 1 200 ? 13.567  41.574  7.646   1   23.29  ? 200 LEU A N   1 
ATOM   1618 C CA  . LEU A 1 200 ? 12.554  41.438  6.614   1   25.05  ? 200 LEU A CA  1 
ATOM   1619 C C   . LEU A 1 200 ? 13.001  42.159  5.365   1   23.28  ? 200 LEU A C   1 
ATOM   1620 O O   . LEU A 1 200 ? 12.75   41.7    4.252   1   23.29  ? 200 LEU A O   1 
ATOM   1621 C CB  . LEU A 1 200 ? 11.174  41.86   7.155   1   27.31  ? 200 LEU A CB  1 
ATOM   1622 C CG  . LEU A 1 200 ? 9.979   41.488  6.27    1   30.33  ? 200 LEU A CG  1 
ATOM   1623 C CD1 . LEU A 1 200 ? 9.801   40.016  5.952   1   28.59  ? 200 LEU A CD1 1 
ATOM   1624 C CD2 . LEU A 1 200 ? 8.715   42.019  6.906   1   32.61  ? 200 LEU A CD2 1 
ATOM   1625 N N   . SER A 1 201 ? 13.641  43.328  5.523   1   22.95  ? 201 SER A N   1 
ATOM   1626 C CA  . SER A 1 201 ? 14.177  44.034  4.36    1   22.13  ? 201 SER A CA  1 
ATOM   1627 C C   . SER A 1 201 ? 15.123  43.142  3.548   1   21.87  ? 201 SER A C   1 
ATOM   1628 O O   . SER A 1 201 ? 15.03   43.125  2.321   1   23.58  ? 201 SER A O   1 
ATOM   1629 C CB  . SER A 1 201 ? 14.885  45.333  4.783   1   22.92  ? 201 SER A CB  1 
ATOM   1630 O OG  . SER A 1 201 ? 15.473  46.019  3.681   1   24.93  ? 201 SER A OG  1 
ATOM   1631 N N   . ASN A 1 202 ? 16.026  42.432  4.229   1   20.28  ? 202 ASN A N   1 
ATOM   1632 C CA  . ASN A 1 202 ? 16.919  41.484  3.582   1   19.93  ? 202 ASN A CA  1 
ATOM   1633 C C   . ASN A 1 202 ? 16.156  40.324  2.946   1   20.31  ? 202 ASN A C   1 
ATOM   1634 O O   . ASN A 1 202 ? 16.548  39.891  1.852   1   20.81  ? 202 ASN A O   1 
ATOM   1635 C CB  . ASN A 1 202 ? 17.981  40.967  4.548   1   19.99  ? 202 ASN A CB  1 
ATOM   1636 C CG  . ASN A 1 202 ? 19.131  41.946  4.672   1   20.67  ? 202 ASN A CG  1 
ATOM   1637 O OD1 . ASN A 1 202 ? 20.106  41.887  3.917   1   23.68  ? 202 ASN A OD1 1 
ATOM   1638 N ND2 . ASN A 1 202 ? 19.037  42.878  5.596   1   24.6   ? 202 ASN A ND2 1 
ATOM   1639 N N   . ILE A 1 203 ? 15.11   39.813  3.635   1   21.06  ? 203 ILE A N   1 
ATOM   1640 C CA  . ILE A 1 203 ? 14.323  38.71   3.088   1   22.74  ? 203 ILE A CA  1 
ATOM   1641 C C   . ILE A 1 203 ? 13.729  39.111  1.744   1   24.28  ? 203 ILE A C   1 
ATOM   1642 O O   . ILE A 1 203 ? 13.833  38.359  0.764   1   21.58  ? 203 ILE A O   1 
ATOM   1643 C CB  . ILE A 1 203 ? 13.28   38.196  4.081   1   22.02  ? 203 ILE A CB  1 
ATOM   1644 C CG1 . ILE A 1 203 ? 13.944  37.465  5.213   1   22.73  ? 203 ILE A CG1 1 
ATOM   1645 C CG2 . ILE A 1 203 ? 12.183  37.371  3.4     1   22.25  ? 203 ILE A CG2 1 
ATOM   1646 C CD1 . ILE A 1 203 ? 13.032  37.267  6.411   1   24.15  ? 203 ILE A CD1 1 
ATOM   1647 N N   . TYR A 1 204 ? 13.153  40.332  1.702   1   21.73  ? 204 TYR A N   1 
ATOM   1648 C CA  . TYR A 1 204 ? 12.548  40.805  0.478   1   22.64  ? 204 TYR A CA  1 
ATOM   1649 C C   . TYR A 1 204 ? 13.59   41.1    -0.586  1   22.02  ? 204 TYR A C   1 
ATOM   1650 O O   . TYR A 1 204 ? 13.268  40.879  -1.752  1   22.76  ? 204 TYR A O   1 
ATOM   1651 C CB  . TYR A 1 204 ? 11.609  41.976  0.789   1   24.58  ? 204 TYR A CB  1 
ATOM   1652 C CG  . TYR A 1 204 ? 10.295  41.586  1.431   1   28.25  ? 204 TYR A CG  1 
ATOM   1653 C CD1 . TYR A 1 204 ? 9.508   40.559  0.904   1   30.9   ? 204 TYR A CD1 1 
ATOM   1654 C CD2 . TYR A 1 204 ? 9.839   42.262  2.574   1   26.15  ? 204 TYR A CD2 1 
ATOM   1655 C CE1 . TYR A 1 204 ? 8.309   40.216  1.504   1   32.39  ? 204 TYR A CE1 1 
ATOM   1656 C CE2 . TYR A 1 204 ? 8.622   41.952  3.145   1   31.61  ? 204 TYR A CE2 1 
ATOM   1657 C CZ  . TYR A 1 204 ? 7.862   40.937  2.595   1   36.36  ? 204 TYR A CZ  1 
ATOM   1658 O OH  . TYR A 1 204 ? 6.685   40.629  3.152   1   38.03  ? 204 TYR A OH  1 
ATOM   1659 N N   . LEU A 1 205 ? 14.777  41.616  -0.191  1   21.67  ? 205 LEU A N   1 
ATOM   1660 C CA  . LEU A 1 205 ? 15.867  41.885  -1.127  1   24.76  ? 205 LEU A CA  1 
ATOM   1661 C C   . LEU A 1 205 ? 16.218  40.601  -1.876  1   21.91  ? 205 LEU A C   1 
ATOM   1662 O O   . LEU A 1 205 ? 16.268  40.594  -3.101  1   22.82  ? 205 LEU A O   1 
ATOM   1663 C CB  . LEU A 1 205 ? 17.087  42.423  -0.391  1   22.51  ? 205 LEU A CB  1 
ATOM   1664 C CG  . LEU A 1 205 ? 18.414  42.555  -1.154  1   25.33  ? 205 LEU A CG  1 
ATOM   1665 C CD1 . LEU A 1 205 ? 18.383  43.763  -2.014  1   27.2   ? 205 LEU A CD1 1 
ATOM   1666 C CD2 . LEU A 1 205 ? 19.635  42.62   -0.286  1   29.44  ? 205 LEU A CD2 1 
ATOM   1667 N N   . ASN A 1 206 ? 16.386  39.513  -1.121  1   20.98  ? 206 ASN A N   1 
ATOM   1668 C CA  . ASN A 1 206 ? 16.819  38.251  -1.687  1   22.64  ? 206 ASN A CA  1 
ATOM   1669 C C   . ASN A 1 206 ? 15.698  37.569  -2.469  1   24.87  ? 206 ASN A C   1 
ATOM   1670 O O   . ASN A 1 206 ? 16.005  36.749  -3.361  1   25.55  ? 206 ASN A O   1 
ATOM   1671 C CB  . ASN A 1 206 ? 17.442  37.387  -0.59   1   22.77  ? 206 ASN A CB  1 
ATOM   1672 C CG  . ASN A 1 206 ? 18.702  37.97   -0.002  1   25.29  ? 206 ASN A CG  1 
ATOM   1673 O OD1 . ASN A 1 206 ? 19.462  38.68   -0.677  1   24.74  ? 206 ASN A OD1 1 
ATOM   1674 N ND2 . ASN A 1 206 ? 18.976  37.652  1.262   1   24.45  ? 206 ASN A ND2 1 
ATOM   1675 N N   . GLU A 1 207 ? 14.419  37.903  -2.186  1   24.8   ? 207 GLU A N   1 
ATOM   1676 C CA  A GLU A 1 207 ? 13.278  37.448  -2.975  0.5 24.2   ? 207 GLU A CA  1 
ATOM   1677 C CA  B GLU A 1 207 ? 13.279  37.45   -2.976  0.5 24.63  ? 207 GLU A CA  1 
ATOM   1678 C C   . GLU A 1 207 ? 13.052  38.364  -4.177  1   23.39  ? 207 GLU A C   1 
ATOM   1679 O O   . GLU A 1 207 ? 12.131  38.132  -4.917  1   24.79  ? 207 GLU A O   1 
ATOM   1680 C CB  A GLU A 1 207 ? 11.978  37.368  -2.169  0.5 24.67  ? 207 GLU A CB  1 
ATOM   1681 C CB  B GLU A 1 207 ? 11.98   37.386  -2.171  0.5 25.66  ? 207 GLU A CB  1 
ATOM   1682 C CG  A GLU A 1 207 ? 11.963  36.284  -1.083  0.5 27.07  ? 207 GLU A CG  1 
ATOM   1683 C CG  B GLU A 1 207 ? 11.878  36.157  -1.267  0.5 29.31  ? 207 GLU A CG  1 
ATOM   1684 C CD  A GLU A 1 207 ? 10.75   36.308  -0.167  0.5 30.13  ? 207 GLU A CD  1 
ATOM   1685 C CD  B GLU A 1 207 ? 11.793  34.87   -2.078  0.5 31.88  ? 207 GLU A CD  1 
ATOM   1686 O OE1 A GLU A 1 207 ? 10.009  37.308  -0.282  0.5 30.43  ? 207 GLU A OE1 1 
ATOM   1687 O OE1 B GLU A 1 207 ? 12.871  34.344  -2.464  0.5 34.77  ? 207 GLU A OE1 1 
ATOM   1688 O OE2 A GLU A 1 207 ? 10.473  35.308  0.567   0.5 29.76  ? 207 GLU A OE2 1 
ATOM   1689 O OE2 B GLU A 1 207 ? 10.663  34.421  -2.362  0.5 38.1   ? 207 GLU A OE2 1 
ATOM   1690 N N   . ASN A 1 208 ? 13.894  39.38   -4.403  1   23.95  ? 208 ASN A N   1 
ATOM   1691 C CA  . ASN A 1 208 ? 13.681  40.293  -5.524  1   26.05  ? 208 ASN A CA  1 
ATOM   1692 C C   . ASN A 1 208 ? 12.347  41.055  -5.432  1   27.3   ? 208 ASN A C   1 
ATOM   1693 O O   . ASN A 1 208 ? 11.712  41.352  -6.456  1   24.6   ? 208 ASN A O   1 
ATOM   1694 C CB  . ASN A 1 208 ? 13.84   39.604  -6.887  1   29.73  ? 208 ASN A CB  1 
ATOM   1695 C CG  . ASN A 1 208 ? 14.04   40.572  -8.027  1   31.04  ? 208 ASN A CG  1 
ATOM   1696 O OD1 . ASN A 1 208 ? 14.638  41.63   -7.86   1   27.92  ? 208 ASN A OD1 1 
ATOM   1697 N ND2 . ASN A 1 208 ? 13.521  40.267  -9.199  1   31.03  ? 208 ASN A ND2 1 
ATOM   1698 N N   . ASN A 1 209 ? 11.882  41.335  -4.196  1   25.18  ? 209 ASN A N   1 
ATOM   1699 C CA  A ASN A 1 209 ? 10.743  42.224  -3.975  0.5 24.89  ? 209 ASN A CA  1 
ATOM   1700 C CA  B ASN A 1 209 ? 10.734  42.178  -3.903  0.5 25.5   ? 209 ASN A CA  1 
ATOM   1701 C C   . ASN A 1 209 ? 11.305  43.535  -3.462  1   25.36  ? 209 ASN A C   1 
ATOM   1702 O O   . ASN A 1 209 ? 11.423  43.79   -2.252  1   24.94  ? 209 ASN A O   1 
ATOM   1703 C CB  A ASN A 1 209 ? 9.702   41.748  -2.982  0.5 26.31  ? 209 ASN A CB  1 
ATOM   1704 C CB  B ASN A 1 209 ? 9.865   41.474  -2.858  0.5 27.93  ? 209 ASN A CB  1 
ATOM   1705 C CG  A ASN A 1 209 ? 8.461   42.626  -2.999  0.5 26.63  ? 209 ASN A CG  1 
ATOM   1706 C CG  B ASN A 1 209 ? 9.148   40.223  -3.364  0.5 29.95  ? 209 ASN A CG  1 
ATOM   1707 O OD1 A ASN A 1 209 ? 8.451   43.831  -3.358  0.5 22.94  ? 209 ASN A OD1 1 
ATOM   1708 O OD1 B ASN A 1 209 ? 8.85    40.107  -4.557  0.5 29.02  ? 209 ASN A OD1 1 
ATOM   1709 N ND2 A ASN A 1 209 ? 7.38    41.986  -2.596  0.5 29.64  ? 209 ASN A ND2 1 
ATOM   1710 N ND2 B ASN A 1 209 ? 8.821   39.268  -2.495  0.5 30.86  ? 209 ASN A ND2 1 
ATOM   1711 N N   . LEU A 1 210 ? 11.902  44.228  -4.387  1   24.01  ? 210 LEU A N   1 
ATOM   1712 C CA  . LEU A 1 210 ? 12.569  45.473  -4.128  1   27.13  ? 210 LEU A CA  1 
ATOM   1713 C C   . LEU A 1 210 ? 11.808  46.581  -3.411  1   28.07  ? 210 LEU A C   1 
ATOM   1714 O O   . LEU A 1 210 ? 12.355  47.233  -2.584  1   26.54  ? 210 LEU A O   1 
ATOM   1715 C CB  . LEU A 1 210 ? 13.286  45.937  -5.376  1   26.99  ? 210 LEU A CB  1 
ATOM   1716 C CG  . LEU A 1 210 ? 14.187  44.858  -5.969  1   29.75  ? 210 LEU A CG  1 
ATOM   1717 C CD1 . LEU A 1 210 ? 15.014  45.331  -7.125  1   32.18  ? 210 LEU A CD1 1 
ATOM   1718 C CD2 . LEU A 1 210 ? 15.033  44.121  -4.962  1   29.72  ? 210 LEU A CD2 1 
ATOM   1719 N N   . GLU A 1 211 ? 10.547  46.752  -3.73   1   28.36  ? 211 GLU A N   1 
ATOM   1720 C CA  . GLU A 1 211 ? 9.734   47.753  -3.105  1   30.41  ? 211 GLU A CA  1 
ATOM   1721 C C   . GLU A 1 211 ? 9.526   47.48   -1.631  1   28.91  ? 211 GLU A C   1 
ATOM   1722 O O   . GLU A 1 211 ? 9.622   48.357  -0.855  1   25.51  ? 211 GLU A O   1 
ATOM   1723 C CB  . GLU A 1 211 ? 8.409   47.854  -3.812  1   37.65  ? 211 GLU A CB  1 
ATOM   1724 C CG  . GLU A 1 211 ? 8.525   48.399  -5.215  1   50.27  ? 211 GLU A CG  1 
ATOM   1725 C CD  . GLU A 1 211 ? 8.819   47.339  -6.269  1   69.98  ? 211 GLU A CD  1 
ATOM   1726 O OE1 . GLU A 1 211 ? 9.054   46.142  -5.942  1   57.82  ? 211 GLU A OE1 1 
ATOM   1727 O OE2 . GLU A 1 211 ? 8.834   47.726  -7.457  1   71.6   ? 211 GLU A OE2 1 
ATOM   1728 N N   . LEU A 1 212 ? 9.271   46.237  -1.278  1   25.67  ? 212 LEU A N   1 
ATOM   1729 C CA  . LEU A 1 212 ? 9.079   45.869  0.098   1   27.57  ? 212 LEU A CA  1 
ATOM   1730 C C   . LEU A 1 212 ? 10.402  45.879  0.846   1   23.62  ? 212 LEU A C   1 
ATOM   1731 O O   . LEU A 1 212 ? 10.446  46.163  1.992   1   23.19  ? 212 LEU A O   1 
ATOM   1732 C CB  . LEU A 1 212 ? 8.399   44.53   0.218   1   29.4   ? 212 LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 212 ? 6.928   44.486  -0.118  1   34.12  ? 212 LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 212 ? 6.371   43.101  0.082   1   37.59  ? 212 LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 212 ? 6.169   45.447  0.743   1   39.05  ? 212 LEU A CD2 1 
ATOM   1736 N N   . CYS A 1 213 ? 11.472  45.532  0.159   1   23.93  ? 213 CYS A N   1 
ATOM   1737 C CA  . CYS A 1 213 ? 12.803  45.602  0.743   1   26.16  ? 213 CYS A CA  1 
ATOM   1738 C C   . CYS A 1 213 ? 13.034  47.041  1.223   1   26.27  ? 213 CYS A C   1 
ATOM   1739 O O   . CYS A 1 213 ? 13.35   47.272  2.34    1   24.59  ? 213 CYS A O   1 
ATOM   1740 C CB  . CYS A 1 213 ? 13.895  45.247  -0.27   1   26.29  ? 213 CYS A CB  1 
ATOM   1741 S SG  . CYS A 1 213 ? 15.543  45.813  0.143   1   25.67  ? 213 CYS A SG  1 
ATOM   1742 N N   . ARG A 1 214 ? 12.837  47.982  0.331   1   23.4   ? 214 ARG A N   1 
ATOM   1743 C CA  . ARG A 1 214 ? 13.017  49.376  0.634   1   25.71  ? 214 ARG A CA  1 
ATOM   1744 C C   . ARG A 1 214 ? 12.069  49.839  1.723   1   25.38  ? 214 ARG A C   1 
ATOM   1745 O O   . ARG A 1 214 ? 12.449  50.561  2.591   1   25.86  ? 214 ARG A O   1 
ATOM   1746 C CB  . ARG A 1 214 ? 12.843  50.233  -0.608  1   28.11  ? 214 ARG A CB  1 
ATOM   1747 C CG  . ARG A 1 214 ? 14.019  50.246  -1.541  1   27.62  ? 214 ARG A CG  1 
ATOM   1748 C CD  . ARG A 1 214 ? 13.636  50.728  -2.914  1   27.21  ? 214 ARG A CD  1 
ATOM   1749 N NE  . ARG A 1 214 ? 14.457  50.019  -3.826  1   33.09  ? 214 ARG A NE  1 
ATOM   1750 C CZ  . ARG A 1 214 ? 14.183  49.752  -5.067  1   33.04  ? 214 ARG A CZ  1 
ATOM   1751 N NH1 . ARG A 1 214 ? 13.064  50.157  -5.61   1   29.35  ? 214 ARG A NH1 1 
ATOM   1752 N NH2 . ARG A 1 214 ? 15.074  49.095  -5.759  1   36.7   ? 214 ARG A NH2 1 
ATOM   1753 N N   . GLU A 1 215 ? 10.833  49.4    1.66    1   25.19  ? 215 GLU A N   1 
ATOM   1754 C CA  . GLU A 1 215 ? 9.849   49.764  2.639   1   23.49  ? 215 GLU A CA  1 
ATOM   1755 C C   . GLU A 1 215 ? 10.272  49.492  4.066   1   24.5   ? 215 GLU A C   1 
ATOM   1756 O O   . GLU A 1 215 ? 10.119  50.312  4.886   1   24.26  ? 215 GLU A O   1 
ATOM   1757 C CB  . GLU A 1 215 ? 8.526   49.044  2.374   1   24.42  ? 215 GLU A CB  1 
ATOM   1758 C CG  . GLU A 1 215 ? 7.485   49.214  3.466   1   26.98  ? 215 GLU A CG  1 
ATOM   1759 C CD  . GLU A 1 215 ? 6.839   50.58   3.484   1   26.96  ? 215 GLU A CD  1 
ATOM   1760 O OE1 . GLU A 1 215 ? 6.906   51.27   2.495   1   27.99  ? 215 GLU A OE1 1 
ATOM   1761 O OE2 . GLU A 1 215 ? 6.25    50.92   4.481   1   27.9   ? 215 GLU A OE2 1 
ATOM   1762 N N   . TYR A 1 216 ? 10.806  48.319  4.321   1   23.41  ? 216 TYR A N   1 
ATOM   1763 C CA  . TYR A 1 216 ? 11.137  47.9    5.67    1   24.05  ? 216 TYR A CA  1 
ATOM   1764 C C   . TYR A 1 216 ? 12.454  48.517  6.151   1   22.83  ? 216 TYR A C   1 
ATOM   1765 O O   . TYR A 1 216 ? 12.549  48.877  7.32    1   22.66  ? 216 TYR A O   1 
ATOM   1766 C CB  . TYR A 1 216 ? 11.038  46.375  5.773   1   25.11  ? 216 TYR A CB  1 
ATOM   1767 C CG  . TYR A 1 216 ? 9.59    45.939  5.91    1   26.15  ? 216 TYR A CG  1 
ATOM   1768 C CD1 . TYR A 1 216 ? 8.929   46.062  7.118   1   26.35  ? 216 TYR A CD1 1 
ATOM   1769 C CD2 . TYR A 1 216 ? 8.878   45.441  4.831   1   25.84  ? 216 TYR A CD2 1 
ATOM   1770 C CE1 . TYR A 1 216 ? 7.609   45.709  7.257   1   28.69  ? 216 TYR A CE1 1 
ATOM   1771 C CE2 . TYR A 1 216 ? 7.558   45.084  4.946   1   30.33  ? 216 TYR A CE2 1 
ATOM   1772 C CZ  . TYR A 1 216 ? 6.924   45.203  6.169   1   31.35  ? 216 TYR A CZ  1 
ATOM   1773 O OH  . TYR A 1 216 ? 5.629   44.846  6.271   1   34.83  ? 216 TYR A OH  1 
ATOM   1774 N N   . ALA A 1 217 ? 13.413  48.741  5.261   1   21.42  ? 217 ALA A N   1 
ATOM   1775 C CA  . ALA A 1 217 ? 14.649  49.434  5.632   1   23.15  ? 217 ALA A CA  1 
ATOM   1776 C C   . ALA A 1 217 ? 14.369  50.902  5.955   1   25.04  ? 217 ALA A C   1 
ATOM   1777 O O   . ALA A 1 217 ? 14.86   51.438  6.964   1   22.59  ? 217 ALA A O   1 
ATOM   1778 C CB  . ALA A 1 217 ? 15.655  49.308  4.54    1   22     ? 217 ALA A CB  1 
ATOM   1779 N N   . GLN A 1 218 ? 13.573  51.55   5.1     1   21.88  ? 218 GLN A N   1 
ATOM   1780 C CA  . GLN A 1 218 ? 13.193  52.947  5.321   1   23.54  ? 218 GLN A CA  1 
ATOM   1781 C C   . GLN A 1 218 ? 12.373  53.105  6.591   1   25.74  ? 218 GLN A C   1 
ATOM   1782 O O   . GLN A 1 218 ? 12.522  54.099  7.303   1   27.74  ? 218 GLN A O   1 
ATOM   1783 C CB  . GLN A 1 218 ? 12.479  53.549  4.104   1   24.85  ? 218 GLN A CB  1 
ATOM   1784 C CG  . GLN A 1 218 ? 13.423  53.698  2.912   1   28.39  ? 218 GLN A CG  1 
ATOM   1785 C CD  . GLN A 1 218 ? 12.716  53.946  1.591   1   35.44  ? 218 GLN A CD  1 
ATOM   1786 O OE1 . GLN A 1 218 ? 11.602  53.489  1.344   1   40.84  ? 218 GLN A OE1 1 
ATOM   1787 N NE2 . GLN A 1 218 ? 13.296  54.816  0.788   1   43.19  ? 218 GLN A NE2 1 
ATOM   1788 N N   . LYS A 1 219 ? 11.52   52.133  6.899   1   23.51  ? 219 LYS A N   1 
ATOM   1789 C CA  . LYS A 1 219 ? 10.785  52.101  8.141   1   24.19  ? 219 LYS A CA  1 
ATOM   1790 C C   . LYS A 1 219 ? 11.722  52.067  9.352   1   26.71  ? 219 LYS A C   1 
ATOM   1791 O O   . LYS A 1 219 ? 11.487  52.818  10.306  1   29.12  ? 219 LYS A O   1 
ATOM   1792 C CB  . LYS A 1 219 ? 9.82    50.914  8.207   1   23.61  ? 219 LYS A CB  1 
ATOM   1793 C CG  . LYS A 1 219 ? 8.789   50.959  9.335   1   24.25  ? 219 LYS A CG  1 
ATOM   1794 C CD  . LYS A 1 219 ? 7.762   49.81   9.315   1   26.71  ? 219 LYS A CD  1 
ATOM   1795 C CE  . LYS A 1 219 ? 7.053   49.735  7.982   1   27.45  ? 219 LYS A CE  1 
ATOM   1796 N NZ  . LYS A 1 219 ? 6.424   51.032  7.59    1   28.07  ? 219 LYS A NZ  1 
ATOM   1797 N N   . ALA A 1 220 ? 12.721  51.178  9.348   1   25.37  ? 220 ALA A N   1 
ATOM   1798 C CA  . ALA A 1 220 ? 13.704  51.089  10.426  1   25.92  ? 220 ALA A CA  1 
ATOM   1799 C C   . ALA A 1 220 ? 14.438  52.415  10.584  1   26.71  ? 220 ALA A C   1 
ATOM   1800 O O   . ALA A 1 220 ? 14.496  52.96   11.681  1   28.15  ? 220 ALA A O   1 
ATOM   1801 C CB  . ALA A 1 220 ? 14.648  49.939  10.143  1   26.39  ? 220 ALA A CB  1 
ATOM   1802 N N   . ILE A 1 221 ? 14.837  53.024  9.453   1   26.63  ? 221 ILE A N   1 
ATOM   1803 C CA  . ILE A 1 221 ? 15.605  54.262  9.466   1   27.37  ? 221 ILE A CA  1 
ATOM   1804 C C   . ILE A 1 221 ? 14.746  55.388  10.059  1   33.76  ? 221 ILE A C   1 
ATOM   1805 O O   . ILE A 1 221 ? 15.267  56.191  10.821  1   30.93  ? 221 ILE A O   1 
ATOM   1806 C CB  . ILE A 1 221 ? 16.095  54.639  8.053   1   28.18  ? 221 ILE A CB  1 
ATOM   1807 C CG1 . ILE A 1 221 ? 17.185  53.704  7.534   1   26.32  ? 221 ILE A CG1 1 
ATOM   1808 C CG2 . ILE A 1 221 ? 16.488  56.134  7.977   1   30.73  ? 221 ILE A CG2 1 
ATOM   1809 C CD1 . ILE A 1 221 ? 17.374  53.711  6.025   1   29.13  ? 221 ILE A CD1 1 
ATOM   1810 N N   . SER A 1 222 ? 13.453  55.473  9.678   1   29.15  ? 222 SER A N   1 
ATOM   1811 C CA  . SER A 1 222 ? 12.557  56.54   10.081  1   28.49  ? 222 SER A CA  1 
ATOM   1812 C C   . SER A 1 222 ? 12.553  56.707  11.607  1   32.33  ? 222 SER A C   1 
ATOM   1813 O O   . SER A 1 222 ? 12.52   57.854  12.064  1   35.11  ? 222 SER A O   1 
ATOM   1814 C CB  . SER A 1 222 ? 11.161  56.332  9.591   1   27.43  ? 222 SER A CB  1 
ATOM   1815 O OG  . SER A 1 222 ? 10.422  57.537  9.726   1   34.34  ? 222 SER A OG  1 
ATOM   1816 N N   . SER A 1 223 ? 12.52   55.617  12.383  1   30.73  ? 223 SER A N   1 
ATOM   1817 C CA  . SER A 1 223 ? 12.336  55.765  13.82   1   35.03  ? 223 SER A CA  1 
ATOM   1818 C C   . SER A 1 223 ? 13.508  55.297  14.7    1   38.65  ? 223 SER A C   1 
ATOM   1819 O O   . SER A 1 223 ? 13.323  55.357  15.911  1   40.18  ? 223 SER A O   1 
ATOM   1820 C CB  . SER A 1 223 ? 11.104  55.042  14.247  1   34.61  ? 223 SER A CB  1 
ATOM   1821 O OG  . SER A 1 223 ? 11.366  53.69   13.925  1   37.32  ? 223 SER A OG  1 
ATOM   1822 N N   . THR A 1 224 ? 14.638  54.822  14.162  1   29.88  ? 224 THR A N   1 
ATOM   1823 C CA  . THR A 1 224 ? 15.731  54.353  15.017  1   30.88  ? 224 THR A CA  1 
ATOM   1824 C C   . THR A 1 224 ? 16.757  55.476  15.179  1   35.12  ? 224 THR A C   1 
ATOM   1825 O O   . THR A 1 224 ? 16.95   56.336  14.294  1   33.35  ? 224 THR A O   1 
ATOM   1826 C CB  . THR A 1 224 ? 16.39   53.109  14.428  1   32.78  ? 224 THR A CB  1 
ATOM   1827 O OG1 . THR A 1 224 ? 17.195  52.523  15.44   1   33.6   ? 224 THR A OG1 1 
ATOM   1828 C CG2 . THR A 1 224 ? 17.296  53.405  13.251  1   32.39  ? 224 THR A CG2 1 
ATOM   1829 N N   . ASP A 1 225 ? 17.489  55.403  16.291  1   39.22  ? 225 ASP A N   1 
ATOM   1830 C CA  . ASP A 1 225 ? 18.702  56.192  16.504  1   42.47  ? 225 ASP A CA  1 
ATOM   1831 C C   . ASP A 1 225 ? 19.909  55.284  16.752  1   39.7   ? 225 ASP A C   1 
ATOM   1832 O O   . ASP A 1 225 ? 20.887  55.759  17.318  1   39.18  ? 225 ASP A O   1 
ATOM   1833 C CB  . ASP A 1 225 ? 18.495  57.147  17.678  1   47.57  ? 225 ASP A CB  1 
ATOM   1834 C CG  . ASP A 1 225 ? 17.459  58.234  17.413  1   55.73  ? 225 ASP A CG  1 
ATOM   1835 O OD1 . ASP A 1 225 ? 17.624  58.964  16.404  1   49.21  ? 225 ASP A OD1 1 
ATOM   1836 O OD2 . ASP A 1 225 ? 16.473  58.324  18.19   1   62.96  ? 225 ASP A OD2 1 
ATOM   1837 N N   . THR A 1 226 ? 19.802  53.982  16.434  1   30.91  ? 226 THR A N   1 
ATOM   1838 C CA  . THR A 1 226 ? 20.846  53.015  16.751  1   33.94  ? 226 THR A CA  1 
ATOM   1839 C C   . THR A 1 226 ? 21.7    52.875  15.497  1   31.31  ? 226 THR A C   1 
ATOM   1840 O O   . THR A 1 226 ? 21.168  52.456  14.473  1   28.59  ? 226 THR A O   1 
ATOM   1841 C CB  . THR A 1 226 ? 20.207  51.673  17.127  1   31.72  ? 226 THR A CB  1 
ATOM   1842 O OG1 . THR A 1 226 ? 19.419  52.021  18.255  1   38.91  ? 226 THR A OG1 1 
ATOM   1843 C CG2 . THR A 1 226 ? 21.187  50.585  17.492  1   31.22  ? 226 THR A CG2 1 
ATOM   1844 N N   . GLN A 1 227 ? 23.004  53.146  15.612  1   29.8   ? 227 GLN A N   1 
ATOM   1845 C CA  . GLN A 1 227 ? 23.93   53.079  14.481  1   30.1   ? 227 GLN A CA  1 
ATOM   1846 C C   . GLN A 1 227 ? 23.777  51.758  13.716  1   26.82  ? 227 GLN A C   1 
ATOM   1847 O O   . GLN A 1 227 ? 23.755  51.765  12.487  1   25.51  ? 227 GLN A O   1 
ATOM   1848 C CB  . GLN A 1 227 ? 25.383  53.168  14.96   1   31.22  ? 227 GLN A CB  1 
ATOM   1849 C CG  . GLN A 1 227 ? 26.45   53.128  13.863  1   30.56  ? 227 GLN A CG  1 
ATOM   1850 C CD  . GLN A 1 227 ? 27.846  53.356  14.407  1   33.89  ? 227 GLN A CD  1 
ATOM   1851 O OE1 . GLN A 1 227 ? 28.203  52.845  15.459  1   32.26  ? 227 GLN A OE1 1 
ATOM   1852 N NE2 . GLN A 1 227 ? 28.675  54.068  13.673  1   32.88  ? 227 GLN A NE2 1 
ATOM   1853 N N   . ARG A 1 228 ? 23.794  50.635  14.433  1   24.11  ? 228 ARG A N   1 
ATOM   1854 C CA  . ARG A 1 228 ? 23.75   49.319  13.788  1   25.3   ? 228 ARG A CA  1 
ATOM   1855 C C   . ARG A 1 228 ? 22.568  49.2    12.807  1   24.71  ? 228 ARG A C   1 
ATOM   1856 O O   . ARG A 1 228 ? 22.727  48.663  11.714  1   23.71  ? 228 ARG A O   1 
ATOM   1857 C CB  . ARG A 1 228 ? 23.785  48.26   14.899  1   25.29  ? 228 ARG A CB  1 
ATOM   1858 C CG  . ARG A 1 228 ? 23.659  46.827  14.387  1   28.97  ? 228 ARG A CG  1 
ATOM   1859 C CD  . ARG A 1 228 ? 22.225  46.338  14.266  1   30.43  ? 228 ARG A CD  1 
ATOM   1860 N NE  . ARG A 1 228 ? 21.996  44.917  13.95   1   29.27  ? 228 ARG A NE  1 
ATOM   1861 C CZ  . ARG A 1 228 ? 22.27   43.876  14.748  1   32.73  ? 228 ARG A CZ  1 
ATOM   1862 N NH1 . ARG A 1 228 ? 22.631  44.022  16.014  1   34.53  ? 228 ARG A NH1 1 
ATOM   1863 N NH2 . ARG A 1 228 ? 22.116  42.662  14.292  1   32.39  ? 228 ARG A NH2 1 
ATOM   1864 N N   . PHE A 1 229 ? 21.369  49.652  13.197  1   27.21  ? 229 PHE A N   1 
ATOM   1865 C CA  . PHE A 1 229 ? 20.165  49.515  12.393  1   26.59  ? 229 PHE A CA  1 
ATOM   1866 C C   . PHE A 1 229 ? 20.191  50.521  11.257  1   26.03  ? 229 PHE A C   1 
ATOM   1867 O O   . PHE A 1 229 ? 19.766  50.191  10.171  1   24.76  ? 229 PHE A O   1 
ATOM   1868 C CB  . PHE A 1 229 ? 18.881  49.642  13.229  1   28.5   ? 229 PHE A CB  1 
ATOM   1869 C CG  . PHE A 1 229 ? 18.732  48.517  14.23   1   27.14  ? 229 PHE A CG  1 
ATOM   1870 C CD1 . PHE A 1 229 ? 18.905  47.182  13.862  1   29.6   ? 229 PHE A CD1 1 
ATOM   1871 C CD2 . PHE A 1 229 ? 18.55   48.809  15.567  1   30.89  ? 229 PHE A CD2 1 
ATOM   1872 C CE1 . PHE A 1 229 ? 18.819  46.168  14.802  1   28.09  ? 229 PHE A CE1 1 
ATOM   1873 C CE2 . PHE A 1 229 ? 18.435  47.797  16.489  1   31.05  ? 229 PHE A CE2 1 
ATOM   1874 C CZ  . PHE A 1 229 ? 18.589  46.492  16.121  1   30.56  ? 229 PHE A CZ  1 
ATOM   1875 N N   . LEU A 1 230 ? 20.699  51.731  11.499  1   26.15  ? 230 LEU A N   1 
ATOM   1876 C CA  . LEU A 1 230 ? 20.908  52.708  10.418  1   27.48  ? 230 LEU A CA  1 
ATOM   1877 C C   . LEU A 1 230 ? 21.85   52.123  9.371   1   25.22  ? 230 LEU A C   1 
ATOM   1878 O O   . LEU A 1 230 ? 21.521  52.162  8.186   1   25.32  ? 230 LEU A O   1 
ATOM   1879 C CB  . LEU A 1 230 ? 21.437  54.058  10.915  1   28.42  ? 230 LEU A CB  1 
ATOM   1880 C CG  . LEU A 1 230 ? 20.422  54.85   11.728  1   32.24  ? 230 LEU A CG  1 
ATOM   1881 C CD1 . LEU A 1 230 ? 21.12   56.001  12.504  1   35.77  ? 230 LEU A CD1 1 
ATOM   1882 C CD2 . LEU A 1 230 ? 19.289  55.389  10.86   1   31.65  ? 230 LEU A CD2 1 
ATOM   1883 N N   . VAL A 1 231 ? 22.967  51.561  9.818   1   23.41  ? 231 VAL A N   1 
ATOM   1884 C CA  . VAL A 1 231 ? 23.985  51.021  8.9     1   26.75  ? 231 VAL A CA  1 
ATOM   1885 C C   . VAL A 1 231 ? 23.361  49.937  8.022   1   24.88  ? 231 VAL A C   1 
ATOM   1886 O O   . VAL A 1 231 ? 23.485  49.991  6.803   1   22.34  ? 231 VAL A O   1 
ATOM   1887 C CB  . VAL A 1 231 ? 25.205  50.527  9.705   1   27.17  ? 231 VAL A CB  1 
ATOM   1888 C CG1 . VAL A 1 231 ? 25.999  49.414  9.054   1   31.94  ? 231 VAL A CG1 1 
ATOM   1889 C CG2 . VAL A 1 231 ? 26.077  51.743  10.103  1   30.33  ? 231 VAL A CG2 1 
ATOM   1890 N N   . PHE A 1 232 ? 22.75   48.925  8.627   1   22.89  ? 232 PHE A N   1 
ATOM   1891 C CA  . PHE A 1 232 ? 22.297  47.809  7.793   1   22.92  ? 232 PHE A CA  1 
ATOM   1892 C C   . PHE A 1 232 ? 21.077  48.175  6.952   1   22.68  ? 232 PHE A C   1 
ATOM   1893 O O   . PHE A 1 232 ? 20.902  47.581  5.897   1   23.78  ? 232 PHE A O   1 
ATOM   1894 C CB  . PHE A 1 232 ? 22.059  46.533  8.612   1   24.53  ? 232 PHE A CB  1 
ATOM   1895 C CG  . PHE A 1 232 ? 23.36   45.949  9.112   1   25.24  ? 232 PHE A CG  1 
ATOM   1896 C CD1 . PHE A 1 232 ? 24.323  45.534  8.206   1   25.29  ? 232 PHE A CD1 1 
ATOM   1897 C CD2 . PHE A 1 232 ? 23.599  45.722  10.462  1   27.75  ? 232 PHE A CD2 1 
ATOM   1898 C CE1 . PHE A 1 232 ? 25.537  45.018  8.637   1   26.97  ? 232 PHE A CE1 1 
ATOM   1899 C CE2 . PHE A 1 232 ? 24.789  45.153  10.885  1   28.72  ? 232 PHE A CE2 1 
ATOM   1900 C CZ  . PHE A 1 232 ? 25.778  44.836  9.978   1   28.9   ? 232 PHE A CZ  1 
ATOM   1901 N N   . SER A 1 233 ? 20.25   49.142  7.393   1   21.09  ? 233 SER A N   1 
ATOM   1902 C CA  . SER A 1 233 ? 19.151  49.589  6.57    1   23.05  ? 233 SER A CA  1 
ATOM   1903 C C   . SER A 1 233 ? 19.679  50.318  5.325   1   23.27  ? 233 SER A C   1 
ATOM   1904 O O   . SER A 1 233 ? 19.251  50.017  4.225   1   24.63  ? 233 SER A O   1 
ATOM   1905 C CB  . SER A 1 233 ? 18.17   50.448  7.346   1   21.57  ? 233 SER A CB  1 
ATOM   1906 O OG  . SER A 1 233 ? 17.677  49.786  8.519   1   23.08  ? 233 SER A OG  1 
ATOM   1907 N N   . TYR A 1 234 ? 20.604  51.266  5.462   1   23.3   ? 234 TYR A N   1 
ATOM   1908 C CA  . TYR A 1 234 ? 21.141  51.935  4.275   1   22.07  ? 234 TYR A CA  1 
ATOM   1909 C C   . TYR A 1 234 ? 21.903  50.97   3.361   1   23.76  ? 234 TYR A C   1 
ATOM   1910 O O   . TYR A 1 234 ? 21.849  51.095  2.124   1   22.65  ? 234 TYR A O   1 
ATOM   1911 C CB  . TYR A 1 234 ? 21.989  53.139  4.706   1   21.73  ? 234 TYR A CB  1 
ATOM   1912 C CG  . TYR A 1 234 ? 21.181  54.363  5.011   1   23.04  ? 234 TYR A CG  1 
ATOM   1913 C CD1 . TYR A 1 234 ? 20.517  55.032  3.989   1   26.53  ? 234 TYR A CD1 1 
ATOM   1914 C CD2 . TYR A 1 234 ? 21.001  54.824  6.314   1   26.36  ? 234 TYR A CD2 1 
ATOM   1915 C CE1 . TYR A 1 234 ? 19.754  56.161  4.24    1   27.85  ? 234 TYR A CE1 1 
ATOM   1916 C CE2 . TYR A 1 234 ? 20.272  55.963  6.568   1   28.29  ? 234 TYR A CE2 1 
ATOM   1917 C CZ  . TYR A 1 234 ? 19.635  56.612  5.524   1   30.68  ? 234 TYR A CZ  1 
ATOM   1918 O OH  . TYR A 1 234 ? 18.92   57.735  5.735   1   32.13  ? 234 TYR A OH  1 
ATOM   1919 N N   . LEU A 1 235 ? 22.611  50.009  3.957   1   23.26  ? 235 LEU A N   1 
ATOM   1920 C CA  . LEU A 1 235 ? 23.321  49.012  3.157   1   22.31  ? 235 LEU A CA  1 
ATOM   1921 C C   . LEU A 1 235 ? 22.324  48.244  2.285   1   21.54  ? 235 LEU A C   1 
ATOM   1922 O O   . LEU A 1 235 ? 22.593  48.007  1.091   1   21.06  ? 235 LEU A O   1 
ATOM   1923 C CB  . LEU A 1 235 ? 24.094  48.077  4.081   1   23.29  ? 235 LEU A CB  1 
ATOM   1924 C CG  . LEU A 1 235 ? 24.999  47.053  3.394   1   21.32  ? 235 LEU A CG  1 
ATOM   1925 C CD1 . LEU A 1 235 ? 26.31   47.74   2.987   1   21.8   ? 235 LEU A CD1 1 
ATOM   1926 C CD2 . LEU A 1 235 ? 25.311  45.816  4.278   1   22.76  ? 235 LEU A CD2 1 
ATOM   1927 N N   . THR A 1 236 ? 21.212  47.79   2.883   1   21.35  ? 236 THR A N   1 
ATOM   1928 C CA  . THR A 1 236 ? 20.26   46.933  2.187   1   21.37  ? 236 THR A CA  1 
ATOM   1929 C C   . THR A 1 236 ? 19.542  47.74   1.098   1   22.79  ? 236 THR A C   1 
ATOM   1930 O O   . THR A 1 236 ? 19.314  47.262  -0.022  1   21.97  ? 236 THR A O   1 
ATOM   1931 C CB  . THR A 1 236 ? 19.288  46.299  3.18    1   22.06  ? 236 THR A CB  1 
ATOM   1932 O OG1 . THR A 1 236 ? 20.043  45.698  4.217   1   20.76  ? 236 THR A OG1 1 
ATOM   1933 C CG2 . THR A 1 236 ? 18.416  45.262  2.512   1   24.04  ? 236 THR A CG2 1 
ATOM   1934 N N   . ILE A 1 237 ? 19.265  49.021  1.373   1   23.55  ? 237 ILE A N   1 
ATOM   1935 C CA  . ILE A 1 237 ? 18.67   49.864  0.364   1   21.3   ? 237 ILE A CA  1 
ATOM   1936 C C   . ILE A 1 237 ? 19.631  50.025  -0.839  1   20.54  ? 237 ILE A C   1 
ATOM   1937 O O   . ILE A 1 237 ? 19.241  49.998  -2.008  1   24.62  ? 237 ILE A O   1 
ATOM   1938 C CB  . ILE A 1 237 ? 18.243  51.241  0.956   1   22.13  ? 237 ILE A CB  1 
ATOM   1939 C CG1 . ILE A 1 237 ? 17.148  51.12   1.959   1   26.24  ? 237 ILE A CG1 1 
ATOM   1940 C CG2 . ILE A 1 237 ? 17.781  52.165  -0.209  1   23.65  ? 237 ILE A CG2 1 
ATOM   1941 C CD1 . ILE A 1 237 ? 16.905  52.425  2.75    1   26.3   ? 237 ILE A CD1 1 
ATOM   1942 N N   . GLY A 1 238 ? 20.906  50.252  -0.564  1   23     ? 238 GLY A N   1 
ATOM   1943 C CA  . GLY A 1 238 ? 21.89   50.459  -1.61   1   24.01  ? 238 GLY A CA  1 
ATOM   1944 C C   . GLY A 1 238 ? 22.015  49.182  -2.446  1   22.51  ? 238 GLY A C   1 
ATOM   1945 O O   . GLY A 1 238 ? 22.075  49.265  -3.661  1   23.53  ? 238 GLY A O   1 
ATOM   1946 N N   . THR A 1 239 ? 21.97   48.013  -1.803  1   21.62  ? 239 THR A N   1 
ATOM   1947 C CA  . THR A 1 239 ? 21.998  46.758  -2.558  1   23.66  ? 239 THR A CA  1 
ATOM   1948 C C   . THR A 1 239 ? 20.777  46.595  -3.452  1   24.46  ? 239 THR A C   1 
ATOM   1949 O O   . THR A 1 239 ? 20.932  46.071  -4.563  1   23.79  ? 239 THR A O   1 
ATOM   1950 C CB  . THR A 1 239 ? 22.172  45.572  -1.616  1   23.09  ? 239 THR A CB  1 
ATOM   1951 O OG1 . THR A 1 239 ? 23.317  45.901  -0.872  1   22.61  ? 239 THR A OG1 1 
ATOM   1952 C CG2 . THR A 1 239 ? 22.44   44.267  -2.357  1   23.64  ? 239 THR A CG2 1 
ATOM   1953 N N   . SER A 1 240 ? 19.606  47.052  -2.975  1   24.26  ? 240 SER A N   1 
ATOM   1954 C CA  . SER A 1 240 ? 18.357  46.987  -3.722  1   23.24  ? 240 SER A CA  1 
ATOM   1955 C C   . SER A 1 240 ? 18.439  47.738  -5.052  1   24.08  ? 240 SER A C   1 
ATOM   1956 O O   . SER A 1 240 ? 17.684  47.414  -5.946  1   24.5   ? 240 SER A O   1 
ATOM   1957 C CB  . SER A 1 240 ? 17.138  47.462  -2.933  1   23.78  ? 240 SER A CB  1 
ATOM   1958 O OG  . SER A 1 240 ? 16.95   48.878  -3.022  1   23.53  ? 240 SER A OG  1 
ATOM   1959 N N   . TYR A 1 241 ? 19.378  48.657  -5.204  1   24.08  ? 241 TYR A N   1 
ATOM   1960 C CA  . TYR A 1 241 ? 19.556  49.438  -6.419  1   23.42  ? 241 TYR A CA  1 
ATOM   1961 C C   . TYR A 1 241 ? 20.766  49.032  -7.248  1   23.82  ? 241 TYR A C   1 
ATOM   1962 O O   . TYR A 1 241 ? 20.984  49.614  -8.309  1   25.5   ? 241 TYR A O   1 
ATOM   1963 C CB  . TYR A 1 241 ? 19.705  50.904  -6.037  1   26.95  ? 241 TYR A CB  1 
ATOM   1964 C CG  . TYR A 1 241 ? 18.409  51.598  -5.658  1   25.43  ? 241 TYR A CG  1 
ATOM   1965 C CD1 . TYR A 1 241 ? 17.387  51.717  -6.595  1   27.87  ? 241 TYR A CD1 1 
ATOM   1966 C CD2 . TYR A 1 241 ? 18.22   52.118  -4.386  1   25.31  ? 241 TYR A CD2 1 
ATOM   1967 C CE1 . TYR A 1 241 ? 16.217  52.378  -6.288  1   31.02  ? 241 TYR A CE1 1 
ATOM   1968 C CE2 . TYR A 1 241 ? 17.038  52.762  -4.05   1   30.26  ? 241 TYR A CE2 1 
ATOM   1969 C CZ  . TYR A 1 241 ? 16.038  52.872  -5.003  1   30.86  ? 241 TYR A CZ  1 
ATOM   1970 O OH  . TYR A 1 241 ? 14.907  53.538  -4.715  1   31.11  ? 241 TYR A OH  1 
ATOM   1971 N N   . ILE A 1 242 ? 21.528  48.049  -6.796  1   22.57  ? 242 ILE A N   1 
ATOM   1972 C CA  . ILE A 1 242 ? 22.863  47.791  -7.328  1   27.92  ? 242 ILE A CA  1 
ATOM   1973 C C   . ILE A 1 242 ? 22.795  47.401  -8.812  1   34.15  ? 242 ILE A C   1 
ATOM   1974 O O   . ILE A 1 242 ? 23.694  47.78   -9.573  1   37.5   ? 242 ILE A O   1 
ATOM   1975 C CB  . ILE A 1 242 ? 23.576  46.777  -6.396  1   33.65  ? 242 ILE A CB  1 
ATOM   1976 C CG1 . ILE A 1 242 ? 25.055  46.964  -6.325  1   40.23  ? 242 ILE A CG1 1 
ATOM   1977 C CG2 . ILE A 1 242 ? 23.19   45.342  -6.7    1   38.77  ? 242 ILE A CG2 1 
ATOM   1978 C CD1 . ILE A 1 242 ? 25.721  46.109  -5.263  1   40.1   ? 242 ILE A CD1 1 
ATOM   1979 N N   . PHE A 1 243 ? 21.698  46.748  -9.256  1   28.91  ? 243 PHE A N   1 
ATOM   1980 C CA  . PHE A 1 243 ? 21.575  46.257  -10.63  1   37.46  ? 243 PHE A CA  1 
ATOM   1981 C C   . PHE A 1 243 ? 20.688  47.177  -11.444 1   38.21  ? 243 PHE A C   1 
ATOM   1982 O O   . PHE A 1 243 ? 20.644  47.004  -12.648 1   54.06  ? 243 PHE A O   1 
ATOM   1983 C CB  . PHE A 1 243 ? 21.061  44.804  -10.757 1   34.69  ? 243 PHE A CB  1 
ATOM   1984 C CG  . PHE A 1 243 ? 21.977  43.856  -10.011 1   43.07  ? 243 PHE A CG  1 
ATOM   1985 C CD1 . PHE A 1 243 ? 23.299  43.735  -10.399 1   43.21  ? 243 PHE A CD1 1 
ATOM   1986 C CD2 . PHE A 1 243 ? 21.562  43.154  -8.882  1   47.27  ? 243 PHE A CD2 1 
ATOM   1987 C CE1 . PHE A 1 243 ? 24.172  42.903  -9.72   1   40.15  ? 243 PHE A CE1 1 
ATOM   1988 C CE2 . PHE A 1 243 ? 22.454  42.345  -8.169  1   48.51  ? 243 PHE A CE2 1 
ATOM   1989 C CZ  . PHE A 1 243 ? 23.755  42.184  -8.62   1   43.31  ? 243 PHE A CZ  1 
ATOM   1990 N N   . SER A 1 244 ? 20.018  48.161  -10.828 1   34.89  ? 244 SER A N   1 
ATOM   1991 C CA  . SER A 1 244 ? 19.02   48.966  -11.495 1   33.68  ? 244 SER A CA  1 
ATOM   1992 C C   . SER A 1 244 ? 19.352  50.463  -11.537 1   37.34  ? 244 SER A C   1 
ATOM   1993 O O   . SER A 1 244 ? 18.901  51.144  -12.45  1   37.82  ? 244 SER A O   1 
ATOM   1994 C CB  . SER A 1 244 ? 17.681  48.749  -10.873 1   36.99  ? 244 SER A CB  1 
ATOM   1995 O OG  . SER A 1 244 ? 17.673  49.069  -9.503  1   36.4   ? 244 SER A OG  1 
ATOM   1996 N N   . ASP A 1 245 ? 20.094  51.003  -10.559 1   31.22  ? 245 ASP A N   1 
ATOM   1997 C CA  . ASP A 1 245 ? 20.286  52.452  -10.507 1   31.37  ? 245 ASP A CA  1 
ATOM   1998 C C   . ASP A 1 245 ? 21.575  52.772  -9.762  1   29.95  ? 245 ASP A C   1 
ATOM   1999 O O   . ASP A 1 245 ? 21.587  52.831  -8.536  1   27.52  ? 245 ASP A O   1 
ATOM   2000 C CB  . ASP A 1 245 ? 19.096  53.152  -9.878  1   30.56  ? 245 ASP A CB  1 
ATOM   2001 C CG  . ASP A 1 245 ? 19.091  54.677  -10.025 1   33.81  ? 245 ASP A CG  1 
ATOM   2002 O OD1 . ASP A 1 245 ? 20.189  55.327  -9.988  1   33.77  ? 245 ASP A OD1 1 
ATOM   2003 O OD2 . ASP A 1 245 ? 17.981  55.229  -10.047 1   36.57  ? 245 ASP A OD2 1 
ATOM   2004 N N   . PHE A 1 246 ? 22.631  52.974  -10.536 1   28.92  ? 246 PHE A N   1 
ATOM   2005 C CA  . PHE A 1 246 ? 23.951  53.247  -10.027 1   25.74  ? 246 PHE A CA  1 
ATOM   2006 C C   . PHE A 1 246 ? 23.928  54.393  -9.035  1   25     ? 246 PHE A C   1 
ATOM   2007 O O   . PHE A 1 246 ? 24.496  54.261  -7.964  1   25.84  ? 246 PHE A O   1 
ATOM   2008 C CB  . PHE A 1 246 ? 24.924  53.509  -11.174 1   26.9   ? 246 PHE A CB  1 
ATOM   2009 C CG  . PHE A 1 246 ? 26.294  53.951  -10.694 1   29.34  ? 246 PHE A CG  1 
ATOM   2010 C CD1 . PHE A 1 246 ? 27.177  53.051  -10.089 1   27.71  ? 246 PHE A CD1 1 
ATOM   2011 C CD2 . PHE A 1 246 ? 26.635  55.307  -10.734 1   33.1   ? 246 PHE A CD2 1 
ATOM   2012 C CE1 . PHE A 1 246 ? 28.406  53.484  -9.634  1   30.77  ? 246 PHE A CE1 1 
ATOM   2013 C CE2 . PHE A 1 246 ? 27.885  55.742  -10.287 1   34.32  ? 246 PHE A CE2 1 
ATOM   2014 C CZ  . PHE A 1 246 ? 28.779  54.82   -9.748  1   30.93  ? 246 PHE A CZ  1 
ATOM   2015 N N   . ASN A 1 247 ? 23.339  55.527  -9.424  1   25     ? 247 ASN A N   1 
ATOM   2016 C CA  . ASN A 1 247 ? 23.399  56.739  -8.613  1   26.38  ? 247 ASN A CA  1 
ATOM   2017 C C   . ASN A 1 247 ? 22.662  56.565  -7.275  1   26.4   ? 247 ASN A C   1 
ATOM   2018 O O   . ASN A 1 247 ? 23.17   56.999  -6.228  1   24.26  ? 247 ASN A O   1 
ATOM   2019 C CB  . ASN A 1 247 ? 22.908  57.917  -9.441  1   27.43  ? 247 ASN A CB  1 
ATOM   2020 C CG  . ASN A 1 247 ? 23.846  58.17   -10.6   1   30.21  ? 247 ASN A CG  1 
ATOM   2021 O OD1 . ASN A 1 247 ? 24.994  58.587  -10.415 1   33.33  ? 247 ASN A OD1 1 
ATOM   2022 N ND2 . ASN A 1 247 ? 23.417  57.855  -11.804 1   32.38  ? 247 ASN A ND2 1 
ATOM   2023 N N   . LEU A 1 248 ? 21.507  55.891  -7.265  1   27.5   ? 248 LEU A N   1 
ATOM   2024 C CA  . LEU A 1 248 ? 20.763  55.68   -6.021  1   25.36  ? 248 LEU A CA  1 
ATOM   2025 C C   . LEU A 1 248 ? 21.446  54.636  -5.14   1   24.02  ? 248 LEU A C   1 
ATOM   2026 O O   . LEU A 1 248 ? 21.405  54.747  -3.936  1   24.63  ? 248 LEU A O   1 
ATOM   2027 C CB  . LEU A 1 248 ? 19.291  55.327  -6.23   1   27.53  ? 248 LEU A CB  1 
ATOM   2028 C CG  . LEU A 1 248 ? 18.383  56.461  -6.709  1   32.38  ? 248 LEU A CG  1 
ATOM   2029 C CD1 . LEU A 1 248 ? 16.984  55.963  -6.931  1   34.67  ? 248 LEU A CD1 1 
ATOM   2030 C CD2 . LEU A 1 248 ? 18.329  57.599  -5.705  1   37.02  ? 248 LEU A CD2 1 
ATOM   2031 N N   . SER A 1 249 ? 22.067  53.621  -5.748  1   25.21  ? 249 SER A N   1 
ATOM   2032 C CA  . SER A 1 249 ? 22.84   52.636  -5.008  1   23.2   ? 249 SER A CA  1 
ATOM   2033 C C   . SER A 1 249 ? 23.977  53.326  -4.267  1   24.01  ? 249 SER A C   1 
ATOM   2034 O O   . SER A 1 249 ? 24.125  53.216  -3.036  1   22.24  ? 249 SER A O   1 
ATOM   2035 C CB  . SER A 1 249 ? 23.321  51.529  -5.911  1   22.72  ? 249 SER A CB  1 
ATOM   2036 O OG  . SER A 1 249 ? 23.985  50.528  -5.151  1   22.61  ? 249 SER A OG  1 
ATOM   2037 N N   . LYS A 1 250 ? 24.749  54.116  -5.001  1   22.38  ? 250 LYS A N   1 
ATOM   2038 C CA  . LYS A 1 250 ? 25.894  54.797  -4.429  1   23.92  ? 250 LYS A CA  1 
ATOM   2039 C C   . LYS A 1 250 ? 25.436  55.771  -3.357  1   22.48  ? 250 LYS A C   1 
ATOM   2040 O O   . LYS A 1 250 ? 26.061  55.85   -2.319  1   24.41  ? 250 LYS A O   1 
ATOM   2041 C CB  . LYS A 1 250 ? 26.683  55.507  -5.527  1   24.18  ? 250 LYS A CB  1 
ATOM   2042 C CG  . LYS A 1 250 ? 27.861  56.316  -5.024  1   28.67  ? 250 LYS A CG  1 
ATOM   2043 C CD  . LYS A 1 250 ? 28.634  56.784  -6.268  1   32.75  ? 250 LYS A CD  1 
ATOM   2044 C CE  . LYS A 1 250 ? 29.487  57.951  -6.058  1   42.79  ? 250 LYS A CE  1 
ATOM   2045 N NZ  . LYS A 1 250 ? 30.206  58.212  -7.319  1   45.75  ? 250 LYS A NZ  1 
ATOM   2046 N N   . GLN A 1 251 ? 24.378  56.53   -3.63   1   24.44  ? 251 GLN A N   1 
ATOM   2047 C CA  . GLN A 1 251 ? 23.844  57.472  -2.651  1   26.72  ? 251 GLN A CA  1 
ATOM   2048 C C   . GLN A 1 251 ? 23.603  56.822  -1.287  1   25.32  ? 251 GLN A C   1 
ATOM   2049 O O   . GLN A 1 251 ? 24.035  57.354  -0.252  1   26.69  ? 251 GLN A O   1 
ATOM   2050 C CB  . GLN A 1 251 ? 22.578  58.107  -3.206  1   27.26  ? 251 GLN A CB  1 
ATOM   2051 C CG  . GLN A 1 251 ? 21.865  59.065  -2.256  1   29.98  ? 251 GLN A CG  1 
ATOM   2052 C CD  . GLN A 1 251 ? 20.468  59.378  -2.737  1   32.73  ? 251 GLN A CD  1 
ATOM   2053 O OE1 . GLN A 1 251 ? 19.49   59.262  -1.997  1   39.54  ? 251 GLN A OE1 1 
ATOM   2054 N NE2 . GLN A 1 251 ? 20.371  59.749  -3.996  1   30.85  ? 251 GLN A NE2 1 
ATOM   2055 N N   . ASN A 1 252 ? 22.858  55.72   -1.303  1   22.74  ? 252 ASN A N   1 
ATOM   2056 C CA  . ASN A 1 252 ? 22.496  54.999  -0.087  1   23.76  ? 252 ASN A CA  1 
ATOM   2057 C C   . ASN A 1 252 ? 23.704  54.379  0.594   1   22.95  ? 252 ASN A C   1 
ATOM   2058 O O   . ASN A 1 252 ? 23.807  54.434  1.806   1   23.4   ? 252 ASN A O   1 
ATOM   2059 C CB  . ASN A 1 252 ? 21.397  53.982  -0.384  1   22.76  ? 252 ASN A CB  1 
ATOM   2060 C CG  . ASN A 1 252 ? 20.075  54.682  -0.47   1   26.96  ? 252 ASN A CG  1 
ATOM   2061 O OD1 . ASN A 1 252 ? 19.478  54.942  0.582   1   26.47  ? 252 ASN A OD1 1 
ATOM   2062 N ND2 . ASN A 1 252 ? 19.596  54.965  -1.682  1   25.25  ? 252 ASN A ND2 1 
ATOM   2063 N N   . TYR A 1 253 ? 24.685  53.848  -0.183  1   22.72  ? 253 TYR A N   1 
ATOM   2064 C CA  . TYR A 1 253 ? 25.891  53.33   0.439   1   23.64  ? 253 TYR A CA  1 
ATOM   2065 C C   . TYR A 1 253 ? 26.702  54.474  1.079   1   24.78  ? 253 TYR A C   1 
ATOM   2066 O O   . TYR A 1 253 ? 27.283  54.285  2.136   1   22.75  ? 253 TYR A O   1 
ATOM   2067 C CB  . TYR A 1 253 ? 26.755  52.545  -0.561  1   21.21  ? 253 TYR A CB  1 
ATOM   2068 C CG  . TYR A 1 253 ? 26.222  51.217  -1.063  1   23.76  ? 253 TYR A CG  1 
ATOM   2069 C CD1 . TYR A 1 253 ? 25.626  50.294  -0.19   1   23.34  ? 253 TYR A CD1 1 
ATOM   2070 C CD2 . TYR A 1 253 ? 26.448  50.811  -2.383  1   25.42  ? 253 TYR A CD2 1 
ATOM   2071 C CE1 . TYR A 1 253 ? 25.13   49.095  -0.636  1   22.05  ? 253 TYR A CE1 1 
ATOM   2072 C CE2 . TYR A 1 253 ? 26.034  49.567  -2.81   1   25.34  ? 253 TYR A CE2 1 
ATOM   2073 C CZ  . TYR A 1 253 ? 25.378  48.71   -1.943  1   23.84  ? 253 TYR A CZ  1 
ATOM   2074 O OH  . TYR A 1 253 ? 24.979  47.489  -2.324  1   21.07  ? 253 TYR A OH  1 
ATOM   2075 N N   . LEU A 1 254 ? 26.727  55.678  0.474   1   25.7   ? 254 LEU A N   1 
ATOM   2076 C CA  . LEU A 1 254 ? 27.547  56.76   0.982   1   24.2   ? 254 LEU A CA  1 
ATOM   2077 C C   . LEU A 1 254 ? 26.928  57.357  2.234   1   27.82  ? 254 LEU A C   1 
ATOM   2078 O O   . LEU A 1 254 ? 27.685  57.751  3.138   1   27.15  ? 254 LEU A O   1 
ATOM   2079 C CB  . LEU A 1 254 ? 27.795  57.868  -0.05   1   26.77  ? 254 LEU A CB  1 
ATOM   2080 C CG  . LEU A 1 254 ? 28.746  57.535  -1.205  1   27.81  ? 254 LEU A CG  1 
ATOM   2081 C CD1 . LEU A 1 254 ? 28.99   58.731  -2.152  1   30.51  ? 254 LEU A CD1 1 
ATOM   2082 C CD2 . LEU A 1 254 ? 30.059  57.025  -0.697  1   30.13  ? 254 LEU A CD2 1 
ATOM   2083 N N   . ILE A 1 255 ? 25.59   57.478  2.26    1   26.27  ? 255 ILE A N   1 
ATOM   2084 C CA  . ILE A 1 255 ? 24.885  57.862  3.479   1   29.1   ? 255 ILE A CA  1 
ATOM   2085 C C   . ILE A 1 255 ? 25.198  56.852  4.583   1   26.99  ? 255 ILE A C   1 
ATOM   2086 O O   . ILE A 1 255 ? 25.562  57.235  5.702   1   24.82  ? 255 ILE A O   1 
ATOM   2087 C CB  . ILE A 1 255 ? 23.377  58.073  3.241   1   28.85  ? 255 ILE A CB  1 
ATOM   2088 C CG1 . ILE A 1 255 ? 23.12   59.274  2.313   1   31.44  ? 255 ILE A CG1 1 
ATOM   2089 C CG2 . ILE A 1 255 ? 22.606  58.22   4.56    1   30.52  ? 255 ILE A CG2 1 
ATOM   2090 C CD1 . ILE A 1 255 ? 21.715  59.299  1.713   1   32.73  ? 255 ILE A CD1 1 
ATOM   2091 N N   . GLY A 1 256 ? 25.015  55.581  4.299   1   29.05  ? 256 GLY A N   1 
ATOM   2092 C CA  . GLY A 1 256 ? 25.316  54.537  5.278   1   26.32  ? 256 GLY A CA  1 
ATOM   2093 C C   . GLY A 1 256 ? 26.749  54.582  5.83    1   26.52  ? 256 GLY A C   1 
ATOM   2094 O O   . GLY A 1 256 ? 26.96   54.424  7.049   1   27.24  ? 256 GLY A O   1 
ATOM   2095 N N   . LEU A 1 257 ? 27.738  54.756  4.926   1   25.96  ? 257 LEU A N   1 
ATOM   2096 C CA  . LEU A 1 257 ? 29.145  54.847  5.278   1   27.46  ? 257 LEU A CA  1 
ATOM   2097 C C   . LEU A 1 257 ? 29.363  56.012  6.236   1   29.04  ? 257 LEU A C   1 
ATOM   2098 O O   . LEU A 1 257 ? 30.117  55.883  7.206   1   29.62  ? 257 LEU A O   1 
ATOM   2099 C CB  . LEU A 1 257 ? 29.982  54.969  3.992   1   29.45  ? 257 LEU A CB  1 
ATOM   2100 C CG  . LEU A 1 257 ? 31.491  55.009  4.187   1   31.37  ? 257 LEU A CG  1 
ATOM   2101 C CD1 . LEU A 1 257 ? 32.029  53.814  4.957   1   29.14  ? 257 LEU A CD1 1 
ATOM   2102 C CD2 . LEU A 1 257 ? 32.216  55.196  2.88    1   32.77  ? 257 LEU A CD2 1 
ATOM   2103 N N   . LYS A 1 258 ? 28.676  57.133  5.986   1   28.9   ? 258 LYS A N   1 
ATOM   2104 C CA  . LYS A 1 258 ? 28.727  58.273  6.885   1   31.87  ? 258 LYS A CA  1 
ATOM   2105 C C   . LYS A 1 258 ? 28.175  57.892  8.264   1   30.2   ? 258 LYS A C   1 
ATOM   2106 O O   . LYS A 1 258 ? 28.795  58.232  9.245   1   29.59  ? 258 LYS A O   1 
ATOM   2107 C CB  . LYS A 1 258 ? 27.986  59.48   6.296   1   34.82  ? 258 LYS A CB  1 
ATOM   2108 C CG  . LYS A 1 258 ? 28.108  60.803  7.087   1   42.72  ? 258 LYS A CG  1 
ATOM   2109 C CD  . LYS A 1 258 ? 26.981  61.804  6.821   1   51.96  ? 258 LYS A CD  1 
ATOM   2110 C CE  . LYS A 1 258 ? 25.687  61.645  7.645   1   60.62  ? 258 LYS A CE  1 
ATOM   2111 N NZ  . LYS A 1 258 ? 24.85   60.475  7.355   1   63.59  ? 258 LYS A NZ  1 
ATOM   2112 N N   . PHE A 1 259 ? 27.059  57.156  8.354   1   27.32  ? 259 PHE A N   1 
ATOM   2113 C CA  . PHE A 1 259 ? 26.577  56.661  9.648   1   26.97  ? 259 PHE A CA  1 
ATOM   2114 C C   . PHE A 1 259 ? 27.502  55.604  10.26   1   28.22  ? 259 PHE A C   1 
ATOM   2115 O O   . PHE A 1 259 ? 27.551  55.443  11.494  1   28.3   ? 259 PHE A O   1 
ATOM   2116 C CB  . PHE A 1 259 ? 25.155  56.11   9.598   1   27.35  ? 259 PHE A CB  1 
ATOM   2117 C CG  . PHE A 1 259 ? 24.08   57.178  9.506   1   29.81  ? 259 PHE A CG  1 
ATOM   2118 C CD1 . PHE A 1 259 ? 23.857  58.076  10.558  1   34.17  ? 259 PHE A CD1 1 
ATOM   2119 C CD2 . PHE A 1 259 ? 23.281  57.294  8.358   1   27.79  ? 259 PHE A CD2 1 
ATOM   2120 C CE1 . PHE A 1 259 ? 22.864  59.048  10.468  1   35.08  ? 259 PHE A CE1 1 
ATOM   2121 C CE2 . PHE A 1 259 ? 22.322  58.304  8.263   1   29.74  ? 259 PHE A CE2 1 
ATOM   2122 C CZ  . PHE A 1 259 ? 22.106  59.174  9.326   1   32.7   ? 259 PHE A CZ  1 
ATOM   2123 N N   . ALA A 1 260 ? 28.238  54.847  9.433   1   25.43  ? 260 ALA A N   1 
ATOM   2124 C CA  . ALA A 1 260 ? 29.194  53.871  9.953   1   28.02  ? 260 ALA A CA  1 
ATOM   2125 C C   . ALA A 1 260 ? 30.478  54.462  10.564  1   30.25  ? 260 ALA A C   1 
ATOM   2126 O O   . ALA A 1 260 ? 31.289  53.71   11.108  1   30.11  ? 260 ALA A O   1 
ATOM   2127 C CB  . ALA A 1 260 ? 29.596  52.883  8.85    1   28.86  ? 260 ALA A CB  1 
ATOM   2128 N N   . LYS A 1 261 ? 30.759  55.732  10.324  1   33.86  ? 261 LYS A N   1 
ATOM   2129 C CA  . LYS A 1 261 ? 32.026  56.392  10.643  1   41.87  ? 261 LYS A CA  1 
ATOM   2130 C C   . LYS A 1 261 ? 32.579  56.003  11.999  1   38.46  ? 261 LYS A C   1 
ATOM   2131 O O   . LYS A 1 261 ? 31.852  56.085  12.973  1   38.51  ? 261 LYS A O   1 
ATOM   2132 C CB  . LYS A 1 261 ? 31.814  57.896  10.807  1   53.04  ? 261 LYS A CB  1 
ATOM   2133 C CG  . LYS A 1 261 ? 32.247  58.719  9.637   1   69.05  ? 261 LYS A CG  1 
ATOM   2134 C CD  . LYS A 1 261 ? 33.706  59.147  9.723   1   71.67  ? 261 LYS A CD  1 
ATOM   2135 C CE  . LYS A 1 261 ? 33.913  60.22   8.687   1   83.08  ? 261 LYS A CE  1 
ATOM   2136 N NZ  . LYS A 1 261 ? 35.28   60.737  8.654   1   88.69  ? 261 LYS A NZ  1 
ATOM   2137 N N   . GLY A 1 262 ? 33.838  55.545  12.03   1   42.87  ? 262 GLY A N   1 
ATOM   2138 C CA  . GLY A 1 262 ? 34.494  55.201  13.289  1   48.89  ? 262 GLY A CA  1 
ATOM   2139 C C   . GLY A 1 262 ? 34.307  53.742  13.724  1   48.15  ? 262 GLY A C   1 
ATOM   2140 O O   . GLY A 1 262 ? 34.883  53.319  14.728  1   42.89  ? 262 GLY A O   1 
ATOM   2141 N N   . ASN A 1 263 ? 33.552  52.936  12.963  1   37.11  ? 263 ASN A N   1 
ATOM   2142 C CA  . ASN A 1 263 ? 33.372  51.532  13.268  1   34.59  ? 263 ASN A CA  1 
ATOM   2143 C C   . ASN A 1 263 ? 33.867  50.772  12.035  1   35.9   ? 263 ASN A C   1 
ATOM   2144 O O   . ASN A 1 263 ? 33.127  50.694  11.043  1   29.63  ? 263 ASN A O   1 
ATOM   2145 C CB  . ASN A 1 263 ? 31.923  51.191  13.613  1   34.61  ? 263 ASN A CB  1 
ATOM   2146 C CG  . ASN A 1 263 ? 31.762  49.735  13.993  1   38.82  ? 263 ASN A CG  1 
ATOM   2147 O OD1 . ASN A 1 263 ? 32.187  48.833  13.251  1   34.71  ? 263 ASN A OD1 1 
ATOM   2148 N ND2 . ASN A 1 263 ? 31.14   49.459  15.133  1   37.44  ? 263 ASN A ND2 1 
ATOM   2149 N N   . PRO A 1 264 ? 35.103  50.227  12.06   1   37.1   ? 264 PRO A N   1 
ATOM   2150 C CA  . PRO A 1 264 ? 35.662  49.592  10.87   1   35.04  ? 264 PRO A CA  1 
ATOM   2151 C C   . PRO A 1 264 ? 34.85   48.441  10.313  1   34.36  ? 264 PRO A C   1 
ATOM   2152 O O   . PRO A 1 264 ? 34.836  48.279  9.092   1   29.55  ? 264 PRO A O   1 
ATOM   2153 C CB  . PRO A 1 264 ? 37.046  49.142  11.307  1   37.18  ? 264 PRO A CB  1 
ATOM   2154 C CG  . PRO A 1 264 ? 37.387  50.145  12.394  1   40.51  ? 264 PRO A CG  1 
ATOM   2155 C CD  . PRO A 1 264 ? 36.087  50.307  13.173  1   39.08  ? 264 PRO A CD  1 
ATOM   2156 N N   . GLY A 1 265 ? 34.224  47.64   11.198  1   32.49  ? 265 GLY A N   1 
ATOM   2157 C CA  . GLY A 1 265 ? 33.388  46.529  10.774  1   31.92  ? 265 GLY A CA  1 
ATOM   2158 C C   . GLY A 1 265 ? 32.201  46.99   9.932   1   29.6   ? 265 GLY A C   1 
ATOM   2159 O O   . GLY A 1 265 ? 31.888  46.403  8.895   1   30.88  ? 265 GLY A O   1 
ATOM   2160 N N   . PHE A 1 266 ? 31.525  48.048  10.381  1   25.58  ? 266 PHE A N   1 
ATOM   2161 C CA  . PHE A 1 266 ? 30.408  48.582  9.655   1   26.44  ? 266 PHE A CA  1 
ATOM   2162 C C   . PHE A 1 266 ? 30.884  49.249  8.382   1   25.04  ? 266 PHE A C   1 
ATOM   2163 O O   . PHE A 1 266 ? 30.247  49.074  7.348   1   26.91  ? 266 PHE A O   1 
ATOM   2164 C CB  . PHE A 1 266 ? 29.631  49.592  10.513  1   25.41  ? 266 PHE A CB  1 
ATOM   2165 C CG  . PHE A 1 266 ? 28.847  49.037  11.707  1   27.34  ? 266 PHE A CG  1 
ATOM   2166 C CD1 . PHE A 1 266 ? 28.43   47.72   11.798  1   28.47  ? 266 PHE A CD1 1 
ATOM   2167 C CD2 . PHE A 1 266 ? 28.529  49.878  12.769  1   31.71  ? 266 PHE A CD2 1 
ATOM   2168 C CE1 . PHE A 1 266 ? 27.709  47.282  12.9    1   33.55  ? 266 PHE A CE1 1 
ATOM   2169 C CE2 . PHE A 1 266 ? 27.831  49.42   13.874  1   30.18  ? 266 PHE A CE2 1 
ATOM   2170 C CZ  . PHE A 1 266 ? 27.434  48.134  13.951  1   30.85  ? 266 PHE A CZ  1 
ATOM   2171 N N   . GLU A 1 267 ? 31.979  50.002  8.449   1   25.22  ? 267 GLU A N   1 
ATOM   2172 C CA  . GLU A 1 267 ? 32.485  50.649  7.241   1   27.69  ? 267 GLU A CA  1 
ATOM   2173 C C   . GLU A 1 267 ? 32.808  49.624  6.158   1   26.1   ? 267 GLU A C   1 
ATOM   2174 O O   . GLU A 1 267 ? 32.563  49.898  4.993   1   26.19  ? 267 GLU A O   1 
ATOM   2175 C CB  . GLU A 1 267 ? 33.716  51.491  7.543   1   28.73  ? 267 GLU A CB  1 
ATOM   2176 C CG  . GLU A 1 267 ? 33.378  52.704  8.383   1   30.47  ? 267 GLU A CG  1 
ATOM   2177 C CD  . GLU A 1 267 ? 34.623  53.474  8.841   1   40.25  ? 267 GLU A CD  1 
ATOM   2178 O OE1 . GLU A 1 267 ? 34.553  54.694  8.889   1   42.85  ? 267 GLU A OE1 1 
ATOM   2179 O OE2 . GLU A 1 267 ? 35.628  52.855  9.186   1   44.21  ? 267 GLU A OE2 1 
ATOM   2180 N N   . GLU A 1 268 ? 33.331  48.457  6.557   1   24.99  ? 268 GLU A N   1 
ATOM   2181 C CA  . GLU A 1 268 ? 33.746  47.44   5.61    1   26.94  ? 268 GLU A CA  1 
ATOM   2182 C C   . GLU A 1 268 ? 32.593  46.912  4.737   1   26.91  ? 268 GLU A C   1 
ATOM   2183 O O   . GLU A 1 268 ? 32.841  46.561  3.586   1   25.94  ? 268 GLU A O   1 
ATOM   2184 C CB  . GLU A 1 268 ? 34.499  46.367  6.386   1   26.74  ? 268 GLU A CB  1 
ATOM   2185 C CG  . GLU A 1 268 ? 34.849  45.145  5.538   1   25.81  ? 268 GLU A CG  1 
ATOM   2186 C CD  . GLU A 1 268 ? 35.596  44.111  6.357   1   32.62  ? 268 GLU A CD  1 
ATOM   2187 O OE1 . GLU A 1 268 ? 36.733  43.75   6.015   1   32.63  ? 268 GLU A OE1 1 
ATOM   2188 O OE2 . GLU A 1 268 ? 34.965  43.654  7.34    1   34.68  ? 268 GLU A OE2 1 
ATOM   2189 N N   . PHE A 1 269 ? 31.366  46.756  5.278   1   25.24  ? 269 PHE A N   1 
ATOM   2190 C CA  . PHE A 1 269 ? 30.202  46.405  4.487   1   23.7   ? 269 PHE A CA  1 
ATOM   2191 C C   . PHE A 1 269 ? 30.046  47.356  3.306   1   25.49  ? 269 PHE A C   1 
ATOM   2192 O O   . PHE A 1 269 ? 29.808  46.907  2.21    1   21.46  ? 269 PHE A O   1 
ATOM   2193 C CB  . PHE A 1 269 ? 28.891  46.388  5.284   1   24.56  ? 269 PHE A CB  1 
ATOM   2194 C CG  . PHE A 1 269 ? 28.806  45.167  6.195   1   24.68  ? 269 PHE A CG  1 
ATOM   2195 C CD1 . PHE A 1 269 ? 28.269  43.971  5.746   1   26.32  ? 269 PHE A CD1 1 
ATOM   2196 C CD2 . PHE A 1 269 ? 29.239  45.236  7.51    1   24.25  ? 269 PHE A CD2 1 
ATOM   2197 C CE1 . PHE A 1 269 ? 28.186  42.868  6.608   1   27.41  ? 269 PHE A CE1 1 
ATOM   2198 C CE2 . PHE A 1 269 ? 29.164  44.136  8.347   1   24.39  ? 269 PHE A CE2 1 
ATOM   2199 C CZ  . PHE A 1 269 ? 28.64   42.959  7.912   1   25.33  ? 269 PHE A CZ  1 
ATOM   2200 N N   . PHE A 1 270 ? 30.16   48.66   3.55    1   23.26  ? 270 PHE A N   1 
ATOM   2201 C CA  . PHE A 1 270 ? 29.928  49.658  2.512   1   23.86  ? 270 PHE A CA  1 
ATOM   2202 C C   . PHE A 1 270 ? 31.078  49.648  1.504   1   22.87  ? 270 PHE A C   1 
ATOM   2203 O O   . PHE A 1 270 ? 30.805  49.685  0.307   1   23.4   ? 270 PHE A O   1 
ATOM   2204 C CB  . PHE A 1 270 ? 29.774  51.061  3.076   1   25.09  ? 270 PHE A CB  1 
ATOM   2205 C CG  . PHE A 1 270 ? 28.507  51.151  3.898   1   26.01  ? 270 PHE A CG  1 
ATOM   2206 C CD1 . PHE A 1 270 ? 27.26   51.213  3.273   1   22.74  ? 270 PHE A CD1 1 
ATOM   2207 C CD2 . PHE A 1 270 ? 28.556  51.084  5.293   1   28.37  ? 270 PHE A CD2 1 
ATOM   2208 C CE1 . PHE A 1 270 ? 26.095  51.228  4.027   1   25.21  ? 270 PHE A CE1 1 
ATOM   2209 C CE2 . PHE A 1 270 ? 27.368  51.114  6.045   1   25.79  ? 270 PHE A CE2 1 
ATOM   2210 C CZ  . PHE A 1 270 ? 26.163  51.192  5.418   1   23.66  ? 270 PHE A CZ  1 
ATOM   2211 N N   . LYS A 1 271 ? 32.316  49.545  1.968   1   24.43  ? 271 LYS A N   1 
ATOM   2212 C CA  . LYS A 1 271 ? 33.49   49.437  1.082   1   27.06  ? 271 LYS A CA  1 
ATOM   2213 C C   . LYS A 1 271 ? 33.364  48.257  0.131   1   25.34  ? 271 LYS A C   1 
ATOM   2214 O O   . LYS A 1 271 ? 33.667  48.362  -1.059  1   22.35  ? 271 LYS A O   1 
ATOM   2215 C CB  . LYS A 1 271 ? 34.796  49.389  1.867   1   27.32  ? 271 LYS A CB  1 
ATOM   2216 C CG  . LYS A 1 271 ? 35.11   50.647  2.654   1   34.02  ? 271 LYS A CG  1 
ATOM   2217 C CD  . LYS A 1 271 ? 36.406  50.423  3.433   1   37.73  ? 271 LYS A CD  1 
ATOM   2218 C CE  . LYS A 1 271 ? 37.341  51.52   3.323   1   54.14  ? 271 LYS A CE  1 
ATOM   2219 N NZ  . LYS A 1 271 ? 36.882  52.69   4.087   1   59.02  ? 271 LYS A NZ  1 
ATOM   2220 N N   . ARG A 1 272 ? 32.931  47.122  0.682   1   23.59  ? 272 ARG A N   1 
ATOM   2221 C CA  . ARG A 1 272 ? 32.753  45.914  -0.101  1   23.02  ? 272 ARG A CA  1 
ATOM   2222 C C   . ARG A 1 272 ? 31.667  46.102  -1.17   1   22.17  ? 272 ARG A C   1 
ATOM   2223 O O   . ARG A 1 272 ? 31.888  45.759  -2.32   1   23.07  ? 272 ARG A O   1 
ATOM   2224 C CB  . ARG A 1 272 ? 32.407  44.766  0.849   1   24.24  ? 272 ARG A CB  1 
ATOM   2225 C CG  . ARG A 1 272 ? 33.645  44.236  1.511   1   25.8   ? 272 ARG A CG  1 
ATOM   2226 C CD  . ARG A 1 272 ? 33.423  43.134  2.488   1   25.31  ? 272 ARG A CD  1 
ATOM   2227 N NE  . ARG A 1 272 ? 34.717  42.591  2.932   1   24.81  ? 272 ARG A NE  1 
ATOM   2228 C CZ  . ARG A 1 272 ? 34.825  41.599  3.816   1   27.45  ? 272 ARG A CZ  1 
ATOM   2229 N NH1 . ARG A 1 272 ? 33.85   41.309  4.652   1   26.95  ? 272 ARG A NH1 1 
ATOM   2230 N NH2 . ARG A 1 272 ? 35.931  40.955  3.929   1   26.85  ? 272 ARG A NH2 1 
ATOM   2231 N N   . ASN A 1 273 ? 30.513  46.671  -0.791  1   22.22  ? 273 ASN A N   1 
ATOM   2232 C CA  . ASN A 1 273 ? 29.43   46.822  -1.752  1   23.25  ? 273 ASN A CA  1 
ATOM   2233 C C   . ASN A 1 273 ? 29.704  47.959  -2.744  1   24.35  ? 273 ASN A C   1 
ATOM   2234 O O   . ASN A 1 273 ? 29.315  47.821  -3.91   1   21.79  ? 273 ASN A O   1 
ATOM   2235 C CB  . ASN A 1 273 ? 28.063  46.92   -1.108  1   21.81  ? 273 ASN A CB  1 
ATOM   2236 C CG  . ASN A 1 273 ? 27.588  45.572  -0.613  1   24.08  ? 273 ASN A CG  1 
ATOM   2237 O OD1 . ASN A 1 273 ? 28.171  44.514  -0.915  1   23.81  ? 273 ASN A OD1 1 
ATOM   2238 N ND2 . ASN A 1 273 ? 26.575  45.595  0.22    1   21.11  ? 273 ASN A ND2 1 
ATOM   2239 N N   . LEU A 1 274 ? 30.38   49.03   -2.296  1   21.04  ? 274 LEU A N   1 
ATOM   2240 C CA  . LEU A 1 274 ? 30.83   50.075  -3.202  1   24.49  ? 274 LEU A CA  1 
ATOM   2241 C C   . LEU A 1 274 ? 31.843  49.53   -4.219  1   23.75  ? 274 LEU A C   1 
ATOM   2242 O O   . LEU A 1 274 ? 31.78   49.931  -5.37   1   25.63  ? 274 LEU A O   1 
ATOM   2243 C CB  . LEU A 1 274 ? 31.375  51.261  -2.406  1   23.66  ? 274 LEU A CB  1 
ATOM   2244 C CG  . LEU A 1 274 ? 30.252  52.137  -1.806  1   25.75  ? 274 LEU A CG  1 
ATOM   2245 C CD1 . LEU A 1 274 ? 30.83   52.95   -0.67   1   25.92  ? 274 LEU A CD1 1 
ATOM   2246 C CD2 . LEU A 1 274 ? 29.646  53.043  -2.864  1   25.27  ? 274 LEU A CD2 1 
ATOM   2247 N N   . SER A 1 275 ? 32.737  48.617  -3.814  1   21.61  ? 275 SER A N   1 
ATOM   2248 C CA  . SER A 1 275 ? 33.641  47.961  -4.738  1   23.3   ? 275 SER A CA  1 
ATOM   2249 C C   . SER A 1 275 ? 32.853  47.204  -5.797  1   22.27  ? 275 SER A C   1 
ATOM   2250 O O   . SER A 1 275 ? 33.181  47.301  -6.993  1   24.19  ? 275 SER A O   1 
ATOM   2251 C CB  . SER A 1 275 ? 34.616  46.947  -4.093  1   24.22  ? 275 SER A CB  1 
ATOM   2252 O OG  . SER A 1 275 ? 35.375  47.553  -3.053  1   33.77  ? 275 SER A OG  1 
ATOM   2253 N N   . PHE A 1 276 ? 31.9    46.398  -5.339  1   21.57  ? 276 PHE A N   1 
ATOM   2254 C CA  . PHE A 1 276 ? 31.085  45.614  -6.261  1   22.27  ? 276 PHE A CA  1 
ATOM   2255 C C   . PHE A 1 276 ? 30.31   46.53   -7.207  1   23.99  ? 276 PHE A C   1 
ATOM   2256 O O   . PHE A 1 276 ? 30.346  46.327  -8.411  1   22.51  ? 276 PHE A O   1 
ATOM   2257 C CB  . PHE A 1 276 ? 30.17   44.626  -5.551  1   23.67  ? 276 PHE A CB  1 
ATOM   2258 C CG  . PHE A 1 276 ? 29.48   43.745  -6.576  1   26.82  ? 276 PHE A CG  1 
ATOM   2259 C CD1 . PHE A 1 276 ? 28.265  44.139  -7.13   1   30.18  ? 276 PHE A CD1 1 
ATOM   2260 C CD2 . PHE A 1 276 ? 30.158  42.673  -7.161  1   31.96  ? 276 PHE A CD2 1 
ATOM   2261 C CE1 . PHE A 1 276 ? 27.69   43.382  -8.145  1   28.33  ? 276 PHE A CE1 1 
ATOM   2262 C CE2 . PHE A 1 276 ? 29.588  41.946  -8.202  1   33.18  ? 276 PHE A CE2 1 
ATOM   2263 C CZ  . PHE A 1 276 ? 28.342  42.296  -8.656  1   28.53  ? 276 PHE A CZ  1 
ATOM   2264 N N   . LEU A 1 277 ? 29.648  47.542  -6.66   1   23.54  ? 277 LEU A N   1 
ATOM   2265 C CA  . LEU A 1 277 ? 28.867  48.458  -7.474  1   24.72  ? 277 LEU A CA  1 
ATOM   2266 C C   . LEU A 1 277 ? 29.705  49.079  -8.595  1   23.46  ? 277 LEU A C   1 
ATOM   2267 O O   . LEU A 1 277 ? 29.309  49.055  -9.778  1   24.46  ? 277 LEU A O   1 
ATOM   2268 C CB  . LEU A 1 277 ? 28.239  49.526  -6.583  1   23.46  ? 277 LEU A CB  1 
ATOM   2269 C CG  . LEU A 1 277 ? 27.471  50.626  -7.341  1   26.15  ? 277 LEU A CG  1 
ATOM   2270 C CD1 . LEU A 1 277 ? 26.159  50.125  -7.874  1   26.25  ? 277 LEU A CD1 1 
ATOM   2271 C CD2 . LEU A 1 277 ? 27.256  51.785  -6.432  1   29.46  ? 277 LEU A CD2 1 
ATOM   2272 N N   . ASN A 1 278 ? 30.853  49.655  -8.235  1   23.81  ? 278 ASN A N   1 
ATOM   2273 C CA  . ASN A 1 278 ? 31.725  50.333  -9.188  1   24.21  ? 278 ASN A CA  1 
ATOM   2274 C C   . ASN A 1 278 ? 32.296  49.343  -10.209 1   26.56  ? 278 ASN A C   1 
ATOM   2275 O O   . ASN A 1 278 ? 32.352  49.657  -11.41  1   27.75  ? 278 ASN A O   1 
ATOM   2276 C CB  . ASN A 1 278 ? 32.751  51.213  -8.479  1   25.73  ? 278 ASN A CB  1 
ATOM   2277 C CG  . ASN A 1 278 ? 32.146  52.471  -7.9    1   28.51  ? 278 ASN A CG  1 
ATOM   2278 O OD1 . ASN A 1 278 ? 31.724  53.363  -8.655  1   27.85  ? 278 ASN A OD1 1 
ATOM   2279 N ND2 . ASN A 1 278 ? 32.098  52.59   -6.585  1   29.34  ? 278 ASN A ND2 1 
ATOM   2280 N N   . ASN A 1 279 ? 32.603  48.109  -9.801  1   25.16  ? 279 ASN A N   1 
ATOM   2281 C CA  . ASN A 1 279 ? 33.038  47.105  -10.749 1   26.5   ? 279 ASN A CA  1 
ATOM   2282 C C   . ASN A 1 279 ? 31.912  46.754  -11.719 1   27.93  ? 279 ASN A C   1 
ATOM   2283 O O   . ASN A 1 279 ? 32.139  46.698  -12.93  1   26.73  ? 279 ASN A O   1 
ATOM   2284 C CB  . ASN A 1 279 ? 33.598  45.858  -10.055 1   25.23  ? 279 ASN A CB  1 
ATOM   2285 C CG  . ASN A 1 279 ? 35.001  46.071  -9.502  1   28.06  ? 279 ASN A CG  1 
ATOM   2286 O OD1 . ASN A 1 279 ? 35.78   46.874  -10.016 1   26.85  ? 279 ASN A OD1 1 
ATOM   2287 N ND2 . ASN A 1 279 ? 35.38   45.315  -8.48   1   26.08  ? 279 ASN A ND2 1 
ATOM   2288 N N   . PHE A 1 280 ? 30.72   46.492  -11.191 1   26.78  ? 280 PHE A N   1 
ATOM   2289 C CA  . PHE A 1 280 ? 29.595  46.05   -11.993 1   25.89  ? 280 PHE A CA  1 
ATOM   2290 C C   . PHE A 1 280 ? 29.227  47.118  -13.043 1   28.54  ? 280 PHE A C   1 
ATOM   2291 O O   . PHE A 1 280 ? 28.911  46.748  -14.162 1   28.07  ? 280 PHE A O   1 
ATOM   2292 C CB  . PHE A 1 280 ? 28.417  45.628  -11.127 1   27.76  ? 280 PHE A CB  1 
ATOM   2293 C CG  . PHE A 1 280 ? 27.303  44.994  -11.951 1   27.7   ? 280 PHE A CG  1 
ATOM   2294 C CD1 . PHE A 1 280 ? 27.395  43.681  -12.374 1   29.63  ? 280 PHE A CD1 1 
ATOM   2295 C CD2 . PHE A 1 280 ? 26.219  45.752  -12.378 1   31.47  ? 280 PHE A CD2 1 
ATOM   2296 C CE1 . PHE A 1 280 ? 26.404  43.123  -13.176 1   33.1   ? 280 PHE A CE1 1 
ATOM   2297 C CE2 . PHE A 1 280 ? 25.231  45.187  -13.188 1   31.39  ? 280 PHE A CE2 1 
ATOM   2298 C CZ  . PHE A 1 280 ? 25.322  43.877  -13.565 1   31.16  ? 280 PHE A CZ  1 
ATOM   2299 N N   . TRP A 1 281 ? 29.361  48.401  -12.722 1   25.42  ? 281 TRP A N   1 
ATOM   2300 C CA  . TRP A 1 281 ? 29.007  49.462  -13.653 1   29.77  ? 281 TRP A CA  1 
ATOM   2301 C C   . TRP A 1 281 ? 30.214  49.994  -14.429 1   29.18  ? 281 TRP A C   1 
ATOM   2302 O O   . TRP A 1 281 ? 30.079  50.967  -15.168 1   31.96  ? 281 TRP A O   1 
ATOM   2303 C CB  . TRP A 1 281 ? 28.289  50.597  -12.912 1   27.37  ? 281 TRP A CB  1 
ATOM   2304 C CG  . TRP A 1 281 ? 26.907  50.214  -12.489 1   28.13  ? 281 TRP A CG  1 
ATOM   2305 C CD1 . TRP A 1 281 ? 26.554  49.57   -11.35  1   28.96  ? 281 TRP A CD1 1 
ATOM   2306 C CD2 . TRP A 1 281 ? 25.69   50.44   -13.217 1   28.21  ? 281 TRP A CD2 1 
ATOM   2307 N NE1 . TRP A 1 281 ? 25.219  49.362  -11.326 1   29.6   ? 281 TRP A NE1 1 
ATOM   2308 C CE2 . TRP A 1 281 ? 24.658  49.878  -12.458 1   28.52  ? 281 TRP A CE2 1 
ATOM   2309 C CE3 . TRP A 1 281 ? 25.386  51.092  -14.421 1   33.63  ? 281 TRP A CE3 1 
ATOM   2310 C CZ2 . TRP A 1 281 ? 23.314  49.924  -12.857 1   33.06  ? 281 TRP A CZ2 1 
ATOM   2311 C CZ3 . TRP A 1 281 ? 24.067  51.122  -14.827 1   39.74  ? 281 TRP A CZ3 1 
ATOM   2312 C CH2 . TRP A 1 281 ? 23.048  50.535  -14.066 1   34.82  ? 281 TRP A CH2 1 
ATOM   2313 N N   . ASN A 1 282 ? 31.394  49.391  -14.249 1   29.27  ? 282 ASN A N   1 
ATOM   2314 C CA  . ASN A 1 282 ? 32.636  49.744  -14.92  1   31.61  ? 282 ASN A CA  1 
ATOM   2315 C C   . ASN A 1 282 ? 33.015  51.201  -14.67  1   35.84  ? 282 ASN A C   1 
ATOM   2316 O O   . ASN A 1 282 ? 33.248  51.952  -15.596 1   32.38  ? 282 ASN A O   1 
ATOM   2317 C CB  . ASN A 1 282 ? 32.566  49.353  -16.393 1   36.73  ? 282 ASN A CB  1 
ATOM   2318 C CG  . ASN A 1 282 ? 33.929  49.365  -17.04  1   41.55  ? 282 ASN A CG  1 
ATOM   2319 O OD1 . ASN A 1 282 ? 34.964  49.486  -16.368 1   38.48  ? 282 ASN A OD1 1 
ATOM   2320 N ND2 . ASN A 1 282 ? 33.933  49.303  -18.363 1   44.7   ? 282 ASN A ND2 1 
ATOM   2321 N N   . LYS A 1 283 ? 33.083  51.583  -13.405 1   33.74  ? 283 LYS A N   1 
ATOM   2322 C CA  . LYS A 1 283 ? 33.447  52.921  -13.004 1   36.66  ? 283 LYS A CA  1 
ATOM   2323 C C   . LYS A 1 283 ? 34.739  52.839  -12.21  1   40.95  ? 283 LYS A C   1 
ATOM   2324 O O   . LYS A 1 283 ? 35.11   51.77   -11.721 1   36.42  ? 283 LYS A O   1 
ATOM   2325 C CB  . LYS A 1 283 ? 32.401  53.538  -12.078 1   40.52  ? 283 LYS A CB  1 
ATOM   2326 C CG  . LYS A 1 283 ? 30.967  53.671  -12.581 1   41.46  ? 283 LYS A CG  1 
ATOM   2327 C CD  . LYS A 1 283 ? 30.717  54.384  -13.9   1   48.56  ? 283 LYS A CD  1 
ATOM   2328 C CE  . LYS A 1 283 ? 29.253  54.702  -14.079 1   57.23  ? 283 LYS A CE  1 
ATOM   2329 N NZ  . LYS A 1 283 ? 28.87   56.03   -13.577 1   65.26  ? 283 LYS A NZ  1 
ATOM   2330 N N   . GLU A 1 284 ? 35.344  54.008  -12.009 1   41.91  ? 284 GLU A N   1 
ATOM   2331 C CA  . GLU A 1 284 ? 36.551  54.142  -11.212 1   48.1   ? 284 GLU A CA  1 
ATOM   2332 C C   . GLU A 1 284 ? 36.2    53.755  -9.771  1   39.42  ? 284 GLU A C   1 
ATOM   2333 O O   . GLU A 1 284 ? 35.133  54.094  -9.226  1   34.85  ? 284 GLU A O   1 
ATOM   2334 C CB  . GLU A 1 284 ? 37.196  55.509  -11.472 1   54.27  ? 284 GLU A CB  1 
ATOM   2335 C CG  . GLU A 1 284 ? 38.373  55.861  -10.555 1   72.32  ? 284 GLU A CG  1 
ATOM   2336 C CD  . GLU A 1 284 ? 38      56.423  -9.18   1   81.34  ? 284 GLU A CD  1 
ATOM   2337 O OE1 . GLU A 1 284 ? 36.8    56.765  -8.947  1   81.21  ? 284 GLU A OE1 1 
ATOM   2338 O OE2 . GLU A 1 284 ? 38.923  56.5    -8.322  1   69.28  ? 284 GLU A OE2 1 
ATOM   2339 N N   . ASN A 1 285 ? 37.098  52.943  -9.19   1   34.45  ? 285 ASN A N   1 
ATOM   2340 C CA  . ASN A 1 285 ? 36.788  52.179  -7.985  1   30.6   ? 285 ASN A CA  1 
ATOM   2341 C C   . ASN A 1 285 ? 37.88   52.392  -6.935  1   30.3   ? 285 ASN A C   1 
ATOM   2342 O O   . ASN A 1 285 ? 38.847  51.644  -6.919  1   29.48  ? 285 ASN A O   1 
ATOM   2343 C CB  . ASN A 1 285 ? 36.688  50.71   -8.361  1   29.08  ? 285 ASN A CB  1 
ATOM   2344 C CG  . ASN A 1 285 ? 36.048  49.875  -7.275  1   28.11  ? 285 ASN A CG  1 
ATOM   2345 O OD1 . ASN A 1 285 ? 35.801  50.335  -6.14   1   25.38  ? 285 ASN A OD1 1 
ATOM   2346 N ND2 . ASN A 1 285 ? 35.615  48.71   -7.686  1   28.63  ? 285 ASN A ND2 1 
ATOM   2347 N N   . GLU A 1 286 ? 37.644  53.292  -5.973  1   28.35  ? 286 GLU A N   1 
ATOM   2348 C CA  . GLU A 1 286 ? 38.615  53.557  -4.931  1   31.48  ? 286 GLU A CA  1 
ATOM   2349 C C   . GLU A 1 286 ? 38.448  52.6    -3.738  1   26.31  ? 286 GLU A C   1 
ATOM   2350 O O   . GLU A 1 286 ? 39.151  52.798  -2.754  1   26.97  ? 286 GLU A O   1 
ATOM   2351 C CB  . GLU A 1 286 ? 38.496  55.02   -4.491  1   33.11  ? 286 GLU A CB  1 
ATOM   2352 C CG  . GLU A 1 286 ? 37.279  55.292  -3.622  1   38.44  ? 286 GLU A CG  1 
ATOM   2353 C CD  . GLU A 1 286 ? 37.182  56.747  -3.189  1   49.39  ? 286 GLU A CD  1 
ATOM   2354 O OE1 . GLU A 1 286 ? 37.374  57.045  -2.002  1   47.47  ? 286 GLU A OE1 1 
ATOM   2355 O OE2 . GLU A 1 286 ? 36.873  57.561  -4.066  1   56.75  ? 286 GLU A OE2 1 
ATOM   2356 N N   . TRP A 1 287 ? 37.611  51.552  -3.834  1   26.11  ? 287 TRP A N   1 
ATOM   2357 C CA  . TRP A 1 287 ? 37.161  50.854  -2.635  1   26.86  ? 287 TRP A CA  1 
ATOM   2358 C C   . TRP A 1 287 ? 37.808  49.485  -2.414  1   26.43  ? 287 TRP A C   1 
ATOM   2359 O O   . TRP A 1 287 ? 37.484  48.777  -1.453  1   27.45  ? 287 TRP A O   1 
ATOM   2360 C CB  . TRP A 1 287 ? 35.647  50.729  -2.702  1   25.02  ? 287 TRP A CB  1 
ATOM   2361 C CG  . TRP A 1 287 ? 34.955  52.049  -2.822  1   27.12  ? 287 TRP A CG  1 
ATOM   2362 C CD1 . TRP A 1 287 ? 34.453  52.613  -3.968  1   30.42  ? 287 TRP A CD1 1 
ATOM   2363 C CD2 . TRP A 1 287 ? 34.743  53.003  -1.771  1   27.67  ? 287 TRP A CD2 1 
ATOM   2364 N NE1 . TRP A 1 287 ? 33.923  53.842  -3.693  1   31.91  ? 287 TRP A NE1 1 
ATOM   2365 C CE2 . TRP A 1 287 ? 34.09   54.115  -2.357  1   28     ? 287 TRP A CE2 1 
ATOM   2366 C CE3 . TRP A 1 287 ? 35.052  53.042  -0.414  1   28.18  ? 287 TRP A CE3 1 
ATOM   2367 C CZ2 . TRP A 1 287 ? 33.729  55.23   -1.607  1   32.05  ? 287 TRP A CZ2 1 
ATOM   2368 C CZ3 . TRP A 1 287 ? 34.678  54.144  0.33    1   31.45  ? 287 TRP A CZ3 1 
ATOM   2369 C CH2 . TRP A 1 287 ? 34.046  55.227  -0.259  1   29.84  ? 287 TRP A CH2 1 
ATOM   2370 N N   . ILE A 1 288 ? 38.617  49.055  -3.359  1   24.24  ? 288 ILE A N   1 
ATOM   2371 C CA  . ILE A 1 288 ? 39.064  47.664  -3.452  1   24.54  ? 288 ILE A CA  1 
ATOM   2372 C C   . ILE A 1 288 ? 40.03   47.371  -2.303  1   25.06  ? 288 ILE A C   1 
ATOM   2373 O O   . ILE A 1 288 ? 40.892  48.18   -2.019  1   24.38  ? 288 ILE A O   1 
ATOM   2374 C CB  . ILE A 1 288 ? 39.69   47.387  -4.84   1   25.54  ? 288 ILE A CB  1 
ATOM   2375 C CG1 . ILE A 1 288 ? 38.565  47.409  -5.845  1   30.12  ? 288 ILE A CG1 1 
ATOM   2376 C CG2 . ILE A 1 288 ? 40.423  46.036  -4.84   1   25.11  ? 288 ILE A CG2 1 
ATOM   2377 C CD1 . ILE A 1 288 ? 38.991  47.365  -7.283  1   32.72  ? 288 ILE A CD1 1 
ATOM   2378 N N   . ASN A 1 289 ? 39.933  46.173  -1.72   1   24.18  ? 289 ASN A N   1 
ATOM   2379 C CA  . ASN A 1 289 ? 40.88   45.721  -0.699  1   25.62  ? 289 ASN A CA  1 
ATOM   2380 C C   . ASN A 1 289 ? 41.825  44.689  -1.305  1   25.97  ? 289 ASN A C   1 
ATOM   2381 O O   . ASN A 1 289 ? 41.469  43.499  -1.383  1   27.39  ? 289 ASN A O   1 
ATOM   2382 C CB  . ASN A 1 289 ? 40.125  45.257  0.542   1   27.41  ? 289 ASN A CB  1 
ATOM   2383 C CG  . ASN A 1 289 ? 41.083  45.021  1.687   1   28.89  ? 289 ASN A CG  1 
ATOM   2384 O OD1 . ASN A 1 289 ? 42.271  44.807  1.483   1   28.08  ? 289 ASN A OD1 1 
ATOM   2385 N ND2 . ASN A 1 289 ? 40.567  44.99   2.892   1   32.56  ? 289 ASN A ND2 1 
ATOM   2386 N N   . TYR A 1 290 ? 43.031  45.155  -1.718  1   24.62  ? 290 TYR A N   1 
ATOM   2387 C CA  . TYR A 1 290 ? 44.017  44.323  -2.402  1   27.34  ? 290 TYR A CA  1 
ATOM   2388 C C   . TYR A 1 290 ? 44.777  43.426  -1.429  1   30.76  ? 290 TYR A C   1 
ATOM   2389 O O   . TYR A 1 290 ? 45.356  42.449  -1.87   1   33.42  ? 290 TYR A O   1 
ATOM   2390 C CB  . TYR A 1 290 ? 45.052  45.189  -3.138  1   29.5   ? 290 TYR A CB  1 
ATOM   2391 C CG  . TYR A 1 290 ? 44.405  46.035  -4.228  1   29.62  ? 290 TYR A CG  1 
ATOM   2392 C CD1 . TYR A 1 290 ? 44.224  45.526  -5.518  1   28.72  ? 290 TYR A CD1 1 
ATOM   2393 C CD2 . TYR A 1 290 ? 43.993  47.338  -3.989  1   30.87  ? 290 TYR A CD2 1 
ATOM   2394 C CE1 . TYR A 1 290 ? 43.624  46.272  -6.522  1   30.16  ? 290 TYR A CE1 1 
ATOM   2395 C CE2 . TYR A 1 290 ? 43.423  48.116  -4.994  1   29.72  ? 290 TYR A CE2 1 
ATOM   2396 C CZ  . TYR A 1 290 ? 43.269  47.593  -6.27   1   30.77  ? 290 TYR A CZ  1 
ATOM   2397 O OH  . TYR A 1 290 ? 42.633  48.321  -7.215  1   28.45  ? 290 TYR A OH  1 
ATOM   2398 N N   . ASP A 1 291 ? 44.794  43.762  -0.129  1   33.91  ? 291 ASP A N   1 
ATOM   2399 C CA  . ASP A 1 291 ? 45.519  42.984  0.871   1   38.56  ? 291 ASP A CA  1 
ATOM   2400 C C   . ASP A 1 291 ? 44.738  41.794  1.444   1   36.68  ? 291 ASP A C   1 
ATOM   2401 O O   . ASP A 1 291 ? 45.374  40.844  1.903   1   40.13  ? 291 ASP A O   1 
ATOM   2402 C CB  . ASP A 1 291 ? 45.925  43.849  2.039   1   39.24  ? 291 ASP A CB  1 
ATOM   2403 C CG  . ASP A 1 291 ? 46.829  45.011  1.669   1   46.58  ? 291 ASP A CG  1 
ATOM   2404 O OD1 . ASP A 1 291 ? 47.856  44.761  1.013   1   46     ? 291 ASP A OD1 1 
ATOM   2405 O OD2 . ASP A 1 291 ? 46.456  46.151  2.02    1   60.09  ? 291 ASP A OD2 1 
ATOM   2406 N N   . SER A 1 292 ? 43.42   41.885  1.468   1   33.7   ? 292 SER A N   1 
ATOM   2407 C CA  . SER A 1 292 ? 42.54   40.938  2.146   1   34.36  ? 292 SER A CA  1 
ATOM   2408 C C   . SER A 1 292 ? 42.63   39.543  1.526   1   35.95  ? 292 SER A C   1 
ATOM   2409 O O   . SER A 1 292 ? 42.692  39.413  0.309   1   30.87  ? 292 SER A O   1 
ATOM   2410 C CB  . SER A 1 292 ? 41.142  41.429  2.071   1   31.41  ? 292 SER A CB  1 
ATOM   2411 O OG  . SER A 1 292 ? 40.182  40.524  2.608   1   30.4   ? 292 SER A OG  1 
ATOM   2412 N N   . ASP A 1 293 ? 42.559  38.512  2.369   1   32.85  ? 293 ASP A N   1 
ATOM   2413 C CA  . ASP A 1 293 ? 42.407  37.148  1.89    1   35.11  ? 293 ASP A CA  1 
ATOM   2414 C C   . ASP A 1 293 ? 40.973  36.657  2.038   1   30.19  ? 293 ASP A C   1 
ATOM   2415 O O   . ASP A 1 293 ? 40.748  35.45   1.969   1   34.33  ? 293 ASP A O   1 
ATOM   2416 C CB  . ASP A 1 293 ? 43.457  36.272  2.552   1   39.4   ? 293 ASP A CB  1 
ATOM   2417 C CG  . ASP A 1 293 ? 43.289  36.06   4.055   1   49.08  ? 293 ASP A CG  1 
ATOM   2418 O OD1 . ASP A 1 293 ? 42.34   36.597  4.623   1   45.07  ? 293 ASP A OD1 1 
ATOM   2419 O OD2 . ASP A 1 293 ? 44.101  35.329  4.666   1   64.65  ? 293 ASP A OD2 1 
ATOM   2420 N N   . ALA A 1 294 ? 39.997  37.548  2.256   1   27.98  ? 294 ALA A N   1 
ATOM   2421 C CA  . ALA A 1 294 ? 38.601  37.163  2.199   1   28.72  ? 294 ALA A CA  1 
ATOM   2422 C C   . ALA A 1 294 ? 38.202  36.955  0.721   1   28.86  ? 294 ALA A C   1 
ATOM   2423 O O   . ALA A 1 294 ? 38.57   37.742  -0.155  1   24.49  ? 294 ALA A O   1 
ATOM   2424 C CB  . ALA A 1 294 ? 37.709  38.166  2.902   1   26.77  ? 294 ALA A CB  1 
ATOM   2425 N N   . VAL A 1 295 ? 37.509  35.853  0.431   1   27.18  ? 295 VAL A N   1 
ATOM   2426 C CA  . VAL A 1 295 ? 37.064  35.572  -0.943  1   27.26  ? 295 VAL A CA  1 
ATOM   2427 C C   . VAL A 1 295 ? 36.31   36.742  -1.576  1   25.08  ? 295 VAL A C   1 
ATOM   2428 O O   . VAL A 1 295 ? 36.603  37.084  -2.73   1   22.8   ? 295 VAL A O   1 
ATOM   2429 C CB  . VAL A 1 295 ? 36.201  34.303  -1.002  1   30.03  ? 295 VAL A CB  1 
ATOM   2430 C CG1 . VAL A 1 295 ? 35.537  34.157  -2.379  1   30.29  ? 295 VAL A CG1 1 
ATOM   2431 C CG2 . VAL A 1 295 ? 37.061  33.097  -0.654  1   28.87  ? 295 VAL A CG2 1 
ATOM   2432 N N   . THR A 1 296 ? 35.409  37.389  -0.831  1   22.86  ? 296 THR A N   1 
ATOM   2433 C CA  . THR A 1 296 ? 34.633  38.477  -1.433  1   23.52  ? 296 THR A CA  1 
ATOM   2434 C C   . THR A 1 296 ? 35.531  39.639  -1.884  1   25.4   ? 296 THR A C   1 
ATOM   2435 O O   . THR A 1 296 ? 35.248  40.27   -2.891  1   23.98  ? 296 THR A O   1 
ATOM   2436 C CB  . THR A 1 296 ? 33.524  38.964  -0.515  1   24.1   ? 296 THR A CB  1 
ATOM   2437 O OG1 . THR A 1 296 ? 32.668  39.809  -1.26   1   25.51  ? 296 THR A OG1 1 
ATOM   2438 C CG2 . THR A 1 296 ? 34.004  39.723  0.704   1   25.01  ? 296 THR A CG2 1 
ATOM   2439 N N   . ASP A 1 297 ? 36.603  39.925  -1.13   1   23.32  ? 297 ASP A N   1 
ATOM   2440 C CA  . ASP A 1 297 ? 37.519  40.987  -1.457  1   24.76  ? 297 ASP A CA  1 
ATOM   2441 C C   . ASP A 1 297 ? 38.364  40.621  -2.672  1   23.45  ? 297 ASP A C   1 
ATOM   2442 O O   . ASP A 1 297 ? 38.64   41.462  -3.534  1   23.77  ? 297 ASP A O   1 
ATOM   2443 C CB  . ASP A 1 297 ? 38.336  41.363  -0.238  1   24.7   ? 297 ASP A CB  1 
ATOM   2444 C CG  . ASP A 1 297 ? 37.511  41.917  0.931   1   24.73  ? 297 ASP A CG  1 
ATOM   2445 O OD1 . ASP A 1 297 ? 36.51   42.615  0.676   1   23.75  ? 297 ASP A OD1 1 
ATOM   2446 O OD2 . ASP A 1 297 ? 37.932  41.724  2.095   1   24.65  ? 297 ASP A OD2 1 
ATOM   2447 N N   . MET A 1 298 ? 38.791  39.374  -2.721  1   24.1   ? 298 MET A N   1 
ATOM   2448 C CA  . MET A 1 298 ? 39.651  38.884  -3.801  1   24.19  ? 298 MET A CA  1 
ATOM   2449 C C   . MET A 1 298 ? 38.873  38.887  -5.128  1   23.79  ? 298 MET A C   1 
ATOM   2450 O O   . MET A 1 298 ? 39.467  39.176  -6.188  1   26.45  ? 298 MET A O   1 
ATOM   2451 C CB  . MET A 1 298 ? 40.2    37.498  -3.43   1   23.36  ? 298 MET A CB  1 
ATOM   2452 C CG  . MET A 1 298 ? 41.073  37.535  -2.192  1   28.29  ? 298 MET A CG  1 
ATOM   2453 S SD  . MET A 1 298 ? 41.454  35.91   -1.502  1   33.27  ? 298 MET A SD  1 
ATOM   2454 C CE  . MET A 1 298 ? 42.577  35.216  -2.71   1   34.12  ? 298 MET A CE  1 
ATOM   2455 N N   . GLN A 1 299 ? 37.577  38.613  -5.039  1   25.87  ? 299 GLN A N   1 
ATOM   2456 C CA  . GLN A 1 299 ? 36.638  38.723  -6.153  1   25.8   ? 299 GLN A CA  1 
ATOM   2457 C C   . GLN A 1 299 ? 36.628  40.114  -6.776  1   27.52  ? 299 GLN A C   1 
ATOM   2458 O O   . GLN A 1 299 ? 36.638  40.214  -7.996  1   23.43  ? 299 GLN A O   1 
ATOM   2459 C CB  . GLN A 1 299 ? 35.229  38.327  -5.786  1   24.14  ? 299 GLN A CB  1 
ATOM   2460 C CG  . GLN A 1 299 ? 35.048  36.843  -5.551  1   24.85  ? 299 GLN A CG  1 
ATOM   2461 C CD  . GLN A 1 299 ? 33.645  36.458  -5.104  1   24.28  ? 299 GLN A CD  1 
ATOM   2462 O OE1 . GLN A 1 299 ? 32.816  37.277  -4.715  1   27.5   ? 299 GLN A OE1 1 
ATOM   2463 N NE2 . GLN A 1 299 ? 33.331  35.175  -5.192  1   26.24  ? 299 GLN A NE2 1 
ATOM   2464 N N   . GLU A 1 300 ? 36.698  41.177  -5.965  1   25.2   ? 300 GLU A N   1 
ATOM   2465 C CA  . GLU A 1 300 ? 36.67   42.524  -6.509  1   25.56  ? 300 GLU A CA  1 
ATOM   2466 C C   . GLU A 1 300 ? 37.955  42.92   -7.207  1   26.87  ? 300 GLU A C   1 
ATOM   2467 O O   . GLU A 1 300 ? 37.878  43.676  -8.198  1   26.11  ? 300 GLU A O   1 
ATOM   2468 C CB  . GLU A 1 300 ? 36.269  43.551  -5.441  1   28.3   ? 300 GLU A CB  1 
ATOM   2469 C CG  . GLU A 1 300 ? 34.882  43.284  -4.888  1   31.34  ? 300 GLU A CG  1 
ATOM   2470 C CD  . GLU A 1 300 ? 33.8    42.96   -5.925  1   36.82  ? 300 GLU A CD  1 
ATOM   2471 O OE1 . GLU A 1 300 ? 33.702  43.623  -6.992  1   37.15  ? 300 GLU A OE1 1 
ATOM   2472 O OE2 . GLU A 1 300 ? 33.092  41.935  -5.714  1   40.1   ? 300 GLU A OE2 1 
ATOM   2473 N N   . VAL A 1 301 ? 39.12   42.414  -6.749  1   25.27  ? 301 VAL A N   1 
ATOM   2474 C CA  . VAL A 1 301 ? 40.385  42.592  -7.431  1   26.26  ? 301 VAL A CA  1 
ATOM   2475 C C   . VAL A 1 301 ? 40.261  41.996  -8.838  1   25.92  ? 301 VAL A C   1 
ATOM   2476 O O   . VAL A 1 301 ? 40.692  42.617  -9.813  1   25.68  ? 301 VAL A O   1 
ATOM   2477 C CB  . VAL A 1 301 ? 41.586  41.968  -6.675  1   27.6   ? 301 VAL A CB  1 
ATOM   2478 C CG1 . VAL A 1 301 ? 42.896  42.113  -7.415  1   28.3   ? 301 VAL A CG1 1 
ATOM   2479 C CG2 . VAL A 1 301 ? 41.693  42.548  -5.247  1   28.71  ? 301 VAL A CG2 1 
ATOM   2480 N N   . ILE A 1 302 ? 39.691  40.789  -8.908  1   24.83  ? 302 ILE A N   1 
ATOM   2481 C CA  . ILE A 1 302 ? 39.504  40.078  -10.177 1   25.82  ? 302 ILE A CA  1 
ATOM   2482 C C   . ILE A 1 302 ? 38.565  40.871  -11.102 1   22.89  ? 302 ILE A C   1 
ATOM   2483 O O   . ILE A 1 302 ? 38.881  41.075  -12.28  1   25.52  ? 302 ILE A O   1 
ATOM   2484 C CB  . ILE A 1 302 ? 39.015  38.644  -9.916  1   26.9   ? 302 ILE A CB  1 
ATOM   2485 C CG1 . ILE A 1 302 ? 40.115  37.766  -9.329  1   26.99  ? 302 ILE A CG1 1 
ATOM   2486 C CG2 . ILE A 1 302 ? 38.468  38.013  -11.199 1   28.24  ? 302 ILE A CG2 1 
ATOM   2487 C CD1 . ILE A 1 302 ? 39.596  36.561  -8.607  1   28.32  ? 302 ILE A CD1 1 
ATOM   2488 N N   . PHE A 1 303 ? 37.463  41.354  -10.58  1   23.44  ? 303 PHE A N   1 
ATOM   2489 C CA  . PHE A 1 303 ? 36.478  42.063  -11.384 1   25.2   ? 303 PHE A CA  1 
ATOM   2490 C C   . PHE A 1 303 ? 37.083  43.341  -11.948 1   27.71  ? 303 PHE A C   1 
ATOM   2491 O O   . PHE A 1 303 ? 36.877  43.645  -13.133 1   25.91  ? 303 PHE A O   1 
ATOM   2492 C CB  . PHE A 1 303 ? 35.201  42.345  -10.59  1   26.62  ? 303 PHE A CB  1 
ATOM   2493 C CG  . PHE A 1 303 ? 33.907  42.498  -11.38  1   28.32  ? 303 PHE A CG  1 
ATOM   2494 C CD1 . PHE A 1 303 ? 33.875  42.703  -12.765 1   28.96  ? 303 PHE A CD1 1 
ATOM   2495 C CD2 . PHE A 1 303 ? 32.687  42.488  -10.712 1   31.02  ? 303 PHE A CD2 1 
ATOM   2496 C CE1 . PHE A 1 303 ? 32.663  42.884  -13.431 1   27.87  ? 303 PHE A CE1 1 
ATOM   2497 C CE2 . PHE A 1 303 ? 31.491  42.653  -11.398 1   29     ? 303 PHE A CE2 1 
ATOM   2498 C CZ  . PHE A 1 303 ? 31.485  42.87   -12.754 1   26.4   ? 303 PHE A CZ  1 
ATOM   2499 N N   . GLU A 1 304 ? 37.889  44.06   -11.138 1   27.63  ? 304 GLU A N   1 
ATOM   2500 C CA  . GLU A 1 304 ? 38.625  45.204  -11.674 1   27.37  ? 304 GLU A CA  1 
ATOM   2501 C C   . GLU A 1 304 ? 39.519  44.832  -12.855 1   28.32  ? 304 GLU A C   1 
ATOM   2502 O O   . GLU A 1 304 ? 39.573  45.558  -13.848 1   27.87  ? 304 GLU A O   1 
ATOM   2503 C CB  . GLU A 1 304 ? 39.364  45.941  -10.557 1   27.13  ? 304 GLU A CB  1 
ATOM   2504 C CG  . GLU A 1 304 ? 40.183  47.121  -11.052 1   29.57  ? 304 GLU A CG  1 
ATOM   2505 C CD  . GLU A 1 304 ? 40.906  47.843  -9.903  1   35.12  ? 304 GLU A CD  1 
ATOM   2506 O OE1 . GLU A 1 304 ? 40.542  49.038  -9.604  1   35.49  ? 304 GLU A OE1 1 
ATOM   2507 O OE2 . GLU A 1 304 ? 41.848  47.228  -9.334  1   32.33  ? 304 GLU A OE2 1 
ATOM   2508 N N   . LEU A 1 305 ? 40.275  43.741  -12.739 1   26.38  ? 305 LEU A N   1 
ATOM   2509 C CA  . LEU A 1 305 ? 41.133  43.283  -13.815 1   30.08  ? 305 LEU A CA  1 
ATOM   2510 C C   . LEU A 1 305 ? 40.323  42.973  -15.1   1   29.79  ? 305 LEU A C   1 
ATOM   2511 O O   . LEU A 1 305 ? 40.767  43.281  -16.219 1   29.99  ? 305 LEU A O   1 
ATOM   2512 C CB  . LEU A 1 305 ? 41.964  42.083  -13.353 1   29.24  ? 305 LEU A CB  1 
ATOM   2513 C CG  . LEU A 1 305 ? 43.098  42.416  -12.378 1   32.38  ? 305 LEU A CG  1 
ATOM   2514 C CD1 . LEU A 1 305 ? 43.645  41.156  -11.709 1   30.22  ? 305 LEU A CD1 1 
ATOM   2515 C CD2 . LEU A 1 305 ? 44.191  43.194  -13.079 1   33.35  ? 305 LEU A CD2 1 
ATOM   2516 N N   . ILE A 1 306 ? 39.151  42.378  -14.927 1   28.96  ? 306 ILE A N   1 
ATOM   2517 C CA  . ILE A 1 306 ? 38.253  42.082  -16.035 1   31.29  ? 306 ILE A CA  1 
ATOM   2518 C C   . ILE A 1 306 ? 37.854  43.371  -16.743 1   33.59  ? 306 ILE A C   1 
ATOM   2519 O O   . ILE A 1 306 ? 38.008  43.423  -17.952 1   33.86  ? 306 ILE A O   1 
ATOM   2520 C CB  . ILE A 1 306 ? 37.041  41.267  -15.604 1   28.81  ? 306 ILE A CB  1 
ATOM   2521 C CG1 . ILE A 1 306 ? 37.465  39.867  -15.15  1   27.46  ? 306 ILE A CG1 1 
ATOM   2522 C CG2 . ILE A 1 306 ? 35.996  41.234  -16.748 1   31.77  ? 306 ILE A CG2 1 
ATOM   2523 C CD1 . ILE A 1 306 ? 36.365  39.123  -14.413 1   28.25  ? 306 ILE A CD1 1 
ATOM   2524 N N   . ASN A 1 307 ? 37.497  44.417  -16     1   31.15  ? 307 ASN A N   1 
ATOM   2525 C CA  . ASN A 1 307 ? 37.206  45.707  -16.596 1   34.17  ? 307 ASN A CA  1 
ATOM   2526 C C   . ASN A 1 307 ? 38.424  46.333  -17.285 1   35.82  ? 307 ASN A C   1 
ATOM   2527 O O   . ASN A 1 307 ? 38.233  47.076  -18.239 1   35.36  ? 307 ASN A O   1 
ATOM   2528 C CB  . ASN A 1 307 ? 36.608  46.676  -15.575 1   33.69  ? 307 ASN A CB  1 
ATOM   2529 C CG  . ASN A 1 307 ? 35.231  46.257  -15.126 1   32.75  ? 307 ASN A CG  1 
ATOM   2530 O OD1 . ASN A 1 307 ? 34.523  45.548  -15.839 1   32.65  ? 307 ASN A OD1 1 
ATOM   2531 N ND2 . ASN A 1 307 ? 34.801  46.677  -13.947 1   29.51  ? 307 ASN A ND2 1 
ATOM   2532 N N   . HIS A 1 308 ? 39.655  46.026  -16.852 1   33.27  ? 308 HIS A N   1 
ATOM   2533 C CA  . HIS A 1 308 ? 40.866  46.508  -17.492 1   38.71  ? 308 HIS A CA  1 
ATOM   2534 C C   . HIS A 1 308 ? 41.3    45.612  -18.666 1   39.25  ? 308 HIS A C   1 
ATOM   2535 O O   . HIS A 1 308 ? 42.341  45.844  -19.222 1   38.45  ? 308 HIS A O   1 
ATOM   2536 C CB  . HIS A 1 308 ? 41.963  46.708  -16.429 1   42.58  ? 308 HIS A CB  1 
ATOM   2537 C CG  . HIS A 1 308 ? 41.751  47.922  -15.596 1   45.37  ? 308 HIS A CG  1 
ATOM   2538 N ND1 . HIS A 1 308 ? 42.48   49.053  -15.895 1   57.49  ? 308 HIS A ND1 1 
ATOM   2539 C CD2 . HIS A 1 308 ? 40.969  48.26   -14.575 1   48.26  ? 308 HIS A CD2 1 
ATOM   2540 C CE1 . HIS A 1 308 ? 42.14   50.034  -15.076 1   53.32  ? 308 HIS A CE1 1 
ATOM   2541 N NE2 . HIS A 1 308 ? 41.231  49.566  -14.255 1   52.81  ? 308 HIS A NE2 1 
ATOM   2542 N N   . LYS A 1 309 ? 40.539  44.564  -18.996 1   38.29  ? 309 LYS A N   1 
ATOM   2543 C CA  . LYS A 1 309 ? 40.804  43.62   -20.073 1   45.23  ? 309 LYS A CA  1 
ATOM   2544 C C   . LYS A 1 309 ? 42.072  42.811  -19.811 1   44.89  ? 309 LYS A C   1 
ATOM   2545 O O   . LYS A 1 309 ? 42.714  42.353  -20.758 1   44.78  ? 309 LYS A O   1 
ATOM   2546 C CB  . LYS A 1 309 ? 40.745  44.335  -21.427 1   53.4   ? 309 LYS A CB  1 
ATOM   2547 C CG  . LYS A 1 309 ? 39.381  45.029  -21.631 1   59.62  ? 309 LYS A CG  1 
ATOM   2548 C CD  . LYS A 1 309 ? 39.388  46.431  -22.236 1   69.24  ? 309 LYS A CD  1 
ATOM   2549 C CE  . LYS A 1 309 ? 39.053  46.444  -23.697 1   79.59  ? 309 LYS A CE  1 
ATOM   2550 N NZ  . LYS A 1 309 ? 37.656  46.064  -23.955 1   82.27  ? 309 LYS A NZ  1 
ATOM   2551 N N   . GLU A 1 310 ? 42.379  42.58   -18.526 1   37.89  ? 310 GLU A N   1 
ATOM   2552 C CA  . GLU A 1 310 ? 43.565  41.837  -18.102 1   37.19  ? 310 GLU A CA  1 
ATOM   2553 C C   . GLU A 1 310 ? 43.093  40.42   -17.75  1   37.29  ? 310 GLU A C   1 
ATOM   2554 O O   . GLU A 1 310 ? 43.092  39.992  -16.576 1   33.85  ? 310 GLU A O   1 
ATOM   2555 C CB  . GLU A 1 310 ? 44.177  42.593  -16.92  1   38.96  ? 310 GLU A CB  1 
ATOM   2556 C CG  . GLU A 1 310 ? 44.835  43.923  -17.299 1   44.67  ? 310 GLU A CG  1 
ATOM   2557 C CD  . GLU A 1 310 ? 46.139  43.866  -18.052 1   51.13  ? 310 GLU A CD  1 
ATOM   2558 O OE1 . GLU A 1 310 ? 46.708  42.765  -18.284 1   53.92  ? 310 GLU A OE1 1 
ATOM   2559 O OE2 . GLU A 1 310 ? 46.591  44.975  -18.441 1   58.74  ? 310 GLU A OE2 1 
ATOM   2560 N N   . LEU A 1 311 ? 42.617  39.711  -18.776 1   35.16  ? 311 LEU A N   1 
ATOM   2561 C CA  . LEU A 1 311 ? 41.901  38.461  -18.571 1   35.61  ? 311 LEU A CA  1 
ATOM   2562 C C   . LEU A 1 311 ? 42.835  37.358  -18.06  1   36.68  ? 311 LEU A C   1 
ATOM   2563 O O   . LEU A 1 311 ? 42.424  36.533  -17.24  1   37.17  ? 311 LEU A O   1 
ATOM   2564 C CB  . LEU A 1 311 ? 41.161  38.094  -19.861 1   38.47  ? 311 LEU A CB  1 
ATOM   2565 C CG  . LEU A 1 311 ? 40.03   39.044  -20.286 1   39.23  ? 311 LEU A CG  1 
ATOM   2566 C CD1 . LEU A 1 311 ? 39.161  38.467  -21.405 1   42.93  ? 311 LEU A CD1 1 
ATOM   2567 C CD2 . LEU A 1 311 ? 39.147  39.444  -19.128 1   37.12  ? 311 LEU A CD2 1 
ATOM   2568 N N   . SER A 1 312 ? 44.072  37.34   -18.546 1   38.6   ? 312 SER A N   1 
ATOM   2569 C CA  . SER A 1 312 ? 45.051  36.343  -18.152 1   42.02  ? 312 SER A CA  1 
ATOM   2570 C C   . SER A 1 312 ? 45.392  36.477  -16.656 1   40.35  ? 312 SER A C   1 
ATOM   2571 O O   . SER A 1 312 ? 45.336  35.507  -15.914 1   38.48  ? 312 SER A O   1 
ATOM   2572 C CB  . SER A 1 312 ? 46.249  36.429  -19.03  1   45.67  ? 312 SER A CB  1 
ATOM   2573 O OG  . SER A 1 312 ? 47.154  35.446  -18.583 1   54.71  ? 312 SER A OG  1 
ATOM   2574 N N   . LYS A 1 313 ? 45.681  37.692  -16.19  1   39.02  ? 313 LYS A N   1 
ATOM   2575 C CA  . LYS A 1 313 ? 45.85   37.956  -14.763 1   40.99  ? 313 LYS A CA  1 
ATOM   2576 C C   . LYS A 1 313 ? 44.603  37.615  -13.934 1   34.87  ? 313 LYS A C   1 
ATOM   2577 O O   . LYS A 1 313 ? 44.74   37.076  -12.838 1   36.61  ? 313 LYS A O   1 
ATOM   2578 C CB  . LYS A 1 313 ? 46.19   39.431  -14.501 1   42.33  ? 313 LYS A CB  1 
ATOM   2579 C CG  . LYS A 1 313 ? 47.671  39.732  -14.625 1   48.37  ? 313 LYS A CG  1 
ATOM   2580 C CD  . LYS A 1 313 ? 47.991  41.106  -14.044 1   50.89  ? 313 LYS A CD  1 
ATOM   2581 C CE  . LYS A 1 313 ? 48.114  42.146  -15.1   1   53.66  ? 313 LYS A CE  1 
ATOM   2582 N NZ  . LYS A 1 313 ? 49.481  42.206  -15.635 1   54.27  ? 313 LYS A NZ  1 
ATOM   2583 N N   . ALA A 1 314 ? 43.405  38.003  -14.409 1   32.79  ? 314 ALA A N   1 
ATOM   2584 C CA  . ALA A 1 314 ? 42.163  37.694  -13.727 1   32.75  ? 314 ALA A CA  1 
ATOM   2585 C C   . ALA A 1 314 ? 42.008  36.193  -13.551 1   33.28  ? 314 ALA A C   1 
ATOM   2586 O O   . ALA A 1 314 ? 41.656  35.741  -12.473 1   29.94  ? 314 ALA A O   1 
ATOM   2587 C CB  . ALA A 1 314 ? 40.978  38.273  -14.472 1   33.2   ? 314 ALA A CB  1 
ATOM   2588 N N   . LEU A 1 315 ? 42.304  35.435  -14.604 1   33.49  ? 315 LEU A N   1 
ATOM   2589 C CA  . LEU A 1 315 ? 42.179  33.979  -14.564 1   36.17  ? 315 LEU A CA  1 
ATOM   2590 C C   . LEU A 1 315 ? 43.136  33.383  -13.531 1   36.45  ? 315 LEU A C   1 
ATOM   2591 O O   . LEU A 1 315 ? 42.724  32.51   -12.778 1   37.77  ? 315 LEU A O   1 
ATOM   2592 C CB  . LEU A 1 315 ? 42.354  33.317  -15.935 1   35.72  ? 315 LEU A CB  1 
ATOM   2593 C CG  . LEU A 1 315 ? 42.052  31.806  -15.996 1   39.72  ? 315 LEU A CG  1 
ATOM   2594 C CD1 . LEU A 1 315 ? 40.641  31.378  -15.555 1   42.28  ? 315 LEU A CD1 1 
ATOM   2595 C CD2 . LEU A 1 315 ? 42.296  31.309  -17.398 1   45.54  ? 315 LEU A CD2 1 
ATOM   2596 N N   . GLN A 1 316 ? 44.383  33.854  -13.479 1   38.77  ? 316 GLN A N   1 
ATOM   2597 C CA  . GLN A 1 316 ? 45.341  33.332  -12.504 1   43.35  ? 316 GLN A CA  1 
ATOM   2598 C C   . GLN A 1 316 ? 44.836  33.55   -11.073 1   37.05  ? 316 GLN A C   1 
ATOM   2599 O O   . GLN A 1 316 ? 44.884  32.623  -10.263 1   35.75  ? 316 GLN A O   1 
ATOM   2600 C CB  . GLN A 1 316 ? 46.764  33.872  -12.657 1   47.4   ? 316 GLN A CB  1 
ATOM   2601 C CG  . GLN A 1 316 ? 47.52   33.359  -13.878 1   55.88  ? 316 GLN A CG  1 
ATOM   2602 C CD  . GLN A 1 316 ? 49.027  33.52   -13.758 1   68.92  ? 316 GLN A CD  1 
ATOM   2603 O OE1 . GLN A 1 316 ? 49.554  34.191  -12.857 1   74.87  ? 316 GLN A OE1 1 
ATOM   2604 N NE2 . GLN A 1 316 ? 49.757  32.905  -14.681 1   72.53  ? 316 GLN A NE2 1 
ATOM   2605 N N   . LEU A 1 317 ? 44.269  34.729  -10.771 1   33.87  ? 317 LEU A N   1 
ATOM   2606 C CA  . LEU A 1 317 ? 43.733  34.979  -9.432  1   34.01  ? 317 LEU A CA  1 
ATOM   2607 C C   . LEU A 1 317 ? 42.466  34.17   -9.158  1   32.78  ? 317 LEU A C   1 
ATOM   2608 O O   . LEU A 1 317 ? 42.244  33.759  -8.014  1   34.88  ? 317 LEU A O   1 
ATOM   2609 C CB  . LEU A 1 317 ? 43.509  36.477  -9.242  1   33.29  ? 317 LEU A CB  1 
ATOM   2610 C CG  . LEU A 1 317 ? 44.801  37.31   -9.202  1   37.89  ? 317 LEU A CG  1 
ATOM   2611 C CD1 . LEU A 1 317 ? 44.44   38.773  -9.281  1   37.25  ? 317 LEU A CD1 1 
ATOM   2612 C CD2 . LEU A 1 317 ? 45.667  37.014  -7.963  1   39.39  ? 317 LEU A CD2 1 
ATOM   2613 N N   . LEU A 1 318 ? 41.604  33.995  -10.178 1   33.46  ? 318 LEU A N   1 
ATOM   2614 C CA  . LEU A 1 318 ? 40.366  33.254  -10.026 1   33.35  ? 318 LEU A CA  1 
ATOM   2615 C C   . LEU A 1 318 ? 40.686  31.804  -9.667  1   32.87  ? 318 LEU A C   1 
ATOM   2616 O O   . LEU A 1 318 ? 40.006  31.224  -8.809  1   31.08  ? 318 LEU A O   1 
ATOM   2617 C CB  . LEU A 1 318 ? 39.451  33.333  -11.251 1   35.37  ? 318 LEU A CB  1 
ATOM   2618 C CG  . LEU A 1 318 ? 38.009  32.853  -11.011 1   37.14  ? 318 LEU A CG  1 
ATOM   2619 C CD1 . LEU A 1 318 ? 37.176  33.679  -10.065 1   37.97  ? 318 LEU A CD1 1 
ATOM   2620 C CD2 . LEU A 1 318 ? 37.259  32.761  -12.292 1   47.04  ? 318 LEU A CD2 1 
ATOM   2621 N N   . ASN A 1 319 ? 41.69   31.219  -10.338 1   35.81  ? 319 ASN A N   1 
ATOM   2622 C CA  . ASN A 1 319 ? 42.129  29.86   -10.06  1   38.22  ? 319 ASN A CA  1 
ATOM   2623 C C   . ASN A 1 319 ? 42.575  29.66   -8.619  1   39.38  ? 319 ASN A C   1 
ATOM   2624 O O   . ASN A 1 319 ? 42.287  28.623  -8.06   1   38.85  ? 319 ASN A O   1 
ATOM   2625 C CB  . ASN A 1 319 ? 43.298  29.424  -10.937 1   43.01  ? 319 ASN A CB  1 
ATOM   2626 C CG  . ASN A 1 319 ? 42.882  29.163  -12.356 1   43.22  ? 319 ASN A CG  1 
ATOM   2627 O OD1 . ASN A 1 319 ? 41.692  29.011  -12.661 1   47.08  ? 319 ASN A OD1 1 
ATOM   2628 N ND2 . ASN A 1 319 ? 43.867  29.14   -13.231 1   47.28  ? 319 ASN A ND2 1 
ATOM   2629 N N   . LYS A 1 320 ? 43.26   30.631  -8.019  1   39.01  ? 320 LYS A N   1 
ATOM   2630 C CA  . LYS A 1 320 ? 43.565  30.574  -6.605  1   41.31  ? 320 LYS A CA  1 
ATOM   2631 C C   . LYS A 1 320 ? 42.315  30.465  -5.726  1   38.76  ? 320 LYS A C   1 
ATOM   2632 O O   . LYS A 1 320 ? 42.393  29.854  -4.656  1   41.45  ? 320 LYS A O   1 
ATOM   2633 C CB  . LYS A 1 320 ? 44.421  31.782  -6.224  1   41.49  ? 320 LYS A CB  1 
ATOM   2634 C CG  . LYS A 1 320 ? 45.871  31.76   -6.749  1   48.03  ? 320 LYS A CG  1 
ATOM   2635 C CD  . LYS A 1 320 ? 46.592  33.084  -6.469  1   57.6   ? 320 LYS A CD  1 
ATOM   2636 C CE  . LYS A 1 320 ? 47.827  33.396  -7.248  1   65.56  ? 320 LYS A CE  1 
ATOM   2637 N NZ  . LYS A 1 320 ? 48.872  32.433  -6.901  1   72.87  ? 320 LYS A NZ  1 
ATOM   2638 N N   . LEU A 1 321 ? 41.195  31.111  -6.116  1   34.73  ? 321 LEU A N   1 
ATOM   2639 C CA  . LEU A 1 321 ? 39.944  31.038  -5.351  1   35.51  ? 321 LEU A CA  1 
ATOM   2640 C C   . LEU A 1 321 ? 39.264  29.672  -5.443  1   35.82  ? 321 LEU A C   1 
ATOM   2641 O O   . LEU A 1 321 ? 38.498  29.33   -4.558  1   32.28  ? 321 LEU A O   1 
ATOM   2642 C CB  . LEU A 1 321 ? 38.951  32.137  -5.745  1   33.95  ? 321 LEU A CB  1 
ATOM   2643 C CG  . LEU A 1 321 ? 39.388  33.539  -5.337  1   33.23  ? 321 LEU A CG  1 
ATOM   2644 C CD1 . LEU A 1 321 ? 38.467  34.597  -5.89   1   32.03  ? 321 LEU A CD1 1 
ATOM   2645 C CD2 . LEU A 1 321 ? 39.475  33.608  -3.829  1   37.16  ? 321 LEU A CD2 1 
ATOM   2646 N N   . GLU A 1 322 ? 39.567  28.871  -6.463  1   36.77  ? 322 GLU A N   1 
ATOM   2647 C CA  . GLU A 1 322 ? 39.008  27.525  -6.552  1   42.74  ? 322 GLU A CA  1 
ATOM   2648 C C   . GLU A 1 322 ? 39.515  26.608  -5.437  1   45.55  ? 322 GLU A C   1 
ATOM   2649 O O   . GLU A 1 322 ? 38.915  25.579  -5.221  1   49.28  ? 322 GLU A O   1 
ATOM   2650 C CB  . GLU A 1 322 ? 39.267  26.899  -7.93   1   46.75  ? 322 GLU A CB  1 
ATOM   2651 C CG  . GLU A 1 322 ? 38.609  27.737  -9.027  1   50.43  ? 322 GLU A CG  1 
ATOM   2652 C CD  . GLU A 1 322 ? 37.792  27.047  -10.103 1   55.1   ? 322 GLU A CD  1 
ATOM   2653 O OE1 . GLU A 1 322 ? 37.005  27.77   -10.773 1   49.4   ? 322 GLU A OE1 1 
ATOM   2654 O OE2 . GLU A 1 322 ? 37.923  25.833  -10.27  1   62.08  ? 322 GLU A OE2 1 
ATOM   2655 N N   . GLU A 1 323 ? 40.645  26.926  -4.802  1   45.65  ? 323 GLU A N   1 
ATOM   2656 C CA  . GLU A 1 323 ? 41.104  26.181  -3.641  1   51.29  ? 323 GLU A CA  1 
ATOM   2657 C C   . GLU A 1 323 ? 40.437  26.64   -2.338  1   44.83  ? 323 GLU A C   1 
ATOM   2658 O O   . GLU A 1 323 ? 40.701  26.03   -1.315  1   45.28  ? 323 GLU A O   1 
ATOM   2659 C CB  . GLU A 1 323 ? 42.623  26.303  -3.641  1   57.61  ? 323 GLU A CB  1 
ATOM   2660 C CG  . GLU A 1 323 ? 43.204  25.47   -4.783  1   68.19  ? 323 GLU A CG  1 
ATOM   2661 C CD  . GLU A 1 323 ? 44.638  25.758  -5.166  1   77.45  ? 323 GLU A CD  1 
ATOM   2662 O OE1 . GLU A 1 323 ? 45.115  24.902  -5.941  1   88.39  ? 323 GLU A OE1 1 
ATOM   2663 O OE2 . GLU A 1 323 ? 45.263  26.766  -4.739  1   72.72  ? 323 GLU A OE2 1 
ATOM   2664 N N   . ARG A 1 324 ? 39.637  27.715  -2.341  1   37.39  ? 324 ARG A N   1 
ATOM   2665 C CA  . ARG A 1 324 ? 39.16   28.316  -1.101  1   36.49  ? 324 ARG A CA  1 
ATOM   2666 C C   . ARG A 1 324 ? 37.738  27.86   -0.792  1   36.59  ? 324 ARG A C   1 
ATOM   2667 O O   . ARG A 1 324 ? 36.942  27.7    -1.701  1   32.4   ? 324 ARG A O   1 
ATOM   2668 C CB  . ARG A 1 324 ? 39.185  29.844  -1.177  1   35.62  ? 324 ARG A CB  1 
ATOM   2669 C CG  . ARG A 1 324 ? 40.585  30.438  -1.297  1   32.47  ? 324 ARG A CG  1 
ATOM   2670 C CD  . ARG A 1 324 ? 41.439  30.26   -0.019  1   34.48  ? 324 ARG A CD  1 
ATOM   2671 N NE  . ARG A 1 324 ? 40.764  30.956  1.078   1   34.33  ? 324 ARG A NE  1 
ATOM   2672 C CZ  . ARG A 1 324 ? 40.707  32.28   1.232   1   33.31  ? 324 ARG A CZ  1 
ATOM   2673 N NH1 . ARG A 1 324 ? 41.537  33.074  0.573   1   33.45  ? 324 ARG A NH1 1 
ATOM   2674 N NH2 . ARG A 1 324 ? 39.854  32.813  2.092   1   31.51  ? 324 ARG A NH2 1 
ATOM   2675 N N   . ASP A 1 325 ? 37.421  27.769  0.514   1   36.09  ? 325 ASP A N   1 
ATOM   2676 C CA  . ASP A 1 325 ? 36.093  27.446  0.978   1   35.34  ? 325 ASP A CA  1 
ATOM   2677 C C   . ASP A 1 325 ? 35.226  28.667  0.718   1   31.99  ? 325 ASP A C   1 
ATOM   2678 O O   . ASP A 1 325 ? 35.638  29.782  1.015   1   29.94  ? 325 ASP A O   1 
ATOM   2679 C CB  . ASP A 1 325 ? 36.025  27.138  2.463   1   38.77  ? 325 ASP A CB  1 
ATOM   2680 C CG  . ASP A 1 325 ? 36.801  25.909  2.914   1   49.28  ? 325 ASP A CG  1 
ATOM   2681 O OD1 . ASP A 1 325 ? 37.067  25.022  2.081   1   45.82  ? 325 ASP A OD1 1 
ATOM   2682 O OD2 . ASP A 1 325 ? 37.201  25.899  4.088   1   62.54  ? 325 ASP A OD2 1 
ATOM   2683 N N   . GLN A 1 326 ? 34.067  28.422  0.108   1   30.22  ? 326 GLN A N   1 
ATOM   2684 C CA  . GLN A 1 326 ? 33.148  29.468  -0.286  1   28.26  ? 326 GLN A CA  1 
ATOM   2685 C C   . GLN A 1 326 ? 31.734  28.995  -0.03   1   27.04  ? 326 GLN A C   1 
ATOM   2686 O O   . GLN A 1 326 ? 31.477  27.826  -0.272  1   29.14  ? 326 GLN A O   1 
ATOM   2687 C CB  . GLN A 1 326 ? 33.222  29.724  -1.779  1   26.08  ? 326 GLN A CB  1 
ATOM   2688 C CG  . GLN A 1 326 ? 34.573  30.266  -2.183  1   28.12  ? 326 GLN A CG  1 
ATOM   2689 C CD  . GLN A 1 326 ? 34.634  30.621  -3.629  1   28.06  ? 326 GLN A CD  1 
ATOM   2690 O OE1 . GLN A 1 326 ? 33.854  31.439  -4.116  1   26.91  ? 326 GLN A OE1 1 
ATOM   2691 N NE2 . GLN A 1 326 ? 35.606  30.067  -4.303  1   33.4   ? 326 GLN A NE2 1 
ATOM   2692 N N   . ASN A 1 327 ? 30.852  29.925  0.381   1   24.07  ? 327 ASN A N   1 
ATOM   2693 C CA  . ASN A 1 327 ? 29.435  29.613  0.49    1   28.6   ? 327 ASN A CA  1 
ATOM   2694 C C   . ASN A 1 327 ? 28.786  29.648  -0.909  1   28.24  ? 327 ASN A C   1 
ATOM   2695 O O   . ASN A 1 327 ? 29.411  30.033  -1.907  1   26.58  ? 327 ASN A O   1 
ATOM   2696 C CB  . ASN A 1 327 ? 28.747  30.454  1.555   1   28.04  ? 327 ASN A CB  1 
ATOM   2697 C CG  . ASN A 1 327 ? 28.536  31.893  1.16    1   30.97  ? 327 ASN A CG  1 
ATOM   2698 O OD1 . ASN A 1 327 ? 28.02   32.198  0.069   1   23.84  ? 327 ASN A OD1 1 
ATOM   2699 N ND2 . ASN A 1 327 ? 28.841  32.808  2.069   1   28.15  ? 327 ASN A ND2 1 
ATOM   2700 N N   . GLU A 1 328 ? 27.529  29.168  -0.988  1   28.95  ? 328 GLU A N   1 
ATOM   2701 C CA  . GLU A 1 328 ? 26.895  28.972  -2.28   1   29.12  ? 328 GLU A CA  1 
ATOM   2702 C C   . GLU A 1 328 ? 26.664  30.324  -2.964  1   26.61  ? 328 GLU A C   1 
ATOM   2703 O O   . GLU A 1 328 ? 26.711  30.383  -4.191  1   26.76  ? 328 GLU A O   1 
ATOM   2704 C CB  . GLU A 1 328 ? 25.604  28.175  -2.163  1   33.78  ? 328 GLU A CB  1 
ATOM   2705 C CG  . GLU A 1 328 ? 25.863  26.69   -1.961  1   40.64  ? 328 GLU A CG  1 
ATOM   2706 C CD  . GLU A 1 328 ? 24.568  25.903  -1.823  1   48.79  ? 328 GLU A CD  1 
ATOM   2707 O OE1 . GLU A 1 328 ? 23.5    26.435  -1.406  1   42.55  ? 328 GLU A OE1 1 
ATOM   2708 O OE2 . GLU A 1 328 ? 24.647  24.719  -2.206  1   56.37  ? 328 GLU A OE2 1 
ATOM   2709 N N   . ASN A 1 329 ? 26.31   31.371  -2.199  1   24.78  ? 329 ASN A N   1 
ATOM   2710 C CA  . ASN A 1 329 ? 26.138  32.689  -2.788  1   23.98  ? 329 ASN A CA  1 
ATOM   2711 C C   . ASN A 1 329 ? 27.472  33.225  -3.342  1   25.14  ? 329 ASN A C   1 
ATOM   2712 O O   . ASN A 1 329 ? 27.571  33.72   -4.48   1   22.18  ? 329 ASN A O   1 
ATOM   2713 C CB  . ASN A 1 329 ? 25.534  33.643  -1.781  1   23.69  ? 329 ASN A CB  1 
ATOM   2714 C CG  . ASN A 1 329 ? 24.953  34.844  -2.473  1   24.87  ? 329 ASN A CG  1 
ATOM   2715 O OD1 . ASN A 1 329 ? 25.517  35.949  -2.49   1   25.04  ? 329 ASN A OD1 1 
ATOM   2716 N ND2 . ASN A 1 329 ? 23.839  34.618  -3.116  1   25.29  ? 329 ASN A ND2 1 
ATOM   2717 N N   . GLU A 1 330 ? 28.565  33.002  -2.594  1   23.83  ? 330 GLU A N   1 
ATOM   2718 C CA  . GLU A 1 330 ? 29.886  33.431  -3.066  1   26.46  ? 330 GLU A CA  1 
ATOM   2719 C C   . GLU A 1 330 ? 30.248  32.686  -4.365  1   24.76  ? 330 GLU A C   1 
ATOM   2720 O O   . GLU A 1 330 ? 30.876  33.238  -5.23   1   22.39  ? 330 GLU A O   1 
ATOM   2721 C CB  . GLU A 1 330 ? 30.985  33.181  -2.017  1   26.52  ? 330 GLU A CB  1 
ATOM   2722 C CG  . GLU A 1 330 ? 30.804  34.06   -0.775  1   27.61  ? 330 GLU A CG  1 
ATOM   2723 C CD  . GLU A 1 330 ? 31.754  33.798  0.401   1   29.54  ? 330 GLU A CD  1 
ATOM   2724 O OE1 . GLU A 1 330 ? 32.154  32.644  0.57    1   29.29  ? 330 GLU A OE1 1 
ATOM   2725 O OE2 . GLU A 1 330 ? 32.131  34.737  1.121   1   27.44  ? 330 GLU A OE2 1 
ATOM   2726 N N   . LEU A 1 331 ? 29.902  31.411  -4.45   1   22.88  ? 331 LEU A N   1 
ATOM   2727 C CA  . LEU A 1 331 ? 30.1    30.614  -5.657  1   24.89  ? 331 LEU A CA  1 
ATOM   2728 C C   . LEU A 1 331 ? 29.325  31.138  -6.864  1   25.01  ? 331 LEU A C   1 
ATOM   2729 O O   . LEU A 1 331 ? 29.852  31.075  -7.987  1   24.99  ? 331 LEU A O   1 
ATOM   2730 C CB  . LEU A 1 331 ? 29.797  29.157  -5.35   1   25.64  ? 331 LEU A CB  1 
ATOM   2731 C CG  . LEU A 1 331 ? 30.939  28.466  -4.587  1   26.1   ? 331 LEU A CG  1 
ATOM   2732 C CD1 . LEU A 1 331 ? 30.527  27.074  -4.141  1   29.09  ? 331 LEU A CD1 1 
ATOM   2733 C CD2 . LEU A 1 331 ? 32.261  28.395  -5.307  1   28.35  ? 331 LEU A CD2 1 
ATOM   2734 N N   . GLY A 1 332 ? 28.108  31.663  -6.643  1   23.99  ? 332 GLY A N   1 
ATOM   2735 C CA  . GLY A 1 332 ? 27.421  32.351  -7.721  1   27.12  ? 332 GLY A CA  1 
ATOM   2736 C C   . GLY A 1 332 ? 28.268  33.484  -8.33   1   26.34  ? 332 GLY A C   1 
ATOM   2737 O O   . GLY A 1 332 ? 28.314  33.659  -9.547  1   23.97  ? 332 GLY A O   1 
ATOM   2738 N N   . PHE A 1 333 ? 28.875  34.315  -7.458  1   24.56  ? 333 PHE A N   1 
ATOM   2739 C CA  . PHE A 1 333 ? 29.763  35.371  -7.908  1   22.81  ? 333 PHE A CA  1 
ATOM   2740 C C   . PHE A 1 333 ? 30.996  34.773  -8.575  1   22.16  ? 333 PHE A C   1 
ATOM   2741 O O   . PHE A 1 333 ? 31.417  35.302  -9.597  1   25.5   ? 333 PHE A O   1 
ATOM   2742 C CB  . PHE A 1 333 ? 30.134  36.327  -6.754  1   25.7   ? 333 PHE A CB  1 
ATOM   2743 C CG  . PHE A 1 333 ? 28.946  37.177  -6.371  1   25.81  ? 333 PHE A CG  1 
ATOM   2744 C CD1 . PHE A 1 333 ? 28.675  38.341  -7.075  1   29.54  ? 333 PHE A CD1 1 
ATOM   2745 C CD2 . PHE A 1 333 ? 28.103  36.819  -5.308  1   28.43  ? 333 PHE A CD2 1 
ATOM   2746 C CE1 . PHE A 1 333 ? 27.526  39.094  -6.776  1   29.21  ? 333 PHE A CE1 1 
ATOM   2747 C CE2 . PHE A 1 333 ? 26.984  37.594  -5.002  1   28.34  ? 333 PHE A CE2 1 
ATOM   2748 C CZ  . PHE A 1 333 ? 26.677  38.701  -5.756  1   27.33  ? 333 PHE A CZ  1 
ATOM   2749 N N   . HIS A 1 334 ? 31.594  33.708  -7.999  1   22.34  ? 334 HIS A N   1 
ATOM   2750 C CA  . HIS A 1 334 ? 32.791  33.08   -8.538  1   24.28  ? 334 HIS A CA  1 
ATOM   2751 C C   . HIS A 1 334 ? 32.601  32.712  -10.024 1   26.41  ? 334 HIS A C   1 
ATOM   2752 O O   . HIS A 1 334 ? 33.426  33.042  -10.887 1   24.52  ? 334 HIS A O   1 
ATOM   2753 C CB  . HIS A 1 334 ? 33.153  31.813  -7.763  1   24.38  ? 334 HIS A CB  1 
ATOM   2754 C CG  . HIS A 1 334 ? 34.352  31.115  -8.249  1   25.5   ? 334 HIS A CG  1 
ATOM   2755 N ND1 . HIS A 1 334 ? 35.594  31.48   -7.793  1   27.1   ? 334 HIS A ND1 1 
ATOM   2756 C CD2 . HIS A 1 334 ? 34.561  30.172  -9.169  1   29.96  ? 334 HIS A CD2 1 
ATOM   2757 C CE1 . HIS A 1 334 ? 36.511  30.727  -8.369  1   28.83  ? 334 HIS A CE1 1 
ATOM   2758 N NE2 . HIS A 1 334 ? 35.917  29.919  -9.227  1   29.51  ? 334 HIS A NE2 1 
ATOM   2759 N N   . TYR A 1 335 ? 31.538  31.964  -10.286 1   24.82  ? 335 TYR A N   1 
ATOM   2760 C CA  . TYR A 1 335 ? 31.249  31.457  -11.618 1   25.48  ? 335 TYR A CA  1 
ATOM   2761 C C   . TYR A 1 335 ? 30.785  32.57   -12.566 1   25.46  ? 335 TYR A C   1 
ATOM   2762 O O   . TYR A 1 335 ? 31.063  32.49   -13.752 1   26.69  ? 335 TYR A O   1 
ATOM   2763 C CB  . TYR A 1 335 ? 30.299  30.266  -11.528 1   25.01  ? 335 TYR A CB  1 
ATOM   2764 C CG  . TYR A 1 335 ? 31.017  28.992  -11.108 1   26.69  ? 335 TYR A CG  1 
ATOM   2765 C CD1 . TYR A 1 335 ? 31.808  28.308  -12.006 1   30.85  ? 335 TYR A CD1 1 
ATOM   2766 C CD2 . TYR A 1 335 ? 30.967  28.524  -9.801  1   27.15  ? 335 TYR A CD2 1 
ATOM   2767 C CE1 . TYR A 1 335 ? 32.539  27.19   -11.632 1   32.84  ? 335 TYR A CE1 1 
ATOM   2768 C CE2 . TYR A 1 335 ? 31.663  27.396  -9.425  1   30.53  ? 335 TYR A CE2 1 
ATOM   2769 C CZ  . TYR A 1 335 ? 32.408  26.702  -10.362 1   32.61  ? 335 TYR A CZ  1 
ATOM   2770 O OH  . TYR A 1 335 ? 33.071  25.593  -9.985  1   34.17  ? 335 TYR A OH  1 
ATOM   2771 N N   . TYR A 1 336 ? 30.178  33.625  -12.054 1   24.65  ? 336 TYR A N   1 
ATOM   2772 C CA  . TYR A 1 336 ? 29.903  34.787  -12.879 1   24.6   ? 336 TYR A CA  1 
ATOM   2773 C C   . TYR A 1 336 ? 31.201  35.392  -13.413 1   29.35  ? 336 TYR A C   1 
ATOM   2774 O O   . TYR A 1 336 ? 31.322  35.641  -14.628 1   27.66  ? 336 TYR A O   1 
ATOM   2775 C CB  . TYR A 1 336 ? 29.1    35.833  -12.123 1   23.81  ? 336 TYR A CB  1 
ATOM   2776 C CG  . TYR A 1 336 ? 28.791  37.063  -12.942 1   24.56  ? 336 TYR A CG  1 
ATOM   2777 C CD1 . TYR A 1 336 ? 27.904  36.997  -14.026 1   27.06  ? 336 TYR A CD1 1 
ATOM   2778 C CD2 . TYR A 1 336 ? 29.426  38.275  -12.679 1   28.89  ? 336 TYR A CD2 1 
ATOM   2779 C CE1 . TYR A 1 336 ? 27.706  38.088  -14.859 1   26.8   ? 336 TYR A CE1 1 
ATOM   2780 C CE2 . TYR A 1 336 ? 29.174  39.394  -13.456 1   28.36  ? 336 TYR A CE2 1 
ATOM   2781 C CZ  . TYR A 1 336 ? 28.316  39.3    -14.542 1   31.46  ? 336 TYR A CZ  1 
ATOM   2782 O OH  . TYR A 1 336 ? 28.061  40.425  -15.245 1   33.16  ? 336 TYR A OH  1 
ATOM   2783 N N   . LEU A 1 337 ? 32.188  35.584  -12.509 1   28.64  ? 337 LEU A N   1 
ATOM   2784 C CA  . LEU A 1 337 ? 33.487  36.101  -12.903 1   27.95  ? 337 LEU A CA  1 
ATOM   2785 C C   . LEU A 1 337 ? 34.139  35.169  -13.911 1   27.57  ? 337 LEU A C   1 
ATOM   2786 O O   . LEU A 1 337 ? 34.701  35.609  -14.91  1   27.85  ? 337 LEU A O   1 
ATOM   2787 C CB  . LEU A 1 337 ? 34.417  36.329  -11.71  1   27.71  ? 337 LEU A CB  1 
ATOM   2788 C CG  . LEU A 1 337 ? 33.91   37.379  -10.735 1   28.49  ? 337 LEU A CG  1 
ATOM   2789 C CD1 . LEU A 1 337 ? 34.796  37.362  -9.471  1   33.71  ? 337 LEU A CD1 1 
ATOM   2790 C CD2 . LEU A 1 337 ? 33.822  38.765  -11.331 1   31.56  ? 337 LEU A CD2 1 
ATOM   2791 N N   . LYS A 1 338 ? 34.072  33.87   -13.626 1   25.74  ? 338 LYS A N   1 
ATOM   2792 C CA  . LYS A 1 338 ? 34.672  32.882  -14.497 1   28.5   ? 338 LYS A CA  1 
ATOM   2793 C C   . LYS A 1 338 ? 34.112  32.976  -15.93  1   28.67  ? 338 LYS A C   1 
ATOM   2794 O O   . LYS A 1 338 ? 34.861  32.857  -16.91  1   33.12  ? 338 LYS A O   1 
ATOM   2795 C CB  . LYS A 1 338 ? 34.436  31.462  -13.975 1   29.45  ? 338 LYS A CB  1 
ATOM   2796 C CG  . LYS A 1 338 ? 35.283  30.435  -14.713 1   32.86  ? 338 LYS A CG  1 
ATOM   2797 C CD  . LYS A 1 338 ? 35.314  29.09   -14.013 1   38.52  ? 338 LYS A CD  1 
ATOM   2798 C CE  . LYS A 1 338 ? 36.499  28.323  -14.534 1   46.63  ? 338 LYS A CE  1 
ATOM   2799 N NZ  . LYS A 1 338 ? 36.749  27.174  -13.664 1   51.92  ? 338 LYS A NZ  1 
ATOM   2800 N N   . GLY A 1 339 ? 32.796  33.112  -16.017 1   29.7   ? 339 GLY A N   1 
ATOM   2801 C CA  . GLY A 1 339 ? 32.102  33.356  -17.282 1   31.05  ? 339 GLY A CA  1 
ATOM   2802 C C   . GLY A 1 339 ? 32.586  34.58   -18.048 1   31.37  ? 339 GLY A C   1 
ATOM   2803 O O   . GLY A 1 339 ? 32.793  34.518  -19.267 1   30.2   ? 339 GLY A O   1 
ATOM   2804 N N   . LEU A 1 340 ? 32.728  35.697  -17.334 1   30.19  ? 340 LEU A N   1 
ATOM   2805 C CA  . LEU A 1 340 ? 33.24   36.918  -17.927 1   30.43  ? 340 LEU A CA  1 
ATOM   2806 C C   . LEU A 1 340 ? 34.652  36.73   -18.455 1   32.69  ? 340 LEU A C   1 
ATOM   2807 O O   . LEU A 1 340 ? 34.98   37.344  -19.463 1   35.26  ? 340 LEU A O   1 
ATOM   2808 C CB  . LEU A 1 340 ? 33.182  38.101  -16.958 1   30.89  ? 340 LEU A CB  1 
ATOM   2809 C CG  . LEU A 1 340 ? 31.819  38.595  -16.476 1   31.93  ? 340 LEU A CG  1 
ATOM   2810 C CD1 . LEU A 1 340 ? 32.013  39.702  -15.442 1   30.6   ? 340 LEU A CD1 1 
ATOM   2811 C CD2 . LEU A 1 340 ? 30.969  39.123  -17.644 1   33.65  ? 340 LEU A CD2 1 
ATOM   2812 N N   . ILE A 1 341 ? 35.493  35.919  -17.794 1   32.08  ? 341 ILE A N   1 
ATOM   2813 C CA  . ILE A 1 341 ? 36.876  35.702  -18.179 1   31.81  ? 341 ILE A CA  1 
ATOM   2814 C C   . ILE A 1 341 ? 36.936  34.764  -19.392 1   35.22  ? 341 ILE A C   1 
ATOM   2815 O O   . ILE A 1 341 ? 37.651  35.062  -20.333 1   34.06  ? 341 ILE A O   1 
ATOM   2816 C CB  . ILE A 1 341 ? 37.726  35.175  -17     1   33.76  ? 341 ILE A CB  1 
ATOM   2817 C CG1 . ILE A 1 341 ? 37.841  36.249  -15.906 1   32.34  ? 341 ILE A CG1 1 
ATOM   2818 C CG2 . ILE A 1 341 ? 39.116  34.69   -17.449 1   37.4   ? 341 ILE A CG2 1 
ATOM   2819 C CD1 . ILE A 1 341 ? 38.162  35.715  -14.539 1   33.53  ? 341 ILE A CD1 1 
ATOM   2820 N N   . THR A 1 342 ? 36.241  33.63   -19.319 1   33.34  ? 342 THR A N   1 
ATOM   2821 C CA  . THR A 1 342 ? 36.381  32.522  -20.244 1   34.83  ? 342 THR A CA  1 
ATOM   2822 C C   . THR A 1 342 ? 35.371  32.583  -21.397 1   34.71  ? 342 THR A C   1 
ATOM   2823 O O   . THR A 1 342 ? 35.548  31.874  -22.371 1   39.97  ? 342 THR A O   1 
ATOM   2824 C CB  . THR A 1 342 ? 36.284  31.196  -19.493 1   36.08  ? 342 THR A CB  1 
ATOM   2825 O OG1 . THR A 1 342 ? 34.957  31.058  -19.008 1   35.24  ? 342 THR A OG1 1 
ATOM   2826 C CG2 . THR A 1 342 ? 37.311  31.044  -18.386 1   37.29  ? 342 THR A CG2 1 
ATOM   2827 N N   . ASN A 1 343 ? 34.304  33.354  -21.29  1   34.15  ? 343 ASN A N   1 
ATOM   2828 C CA  . ASN A 1 343 ? 33.205  33.354  -22.245 1   41.03  ? 343 ASN A CA  1 
ATOM   2829 C C   . ASN A 1 343 ? 32.528  31.98   -22.437 1   43.57  ? 343 ASN A C   1 
ATOM   2830 O O   . ASN A 1 343 ? 31.943  31.734  -23.496 1   45.11  ? 343 ASN A O   1 
ATOM   2831 C CB  . ASN A 1 343 ? 33.697  33.91   -23.585 1   44.76  ? 343 ASN A CB  1 
ATOM   2832 C CG  . ASN A 1 343 ? 32.576  34.444  -24.433 1   47.75  ? 343 ASN A CG  1 
ATOM   2833 O OD1 . ASN A 1 343 ? 32.584  34.213  -25.639 1   56.37  ? 343 ASN A OD1 1 
ATOM   2834 N ND2 . ASN A 1 343 ? 31.64   35.192  -23.872 1   51.35  ? 343 ASN A ND2 1 
ATOM   2835 N N   . GLU A 1 344 ? 32.592  31.1    -21.425 1   41.24  ? 344 GLU A N   1 
ATOM   2836 C CA  . GLU A 1 344 ? 31.997  29.77   -21.476 1   40.74  ? 344 GLU A CA  1 
ATOM   2837 C C   . GLU A 1 344 ? 30.589  29.871  -20.893 1   39.07  ? 344 GLU A C   1 
ATOM   2838 O O   . GLU A 1 344 ? 30.418  30.305  -19.737 1   32.87  ? 344 GLU A O   1 
ATOM   2839 C CB  . GLU A 1 344 ? 32.779  28.749  -20.653 1   43.36  ? 344 GLU A CB  1 
ATOM   2840 C CG  . GLU A 1 344 ? 34.151  28.409  -21.206 1   51.59  ? 344 GLU A CG  1 
ATOM   2841 C CD  . GLU A 1 344 ? 34.149  27.62   -22.505 1   66.43  ? 344 GLU A CD  1 
ATOM   2842 O OE1 . GLU A 1 344 ? 33.052  27.193  -22.981 1   67.13  ? 344 GLU A OE1 1 
ATOM   2843 O OE2 . GLU A 1 344 ? 35.284  27.434  -23.033 1   73.23  ? 344 GLU A OE2 1 
ATOM   2844 N N   . LYS A 1 345 ? 29.587  29.454  -21.684 1   35.91  ? 345 LYS A N   1 
ATOM   2845 C CA  . LYS A 1 345 ? 28.214  29.372  -21.201 1   37.17  ? 345 LYS A CA  1 
ATOM   2846 C C   . LYS A 1 345 ? 28.129  28.541  -19.924 1   31.5   ? 345 LYS A C   1 
ATOM   2847 O O   . LYS A 1 345 ? 27.363  28.883  -19.027 1   30.32  ? 345 LYS A O   1 
ATOM   2848 C CB  . LYS A 1 345 ? 27.241  28.714  -22.19  1   39.19  ? 345 LYS A CB  1 
ATOM   2849 C CG  . LYS A 1 345 ? 26.876  29.48   -23.417 1   46.99  ? 345 LYS A CG  1 
ATOM   2850 C CD  . LYS A 1 345 ? 26.123  28.535  -24.358 1   49.62  ? 345 LYS A CD  1 
ATOM   2851 C CE  . LYS A 1 345 ? 25.92   29.005  -25.725 1   58.5   ? 345 LYS A CE  1 
ATOM   2852 N NZ  . LYS A 1 345 ? 24.832  29.981  -25.808 1   65.24  ? 345 LYS A NZ  1 
ATOM   2853 N N   . GLU A 1 346 ? 28.91   27.463  -19.845 1   30.64  ? 346 GLU A N   1 
ATOM   2854 C CA  . GLU A 1 346 ? 28.871  26.58   -18.683 1   32.73  ? 346 GLU A CA  1 
ATOM   2855 C C   . GLU A 1 346 ? 29.056  27.354  -17.366 1   31.16  ? 346 GLU A C   1 
ATOM   2856 O O   . GLU A 1 346 ? 28.376  27.099  -16.342 1   28.13  ? 346 GLU A O   1 
ATOM   2857 C CB  . GLU A 1 346 ? 29.877  25.446  -18.874 1   36.47  ? 346 GLU A CB  1 
ATOM   2858 C CG  . GLU A 1 346 ? 29.96   24.47   -17.706 1   36.4   ? 346 GLU A CG  1 
ATOM   2859 C CD  . GLU A 1 346 ? 28.68   23.763  -17.289 1   36.3   ? 346 GLU A CD  1 
ATOM   2860 O OE1 . GLU A 1 346 ? 27.775  23.587  -18.138 1   35.66  ? 346 GLU A OE1 1 
ATOM   2861 O OE2 . GLU A 1 346 ? 28.559  23.421  -16.077 1   34.85  ? 346 GLU A OE2 1 
ATOM   2862 N N   . ALA A 1 347 ? 30.025  28.265  -17.335 1   30.31  ? 347 ALA A N   1 
ATOM   2863 C CA  . ALA A 1 347 ? 30.273  28.972  -16.071 1   30.56  ? 347 ALA A CA  1 
ATOM   2864 C C   . ALA A 1 347 ? 29.052  29.808  -15.676 1   27.22  ? 347 ALA A C   1 
ATOM   2865 O O   . ALA A 1 347 ? 28.696  29.89   -14.491 1   26.44  ? 347 ALA A O   1 
ATOM   2866 C CB  . ALA A 1 347 ? 31.55   29.797  -16.168 1   30.5   ? 347 ALA A CB  1 
ATOM   2867 N N   . PHE A 1 348 ? 28.374  30.423  -16.659 1   26.83  ? 348 PHE A N   1 
ATOM   2868 C CA  . PHE A 1 348 ? 27.184  31.199  -16.368 1   26.18  ? 348 PHE A CA  1 
ATOM   2869 C C   . PHE A 1 348 ? 26.034  30.303  -15.898 1   26.76  ? 348 PHE A C   1 
ATOM   2870 O O   . PHE A 1 348 ? 25.312  30.688  -14.961 1   24.04  ? 348 PHE A O   1 
ATOM   2871 C CB  . PHE A 1 348 ? 26.806  32.037  -17.593 1   29.5   ? 348 PHE A CB  1 
ATOM   2872 C CG  . PHE A 1 348 ? 27.74   33.19   -17.914 1   26.92  ? 348 PHE A CG  1 
ATOM   2873 C CD1 . PHE A 1 348 ? 28.034  34.159  -16.966 1   29.15  ? 348 PHE A CD1 1 
ATOM   2874 C CD2 . PHE A 1 348 ? 28.367  33.26   -19.159 1   29.86  ? 348 PHE A CD2 1 
ATOM   2875 C CE1 . PHE A 1 348 ? 28.935  35.184  -17.276 1   29.2   ? 348 PHE A CE1 1 
ATOM   2876 C CE2 . PHE A 1 348 ? 29.224  34.295  -19.48  1   31.58  ? 348 PHE A CE2 1 
ATOM   2877 C CZ  . PHE A 1 348 ? 29.487  35.265  -18.551 1   29.98  ? 348 PHE A CZ  1 
ATOM   2878 N N   . PHE A 1 349 ? 25.899  29.112  -16.495 1   26.36  ? 349 PHE A N   1 
ATOM   2879 C CA  . PHE A 1 349 ? 24.899  28.159  -16.008 1   29.23  ? 349 PHE A CA  1 
ATOM   2880 C C   . PHE A 1 349 ? 25.133  27.776  -14.536 1   28.08  ? 349 PHE A C   1 
ATOM   2881 O O   . PHE A 1 349 ? 24.173  27.757  -13.763 1   25.01  ? 349 PHE A O   1 
ATOM   2882 C CB  . PHE A 1 349 ? 24.843  26.857  -16.798 1   27.91  ? 349 PHE A CB  1 
ATOM   2883 C CG  . PHE A 1 349 ? 24.376  26.958  -18.246 1   29.35  ? 349 PHE A CG  1 
ATOM   2884 C CD1 . PHE A 1 349 ? 23.297  27.734  -18.614 1   30.2   ? 349 PHE A CD1 1 
ATOM   2885 C CD2 . PHE A 1 349 ? 25.033  26.25   -19.247 1   35.46  ? 349 PHE A CD2 1 
ATOM   2886 C CE1 . PHE A 1 349 ? 22.875  27.793  -19.947 1   33.91  ? 349 PHE A CE1 1 
ATOM   2887 C CE2 . PHE A 1 349 ? 24.607  26.321  -20.593 1   35.09  ? 349 PHE A CE2 1 
ATOM   2888 C CZ  . PHE A 1 349 ? 23.522  27.065  -20.922 1   32.41  ? 349 PHE A CZ  1 
ATOM   2889 N N   . LYS A 1 350 ? 26.391  27.463  -14.17  1   27.55  ? 350 LYS A N   1 
ATOM   2890 C CA  . LYS A 1 350 ? 26.72   27.165  -12.776 1   27.09  ? 350 LYS A CA  1 
ATOM   2891 C C   . LYS A 1 350 ? 26.425  28.364  -11.872 1   24.58  ? 350 LYS A C   1 
ATOM   2892 O O   . LYS A 1 350 ? 25.923  28.148  -10.796 1   23.39  ? 350 LYS A O   1 
ATOM   2893 C CB  . LYS A 1 350 ? 28.195  26.787  -12.594 1   29.4   ? 350 LYS A CB  1 
ATOM   2894 C CG  . LYS A 1 350 ? 28.59   25.415  -13.13  1   33.34  ? 350 LYS A CG  1 
ATOM   2895 C CD  . LYS A 1 350 ? 29.983  25.027  -12.648 1   37     ? 350 LYS A CD  1 
ATOM   2896 C CE  . LYS A 1 350 ? 30.39   23.623  -12.904 1   42.61  ? 350 LYS A CE  1 
ATOM   2897 N NZ  . LYS A 1 350 ? 30.822  23.492  -14.302 1   42.86  ? 350 LYS A NZ  1 
ATOM   2898 N N   . SER A 1 351 ? 26.752  29.589  -12.312 1   24.37  ? 351 SER A N   1 
ATOM   2899 C CA  . SER A 1 351 ? 26.448  30.798  -11.556 1   25.37  ? 351 SER A CA  1 
ATOM   2900 C C   . SER A 1 351 ? 24.952  30.869  -11.203 1   25.26  ? 351 SER A C   1 
ATOM   2901 O O   . SER A 1 351 ? 24.59   31.065  -10.026 1   21.95  ? 351 SER A O   1 
ATOM   2902 C CB  . SER A 1 351 ? 26.933  32.005  -12.303 1   24.95  ? 351 SER A CB  1 
ATOM   2903 O OG  . SER A 1 351 ? 26.624  33.203  -11.6   1   24.71  ? 351 SER A OG  1 
ATOM   2904 N N   . VAL A 1 352 ? 24.101  30.614  -12.229 1   24.67  ? 352 VAL A N   1 
ATOM   2905 C CA  . VAL A 1 352 ? 22.657  30.567  -12.114 1   23.93  ? 352 VAL A CA  1 
ATOM   2906 C C   . VAL A 1 352 ? 22.267  29.529  -11.063 1   22.36  ? 352 VAL A C   1 
ATOM   2907 O O   . VAL A 1 352 ? 21.475  29.849  -10.176 1   22.9   ? 352 VAL A O   1 
ATOM   2908 C CB  . VAL A 1 352 ? 21.922  30.325  -13.46  1   25.27  ? 352 VAL A CB  1 
ATOM   2909 C CG1 . VAL A 1 352 ? 20.411  30.101  -13.248 1   25.36  ? 352 VAL A CG1 1 
ATOM   2910 C CG2 . VAL A 1 352 ? 22.102  31.505  -14.396 1   26.98  ? 352 VAL A CG2 1 
ATOM   2911 N N   . GLU A 1 353 ? 22.86   28.341  -11.145 1   23     ? 353 GLU A N   1 
ATOM   2912 C CA  . GLU A 1 353 ? 22.518  27.253  -10.236 1   23.3   ? 353 GLU A CA  1 
ATOM   2913 C C   . GLU A 1 353 ? 22.858  27.602  -8.789  1   23.94  ? 353 GLU A C   1 
ATOM   2914 O O   . GLU A 1 353 ? 22.081  27.276  -7.883  1   24.9   ? 353 GLU A O   1 
ATOM   2915 C CB  . GLU A 1 353 ? 23.134  25.932  -10.67  1   27.17  ? 353 GLU A CB  1 
ATOM   2916 C CG  . GLU A 1 353 ? 22.491  25.415  -11.965 1   27.24  ? 353 GLU A CG  1 
ATOM   2917 C CD  . GLU A 1 353 ? 23.246  24.305  -12.655 1   31.21  ? 353 GLU A CD  1 
ATOM   2918 O OE1 . GLU A 1 353 ? 24.483  24.276  -12.611 1   31.62  ? 353 GLU A OE1 1 
ATOM   2919 O OE2 . GLU A 1 353 ? 22.549  23.534  -13.346 1   31.9   ? 353 GLU A OE2 1 
ATOM   2920 N N   . TYR A 1 354 ? 24.036  28.18   -8.573  1   23.79  ? 354 TYR A N   1 
ATOM   2921 C CA  . TYR A 1 354 ? 24.437  28.551  -7.211  1   23.87  ? 354 TYR A CA  1 
ATOM   2922 C C   . TYR A 1 354 ? 23.516  29.635  -6.658  1   23.09  ? 354 TYR A C   1 
ATOM   2923 O O   . TYR A 1 354 ? 23.195  29.588  -5.475  1   21.93  ? 354 TYR A O   1 
ATOM   2924 C CB  . TYR A 1 354 ? 25.909  28.936  -7.135  1   21.3   ? 354 TYR A CB  1 
ATOM   2925 C CG  . TYR A 1 354 ? 26.858  27.767  -7.116  1   24.76  ? 354 TYR A CG  1 
ATOM   2926 C CD1 . TYR A 1 354 ? 26.889  26.912  -6.018  1   25.29  ? 354 TYR A CD1 1 
ATOM   2927 C CD2 . TYR A 1 354 ? 27.689  27.477  -8.191  1   25.11  ? 354 TYR A CD2 1 
ATOM   2928 C CE1 . TYR A 1 354 ? 27.752  25.833  -5.96   1   28.75  ? 354 TYR A CE1 1 
ATOM   2929 C CE2 . TYR A 1 354 ? 28.553  26.383  -8.145  1   27.06  ? 354 TYR A CE2 1 
ATOM   2930 C CZ  . TYR A 1 354 ? 28.614  25.601  -7.013  1   29.95  ? 354 TYR A CZ  1 
ATOM   2931 O OH  . TYR A 1 354 ? 29.438  24.528  -6.937  1   33.55  ? 354 TYR A OH  1 
ATOM   2932 N N   . PHE A 1 355 ? 23.103  30.604  -7.497  1   23.08  ? 355 PHE A N   1 
ATOM   2933 C CA  . PHE A 1 355 ? 22.157  31.609  -7.039  1   24.88  ? 355 PHE A CA  1 
ATOM   2934 C C   . PHE A 1 355 ? 20.789  31.003  -6.721  1   24.54  ? 355 PHE A C   1 
ATOM   2935 O O   . PHE A 1 355 ? 20.162  31.381  -5.73   1   23.09  ? 355 PHE A O   1 
ATOM   2936 C CB  . PHE A 1 355 ? 22.059  32.795  -7.98   1   23.39  ? 355 PHE A CB  1 
ATOM   2937 C CG  . PHE A 1 355 ? 23.273  33.694  -7.936  1   22.3   ? 355 PHE A CG  1 
ATOM   2938 C CD1 . PHE A 1 355 ? 23.816  34.168  -6.737  1   22.62  ? 355 PHE A CD1 1 
ATOM   2939 C CD2 . PHE A 1 355 ? 23.926  34.048  -9.105  1   21.32  ? 355 PHE A CD2 1 
ATOM   2940 C CE1 . PHE A 1 355 ? 24.923  34.997  -6.732  1   22.9   ? 355 PHE A CE1 1 
ATOM   2941 C CE2 . PHE A 1 355 ? 25.026  34.874  -9.105  1   22.18  ? 355 PHE A CE2 1 
ATOM   2942 C CZ  . PHE A 1 355 ? 25.52   35.374  -7.897  1   23.63  ? 355 PHE A CZ  1 
ATOM   2943 N N   . LYS A 1 356 ? 20.349  30.01   -7.499  1   23.18  ? 356 LYS A N   1 
ATOM   2944 C CA  . LYS A 1 356 ? 19.153  29.249  -7.156  1   22.83  ? 356 LYS A CA  1 
ATOM   2945 C C   . LYS A 1 356 ? 19.308  28.526  -5.829  1   25.57  ? 356 LYS A C   1 
ATOM   2946 O O   . LYS A 1 356 ? 18.397  28.559  -4.977  1   25.22  ? 356 LYS A O   1 
ATOM   2947 C CB  . LYS A 1 356 ? 18.812  28.234  -8.252  1   26.04  ? 356 LYS A CB  1 
ATOM   2948 C CG  . LYS A 1 356 ? 18.127  28.931  -9.425  1   29.3   ? 356 LYS A CG  1 
ATOM   2949 C CD  . LYS A 1 356 ? 16.657  29.276  -9.152  1   31.42  ? 356 LYS A CD  1 
ATOM   2950 C CE  . LYS A 1 356 ? 16.072  29.823  -10.395 1   31.43  ? 356 LYS A CE  1 
ATOM   2951 N NZ  . LYS A 1 356 ? 14.669  30.113  -10.254 1   31.26  ? 356 LYS A NZ  1 
ATOM   2952 N N   . ALA A 1 357 ? 20.456  27.875  -5.629  1   26.46  ? 357 ALA A N   1 
ATOM   2953 C CA  . ALA A 1 357 ? 20.642  27.124  -4.393  1   26.8   ? 357 ALA A CA  1 
ATOM   2954 C C   . ALA A 1 357 ? 20.658  28.057  -3.157  1   25.89  ? 357 ALA A C   1 
ATOM   2955 O O   . ALA A 1 357 ? 20.104  27.711  -2.107  1   24.84  ? 357 ALA A O   1 
ATOM   2956 C CB  . ALA A 1 357 ? 21.872  26.26   -4.502  1   27.58  ? 357 ALA A CB  1 
ATOM   2957 N N   . SER A 1 358 ? 21.289  29.227  -3.261  1   23.49  ? 358 SER A N   1 
ATOM   2958 C CA  . SER A 1 358 ? 21.283  30.179  -2.151  1   25.54  ? 358 SER A CA  1 
ATOM   2959 C C   . SER A 1 358 ? 19.945  30.961  -2.007  1   24.83  ? 358 SER A C   1 
ATOM   2960 O O   . SER A 1 358 ? 19.778  31.704  -1.059  1   24.59  ? 358 SER A O   1 
ATOM   2961 C CB  . SER A 1 358 ? 22.448  31.11   -2.244  1   27.9   ? 358 SER A CB  1 
ATOM   2962 O OG  . SER A 1 358 ? 22.435  31.798  -3.468  1   30.5   ? 358 SER A OG  1 
ATOM   2963 N N   . GLN A 1 359 ? 19.006  30.804  -2.947  1   24.9   ? 359 GLN A N   1 
ATOM   2964 C CA  . GLN A 1 359 ? 17.748  31.507  -3.065  1   25.04  ? 359 GLN A CA  1 
ATOM   2965 C C   . GLN A 1 359 ? 18.014  33.001  -3.155  1   25.78  ? 359 GLN A C   1 
ATOM   2966 O O   . GLN A 1 359 ? 17.357  33.805  -2.476  1   24.03  ? 359 GLN A O   1 
ATOM   2967 C CB  . GLN A 1 359 ? 16.717  31.075  -2.017  1   24.82  ? 359 GLN A CB  1 
ATOM   2968 C CG  . GLN A 1 359 ? 15.287  31.285  -2.495  1   34.08  ? 359 GLN A CG  1 
ATOM   2969 C CD  . GLN A 1 359 ? 14.27   30.974  -1.426  1   36.61  ? 359 GLN A CD  1 
ATOM   2970 O OE1 . GLN A 1 359 ? 13.942  29.805  -1.181  1   39.8   ? 359 GLN A OE1 1 
ATOM   2971 N NE2 . GLN A 1 359 ? 13.867  31.996  -0.697  1   34.4   ? 359 GLN A NE2 1 
ATOM   2972 N N   . ASP A 1 360 ? 18.951  33.354  -4.033  1   21.87  ? 360 ASP A N   1 
ATOM   2973 C CA  . ASP A 1 360 ? 19.225  34.75   -4.328  1   23.63  ? 360 ASP A CA  1 
ATOM   2974 C C   . ASP A 1 360 ? 18.527  35.065  -5.657  1   25.48  ? 360 ASP A C   1 
ATOM   2975 O O   . ASP A 1 360 ? 19.066  34.783  -6.714  1   24.82  ? 360 ASP A O   1 
ATOM   2976 C CB  . ASP A 1 360 ? 20.706  35.015  -4.312  1   22.55  ? 360 ASP A CB  1 
ATOM   2977 C CG  . ASP A 1 360 ? 21.125  36.461  -4.517  1   22.03  ? 360 ASP A CG  1 
ATOM   2978 O OD1 . ASP A 1 360 ? 20.211  37.33   -4.838  1   24.52  ? 360 ASP A OD1 1 
ATOM   2979 O OD2 . ASP A 1 360 ? 22.333  36.722  -4.33   1   23.75  ? 360 ASP A OD2 1 
ATOM   2980 N N   . LYS A 1 361 ? 17.362  35.703  -5.573  1   24.72  ? 361 LYS A N   1 
ATOM   2981 C CA  . LYS A 1 361 ? 16.592  36.059  -6.757  1   26.23  ? 361 LYS A CA  1 
ATOM   2982 C C   . LYS A 1 361 ? 17.001  37.426  -7.306  1   25.46  ? 361 LYS A C   1 
ATOM   2983 O O   . LYS A 1 361 ? 16.466  37.826  -8.311  1   25.67  ? 361 LYS A O   1 
ATOM   2984 C CB  . LYS A 1 361 ? 15.115  36.064  -6.434  1   26.98  ? 361 LYS A CB  1 
ATOM   2985 C CG  . LYS A 1 361 ? 14.557  34.741  -6.013  1   28.82  ? 361 LYS A CG  1 
ATOM   2986 C CD  . LYS A 1 361 ? 13.042  34.785  -6.009  1   35.72  ? 361 LYS A CD  1 
ATOM   2987 C CE  . LYS A 1 361 ? 12.37   33.493  -6.126  1   51.13  ? 361 LYS A CE  1 
ATOM   2988 N NZ  . LYS A 1 361 ? 12.685  32.644  -4.967  1   58.32  ? 361 LYS A NZ  1 
ATOM   2989 N N   . LEU A 1 362 ? 17.91   38.136  -6.645  1   26.34  ? 362 LEU A N   1 
ATOM   2990 C CA  . LEU A 1 362 ? 18.442  39.411  -7.116  1   24.79  ? 362 LEU A CA  1 
ATOM   2991 C C   . LEU A 1 362 ? 19.673  39.192  -7.989  1   24.09  ? 362 LEU A C   1 
ATOM   2992 O O   . LEU A 1 362 ? 19.714  39.587  -9.146  1   23.97  ? 362 LEU A O   1 
ATOM   2993 C CB  . LEU A 1 362 ? 18.743  40.258  -5.875  1   27.23  ? 362 LEU A CB  1 
ATOM   2994 C CG  . LEU A 1 362 ? 19.259  41.668  -6.213  1   30.45  ? 362 LEU A CG  1 
ATOM   2995 C CD1 . LEU A 1 362 ? 18.276  42.475  -7.047  1   33.98  ? 362 LEU A CD1 1 
ATOM   2996 C CD2 . LEU A 1 362 ? 19.579  42.414  -4.998  1   32.68  ? 362 LEU A CD2 1 
ATOM   2997 N N   . SER A 1 363 ? 20.726  38.58   -7.426  1   23.26  ? 363 SER A N   1 
ATOM   2998 C CA  . SER A 1 363 ? 22.039  38.48   -8.066  1   23.44  ? 363 SER A CA  1 
ATOM   2999 C C   . SER A 1 363 ? 21.997  37.621  -9.335  1   23.92  ? 363 SER A C   1 
ATOM   3000 O O   . SER A 1 363 ? 22.842  37.781  -10.207 1   23.66  ? 363 SER A O   1 
ATOM   3001 C CB  . SER A 1 363 ? 23.108  37.956  -7.129  1   25.43  ? 363 SER A CB  1 
ATOM   3002 O OG  . SER A 1 363 ? 23.183  38.771  -5.946  1   26.3   ? 363 SER A OG  1 
ATOM   3003 N N   . ILE A 1 364 ? 21.023  36.716  -9.406  1   24.53  ? 364 ILE A N   1 
ATOM   3004 C CA  . ILE A 1 364 ? 20.861  35.771  -10.521 1   24.27  ? 364 ILE A CA  1 
ATOM   3005 C C   . ILE A 1 364 ? 20.707  36.5    -11.854 1   28.2   ? 364 ILE A C   1 
ATOM   3006 O O   . ILE A 1 364 ? 21.016  35.921  -12.888 1   25.03  ? 364 ILE A O   1 
ATOM   3007 C CB  . ILE A 1 364 ? 19.687  34.83   -10.221 1   22.31  ? 364 ILE A CB  1 
ATOM   3008 C CG1 . ILE A 1 364 ? 19.715  33.562  -11.117 1   25.2   ? 364 ILE A CG1 1 
ATOM   3009 C CG2 . ILE A 1 364 ? 18.334  35.519  -10.324 1   24     ? 364 ILE A CG2 1 
ATOM   3010 C CD1 . ILE A 1 364 ? 18.592  32.574  -10.766 1   25.1   ? 364 ILE A CD1 1 
ATOM   3011 N N   . LYS A 1 365 ? 20.249  37.759  -11.825 1   28.13  ? 365 LYS A N   1 
ATOM   3012 C CA  . LYS A 1 365 ? 20.1    38.585  -13.013 1   31.3   ? 365 LYS A CA  1 
ATOM   3013 C C   . LYS A 1 365 ? 21.425  38.728  -13.742 1   29.83  ? 365 LYS A C   1 
ATOM   3014 O O   . LYS A 1 365 ? 21.406  38.791  -14.952 1   30.93  ? 365 LYS A O   1 
ATOM   3015 C CB  . LYS A 1 365 ? 19.588  40.017  -12.736 1   35.25  ? 365 LYS A CB  1 
ATOM   3016 C CG  . LYS A 1 365 ? 18.151  40.063  -12.175 1   53.17  ? 365 LYS A CG  1 
ATOM   3017 C CD  . LYS A 1 365 ? 17.748  41.361  -11.467 1   60.95  ? 365 LYS A CD  1 
ATOM   3018 C CE  . LYS A 1 365 ? 16.574  41.24   -10.499 1   58.65  ? 365 LYS A CE  1 
ATOM   3019 N NZ  . LYS A 1 365 ? 15.971  42.537  -10.041 1   43.14  ? 365 LYS A NZ  1 
ATOM   3020 N N   . MET A 1 366 ? 22.563  38.767  -13.037 1   27.39  ? 366 MET A N   1 
ATOM   3021 C CA  . MET A 1 366 ? 23.838  39.009  -13.673 1   30.61  ? 366 MET A CA  1 
ATOM   3022 C C   . MET A 1 366 ? 24.164  37.916  -14.684 1   29.2   ? 366 MET A C   1 
ATOM   3023 O O   . MET A 1 366 ? 24.358  38.249  -15.863 1   27.79  ? 366 MET A O   1 
ATOM   3024 C CB  . MET A 1 366 ? 24.99   39.133  -12.676 1   32.31  ? 366 MET A CB  1 
ATOM   3025 C CG  . MET A 1 366 ? 24.814  40.218  -11.637 1   36.52  ? 366 MET A CG  1 
ATOM   3026 S SD  . MET A 1 366 ? 26.31   40.236  -10.64  1   36.01  ? 366 MET A SD  1 
ATOM   3027 C CE  . MET A 1 366 ? 26.483  38.568  -10.003 1   33.34  ? 366 MET A CE  1 
ATOM   3028 N N   . PRO A 1 367 ? 24.269  36.613  -14.322 1   24.22  ? 367 PRO A N   1 
ATOM   3029 C CA  . PRO A 1 367 ? 24.547  35.581  -15.315 1   26.26  ? 367 PRO A CA  1 
ATOM   3030 C C   . PRO A 1 367 ? 23.439  35.435  -16.347 1   26.88  ? 367 PRO A C   1 
ATOM   3031 O O   . PRO A 1 367 ? 23.751  35.081  -17.476 1   28.19  ? 367 PRO A O   1 
ATOM   3032 C CB  . PRO A 1 367 ? 24.789  34.292  -14.509 1   24.12  ? 367 PRO A CB  1 
ATOM   3033 C CG  . PRO A 1 367 ? 24.034  34.572  -13.217 1   22.99  ? 367 PRO A CG  1 
ATOM   3034 C CD  . PRO A 1 367 ? 24.288  36.037  -12.968 1   24.7   ? 367 PRO A CD  1 
ATOM   3035 N N   . LEU A 1 368 ? 22.185  35.722  -15.982 1   26.94  ? 368 LEU A N   1 
ATOM   3036 C CA  . LEU A 1 368 ? 21.089  35.599  -16.956 1   28.84  ? 368 LEU A CA  1 
ATOM   3037 C C   . LEU A 1 368 ? 21.234  36.64   -18.071 1   30.94  ? 368 LEU A C   1 
ATOM   3038 O O   . LEU A 1 368 ? 21.018  36.33   -19.222 1   29.44  ? 368 LEU A O   1 
ATOM   3039 C CB  . LEU A 1 368 ? 19.733  35.74   -16.273 1   27.59  ? 368 LEU A CB  1 
ATOM   3040 C CG  . LEU A 1 368 ? 19.373  34.612  -15.304 1   26.03  ? 368 LEU A CG  1 
ATOM   3041 C CD1 . LEU A 1 368 ? 18.156  34.971  -14.562 1   28.57  ? 368 LEU A CD1 1 
ATOM   3042 C CD2 . LEU A 1 368 ? 19.212  33.299  -16.014 1   28.27  ? 368 LEU A CD2 1 
ATOM   3043 N N   . ILE A 1 369 ? 21.578  37.872  -17.74  1   28.91  ? 369 ILE A N   1 
ATOM   3044 C CA  . ILE A 1 369 ? 21.908  38.885  -18.74  1   31.43  ? 369 ILE A CA  1 
ATOM   3045 C C   . ILE A 1 369 ? 22.975  38.401  -19.715 1   32.01  ? 369 ILE A C   1 
ATOM   3046 O O   . ILE A 1 369 ? 22.831  38.604  -20.921 1   31.44  ? 369 ILE A O   1 
ATOM   3047 C CB  . ILE A 1 369 ? 22.297  40.213  -18.07  1   32.99  ? 369 ILE A CB  1 
ATOM   3048 C CG1 . ILE A 1 369 ? 21.076  40.864  -17.451 1   34.83  ? 369 ILE A CG1 1 
ATOM   3049 C CG2 . ILE A 1 369 ? 23.007  41.17   -19.06  1   38.09  ? 369 ILE A CG2 1 
ATOM   3050 C CD1 . ILE A 1 369 ? 21.379  41.966  -16.45  1   37.48  ? 369 ILE A CD1 1 
ATOM   3051 N N   . GLN A 1 370 ? 24.051  37.765  -19.215 1   28.91  ? 370 GLN A N   1 
ATOM   3052 C CA  . GLN A 1 370 ? 25.124  37.316  -20.08  1   29.47  ? 370 GLN A CA  1 
ATOM   3053 C C   . GLN A 1 370 ? 24.645  36.163  -20.961 1   31.22  ? 370 GLN A C   1 
ATOM   3054 O O   . GLN A 1 370 ? 24.991  36.063  -22.153 1   31.69  ? 370 GLN A O   1 
ATOM   3055 C CB  . GLN A 1 370 ? 26.365  36.906  -19.294 1   30.71  ? 370 GLN A CB  1 
ATOM   3056 C CG  . GLN A 1 370 ? 27.013  38.061  -18.519 1   28.63  ? 370 GLN A CG  1 
ATOM   3057 C CD  . GLN A 1 370 ? 27.418  39.238  -19.385 1   32.18  ? 370 GLN A CD  1 
ATOM   3058 O OE1 . GLN A 1 370 ? 27.071  40.39   -19.14  1   36.49  ? 370 GLN A OE1 1 
ATOM   3059 N NE2 . GLN A 1 370 ? 28.12   38.925  -20.415 1   28.93  ? 370 GLN A NE2 1 
ATOM   3060 N N   . LEU A 1 371 ? 23.826  35.267  -20.403 1   28.57  ? 371 LEU A N   1 
ATOM   3061 C CA  . LEU A 1 371 ? 23.275  34.201  -21.251 1   28.77  ? 371 LEU A CA  1 
ATOM   3062 C C   . LEU A 1 371 ? 22.348  34.756  -22.344 1   28.45  ? 371 LEU A C   1 
ATOM   3063 O O   . LEU A 1 371 ? 22.372  34.25   -23.466 1   32.28  ? 371 LEU A O   1 
ATOM   3064 C CB  . LEU A 1 371 ? 22.591  33.171  -20.368 1   27.33  ? 371 LEU A CB  1 
ATOM   3065 C CG  . LEU A 1 371 ? 23.516  32.344  -19.476 1   26.79  ? 371 LEU A CG  1 
ATOM   3066 C CD1 . LEU A 1 371 ? 22.724  31.591  -18.423 1   26.77  ? 371 LEU A CD1 1 
ATOM   3067 C CD2 . LEU A 1 371 ? 24.308  31.395  -20.289 1   30.37  ? 371 LEU A CD2 1 
ATOM   3068 N N   . GLU A 1 372 ? 21.569  35.807  -22.046 1   32.86  ? 372 GLU A N   1 
ATOM   3069 C CA  . GLU A 1 372 ? 20.745  36.44   -23.081 1   39.58  ? 372 GLU A CA  1 
ATOM   3070 C C   . GLU A 1 372 ? 21.609  37.031  -24.205 1   42.09  ? 372 GLU A C   1 
ATOM   3071 O O   . GLU A 1 372 ? 21.28   36.913  -25.387 1   36.11  ? 372 GLU A O   1 
ATOM   3072 C CB  . GLU A 1 372 ? 19.887  37.54   -22.466 1   42.82  ? 372 GLU A CB  1 
ATOM   3073 C CG  . GLU A 1 372 ? 18.815  38.046  -23.431 1   50.94  ? 372 GLU A CG  1 
ATOM   3074 C CD  . GLU A 1 372 ? 18.064  39.26   -22.919 1   61.94  ? 372 GLU A CD  1 
ATOM   3075 O OE1 . GLU A 1 372 ? 16.868  39.156  -22.57  1   70.09  ? 372 GLU A OE1 1 
ATOM   3076 O OE2 . GLU A 1 372 ? 18.707  40.335  -22.907 1   74.48  ? 372 GLU A OE2 1 
ATOM   3077 N N   . LYS A 1 373 ? 22.733  37.651  -23.843 1   40.13  ? 373 LYS A N   1 
ATOM   3078 C CA  . LYS A 1 373 ? 23.694  38.171  -24.817 1   45.28  ? 373 LYS A CA  1 
ATOM   3079 C C   . LYS A 1 373 ? 24.352  37.069  -25.632 1   39.02  ? 373 LYS A C   1 
ATOM   3080 O O   . LYS A 1 373 ? 24.745  37.318  -26.747 1   44.65  ? 373 LYS A O   1 
ATOM   3081 C CB  . LYS A 1 373 ? 24.819  38.984  -24.157 1   46.02  ? 373 LYS A CB  1 
ATOM   3082 C CG  . LYS A 1 373 ? 24.295  40.313  -23.648 1   57.85  ? 373 LYS A CG  1 
ATOM   3083 C CD  . LYS A 1 373 ? 25.315  41.257  -23.014 1   66.34  ? 373 LYS A CD  1 
ATOM   3084 C CE  . LYS A 1 373 ? 24.935  42.696  -23.233 1   75.91  ? 373 LYS A CE  1 
ATOM   3085 N NZ  . LYS A 1 373 ? 25.358  43.551  -22.122 1   82.27  ? 373 LYS A NZ  1 
ATOM   3086 N N   . MET A 1 374 ? 24.484  35.861  -25.077 1   36.43  ? 374 MET A N   1 
ATOM   3087 C CA  . MET A 1 374 ? 25.06   34.728  -25.779 1   39.02  ? 374 MET A CA  1 
ATOM   3088 C C   . MET A 1 374 ? 24.005  33.925  -26.558 1   40     ? 374 MET A C   1 
ATOM   3089 O O   . MET A 1 374 ? 24.31   32.824  -27.017 1   39.6   ? 374 MET A O   1 
ATOM   3090 C CB  . MET A 1 374 ? 25.829  33.823  -24.814 1   38.24  ? 374 MET A CB  1 
ATOM   3091 C CG  . MET A 1 374 ? 27.011  34.568  -24.171 1   44.52  ? 374 MET A CG  1 
ATOM   3092 S SD  . MET A 1 374 ? 27.675  33.714  -22.735 1   47.99  ? 374 MET A SD  1 
ATOM   3093 C CE  . MET A 1 374 ? 28.908  32.637  -23.45  1   47.81  ? 374 MET A CE  1 
ATOM   3094 N N   . GLY A 1 375 ? 22.783  34.47   -26.735 1   37.66  ? 375 GLY A N   1 
ATOM   3095 C CA  . GLY A 1 375 ? 21.781  33.851  -27.602 1   37.49  ? 375 GLY A CA  1 
ATOM   3096 C C   . GLY A 1 375 ? 20.878  32.809  -26.925 1   37.63  ? 375 GLY A C   1 
ATOM   3097 O O   . GLY A 1 375 ? 20.131  32.132  -27.629 1   35.9   ? 375 GLY A O   1 
ATOM   3098 N N   . GLU A 1 376 ? 20.894  32.664  -25.579 1   31.96  ? 376 GLU A N   1 
ATOM   3099 C CA  . GLU A 1 376 ? 19.942  31.747  -24.95  1   33.74  ? 376 GLU A CA  1 
ATOM   3100 C C   . GLU A 1 376 ? 18.542  32.375  -24.975 1   35.93  ? 376 GLU A C   1 
ATOM   3101 O O   . GLU A 1 376 ? 18.402  33.612  -24.967 1   31.48  ? 376 GLU A O   1 
ATOM   3102 C CB  . GLU A 1 376 ? 20.416  31.435  -23.523 1   32.28  ? 376 GLU A CB  1 
ATOM   3103 C CG  . GLU A 1 376 ? 21.675  30.56   -23.492 1   32.37  ? 376 GLU A CG  1 
ATOM   3104 C CD  . GLU A 1 376 ? 21.541  29.181  -24.071 1   38.62  ? 376 GLU A CD  1 
ATOM   3105 O OE1 . GLU A 1 376 ? 22.414  28.712  -24.802 1   44.25  ? 376 GLU A OE1 1 
ATOM   3106 O OE2 . GLU A 1 376 ? 20.515  28.546  -23.771 1   46.92  ? 376 GLU A OE2 1 
ATOM   3107 N N   . ASN A 1 377 ? 17.514  31.506  -25.01  1   38.7   ? 377 ASN A N   1 
ATOM   3108 C CA  . ASN A 1 377 ? 16.132  31.9    -25.221 1   37.15  ? 377 ASN A CA  1 
ATOM   3109 C C   . ASN A 1 377 ? 15.699  32.845  -24.099 1   33.93  ? 377 ASN A C   1 
ATOM   3110 O O   . ASN A 1 377 ? 15.623  32.425  -22.94  1   34.99  ? 377 ASN A O   1 
ATOM   3111 C CB  . ASN A 1 377 ? 15.188  30.686  -25.302 1   36.99  ? 377 ASN A CB  1 
ATOM   3112 C CG  . ASN A 1 377 ? 13.763  31.087  -25.626 1   40.51  ? 377 ASN A CG  1 
ATOM   3113 O OD1 . ASN A 1 377 ? 13.38   32.259  -25.503 1   42.7   ? 377 ASN A OD1 1 
ATOM   3114 N ND2 . ASN A 1 377 ? 12.95   30.17   -26.12  1   42.24  ? 377 ASN A ND2 1 
ATOM   3115 N N   . PRO A 1 378 ? 15.357  34.133  -24.383 1   33.17  ? 378 PRO A N   1 
ATOM   3116 C CA  . PRO A 1 378 ? 14.96   35.071  -23.334 1   34.02  ? 378 PRO A CA  1 
ATOM   3117 C C   . PRO A 1 378 ? 13.738  34.633  -22.523 1   31.04  ? 378 PRO A C   1 
ATOM   3118 O O   . PRO A 1 378 ? 13.619  35.002  -21.358 1   33.01  ? 378 PRO A O   1 
ATOM   3119 C CB  . PRO A 1 378 ? 14.681  36.376  -24.124 1   38.45  ? 378 PRO A CB  1 
ATOM   3120 C CG  . PRO A 1 378 ? 15.514  36.233  -25.363 1   39.5   ? 378 PRO A CG  1 
ATOM   3121 C CD  . PRO A 1 378 ? 15.4    34.78   -25.709 1   38.62  ? 378 PRO A CD  1 
ATOM   3122 N N   . ARG A 1 379 ? 12.83   33.897  -23.154 1   31.8   ? 379 ARG A N   1 
ATOM   3123 C CA  . ARG A 1 379 ? 11.639  33.423  -22.477 1   33     ? 379 ARG A CA  1 
ATOM   3124 C C   . ARG A 1 379 ? 12.011  32.5    -21.311 1   31     ? 379 ARG A C   1 
ATOM   3125 O O   . ARG A 1 379 ? 11.42   32.628  -20.241 1   31.36  ? 379 ARG A O   1 
ATOM   3126 C CB  . ARG A 1 379 ? 10.701  32.749  -23.47  1   34.25  ? 379 ARG A CB  1 
ATOM   3127 C CG  . ARG A 1 379 ? 9.328   32.368  -22.945 1   35.35  ? 379 ARG A CG  1 
ATOM   3128 C CD  . ARG A 1 379 ? 8.603   33.523  -22.26  1   38.53  ? 379 ARG A CD  1 
ATOM   3129 N NE  . ARG A 1 379 ? 7.189   33.279  -21.95  1   39.12  ? 379 ARG A NE  1 
ATOM   3130 C CZ  . ARG A 1 379 ? 6.244   33.124  -22.823 1   38     ? 379 ARG A CZ  1 
ATOM   3131 N NH1 . ARG A 1 379 ? 6.453   33.282  -24.133 1   40.32  ? 379 ARG A NH1 1 
ATOM   3132 N NH2 . ARG A 1 379 ? 5.039   32.863  -22.376 1   40.86  ? 379 ARG A NH2 1 
ATOM   3133 N N   . LEU A 1 380 ? 12.94   31.558  -21.559 1   33.17  ? 380 LEU A N   1 
ATOM   3134 C CA  . LEU A 1 380 ? 13.408  30.652  -20.516 1   33.17  ? 380 LEU A CA  1 
ATOM   3135 C C   . LEU A 1 380 ? 14.149  31.413  -19.436 1   32.36  ? 380 LEU A C   1 
ATOM   3136 O O   . LEU A 1 380 ? 13.893  31.159  -18.253 1   29.87  ? 380 LEU A O   1 
ATOM   3137 C CB  . LEU A 1 380 ? 14.24   29.488  -21.033 1   35.51  ? 380 LEU A CB  1 
ATOM   3138 C CG  . LEU A 1 380 ? 13.541  28.538  -21.997 1   38.84  ? 380 LEU A CG  1 
ATOM   3139 C CD1 . LEU A 1 380 ? 14.509  27.509  -22.465 1   42.13  ? 380 LEU A CD1 1 
ATOM   3140 C CD2 . LEU A 1 380 ? 12.301  27.889  -21.439 1   41.9   ? 380 LEU A CD2 1 
ATOM   3141 N N   . LEU A 1 381 ? 14.958  32.408  -19.817 1   27.46  ? 381 LEU A N   1 
ATOM   3142 C CA  . LEU A 1 381 ? 15.65   33.243  -18.844 1   28.99  ? 381 LEU A CA  1 
ATOM   3143 C C   . LEU A 1 381 ? 14.656  34.038  -17.982 1   30.21  ? 381 LEU A C   1 
ATOM   3144 O O   . LEU A 1 381 ? 14.845  34.173  -16.771 1   30     ? 381 LEU A O   1 
ATOM   3145 C CB  . LEU A 1 381 ? 16.688  34.138  -19.529 1   29.25  ? 381 LEU A CB  1 
ATOM   3146 C CG  . LEU A 1 381 ? 17.7    33.407  -20.412 1   32.19  ? 381 LEU A CG  1 
ATOM   3147 C CD1 . LEU A 1 381 ? 18.553  34.414  -21.163 1   35.24  ? 381 LEU A CD1 1 
ATOM   3148 C CD2 . LEU A 1 381 ? 18.557  32.422  -19.708 1   32.04  ? 381 LEU A CD2 1 
ATOM   3149 N N   . LYS A 1 382 ? 13.549  34.492  -18.563 1   29.05  ? 382 LYS A N   1 
ATOM   3150 C CA  . LYS A 1 382 ? 12.534  35.189  -17.795 1   30.52  ? 382 LYS A CA  1 
ATOM   3151 C C   . LYS A 1 382 ? 11.833  34.252  -16.81  1   26.5   ? 382 LYS A C   1 
ATOM   3152 O O   . LYS A 1 382 ? 11.677  34.601  -15.64  1   29.81  ? 382 LYS A O   1 
ATOM   3153 C CB  . LYS A 1 382 ? 11.517  35.807  -18.748 1   33.66  ? 382 LYS A CB  1 
ATOM   3154 C CG  . LYS A 1 382 ? 10.424  36.645  -18.122 1   38.87  ? 382 LYS A CG  1 
ATOM   3155 C CD  . LYS A 1 382 ? 9.518   37.124  -19.27  1   52.96  ? 382 LYS A CD  1 
ATOM   3156 C CE  . LYS A 1 382 ? 8.137   37.498  -18.844 1   62.35  ? 382 LYS A CE  1 
ATOM   3157 N NZ  . LYS A 1 382 ? 8.136   38.583  -17.87  1   62.16  ? 382 LYS A NZ  1 
ATOM   3158 N N   . ILE A 1 383 ? 11.543  33.035  -17.24  1   27.08  ? 383 ILE A N   1 
ATOM   3159 C CA  . ILE A 1 383 ? 10.909  32.052  -16.369 1   27.91  ? 383 ILE A CA  1 
ATOM   3160 C C   . ILE A 1 383 ? 11.814  31.751  -15.166 1   28.24  ? 383 ILE A C   1 
ATOM   3161 O O   . ILE A 1 383 ? 11.3    31.61   -14.033 1   29.9   ? 383 ILE A O   1 
ATOM   3162 C CB  . ILE A 1 383 ? 10.5    30.802  -17.159 1   27.34  ? 383 ILE A CB  1 
ATOM   3163 C CG1 . ILE A 1 383 ? 9.404   31.13   -18.121 1   28.69  ? 383 ILE A CG1 1 
ATOM   3164 C CG2 . ILE A 1 383 ? 10.121  29.662  -16.196 1   28.91  ? 383 ILE A CG2 1 
ATOM   3165 C CD1 . ILE A 1 383 ? 9.106   30.051  -19.111 1   29.61  ? 383 ILE A CD1 1 
ATOM   3166 N N   . ILE A 1 384 ? 13.138  31.701  -15.392 1   29.05  ? 384 ILE A N   1 
ATOM   3167 C CA  . ILE A 1 384 ? 14.114  31.427  -14.344 1   28.73  ? 384 ILE A CA  1 
ATOM   3168 C C   . ILE A 1 384 ? 14.105  32.518  -13.268 1   29.89  ? 384 ILE A C   1 
ATOM   3169 O O   . ILE A 1 384 ? 14.395  32.214  -12.099 1   29.88  ? 384 ILE A O   1 
ATOM   3170 C CB  . ILE A 1 384 ? 15.511  31.162  -14.955 1   28.04  ? 384 ILE A CB  1 
ATOM   3171 C CG1 . ILE A 1 384 ? 15.504  29.841  -15.717 1   29.5   ? 384 ILE A CG1 1 
ATOM   3172 C CG2 . ILE A 1 384 ? 16.607  31.182  -13.882 1   29.16  ? 384 ILE A CG2 1 
ATOM   3173 C CD1 . ILE A 1 384 ? 16.756  29.542  -16.508 1   30.43  ? 384 ILE A CD1 1 
ATOM   3174 N N   . THR A 1 385 ? 13.705  33.755  -13.612 1   30.28  ? 385 THR A N   1 
ATOM   3175 C CA  . THR A 1 385 ? 13.619  34.828  -12.623 1   31.73  ? 385 THR A CA  1 
ATOM   3176 C C   . THR A 1 385 ? 12.375  34.724  -11.738 1   34.73  ? 385 THR A C   1 
ATOM   3177 O O   . THR A 1 385 ? 12.367  35.385  -10.716 1   37.97  ? 385 THR A O   1 
ATOM   3178 C CB  . THR A 1 385 ? 13.7    36.21   -13.295 1   33.47  ? 385 THR A CB  1 
ATOM   3179 O OG1 . THR A 1 385 ? 12.469  36.399  -13.98  1   40.29  ? 385 THR A OG1 1 
ATOM   3180 C CG2 . THR A 1 385 ? 14.898  36.352  -14.213 1   32.27  ? 385 THR A CG2 1 
ATOM   3181 N N   . MET A 1 386 ? 11.353  33.909  -12.049 1   36.03  ? 386 MET A N   1 
ATOM   3182 C CA  . MET A 1 386 ? 10.06   33.963  -11.363 1   37.42  ? 386 MET A CA  1 
ATOM   3183 C C   . MET A 1 386 ? 10.087  33.439  -9.893  1   39.72  ? 386 MET A C   1 
ATOM   3184 O O   . MET A 1 386 ? 10.89   32.478  -9.67   1   46.51  ? 386 MET A O   1 
ATOM   3185 C CB  . MET A 1 386 ? 9.018   33.156  -12.134 1   36.4   ? 386 MET A CB  1 
ATOM   3186 C CG  . MET A 1 386 ? 8.597   33.748  -13.483 1   34.82  ? 386 MET A CG  1 
ATOM   3187 S SD  . MET A 1 386 ? 7.476   32.597  -14.331 1   35.52  ? 386 MET A SD  1 
ATOM   3188 C CE  . MET A 1 386 ? 5.904   32.936  -13.524 1   40.32  ? 386 MET A CE  1 
ATOM   3189 N N   . MET B 1 1   ? -34.04  11.18   25.658  1   83.25  ? 1   MET B N   1 
ATOM   3190 C CA  . MET B 1 1   ? -32.754 10.436  25.726  1   79.62  ? 1   MET B CA  1 
ATOM   3191 C C   . MET B 1 1   ? -32.199 10.29   24.305  1   71.83  ? 1   MET B C   1 
ATOM   3192 O O   . MET B 1 1   ? -32.935 10.058  23.35   1   71.11  ? 1   MET B O   1 
ATOM   3193 C CB  . MET B 1 1   ? -32.94  9.07    26.413  1   77.77  ? 1   MET B CB  1 
ATOM   3194 C CG  . MET B 1 1   ? -31.647 8.454   26.944  1   79.71  ? 1   MET B CG  1 
ATOM   3195 S SD  . MET B 1 1   ? -31.813 7.263   28.291  1   98.18  ? 1   MET B SD  1 
ATOM   3196 C CE  . MET B 1 1   ? -32.372 5.676   27.652  1   96.12  ? 1   MET B CE  1 
ATOM   3197 N N   . GLU B 1 2   ? -30.879 10.393  24.165  1   69.65  ? 2   GLU B N   1 
ATOM   3198 C CA  . GLU B 1 2   ? -30.242 10.269  22.853  1   66.94  ? 2   GLU B CA  1 
ATOM   3199 C C   . GLU B 1 2   ? -30.155 8.774   22.5    1   63.19  ? 2   GLU B C   1 
ATOM   3200 O O   . GLU B 1 2   ? -30.171 7.916   23.385  1   59.4   ? 2   GLU B O   1 
ATOM   3201 C CB  . GLU B 1 2   ? -28.954 11.091  22.748  1   68.79  ? 2   GLU B CB  1 
ATOM   3202 C CG  . GLU B 1 2   ? -28.05  11.12   23.981  1   70.05  ? 2   GLU B CG  1 
ATOM   3203 C CD  . GLU B 1 2   ? -28.405 12.071  25.108  1   65.69  ? 2   GLU B CD  1 
ATOM   3204 O OE1 . GLU B 1 2   ? -29.137 11.587  25.986  1   69.36  ? 2   GLU B OE1 1 
ATOM   3205 O OE2 . GLU B 1 2   ? -27.954 13.219  25.181  1   60.13  ? 2   GLU B OE2 1 
ATOM   3206 N N   . LEU B 1 3   ? -30.145 8.476   21.199  1   58.55  ? 3   LEU B N   1 
ATOM   3207 C CA  . LEU B 1 3   ? -30.26  7.117   20.675  1   60.61  ? 3   LEU B CA  1 
ATOM   3208 C C   . LEU B 1 3   ? -29.096 6.238   21.141  1   60.53  ? 3   LEU B C   1 
ATOM   3209 O O   . LEU B 1 3   ? -29.289 5.055   21.405  1   63.1   ? 3   LEU B O   1 
ATOM   3210 C CB  . LEU B 1 3   ? -30.343 7.11    19.146  1   60.23  ? 3   LEU B CB  1 
ATOM   3211 C CG  . LEU B 1 3   ? -31.602 7.708   18.507  1   62.49  ? 3   LEU B CG  1 
ATOM   3212 C CD1 . LEU B 1 3   ? -31.406 7.909   16.998  1   62.59  ? 3   LEU B CD1 1 
ATOM   3213 C CD2 . LEU B 1 3   ? -32.837 6.845   18.813  1   65.85  ? 3   LEU B CD2 1 
ATOM   3214 N N   . ILE B 1 4   ? -27.893 6.811   21.223  1   56.28  ? 4   ILE B N   1 
ATOM   3215 C CA  . ILE B 1 4   ? -26.697 6.101   21.664  1   55.53  ? 4   ILE B CA  1 
ATOM   3216 C C   . ILE B 1 4   ? -26.902 5.55    23.077  1   57.07  ? 4   ILE B C   1 
ATOM   3217 O O   . ILE B 1 4   ? -26.588 4.388   23.302  1   58.92  ? 4   ILE B O   1 
ATOM   3218 C CB  . ILE B 1 4   ? -25.405 6.951   21.532  1   52.86  ? 4   ILE B CB  1 
ATOM   3219 C CG1 . ILE B 1 4   ? -24.129 6.166   21.873  1   51.58  ? 4   ILE B CG1 1 
ATOM   3220 C CG2 . ILE B 1 4   ? -25.457 8.23    22.379  1   53.38  ? 4   ILE B CG2 1 
ATOM   3221 C CD1 . ILE B 1 4   ? -23.982 4.833   21.159  1   56.2   ? 4   ILE B CD1 1 
ATOM   3222 N N   . ARG B 1 5   ? -27.461 6.354   23.993  1   57.2   ? 5   ARG B N   1 
ATOM   3223 C CA  . ARG B 1 5   ? -27.708 5.94    25.369  1   62.7   ? 5   ARG B CA  1 
ATOM   3224 C C   . ARG B 1 5   ? -28.722 4.801   25.431  1   62.5   ? 5   ARG B C   1 
ATOM   3225 O O   . ARG B 1 5   ? -28.512 3.889   26.222  1   59.62  ? 5   ARG B O   1 
ATOM   3226 C CB  . ARG B 1 5   ? -28.086 7.129   26.267  1   65.2   ? 5   ARG B CB  1 
ATOM   3227 C CG  . ARG B 1 5   ? -26.827 7.885   26.667  1   65.42  ? 5   ARG B CG  1 
ATOM   3228 C CD  . ARG B 1 5   ? -27.097 9.258   27.241  1   65.75  ? 5   ARG B CD  1 
ATOM   3229 N NE  . ARG B 1 5   ? -27.554 9.178   28.623  1   64.69  ? 5   ARG B NE  1 
ATOM   3230 C CZ  . ARG B 1 5   ? -28.569 9.842   29.194  1   68.81  ? 5   ARG B CZ  1 
ATOM   3231 N NH1 . ARG B 1 5   ? -28.928 9.536   30.424  1   64.41  ? 5   ARG B NH1 1 
ATOM   3232 N NH2 . ARG B 1 5   ? -29.246 10.78   28.548  1   66.61  ? 5   ARG B NH2 1 
ATOM   3233 N N   . ILE B 1 6   ? -29.764 4.841   24.579  1   64.73  ? 6   ILE B N   1 
ATOM   3234 C CA  . ILE B 1 6   ? -30.793 3.811   24.523  1   66.52  ? 6   ILE B CA  1 
ATOM   3235 C C   . ILE B 1 6   ? -30.15  2.492   24.088  1   66.31  ? 6   ILE B C   1 
ATOM   3236 O O   . ILE B 1 6   ? -30.388 1.461   24.736  1   65.09  ? 6   ILE B O   1 
ATOM   3237 C CB  . ILE B 1 6   ? -31.985 4.211   23.617  1   69.21  ? 6   ILE B CB  1 
ATOM   3238 C CG1 . ILE B 1 6   ? -32.791 5.382   24.198  1   71.36  ? 6   ILE B CG1 1 
ATOM   3239 C CG2 . ILE B 1 6   ? -32.907 3.009   23.346  1   71.07  ? 6   ILE B CG2 1 
ATOM   3240 C CD1 . ILE B 1 6   ? -33.726 6.085   23.219  1   71.99  ? 6   ILE B CD1 1 
ATOM   3241 N N   . ALA B 1 7   ? -29.375 2.527   22.988  1   61.31  ? 7   ALA B N   1 
ATOM   3242 C CA  . ALA B 1 7   ? -28.759 1.326   22.439  1   60.21  ? 7   ALA B CA  1 
ATOM   3243 C C   . ALA B 1 7   ? -27.789 0.676   23.433  1   60.65  ? 7   ALA B C   1 
ATOM   3244 O O   . ALA B 1 7   ? -27.81  -0.544  23.611  1   58.53  ? 7   ALA B O   1 
ATOM   3245 C CB  . ALA B 1 7   ? -28.08  1.664   21.144  1   59.55  ? 7   ALA B CB  1 
ATOM   3246 N N   . MET B 1 8   ? -26.967 1.501   24.1    1   59.34  ? 8   MET B N   1 
ATOM   3247 C CA  . MET B 1 8   ? -25.966 1.014   25.042  1   59.36  ? 8   MET B CA  1 
ATOM   3248 C C   . MET B 1 8   ? -26.61  0.314   26.236  1   61.81  ? 8   MET B C   1 
ATOM   3249 O O   . MET B 1 8   ? -26.137 -0.74   26.635  1   58.64  ? 8   MET B O   1 
ATOM   3250 C CB  . MET B 1 8   ? -25.033 2.132   25.517  1   59.63  ? 8   MET B CB  1 
ATOM   3251 C CG  . MET B 1 8   ? -24.035 2.564   24.427  1   58.94  ? 8   MET B CG  1 
ATOM   3252 S SD  . MET B 1 8   ? -22.876 3.86    24.934  1   58.65  ? 8   MET B SD  1 
ATOM   3253 C CE  . MET B 1 8   ? -24.117 5.08    25.343  1   69.46  ? 8   MET B CE  1 
ATOM   3254 N N   . LYS B 1 9   ? -27.701 0.868   26.766  1   64.19  ? 9   LYS B N   1 
ATOM   3255 C CA  . LYS B 1 9   ? -28.451 0.226   27.843  1   67.88  ? 9   LYS B CA  1 
ATOM   3256 C C   . LYS B 1 9   ? -29.039 -1.12   27.425  1   66.72  ? 9   LYS B C   1 
ATOM   3257 O O   . LYS B 1 9   ? -28.864 -2.092  28.153  1   76.98  ? 9   LYS B O   1 
ATOM   3258 C CB  . LYS B 1 9   ? -29.556 1.171   28.311  1   70.47  ? 9   LYS B CB  1 
ATOM   3259 C CG  . LYS B 1 9   ? -28.99  2.336   29.059  1   70.9   ? 9   LYS B CG  1 
ATOM   3260 C CD  . LYS B 1 9   ? -30.085 3.341   29.36   1   75.45  ? 9   LYS B CD  1 
ATOM   3261 C CE  . LYS B 1 9   ? -29.52  4.475   30.133  1   78.33  ? 9   LYS B CE  1 
ATOM   3262 N NZ  . LYS B 1 9   ? -30.563 5.205   30.85   1   84.63  ? 9   LYS B NZ  1 
ATOM   3263 N N   . LYS B 1 10  ? -29.769 -1.154  26.295  1   68.91  ? 10  LYS B N   1 
ATOM   3264 C CA  . LYS B 1 10  ? -30.273 -2.367  25.644  1   75.32  ? 10  LYS B CA  1 
ATOM   3265 C C   . LYS B 1 10  ? -29.195 -3.453  25.602  1   74.51  ? 10  LYS B C   1 
ATOM   3266 O O   . LYS B 1 10  ? -29.43  -4.562  26.087  1   77.82  ? 10  LYS B O   1 
ATOM   3267 C CB  . LYS B 1 10  ? -30.753 -2.133  24.194  1   79.16  ? 10  LYS B CB  1 
ATOM   3268 C CG  . LYS B 1 10  ? -32.228 -1.864  23.945  1   83.8   ? 10  LYS B CG  1 
ATOM   3269 C CD  . LYS B 1 10  ? -33.027 -3.088  23.497  1   89.05  ? 10  LYS B CD  1 
ATOM   3270 C CE  . LYS B 1 10  ? -34.454 -2.959  23.94   1   91.4   ? 10  LYS B CE  1 
ATOM   3271 N NZ  . LYS B 1 10  ? -35.288 -4.069  23.491  1   93.74  ? 10  LYS B NZ  1 
ATOM   3272 N N   . ASP B 1 11  ? -28.025 -3.102  25.036  1   70.58  ? 11  ASP B N   1 
ATOM   3273 C CA  . ASP B 1 11  ? -26.927 -4.034  24.808  1   70.13  ? 11  ASP B CA  1 
ATOM   3274 C C   . ASP B 1 11  ? -26.274 -4.431  26.132  1   71.11  ? 11  ASP B C   1 
ATOM   3275 O O   . ASP B 1 11  ? -25.931 -5.603  26.288  1   69.71  ? 11  ASP B O   1 
ATOM   3276 C CB  . ASP B 1 11  ? -25.926 -3.493  23.793  1   69.08  ? 11  ASP B CB  1 
ATOM   3277 C CG  . ASP B 1 11  ? -26.386 -3.452  22.337  1   70.54  ? 11  ASP B CG  1 
ATOM   3278 O OD1 . ASP B 1 11  ? -27.375 -4.121  21.991  1   75.5   ? 11  ASP B OD1 1 
ATOM   3279 O OD2 . ASP B 1 11  ? -25.775 -2.711  21.552  1   63.69  ? 11  ASP B OD2 1 
ATOM   3280 N N   . LEU B 1 12  ? -26.138 -3.478  27.075  1   69.26  ? 12  LEU B N   1 
ATOM   3281 C CA  . LEU B 1 12  ? -25.517 -3.722  28.37   1   72.47  ? 12  LEU B CA  1 
ATOM   3282 C C   . LEU B 1 12  ? -26.372 -4.641  29.264  1   79.56  ? 12  LEU B C   1 
ATOM   3283 O O   . LEU B 1 12  ? -25.796 -5.388  30.059  1   80.59  ? 12  LEU B O   1 
ATOM   3284 C CB  . LEU B 1 12  ? -25.206 -2.371  29.024  1   70.71  ? 12  LEU B CB  1 
ATOM   3285 C CG  . LEU B 1 12  ? -24.496 -2.382  30.385  1   71.78  ? 12  LEU B CG  1 
ATOM   3286 C CD1 . LEU B 1 12  ? -23.097 -2.974  30.324  1   70.96  ? 12  LEU B CD1 1 
ATOM   3287 C CD2 . LEU B 1 12  ? -24.439 -0.963  30.93   1   71.39  ? 12  LEU B CD2 1 
ATOM   3288 N N   . GLU B 1 13  ? -27.715 -4.594  29.187  1   84.16  ? 13  GLU B N   1 
ATOM   3289 C CA  . GLU B 1 13  ? -28.528 -5.471  30.037  1   91.26  ? 13  GLU B CA  1 
ATOM   3290 C C   . GLU B 1 13  ? -28.357 -6.934  29.607  1   93.31  ? 13  GLU B C   1 
ATOM   3291 O O   . GLU B 1 13  ? -28.548 -7.798  30.443  1   101.17 ? 13  GLU B O   1 
ATOM   3292 C CB  . GLU B 1 13  ? -29.998 -5.054  30.193  1   97.55  ? 13  GLU B CB  1 
ATOM   3293 C CG  . GLU B 1 13  ? -30.794 -5.03   28.887  1   102.69 ? 13  GLU B CG  1 
ATOM   3294 C CD  . GLU B 1 13  ? -32.293 -4.773  28.948  1   104.87 ? 13  GLU B CD  1 
ATOM   3295 O OE1 . GLU B 1 13  ? -32.766 -3.905  28.17   1   99.9   ? 13  GLU B OE1 1 
ATOM   3296 O OE2 . GLU B 1 13  ? -32.977 -5.452  29.745  1   106.01 ? 13  GLU B OE2 1 
ATOM   3297 N N   . ASN B 1 14  ? -27.985 -7.203  28.336  1   97.33  ? 14  ASN B N   1 
ATOM   3298 C CA  . ASN B 1 14  ? -27.66  -8.533  27.823  1   95.82  ? 14  ASN B CA  1 
ATOM   3299 C C   . ASN B 1 14  ? -26.234 -9.009  28.131  1   93.42  ? 14  ASN B C   1 
ATOM   3300 O O   . ASN B 1 14  ? -25.984 -10.212 28.058  1   91.55  ? 14  ASN B O   1 
ATOM   3301 C CB  . ASN B 1 14  ? -27.762 -8.583  26.301  1   94.89  ? 14  ASN B CB  1 
ATOM   3302 C CG  . ASN B 1 14  ? -29.196 -8.54   25.862  1   96.72  ? 14  ASN B CG  1 
ATOM   3303 O OD1 . ASN B 1 14  ? -29.796 -9.602  25.666  1   102.85 ? 14  ASN B OD1 1 
ATOM   3304 N ND2 . ASN B 1 14  ? -29.779 -7.356  25.803  1   93.33  ? 14  ASN B ND2 1 
ATOM   3305 N N   . ASP B 1 15  ? -25.296 -8.079  28.392  1   86.13  ? 15  ASP B N   1 
ATOM   3306 C CA  . ASP B 1 15  ? -23.87  -8.384  28.424  1   80.22  ? 15  ASP B CA  1 
ATOM   3307 C C   . ASP B 1 15  ? -23.138 -7.359  29.298  1   78.15  ? 15  ASP B C   1 
ATOM   3308 O O   . ASP B 1 15  ? -22.744 -6.305  28.792  1   78.51  ? 15  ASP B O   1 
ATOM   3309 C CB  . ASP B 1 15  ? -23.328 -8.496  27      1   75.62  ? 15  ASP B CB  1 
ATOM   3310 C CG  . ASP B 1 15  ? -21.874 -8.934  26.853  1   72.36  ? 15  ASP B CG  1 
ATOM   3311 O OD1 . ASP B 1 15  ? -21.267 -9.311  27.876  1   75.38  ? 15  ASP B OD1 1 
ATOM   3312 O OD2 . ASP B 1 15  ? -21.346 -8.89   25.727  1   67.99  ? 15  ASP B OD2 1 
ATOM   3313 N N   . ASN B 1 16  ? -22.904 -7.709  30.581  1   78.08  ? 16  ASN B N   1 
ATOM   3314 C CA  . ASN B 1 16  ? -22.244 -6.829  31.545  1   80.12  ? 16  ASN B CA  1 
ATOM   3315 C C   . ASN B 1 16  ? -20.73  -6.703  31.307  1   75.8   ? 16  ASN B C   1 
ATOM   3316 O O   . ASN B 1 16  ? -20.122 -5.75   31.818  1   68.79  ? 16  ASN B O   1 
ATOM   3317 C CB  . ASN B 1 16  ? -22.558 -7.232  32.986  1   83.41  ? 16  ASN B CB  1 
ATOM   3318 C CG  . ASN B 1 16  ? -23.911 -6.748  33.471  1   89.48  ? 16  ASN B CG  1 
ATOM   3319 O OD1 . ASN B 1 16  ? -24.669 -6.088  32.746  1   95.2   ? 16  ASN B OD1 1 
ATOM   3320 N ND2 . ASN B 1 16  ? -24.235 -7.041  34.718  1   90.21  ? 16  ASN B ND2 1 
ATOM   3321 N N   . SER B 1 17  ? -20.141 -7.639  30.527  1   73.63  ? 17  SER B N   1 
ATOM   3322 C CA  . SER B 1 17  ? -18.77  -7.523  30.035  1   73.53  ? 17  SER B CA  1 
ATOM   3323 C C   . SER B 1 17  ? -18.553 -6.239  29.221  1   67.92  ? 17  SER B C   1 
ATOM   3324 O O   . SER B 1 17  ? -17.427 -5.753  29.205  1   70.17  ? 17  SER B O   1 
ATOM   3325 C CB  . SER B 1 17  ? -18.322 -8.764  29.237  1   72.56  ? 17  SER B CB  1 
ATOM   3326 O OG  . SER B 1 17  ? -18.714 -8.759  27.86   1   69.83  ? 17  SER B OG  1 
ATOM   3327 N N   . LEU B 1 18  ? -19.594 -5.732  28.526  1   66.91  ? 18  LEU B N   1 
ATOM   3328 C CA  . LEU B 1 18  ? -19.498 -4.537  27.68   1   66.51  ? 18  LEU B CA  1 
ATOM   3329 C C   . LEU B 1 18  ? -19.012 -3.298  28.438  1   65.46  ? 18  LEU B C   1 
ATOM   3330 O O   . LEU B 1 18  ? -18.334 -2.469  27.826  1   63.14  ? 18  LEU B O   1 
ATOM   3331 C CB  . LEU B 1 18  ? -20.808 -4.231  26.947  1   63.75  ? 18  LEU B CB  1 
ATOM   3332 C CG  . LEU B 1 18  ? -21.145 -5.157  25.777  1   64.43  ? 18  LEU B CG  1 
ATOM   3333 C CD1 . LEU B 1 18  ? -22.551 -4.93   25.273  1   64.5   ? 18  LEU B CD1 1 
ATOM   3334 C CD2 . LEU B 1 18  ? -20.122 -5.01   24.643  1   59.93  ? 18  LEU B CD2 1 
ATOM   3335 N N   . MET B 1 19  ? -19.35  -3.179  29.73   1   67.42  ? 19  MET B N   1 
ATOM   3336 C CA  . MET B 1 19  ? -18.868 -2.087  30.573  1   68.5   ? 19  MET B CA  1 
ATOM   3337 C C   . MET B 1 19  ? -17.342 -1.965  30.553  1   65.1   ? 19  MET B C   1 
ATOM   3338 O O   . MET B 1 19  ? -16.847 -0.885  30.284  1   60.9   ? 19  MET B O   1 
ATOM   3339 C CB  . MET B 1 19  ? -19.319 -2.229  32.037  1   72.77  ? 19  MET B CB  1 
ATOM   3340 C CG  . MET B 1 19  ? -20.458 -1.334  32.428  1   77.27  ? 19  MET B CG  1 
ATOM   3341 S SD  . MET B 1 19  ? -20.002 0.416   32.415  1   81.25  ? 19  MET B SD  1 
ATOM   3342 C CE  . MET B 1 19  ? -21.725 0.904   32.592  1   81.66  ? 19  MET B CE  1 
ATOM   3343 N N   . ASN B 1 20  ? -16.595 -3.054  30.815  1   63.79  ? 20  ASN B N   1 
ATOM   3344 C CA  . ASN B 1 20  ? -15.132 -3.004  30.798  1   64.41  ? 20  ASN B CA  1 
ATOM   3345 C C   . ASN B 1 20  ? -14.559 -2.769  29.401  1   59.41  ? 20  ASN B C   1 
ATOM   3346 O O   . ASN B 1 20  ? -13.542 -2.091  29.268  1   56.73  ? 20  ASN B O   1 
ATOM   3347 C CB  . ASN B 1 20  ? -14.489 -4.238  31.414  1   66.62  ? 20  ASN B CB  1 
ATOM   3348 C CG  . ASN B 1 20  ? -14.779 -4.297  32.886  1   70.41  ? 20  ASN B CG  1 
ATOM   3349 O OD1 . ASN B 1 20  ? -14.729 -3.278  33.588  1   77.3   ? 20  ASN B OD1 1 
ATOM   3350 N ND2 . ASN B 1 20  ? -15.137 -5.472  33.357  1   70.76  ? 20  ASN B ND2 1 
ATOM   3351 N N   . LYS B 1 21  ? -15.199 -3.326  28.367  1   60.77  ? 21  LYS B N   1 
ATOM   3352 C CA  . LYS B 1 21  ? -14.784 -3.115  26.986  1   59.37  ? 21  LYS B CA  1 
ATOM   3353 C C   . LYS B 1 21  ? -14.916 -1.621  26.668  1   58.72  ? 21  LYS B C   1 
ATOM   3354 O O   . LYS B 1 21  ? -13.991 -1.033  26.103  1   55.94  ? 21  LYS B O   1 
ATOM   3355 C CB  . LYS B 1 21  ? -15.551 -4.041  26.023  1   59     ? 21  LYS B CB  1 
ATOM   3356 C CG  . LYS B 1 21  ? -15.21  -3.832  24.522  1   55.09  ? 21  LYS B CG  1 
ATOM   3357 C CD  . LYS B 1 21  ? -15.759 -4.821  23.498  1   56.48  ? 21  LYS B CD  1 
ATOM   3358 C CE  . LYS B 1 21  ? -15.277 -6.276  23.676  1   57     ? 21  LYS B CE  1 
ATOM   3359 N NZ  . LYS B 1 21  ? -13.83  -6.39   23.454  1   53.14  ? 21  LYS B NZ  1 
ATOM   3360 N N   . TRP B 1 22  ? -16.034 -0.989  27.083  1   57.91  ? 22  TRP B N   1 
ATOM   3361 C CA  . TRP B 1 22  ? -16.297 0.407   26.704  1   54.77  ? 22  TRP B CA  1 
ATOM   3362 C C   . TRP B 1 22  ? -15.392 1.362   27.476  1   50.61  ? 22  TRP B C   1 
ATOM   3363 O O   . TRP B 1 22  ? -14.856 2.283   26.87   1   47.54  ? 22  TRP B O   1 
ATOM   3364 C CB  . TRP B 1 22  ? -17.771 0.762   26.91   1   55.33  ? 22  TRP B CB  1 
ATOM   3365 C CG  . TRP B 1 22  ? -18.718 0.09    25.954  1   54.85  ? 22  TRP B CG  1 
ATOM   3366 C CD1 . TRP B 1 22  ? -18.464 -0.462  24.725  1   53.12  ? 22  TRP B CD1 1 
ATOM   3367 C CD2 . TRP B 1 22  ? -20.128 -0.09   26.197  1   54.82  ? 22  TRP B CD2 1 
ATOM   3368 N NE1 . TRP B 1 22  ? -19.622 -0.962  24.188  1   52.86  ? 22  TRP B NE1 1 
ATOM   3369 C CE2 . TRP B 1 22  ? -20.654 -0.749  25.062  1   53     ? 22  TRP B CE2 1 
ATOM   3370 C CE3 . TRP B 1 22  ? -20.986 0.257   27.254  1   57.08  ? 22  TRP B CE3 1 
ATOM   3371 C CZ2 . TRP B 1 22  ? -22.004 -1.067  24.956  1   55.23  ? 22  TRP B CZ2 1 
ATOM   3372 C CZ3 . TRP B 1 22  ? -22.328 -0.041  27.138  1   57.68  ? 22  TRP B CZ3 1 
ATOM   3373 C CH2 . TRP B 1 22  ? -22.825 -0.688  25.996  1   56.77  ? 22  TRP B CH2 1 
ATOM   3374 N N   . ALA B 1 23  ? -15.201 1.083   28.773  1   51.57  ? 23  ALA B N   1 
ATOM   3375 C CA  . ALA B 1 23  ? -14.255 1.796   29.623  1   52.44  ? 23  ALA B CA  1 
ATOM   3376 C C   . ALA B 1 23  ? -12.856 1.823   29.004  1   51.32  ? 23  ALA B C   1 
ATOM   3377 O O   . ALA B 1 23  ? -12.268 2.889   28.841  1   49.23  ? 23  ALA B O   1 
ATOM   3378 C CB  . ALA B 1 23  ? -14.227 1.19    30.995  1   55.49  ? 23  ALA B CB  1 
ATOM   3379 N N   . THR B 1 24  ? -12.354 0.654   28.584  1   52.12  ? 24  THR B N   1 
ATOM   3380 C CA  . THR B 1 24  ? -11.03  0.554   27.989  1   50.91  ? 24  THR B CA  1 
ATOM   3381 C C   . THR B 1 24  ? -10.997 1.324   26.674  1   50.1   ? 24  THR B C   1 
ATOM   3382 O O   . THR B 1 24  ? -10.072 2.107   26.492  1   52.05  ? 24  THR B O   1 
ATOM   3383 C CB  . THR B 1 24  ? -10.637 -0.904  27.736  1   52.54  ? 24  THR B CB  1 
ATOM   3384 O OG1 . THR B 1 24  ? -10.906 -1.554  28.962  1   52.82  ? 24  THR B OG1 1 
ATOM   3385 C CG2 . THR B 1 24  ? -9.191  -1.061  27.29   1   53.2   ? 24  THR B CG2 1 
ATOM   3386 N N   . VAL B 1 25  ? -11.946 1.028   25.757  1   50.25  ? 25  VAL B N   1 
ATOM   3387 C CA  . VAL B 1 25  ? -12.081 1.682   24.441  1   51.15  ? 25  VAL B CA  1 
ATOM   3388 C C   . VAL B 1 25  ? -12.113 3.209   24.582  1   48.69  ? 25  VAL B C   1 
ATOM   3389 O O   . VAL B 1 25  ? -11.537 3.935   23.78   1   45.13  ? 25  VAL B O   1 
ATOM   3390 C CB  . VAL B 1 25  ? -13.366 1.144   23.755  1   55.69  ? 25  VAL B CB  1 
ATOM   3391 C CG1 . VAL B 1 25  ? -13.948 2.042   22.686  1   60.31  ? 25  VAL B CG1 1 
ATOM   3392 C CG2 . VAL B 1 25  ? -13.158 -0.244  23.158  1   61.74  ? 25  VAL B CG2 1 
ATOM   3393 N N   . ALA B 1 26  ? -12.83  3.69    25.597  1   51.78  ? 26  ALA B N   1 
ATOM   3394 C CA  . ALA B 1 26  ? -13.003 5.118   25.836  1   54.54  ? 26  ALA B CA  1 
ATOM   3395 C C   . ALA B 1 26  ? -11.8   5.762   26.543  1   56.01  ? 26  ALA B C   1 
ATOM   3396 O O   . ALA B 1 26  ? -11.82  6.965   26.76   1   57.72  ? 26  ALA B O   1 
ATOM   3397 C CB  . ALA B 1 26  ? -14.272 5.314   26.653  1   56.7   ? 26  ALA B CB  1 
ATOM   3398 N N   . GLY B 1 27  ? -10.792 4.979   26.964  1   55.7   ? 27  GLY B N   1 
ATOM   3399 C CA  . GLY B 1 27  ? -9.582  5.52    27.566  1   53.42  ? 27  GLY B CA  1 
ATOM   3400 C C   . GLY B 1 27  ? -9.832  5.963   29.005  1   56.43  ? 27  GLY B C   1 
ATOM   3401 O O   . GLY B 1 27  ? -9.12   6.809   29.506  1   62.48  ? 27  GLY B O   1 
ATOM   3402 N N   . LEU B 1 28  ? -10.81  5.353   29.68   1   56.61  ? 28  LEU B N   1 
ATOM   3403 C CA  . LEU B 1 28  ? -11.148 5.692   31.051  1   60.98  ? 28  LEU B CA  1 
ATOM   3404 C C   . LEU B 1 28  ? -10.253 4.884   31.991  1   71.31  ? 28  LEU B C   1 
ATOM   3405 O O   . LEU B 1 28  ? -9.834  3.779   31.649  1   71.88  ? 28  LEU B O   1 
ATOM   3406 C CB  . LEU B 1 28  ? -12.635 5.41    31.304  1   58.38  ? 28  LEU B CB  1 
ATOM   3407 C CG  . LEU B 1 28  ? -13.635 6.06    30.333  1   55.54  ? 28  LEU B CG  1 
ATOM   3408 C CD1 . LEU B 1 28  ? -15.067 5.738   30.734  1   55.44  ? 28  LEU B CD1 1 
ATOM   3409 C CD2 . LEU B 1 28  ? -13.453 7.561   30.185  1   54.44  ? 28  LEU B CD2 1 
ATOM   3410 N N   . LYS B 1 29  ? -10.019 5.425   33.194  1   77.35  ? 29  LYS B N   1 
ATOM   3411 C CA  . LYS B 1 29  ? -9.268  4.741   34.239  1   84.03  ? 29  LYS B CA  1 
ATOM   3412 C C   . LYS B 1 29  ? -10.136 3.617   34.818  1   91.17  ? 29  LYS B C   1 
ATOM   3413 O O   . LYS B 1 29  ? -9.662  2.497   35.006  1   99.5   ? 29  LYS B O   1 
ATOM   3414 C CB  . LYS B 1 29  ? -8.863  5.647   35.414  1   90.95  ? 29  LYS B CB  1 
ATOM   3415 C CG  . LYS B 1 29  ? -8.466  7.108   35.194  1   96.42  ? 29  LYS B CG  1 
ATOM   3416 C CD  . LYS B 1 29  ? -7      7.487   35.358  1   102.29 ? 29  LYS B CD  1 
ATOM   3417 C CE  . LYS B 1 29  ? -6.897  8.947   35.706  1   107.29 ? 29  LYS B CE  1 
ATOM   3418 N NZ  . LYS B 1 29  ? -5.605  9.517   35.321  1   111.98 ? 29  LYS B NZ  1 
ATOM   3419 N N   . ASN B 1 30  ? -11.399 3.956   35.131  1   85.19  ? 30  ASN B N   1 
ATOM   3420 C CA  . ASN B 1 30  ? -12.375 3.052   35.716  1   81.91  ? 30  ASN B CA  1 
ATOM   3421 C C   . ASN B 1 30  ? -13.702 3.213   34.969  1   80.04  ? 30  ASN B C   1 
ATOM   3422 O O   . ASN B 1 30  ? -13.836 4.115   34.145  1   71.98  ? 30  ASN B O   1 
ATOM   3423 C CB  . ASN B 1 30  ? -12.474 3.304   37.217  1   81.56  ? 30  ASN B CB  1 
ATOM   3424 C CG  . ASN B 1 30  ? -12.965 4.691   37.561  1   81.59  ? 30  ASN B CG  1 
ATOM   3425 O OD1 . ASN B 1 30  ? -12.685 5.663   36.859  1   78.92  ? 30  ASN B OD1 1 
ATOM   3426 N ND2 . ASN B 1 30  ? -13.703 4.815   38.649  1   92.17  ? 30  ASN B ND2 1 
ATOM   3427 N N   . PRO B 1 31  ? -14.704 2.32    35.163  1   80     ? 31  PRO B N   1 
ATOM   3428 C CA  . PRO B 1 31  ? -16.046 2.549   34.604  1   80.89  ? 31  PRO B CA  1 
ATOM   3429 C C   . PRO B 1 31  ? -16.944 3.705   35.075  1   77.31  ? 31  PRO B C   1 
ATOM   3430 O O   . PRO B 1 31  ? -18.01  3.872   34.498  1   68.61  ? 31  PRO B O   1 
ATOM   3431 C CB  . PRO B 1 31  ? -16.747 1.184   34.876  1   84.4   ? 31  PRO B CB  1 
ATOM   3432 C CG  . PRO B 1 31  ? -15.622 0.175   35.005  1   83.66  ? 31  PRO B CG  1 
ATOM   3433 C CD  . PRO B 1 31  ? -14.555 0.968   35.735  1   80.96  ? 31  PRO B CD  1 
ATOM   3434 N N   . ASN B 1 32  ? -16.553 4.498   36.09   1   79.34  ? 32  ASN B N   1 
ATOM   3435 C CA  . ASN B 1 32  ? -17.47  5.446   36.73   1   76.77  ? 32  ASN B CA  1 
ATOM   3436 C C   . ASN B 1 32  ? -17.981 6.556   35.805  1   70.6   ? 32  ASN B C   1 
ATOM   3437 O O   . ASN B 1 32  ? -19.185 6.816   35.819  1   68.85  ? 32  ASN B O   1 
ATOM   3438 C CB  . ASN B 1 32  ? -16.897 6.046   38.007  1   76.81  ? 32  ASN B CB  1 
ATOM   3439 C CG  . ASN B 1 32  ? -17.276 5.175   39.175  1   81.32  ? 32  ASN B CG  1 
ATOM   3440 O OD1 . ASN B 1 32  ? -16.487 4.305   39.554  1   87.38  ? 32  ASN B OD1 1 
ATOM   3441 N ND2 . ASN B 1 32  ? -18.379 5.471   39.843  1   82.41  ? 32  ASN B ND2 1 
ATOM   3442 N N   . PRO B 1 33  ? -17.14  7.25    34.992  1   65.18  ? 33  PRO B N   1 
ATOM   3443 C CA  . PRO B 1 33  ? -17.664 8.2     33.99   1   62.68  ? 33  PRO B CA  1 
ATOM   3444 C C   . PRO B 1 33  ? -18.726 7.62    33.049  1   64     ? 33  PRO B C   1 
ATOM   3445 O O   . PRO B 1 33  ? -19.643 8.337   32.655  1   61.77  ? 33  PRO B O   1 
ATOM   3446 C CB  . PRO B 1 33  ? -16.417 8.703   33.225  1   60.25  ? 33  PRO B CB  1 
ATOM   3447 C CG  . PRO B 1 33  ? -15.288 8.474   34.219  1   60.61  ? 33  PRO B CG  1 
ATOM   3448 C CD  . PRO B 1 33  ? -15.665 7.217   35.016  1   61.73  ? 33  PRO B CD  1 
ATOM   3449 N N   . LEU B 1 34  ? -18.617 6.311   32.739  1   65.09  ? 34  LEU B N   1 
ATOM   3450 C CA  . LEU B 1 34  ? -19.522 5.611   31.837  1   64.95  ? 34  LEU B CA  1 
ATOM   3451 C C   . LEU B 1 34  ? -20.864 5.318   32.517  1   62.9   ? 34  LEU B C   1 
ATOM   3452 O O   . LEU B 1 34  ? -21.903 5.408   31.862  1   56.45  ? 34  LEU B O   1 
ATOM   3453 C CB  . LEU B 1 34  ? -18.774 4.355   31.38   1   66.71  ? 34  LEU B CB  1 
ATOM   3454 C CG  . LEU B 1 34  ? -19.317 3.553   30.194  1   69.98  ? 34  LEU B CG  1 
ATOM   3455 C CD1 . LEU B 1 34  ? -19.588 4.356   28.942  1   67.69  ? 34  LEU B CD1 1 
ATOM   3456 C CD2 . LEU B 1 34  ? -18.312 2.443   29.892  1   70.93  ? 34  LEU B CD2 1 
ATOM   3457 N N   . TYR B 1 35  ? -20.837 4.933   33.807  1   71.69  ? 35  TYR B N   1 
ATOM   3458 C CA  . TYR B 1 35  ? -22.031 4.844   34.648  1   75.92  ? 35  TYR B CA  1 
ATOM   3459 C C   . TYR B 1 35  ? -22.773 6.179   34.64   1   72.78  ? 35  TYR B C   1 
ATOM   3460 O O   . TYR B 1 35  ? -23.975 6.21    34.384  1   70.86  ? 35  TYR B O   1 
ATOM   3461 C CB  . TYR B 1 35  ? -21.746 4.458   36.111  1   83.18  ? 35  TYR B CB  1 
ATOM   3462 C CG  . TYR B 1 35  ? -21.713 2.96    36.343  1   93.24  ? 35  TYR B CG  1 
ATOM   3463 C CD1 . TYR B 1 35  ? -20.559 2.228   36.081  1   96.56  ? 35  TYR B CD1 1 
ATOM   3464 C CD2 . TYR B 1 35  ? -22.838 2.271   36.798  1   102.09 ? 35  TYR B CD2 1 
ATOM   3465 C CE1 . TYR B 1 35  ? -20.519 0.851   36.249  1   103.14 ? 35  TYR B CE1 1 
ATOM   3466 C CE2 . TYR B 1 35  ? -22.807 0.894   36.981  1   111.29 ? 35  TYR B CE2 1 
ATOM   3467 C CZ  . TYR B 1 35  ? -21.644 0.183   36.705  1   110.39 ? 35  TYR B CZ  1 
ATOM   3468 O OH  . TYR B 1 35  ? -21.562 -1.169  36.877  1   117.2  ? 35  TYR B OH  1 
ATOM   3469 N N   . ASP B 1 36  ? -22.038 7.261   34.935  1   73.56  ? 36  ASP B N   1 
ATOM   3470 C CA  . ASP B 1 36  ? -22.596 8.611   35.001  1   71.64  ? 36  ASP B CA  1 
ATOM   3471 C C   . ASP B 1 36  ? -23.189 9.004   33.648  1   67.77  ? 36  ASP B C   1 
ATOM   3472 O O   . ASP B 1 36  ? -24.292 9.547   33.585  1   63.14  ? 36  ASP B O   1 
ATOM   3473 C CB  . ASP B 1 36  ? -21.56  9.625   35.454  1   73.27  ? 36  ASP B CB  1 
ATOM   3474 C CG  . ASP B 1 36  ? -21.203 9.648   36.933  1   81.79  ? 36  ASP B CG  1 
ATOM   3475 O OD1 . ASP B 1 36  ? -21.811 8.887   37.72   1   89.27  ? 36  ASP B OD1 1 
ATOM   3476 O OD2 . ASP B 1 36  ? -20.321 10.453  37.292  1   87.45  ? 36  ASP B OD2 1 
ATOM   3477 N N   . PHE B 1 37  ? -22.466 8.695   32.564  1   64.87  ? 37  PHE B N   1 
ATOM   3478 C CA  . PHE B 1 37  ? -22.931 9.005   31.22   1   61.75  ? 37  PHE B CA  1 
ATOM   3479 C C   . PHE B 1 37  ? -24.256 8.301   30.898  1   63.16  ? 37  PHE B C   1 
ATOM   3480 O O   . PHE B 1 37  ? -25.116 8.895   30.248  1   59.72  ? 37  PHE B O   1 
ATOM   3481 C CB  . PHE B 1 37  ? -21.858 8.602   30.204  1   61.03  ? 37  PHE B CB  1 
ATOM   3482 C CG  . PHE B 1 37  ? -22.318 8.798   28.773  1   58.98  ? 37  PHE B CG  1 
ATOM   3483 C CD1 . PHE B 1 37  ? -22.339 10.077  28.226  1   61.67  ? 37  PHE B CD1 1 
ATOM   3484 C CD2 . PHE B 1 37  ? -22.717 7.734   27.974  1   58.97  ? 37  PHE B CD2 1 
ATOM   3485 C CE1 . PHE B 1 37  ? -22.729 10.29   26.907  1   58.1   ? 37  PHE B CE1 1 
ATOM   3486 C CE2 . PHE B 1 37  ? -23.127 7.964   26.668  1   56.43  ? 37  PHE B CE2 1 
ATOM   3487 C CZ  . PHE B 1 37  ? -23.131 9.233   26.137  1   56.87  ? 37  PHE B CZ  1 
ATOM   3488 N N   . LEU B 1 38  ? -24.388 7.021   31.282  1   67.37  ? 38  LEU B N   1 
ATOM   3489 C CA  . LEU B 1 38  ? -25.586 6.235   30.981  1   71.18  ? 38  LEU B CA  1 
ATOM   3490 C C   . LEU B 1 38  ? -26.797 6.693   31.798  1   71.92  ? 38  LEU B C   1 
ATOM   3491 O O   . LEU B 1 38  ? -27.9   6.721   31.259  1   73.24  ? 38  LEU B O   1 
ATOM   3492 C CB  . LEU B 1 38  ? -25.349 4.736   31.173  1   73.11  ? 38  LEU B CB  1 
ATOM   3493 C CG  . LEU B 1 38  ? -24.516 4.042   30.089  1   75.71  ? 38  LEU B CG  1 
ATOM   3494 C CD1 . LEU B 1 38  ? -24.27  2.586   30.456  1   76.59  ? 38  LEU B CD1 1 
ATOM   3495 C CD2 . LEU B 1 38  ? -25.166 4.139   28.706  1   78.69  ? 38  LEU B CD2 1 
ATOM   3496 N N   . ASN B 1 39  ? -26.588 7.076   33.061  1   70.77  ? 39  ASN B N   1 
ATOM   3497 C CA  . ASN B 1 39  ? -27.674 7.234   34.028  1   78.32  ? 39  ASN B CA  1 
ATOM   3498 C C   . ASN B 1 39  ? -28.118 8.691   34.249  1   77.11  ? 39  ASN B C   1 
ATOM   3499 O O   . ASN B 1 39  ? -29.206 8.895   34.773  1   77.67  ? 39  ASN B O   1 
ATOM   3500 C CB  . ASN B 1 39  ? -27.29  6.58    35.36   1   81.01  ? 39  ASN B CB  1 
ATOM   3501 C CG  . ASN B 1 39  ? -27.105 5.077   35.269  1   83.37  ? 39  ASN B CG  1 
ATOM   3502 O OD1 . ASN B 1 39  ? -27.647 4.426   34.36   1   81.81  ? 39  ASN B OD1 1 
ATOM   3503 N ND2 . ASN B 1 39  ? -26.356 4.505   36.209  1   88.86  ? 39  ASN B ND2 1 
ATOM   3504 N N   . HIS B 1 40  ? -27.294 9.697   33.91   1   74.94  ? 40  HIS B N   1 
ATOM   3505 C CA  . HIS B 1 40  ? -27.573 11.103  34.216  1   75     ? 40  HIS B CA  1 
ATOM   3506 C C   . HIS B 1 40  ? -27.495 11.918  32.931  1   73.44  ? 40  HIS B C   1 
ATOM   3507 O O   . HIS B 1 40  ? -26.432 11.941  32.306  1   72     ? 40  HIS B O   1 
ATOM   3508 C CB  . HIS B 1 40  ? -26.576 11.658  35.241  1   73.92  ? 40  HIS B CB  1 
ATOM   3509 C CG  . HIS B 1 40  ? -26.58  10.888  36.521  1   83.46  ? 40  HIS B CG  1 
ATOM   3510 N ND1 . HIS B 1 40  ? -27.702 10.223  36.977  1   85.61  ? 40  HIS B ND1 1 
ATOM   3511 C CD2 . HIS B 1 40  ? -25.621 10.668  37.431  1   86.12  ? 40  HIS B CD2 1 
ATOM   3512 C CE1 . HIS B 1 40  ? -27.425 9.623   38.122  1   87.96  ? 40  HIS B CE1 1 
ATOM   3513 N NE2 . HIS B 1 40  ? -26.169 9.879   38.419  1   91.05  ? 40  HIS B NE2 1 
ATOM   3514 N N   . ASP B 1 41  ? -28.621 12.56   32.548  1   73.76  ? 41  ASP B N   1 
ATOM   3515 C CA  . ASP B 1 41  ? -28.73  13.355  31.328  1   72.4   ? 41  ASP B CA  1 
ATOM   3516 C C   . ASP B 1 41  ? -27.7   14.488  31.357  1   69.31  ? 41  ASP B C   1 
ATOM   3517 O O   . ASP B 1 41  ? -27.446 15.08   32.407  1   64     ? 41  ASP B O   1 
ATOM   3518 C CB  . ASP B 1 41  ? -30.108 13.99   31.164  1   75.75  ? 41  ASP B CB  1 
ATOM   3519 C CG  . ASP B 1 41  ? -31.291 13.04   31.04   1   77.43  ? 41  ASP B CG  1 
ATOM   3520 O OD1 . ASP B 1 41  ? -31.257 12.181  30.155  1   79.34  ? 41  ASP B OD1 1 
ATOM   3521 O OD2 . ASP B 1 41  ? -32.252 13.178  31.818  1   86.22  ? 41  ASP B OD2 1 
ATOM   3522 N N   . GLY B 1 42  ? -27.067 14.746  30.206  1   65.61  ? 42  GLY B N   1 
ATOM   3523 C CA  . GLY B 1 42  ? -26.132 15.845  30.071  1   65.4   ? 42  GLY B CA  1 
ATOM   3524 C C   . GLY B 1 42  ? -24.759 15.579  30.692  1   66.67  ? 42  GLY B C   1 
ATOM   3525 O O   . GLY B 1 42  ? -23.932 16.486  30.685  1   70.46  ? 42  GLY B O   1 
ATOM   3526 N N   . LYS B 1 43  ? -24.464 14.36   31.181  1   64.21  ? 43  LYS B N   1 
ATOM   3527 C CA  . LYS B 1 43  ? -23.104 14.082  31.624  1   67.36  ? 43  LYS B CA  1 
ATOM   3528 C C   . LYS B 1 43  ? -22.254 13.793  30.386  1   59.97  ? 43  LYS B C   1 
ATOM   3529 O O   . LYS B 1 43  ? -22.583 12.895  29.634  1   59.85  ? 43  LYS B O   1 
ATOM   3530 C CB  . LYS B 1 43  ? -23.041 12.945  32.651  1   77.74  ? 43  LYS B CB  1 
ATOM   3531 C CG  . LYS B 1 43  ? -21.617 12.602  33.133  1   86.04  ? 43  LYS B CG  1 
ATOM   3532 C CD  . LYS B 1 43  ? -20.623 13.722  33.463  1   89.92  ? 43  LYS B CD  1 
ATOM   3533 C CE  . LYS B 1 43  ? -21.081 14.764  34.453  1   95.21  ? 43  LYS B CE  1 
ATOM   3534 N NZ  . LYS B 1 43  ? -21.777 14.207  35.617  1   97.83  ? 43  LYS B NZ  1 
ATOM   3535 N N   . THR B 1 44  ? -21.219 14.593  30.147  1   56.07  ? 44  THR B N   1 
ATOM   3536 C CA  . THR B 1 44  ? -20.308 14.393  29.022  1   51.58  ? 44  THR B CA  1 
ATOM   3537 C C   . THR B 1 44  ? -19.005 13.796  29.557  1   52.61  ? 44  THR B C   1 
ATOM   3538 O O   . THR B 1 44  ? -18.649 14.017  30.72   1   54.71  ? 44  THR B O   1 
ATOM   3539 C CB  . THR B 1 44  ? -20.084 15.724  28.287  1   48.61  ? 44  THR B CB  1 
ATOM   3540 O OG1 . THR B 1 44  ? -19.458 16.615  29.203  1   45.59  ? 44  THR B OG1 1 
ATOM   3541 C CG2 . THR B 1 44  ? -21.377 16.361  27.799  1   45.96  ? 44  THR B CG2 1 
ATOM   3542 N N   . PHE B 1 45  ? -18.311 13.024  28.702  1   50.61  ? 45  PHE B N   1 
ATOM   3543 C CA  . PHE B 1 45  ? -16.96  12.593  29.016  1   51.46  ? 45  PHE B CA  1 
ATOM   3544 C C   . PHE B 1 45  ? -16.023 13.795  28.922  1   52.18  ? 45  PHE B C   1 
ATOM   3545 O O   . PHE B 1 45  ? -16.294 14.701  28.127  1   50.5   ? 45  PHE B O   1 
ATOM   3546 C CB  . PHE B 1 45  ? -16.518 11.495  28.054  1   50.77  ? 45  PHE B CB  1 
ATOM   3547 C CG  . PHE B 1 45  ? -17.358 10.228  28.137  1   51.58  ? 45  PHE B CG  1 
ATOM   3548 C CD1 . PHE B 1 45  ? -17.182 9.322   29.188  1   54.03  ? 45  PHE B CD1 1 
ATOM   3549 C CD2 . PHE B 1 45  ? -18.302 9.939   27.148  1   50.11  ? 45  PHE B CD2 1 
ATOM   3550 C CE1 . PHE B 1 45  ? -17.932 8.14    29.239  1   53.01  ? 45  PHE B CE1 1 
ATOM   3551 C CE2 . PHE B 1 45  ? -19.072 8.777   27.221  1   52.95  ? 45  PHE B CE2 1 
ATOM   3552 C CZ  . PHE B 1 45  ? -18.876 7.872   28.249  1   50.78  ? 45  PHE B CZ  1 
ATOM   3553 N N   . ASN B 1 46  ? -14.92  13.752  29.702  1   50.8   ? 46  ASN B N   1 
ATOM   3554 C CA  . ASN B 1 46  ? -13.865 14.754  29.687  1   52.38  ? 46  ASN B CA  1 
ATOM   3555 C C   . ASN B 1 46  ? -13.275 14.925  28.291  1   47.39  ? 46  ASN B C   1 
ATOM   3556 O O   . ASN B 1 46  ? -12.917 16.045  27.927  1   43.31  ? 46  ASN B O   1 
ATOM   3557 C CB  . ASN B 1 46  ? -12.719 14.412  30.641  1   58.67  ? 46  ASN B CB  1 
ATOM   3558 C CG  . ASN B 1 46  ? -13.059 14.675  32.094  1   73.62  ? 46  ASN B CG  1 
ATOM   3559 O OD1 . ASN B 1 46  ? -14.121 15.23   32.424  1   80.52  ? 46  ASN B OD1 1 
ATOM   3560 N ND2 . ASN B 1 46  ? -12.15  14.31   32.992  1   80.92  ? 46  ASN B ND2 1 
ATOM   3561 N N   . GLU B 1 47  ? -13.151 13.812  27.541  1   46.4   ? 47  GLU B N   1 
ATOM   3562 C CA  . GLU B 1 47  ? -12.62  13.843  26.185  1   46.13  ? 47  GLU B CA  1 
ATOM   3563 C C   . GLU B 1 47  ? -13.636 13.194  25.247  1   47.09  ? 47  GLU B C   1 
ATOM   3564 O O   . GLU B 1 47  ? -14.175 12.123  25.517  1   47.63  ? 47  GLU B O   1 
ATOM   3565 C CB  . GLU B 1 47  ? -11.213 13.249  26.134  1   48.62  ? 47  GLU B CB  1 
ATOM   3566 C CG  . GLU B 1 47  ? -10.13  14.207  26.623  1   49.29  ? 47  GLU B CG  1 
ATOM   3567 C CD  . GLU B 1 47  ? -9.894  15.467  25.79   1   52.45  ? 47  GLU B CD  1 
ATOM   3568 O OE1 . GLU B 1 47  ? -10.318 15.585  24.6    1   46.64  ? 47  GLU B OE1 1 
ATOM   3569 O OE2 . GLU B 1 47  ? -9.325  16.404  26.381  1   49.34  ? 47  GLU B OE2 1 
ATOM   3570 N N   . PHE B 1 48  ? -13.892 13.872  24.128  1   40.91  ? 48  PHE B N   1 
ATOM   3571 C CA  . PHE B 1 48  ? -14.924 13.459  23.196  1   41.49  ? 48  PHE B CA  1 
ATOM   3572 C C   . PHE B 1 48  ? -14.583 12.131  22.507  1   43.51  ? 48  PHE B C   1 
ATOM   3573 O O   . PHE B 1 48  ? -15.487 11.447  22.01   1   40.85  ? 48  PHE B O   1 
ATOM   3574 C CB  . PHE B 1 48  ? -15.015 14.575  22.153  1   40.65  ? 48  PHE B CB  1 
ATOM   3575 C CG  . PHE B 1 48  ? -16.281 14.5    21.333  1   38.1   ? 48  PHE B CG  1 
ATOM   3576 C CD1 . PHE B 1 48  ? -17.495 14.894  21.899  1   39.29  ? 48  PHE B CD1 1 
ATOM   3577 C CD2 . PHE B 1 48  ? -16.236 14.103  20.007  1   35.47  ? 48  PHE B CD2 1 
ATOM   3578 C CE1 . PHE B 1 48  ? -18.664 14.828  21.152  1   39.19  ? 48  PHE B CE1 1 
ATOM   3579 C CE2 . PHE B 1 48  ? -17.403 14.074  19.26   1   36.62  ? 48  PHE B CE2 1 
ATOM   3580 C CZ  . PHE B 1 48  ? -18.611 14.422  19.833  1   35.84  ? 48  PHE B CZ  1 
ATOM   3581 N N   . SER B 1 49  ? -13.28  11.799  22.453  1   41.25  ? 49  SER B N   1 
ATOM   3582 C CA  . SER B 1 49  ? -12.789 10.511  21.975  1   43.26  ? 49  SER B CA  1 
ATOM   3583 C C   . SER B 1 49  ? -13.5   9.343   22.672  1   41.5   ? 49  SER B C   1 
ATOM   3584 O O   . SER B 1 49  ? -13.74  8.323   22.037  1   41.22  ? 49  SER B O   1 
ATOM   3585 C CB  . SER B 1 49  ? -11.268 10.43   22.124  1   42.79  ? 49  SER B CB  1 
ATOM   3586 O OG  . SER B 1 49  ? -10.93  10.83   23.439  1   43.99  ? 49  SER B OG  1 
ATOM   3587 N N   . SER B 1 50  ? -13.901 9.512   23.941  1   40.44  ? 50  SER B N   1 
ATOM   3588 C CA  . SER B 1 50  ? -14.649 8.487   24.669  1   42.28  ? 50  SER B CA  1 
ATOM   3589 C C   . SER B 1 50  ? -15.912 8.018   23.944  1   42.83  ? 50  SER B C   1 
ATOM   3590 O O   . SER B 1 50  ? -16.097 6.822   23.725  1   41.69  ? 50  SER B O   1 
ATOM   3591 C CB  . SER B 1 50  ? -14.976 8.945   26.059  1   44.42  ? 50  SER B CB  1 
ATOM   3592 O OG  . SER B 1 50  ? -13.766 9.095   26.782  1   44.22  ? 50  SER B OG  1 
ATOM   3593 N N   . ILE B 1 51  ? -16.782 8.959   23.575  1   42.35  ? 51  ILE B N   1 
ATOM   3594 C CA  . ILE B 1 51  ? -18.036 8.608   22.928  1   44.82  ? 51  ILE B CA  1 
ATOM   3595 C C   . ILE B 1 51  ? -17.801 8.173   21.478  1   42.44  ? 51  ILE B C   1 
ATOM   3596 O O   . ILE B 1 51  ? -18.445 7.229   21.023  1   42.96  ? 51  ILE B O   1 
ATOM   3597 C CB  . ILE B 1 51  ? -19.08  9.734   23.081  1   49.05  ? 51  ILE B CB  1 
ATOM   3598 C CG1 . ILE B 1 51  ? -20.466 9.298   22.588  1   48.44  ? 51  ILE B CG1 1 
ATOM   3599 C CG2 . ILE B 1 51  ? -18.643 11.028  22.39   1   47.04  ? 51  ILE B CG2 1 
ATOM   3600 C CD1 . ILE B 1 51  ? -21.02  8.066   23.254  1   52.25  ? 51  ILE B CD1 1 
ATOM   3601 N N   . VAL B 1 52  ? -16.871 8.804   20.77   1   38.22  ? 52  VAL B N   1 
ATOM   3602 C CA  . VAL B 1 52  ? -16.601 8.427   19.376  1   41.63  ? 52  VAL B CA  1 
ATOM   3603 C C   . VAL B 1 52  ? -16.065 6.995   19.337  1   39.83  ? 52  VAL B C   1 
ATOM   3604 O O   . VAL B 1 52  ? -16.466 6.211   18.483  1   39.71  ? 52  VAL B O   1 
ATOM   3605 C CB  . VAL B 1 52  ? -15.629 9.374   18.641  1   41.89  ? 52  VAL B CB  1 
ATOM   3606 C CG1 . VAL B 1 52  ? -15.29  8.885   17.224  1   42.06  ? 52  VAL B CG1 1 
ATOM   3607 C CG2 . VAL B 1 52  ? -16.148 10.804  18.583  1   42.88  ? 52  VAL B CG2 1 
ATOM   3608 N N   . ASN B 1 53  ? -15.118 6.684   20.22   1   39.54  ? 53  ASN B N   1 
ATOM   3609 C CA  . ASN B 1 53  ? -14.485 5.37    20.228  1   42.25  ? 53  ASN B CA  1 
ATOM   3610 C C   . ASN B 1 53  ? -15.508 4.281   20.528  1   43.38  ? 53  ASN B C   1 
ATOM   3611 O O   . ASN B 1 53  ? -15.427 3.199   19.941  1   43.25  ? 53  ASN B O   1 
ATOM   3612 C CB  . ASN B 1 53  ? -13.295 5.302   21.187  1   44.1   ? 53  ASN B CB  1 
ATOM   3613 C CG  . ASN B 1 53  ? -12.098 6.1     20.705  1   46.21  ? 53  ASN B CG  1 
ATOM   3614 O OD1 . ASN B 1 53  ? -12.123 6.717   19.639  1   43.46  ? 53  ASN B OD1 1 
ATOM   3615 N ND2 . ASN B 1 53  ? -11.041 6.137   21.491  1   49.61  ? 53  ASN B ND2 1 
ATOM   3616 N N   . ILE B 1 54  ? -16.449 4.545   21.445  1   41.94  ? 54  ILE B N   1 
ATOM   3617 C CA  . ILE B 1 54  ? -17.511 3.591   21.727  1   44.38  ? 54  ILE B CA  1 
ATOM   3618 C C   . ILE B 1 54  ? -18.396 3.374   20.501  1   45.4   ? 54  ILE B C   1 
ATOM   3619 O O   . ILE B 1 54  ? -18.704 2.23    20.208  1   47.15  ? 54  ILE B O   1 
ATOM   3620 C CB  . ILE B 1 54  ? -18.342 4.01    22.951  1   45.93  ? 54  ILE B CB  1 
ATOM   3621 C CG1 . ILE B 1 54  ? -17.494 3.913   24.231  1   48.19  ? 54  ILE B CG1 1 
ATOM   3622 C CG2 . ILE B 1 54  ? -19.613 3.161   23.05   1   49.27  ? 54  ILE B CG2 1 
ATOM   3623 C CD1 . ILE B 1 54  ? -18.081 4.59    25.467  1   51.18  ? 54  ILE B CD1 1 
ATOM   3624 N N   . VAL B 1 55  ? -18.851 4.457   19.856  1   43.1   ? 55  VAL B N   1 
ATOM   3625 C CA  . VAL B 1 55  ? -19.759 4.385   18.719  1   47.75  ? 55  VAL B CA  1 
ATOM   3626 C C   . VAL B 1 55  ? -19.086 3.603   17.583  1   48.28  ? 55  VAL B C   1 
ATOM   3627 O O   . VAL B 1 55  ? -19.715 2.709   17.033  1   51.33  ? 55  VAL B O   1 
ATOM   3628 C CB  . VAL B 1 55  ? -20.225 5.791   18.252  1   47.17  ? 55  VAL B CB  1 
ATOM   3629 C CG1 . VAL B 1 55  ? -20.954 5.781   16.92   1   47.85  ? 55  VAL B CG1 1 
ATOM   3630 C CG2 . VAL B 1 55  ? -21.133 6.435   19.284  1   51.4   ? 55  VAL B CG2 1 
ATOM   3631 N N   . LYS B 1 56  ? -17.828 3.941   17.264  1   44.42  ? 56  LYS B N   1 
ATOM   3632 C CA  . LYS B 1 56  ? -17.069 3.288   16.198  1   46.19  ? 56  LYS B CA  1 
ATOM   3633 C C   . LYS B 1 56  ? -16.808 1.805   16.49   1   46.34  ? 56  LYS B C   1 
ATOM   3634 O O   . LYS B 1 56  ? -16.806 1.009   15.575  1   47.31  ? 56  LYS B O   1 
ATOM   3635 C CB  . LYS B 1 56  ? -15.702 3.952   15.98   1   45.65  ? 56  LYS B CB  1 
ATOM   3636 C CG  . LYS B 1 56  ? -15.767 5.255   15.2    1   47.93  ? 56  LYS B CG  1 
ATOM   3637 C CD  . LYS B 1 56  ? -14.38  5.765   14.832  1   48.02  ? 56  LYS B CD  1 
ATOM   3638 C CE  . LYS B 1 56  ? -14.434 6.977   13.938  1   52.63  ? 56  LYS B CE  1 
ATOM   3639 N NZ  . LYS B 1 56  ? -14.782 6.664   12.536  1   47.96  ? 56  LYS B NZ  1 
ATOM   3640 N N   . SER B 1 57  ? -16.537 1.453   17.741  1   44.06  ? 57  SER B N   1 
ATOM   3641 C CA  . SER B 1 57  ? -16.194 0.088   18.096  1   49.48  ? 57  SER B CA  1 
ATOM   3642 C C   . SER B 1 57  ? -17.457 -0.763  18.237  1   53.07  ? 57  SER B C   1 
ATOM   3643 O O   . SER B 1 57  ? -17.498 -1.903  17.766  1   53.49  ? 57  SER B O   1 
ATOM   3644 C CB  . SER B 1 57  ? -15.353 0.043   19.351  1   52.99  ? 57  SER B CB  1 
ATOM   3645 O OG  . SER B 1 57  ? -16.083 0.473   20.487  1   54.93  ? 57  SER B OG  1 
ATOM   3646 N N   . GLN B 1 58  ? -18.486 -0.232  18.911  1   53.05  ? 58  GLN B N   1 
ATOM   3647 C CA  . GLN B 1 58  ? -19.706 -0.985  19.185  1   53.69  ? 58  GLN B CA  1 
ATOM   3648 C C   . GLN B 1 58  ? -20.715 -0.893  18.043  1   49.67  ? 58  GLN B C   1 
ATOM   3649 O O   . GLN B 1 58  ? -21.459 -1.846  17.858  1   50.57  ? 58  GLN B O   1 
ATOM   3650 C CB  . GLN B 1 58  ? -20.336 -0.488  20.489  1   58.45  ? 58  GLN B CB  1 
ATOM   3651 C CG  . GLN B 1 58  ? -21.476 -1.353  21.017  1   62.21  ? 58  GLN B CG  1 
ATOM   3652 C CD  . GLN B 1 58  ? -21.147 -2.794  21.363  1   66.98  ? 58  GLN B CD  1 
ATOM   3653 O OE1 . GLN B 1 58  ? -22.052 -3.644  21.367  1   72.56  ? 58  GLN B OE1 1 
ATOM   3654 N NE2 . GLN B 1 58  ? -19.893 -3.12   21.655  1   64.3   ? 58  GLN B NE2 1 
ATOM   3655 N N   . TYR B 1 59  ? -20.804 0.258   17.352  1   47.53  ? 59  TYR B N   1 
ATOM   3656 C CA  . TYR B 1 59  ? -21.891 0.518   16.41   1   48.51  ? 59  TYR B CA  1 
ATOM   3657 C C   . TYR B 1 59  ? -21.323 1.06    15.107  1   45.58  ? 59  TYR B C   1 
ATOM   3658 O O   . TYR B 1 59  ? -21.827 2.048   14.6    1   47.33  ? 59  TYR B O   1 
ATOM   3659 C CB  . TYR B 1 59  ? -22.949 1.487   16.957  1   48.08  ? 59  TYR B CB  1 
ATOM   3660 C CG  . TYR B 1 59  ? -23.532 1.043   18.289  1   50.21  ? 59  TYR B CG  1 
ATOM   3661 C CD1 . TYR B 1 59  ? -24.423 -0.02   18.361  1   52.52  ? 59  TYR B CD1 1 
ATOM   3662 C CD2 . TYR B 1 59  ? -23.166 1.676   19.471  1   49.95  ? 59  TYR B CD2 1 
ATOM   3663 C CE1 . TYR B 1 59  ? -24.94  -0.441  19.577  1   56.43  ? 59  TYR B CE1 1 
ATOM   3664 C CE2 . TYR B 1 59  ? -23.657 1.264   20.696  1   54.02  ? 59  TYR B CE2 1 
ATOM   3665 C CZ  . TYR B 1 59  ? -24.56  0.211   20.747  1   55.1   ? 59  TYR B CZ  1 
ATOM   3666 O OH  . TYR B 1 59  ? -25.008 -0.133  21.978  1   56.9   ? 59  TYR B OH  1 
ATOM   3667 N N   . PRO B 1 60  ? -20.301 0.417   14.49   1   46.38  ? 60  PRO B N   1 
ATOM   3668 C CA  . PRO B 1 60  ? -19.604 1.007   13.35   1   49.18  ? 60  PRO B CA  1 
ATOM   3669 C C   . PRO B 1 60  ? -20.542 1.364   12.197  1   50.35  ? 60  PRO B C   1 
ATOM   3670 O O   . PRO B 1 60  ? -20.367 2.399   11.551  1   49.63  ? 60  PRO B O   1 
ATOM   3671 C CB  . PRO B 1 60  ? -18.559 -0.083  12.959  1   48.7   ? 60  PRO B CB  1 
ATOM   3672 C CG  . PRO B 1 60  ? -19.165 -1.365  13.48   1   51.54  ? 60  PRO B CG  1 
ATOM   3673 C CD  . PRO B 1 60  ? -19.808 -0.939  14.789  1   50.73  ? 60  PRO B CD  1 
ATOM   3674 N N   . ASP B 1 61  ? -21.572 0.532   11.993  1   52.46  ? 61  ASP B N   1 
ATOM   3675 C CA  . ASP B 1 61  ? -22.505 0.71    10.894  1   55.84  ? 61  ASP B CA  1 
ATOM   3676 C C   . ASP B 1 61  ? -23.491 1.852   11.138  1   52.14  ? 61  ASP B C   1 
ATOM   3677 O O   . ASP B 1 61  ? -24.067 2.315   10.172  1   54.18  ? 61  ASP B O   1 
ATOM   3678 C CB  . ASP B 1 61  ? -23.202 -0.597  10.55   1   59.21  ? 61  ASP B CB  1 
ATOM   3679 C CG  . ASP B 1 61  ? -22.254 -1.694  10.073  1   64.54  ? 61  ASP B CG  1 
ATOM   3680 O OD1 . ASP B 1 61  ? -21.293 -1.372  9.324   1   66.3   ? 61  ASP B OD1 1 
ATOM   3681 O OD2 . ASP B 1 61  ? -22.482 -2.863  10.434  1   68.24  ? 61  ASP B OD2 1 
ATOM   3682 N N   . ARG B 1 62  ? -23.694 2.312   12.381  1   51.23  ? 62  ARG B N   1 
ATOM   3683 C CA  . ARG B 1 62  ? -24.681 3.347   12.684  1   50.02  ? 62  ARG B CA  1 
ATOM   3684 C C   . ARG B 1 62  ? -24.013 4.643   13.165  1   50.73  ? 62  ARG B C   1 
ATOM   3685 O O   . ARG B 1 62  ? -24.68  5.452   13.802  1   51.19  ? 62  ARG B O   1 
ATOM   3686 C CB  . ARG B 1 62  ? -25.63  2.764   13.742  1   54.34  ? 62  ARG B CB  1 
ATOM   3687 C CG  . ARG B 1 62  ? -26.407 1.487   13.399  1   54.66  ? 62  ARG B CG  1 
ATOM   3688 C CD  . ARG B 1 62  ? -27.206 0.989   14.602  1   55.71  ? 62  ARG B CD  1 
ATOM   3689 N NE  . ARG B 1 62  ? -28.219 1.954   15.07   1   57.45  ? 62  ARG B NE  1 
ATOM   3690 C CZ  . ARG B 1 62  ? -28.866 1.911   16.246  1   61.81  ? 62  ARG B CZ  1 
ATOM   3691 N NH1 . ARG B 1 62  ? -28.59  0.996   17.169  1   60.72  ? 62  ARG B NH1 1 
ATOM   3692 N NH2 . ARG B 1 62  ? -29.787 2.819   16.534  1   64.75  ? 62  ARG B NH2 1 
ATOM   3693 N N   . GLU B 1 63  ? -22.722 4.892   12.822  1   51.07  ? 63  GLU B N   1 
ATOM   3694 C CA  . GLU B 1 63  ? -21.978 6.025   13.369  1   45.94  ? 63  GLU B CA  1 
ATOM   3695 C C   . GLU B 1 63  ? -22.712 7.344   13.099  1   43.9   ? 63  GLU B C   1 
ATOM   3696 O O   . GLU B 1 63  ? -23.005 8.087   14.043  1   45.14  ? 63  GLU B O   1 
ATOM   3697 C CB  . GLU B 1 63  ? -20.532 6.098   12.865  1   43.99  ? 63  GLU B CB  1 
ATOM   3698 C CG  . GLU B 1 63  ? -19.702 7.203   13.51   1   41.06  ? 63  GLU B CG  1 
ATOM   3699 C CD  . GLU B 1 63  ? -18.301 7.375   12.956  1   41.78  ? 63  GLU B CD  1 
ATOM   3700 O OE1 . GLU B 1 63  ? -17.803 6.414   12.318  1   42.68  ? 63  GLU B OE1 1 
ATOM   3701 O OE2 . GLU B 1 63  ? -17.668 8.447   13.191  1   38.69  ? 63  GLU B OE2 1 
ATOM   3702 N N   . TYR B 1 64  ? -23.066 7.6     11.837  1   40.33  ? 64  TYR B N   1 
ATOM   3703 C CA  . TYR B 1 64  ? -23.647 8.885   11.466  1   43.43  ? 64  TYR B CA  1 
ATOM   3704 C C   . TYR B 1 64  ? -24.945 9.154   12.236  1   45.72  ? 64  TYR B C   1 
ATOM   3705 O O   . TYR B 1 64  ? -25.071 10.186  12.922  1   43.78  ? 64  TYR B O   1 
ATOM   3706 C CB  . TYR B 1 64  ? -23.769 8.992   9.943   1   42.92  ? 64  TYR B CB  1 
ATOM   3707 C CG  . TYR B 1 64  ? -24.311 10.361  9.569   1   44.5   ? 64  TYR B CG  1 
ATOM   3708 C CD1 . TYR B 1 64  ? -23.473 11.475  9.471   1   44.15  ? 64  TYR B CD1 1 
ATOM   3709 C CD2 . TYR B 1 64  ? -25.671 10.554  9.377   1   45.05  ? 64  TYR B CD2 1 
ATOM   3710 C CE1 . TYR B 1 64  ? -23.968 12.726  9.147   1   44.02  ? 64  TYR B CE1 1 
ATOM   3711 C CE2 . TYR B 1 64  ? -26.182 11.805  9.052   1   46.78  ? 64  TYR B CE2 1 
ATOM   3712 C CZ  . TYR B 1 64  ? -25.318 12.883  8.928   1   45.78  ? 64  TYR B CZ  1 
ATOM   3713 O OH  . TYR B 1 64  ? -25.811 14.095  8.642   1   47.4   ? 64  TYR B OH  1 
ATOM   3714 N N   . GLU B 1 65  ? -25.871 8.179   12.171  1   46.95  ? 65  GLU B N   1 
ATOM   3715 C CA  . GLU B 1 65  ? -27.183 8.252   12.806  1   46.52  ? 65  GLU B CA  1 
ATOM   3716 C C   . GLU B 1 65  ? -27.021 8.583   14.286  1   46.7   ? 65  GLU B C   1 
ATOM   3717 O O   . GLU B 1 65  ? -27.679 9.493   14.786  1   48.95  ? 65  GLU B O   1 
ATOM   3718 C CB  . GLU B 1 65  ? -27.887 6.906   12.582  1   50.66  ? 65  GLU B CB  1 
ATOM   3719 C CG  . GLU B 1 65  ? -29.207 6.672   13.326  1   56.31  ? 65  GLU B CG  1 
ATOM   3720 C CD  . GLU B 1 65  ? -29.557 5.201   13.629  1   58.22  ? 65  GLU B CD  1 
ATOM   3721 O OE1 . GLU B 1 65  ? -28.856 4.27    13.153  1   61.32  ? 65  GLU B OE1 1 
ATOM   3722 O OE2 . GLU B 1 65  ? -30.527 4.975   14.406  1   62.85  ? 65  GLU B OE2 1 
ATOM   3723 N N   . LEU B 1 66  ? -26.17  7.821   14.98   1   42.95  ? 66  LEU B N   1 
ATOM   3724 C CA  . LEU B 1 66  ? -26.044 7.983   16.419  1   44.62  ? 66  LEU B CA  1 
ATOM   3725 C C   . LEU B 1 66  ? -25.347 9.295   16.766  1   44.88  ? 66  LEU B C   1 
ATOM   3726 O O   . LEU B 1 66  ? -25.737 9.933   17.74   1   45.66  ? 66  LEU B O   1 
ATOM   3727 C CB  . LEU B 1 66  ? -25.332 6.778   17.03   1   44.44  ? 66  LEU B CB  1 
ATOM   3728 C CG  . LEU B 1 66  ? -26.102 5.453   16.924  1   47.13  ? 66  LEU B CG  1 
ATOM   3729 C CD1 . LEU B 1 66  ? -25.216 4.288   17.358  1   50.24  ? 66  LEU B CD1 1 
ATOM   3730 C CD2 . LEU B 1 66  ? -27.383 5.461   17.717  1   48.62  ? 66  LEU B CD2 1 
ATOM   3731 N N   . MET B 1 67  ? -24.283 9.656   16.026  1   44.36  ? 67  MET B N   1 
ATOM   3732 C CA  . MET B 1 67  ? -23.516 10.857  16.339  1   43.11  ? 67  MET B CA  1 
ATOM   3733 C C   . MET B 1 67  ? -24.315 12.127  16.022  1   44.13  ? 67  MET B C   1 
ATOM   3734 O O   . MET B 1 67  ? -24.24  13.095  16.787  1   45.29  ? 67  MET B O   1 
ATOM   3735 C CB  . MET B 1 67  ? -22.157 10.825  15.626  1   41.03  ? 67  MET B CB  1 
ATOM   3736 C CG  . MET B 1 67  ? -21.198 9.815   16.233  1   42.02  ? 67  MET B CG  1 
ATOM   3737 S SD  . MET B 1 67  ? -20.923 10.028  18.013  1   44.71  ? 67  MET B SD  1 
ATOM   3738 C CE  . MET B 1 67  ? -20.111 11.637  18.03   1   45.41  ? 67  MET B CE  1 
ATOM   3739 N N   . LYS B 1 68  ? -25.089 12.111  14.923  1   46.17  ? 68  LYS B N   1 
ATOM   3740 C CA  . LYS B 1 68  ? -26.013 13.196  14.609  1   49.11  ? 68  LYS B CA  1 
ATOM   3741 C C   . LYS B 1 68  ? -26.973 13.485  15.763  1   49.47  ? 68  LYS B C   1 
ATOM   3742 O O   . LYS B 1 68  ? -27.13  14.608  16.239  1   44.85  ? 68  LYS B O   1 
ATOM   3743 C CB  . LYS B 1 68  ? -26.808 12.829  13.355  1   53.11  ? 68  LYS B CB  1 
ATOM   3744 C CG  . LYS B 1 68  ? -27.818 13.903  12.993  1   55.42  ? 68  LYS B CG  1 
ATOM   3745 C CD  . LYS B 1 68  ? -28.058 13.906  11.492  1   61.19  ? 68  LYS B CD  1 
ATOM   3746 C CE  . LYS B 1 68  ? -28.699 15.151  10.979  1   66.76  ? 68  LYS B CE  1 
ATOM   3747 N NZ  . LYS B 1 68  ? -30.046 14.879  10.484  1   68.03  ? 68  LYS B NZ  1 
ATOM   3748 N N   . ASP B 1 69  ? -27.628 12.428  16.23   1   47.94  ? 69  ASP B N   1 
ATOM   3749 C CA  . ASP B 1 69  ? -28.547 12.543  17.333  1   48.62  ? 69  ASP B CA  1 
ATOM   3750 C C   . ASP B 1 69  ? -27.828 12.973  18.617  1   45.84  ? 69  ASP B C   1 
ATOM   3751 O O   . ASP B 1 69  ? -28.36  13.788  19.358  1   47.21  ? 69  ASP B O   1 
ATOM   3752 C CB  . ASP B 1 69  ? -29.285 11.222  17.492  1   51.05  ? 69  ASP B CB  1 
ATOM   3753 C CG  . ASP B 1 69  ? -30.203 11.222  18.688  1   51.83  ? 69  ASP B CG  1 
ATOM   3754 O OD1 . ASP B 1 69  ? -31.314 11.756  18.538  1   53.1   ? 69  ASP B OD1 1 
ATOM   3755 O OD2 . ASP B 1 69  ? -29.755 10.747  19.745  1   52.78  ? 69  ASP B OD2 1 
ATOM   3756 N N   . TYR B 1 70  ? -26.655 12.396  18.917  1   43.32  ? 70  TYR B N   1 
ATOM   3757 C CA  . TYR B 1 70  ? -25.923 12.753  20.13   1   43.58  ? 70  TYR B CA  1 
ATOM   3758 C C   . TYR B 1 70  ? -25.515 14.238  20.066  1   46.18  ? 70  TYR B C   1 
ATOM   3759 O O   . TYR B 1 70  ? -25.753 14.99   21.027  1   43.99  ? 70  TYR B O   1 
ATOM   3760 C CB  . TYR B 1 70  ? -24.672 11.9    20.355  1   43.16  ? 70  TYR B CB  1 
ATOM   3761 C CG  . TYR B 1 70  ? -23.875 12.279  21.598  1   45.26  ? 70  TYR B CG  1 
ATOM   3762 C CD1 . TYR B 1 70  ? -24.395 12.046  22.868  1   46.17  ? 70  TYR B CD1 1 
ATOM   3763 C CD2 . TYR B 1 70  ? -22.614 12.887  21.511  1   45.14  ? 70  TYR B CD2 1 
ATOM   3764 C CE1 . TYR B 1 70  ? -23.69  12.383  24.02   1   48.8   ? 70  TYR B CE1 1 
ATOM   3765 C CE2 . TYR B 1 70  ? -21.898 13.218  22.658  1   47.27  ? 70  TYR B CE2 1 
ATOM   3766 C CZ  . TYR B 1 70  ? -22.443 12.975  23.913  1   47.8   ? 70  TYR B CZ  1 
ATOM   3767 O OH  . TYR B 1 70  ? -21.756 13.296  25.043  1   49.97  ? 70  TYR B OH  1 
ATOM   3768 N N   . CYS B 1 71  ? -24.915 14.661  18.934  1   41.79  ? 71  CYS B N   1 
ATOM   3769 C CA  . CYS B 1 71  ? -24.356 16.014  18.811  1   43.66  ? 71  CYS B CA  1 
ATOM   3770 C C   . CYS B 1 71  ? -25.438 17.091  18.906  1   44.59  ? 71  CYS B C   1 
ATOM   3771 O O   . CYS B 1 71  ? -25.265 18.092  19.606  1   44.51  ? 71  CYS B O   1 
ATOM   3772 C CB  . CYS B 1 71  ? -23.572 16.197  17.515  1   40.55  ? 71  CYS B CB  1 
ATOM   3773 S SG  . CYS B 1 71  ? -22.077 15.177  17.421  1   45.14  ? 71  CYS B SG  1 
ATOM   3774 N N   . LEU B 1 72  ? -26.583 16.849  18.263  1   47.88  ? 72  LEU B N   1 
ATOM   3775 C CA  . LEU B 1 72  ? -27.661 17.82   18.224  1   54.33  ? 72  LEU B CA  1 
ATOM   3776 C C   . LEU B 1 72  ? -28.475 17.832  19.519  1   54.05  ? 72  LEU B C   1 
ATOM   3777 O O   . LEU B 1 72  ? -29.32  18.702  19.65   1   57.59  ? 72  LEU B O   1 
ATOM   3778 C CB  . LEU B 1 72  ? -28.457 17.606  16.933  1   60.97  ? 72  LEU B CB  1 
ATOM   3779 C CG  . LEU B 1 72  ? -27.608 17.668  15.641  1   59.26  ? 72  LEU B CG  1 
ATOM   3780 C CD1 . LEU B 1 72  ? -28.475 17.819  14.395  1   62.96  ? 72  LEU B CD1 1 
ATOM   3781 C CD2 . LEU B 1 72  ? -26.452 18.716  15.625  1   58.45  ? 72  LEU B CD2 1 
ATOM   3782 N N   . ASN B 1 73  ? -28.16  16.964  20.498  1   50.83  ? 73  ASN B N   1 
ATOM   3783 C CA  . ASN B 1 73  ? -28.644 17.066  21.872  1   50.73  ? 73  ASN B CA  1 
ATOM   3784 C C   . ASN B 1 73  ? -27.66  17.72   22.848  1   46.26  ? 73  ASN B C   1 
ATOM   3785 O O   . ASN B 1 73  ? -28.054 17.972  23.986  1   46.15  ? 73  ASN B O   1 
ATOM   3786 C CB  . ASN B 1 73  ? -29.073 15.697  22.408  1   52     ? 73  ASN B CB  1 
ATOM   3787 C CG  . ASN B 1 73  ? -30.561 15.546  22.26   1   57.55  ? 73  ASN B CG  1 
ATOM   3788 O OD1 . ASN B 1 73  ? -31.307 16.079  23.084  1   61.62  ? 73  ASN B OD1 1 
ATOM   3789 N ND2 . ASN B 1 73  ? -31.001 14.899  21.191  1   60.4   ? 73  ASN B ND2 1 
ATOM   3790 N N   . LEU B 1 74  ? -26.418 18.003  22.44   1   45.49  ? 74  LEU B N   1 
ATOM   3791 C CA  . LEU B 1 74  ? -25.414 18.56   23.339  1   45.05  ? 74  LEU B CA  1 
ATOM   3792 C C   . LEU B 1 74  ? -25.774 19.995  23.722  1   45.61  ? 74  LEU B C   1 
ATOM   3793 O O   . LEU B 1 74  ? -26.355 20.74   22.93   1   46.41  ? 74  LEU B O   1 
ATOM   3794 C CB  . LEU B 1 74  ? -24.02  18.541  22.709  1   45.48  ? 74  LEU B CB  1 
ATOM   3795 C CG  . LEU B 1 74  ? -23.319 17.19   22.593  1   45.22  ? 74  LEU B CG  1 
ATOM   3796 C CD1 . LEU B 1 74  ? -22.129 17.366  21.678  1   44.27  ? 74  LEU B CD1 1 
ATOM   3797 C CD2 . LEU B 1 74  ? -22.862 16.633  23.953  1   46.95  ? 74  LEU B CD2 1 
ATOM   3798 N N   . ASP B 1 75  ? -25.401 20.358  24.952  1   44.83  ? 75  ASP B N   1 
ATOM   3799 C CA  . ASP B 1 75  ? -25.349 21.737  25.397  1   46.74  ? 75  ASP B CA  1 
ATOM   3800 C C   . ASP B 1 75  ? -24.201 22.417  24.657  1   45.48  ? 75  ASP B C   1 
ATOM   3801 O O   . ASP B 1 75  ? -23.039 22.078  24.873  1   44.74  ? 75  ASP B O   1 
ATOM   3802 C CB  . ASP B 1 75  ? -25.178 21.804  26.906  1   47.08  ? 75  ASP B CB  1 
ATOM   3803 C CG  . ASP B 1 75  ? -25.094 23.185  27.538  1   49.08  ? 75  ASP B CG  1 
ATOM   3804 O OD1 . ASP B 1 75  ? -24.925 24.191  26.808  1   45.28  ? 75  ASP B OD1 1 
ATOM   3805 O OD2 . ASP B 1 75  ? -25.16  23.238  28.791  1   51.29  ? 75  ASP B OD2 1 
ATOM   3806 N N   . VAL B 1 76  ? -24.538 23.437  23.848  1   46.38  ? 76  VAL B N   1 
ATOM   3807 C CA  . VAL B 1 76  ? -23.6   24.017  22.897  1   44.44  ? 76  VAL B CA  1 
ATOM   3808 C C   . VAL B 1 76  ? -22.557 24.901  23.596  1   42.98  ? 76  VAL B C   1 
ATOM   3809 O O   . VAL B 1 76  ? -21.552 25.232  22.983  1   41.68  ? 76  VAL B O   1 
ATOM   3810 C CB  . VAL B 1 76  ? -24.317 24.755  21.749  1   46.62  ? 76  VAL B CB  1 
ATOM   3811 C CG1 . VAL B 1 76  ? -25.156 23.786  20.944  1   48.07  ? 76  VAL B CG1 1 
ATOM   3812 C CG2 . VAL B 1 76  ? -25.159 25.935  22.202  1   47.61  ? 76  VAL B CG2 1 
ATOM   3813 N N   . LYS B 1 77  ? -22.756 25.206  24.891  1   43.36  ? 77  LYS B N   1 
ATOM   3814 C CA  . LYS B 1 77  ? -21.798 25.947  25.693  1   42.65  ? 77  LYS B CA  1 
ATOM   3815 C C   . LYS B 1 77  ? -20.651 25.081  26.203  1   43.04  ? 77  LYS B C   1 
ATOM   3816 O O   . LYS B 1 77  ? -19.699 25.655  26.723  1   44.71  ? 77  LYS B O   1 
ATOM   3817 C CB  . LYS B 1 77  ? -22.509 26.659  26.848  1   45.3   ? 77  LYS B CB  1 
ATOM   3818 C CG  . LYS B 1 77  ? -23.654 27.584  26.458  1   48.57  ? 77  LYS B CG  1 
ATOM   3819 C CD  . LYS B 1 77  ? -24.287 28.451  27.555  1   52.22  ? 77  LYS B CD  1 
ATOM   3820 C CE  . LYS B 1 77  ? -24.632 27.756  28.817  1   55.17  ? 77  LYS B CE  1 
ATOM   3821 N NZ  . LYS B 1 77  ? -25.394 26.516  28.606  1   58.18  ? 77  LYS B NZ  1 
ATOM   3822 N N   . THR B 1 78  ? -20.65  23.754  25.952  1   45.7   ? 78  THR B N   1 
ATOM   3823 C CA  . THR B 1 78  ? -19.679 22.84   26.56   1   45.59  ? 78  THR B CA  1 
ATOM   3824 C C   . THR B 1 78  ? -18.484 22.553  25.652  1   43.98  ? 78  THR B C   1 
ATOM   3825 O O   . THR B 1 78  ? -18.56  22.653  24.415  1   40.09  ? 78  THR B O   1 
ATOM   3826 C CB  . THR B 1 78  ? -20.34  21.517  26.961  1   44.24  ? 78  THR B CB  1 
ATOM   3827 O OG1 . THR B 1 78  ? -20.719 20.83   25.773  1   41.32  ? 78  THR B OG1 1 
ATOM   3828 C CG2 . THR B 1 78  ? -21.515 21.686  27.912  1   48.62  ? 78  THR B CG2 1 
ATOM   3829 N N   . LYS B 1 79  ? -17.39  22.116  26.306  1   42.22  ? 79  LYS B N   1 
ATOM   3830 C CA  . LYS B 1 79  ? -16.248 21.476  25.669  1   41.68  ? 79  LYS B CA  1 
ATOM   3831 C C   . LYS B 1 79  ? -16.677 20.357  24.716  1   41.55  ? 79  LYS B C   1 
ATOM   3832 O O   . LYS B 1 79  ? -16.106 20.183  23.607  1   36.71  ? 79  LYS B O   1 
ATOM   3833 C CB  . LYS B 1 79  ? -15.302 20.922  26.743  1   43.88  ? 79  LYS B CB  1 
ATOM   3834 C CG  . LYS B 1 79  ? -13.975 20.416  26.203  1   43.64  ? 79  LYS B CG  1 
ATOM   3835 C CD  . LYS B 1 79  ? -13.093 19.768  27.26   1   46.48  ? 79  LYS B CD  1 
ATOM   3836 C CE  . LYS B 1 79  ? -11.908 19.128  26.637  1   48.3   ? 79  LYS B CE  1 
ATOM   3837 N NZ  . LYS B 1 79  ? -11.254 18.222  27.577  1   52.2   ? 79  LYS B NZ  1 
ATOM   3838 N N   . ALA B 1 80  ? -17.649 19.558  25.173  1   39.71  ? 80  ALA B N   1 
ATOM   3839 C CA  . ALA B 1 80  ? -18.132 18.464  24.351  1   39.47  ? 80  ALA B CA  1 
ATOM   3840 C C   . ALA B 1 80  ? -18.688 18.973  23.021  1   37.97  ? 80  ALA B C   1 
ATOM   3841 O O   . ALA B 1 80  ? -18.404 18.383  21.977  1   35.23  ? 80  ALA B O   1 
ATOM   3842 C CB  . ALA B 1 80  ? -19.141 17.647  25.107  1   38.36  ? 80  ALA B CB  1 
ATOM   3843 N N   . ALA B 1 81  ? -19.487 20.049  23.051  1   39.9   ? 81  ALA B N   1 
ATOM   3844 C CA  . ALA B 1 81  ? -20.046 20.614  21.818  1   38.67  ? 81  ALA B CA  1 
ATOM   3845 C C   . ALA B 1 81  ? -18.955 21.146  20.888  1   36.97  ? 81  ALA B C   1 
ATOM   3846 O O   . ALA B 1 81  ? -19.046 20.993  19.657  1   32.34  ? 81  ALA B O   1 
ATOM   3847 C CB  . ALA B 1 81  ? -21.045 21.702  22.12   1   38.61  ? 81  ALA B CB  1 
ATOM   3848 N N   . ARG B 1 82  ? -17.961 21.849  21.467  1   36.83  ? 82  ARG B N   1 
ATOM   3849 C CA  . ARG B 1 82  ? -16.835 22.339  20.696  1   35.4   ? 82  ARG B CA  1 
ATOM   3850 C C   . ARG B 1 82  ? -16.057 21.197  20.029  1   36.82  ? 82  ARG B C   1 
ATOM   3851 O O   . ARG B 1 82  ? -15.73  21.295  18.837  1   32.37  ? 82  ARG B O   1 
ATOM   3852 C CB  . ARG B 1 82  ? -15.955 23.231  21.565  1   38.97  ? 82  ARG B CB  1 
ATOM   3853 C CG  . ARG B 1 82  ? -16.676 24.525  21.925  1   37.6   ? 82  ARG B CG  1 
ATOM   3854 C CD  . ARG B 1 82  ? -15.72  25.478  22.602  1   39.07  ? 82  ARG B CD  1 
ATOM   3855 N NE  . ARG B 1 82  ? -15.272 25.055  23.935  1   38.36  ? 82  ARG B NE  1 
ATOM   3856 C CZ  . ARG B 1 82  ? -15.965 25.23   25.062  1   40.2   ? 82  ARG B CZ  1 
ATOM   3857 N NH1 . ARG B 1 82  ? -15.402 24.849  26.194  1   41.39  ? 82  ARG B NH1 1 
ATOM   3858 N NH2 . ARG B 1 82  ? -17.184 25.792  25.096  1   40.98  ? 82  ARG B NH2 1 
ATOM   3859 N N   . SER B 1 83  ? -15.853 20.082  20.766  1   34.43  ? 83  SER B N   1 
ATOM   3860 C CA  . SER B 1 83  ? -15.228 18.895  20.187  1   34.58  ? 83  SER B CA  1 
ATOM   3861 C C   . SER B 1 83  ? -16.078 18.29   19.064  1   32.81  ? 83  SER B C   1 
ATOM   3862 O O   . SER B 1 83  ? -15.53  17.823  18.069  1   32.73  ? 83  SER B O   1 
ATOM   3863 C CB  . SER B 1 83  ? -14.928 17.867  21.243  1   34.49  ? 83  SER B CB  1 
ATOM   3864 O OG  . SER B 1 83  ? -14.183 18.432  22.312  1   36.39  ? 83  SER B OG  1 
ATOM   3865 N N   . ALA B 1 84  ? -17.401 18.259  19.267  1   35.69  ? 84  ALA B N   1 
ATOM   3866 C CA  . ALA B 1 84  ? -18.374 17.742  18.309  1   36.39  ? 84  ALA B CA  1 
ATOM   3867 C C   . ALA B 1 84  ? -18.351 18.536  17.008  1   33.65  ? 84  ALA B C   1 
ATOM   3868 O O   . ALA B 1 84  ? -18.507 17.96   15.935  1   34.89  ? 84  ALA B O   1 
ATOM   3869 C CB  . ALA B 1 84  ? -19.764 17.747  18.929  1   38.63  ? 84  ALA B CB  1 
ATOM   3870 N N   . LEU B 1 85  ? -18.153 19.857  17.09   1   32.5   ? 85  LEU B N   1 
ATOM   3871 C CA  . LEU B 1 85  ? -18.001 20.668  15.89   1   30.66  ? 85  LEU B CA  1 
ATOM   3872 C C   . LEU B 1 85  ? -16.769 20.254  15.084  1   29.34  ? 85  LEU B C   1 
ATOM   3873 O O   . LEU B 1 85  ? -16.85  20.149  13.866  1   30.57  ? 85  LEU B O   1 
ATOM   3874 C CB  . LEU B 1 85  ? -17.983 22.159  16.273  1   31.03  ? 85  LEU B CB  1 
ATOM   3875 C CG  . LEU B 1 85  ? -17.797 23.147  15.109  1   30.96  ? 85  LEU B CG  1 
ATOM   3876 C CD1 . LEU B 1 85  ? -18.773 22.892  13.973  1   30.92  ? 85  LEU B CD1 1 
ATOM   3877 C CD2 . LEU B 1 85  ? -18.011 24.55   15.658  1   34.15  ? 85  LEU B CD2 1 
ATOM   3878 N N   . GLU B 1 86  ? -15.621 20.041  15.738  1   28.91  ? 86  GLU B N   1 
ATOM   3879 C CA  . GLU B 1 86  ? -14.429 19.567  15.059  1   29.16  ? 86  GLU B CA  1 
ATOM   3880 C C   . GLU B 1 86  ? -14.694 18.192  14.45   1   29.74  ? 86  GLU B C   1 
ATOM   3881 O O   . GLU B 1 86  ? -14.302 17.951  13.339  1   30.07  ? 86  GLU B O   1 
ATOM   3882 C CB  . GLU B 1 86  ? -13.207 19.597  15.992  1   31.33  ? 86  GLU B CB  1 
ATOM   3883 C CG  . GLU B 1 86  ? -11.972 18.868  15.485  1   30.25  ? 86  GLU B CG  1 
ATOM   3884 C CD  . GLU B 1 86  ? -11.44  19.392  14.159  1   31.33  ? 86  GLU B CD  1 
ATOM   3885 O OE1 . GLU B 1 86  ? -11.881 20.474  13.711  1   32.42  ? 86  GLU B OE1 1 
ATOM   3886 O OE2 . GLU B 1 86  ? -10.519 18.74   13.605  1   31.44  ? 86  GLU B OE2 1 
ATOM   3887 N N   . TYR B 1 87  ? -15.339 17.284  15.206  1   31.8   ? 87  TYR B N   1 
ATOM   3888 C CA  . TYR B 1 87  ? -15.719 15.984  14.678  1   32.31  ? 87  TYR B CA  1 
ATOM   3889 C C   . TYR B 1 87  ? -16.515 16.169  13.377  1   28.83  ? 87  TYR B C   1 
ATOM   3890 O O   . TYR B 1 87  ? -16.199 15.57   12.349  1   31.38  ? 87  TYR B O   1 
ATOM   3891 C CB  . TYR B 1 87  ? -16.458 15.212  15.778  1   31.7   ? 87  TYR B CB  1 
ATOM   3892 C CG  . TYR B 1 87  ? -17.165 13.959  15.289  1   31.65  ? 87  TYR B CG  1 
ATOM   3893 C CD1 . TYR B 1 87  ? -16.466 12.773  15.131  1   32.07  ? 87  TYR B CD1 1 
ATOM   3894 C CD2 . TYR B 1 87  ? -18.515 13.978  14.932  1   33.91  ? 87  TYR B CD2 1 
ATOM   3895 C CE1 . TYR B 1 87  ? -17.088 11.649  14.591  1   34.03  ? 87  TYR B CE1 1 
ATOM   3896 C CE2 . TYR B 1 87  ? -19.164 12.851  14.447  1   34.61  ? 87  TYR B CE2 1 
ATOM   3897 C CZ  . TYR B 1 87  ? -18.441 11.685  14.273  1   34.27  ? 87  TYR B CZ  1 
ATOM   3898 O OH  . TYR B 1 87  ? -19.056 10.575  13.779  1   35.97  ? 87  TYR B OH  1 
ATOM   3899 N N   . ALA B 1 88  ? -17.576 16.947  13.448  1   27.21  ? 88  ALA B N   1 
ATOM   3900 C CA  . ALA B 1 88  ? -18.466 17.152  12.314  1   30.81  ? 88  ALA B CA  1 
ATOM   3901 C C   . ALA B 1 88  ? -17.713 17.782  11.127  1   30.73  ? 88  ALA B C   1 
ATOM   3902 O O   . ALA B 1 88  ? -17.807 17.326  9.98    1   31.77  ? 88  ALA B O   1 
ATOM   3903 C CB  . ALA B 1 88  ? -19.647 17.983  12.762  1   32.17  ? 88  ALA B CB  1 
ATOM   3904 N N   . ASP B 1 89  ? -16.891 18.8    11.396  1   30.56  ? 89  ASP B N   1 
ATOM   3905 C CA  . ASP B 1 89  ? -16.148 19.445  10.31   1   28.93  ? 89  ASP B CA  1 
ATOM   3906 C C   . ASP B 1 89  ? -15.093 18.513  9.707   1   27.54  ? 89  ASP B C   1 
ATOM   3907 O O   . ASP B 1 89  ? -15     18.417  8.48    1   30.21  ? 89  ASP B O   1 
ATOM   3908 C CB  . ASP B 1 89  ? -15.484 20.744  10.737  1   29.15  ? 89  ASP B CB  1 
ATOM   3909 C CG  . ASP B 1 89  ? -14.841 21.502  9.584   1   29.77  ? 89  ASP B CG  1 
ATOM   3910 O OD1 . ASP B 1 89  ? -15.574 22.26   8.902   1   30.25  ? 89  ASP B OD1 1 
ATOM   3911 O OD2 . ASP B 1 89  ? -13.651 21.22   9.326   1   29.94  ? 89  ASP B OD2 1 
ATOM   3912 N N   . ALA B 1 90  ? -14.323 17.824  10.549  1   28     ? 90  ALA B N   1 
ATOM   3913 C CA  . ALA B 1 90  ? -13.312 16.871  10.088  1   28.68  ? 90  ALA B CA  1 
ATOM   3914 C C   . ALA B 1 90  ? -13.915 15.814  9.168   1   28.92  ? 90  ALA B C   1 
ATOM   3915 O O   . ALA B 1 90  ? -13.292 15.437  8.183   1   28.69  ? 90  ALA B O   1 
ATOM   3916 C CB  . ALA B 1 90  ? -12.666 16.21   11.273  1   28.09  ? 90  ALA B CB  1 
ATOM   3917 N N   . ASN B 1 91  ? -15.1   15.315  9.514   1   28.22  ? 91  ASN B N   1 
ATOM   3918 C CA  . ASN B 1 91  ? -15.769 14.253  8.775   1   31.06  ? 91  ASN B CA  1 
ATOM   3919 C C   . ASN B 1 91  ? -16.542 14.798  7.578   1   35.41  ? 91  ASN B C   1 
ATOM   3920 O O   . ASN B 1 91  ? -17.053 13.997  6.818   1   34.42  ? 91  ASN B O   1 
ATOM   3921 C CB  . ASN B 1 91  ? -16.73  13.46   9.656   1   31.34  ? 91  ASN B CB  1 
ATOM   3922 C CG  . ASN B 1 91  ? -16.052 12.418  10.505  1   32.06  ? 91  ASN B CG  1 
ATOM   3923 O OD1 . ASN B 1 91  ? -15.698 11.346  10.002  1   31.78  ? 91  ASN B OD1 1 
ATOM   3924 N ND2 . ASN B 1 91  ? -15.745 12.757  11.748  1   31.23  ? 91  ASN B ND2 1 
ATOM   3925 N N   . MET B 1 92  ? -16.679 16.132  7.44    1   32.88  ? 92  MET B N   1 
ATOM   3926 C CA  . MET B 1 92  ? -17.532 16.756  6.43    1   37.69  ? 92  MET B CA  1 
ATOM   3927 C C   . MET B 1 92  ? -18.987 16.283  6.571   1   38.92  ? 92  MET B C   1 
ATOM   3928 O O   . MET B 1 92  ? -19.702 16.112  5.574   1   35.54  ? 92  MET B O   1 
ATOM   3929 C CB  . MET B 1 92  ? -16.963 16.573  5.008   1   34.26  ? 92  MET B CB  1 
ATOM   3930 C CG  . MET B 1 92  ? -15.601 17.18   4.859   1   37.39  ? 92  MET B CG  1 
ATOM   3931 S SD  . MET B 1 92  ? -14.972 17.229  3.166   1   39.48  ? 92  MET B SD  1 
ATOM   3932 C CE  . MET B 1 92  ? -13.45  18.169  3.329   1   41     ? 92  MET B CE  1 
ATOM   3933 N N   . PHE B 1 93  ? -19.452 16.201  7.827   1   35.71  ? 93  PHE B N   1 
ATOM   3934 C CA  . PHE B 1 93  ? -20.847 15.958  8.146   1   35.76  ? 93  PHE B CA  1 
ATOM   3935 C C   . PHE B 1 93  ? -21.534 17.31   8.261   1   36.08  ? 93  PHE B C   1 
ATOM   3936 O O   . PHE B 1 93  ? -21.788 17.781  9.377   1   36.9   ? 93  PHE B O   1 
ATOM   3937 C CB  . PHE B 1 93  ? -20.95  15.145  9.438   1   36.63  ? 93  PHE B CB  1 
ATOM   3938 C CG  . PHE B 1 93  ? -20.433 13.713  9.402   1   37.52  ? 93  PHE B CG  1 
ATOM   3939 C CD1 . PHE B 1 93  ? -20.275 13.007  8.205   1   37.86  ? 93  PHE B CD1 1 
ATOM   3940 C CD2 . PHE B 1 93  ? -20.092 13.082  10.596  1   36.12  ? 93  PHE B CD2 1 
ATOM   3941 C CE1 . PHE B 1 93  ? -19.792 11.712  8.208   1   37.72  ? 93  PHE B CE1 1 
ATOM   3942 C CE2 . PHE B 1 93  ? -19.588 11.793  10.588  1   38.3   ? 93  PHE B CE2 1 
ATOM   3943 C CZ  . PHE B 1 93  ? -19.458 11.103  9.394   1   37.36  ? 93  PHE B CZ  1 
ATOM   3944 N N   . PHE B 1 94  ? -21.833 17.901  7.097   1   34.12  ? 94  PHE B N   1 
ATOM   3945 C CA  . PHE B 1 94  ? -22.228 19.309  7.007   1   39.09  ? 94  PHE B CA  1 
ATOM   3946 C C   . PHE B 1 94  ? -23.529 19.61   7.746   1   38.4   ? 94  PHE B C   1 
ATOM   3947 O O   . PHE B 1 94  ? -23.662 20.681  8.315   1   39.26  ? 94  PHE B O   1 
ATOM   3948 C CB  . PHE B 1 94  ? -22.335 19.778  5.541   1   39.55  ? 94  PHE B CB  1 
ATOM   3949 C CG  . PHE B 1 94  ? -21.052 19.655  4.721   1   38.76  ? 94  PHE B CG  1 
ATOM   3950 C CD1 . PHE B 1 94  ? -19.795 19.981  5.244   1   38.87  ? 94  PHE B CD1 1 
ATOM   3951 C CD2 . PHE B 1 94  ? -21.102 19.198  3.405   1   43.61  ? 94  PHE B CD2 1 
ATOM   3952 C CE1 . PHE B 1 94  ? -18.637 19.874  4.469   1   39.76  ? 94  PHE B CE1 1 
ATOM   3953 C CE2 . PHE B 1 94  ? -19.942 19.083  2.637   1   40.66  ? 94  PHE B CE2 1 
ATOM   3954 C CZ  . PHE B 1 94  ? -18.71  19.392  3.176   1   40.4   ? 94  PHE B CZ  1 
ATOM   3955 N N   . GLU B 1 95  ? -24.486 18.672  7.777   1   39.23  ? 95  GLU B N   1 
ATOM   3956 C CA  . GLU B 1 95  ? -25.752 18.92   8.44    1   44.22  ? 95  GLU B CA  1 
ATOM   3957 C C   . GLU B 1 95  ? -25.548 18.976  9.953   1   42.1   ? 95  GLU B C   1 
ATOM   3958 O O   . GLU B 1 95  ? -26.184 19.78   10.599  1   42.28  ? 95  GLU B O   1 
ATOM   3959 C CB  . GLU B 1 95  ? -26.822 17.889  8.099   1   50.12  ? 95  GLU B CB  1 
ATOM   3960 C CG  . GLU B 1 95  ? -27.147 17.879  6.606   1   53.63  ? 95  GLU B CG  1 
ATOM   3961 C CD  . GLU B 1 95  ? -28.336 16.994  6.229   1   62.05  ? 95  GLU B CD  1 
ATOM   3962 O OE1 . GLU B 1 95  ? -29.277 16.715  7.032   1   65.79  ? 95  GLU B OE1 1 
ATOM   3963 O OE2 . GLU B 1 95  ? -28.287 16.531  5.077   1   65.38  ? 95  GLU B OE2 1 
ATOM   3964 N N   . ILE B 1 96  ? -24.626 18.171  10.504  1   40.81  ? 96  ILE B N   1 
ATOM   3965 C CA  . ILE B 1 96  ? -24.331 18.251  11.928  1   39.62  ? 96  ILE B CA  1 
ATOM   3966 C C   . ILE B 1 96  ? -23.622 19.583  12.197  1   37.72  ? 96  ILE B C   1 
ATOM   3967 O O   . ILE B 1 96  ? -23.98  20.303  13.125  1   38.93  ? 96  ILE B O   1 
ATOM   3968 C CB  . ILE B 1 96  ? -23.518 17.045  12.434  1   40.22  ? 96  ILE B CB  1 
ATOM   3969 C CG1 . ILE B 1 96  ? -24.211 15.676  12.114  1   40.1   ? 96  ILE B CG1 1 
ATOM   3970 C CG2 . ILE B 1 96  ? -23.267 17.168  13.936  1   40.79  ? 96  ILE B CG2 1 
ATOM   3971 C CD1 . ILE B 1 96  ? -23.335 14.479  12.39   1   40.58  ? 96  ILE B CD1 1 
ATOM   3972 N N   . GLU B 1 97  ? -22.574 19.848  11.421  1   35.25  ? 97  GLU B N   1 
ATOM   3973 C CA  . GLU B 1 97  ? -21.738 21.035  11.575  1   36.58  ? 97  GLU B CA  1 
ATOM   3974 C C   . GLU B 1 97  ? -22.551 22.322  11.542  1   33.93  ? 97  GLU B C   1 
ATOM   3975 O O   . GLU B 1 97  ? -22.403 23.178  12.411  1   36.39  ? 97  GLU B O   1 
ATOM   3976 C CB  . GLU B 1 97  ? -20.69  20.986  10.463  1   38.23  ? 97  GLU B CB  1 
ATOM   3977 C CG  . GLU B 1 97  ? -19.859 22.247  10.415  1   36.44  ? 97  GLU B CG  1 
ATOM   3978 C CD  . GLU B 1 97  ? -18.614 22.088  9.585   1   36.2   ? 97  GLU B CD  1 
ATOM   3979 O OE1 . GLU B 1 97  ? -18.534 21.207  8.698   1   36.88  ? 97  GLU B OE1 1 
ATOM   3980 O OE2 . GLU B 1 97  ? -17.746 22.948  9.826   1   35.4   ? 97  GLU B OE2 1 
ATOM   3981 N N   . ASP B 1 98  ? -23.395 22.477  10.525  1   34.75  ? 98  ASP B N   1 
ATOM   3982 C CA  . ASP B 1 98  ? -24.128 23.724  10.324  1   37.74  ? 98  ASP B CA  1 
ATOM   3983 C C   . ASP B 1 98  ? -25.125 23.979  11.452  1   37.4   ? 98  ASP B C   1 
ATOM   3984 O O   . ASP B 1 98  ? -25.317 25.137  11.86   1   38.33  ? 98  ASP B O   1 
ATOM   3985 C CB  . ASP B 1 98  ? -24.746 23.777  8.936   1   41.15  ? 98  ASP B CB  1 
ATOM   3986 C CG  . ASP B 1 98  ? -23.743 23.796  7.783   1   41.57  ? 98  ASP B CG  1 
ATOM   3987 O OD1 . ASP B 1 98  ? -22.53  24.093  7.977   1   40.1   ? 98  ASP B OD1 1 
ATOM   3988 O OD2 . ASP B 1 98  ? -24.176 23.478  6.675   1   41.01  ? 98  ASP B OD2 1 
ATOM   3989 N N   . ALA B 1 99  ? -25.747 22.9    11.971  1   38.62  ? 99  ALA B N   1 
ATOM   3990 C CA  . ALA B 1 99  ? -26.672 23.038  13.093  1   40.57  ? 99  ALA B CA  1 
ATOM   3991 C C   . ALA B 1 99  ? -25.917 23.435  14.373  1   38.73  ? 99  ALA B C   1 
ATOM   3992 O O   . ALA B 1 99  ? -26.358 24.304  15.124  1   40.56  ? 99  ALA B O   1 
ATOM   3993 C CB  . ALA B 1 99  ? -27.434 21.738  13.259  1   40.86  ? 99  ALA B CB  1 
ATOM   3994 N N   . LEU B 1 100 ? -24.75  22.813  14.609  1   38.82  ? 100 LEU B N   1 
ATOM   3995 C CA  . LEU B 1 100 ? -23.894 23.196  15.735  1   38.33  ? 100 LEU B CA  1 
ATOM   3996 C C   . LEU B 1 100 ? -23.429 24.658  15.608  1   38.82  ? 100 LEU B C   1 
ATOM   3997 O O   . LEU B 1 100 ? -23.534 25.452  16.553  1   36.29  ? 100 LEU B O   1 
ATOM   3998 C CB  . LEU B 1 100 ? -22.721 22.232  15.858  1   38.49  ? 100 LEU B CB  1 
ATOM   3999 C CG  . LEU B 1 100 ? -23.023 20.862  16.479  1   39.54  ? 100 LEU B CG  1 
ATOM   4000 C CD1 . LEU B 1 100 ? -21.794 19.981  16.317  1   41.13  ? 100 LEU B CD1 1 
ATOM   4001 C CD2 . LEU B 1 100 ? -23.435 20.947  17.954  1   43.83  ? 100 LEU B CD2 1 
ATOM   4002 N N   . ILE B 1 101 ? -22.957 25.031  14.405  1   37     ? 101 ILE B N   1 
ATOM   4003 C CA  . ILE B 1 101 ? -22.509 26.401  14.171  1   35.34  ? 101 ILE B CA  1 
ATOM   4004 C C   . ILE B 1 101 ? -23.609 27.41   14.53   1   37.98  ? 101 ILE B C   1 
ATOM   4005 O O   . ILE B 1 101 ? -23.366 28.367  15.281  1   40.11  ? 101 ILE B O   1 
ATOM   4006 C CB  . ILE B 1 101 ? -22.009 26.569  12.724  1   34.43  ? 101 ILE B CB  1 
ATOM   4007 C CG1 . ILE B 1 101 ? -20.66  25.912  12.524  1   33.9   ? 101 ILE B CG1 1 
ATOM   4008 C CG2 . ILE B 1 101 ? -21.969 28.046  12.367  1   36.13  ? 101 ILE B CG2 1 
ATOM   4009 C CD1 . ILE B 1 101 ? -20.204 25.765  11.065  1   33.07  ? 101 ILE B CD1 1 
ATOM   4010 N N   . ASP B 1 102 ? -24.816 27.191  13.981  1   41.85  ? 102 ASP B N   1 
ATOM   4011 C CA  . ASP B 1 102 ? -25.922 28.121  14.119  1   44.68  ? 102 ASP B CA  1 
ATOM   4012 C C   . ASP B 1 102 ? -26.294 28.315  15.593  1   46.17  ? 102 ASP B C   1 
ATOM   4013 O O   . ASP B 1 102 ? -26.487 29.455  16.033  1   44.49  ? 102 ASP B O   1 
ATOM   4014 C CB  . ASP B 1 102 ? -27.106 27.712  13.256  1   49.54  ? 102 ASP B CB  1 
ATOM   4015 C CG  . ASP B 1 102 ? -28.114 28.816  12.939  1   57.5   ? 102 ASP B CG  1 
ATOM   4016 O OD1 . ASP B 1 102 ? -27.72  29.803  12.292  1   57.6   ? 102 ASP B OD1 1 
ATOM   4017 O OD2 . ASP B 1 102 ? -29.309 28.678  13.311  1   68.38  ? 102 ASP B OD2 1 
ATOM   4018 N N   . SER B 1 103 ? -26.31  27.237  16.383  1   41.23  ? 103 SER B N   1 
ATOM   4019 C CA  . SER B 1 103 ? -26.667 27.397  17.788  1   44.35  ? 103 SER B CA  1 
ATOM   4020 C C   . SER B 1 103 ? -25.472 27.857  18.634  1   42.58  ? 103 SER B C   1 
ATOM   4021 O O   . SER B 1 103 ? -25.681 28.499  19.665  1   43.89  ? 103 SER B O   1 
ATOM   4022 C CB  . SER B 1 103 ? -27.378 26.191  18.34   1   45.06  ? 103 SER B CB  1 
ATOM   4023 O OG  . SER B 1 103 ? -26.7   25.005  18.022  1   48.45  ? 103 SER B OG  1 
ATOM   4024 N N   . MET B 1 104 ? -24.229 27.603  18.207  1   41.37  ? 104 MET B N   1 
ATOM   4025 C CA  . MET B 1 104 ? -23.053 28.074  18.94   1   41.04  ? 104 MET B CA  1 
ATOM   4026 C C   . MET B 1 104 ? -22.854 29.59   18.793  1   40.59  ? 104 MET B C   1 
ATOM   4027 O O   . MET B 1 104 ? -22.536 30.271  19.776  1   39.49  ? 104 MET B O   1 
ATOM   4028 C CB  . MET B 1 104 ? -21.818 27.281  18.528  1   42.77  ? 104 MET B CB  1 
ATOM   4029 C CG  . MET B 1 104 ? -21.868 25.901  19.116  1   43.09  ? 104 MET B CG  1 
ATOM   4030 S SD  . MET B 1 104 ? -20.628 24.749  18.517  1   44.32  ? 104 MET B SD  1 
ATOM   4031 C CE  . MET B 1 104 ? -19.249 25.519  19.355  1   44.69  ? 104 MET B CE  1 
ATOM   4032 N N   . ILE B 1 105 ? -23.098 30.111  17.585  1   40.85  ? 105 ILE B N   1 
ATOM   4033 C CA  . ILE B 1 105 ? -22.998 31.539  17.329  1   46.73  ? 105 ILE B CA  1 
ATOM   4034 C C   . ILE B 1 105 ? -23.938 32.336  18.252  1   49.84  ? 105 ILE B C   1 
ATOM   4035 O O   . ILE B 1 105 ? -23.545 33.408  18.698  1   55.69  ? 105 ILE B O   1 
ATOM   4036 C CB  . ILE B 1 105 ? -23.205 31.829  15.827  1   46.89  ? 105 ILE B CB  1 
ATOM   4037 C CG1 . ILE B 1 105 ? -21.97  31.42   15.056  1   45.64  ? 105 ILE B CG1 1 
ATOM   4038 C CG2 . ILE B 1 105 ? -23.589 33.295  15.569  1   49.72  ? 105 ILE B CG2 1 
ATOM   4039 C CD1 . ILE B 1 105 ? -22.179 31.342  13.566  1   48.27  ? 105 ILE B CD1 1 
ATOM   4040 N N   . SER B 1 106 ? -25.131 31.809  18.562  1   51.4   ? 106 SER B N   1 
ATOM   4041 C CA  . SER B 1 106 ? -26.143 32.482  19.37   1   53.4   ? 106 SER B CA  1 
ATOM   4042 C C   . SER B 1 106 ? -25.942 32.324  20.881  1   53.44  ? 106 SER B C   1 
ATOM   4043 O O   . SER B 1 106 ? -26.643 32.994  21.619  1   54.38  ? 106 SER B O   1 
ATOM   4044 C CB  . SER B 1 106 ? -27.517 31.943  19.038  1   56.92  ? 106 SER B CB  1 
ATOM   4045 O OG  . SER B 1 106 ? -27.843 32.222  17.692  1   61.48  ? 106 SER B OG  1 
ATOM   4046 N N   . CYS B 1 107 ? -25.094 31.405  21.364  1   50.81  ? 107 CYS B N   1 
ATOM   4047 C CA  . CYS B 1 107 ? -25.082 31.081  22.786  1   52.84  ? 107 CYS B CA  1 
ATOM   4048 C C   . CYS B 1 107 ? -24.206 32.09   23.518  1   50.78  ? 107 CYS B C   1 
ATOM   4049 O O   . CYS B 1 107 ? -23.459 32.837  22.895  1   52.4   ? 107 CYS B O   1 
ATOM   4050 C CB  . CYS B 1 107 ? -24.657 29.632  23.028  1   51.85  ? 107 CYS B CB  1 
ATOM   4051 S SG  . CYS B 1 107 ? -22.866 29.365  22.968  1   51.53  ? 107 CYS B SG  1 
ATOM   4052 N N   . SER B 1 108 ? -24.242 32.024  24.851  1   49.49  ? 108 SER B N   1 
ATOM   4053 C CA  . SER B 1 108 ? -23.587 32.991  25.718  1   51.45  ? 108 SER B CA  1 
ATOM   4054 C C   . SER B 1 108 ? -22.166 32.571  26.114  1   50.61  ? 108 SER B C   1 
ATOM   4055 O O   . SER B 1 108 ? -21.516 33.285  26.864  1   56     ? 108 SER B O   1 
ATOM   4056 C CB  . SER B 1 108 ? -24.45  33.229  26.934  1   53.04  ? 108 SER B CB  1 
ATOM   4057 O OG  . SER B 1 108 ? -24.714 31.98   27.555  1   53.93  ? 108 SER B OG  1 
ATOM   4058 N N   . ASN B 1 109 ? -21.671 31.424  25.644  1   45.75  ? 109 ASN B N   1 
ATOM   4059 C CA  . ASN B 1 109 ? -20.319 31.01   25.925  1   44.82  ? 109 ASN B CA  1 
ATOM   4060 C C   . ASN B 1 109 ? -19.415 31.583  24.836  1   42.86  ? 109 ASN B C   1 
ATOM   4061 O O   . ASN B 1 109 ? -19.617 31.29   23.647  1   40.38  ? 109 ASN B O   1 
ATOM   4062 C CB  . ASN B 1 109 ? -20.226 29.495  26.012  1   44.72  ? 109 ASN B CB  1 
ATOM   4063 C CG  . ASN B 1 109 ? -18.835 29.077  26.397  1   45.65  ? 109 ASN B CG  1 
ATOM   4064 O OD1 . ASN B 1 109 ? -17.93  29.049  25.561  1   44.01  ? 109 ASN B OD1 1 
ATOM   4065 N ND2 . ASN B 1 109 ? -18.627 28.759  27.658  1   48.38  ? 109 ASN B ND2 1 
ATOM   4066 N N   . MET B 1 110 ? -18.392 32.351  25.257  1   42.76  ? 110 MET B N   1 
ATOM   4067 C CA  . MET B 1 110 ? -17.559 33.111  24.326  1   47.11  ? 110 MET B CA  1 
ATOM   4068 C C   . MET B 1 110 ? -16.685 32.187  23.468  1   44.53  ? 110 MET B C   1 
ATOM   4069 O O   . MET B 1 110 ? -16.441 32.489  22.299  1   41.34  ? 110 MET B O   1 
ATOM   4070 C CB  . MET B 1 110 ? -16.661 34.131  25.049  1   52.06  ? 110 MET B CB  1 
ATOM   4071 C CG  . MET B 1 110 ? -17.412 35.284  25.677  1   58.04  ? 110 MET B CG  1 
ATOM   4072 S SD  . MET B 1 110 ? -18.284 36.341  24.499  1   68.18  ? 110 MET B SD  1 
ATOM   4073 C CE  . MET B 1 110 ? -19.999 35.822  24.628  1   71.17  ? 110 MET B CE  1 
ATOM   4074 N N   . LYS B 1 111 ? -16.179 31.097  24.064  1   43.66  ? 111 LYS B N   1 
ATOM   4075 C CA  . LYS B 1 111 ? -15.418 30.078  23.357  1   44.59  ? 111 LYS B CA  1 
ATOM   4076 C C   . LYS B 1 111 ? -16.266 29.388  22.279  1   40.12  ? 111 LYS B C   1 
ATOM   4077 O O   . LYS B 1 111 ? -15.821 29.234  21.148  1   37.78  ? 111 LYS B O   1 
ATOM   4078 C CB  . LYS B 1 111 ? -14.859 29.021  24.318  1   50.59  ? 111 LYS B CB  1 
ATOM   4079 C CG  . LYS B 1 111 ? -13.43  29.227  24.707  1   60.6   ? 111 LYS B CG  1 
ATOM   4080 C CD  . LYS B 1 111 ? -12.927 28.157  25.659  1   64.09  ? 111 LYS B CD  1 
ATOM   4081 C CE  . LYS B 1 111 ? -11.698 28.645  26.334  1   70.63  ? 111 LYS B CE  1 
ATOM   4082 N NZ  . LYS B 1 111 ? -11.068 27.571  27.1    1   76.54  ? 111 LYS B NZ  1 
ATOM   4083 N N   . SER B 1 112 ? -17.448 28.902  22.664  1   39.76  ? 112 SER B N   1 
ATOM   4084 C CA  . SER B 1 112 ? -18.341 28.25   21.721  1   39.2   ? 112 SER B CA  1 
ATOM   4085 C C   . SER B 1 112 ? -18.725 29.228  20.607  1   39.46  ? 112 SER B C   1 
ATOM   4086 O O   . SER B 1 112 ? -18.775 28.851  19.444  1   37.98  ? 112 SER B O   1 
ATOM   4087 C CB  . SER B 1 112 ? -19.552 27.673  22.428  1   40.86  ? 112 SER B CB  1 
ATOM   4088 O OG  . SER B 1 112 ? -19.198 26.589  23.291  1   37.78  ? 112 SER B OG  1 
ATOM   4089 N N   . LYS B 1 113 ? -18.953 30.498  20.941  1   39.87  ? 113 LYS B N   1 
ATOM   4090 C CA  . LYS B 1 113 ? -19.248 31.502  19.926  1   42.82  ? 113 LYS B CA  1 
ATOM   4091 C C   . LYS B 1 113 ? -18.074 31.647  18.949  1   38.16  ? 113 LYS B C   1 
ATOM   4092 O O   . LYS B 1 113 ? -18.283 31.647  17.744  1   33.92  ? 113 LYS B O   1 
ATOM   4093 C CB  . LYS B 1 113 ? -19.635 32.792  20.64   1   45.84  ? 113 LYS B CB  1 
ATOM   4094 C CG  . LYS B 1 113 ? -20.206 33.885  19.764  1   53.28  ? 113 LYS B CG  1 
ATOM   4095 C CD  . LYS B 1 113 ? -20.507 35.189  20.507  1   57.29  ? 113 LYS B CD  1 
ATOM   4096 C CE  . LYS B 1 113 ? -21.502 35.121  21.631  1   63.29  ? 113 LYS B CE  1 
ATOM   4097 N NZ  . LYS B 1 113 ? -22.895 35.02   21.2    1   68.45  ? 113 LYS B NZ  1 
ATOM   4098 N N   . GLU B 1 114 ? -16.849 31.758  19.478  1   37.26  ? 114 GLU B N   1 
ATOM   4099 C CA  . GLU B 1 114 ? -15.65  31.87   18.657  1   36.41  ? 114 GLU B CA  1 
ATOM   4100 C C   . GLU B 1 114 ? -15.518 30.673  17.707  1   37.55  ? 114 GLU B C   1 
ATOM   4101 O O   . GLU B 1 114 ? -15.269 30.831  16.501  1   30.1   ? 114 GLU B O   1 
ATOM   4102 C CB  . GLU B 1 114 ? -14.419 32.044  19.546  1   35.28  ? 114 GLU B CB  1 
ATOM   4103 C CG  . GLU B 1 114 ? -13.125 32.159  18.757  1   34.93  ? 114 GLU B CG  1 
ATOM   4104 C CD  . GLU B 1 114 ? -11.931 32.513  19.616  1   38.49  ? 114 GLU B CD  1 
ATOM   4105 O OE1 . GLU B 1 114 ? -11.976 33.64   20.21   1   35.77  ? 114 GLU B OE1 1 
ATOM   4106 O OE2 . GLU B 1 114 ? -10.945 31.725  19.628  1   36.89  ? 114 GLU B OE2 1 
ATOM   4107 N N   . TYR B 1 115 ? -15.671 29.457  18.254  1   36.49  ? 115 TYR B N   1 
ATOM   4108 C CA  . TYR B 1 115 ? -15.575 28.266  17.408  1   33.89  ? 115 TYR B CA  1 
ATOM   4109 C C   . TYR B 1 115 ? -16.651 28.295  16.323  1   32.67  ? 115 TYR B C   1 
ATOM   4110 O O   . TYR B 1 115 ? -16.362 28.048  15.156  1   31.37  ? 115 TYR B O   1 
ATOM   4111 C CB  . TYR B 1 115 ? -15.782 26.965  18.178  1   34.15  ? 115 TYR B CB  1 
ATOM   4112 C CG  . TYR B 1 115 ? -14.609 26.406  18.953  1   33.52  ? 115 TYR B CG  1 
ATOM   4113 C CD1 . TYR B 1 115 ? -13.76  27.196  19.71   1   33.79  ? 115 TYR B CD1 1 
ATOM   4114 C CD2 . TYR B 1 115 ? -14.357 25.037  18.911  1   34.22  ? 115 TYR B CD2 1 
ATOM   4115 C CE1 . TYR B 1 115 ? -12.71  26.65   20.427  1   33.39  ? 115 TYR B CE1 1 
ATOM   4116 C CE2 . TYR B 1 115 ? -13.315 24.475  19.638  1   34.9   ? 115 TYR B CE2 1 
ATOM   4117 C CZ  . TYR B 1 115 ? -12.524 25.276  20.436  1   34.28  ? 115 TYR B CZ  1 
ATOM   4118 O OH  . TYR B 1 115 ? -11.532 24.675  21.146  1   35.42  ? 115 TYR B OH  1 
ATOM   4119 N N   . GLY B 1 116 ? -17.886 28.632  16.692  1   34.14  ? 116 GLY B N   1 
ATOM   4120 C CA  . GLY B 1 116 ? -18.96  28.672  15.711  1   34.84  ? 116 GLY B CA  1 
ATOM   4121 C C   . GLY B 1 116 ? -18.656 29.635  14.562  1   34.13  ? 116 GLY B C   1 
ATOM   4122 O O   . GLY B 1 116 ? -18.844 29.284  13.414  1   32.25  ? 116 GLY B O   1 
ATOM   4123 N N   . LYS B 1 117 ? -18.181 30.841  14.889  1   33.42  ? 117 LYS B N   1 
ATOM   4124 C CA  . LYS B 1 117 ? -17.927 31.867  13.878  1   35.14  ? 117 LYS B CA  1 
ATOM   4125 C C   . LYS B 1 117 ? -16.777 31.471  12.946  1   34.59  ? 117 LYS B C   1 
ATOM   4126 O O   . LYS B 1 117 ? -16.879 31.652  11.732  1   32.1   ? 117 LYS B O   1 
ATOM   4127 C CB  . LYS B 1 117 ? -17.598 33.183  14.588  1   38.54  ? 117 LYS B CB  1 
ATOM   4128 C CG  . LYS B 1 117 ? -18.768 33.844  15.344  1   45.62  ? 117 LYS B CG  1 
ATOM   4129 C CD  . LYS B 1 117 ? -19.868 34.523  14.542  1   51.5   ? 117 LYS B CD  1 
ATOM   4130 C CE  . LYS B 1 117 ? -19.528 35.913  14.106  1   57.66  ? 117 LYS B CE  1 
ATOM   4131 N NZ  . LYS B 1 117 ? -20.456 36.334  13.054  1   59.67  ? 117 LYS B NZ  1 
ATOM   4132 N N   . VAL B 1 118 ? -15.71  30.881  13.502  1   31.18  ? 118 VAL B N   1 
ATOM   4133 C CA  . VAL B 1 118 ? -14.532 30.555  12.722  1   31.16  ? 118 VAL B CA  1 
ATOM   4134 C C   . VAL B 1 118 ? -14.808 29.378  11.79   1   33.27  ? 118 VAL B C   1 
ATOM   4135 O O   . VAL B 1 118 ? -14.358 29.414  10.641  1   27.4   ? 118 VAL B O   1 
ATOM   4136 C CB  . VAL B 1 118 ? -13.3   30.361  13.629  1   30.37  ? 118 VAL B CB  1 
ATOM   4137 C CG1 . VAL B 1 118 ? -12.092 29.907  12.857  1   29.29  ? 118 VAL B CG1 1 
ATOM   4138 C CG2 . VAL B 1 118 ? -12.958 31.67   14.333  1   30.84  ? 118 VAL B CG2 1 
ATOM   4139 N N   . TYR B 1 119 ? -15.469 28.309  12.294  1   30.18  ? 119 TYR B N   1 
ATOM   4140 C CA  . TYR B 1 119 ? -15.843 27.207  11.419  1   30.25  ? 119 TYR B CA  1 
ATOM   4141 C C   . TYR B 1 119 ? -16.801 27.698  10.322  1   29.29  ? 119 TYR B C   1 
ATOM   4142 O O   . TYR B 1 119 ? -16.75  27.209  9.187   1   30.41  ? 119 TYR B O   1 
ATOM   4143 C CB  . TYR B 1 119 ? -16.442 26.043  12.217  1   29.94  ? 119 TYR B CB  1 
ATOM   4144 C CG  . TYR B 1 119 ? -15.412 25.147  12.895  1   29.6   ? 119 TYR B CG  1 
ATOM   4145 C CD1 . TYR B 1 119 ? -14.879 24.043  12.258  1   28.64  ? 119 TYR B CD1 1 
ATOM   4146 C CD2 . TYR B 1 119 ? -14.975 25.396  14.205  1   29.65  ? 119 TYR B CD2 1 
ATOM   4147 C CE1 . TYR B 1 119 ? -13.927 23.24   12.878  1   29.15  ? 119 TYR B CE1 1 
ATOM   4148 C CE2 . TYR B 1 119 ? -14.037 24.588  14.832  1   28.97  ? 119 TYR B CE2 1 
ATOM   4149 C CZ  . TYR B 1 119 ? -13.511 23.499  14.183  1   28.64  ? 119 TYR B CZ  1 
ATOM   4150 O OH  . TYR B 1 119 ? -12.572 22.752  14.843  1   28.21  ? 119 TYR B OH  1 
ATOM   4151 N N   . LYS B 1 120 ? -17.663 28.658  10.663  1   29.25  ? 120 LYS B N   1 
ATOM   4152 C CA  . LYS B 1 120 ? -18.557 29.263  9.687   1   32.33  ? 120 LYS B CA  1 
ATOM   4153 C C   . LYS B 1 120 ? -17.81  29.963  8.557   1   32.06  ? 120 LYS B C   1 
ATOM   4154 O O   . LYS B 1 120 ? -18.235 29.868  7.415   1   33.97  ? 120 LYS B O   1 
ATOM   4155 C CB  . LYS B 1 120 ? -19.601 30.191  10.285  1   32.95  ? 120 LYS B CB  1 
ATOM   4156 C CG  . LYS B 1 120 ? -20.784 30.414  9.337   1   35.99  ? 120 LYS B CG  1 
ATOM   4157 C CD  . LYS B 1 120 ? -21.975 31.125  9.957   1   39.72  ? 120 LYS B CD  1 
ATOM   4158 C CE  . LYS B 1 120 ? -23.133 31.028  9.036   1   44.07  ? 120 LYS B CE  1 
ATOM   4159 N NZ  . LYS B 1 120 ? -24.28  31.719  9.62    1   50.95  ? 120 LYS B NZ  1 
ATOM   4160 N N   . ILE B 1 121 ? -16.72  30.653  8.873   1   31.41  ? 121 ILE B N   1 
ATOM   4161 C CA  . ILE B 1 121 ? -15.881 31.288  7.86    1   29.9   ? 121 ILE B CA  1 
ATOM   4162 C C   . ILE B 1 121 ? -15.363 30.212  6.926   1   30.01  ? 121 ILE B C   1 
ATOM   4163 O O   . ILE B 1 121 ? -15.466 30.384  5.706   1   28     ? 121 ILE B O   1 
ATOM   4164 C CB  . ILE B 1 121 ? -14.753 32.147  8.476   1   30.79  ? 121 ILE B CB  1 
ATOM   4165 C CG1 . ILE B 1 121 ? -15.278 33.299  9.264   1   32.18  ? 121 ILE B CG1 1 
ATOM   4166 C CG2 . ILE B 1 121 ? -13.762 32.605  7.399   1   32.46  ? 121 ILE B CG2 1 
ATOM   4167 C CD1 . ILE B 1 121 ? -14.293 33.898  10.279  1   33.26  ? 121 ILE B CD1 1 
ATOM   4168 N N   . HIS B 1 122 ? -14.88  29.095  7.487   1   27.13  ? 122 HIS B N   1 
ATOM   4169 C CA  . HIS B 1 122 ? -14.408 27.995  6.674   1   27.9   ? 122 HIS B CA  1 
ATOM   4170 C C   . HIS B 1 122 ? -15.523 27.487  5.747   1   28.93  ? 122 HIS B C   1 
ATOM   4171 O O   . HIS B 1 122 ? -15.262 27.197  4.575   1   27.82  ? 122 HIS B O   1 
ATOM   4172 C CB  . HIS B 1 122 ? -13.792 26.881  7.533   1   29.75  ? 122 HIS B CB  1 
ATOM   4173 C CG  . HIS B 1 122 ? -13.532 25.625  6.797   1   31.12  ? 122 HIS B CG  1 
ATOM   4174 N ND1 . HIS B 1 122 ? -12.777 25.632  5.639   1   31.5   ? 122 HIS B ND1 1 
ATOM   4175 C CD2 . HIS B 1 122 ? -14.002 24.353  6.939   1   31.56  ? 122 HIS B CD2 1 
ATOM   4176 C CE1 . HIS B 1 122 ? -12.695 24.379  5.15    1   32.49  ? 122 HIS B CE1 1 
ATOM   4177 N NE2 . HIS B 1 122 ? -13.46  23.595  5.908   1   32.36  ? 122 HIS B NE2 1 
ATOM   4178 N N   . ARG B 1 123 ? -16.72  27.246  6.306   1   30.88  ? 123 ARG B N   1 
ATOM   4179 C CA  . ARG B 1 123 ? -17.85  26.749  5.522   1   32.44  ? 123 ARG B CA  1 
ATOM   4180 C C   . ARG B 1 123 ? -18.243 27.722  4.398   1   31.71  ? 123 ARG B C   1 
ATOM   4181 O O   . ARG B 1 123 ? -18.393 27.309  3.236   1   31.26  ? 123 ARG B O   1 
ATOM   4182 C CB  . ARG B 1 123 ? -19.043 26.491  6.447   1   33.69  ? 123 ARG B CB  1 
ATOM   4183 C CG  . ARG B 1 123 ? -18.886 25.226  7.289   1   33.85  ? 123 ARG B CG  1 
ATOM   4184 C CD  . ARG B 1 123 ? -18.999 23.909  6.503   1   36.01  ? 123 ARG B CD  1 
ATOM   4185 N NE  . ARG B 1 123 ? -20.373 23.719  6.012   1   37.76  ? 123 ARG B NE  1 
ATOM   4186 C CZ  . ARG B 1 123 ? -20.793 23.361  4.785   1   36.14  ? 123 ARG B CZ  1 
ATOM   4187 N NH1 . ARG B 1 123 ? -19.949 23.062  3.826   1   35.04  ? 123 ARG B NH1 1 
ATOM   4188 N NH2 . ARG B 1 123 ? -22.08  23.307  4.531   1   36.34  ? 123 ARG B NH2 1 
ATOM   4189 N N   . GLU B 1 124 ? -18.297 29.022  4.719   1   32.27  ? 124 GLU B N   1 
ATOM   4190 C CA  . GLU B 1 124 ? -18.624 30.048  3.732   1   32.89  ? 124 GLU B CA  1 
ATOM   4191 C C   . GLU B 1 124 ? -17.569 30.123  2.627   1   32.57  ? 124 GLU B C   1 
ATOM   4192 O O   . GLU B 1 124 ? -17.925 30.167  1.441   1   32.51  ? 124 GLU B O   1 
ATOM   4193 C CB  . GLU B 1 124 ? -18.9   31.373  4.432   1   34.17  ? 124 GLU B CB  1 
ATOM   4194 C CG  . GLU B 1 124 ? -20.243 31.338  5.152   1   39.85  ? 124 GLU B CG  1 
ATOM   4195 C CD  . GLU B 1 124 ? -20.685 32.635  5.791   1   45.7   ? 124 GLU B CD  1 
ATOM   4196 O OE1 . GLU B 1 124 ? -19.907 33.608  5.806   1   45.73  ? 124 GLU B OE1 1 
ATOM   4197 O OE2 . GLU B 1 124 ? -21.848 32.638  6.238   1   55.59  ? 124 GLU B OE2 1 
ATOM   4198 N N   . LEU B 1 125 ? -16.283 30.127  3.004   1   31.57  ? 125 LEU B N   1 
ATOM   4199 C CA  . LEU B 1 125 ? -15.191 30.237  2.035   1   32.44  ? 125 LEU B CA  1 
ATOM   4200 C C   . LEU B 1 125 ? -15.178 29.004  1.129   1   32.12  ? 125 LEU B C   1 
ATOM   4201 O O   . LEU B 1 125 ? -15.116 29.118  -0.082  1   30.28  ? 125 LEU B O   1 
ATOM   4202 C CB  . LEU B 1 125 ? -13.841 30.436  2.694   1   29.55  ? 125 LEU B CB  1 
ATOM   4203 C CG  . LEU B 1 125 ? -12.623 30.619  1.779   1   28.48  ? 125 LEU B CG  1 
ATOM   4204 C CD1 . LEU B 1 125 ? -12.75  31.786  0.819   1   30.67  ? 125 LEU B CD1 1 
ATOM   4205 C CD2 . LEU B 1 125 ? -11.441 30.857  2.659   1   29.49  ? 125 LEU B CD2 1 
ATOM   4206 N N   . SER B 1 126 ? -15.339 27.817  1.717   1   32.46  ? 126 SER B N   1 
ATOM   4207 C CA  . SER B 1 126 ? -15.294 26.59   0.93    1   36.17  ? 126 SER B CA  1 
ATOM   4208 C C   . SER B 1 126 ? -16.488 26.491  -0.034  1   37.17  ? 126 SER B C   1 
ATOM   4209 O O   . SER B 1 126 ? -16.347 25.896  -1.095  1   34.63  ? 126 SER B O   1 
ATOM   4210 C CB  . SER B 1 126 ? -15.194 25.369  1.814   1   34.44  ? 126 SER B CB  1 
ATOM   4211 O OG  . SER B 1 126 ? -16.409 25.225  2.507   1   38.52  ? 126 SER B OG  1 
ATOM   4212 N N   . LYS B 1 127 ? -17.653 27.06   0.312   1   35.39  ? 127 LYS B N   1 
ATOM   4213 C CA  . LYS B 1 127 ? -18.816 27.024  -0.566  1   37.88  ? 127 LYS B CA  1 
ATOM   4214 C C   . LYS B 1 127 ? -18.773 28.146  -1.608  1   40.47  ? 127 LYS B C   1 
ATOM   4215 O O   . LYS B 1 127 ? -19.661 28.157  -2.436  1   38.64  ? 127 LYS B O   1 
ATOM   4216 C CB  . LYS B 1 127 ? -20.125 27.116  0.233   1   37.75  ? 127 LYS B CB  1 
ATOM   4217 C CG  . LYS B 1 127 ? -20.463 25.855  1.033   1   42.75  ? 127 LYS B CG  1 
ATOM   4218 C CD  . LYS B 1 127 ? -21.144 26.141  2.369   1   45.61  ? 127 LYS B CD  1 
ATOM   4219 C CE  . LYS B 1 127 ? -22.573 26.283  2.336   1   46     ? 127 LYS B CE  1 
ATOM   4220 N NZ  . LYS B 1 127 ? -23.017 27.088  3.486   1   48.63  ? 127 LYS B NZ  1 
ATOM   4221 N N   . GLY B 1 128 ? -17.849 29.128  -1.513  1   34.72  ? 128 GLY B N   1 
ATOM   4222 C CA  . GLY B 1 128 ? -17.848 30.271  -2.412  1   34.01  ? 128 GLY B CA  1 
ATOM   4223 C C   . GLY B 1 128 ? -18.906 31.312  -2.069  1   34.64  ? 128 GLY B C   1 
ATOM   4224 O O   . GLY B 1 128 ? -19.243 32.131  -2.892  1   36.84  ? 128 GLY B O   1 
ATOM   4225 N N   . GLU B 1 129 ? -19.44  31.327  -0.844  1   36.62  ? 129 GLU B N   1 
ATOM   4226 C CA  . GLU B 1 129 ? -20.322 32.39   -0.385  1   37.39  ? 129 GLU B CA  1 
ATOM   4227 C C   . GLU B 1 129 ? -19.538 33.656  -0.021  1   35.22  ? 129 GLU B C   1 
ATOM   4228 O O   . GLU B 1 129 ? -20.103 34.746  -0.013  1   33.31  ? 129 GLU B O   1 
ATOM   4229 C CB  . GLU B 1 129 ? -21.161 31.913  0.8     1   43.51  ? 129 GLU B CB  1 
ATOM   4230 C CG  . GLU B 1 129 ? -22.066 30.736  0.432   1   48.07  ? 129 GLU B CG  1 
ATOM   4231 C CD  . GLU B 1 129 ? -22.815 30.147  1.61    1   55.63  ? 129 GLU B CD  1 
ATOM   4232 O OE1 . GLU B 1 129 ? -23.462 29.115  1.357   1   61.5   ? 129 GLU B OE1 1 
ATOM   4233 O OE2 . GLU B 1 129 ? -22.776 30.681  2.748   1   60.42  ? 129 GLU B OE2 1 
ATOM   4234 N N   . ILE B 1 130 ? -18.264 33.508  0.364   1   34.41  ? 130 ILE B N   1 
ATOM   4235 C CA  . ILE B 1 130 ? -17.377 34.644  0.55    1   30.85  ? 130 ILE B CA  1 
ATOM   4236 C C   . ILE B 1 130 ? -16.091 34.344  -0.2    1   31.22  ? 130 ILE B C   1 
ATOM   4237 O O   . ILE B 1 130 ? -15.829 33.185  -0.482  1   30.92  ? 130 ILE B O   1 
ATOM   4238 C CB  . ILE B 1 130 ? -17.106 34.928  2.041   1   30.19  ? 130 ILE B CB  1 
ATOM   4239 C CG1 . ILE B 1 130 ? -16.321 33.783  2.721   1   29.39  ? 130 ILE B CG1 1 
ATOM   4240 C CG2 . ILE B 1 130 ? -18.385 35.343  2.763   1   31.93  ? 130 ILE B CG2 1 
ATOM   4241 C CD1 . ILE B 1 130 ? -16.123 33.911  4.227   1   30.8   ? 130 ILE B CD1 1 
ATOM   4242 N N   . ASP B 1 131 ? -15.321 35.397  -0.516  1   32.23  ? 131 ASP B N   1 
ATOM   4243 C CA  . ASP B 1 131 ? -13.986 35.257  -1.066  1   35.04  ? 131 ASP B CA  1 
ATOM   4244 C C   . ASP B 1 131 ? -12.973 35.327  0.089   1   33.32  ? 131 ASP B C   1 
ATOM   4245 O O   . ASP B 1 131 ? -13.345 35.561  1.245   1   32.6   ? 131 ASP B O   1 
ATOM   4246 C CB  . ASP B 1 131 ? -13.755 36.226  -2.219  1   37.38  ? 131 ASP B CB  1 
ATOM   4247 C CG  . ASP B 1 131 ? -13.6   37.704  -1.882  1   45.77  ? 131 ASP B CG  1 
ATOM   4248 O OD1 . ASP B 1 131 ? -13.425 38.056  -0.681  1   46.35  ? 131 ASP B OD1 1 
ATOM   4249 O OD2 . ASP B 1 131 ? -13.704 38.53   -2.834  1   52.56  ? 131 ASP B OD2 1 
ATOM   4250 N N   . VAL B 1 132 ? -11.698 35.168  -0.268  1   31.43  ? 132 VAL B N   1 
ATOM   4251 C CA  . VAL B 1 132 ? -10.613 35.074  0.686   1   33.29  ? 132 VAL B CA  1 
ATOM   4252 C C   . VAL B 1 132 ? -10.382 36.412  1.39    1   31.26  ? 132 VAL B C   1 
ATOM   4253 O O   . VAL B 1 132 ? -10.052 36.411  2.576   1   30.2   ? 132 VAL B O   1 
ATOM   4254 C CB  . VAL B 1 132 ? -9.349  34.534  -0.011  1   35.87  ? 132 VAL B CB  1 
ATOM   4255 C CG1 . VAL B 1 132 ? -8.686  35.54   -0.964  1   36.89  ? 132 VAL B CG1 1 
ATOM   4256 C CG2 . VAL B 1 132 ? -8.347  34.03   1.019   1   37.44  ? 132 VAL B CG2 1 
ATOM   4257 N N   . PHE B 1 133 ? -10.612 37.539  0.722   1   32.05  ? 133 PHE B N   1 
ATOM   4258 C CA  . PHE B 1 133 ? -10.505 38.833  1.383   1   34.14  ? 133 PHE B CA  1 
ATOM   4259 C C   . PHE B 1 133 ? -11.59  39.029  2.455   1   31.44  ? 133 PHE B C   1 
ATOM   4260 O O   . PHE B 1 133 ? -11.305 39.533  3.545   1   30.14  ? 133 PHE B O   1 
ATOM   4261 C CB  . PHE B 1 133 ? -10.539 39.988  0.378   1   38.83  ? 133 PHE B CB  1 
ATOM   4262 C CG  . PHE B 1 133 ? -9.406  39.949  -0.627  1   40.12  ? 133 PHE B CG  1 
ATOM   4263 C CD1 . PHE B 1 133 ? -8.111  40.323  -0.259  1   42.84  ? 133 PHE B CD1 1 
ATOM   4264 C CD2 . PHE B 1 133 ? -9.629  39.506  -1.934  1   48.06  ? 133 PHE B CD2 1 
ATOM   4265 C CE1 . PHE B 1 133 ? -7.056  40.257  -1.179  1   44.91  ? 133 PHE B CE1 1 
ATOM   4266 C CE2 . PHE B 1 133 ? -8.59   39.484  -2.861  1   47.68  ? 133 PHE B CE2 1 
ATOM   4267 C CZ  . PHE B 1 133 ? -7.305  39.881  -2.48   1   47.23  ? 133 PHE B CZ  1 
ATOM   4268 N N   . GLU B 1 134 ? -12.823 38.645  2.161   1   32.95  ? 134 GLU B N   1 
ATOM   4269 C CA  . GLU B 1 134 ? -13.892 38.656  3.164   1   35.87  ? 134 GLU B CA  1 
ATOM   4270 C C   . GLU B 1 134 ? -13.583 37.681  4.307   1   30.89  ? 134 GLU B C   1 
ATOM   4271 O O   . GLU B 1 134 ? -13.825 38.026  5.473   1   29.16  ? 134 GLU B O   1 
ATOM   4272 C CB  . GLU B 1 134 ? -15.291 38.312  2.651   1   36.72  ? 134 GLU B CB  1 
ATOM   4273 C CG  . GLU B 1 134 ? -15.804 39.225  1.537   1   48.14  ? 134 GLU B CG  1 
ATOM   4274 C CD  . GLU B 1 134 ? -16.993 38.615  0.797   1   50.34  ? 134 GLU B CD  1 
ATOM   4275 O OE1 . GLU B 1 134 ? -18.079 38.782  1.406   1   49.03  ? 134 GLU B OE1 1 
ATOM   4276 O OE2 . GLU B 1 134 ? -16.816 37.898  -0.244  1   39.88  ? 134 GLU B OE2 1 
ATOM   4277 N N   . ALA B 1 135 ? -13.101 36.472  3.964   1   33.05  ? 135 ALA B N   1 
ATOM   4278 C CA  . ALA B 1 135 ? -12.712 35.51   4.988   1   30.87  ? 135 ALA B CA  1 
ATOM   4279 C C   . ALA B 1 135 ? -11.668 36.097  5.936   1   32.1   ? 135 ALA B C   1 
ATOM   4280 O O   . ALA B 1 135 ? -11.861 36.059  7.155   1   32.19  ? 135 ALA B O   1 
ATOM   4281 C CB  . ALA B 1 135 ? -12.216 34.252  4.382   1   30.09  ? 135 ALA B CB  1 
ATOM   4282 N N   . SER B 1 136 ? -10.616 36.732  5.378   1   31.4   ? 136 SER B N   1 
ATOM   4283 C CA  . SER B 1 136 ? -9.583  37.345  6.207   1   31.79  ? 136 SER B CA  1 
ATOM   4284 C C   . SER B 1 136 ? -10.154 38.44   7.077   1   31.62  ? 136 SER B C   1 
ATOM   4285 O O   . SER B 1 136 ? -9.78   38.548  8.248   1   32.09  ? 136 SER B O   1 
ATOM   4286 C CB  . SER B 1 136 ? -8.404  37.884  5.41    1   34.02  ? 136 SER B CB  1 
ATOM   4287 O OG  . SER B 1 136 ? -7.853  36.735  4.822   1   41.1   ? 136 SER B OG  1 
ATOM   4288 N N   . ALA B 1 137 ? -10.981 39.317  6.492   1   31.21  ? 137 ALA B N   1 
ATOM   4289 C CA  . ALA B 1 137 ? -11.63  40.366  7.265   1   32.3   ? 137 ALA B CA  1 
ATOM   4290 C C   . ALA B 1 137 ? -12.439 39.774  8.414   1   32.62  ? 137 ALA B C   1 
ATOM   4291 O O   . ALA B 1 137 ? -12.44  40.289  9.525   1   33.95  ? 137 ALA B O   1 
ATOM   4292 C CB  . ALA B 1 137 ? -12.556 41.18   6.396   1   33.12  ? 137 ALA B CB  1 
ATOM   4293 N N   . ASN B 1 138 ? -13.181 38.714  8.132   1   32.88  ? 138 ASN B N   1 
ATOM   4294 C CA  . ASN B 1 138 ? -14.006 38.09   9.168   1   32.68  ? 138 ASN B CA  1 
ATOM   4295 C C   . ASN B 1 138 ? -13.146 37.475  10.28   1   30.21  ? 138 ASN B C   1 
ATOM   4296 O O   . ASN B 1 138 ? -13.553 37.521  11.425  1   33.68  ? 138 ASN B O   1 
ATOM   4297 C CB  . ASN B 1 138 ? -14.947 37.083  8.527   1   32.52  ? 138 ASN B CB  1 
ATOM   4298 C CG  . ASN B 1 138 ? -16.04  37.745  7.721   1   35.3   ? 138 ASN B CG  1 
ATOM   4299 O OD1 . ASN B 1 138 ? -16.155 38.973  7.674   1   35.47  ? 138 ASN B OD1 1 
ATOM   4300 N ND2 . ASN B 1 138 ? -16.835 36.929  7.059   1   36.27  ? 138 ASN B ND2 1 
ATOM   4301 N N   . ILE B 1 139 ? -11.983 36.921  9.95    1   29.64  ? 139 ILE B N   1 
ATOM   4302 C CA  . ILE B 1 139 ? -11.053 36.413  10.941  1   30.13  ? 139 ILE B CA  1 
ATOM   4303 C C   . ILE B 1 139 ? -10.611 37.57   11.843  1   32     ? 139 ILE B C   1 
ATOM   4304 O O   . ILE B 1 139 ? -10.715 37.475  13.064  1   32.42  ? 139 ILE B O   1 
ATOM   4305 C CB  . ILE B 1 139 ? -9.888  35.678  10.261  1   30.65  ? 139 ILE B CB  1 
ATOM   4306 C CG1 . ILE B 1 139 ? -10.365 34.375  9.618   1   31.15  ? 139 ILE B CG1 1 
ATOM   4307 C CG2 . ILE B 1 139 ? -8.761  35.399  11.26   1   32.56  ? 139 ILE B CG2 1 
ATOM   4308 C CD1 . ILE B 1 139 ? -9.423  33.756  8.609   1   30.83  ? 139 ILE B CD1 1 
ATOM   4309 N N   . GLY B 1 140 ? -10.169 38.692  11.236  1   32.31  ? 140 GLY B N   1 
ATOM   4310 C CA  . GLY B 1 140 ? -9.77   39.867  11.992  1   32.7   ? 140 GLY B CA  1 
ATOM   4311 C C   . GLY B 1 140 ? -10.893 40.409  12.865  1   34.55  ? 140 GLY B C   1 
ATOM   4312 O O   . GLY B 1 140 ? -10.654 40.778  14.008  1   34.7   ? 140 GLY B O   1 
ATOM   4313 N N   . LYS B 1 141 ? -12.122 40.49   12.332  1   35.27  ? 141 LYS B N   1 
ATOM   4314 C CA  . LYS B 1 141 ? -13.27  40.999  13.09   1   38.05  ? 141 LYS B CA  1 
ATOM   4315 C C   . LYS B 1 141 ? -13.561 40.124  14.315  1   35.79  ? 141 LYS B C   1 
ATOM   4316 O O   . LYS B 1 141 ? -14.072 40.631  15.292  1   37.39  ? 141 LYS B O   1 
ATOM   4317 C CB  . LYS B 1 141 ? -14.571 40.907  12.279  1   41.73  ? 141 LYS B CB  1 
ATOM   4318 C CG  . LYS B 1 141 ? -14.842 41.968  11.261  1   48.91  ? 141 LYS B CG  1 
ATOM   4319 C CD  . LYS B 1 141 ? -15.996 41.54   10.345  1   54.05  ? 141 LYS B CD  1 
ATOM   4320 C CE  . LYS B 1 141 ? -16.529 42.656  9.47    1   58.8   ? 141 LYS B CE  1 
ATOM   4321 N NZ  . LYS B 1 141 ? -17.079 43.792  10.231  1   61.37  ? 141 LYS B NZ  1 
ATOM   4322 N N   . GLN B 1 142 ? -13.241 38.831  14.244  1   35.01  ? 142 GLN B N   1 
ATOM   4323 C CA  . GLN B 1 142 ? -13.567 37.897  15.321  1   38.2   ? 142 GLN B CA  1 
ATOM   4324 C C   . GLN B 1 142 ? -12.767 38.135  16.607  1   37.85  ? 142 GLN B C   1 
ATOM   4325 O O   . GLN B 1 142 ? -13.226 37.739  17.683  1   36.1   ? 142 GLN B O   1 
ATOM   4326 C CB  . GLN B 1 142 ? -13.41  36.471  14.786  1   37.92  ? 142 GLN B CB  1 
ATOM   4327 C CG  . GLN B 1 142 ? -14.023 35.388  15.676  1   39.96  ? 142 GLN B CG  1 
ATOM   4328 C CD  . GLN B 1 142 ? -15.465 35.656  16.033  1   38.38  ? 142 GLN B CD  1 
ATOM   4329 O OE1 . GLN B 1 142 ? -16.283 36.017  15.175  1   40.18  ? 142 GLN B OE1 1 
ATOM   4330 N NE2 . GLN B 1 142 ? -15.791 35.513  17.31   1   38.62  ? 142 GLN B NE2 1 
ATOM   4331 N N   . ARG B 1 143 ? -11.574 38.749  16.516  1   37.02  ? 143 ARG B N   1 
ATOM   4332 C CA  . ARG B 1 143 ? -10.709 38.995  17.673  1   40.12  ? 143 ARG B CA  1 
ATOM   4333 C C   . ARG B 1 143 ? -10.502 37.652  18.386  1   39.9   ? 143 ARG B C   1 
ATOM   4334 O O   . ARG B 1 143 ? -10.946 37.462  19.512  1   39.16  ? 143 ARG B O   1 
ATOM   4335 C CB  . ARG B 1 143 ? -11.286 40.133  18.533  1   45.67  ? 143 ARG B CB  1 
ATOM   4336 C CG  . ARG B 1 143 ? -11.325 41.462  17.763  1   54.5   ? 143 ARG B CG  1 
ATOM   4337 C CD  . ARG B 1 143 ? -11.91  42.706  18.406  1   64.18  ? 143 ARG B CD  1 
ATOM   4338 N NE  . ARG B 1 143 ? -11.496 42.874  19.8    1   76.25  ? 143 ARG B NE  1 
ATOM   4339 C CZ  . ARG B 1 143 ? -10.249 42.952  20.281  1   89.35  ? 143 ARG B CZ  1 
ATOM   4340 N NH1 . ARG B 1 143 ? -9.19   42.706  19.523  1   86.87  ? 143 ARG B NH1 1 
ATOM   4341 N NH2 . ARG B 1 143 ? -10.067 43.255  21.559  1   98.25  ? 143 ARG B NH2 1 
ATOM   4342 N N   . ILE B 1 144 ? -9.886  36.701  17.676  1   36.39  ? 144 ILE B N   1 
ATOM   4343 C CA  . ILE B 1 144 ? -9.769  35.32   18.139  1   37.79  ? 144 ILE B CA  1 
ATOM   4344 C C   . ILE B 1 144 ? -8.9    35.244  19.405  1   40.38  ? 144 ILE B C   1 
ATOM   4345 O O   . ILE B 1 144 ? -7.812  35.814  19.414  1   43.32  ? 144 ILE B O   1 
ATOM   4346 C CB  . ILE B 1 144 ? -9.189  34.472  17.003  1   35.25  ? 144 ILE B CB  1 
ATOM   4347 C CG1 . ILE B 1 144 ? -10.203 34.385  15.86   1   33.29  ? 144 ILE B CG1 1 
ATOM   4348 C CG2 . ILE B 1 144 ? -8.729  33.073  17.449  1   37.68  ? 144 ILE B CG2 1 
ATOM   4349 C CD1 . ILE B 1 144 ? -9.717  33.569  14.685  1   31.61  ? 144 ILE B CD1 1 
ATOM   4350 N N   . LYS B 1 145 ? -9.385  34.549  20.448  1   39.3   ? 145 LYS B N   1 
ATOM   4351 C CA  . LYS B 1 145 ? -8.678  34.416  21.712  1   43.53  ? 145 LYS B CA  1 
ATOM   4352 C C   . LYS B 1 145 ? -8.082  33.024  21.902  1   41.7   ? 145 LYS B C   1 
ATOM   4353 O O   . LYS B 1 145 ? -7.132  32.929  22.664  1   43.17  ? 145 LYS B O   1 
ATOM   4354 C CB  . LYS B 1 145 ? -9.574  34.762  22.909  1   47.24  ? 145 LYS B CB  1 
ATOM   4355 C CG  . LYS B 1 145 ? -9.942  36.245  23.027  1   53.68  ? 145 LYS B CG  1 
ATOM   4356 C CD  . LYS B 1 145 ? -11.399 36.411  23.469  1   68.69  ? 145 LYS B CD  1 
ATOM   4357 C CE  . LYS B 1 145 ? -11.833 37.777  23.914  1   74.63  ? 145 LYS B CE  1 
ATOM   4358 N NZ  . LYS B 1 145 ? -11.778 37.91   25.371  1   79.25  ? 145 LYS B NZ  1 
ATOM   4359 N N   . THR B 1 146 ? -8.65   31.957  21.309  1   34.78  ? 146 THR B N   1 
ATOM   4360 C CA  . THR B 1 146 ? -8.165  30.601  21.589  1   35.29  ? 146 THR B CA  1 
ATOM   4361 C C   . THR B 1 146 ? -7.005  30.258  20.659  1   37.84  ? 146 THR B C   1 
ATOM   4362 O O   . THR B 1 146 ? -6.996  30.621  19.472  1   34.66  ? 146 THR B O   1 
ATOM   4363 C CB  . THR B 1 146 ? -9.279  29.565  21.504  1   35     ? 146 THR B CB  1 
ATOM   4364 O OG1 . THR B 1 146 ? -9.747  29.428  20.158  1   35.79  ? 146 THR B OG1 1 
ATOM   4365 C CG2 . THR B 1 146 ? -10.421 29.915  22.429  1   37.64  ? 146 THR B CG2 1 
ATOM   4366 N N   . ALA B 1 147 ? -6.057  29.467  21.183  1   36.62  ? 147 ALA B N   1 
ATOM   4367 C CA  . ALA B 1 147 ? -4.967  28.975  20.36   1   37.22  ? 147 ALA B CA  1 
ATOM   4368 C C   . ALA B 1 147 ? -5.527  28.123  19.229  1   34.51  ? 147 ALA B C   1 
ATOM   4369 O O   . ALA B 1 147 ? -5.021  28.154  18.113  1   34.71  ? 147 ALA B O   1 
ATOM   4370 C CB  . ALA B 1 147 ? -4.012  28.19   21.226  1   40.4   ? 147 ALA B CB  1 
ATOM   4371 N N   . GLU B 1 148 ? -6.577  27.347  19.531  1   32.28  ? 148 GLU B N   1 
ATOM   4372 C CA  . GLU B 1 148 ? -7.142  26.433  18.55   1   33.45  ? 148 GLU B CA  1 
ATOM   4373 C C   . GLU B 1 148 ? -7.806  27.127  17.36   1   29.98  ? 148 GLU B C   1 
ATOM   4374 O O   . GLU B 1 148 ? -7.607  26.674  16.245  1   29.62  ? 148 GLU B O   1 
ATOM   4375 C CB  . GLU B 1 148 ? -7.956  25.318  19.18   1   36.73  ? 148 GLU B CB  1 
ATOM   4376 C CG  . GLU B 1 148 ? -9.055  25.766  20.094  1   40.5   ? 148 GLU B CG  1 
ATOM   4377 C CD  . GLU B 1 148 ? -8.698  25.928  21.571  1   44.59  ? 148 GLU B CD  1 
ATOM   4378 O OE1 . GLU B 1 148 ? -7.512  26.102  21.929  1   38.3   ? 148 GLU B OE1 1 
ATOM   4379 O OE2 . GLU B 1 148 ? -9.723  25.95   22.331  1   47.03  ? 148 GLU B OE2 1 
ATOM   4380 N N   . MET B 1 149 ? -8.587  28.19   17.558  1   30.63  ? 149 MET B N   1 
ATOM   4381 C CA  . MET B 1 149 ? -9.201  28.88   16.436  1   32.61  ? 149 MET B CA  1 
ATOM   4382 C C   . MET B 1 149 ? -8.208  29.793  15.722  1   31.09  ? 149 MET B C   1 
ATOM   4383 O O   . MET B 1 149 ? -8.354  30.02   14.517  1   29.97  ? 149 MET B O   1 
ATOM   4384 C CB  . MET B 1 149 ? -10.465 29.63   16.875  1   33.5   ? 149 MET B CB  1 
ATOM   4385 C CG  . MET B 1 149 ? -11.587 28.701  17.251  1   33.81  ? 149 MET B CG  1 
ATOM   4386 S SD  . MET B 1 149 ? -12.019 27.515  15.963  1   30.76  ? 149 MET B SD  1 
ATOM   4387 C CE  . MET B 1 149 ? -11.209 26.008  16.518  1   31.64  ? 149 MET B CE  1 
ATOM   4388 N N   . ASN B 1 150 ? -7.164  30.264  16.422  1   34.21  ? 150 ASN B N   1 
ATOM   4389 C CA  . ASN B 1 150 ? -6.049  30.935  15.746  1   32.49  ? 150 ASN B CA  1 
ATOM   4390 C C   . ASN B 1 150 ? -5.422  29.982  14.716  1   34.94  ? 150 ASN B C   1 
ATOM   4391 O O   . ASN B 1 150 ? -5.231  30.331  13.542  1   30.42  ? 150 ASN B O   1 
ATOM   4392 C CB  . ASN B 1 150 ? -5.077  31.507  16.776  1   38.47  ? 150 ASN B CB  1 
ATOM   4393 C CG  . ASN B 1 150 ? -3.882  32.118  16.091  1   41.58  ? 150 ASN B CG  1 
ATOM   4394 O OD1 . ASN B 1 150 ? -4.044  32.998  15.24   1   45.45  ? 150 ASN B OD1 1 
ATOM   4395 N ND2 . ASN B 1 150 ? -2.691  31.586  16.321  1   46.48  ? 150 ASN B ND2 1 
ATOM   4396 N N   . ILE B 1 151 ? -5.198  28.718  15.134  1   31.25  ? 151 ILE B N   1 
ATOM   4397 C CA  . ILE B 1 151 ? -4.678  27.686  14.242  1   28.43  ? 151 ILE B CA  1 
ATOM   4398 C C   . ILE B 1 151 ? -5.671  27.342  13.137  1   26.66  ? 151 ILE B C   1 
ATOM   4399 O O   . ILE B 1 151 ? -5.263  27.237  11.962  1   24.3   ? 151 ILE B O   1 
ATOM   4400 C CB  . ILE B 1 151 ? -4.194  26.457  15.025  1   29.31  ? 151 ILE B CB  1 
ATOM   4401 C CG1 . ILE B 1 151 ? -2.961  26.828  15.858  1   31.4   ? 151 ILE B CG1 1 
ATOM   4402 C CG2 . ILE B 1 151 ? -3.901  25.294  14.086  1   30.38  ? 151 ILE B CG2 1 
ATOM   4403 C CD1 . ILE B 1 151 ? -2.644  25.862  16.982  1   34.39  ? 151 ILE B CD1 1 
ATOM   4404 N N   . PHE B 1 152 ? -6.942  27.136  13.508  1   26.8   ? 152 PHE B N   1 
ATOM   4405 C CA  . PHE B 1 152 ? -7.967  26.785  12.536  1   27.87  ? 152 PHE B CA  1 
ATOM   4406 C C   . PHE B 1 152 ? -8.104  27.901  11.496  1   28.34  ? 152 PHE B C   1 
ATOM   4407 O O   . PHE B 1 152 ? -8.342  27.611  10.308  1   26.8   ? 152 PHE B O   1 
ATOM   4408 C CB  . PHE B 1 152 ? -9.33   26.436  13.166  1   28.49  ? 152 PHE B CB  1 
ATOM   4409 C CG  . PHE B 1 152 ? -10.207 25.677  12.184  1   28.46  ? 152 PHE B CG  1 
ATOM   4410 C CD1 . PHE B 1 152 ? -9.927  24.357  11.863  1   31.89  ? 152 PHE B CD1 1 
ATOM   4411 C CD2 . PHE B 1 152 ? -11.243 26.281  11.51   1   28.4   ? 152 PHE B CD2 1 
ATOM   4412 C CE1 . PHE B 1 152 ? -10.67  23.662  10.912  1   32.4   ? 152 PHE B CE1 1 
ATOM   4413 C CE2 . PHE B 1 152 ? -12.029 25.581  10.591  1   31.53  ? 152 PHE B CE2 1 
ATOM   4414 C CZ  . PHE B 1 152 ? -11.729 24.286  10.272  1   31.47  ? 152 PHE B CZ  1 
ATOM   4415 N N   . SER B 1 153 ? -7.948  29.172  11.914  1   28.03  ? 153 SER B N   1 
ATOM   4416 C CA  . SER B 1 153 ? -8.056  30.268  10.953  1   31.58  ? 153 SER B CA  1 
ATOM   4417 C C   . SER B 1 153 ? -6.953  30.197  9.877   1   32.3   ? 153 SER B C   1 
ATOM   4418 O O   . SER B 1 153 ? -7.189  30.528  8.7     1   32.41  ? 153 SER B O   1 
ATOM   4419 C CB  . SER B 1 153 ? -8.118  31.61   11.646  1   33.96  ? 153 SER B CB  1 
ATOM   4420 O OG  . SER B 1 153 ? -6.848  31.976  12.164  1   31.62  ? 153 SER B OG  1 
ATOM   4421 N N   . LYS B 1 154 ? -5.774  29.668  10.245  1   28.56  ? 154 LYS B N   1 
ATOM   4422 C CA  . LYS B 1 154 ? -4.688  29.444  9.299   1   27.73  ? 154 LYS B CA  1 
ATOM   4423 C C   . LYS B 1 154 ? -4.998  28.253  8.425   1   28.68  ? 154 LYS B C   1 
ATOM   4424 O O   . LYS B 1 154 ? -4.801  28.299  7.207   1   27.33  ? 154 LYS B O   1 
ATOM   4425 C CB  . LYS B 1 154 ? -3.37   29.293  10.049  1   30.93  ? 154 LYS B CB  1 
ATOM   4426 C CG  . LYS B 1 154 ? -3.04   30.647  10.774  1   33.98  ? 154 LYS B CG  1 
ATOM   4427 C CD  . LYS B 1 154 ? -2.014  30.442  11.856  1   40.97  ? 154 LYS B CD  1 
ATOM   4428 C CE  . LYS B 1 154 ? -1.834  31.701  12.709  1   43.6   ? 154 LYS B CE  1 
ATOM   4429 N NZ  . LYS B 1 154 ? -1.801  32.931  11.91   1   41.9   ? 154 LYS B NZ  1 
ATOM   4430 N N   . MET B 1 155 ? -5.538  27.192  9.042   1   25.68  ? 155 MET B N   1 
ATOM   4431 C CA  . MET B 1 155 ? -5.844  25.996  8.29    1   26.79  ? 155 MET B CA  1 
ATOM   4432 C C   . MET B 1 155 ? -6.904  26.275  7.236   1   27.09  ? 155 MET B C   1 
ATOM   4433 O O   . MET B 1 155 ? -6.774  25.743  6.127   1   25.23  ? 155 MET B O   1 
ATOM   4434 C CB  . MET B 1 155 ? -6.277  24.856  9.214   1   28.27  ? 155 MET B CB  1 
ATOM   4435 C CG  . MET B 1 155 ? -5.115  24.274  10.001  1   29.62  ? 155 MET B CG  1 
ATOM   4436 S SD  . MET B 1 155 ? -5.609  22.888  11.067  1   35.74  ? 155 MET B SD  1 
ATOM   4437 C CE  . MET B 1 155 ? -6.929  23.413  12.091  1   36.64  ? 155 MET B CE  1 
ATOM   4438 N N   . LEU B 1 156 ? -7.956  27.046  7.57    1   24.49  ? 156 LEU B N   1 
ATOM   4439 C CA  . LEU B 1 156 ? -9.021  27.255  6.589   1   28.11  ? 156 LEU B CA  1 
ATOM   4440 C C   . LEU B 1 156 ? -8.477  27.996  5.349   1   27.57  ? 156 LEU B C   1 
ATOM   4441 O O   . LEU B 1 156 ? -8.92   27.716  4.242   1   24.99  ? 156 LEU B O   1 
ATOM   4442 C CB  . LEU B 1 156 ? -10.278 27.9    7.161   1   26.5   ? 156 LEU B CB  1 
ATOM   4443 C CG  . LEU B 1 156 ? -10.194 29.378  7.545   1   29.05  ? 156 LEU B CG  1 
ATOM   4444 C CD1 . LEU B 1 156 ? -10.582 30.303  6.379   1   29.26  ? 156 LEU B CD1 1 
ATOM   4445 C CD2 . LEU B 1 156 ? -11.043 29.66   8.806   1   32.97  ? 156 LEU B CD2 1 
ATOM   4446 N N   . LEU B 1 157 ? -7.5    28.9    5.534   1   25.92  ? 157 LEU B N   1 
ATOM   4447 C CA  . LEU B 1 157 ? -6.804  29.548  4.425   1   26.36  ? 157 LEU B CA  1 
ATOM   4448 C C   . LEU B 1 157 ? -5.95   28.581  3.614   1   25.15  ? 157 LEU B C   1 
ATOM   4449 O O   . LEU B 1 157 ? -5.947  28.661  2.384   1   27.15  ? 157 LEU B O   1 
ATOM   4450 C CB  . LEU B 1 157 ? -6.002  30.746  4.926   1   25.48  ? 157 LEU B CB  1 
ATOM   4451 C CG  . LEU B 1 157 ? -6.865  31.87   5.506   1   28.31  ? 157 LEU B CG  1 
ATOM   4452 C CD1 . LEU B 1 157 ? -6.024  32.947  6.205   1   30.96  ? 157 LEU B CD1 1 
ATOM   4453 C CD2 . LEU B 1 157 ? -7.754  32.497  4.417   1   27.84  ? 157 LEU B CD2 1 
ATOM   4454 N N   . MET B 1 158 ? -5.307  27.624  4.292   1   26.83  ? 158 MET B N   1 
ATOM   4455 C CA  . MET B 1 158 ? -4.556  26.554  3.632   1   23.5   ? 158 MET B CA  1 
ATOM   4456 C C   . MET B 1 158 ? -5.461  25.687  2.76    1   25.19  ? 158 MET B C   1 
ATOM   4457 O O   . MET B 1 158 ? -5.046  25.347  1.648   1   24.55  ? 158 MET B O   1 
ATOM   4458 C CB  . MET B 1 158 ? -3.794  25.665  4.611   1   23.76  ? 158 MET B CB  1 
ATOM   4459 C CG  . MET B 1 158 ? -2.724  26.424  5.399   1   27.92  ? 158 MET B CG  1 
ATOM   4460 S SD  . MET B 1 158 ? -2.004  25.533  6.798   1   30.89  ? 158 MET B SD  1 
ATOM   4461 C CE  . MET B 1 158 ? -1.017  24.381  5.848   1   29.31  ? 158 MET B CE  1 
ATOM   4462 N N   . TYR B 1 159 ? -6.662  25.331  3.256   1   24.52  ? 159 TYR B N   1 
ATOM   4463 C CA  . TYR B 1 159 ? -7.597  24.511  2.498   1   27.27  ? 159 TYR B CA  1 
ATOM   4464 C C   . TYR B 1 159 ? -8.043  25.248  1.245   1   27.23  ? 159 TYR B C   1 
ATOM   4465 O O   . TYR B 1 159 ? -8.147  24.629  0.186   1   25.15  ? 159 TYR B O   1 
ATOM   4466 C CB  . TYR B 1 159 ? -8.834  24.11   3.319   1   25.65  ? 159 TYR B CB  1 
ATOM   4467 C CG  . TYR B 1 159 ? -8.568  23.091  4.408   1   25.56  ? 159 TYR B CG  1 
ATOM   4468 C CD1 . TYR B 1 159 ? -7.894  21.895  4.134   1   27.32  ? 159 TYR B CD1 1 
ATOM   4469 C CD2 . TYR B 1 159 ? -8.948  23.334  5.715   1   25.68  ? 159 TYR B CD2 1 
ATOM   4470 C CE1 . TYR B 1 159 ? -7.652  20.947  5.122   1   27.81  ? 159 TYR B CE1 1 
ATOM   4471 C CE2 . TYR B 1 159 ? -8.729  22.384  6.701   1   27.04  ? 159 TYR B CE2 1 
ATOM   4472 C CZ  . TYR B 1 159 ? -8.055  21.202  6.418   1   27.17  ? 159 TYR B CZ  1 
ATOM   4473 O OH  . TYR B 1 159 ? -7.838  20.323  7.418   1   26.73  ? 159 TYR B OH  1 
ATOM   4474 N N   . ASP B 1 160 ? -8.353  26.544  1.4     1   25.09  ? 160 ASP B N   1 
ATOM   4475 C CA  . ASP B 1 160 ? -8.765  27.35   0.263   1   26.99  ? 160 ASP B CA  1 
ATOM   4476 C C   . ASP B 1 160 ? -7.638  27.451  -0.778  1   27.19  ? 160 ASP B C   1 
ATOM   4477 O O   . ASP B 1 160 ? -7.905  27.355  -1.974  1   26.08  ? 160 ASP B O   1 
ATOM   4478 C CB  . ASP B 1 160 ? -9.243  28.702  0.743   1   27.51  ? 160 ASP B CB  1 
ATOM   4479 C CG  . ASP B 1 160 ? -9.748  29.627  -0.351  1   34.12  ? 160 ASP B CG  1 
ATOM   4480 O OD1 . ASP B 1 160 ? -10.7   29.243  -1.037  1   35.3   ? 160 ASP B OD1 1 
ATOM   4481 O OD2 . ASP B 1 160 ? -9.167  30.702  -0.507  1   34.75  ? 160 ASP B OD2 1 
ATOM   4482 N N   . CYS B 1 161 ? -6.405  27.763  -0.343  1   26.13  ? 161 CYS B N   1 
ATOM   4483 C CA  . CYS B 1 161 ? -5.243  27.773  -1.231  1   28.93  ? 161 CYS B CA  1 
ATOM   4484 C C   . CYS B 1 161 ? -5.111  26.477  -2.019  1   28.54  ? 161 CYS B C   1 
ATOM   4485 O O   . CYS B 1 161 ? -4.917  26.506  -3.224  1   25.83  ? 161 CYS B O   1 
ATOM   4486 C CB  . CYS B 1 161 ? -3.928  27.911  -0.484  1   27.89  ? 161 CYS B CB  1 
ATOM   4487 S SG  . CYS B 1 161 ? -3.668  29.561  0.183   1   32.54  ? 161 CYS B SG  1 
ATOM   4488 N N   . LEU B 1 162 ? -5.26   25.334  -1.353  1   27.14  ? 162 LEU B N   1 
ATOM   4489 C CA  . LEU B 1 162 ? -5.122  24.056  -2.05   1   27.84  ? 162 LEU B CA  1 
ATOM   4490 C C   . LEU B 1 162 ? -6.235  23.885  -3.093  1   29.89  ? 162 LEU B C   1 
ATOM   4491 O O   . LEU B 1 162 ? -5.98   23.462  -4.235  1   27.29  ? 162 LEU B O   1 
ATOM   4492 C CB  . LEU B 1 162 ? -5.117  22.93   -1.019  1   29.55  ? 162 LEU B CB  1 
ATOM   4493 C CG  . LEU B 1 162 ? -4.824  21.518  -1.561  1   30.56  ? 162 LEU B CG  1 
ATOM   4494 C CD1 . LEU B 1 162 ? -3.413  21.422  -2.054  1   27.48  ? 162 LEU B CD1 1 
ATOM   4495 C CD2 . LEU B 1 162 ? -5.081  20.456  -0.49   1   31.41  ? 162 LEU B CD2 1 
ATOM   4496 N N   . ASN B 1 163 ? -7.476  24.2    -2.698  1   28.7   ? 163 ASN B N   1 
ATOM   4497 C CA  . ASN B 1 163 ? -8.623  24.1    -3.588  1   29.59  ? 163 ASN B CA  1 
ATOM   4498 C C   . ASN B 1 163 ? -8.51   25.07   -4.753  1   30.15  ? 163 ASN B C   1 
ATOM   4499 O O   . ASN B 1 163 ? -9.086  24.791  -5.782  1   29.56  ? 163 ASN B O   1 
ATOM   4500 C CB  . ASN B 1 163 ? -9.959  24.413  -2.922  1   33.26  ? 163 ASN B CB  1 
ATOM   4501 C CG  . ASN B 1 163 ? -10.289 23.459  -1.801  1   43.43  ? 163 ASN B CG  1 
ATOM   4502 O OD1 . ASN B 1 163 ? -9.712  22.362  -1.722  1   48.96  ? 163 ASN B OD1 1 
ATOM   4503 N ND2 . ASN B 1 163 ? -11.172 23.876  -0.895  1   47.16  ? 163 ASN B ND2 1 
ATOM   4504 N N   . LYS B 1 164 ? -7.89   26.242  -4.571  1   27.93  ? 164 LYS B N   1 
ATOM   4505 C CA  . LYS B 1 164 ? -7.882  27.262  -5.631  1   32.46  ? 164 LYS B CA  1 
ATOM   4506 C C   . LYS B 1 164 ? -6.583  27.234  -6.446  1   29.98  ? 164 LYS B C   1 
ATOM   4507 O O   . LYS B 1 164 ? -6.279  28.219  -7.116  1   27.7   ? 164 LYS B O   1 
ATOM   4508 C CB  . LYS B 1 164 ? -8.075  28.641  -4.972  1   36.22  ? 164 LYS B CB  1 
ATOM   4509 C CG  . LYS B 1 164 ? -9.416  28.889  -4.261  1   42.88  ? 164 LYS B CG  1 
ATOM   4510 C CD  . LYS B 1 164 ? -10.625 29.127  -5.157  1   52.23  ? 164 LYS B CD  1 
ATOM   4511 C CE  . LYS B 1 164 ? -11.939 29.246  -4.4    1   52.86  ? 164 LYS B CE  1 
ATOM   4512 N NZ  . LYS B 1 164 ? -11.892 30.282  -3.359  1   48.82  ? 164 LYS B NZ  1 
ATOM   4513 N N   . GLY B 1 165 ? -5.744  26.21   -6.297  1   29.04  ? 165 GLY B N   1 
ATOM   4514 C CA  . GLY B 1 165 ? -4.476  26.104  -7.011  1   32.05  ? 165 GLY B CA  1 
ATOM   4515 C C   . GLY B 1 165 ? -3.474  27.204  -6.675  1   32.62  ? 165 GLY B C   1 
ATOM   4516 O O   . GLY B 1 165 ? -2.746  27.628  -7.546  1   33.23  ? 165 GLY B O   1 
ATOM   4517 N N   . ASN B 1 166 ? -3.53   27.768  -5.464  1   27.38  ? 166 ASN B N   1 
ATOM   4518 C CA  . ASN B 1 166 ? -2.627  28.828  -5.053  1   26.31  ? 166 ASN B CA  1 
ATOM   4519 C C   . ASN B 1 166 ? -1.731  28.25   -3.956  1   26.84  ? 166 ASN B C   1 
ATOM   4520 O O   . ASN B 1 166 ? -1.973  28.482  -2.781  1   28.1   ? 166 ASN B O   1 
ATOM   4521 C CB  . ASN B 1 166 ? -3.413  30.055  -4.613  1   27.85  ? 166 ASN B CB  1 
ATOM   4522 C CG  . ASN B 1 166 ? -2.516  31.208  -4.229  1   29.93  ? 166 ASN B CG  1 
ATOM   4523 O OD1 . ASN B 1 166 ? -1.372  31.283  -4.662  1   32.52  ? 166 ASN B OD1 1 
ATOM   4524 N ND2 . ASN B 1 166 ? -2.936  32.017  -3.277  1   33.89  ? 166 ASN B ND2 1 
ATOM   4525 N N   . PHE B 1 167 ? -0.689  27.515  -4.324  1   26.7   ? 167 PHE B N   1 
ATOM   4526 C CA  . PHE B 1 167 ? 0.073   26.715  -3.377  1   24.46  ? 167 PHE B CA  1 
ATOM   4527 C C   . PHE B 1 167 ? 1.118   27.474  -2.583  1   26.89  ? 167 PHE B C   1 
ATOM   4528 O O   . PHE B 1 167 ? 1.441   27.044  -1.47   1   28.91  ? 167 PHE B O   1 
ATOM   4529 C CB  . PHE B 1 167 ? 0.662   25.489  -4.073  1   25.28  ? 167 PHE B CB  1 
ATOM   4530 C CG  . PHE B 1 167 ? -0.347  24.637  -4.828  1   26.12  ? 167 PHE B CG  1 
ATOM   4531 C CD1 . PHE B 1 167 ? -1.67   24.48   -4.383  1   28.01  ? 167 PHE B CD1 1 
ATOM   4532 C CD2 . PHE B 1 167 ? -0.005  24.056  -6.049  1   25.73  ? 167 PHE B CD2 1 
ATOM   4533 C CE1 . PHE B 1 167 ? -2.59   23.733  -5.107  1   27.69  ? 167 PHE B CE1 1 
ATOM   4534 C CE2 . PHE B 1 167 ? -0.929  23.283  -6.744  1   25.57  ? 167 PHE B CE2 1 
ATOM   4535 C CZ  . PHE B 1 167 ? -2.21   23.132  -6.297  1   27.17  ? 167 PHE B CZ  1 
ATOM   4536 N N   . ALA B 1 168 ? 1.616   28.621  -3.085  1   28.92  ? 168 ALA B N   1 
ATOM   4537 C CA  . ALA B 1 168 ? 2.758   29.268  -2.453  1   29.76  ? 168 ALA B CA  1 
ATOM   4538 C C   . ALA B 1 168 ? 2.505   29.61   -0.978  1   28.96  ? 168 ALA B C   1 
ATOM   4539 O O   . ALA B 1 168 ? 3.386   29.415  -0.151  1   30.98  ? 168 ALA B O   1 
ATOM   4540 C CB  . ALA B 1 168 ? 3.173   30.492  -3.245  1   29.54  ? 168 ALA B CB  1 
ATOM   4541 N N   . PRO B 1 169 ? 1.334   30.152  -0.576  1   26.83  ? 169 PRO B N   1 
ATOM   4542 C CA  . PRO B 1 169 ? 1.137   30.531  0.798   1   26.96  ? 169 PRO B CA  1 
ATOM   4543 C C   . PRO B 1 169 ? 1.066   29.377  1.788   1   26.51  ? 169 PRO B C   1 
ATOM   4544 O O   . PRO B 1 169 ? 1.227   29.636  2.965   1   25.2   ? 169 PRO B O   1 
ATOM   4545 C CB  . PRO B 1 169 ? -0.164  31.344  0.819   1   29.24  ? 169 PRO B CB  1 
ATOM   4546 C CG  . PRO B 1 169 ? -0.395  31.702  -0.62   1   28.13  ? 169 PRO B CG  1 
ATOM   4547 C CD  . PRO B 1 169 ? 0.189   30.557  -1.401  1   28.08  ? 169 PRO B CD  1 
ATOM   4548 N N   . MET B 1 170 ? 0.798   28.15   1.332   1   27.19  ? 170 MET B N   1 
ATOM   4549 C CA  . MET B 1 170 ? 0.51    27.059  2.252   1   28.05  ? 170 MET B CA  1 
ATOM   4550 C C   . MET B 1 170 ? 1.68    26.781  3.202   1   25.79  ? 170 MET B C   1 
ATOM   4551 O O   . MET B 1 170 ? 1.438   26.629  4.377   1   27.83  ? 170 MET B O   1 
ATOM   4552 C CB  . MET B 1 170 ? 0.096   25.808  1.487   1   27.39  ? 170 MET B CB  1 
ATOM   4553 C CG  . MET B 1 170 ? -1.214  25.997  0.72    1   27.42  ? 170 MET B CG  1 
ATOM   4554 S SD  . MET B 1 170 ? -1.696  24.466  -0.112  1   27.47  ? 170 MET B SD  1 
ATOM   4555 C CE  . MET B 1 170 ? -2.074  23.366  1.262   1   26.67  ? 170 MET B CE  1 
ATOM   4556 N N   . MET B 1 171 ? 2.926   26.726  2.713   1   31.36  ? 171 MET B N   1 
ATOM   4557 C CA  . MET B 1 171 ? 4.082   26.457  3.572   1   32.06  ? 171 MET B CA  1 
ATOM   4558 C C   . MET B 1 171 ? 4.332   27.606  4.56    1   30.49  ? 171 MET B C   1 
ATOM   4559 O O   . MET B 1 171 ? 4.734   27.378  5.717   1   31.35  ? 171 MET B O   1 
ATOM   4560 C CB  . MET B 1 171 ? 5.341   26.145  2.75    1   34.31  ? 171 MET B CB  1 
ATOM   4561 C CG  . MET B 1 171 ? 6.54    25.749  3.639   1   45.21  ? 171 MET B CG  1 
ATOM   4562 S SD  . MET B 1 171 ? 6.324   24.391  4.829   1   47.81  ? 171 MET B SD  1 
ATOM   4563 C CE  . MET B 1 171 ? 7.34    23.122  4.039   1   50.63  ? 171 MET B CE  1 
ATOM   4564 N N   . LEU B 1 172 ? 4.016   28.837  4.132   1   29.27  ? 172 LEU B N   1 
ATOM   4565 C CA  . LEU B 1 172 ? 4.116   30.015  4.998   1   28.24  ? 172 LEU B CA  1 
ATOM   4566 C C   . LEU B 1 172 ? 3.109   29.939  6.142   1   26.49  ? 172 LEU B C   1 
ATOM   4567 O O   . LEU B 1 172 ? 3.494   30.117  7.311   1   26.69  ? 172 LEU B O   1 
ATOM   4568 C CB  . LEU B 1 172 ? 3.951   31.321  4.211   1   32.09  ? 172 LEU B CB  1 
ATOM   4569 C CG  . LEU B 1 172 ? 4.931   31.524  3.03    1   36.97  ? 172 LEU B CG  1 
ATOM   4570 C CD1 . LEU B 1 172 ? 4.877   32.927  2.455   1   38.37  ? 172 LEU B CD1 1 
ATOM   4571 C CD2 . LEU B 1 172 ? 6.37    31.208  3.375   1   38.84  ? 172 LEU B CD2 1 
ATOM   4572 N N   . LEU B 1 173 ? 1.852   29.627  5.805   1   26.45  ? 173 LEU B N   1 
ATOM   4573 C CA  . LEU B 1 173 ? 0.799   29.478  6.819   1   27.98  ? 173 LEU B CA  1 
ATOM   4574 C C   . LEU B 1 173 ? 1.129   28.333  7.782   1   27.53  ? 173 LEU B C   1 
ATOM   4575 O O   . LEU B 1 173 ? 0.947   28.5    8.988   1   28.7   ? 173 LEU B O   1 
ATOM   4576 C CB  . LEU B 1 173 ? -0.558  29.268  6.171   1   26.1   ? 173 LEU B CB  1 
ATOM   4577 C CG  . LEU B 1 173 ? -1.133  30.514  5.505   1   27.18  ? 173 LEU B CG  1 
ATOM   4578 C CD1 . LEU B 1 173 ? -2.073  30.086  4.414   1   29.43  ? 173 LEU B CD1 1 
ATOM   4579 C CD2 . LEU B 1 173 ? -1.831  31.413  6.509   1   31.17  ? 173 LEU B CD2 1 
ATOM   4580 N N   . PHE B 1 174 ? 1.629   27.208  7.252   1   29.01  ? 174 PHE B N   1 
ATOM   4581 C CA  . PHE B 1 174 ? 2.057   26.09   8.082   1   26.96  ? 174 PHE B CA  1 
ATOM   4582 C C   . PHE B 1 174 ? 3.046   26.538  9.171   1   27.81  ? 174 PHE B C   1 
ATOM   4583 O O   . PHE B 1 174 ? 2.926   26.15   10.336  1   25.63  ? 174 PHE B O   1 
ATOM   4584 C CB  . PHE B 1 174 ? 2.657   24.978  7.191   1   29.96  ? 174 PHE B CB  1 
ATOM   4585 C CG  . PHE B 1 174 ? 3.28    23.881  8.072   1   29.65  ? 174 PHE B CG  1 
ATOM   4586 C CD1 . PHE B 1 174 ? 2.48    22.963  8.752   1   34.23  ? 174 PHE B CD1 1 
ATOM   4587 C CD2 . PHE B 1 174 ? 4.655   23.814  8.261   1   36.18  ? 174 PHE B CD2 1 
ATOM   4588 C CE1 . PHE B 1 174 ? 3.054   22.046  9.632   1   35.73  ? 174 PHE B CE1 1 
ATOM   4589 C CE2 . PHE B 1 174 ? 5.218   22.914  9.165   1   36.83  ? 174 PHE B CE2 1 
ATOM   4590 C CZ  . PHE B 1 174 ? 4.408   22.014  9.827   1   35.26  ? 174 PHE B CZ  1 
ATOM   4591 N N   . GLN B 1 175 ? 4.042   27.371  8.822   1   28.32  ? 175 GLN B N   1 
ATOM   4592 C CA  . GLN B 1 175 ? 5.041   27.859  9.774   1   28.89  ? 175 GLN B CA  1 
ATOM   4593 C C   . GLN B 1 175 ? 4.44    28.682  10.898  1   29.08  ? 175 GLN B C   1 
ATOM   4594 O O   . GLN B 1 175 ? 5.04    28.764  11.973  1   30.85  ? 175 GLN B O   1 
ATOM   4595 C CB  . GLN B 1 175 ? 6.136   28.718  9.117   1   30.78  ? 175 GLN B CB  1 
ATOM   4596 C CG  . GLN B 1 175 ? 6.879   27.998  8.008   1   32.17  ? 175 GLN B CG  1 
ATOM   4597 C CD  . GLN B 1 175 ? 7.63    26.768  8.457   1   32.29  ? 175 GLN B CD  1 
ATOM   4598 O OE1 . GLN B 1 175 ? 8.172   26.734  9.549   1   34.62  ? 175 GLN B OE1 1 
ATOM   4599 N NE2 . GLN B 1 175 ? 7.75    25.783  7.586   1   41.3   ? 175 GLN B NE2 1 
ATOM   4600 N N   . GLN B 1 176 ? 3.247   29.256  10.698  1   30     ? 176 GLN B N   1 
ATOM   4601 C CA  . GLN B 1 176 ? 2.572   30.001  11.754  1   30.61  ? 176 GLN B CA  1 
ATOM   4602 C C   . GLN B 1 176 ? 1.854   29.121  12.773  1   33.67  ? 176 GLN B C   1 
ATOM   4603 O O   . GLN B 1 176 ? 1.371   29.646  13.779  1   35.09  ? 176 GLN B O   1 
ATOM   4604 C CB  . GLN B 1 176 ? 1.592   31.027  11.18   1   33.14  ? 176 GLN B CB  1 
ATOM   4605 C CG  . GLN B 1 176 ? 2.235   31.986  10.184  1   34.06  ? 176 GLN B CG  1 
ATOM   4606 C CD  . GLN B 1 176 ? 1.241   32.762  9.36    1   37.14  ? 176 GLN B CD  1 
ATOM   4607 O OE1 . GLN B 1 176 ? 0.103   32.961  9.77    1   41     ? 176 GLN B OE1 1 
ATOM   4608 N NE2 . GLN B 1 176 ? 1.685   33.281  8.229   1   38.28  ? 176 GLN B NE2 1 
ATOM   4609 N N   . ILE B 1 177 ? 1.717   27.814  12.519  1   31.07  ? 177 ILE B N   1 
ATOM   4610 C CA  . ILE B 1 177 ? 1       26.933  13.428  1   31.65  ? 177 ILE B CA  1 
ATOM   4611 C C   . ILE B 1 177 ? 1.954   26.298  14.449  1   36.74  ? 177 ILE B C   1 
ATOM   4612 O O   . ILE B 1 177 ? 2.957   25.698  14.071  1   34.31  ? 177 ILE B O   1 
ATOM   4613 C CB  . ILE B 1 177 ? 0.271   25.856  12.597  1   31.57  ? 177 ILE B CB  1 
ATOM   4614 C CG1 . ILE B 1 177 ? -0.82   26.51   11.774  1   29.71  ? 177 ILE B CG1 1 
ATOM   4615 C CG2 . ILE B 1 177 ? -0.286  24.748  13.504  1   32.07  ? 177 ILE B CG2 1 
ATOM   4616 C CD1 . ILE B 1 177 ? -1.356  25.667  10.636  1   31.19  ? 177 ILE B CD1 1 
ATOM   4617 N N   . ASP B 1 178 ? 1.521   26.273  15.723  1   39.13  ? 178 ASP B N   1 
ATOM   4618 C CA  . ASP B 1 178 ? 2.169   25.526  16.795  1   36.32  ? 178 ASP B CA  1 
ATOM   4619 C C   . ASP B 1 178 ? 1.105   24.767  17.593  1   33.7   ? 178 ASP B C   1 
ATOM   4620 O O   . ASP B 1 178 ? 0.483   25.322  18.501  1   37.92  ? 178 ASP B O   1 
ATOM   4621 C CB  . ASP B 1 178 ? 3.028   26.465  17.623  1   38.97  ? 178 ASP B CB  1 
ATOM   4622 C CG  . ASP B 1 178 ? 3.806   25.834  18.78   1   45.41  ? 178 ASP B CG  1 
ATOM   4623 O OD1 . ASP B 1 178 ? 3.769   24.596  18.968  1   50     ? 178 ASP B OD1 1 
ATOM   4624 O OD2 . ASP B 1 178 ? 4.411   26.588  19.514  1   52.4   ? 178 ASP B OD2 1 
ATOM   4625 N N   . LEU B 1 179 ? 0.928   23.467  17.284  1   38.17  ? 179 LEU B N   1 
ATOM   4626 C CA  . LEU B 1 179 ? -0.079  22.623  17.918  1   37.66  ? 179 LEU B CA  1 
ATOM   4627 C C   . LEU B 1 179 ? 0.133   22.492  19.434  1   40.11  ? 179 LEU B C   1 
ATOM   4628 O O   . LEU B 1 179 ? -0.831  22.307  20.173  1   38.84  ? 179 LEU B O   1 
ATOM   4629 C CB  . LEU B 1 179 ? -0.174  21.252  17.253  1   37.93  ? 179 LEU B CB  1 
ATOM   4630 C CG  . LEU B 1 179 ? -0.624  21.228  15.792  1   38.98  ? 179 LEU B CG  1 
ATOM   4631 C CD1 . LEU B 1 179 ? -0.786  19.79   15.362  1   40.8   ? 179 LEU B CD1 1 
ATOM   4632 C CD2 . LEU B 1 179 ? -1.925  21.977  15.561  1   40.41  ? 179 LEU B CD2 1 
ATOM   4633 N N   . SER B 1 180 ? 1.359   22.678  19.906  1   38.82  ? 180 SER B N   1 
ATOM   4634 C CA  . SER B 1 180 ? 1.647   22.601  21.331  1   42.1   ? 180 SER B CA  1 
ATOM   4635 C C   . SER B 1 180 ? 0.946   23.706  22.109  1   44.42  ? 180 SER B C   1 
ATOM   4636 O O   . SER B 1 180 ? 0.882   23.624  23.328  1   41.24  ? 180 SER B O   1 
ATOM   4637 C CB  . SER B 1 180 ? 3.134   22.606  21.597  1   42.39  ? 180 SER B CB  1 
ATOM   4638 O OG  . SER B 1 180 ? 3.655   23.922  21.615  1   42.18  ? 180 SER B OG  1 
ATOM   4639 N N   . GLU B 1 181 ? 0.441   24.751  21.431  1   45.96  ? 181 GLU B N   1 
ATOM   4640 C CA  . GLU B 1 181 ? -0.321  25.786  22.111  1   45.6   ? 181 GLU B CA  1 
ATOM   4641 C C   . GLU B 1 181 ? -1.734  25.35   22.464  1   42.96  ? 181 GLU B C   1 
ATOM   4642 O O   . GLU B 1 181 ? -2.36   26.042  23.247  1   42.78  ? 181 GLU B O   1 
ATOM   4643 C CB  . GLU B 1 181 ? -0.436  27.056  21.284  1   51.87  ? 181 GLU B CB  1 
ATOM   4644 C CG  . GLU B 1 181 ? 0.937   27.651  21.009  1   59.75  ? 181 GLU B CG  1 
ATOM   4645 C CD  . GLU B 1 181 ? 0.862   29.141  20.906  1   67.84  ? 181 GLU B CD  1 
ATOM   4646 O OE1 . GLU B 1 181 ? 0.964   29.692  19.767  1   66.75  ? 181 GLU B OE1 1 
ATOM   4647 O OE2 . GLU B 1 181 ? 0.689   29.67   22.038  1   66.74  ? 181 GLU B OE2 1 
ATOM   4648 N N   . ILE B 1 182 ? -2.243  24.256  21.886  1   43.74  ? 182 ILE B N   1 
ATOM   4649 C CA  . ILE B 1 182 ? -3.567  23.734  22.227  1   43.82  ? 182 ILE B CA  1 
ATOM   4650 C C   . ILE B 1 182 ? -3.445  22.913  23.519  1   47.55  ? 182 ILE B C   1 
ATOM   4651 O O   . ILE B 1 182 ? -2.852  21.833  23.504  1   45.33  ? 182 ILE B O   1 
ATOM   4652 C CB  . ILE B 1 182 ? -4.146  22.902  21.065  1   39.05  ? 182 ILE B CB  1 
ATOM   4653 C CG1 . ILE B 1 182 ? -4.169  23.681  19.767  1   35.72  ? 182 ILE B CG1 1 
ATOM   4654 C CG2 . ILE B 1 182 ? -5.54   22.361  21.399  1   40.18  ? 182 ILE B CG2 1 
ATOM   4655 C CD1 . ILE B 1 182 ? -4.635  22.881  18.554  1   36.43  ? 182 ILE B CD1 1 
ATOM   4656 N N   . LYS B 1 183 ? -4.033  23.404  24.618  1   48.24  ? 183 LYS B N   1 
ATOM   4657 C CA  . LYS B 1 183 ? -3.804  22.799  25.927  1   55.61  ? 183 LYS B CA  1 
ATOM   4658 C C   . LYS B 1 183 ? -5.006  22.009  26.442  1   56.9   ? 183 LYS B C   1 
ATOM   4659 O O   . LYS B 1 183 ? -4.825  20.936  27.019  1   64.69  ? 183 LYS B O   1 
ATOM   4660 C CB  . LYS B 1 183 ? -3.299  23.887  26.884  1   60     ? 183 LYS B CB  1 
ATOM   4661 C CG  . LYS B 1 183 ? -1.862  24.303  26.516  1   61.05  ? 183 LYS B CG  1 
ATOM   4662 C CD  . LYS B 1 183 ? -1.106  25.152  27.531  1   71.14  ? 183 LYS B CD  1 
ATOM   4663 C CE  . LYS B 1 183 ? 0.378   24.891  27.507  1   71.28  ? 183 LYS B CE  1 
ATOM   4664 N NZ  . LYS B 1 183 ? 0.938   24.974  26.153  1   70.56  ? 183 LYS B NZ  1 
ATOM   4665 N N   . GLU B 1 184 ? -6.218  22.527  26.264  1   58.05  ? 184 GLU B N   1 
ATOM   4666 C CA  . GLU B 1 184 ? -7.328  22.004  27.047  1   69.64  ? 184 GLU B CA  1 
ATOM   4667 C C   . GLU B 1 184 ? -7.985  20.81   26.349  1   58.88  ? 184 GLU B C   1 
ATOM   4668 O O   . GLU B 1 184 ? -8.589  20.021  27.051  1   59.62  ? 184 GLU B O   1 
ATOM   4669 C CB  . GLU B 1 184 ? -8.217  23.16   27.533  1   82.91  ? 184 GLU B CB  1 
ATOM   4670 C CG  . GLU B 1 184 ? -7.505  24.104  28.512  1   91.83  ? 184 GLU B CG  1 
ATOM   4671 C CD  . GLU B 1 184 ? -7.072  23.548  29.869  1   102.68 ? 184 GLU B CD  1 
ATOM   4672 O OE1 . GLU B 1 184 ? -7.928  23.457  30.778  1   105.25 ? 184 GLU B OE1 1 
ATOM   4673 O OE2 . GLU B 1 184 ? -5.876  23.192  30.024  1   107.01 ? 184 GLU B OE2 1 
ATOM   4674 N N   . ASN B 1 185 ? -7.82   20.61   25.028  1   48.68  ? 185 ASN B N   1 
ATOM   4675 C CA  . ASN B 1 185 ? -8.685  19.708  24.28   1   43.92  ? 185 ASN B CA  1 
ATOM   4676 C C   . ASN B 1 185 ? -7.849  18.688  23.506  1   43.61  ? 185 ASN B C   1 
ATOM   4677 O O   . ASN B 1 185 ? -7.514  18.916  22.36   1   38.25  ? 185 ASN B O   1 
ATOM   4678 C CB  . ASN B 1 185 ? -9.686  20.523  23.471  1   39.28  ? 185 ASN B CB  1 
ATOM   4679 C CG  . ASN B 1 185 ? -10.787 19.674  22.877  1   41.15  ? 185 ASN B CG  1 
ATOM   4680 O OD1 . ASN B 1 185 ? -10.601 18.469  22.622  1   38.56  ? 185 ASN B OD1 1 
ATOM   4681 N ND2 . ASN B 1 185 ? -11.938 20.297  22.622  1   43.6   ? 185 ASN B ND2 1 
ATOM   4682 N N   . ARG B 1 186 ? -7.565  17.524  24.12   1   45.06  ? 186 ARG B N   1 
ATOM   4683 C CA  . ARG B 1 186 ? -6.734  16.507  23.483  1   48.23  ? 186 ARG B CA  1 
ATOM   4684 C C   . ARG B 1 186 ? -7.382  15.934  22.211  1   43.04  ? 186 ARG B C   1 
ATOM   4685 O O   . ARG B 1 186 ? -6.668  15.61   21.24   1   38.26  ? 186 ARG B O   1 
ATOM   4686 C CB  . ARG B 1 186 ? -6.372  15.398  24.475  1   51.77  ? 186 ARG B CB  1 
ATOM   4687 C CG  . ARG B 1 186 ? -5.406  14.371  23.89   1   63.14  ? 186 ARG B CG  1 
ATOM   4688 C CD  . ARG B 1 186 ? -4.452  13.654  24.872  1   77     ? 186 ARG B CD  1 
ATOM   4689 N NE  . ARG B 1 186 ? -4.955  13.525  26.252  1   80.68  ? 186 ARG B NE  1 
ATOM   4690 C CZ  . ARG B 1 186 ? -6.109  12.957  26.665  1   75.54  ? 186 ARG B CZ  1 
ATOM   4691 N NH1 . ARG B 1 186 ? -6.508  13.155  27.907  1   78.08  ? 186 ARG B NH1 1 
ATOM   4692 N NH2 . ARG B 1 186 ? -6.894  12.253  25.844  1   74.62  ? 186 ARG B NH2 1 
ATOM   4693 N N   . TYR B 1 187 ? -8.723  15.794  22.221  1   40.05  ? 187 TYR B N   1 
ATOM   4694 C CA  . TYR B 1 187 ? -9.482  15.276  21.088  1   38.29  ? 187 TYR B CA  1 
ATOM   4695 C C   . TYR B 1 187 ? -9.228  16.166  19.879  1   37.82  ? 187 TYR B C   1 
ATOM   4696 O O   . TYR B 1 187 ? -8.899  15.681  18.786  1   35.02  ? 187 TYR B O   1 
ATOM   4697 C CB  . TYR B 1 187 ? -10.991 15.188  21.302  1   37.95  ? 187 TYR B CB  1 
ATOM   4698 C CG  . TYR B 1 187 ? -11.707 14.786  20.024  1   35.58  ? 187 TYR B CG  1 
ATOM   4699 C CD1 . TYR B 1 187 ? -11.689 13.459  19.573  1   37.29  ? 187 TYR B CD1 1 
ATOM   4700 C CD2 . TYR B 1 187 ? -12.347 15.734  19.248  1   35.65  ? 187 TYR B CD2 1 
ATOM   4701 C CE1 . TYR B 1 187 ? -12.304 13.099  18.388  1   33.83  ? 187 TYR B CE1 1 
ATOM   4702 C CE2 . TYR B 1 187 ? -12.927 15.391  18.035  1   35.67  ? 187 TYR B CE2 1 
ATOM   4703 C CZ  . TYR B 1 187 ? -12.922 14.069  17.623  1   36.59  ? 187 TYR B CZ  1 
ATOM   4704 O OH  . TYR B 1 187 ? -13.466 13.765  16.417  1   40.23  ? 187 TYR B OH  1 
ATOM   4705 N N   . LEU B 1 188 ? -9.382  17.465  20.098  1   35.43  ? 188 LEU B N   1 
ATOM   4706 C CA  . LEU B 1 188 ? -9.189  18.409  19.026  1   36.54  ? 188 LEU B CA  1 
ATOM   4707 C C   . LEU B 1 188 ? -7.722  18.491  18.606  1   34.15  ? 188 LEU B C   1 
ATOM   4708 O O   . LEU B 1 188 ? -7.421  18.553  17.407  1   31.64  ? 188 LEU B O   1 
ATOM   4709 C CB  . LEU B 1 188 ? -9.777  19.744  19.479  1   37.8   ? 188 LEU B CB  1 
ATOM   4710 C CG  . LEU B 1 188 ? -9.72   20.862  18.438  1   38.89  ? 188 LEU B CG  1 
ATOM   4711 C CD1 . LEU B 1 188 ? -10.869 21.807  18.602  1   41.19  ? 188 LEU B CD1 1 
ATOM   4712 C CD2 . LEU B 1 188 ? -8.414  21.625  18.562  1   41.04  ? 188 LEU B CD2 1 
ATOM   4713 N N   . LYS B 1 189 ? -6.791  18.51   19.559  1   33.59  ? 189 LYS B N   1 
ATOM   4714 C CA  . LYS B 1 189 ? -5.377  18.594  19.193  1   36.15  ? 189 LYS B CA  1 
ATOM   4715 C C   . LYS B 1 189 ? -5.001  17.417  18.294  1   33.84  ? 189 LYS B C   1 
ATOM   4716 O O   . LYS B 1 189 ? -4.286  17.549  17.308  1   31.81  ? 189 LYS B O   1 
ATOM   4717 C CB  . LYS B 1 189 ? -4.51   18.548  20.449  1   40.27  ? 189 LYS B CB  1 
ATOM   4718 C CG  . LYS B 1 189 ? -3.027  18.837  20.287  1   43.51  ? 189 LYS B CG  1 
ATOM   4719 C CD  . LYS B 1 189 ? -2.339  18.505  21.605  1   50.83  ? 189 LYS B CD  1 
ATOM   4720 C CE  . LYS B 1 189 ? -1.17   19.323  21.967  1   57.81  ? 189 LYS B CE  1 
ATOM   4721 N NZ  . LYS B 1 189 ? 0.041   18.75   21.402  1   60.69  ? 189 LYS B NZ  1 
ATOM   4722 N N   . ASN B 1 190 ? -5.513  16.247  18.653  1   35.96  ? 190 ASN B N   1 
ATOM   4723 C CA  . ASN B 1 190 ? -5.276  15.035  17.88   1   37.06  ? 190 ASN B CA  1 
ATOM   4724 C C   . ASN B 1 190 ? -5.859  15.087  16.476  1   30.85  ? 190 ASN B C   1 
ATOM   4725 O O   . ASN B 1 190 ? -5.213  14.665  15.51   1   31.89  ? 190 ASN B O   1 
ATOM   4726 C CB  . ASN B 1 190 ? -5.816  13.796  18.572  1   42.52  ? 190 ASN B CB  1 
ATOM   4727 C CG  . ASN B 1 190 ? -4.66   12.915  18.894  1   57.56  ? 190 ASN B CG  1 
ATOM   4728 O OD1 . ASN B 1 190 ? -3.916  13.205  19.848  1   61.81  ? 190 ASN B OD1 1 
ATOM   4729 N ND2 . ASN B 1 190 ? -4.456  11.927  18.02   1   54.41  ? 190 ASN B ND2 1 
ATOM   4730 N N   . SER B 1 191 ? -7.097  15.561  16.379  1   30.24  ? 191 SER B N   1 
ATOM   4731 C CA  . SER B 1 191 ? -7.722  15.8    15.079  1   29.87  ? 191 SER B CA  1 
ATOM   4732 C C   . SER B 1 191 ? -6.881  16.764  14.226  1   28.83  ? 191 SER B C   1 
ATOM   4733 O O   . SER B 1 191 ? -6.7    16.531  13.027  1   27.82  ? 191 SER B O   1 
ATOM   4734 C CB  . SER B 1 191 ? -9.127  16.271  15.262  1   28.97  ? 191 SER B CB  1 
ATOM   4735 O OG  . SER B 1 191 ? -9.818  16.232  14.017  1   27.44  ? 191 SER B OG  1 
ATOM   4736 N N   . PHE B 1 192 ? -6.423  17.87   14.829  1   28.8   ? 192 PHE B N   1 
ATOM   4737 C CA  . PHE B 1 192 ? -5.58   18.842  14.131  1   28.73  ? 192 PHE B CA  1 
ATOM   4738 C C   . PHE B 1 192 ? -4.241  18.234  13.67   1   29.88  ? 192 PHE B C   1 
ATOM   4739 O O   . PHE B 1 192 ? -3.729  18.586  12.603  1   28.73  ? 192 PHE B O   1 
ATOM   4740 C CB  . PHE B 1 192 ? -5.345  20.078  15.005  1   28.95  ? 192 PHE B CB  1 
ATOM   4741 C CG  . PHE B 1 192 ? -6.48   21.09   15.031  1   27.12  ? 192 PHE B CG  1 
ATOM   4742 C CD1 . PHE B 1 192 ? -7.807  20.749  14.708  1   26.03  ? 192 PHE B CD1 1 
ATOM   4743 C CD2 . PHE B 1 192 ? -6.197  22.403  15.414  1   27.85  ? 192 PHE B CD2 1 
ATOM   4744 C CE1 . PHE B 1 192 ? -8.824  21.717  14.733  1   26.16  ? 192 PHE B CE1 1 
ATOM   4745 C CE2 . PHE B 1 192 ? -7.224  23.346  15.484  1   29.22  ? 192 PHE B CE2 1 
ATOM   4746 C CZ  . PHE B 1 192 ? -8.534  22.99   15.154  1   27.88  ? 192 PHE B CZ  1 
ATOM   4747 N N   . GLU B 1 193 ? -3.671  17.317  14.45   1   30.31  ? 193 GLU B N   1 
ATOM   4748 C CA  . GLU B 1 193 ? -2.453  16.644  14.033  1   30.54  ? 193 GLU B CA  1 
ATOM   4749 C C   . GLU B 1 193 ? -2.702  15.876  12.733  1   29.3   ? 193 GLU B C   1 
ATOM   4750 O O   . GLU B 1 193 ? -1.862  15.916  11.815  1   28.33  ? 193 GLU B O   1 
ATOM   4751 C CB  . GLU B 1 193 ? -1.902  15.703  15.11   1   32.57  ? 193 GLU B CB  1 
ATOM   4752 C CG  . GLU B 1 193 ? -1.271  16.435  16.296  1   36.98  ? 193 GLU B CG  1 
ATOM   4753 C CD  . GLU B 1 193 ? -1.028  15.552  17.533  1   44.33  ? 193 GLU B CD  1 
ATOM   4754 O OE1 . GLU B 1 193 ? -0.712  14.373  17.354  1   51.32  ? 193 GLU B OE1 1 
ATOM   4755 O OE2 . GLU B 1 193 ? -1.158  16.027  18.656  1   51.23  ? 193 GLU B OE2 1 
ATOM   4756 N N   . THR B 1 194 ? -3.847  15.166  12.638  1   27.74  ? 194 THR B N   1 
ATOM   4757 C CA  . THR B 1 194 ? -4.176  14.45   11.418  1   27.57  ? 194 THR B CA  1 
ATOM   4758 C C   . THR B 1 194 ? -4.377  15.45   10.282  1   28.31  ? 194 THR B C   1 
ATOM   4759 O O   . THR B 1 194 ? -3.903  15.216  9.175   1   25.13  ? 194 THR B O   1 
ATOM   4760 C CB  . THR B 1 194 ? -5.428  13.592  11.58   1   29.75  ? 194 THR B CB  1 
ATOM   4761 O OG1 . THR B 1 194 ? -5.211  12.712  12.669  1   29.02  ? 194 THR B OG1 1 
ATOM   4762 C CG2 . THR B 1 194 ? -5.665  12.724  10.36   1   31.9   ? 194 THR B CG2 1 
ATOM   4763 N N   . ARG B 1 195 ? -5.128  16.533  10.534  1   26.35  ? 195 ARG B N   1 
ATOM   4764 C CA  . ARG B 1 195 ? -5.284  17.566  9.516   1   26.44  ? 195 ARG B CA  1 
ATOM   4765 C C   . ARG B 1 195 ? -3.949  18.023  8.945   1   26.08  ? 195 ARG B C   1 
ATOM   4766 O O   . ARG B 1 195 ? -3.825  18.182  7.716   1   26.04  ? 195 ARG B O   1 
ATOM   4767 C CB  . ARG B 1 195 ? -6.036  18.821  9.989   1   26.06  ? 195 ARG B CB  1 
ATOM   4768 C CG  . ARG B 1 195 ? -7.496  18.585  10.317  1   26.84  ? 195 ARG B CG  1 
ATOM   4769 C CD  . ARG B 1 195 ? -8.108  19.875  10.859  1   28.54  ? 195 ARG B CD  1 
ATOM   4770 N NE  . ARG B 1 195 ? -9.51   19.703  11.22   1   27.37  ? 195 ARG B NE  1 
ATOM   4771 C CZ  . ARG B 1 195 ? -10.508 19.983  10.39   1   29.48  ? 195 ARG B CZ  1 
ATOM   4772 N NH1 . ARG B 1 195 ? -11.737 20.054  10.876  1   30.39  ? 195 ARG B NH1 1 
ATOM   4773 N NH2 . ARG B 1 195 ? -10.284 20.27   9.107   1   27.84  ? 195 ARG B NH2 1 
ATOM   4774 N N   . ILE B 1 196 ? -2.982  18.26   9.836   1   26.83  ? 196 ILE B N   1 
ATOM   4775 C CA  . ILE B 1 196 ? -1.688  18.81   9.47    1   29.52  ? 196 ILE B CA  1 
ATOM   4776 C C   . ILE B 1 196 ? -0.877  17.784  8.686   1   27.86  ? 196 ILE B C   1 
ATOM   4777 O O   . ILE B 1 196 ? -0.217  18.153  7.735   1   25.22  ? 196 ILE B O   1 
ATOM   4778 C CB  . ILE B 1 196 ? -0.952  19.327  10.717  1   31.75  ? 196 ILE B CB  1 
ATOM   4779 C CG1 . ILE B 1 196 ? -1.61   20.643  11.17   1   34.94  ? 196 ILE B CG1 1 
ATOM   4780 C CG2 . ILE B 1 196 ? 0.558   19.475  10.512  1   35.11  ? 196 ILE B CG2 1 
ATOM   4781 C CD1 . ILE B 1 196 ? -1.451  21.799  10.182  1   39.43  ? 196 ILE B CD1 1 
ATOM   4782 N N   . ASN B 1 197 ? -0.972  16.508  9.065   1   27.9   ? 197 ASN B N   1 
ATOM   4783 C CA  . ASN B 1 197 ? -0.299  15.469  8.293   1   27.18  ? 197 ASN B CA  1 
ATOM   4784 C C   . ASN B 1 197 ? -0.792  15.434  6.841   1   24.71  ? 197 ASN B C   1 
ATOM   4785 O O   . ASN B 1 197 ? 0.018   15.295  5.924   1   26.15  ? 197 ASN B O   1 
ATOM   4786 C CB  . ASN B 1 197 ? -0.414  14.108  8.973   1   27.48  ? 197 ASN B CB  1 
ATOM   4787 C CG  . ASN B 1 197 ? 0.487   13.998  10.191  1   30.54  ? 197 ASN B CG  1 
ATOM   4788 O OD1 . ASN B 1 197 ? 1.578   14.558  10.211  1   33.26  ? 197 ASN B OD1 1 
ATOM   4789 N ND2 . ASN B 1 197 ? 0.064   13.309  11.235  1   29.95  ? 197 ASN B ND2 1 
ATOM   4790 N N   . VAL B 1 198 ? -2.092  15.526  6.631   1   24.13  ? 198 VAL B N   1 
ATOM   4791 C CA  . VAL B 1 198 ? -2.642  15.469  5.276   1   23.95  ? 198 VAL B CA  1 
ATOM   4792 C C   . VAL B 1 198 ? -2.316  16.767  4.531   1   25.56  ? 198 VAL B C   1 
ATOM   4793 O O   . VAL B 1 198 ? -1.973  16.721  3.342   1   27.73  ? 198 VAL B O   1 
ATOM   4794 C CB  . VAL B 1 198 ? -4.146  15.168  5.252   1   25.85  ? 198 VAL B CB  1 
ATOM   4795 C CG1 . VAL B 1 198 ? -4.647  14.966  3.826   1   28.04  ? 198 VAL B CG1 1 
ATOM   4796 C CG2 . VAL B 1 198 ? -4.474  13.937  6.068   1   25.26  ? 198 VAL B CG2 1 
ATOM   4797 N N   . LEU B 1 199 ? -2.392  17.907  5.214   1   25.65  ? 199 LEU B N   1 
ATOM   4798 C CA  . LEU B 1 199 ? -1.954  19.163  4.599   1   26.52  ? 199 LEU B CA  1 
ATOM   4799 C C   . LEU B 1 199 ? -0.477  19.116  4.215   1   26.41  ? 199 LEU B C   1 
ATOM   4800 O O   . LEU B 1 199 ? -0.148  19.499  3.076   1   25.07  ? 199 LEU B O   1 
ATOM   4801 C CB  . LEU B 1 199 ? -2.249  20.356  5.485   1   26.54  ? 199 LEU B CB  1 
ATOM   4802 C CG  . LEU B 1 199 ? -3.706  20.797  5.464   1   26.87  ? 199 LEU B CG  1 
ATOM   4803 C CD1 . LEU B 1 199 ? -4.043  21.64   6.722   1   27.06  ? 199 LEU B CD1 1 
ATOM   4804 C CD2 . LEU B 1 199 ? -4.039  21.531  4.207   1   27.4   ? 199 LEU B CD2 1 
ATOM   4805 N N   . LEU B 1 200 ? 0.39    18.612  5.118   1   25.71  ? 200 LEU B N   1 
ATOM   4806 C CA  . LEU B 1 200 ? 1.811   18.521  4.831   1   25.59  ? 200 LEU B CA  1 
ATOM   4807 C C   . LEU B 1 200 ? 2.065   17.592  3.652   1   25.38  ? 200 LEU B C   1 
ATOM   4808 O O   . LEU B 1 200 ? 2.938   17.889  2.822   1   24.97  ? 200 LEU B O   1 
ATOM   4809 C CB  . LEU B 1 200 ? 2.663   18.112  6.03    1   26.83  ? 200 LEU B CB  1 
ATOM   4810 C CG  . LEU B 1 200 ? 3.054   19.239  6.951   1   30.17  ? 200 LEU B CG  1 
ATOM   4811 C CD1 . LEU B 1 200 ? 3.718   18.573  8.195   1   31.66  ? 200 LEU B CD1 1 
ATOM   4812 C CD2 . LEU B 1 200 ? 4       20.239  6.259   1   33.22  ? 200 LEU B CD2 1 
ATOM   4813 N N   . SER B 1 201 ? 1.301   16.486  3.58    1   24.84  ? 201 SER B N   1 
ATOM   4814 C CA  . SER B 1 201 ? 1.406   15.587  2.447   1   25.79  ? 201 SER B CA  1 
ATOM   4815 C C   . SER B 1 201 ? 1.227   16.344  1.122   1   26.61  ? 201 SER B C   1 
ATOM   4816 O O   . SER B 1 201 ? 1.979   16.124  0.162   1   24.45  ? 201 SER B O   1 
ATOM   4817 C CB  . SER B 1 201 ? 0.426   14.399  2.578   1   27.37  ? 201 SER B CB  1 
ATOM   4818 O OG  . SER B 1 201 ? 0.605   13.51   1.486   1   26.32  ? 201 SER B OG  1 
ATOM   4819 N N   . ASN B 1 202 ? 0.195   17.18   1.068   1   25.2   ? 202 ASN B N   1 
ATOM   4820 C CA  . ASN B 1 202 ? -0.077  17.981  -0.124  1   26.51  ? 202 ASN B CA  1 
ATOM   4821 C C   . ASN B 1 202 ? 1.011   19.023  -0.353  1   25.87  ? 202 ASN B C   1 
ATOM   4822 O O   . ASN B 1 202 ? 1.355   19.258  -1.513  1   25.56  ? 202 ASN B O   1 
ATOM   4823 C CB  . ASN B 1 202 ? -1.446  18.65   -0.054  1   24.99  ? 202 ASN B CB  1 
ATOM   4824 C CG  . ASN B 1 202 ? -2.53   17.709  -0.45   1   25.92  ? 202 ASN B CG  1 
ATOM   4825 O OD1 . ASN B 1 202 ? -2.915  17.637  -1.633  1   24.82  ? 202 ASN B OD1 1 
ATOM   4826 N ND2 . ASN B 1 202 ? -3.091  17.039  0.549   1   27.94  ? 202 ASN B ND2 1 
ATOM   4827 N N   . ILE B 1 203 ? 1.521   19.67   0.72    1   24.19  ? 203 ILE B N   1 
ATOM   4828 C CA  . ILE B 1 203 ? 2.57    20.685  0.581   1   23.28  ? 203 ILE B CA  1 
ATOM   4829 C C   . ILE B 1 203 ? 3.812   20.053  -0.087  1   27.5   ? 203 ILE B C   1 
ATOM   4830 O O   . ILE B 1 203 ? 4.409   20.629  -1.01   1   26.2   ? 203 ILE B O   1 
ATOM   4831 C CB  . ILE B 1 203 ? 2.879   21.327  1.959   1   23.94  ? 203 ILE B CB  1 
ATOM   4832 C CG1 . ILE B 1 203 ? 1.768   22.27   2.348   1   26.87  ? 203 ILE B CG1 1 
ATOM   4833 C CG2 . ILE B 1 203 ? 4.22    22.05   1.952   1   26.6   ? 203 ILE B CG2 1 
ATOM   4834 C CD1 . ILE B 1 203 ? 1.77    22.763  3.788   1   26.02  ? 203 ILE B CD1 1 
ATOM   4835 N N   . TYR B 1 204 ? 4.197   18.85   0.361   1   23.63  ? 204 TYR B N   1 
ATOM   4836 C CA  . TYR B 1 204 ? 5.345   18.166  -0.181  1   25.19  ? 204 TYR B CA  1 
ATOM   4837 C C   . TYR B 1 204 ? 5.085   17.638  -1.583  1   25.5   ? 204 TYR B C   1 
ATOM   4838 O O   . TYR B 1 204 ? 6.02    17.655  -2.406  1   25.97  ? 204 TYR B O   1 
ATOM   4839 C CB  . TYR B 1 204 ? 5.837   17.075  0.775   1   24.01  ? 204 TYR B CB  1 
ATOM   4840 C CG  . TYR B 1 204 ? 6.603   17.65   1.96    1   29.42  ? 204 TYR B CG  1 
ATOM   4841 C CD1 . TYR B 1 204 ? 7.65    18.565  1.793   1   31.01  ? 204 TYR B CD1 1 
ATOM   4842 C CD2 . TYR B 1 204 ? 6.219   17.326  3.258   1   33.37  ? 204 TYR B CD2 1 
ATOM   4843 C CE1 . TYR B 1 204 ? 8.35    19.055  2.893   1   35.27  ? 204 TYR B CE1 1 
ATOM   4844 C CE2 . TYR B 1 204 ? 6.857   17.87   4.357   1   34.56  ? 204 TYR B CE2 1 
ATOM   4845 C CZ  . TYR B 1 204 ? 7.931   18.727  4.176   1   37.81  ? 204 TYR B CZ  1 
ATOM   4846 O OH  . TYR B 1 204 ? 8.574   19.133  5.32    1   40.91  ? 204 TYR B OH  1 
ATOM   4847 N N   . LEU B 1 205 ? 3.851   17.168  -1.852  1   24.37  ? 205 LEU B N   1 
ATOM   4848 C CA  . LEU B 1 205 ? 3.471   16.824  -3.209  1   25     ? 205 LEU B CA  1 
ATOM   4849 C C   . LEU B 1 205 ? 3.738   18.002  -4.166  1   28.07  ? 205 LEU B C   1 
ATOM   4850 O O   . LEU B 1 205 ? 4.394   17.837  -5.192  1   24.87  ? 205 LEU B O   1 
ATOM   4851 C CB  . LEU B 1 205 ? 2.003   16.409  -3.247  1   26.01  ? 205 LEU B CB  1 
ATOM   4852 C CG  . LEU B 1 205 ? 1.416   16.084  -4.631  1   27.9   ? 205 LEU B CG  1 
ATOM   4853 C CD1 . LEU B 1 205 ? 1.926   14.76   -5.133  1   27.27  ? 205 LEU B CD1 1 
ATOM   4854 C CD2 . LEU B 1 205 ? -0.075  16.086  -4.623  1   31.7   ? 205 LEU B CD2 1 
ATOM   4855 N N   . ASN B 1 206 ? 3.293   19.197  -3.783  1   25.46  ? 206 ASN B N   1 
ATOM   4856 C CA  . ASN B 1 206 ? 3.385   20.372  -4.654  1   27.08  ? 206 ASN B CA  1 
ATOM   4857 C C   . ASN B 1 206 ? 4.813   20.898  -4.777  1   30.13  ? 206 ASN B C   1 
ATOM   4858 O O   . ASN B 1 206 ? 5.131   21.597  -5.742  1   31.01  ? 206 ASN B O   1 
ATOM   4859 C CB  . ASN B 1 206 ? 2.365   21.428  -4.239  1   25.93  ? 206 ASN B CB  1 
ATOM   4860 C CG  . ASN B 1 206 ? 0.93    20.975  -4.38   1   26.78  ? 206 ASN B CG  1 
ATOM   4861 O OD1 . ASN B 1 206 ? 0.017   21.412  -3.64   1   29.39  ? 206 ASN B OD1 1 
ATOM   4862 N ND2 . ASN B 1 206 ? 0.716   20.038  -5.255  1   27.63  ? 206 ASN B ND2 1 
ATOM   4863 N N   . GLU B 1 207 ? 5.679   20.572  -3.81   1   26.6   ? 207 GLU B N   1 
ATOM   4864 C CA  . GLU B 1 207 ? 7.1     20.832  -3.835  1   28.09  ? 207 GLU B CA  1 
ATOM   4865 C C   . GLU B 1 207 ? 7.857   19.738  -4.568  1   28.15  ? 207 GLU B C   1 
ATOM   4866 O O   . GLU B 1 207 ? 9.061   19.838  -4.672  1   29.27  ? 207 GLU B O   1 
ATOM   4867 C CB  . GLU B 1 207 ? 7.672   21.01   -2.418  1   29.95  ? 207 GLU B CB  1 
ATOM   4868 C CG  . GLU B 1 207 ? 7.363   22.379  -1.824  1   32.67  ? 207 GLU B CG  1 
ATOM   4869 C CD  . GLU B 1 207 ? 8.2     23.435  -2.528  1   39.34  ? 207 GLU B CD  1 
ATOM   4870 O OE1 . GLU B 1 207 ? 9.432   23.532  -2.267  1   47.57  ? 207 GLU B OE1 1 
ATOM   4871 O OE2 . GLU B 1 207 ? 7.648   24.027  -3.484  1   44.54  ? 207 GLU B OE2 1 
ATOM   4872 N N   . ASN B 1 208 ? 7.184   18.72   -5.107  1   27.22  ? 208 ASN B N   1 
ATOM   4873 C CA  . ASN B 1 208 ? 7.871   17.615  -5.775  1   29.8   ? 208 ASN B CA  1 
ATOM   4874 C C   . ASN B 1 208 ? 8.823   16.853  -4.825  1   33.24  ? 208 ASN B C   1 
ATOM   4875 O O   . ASN B 1 208 ? 9.851   16.302  -5.263  1   33.23  ? 208 ASN B O   1 
ATOM   4876 C CB  . ASN B 1 208 ? 8.573   18.074  -7.072  1   32.12  ? 208 ASN B CB  1 
ATOM   4877 C CG  . ASN B 1 208 ? 8.918   16.92   -7.978  1   34.15  ? 208 ASN B CG  1 
ATOM   4878 O OD1 . ASN B 1 208 ? 9.891   16.955  -8.732  1   45.57  ? 208 ASN B OD1 1 
ATOM   4879 N ND2 . ASN B 1 208 ? 8.088   15.912  -7.991  1   34.39  ? 208 ASN B ND2 1 
ATOM   4880 N N   . ASN B 1 209 ? 8.479   16.788  -3.532  1   30.73  ? 209 ASN B N   1 
ATOM   4881 C CA  . ASN B 1 209 ? 9.169   15.916  -2.582  1   28.13  ? 209 ASN B CA  1 
ATOM   4882 C C   . ASN B 1 209 ? 8.278   14.702  -2.331  1   30.32  ? 209 ASN B C   1 
ATOM   4883 O O   . ASN B 1 209 ? 7.499   14.665  -1.375  1   28.89  ? 209 ASN B O   1 
ATOM   4884 C CB  . ASN B 1 209 ? 9.506   16.608  -1.28   1   30.82  ? 209 ASN B CB  1 
ATOM   4885 C CG  . ASN B 1 209 ? 10.443  15.701  -0.47   1   42.57  ? 209 ASN B CG  1 
ATOM   4886 O OD1 . ASN B 1 209 ? 10.515  14.445  -0.602  1   37.92  ? 209 ASN B OD1 1 
ATOM   4887 N ND2 . ASN B 1 209 ? 11.232  16.353  0.358   1   49.01  ? 209 ASN B ND2 1 
ATOM   4888 N N   . LEU B 1 210 ? 8.372   13.723  -3.219  1   26.95  ? 210 LEU B N   1 
ATOM   4889 C CA  . LEU B 1 210 ? 7.354   12.69   -3.282  1   31.21  ? 210 LEU B CA  1 
ATOM   4890 C C   . LEU B 1 210 ? 7.507   11.691  -2.118  1   32.19  ? 210 LEU B C   1 
ATOM   4891 O O   . LEU B 1 210 ? 6.492   11.202  -1.614  1   29.44  ? 210 LEU B O   1 
ATOM   4892 C CB  . LEU B 1 210 ? 7.412   12.022  -4.648  1   30.49  ? 210 LEU B CB  1 
ATOM   4893 C CG  . LEU B 1 210 ? 7.225   12.985  -5.842  1   32.5   ? 210 LEU B CG  1 
ATOM   4894 C CD1 . LEU B 1 210 ? 7.222   12.245  -7.152  1   34.43  ? 210 LEU B CD1 1 
ATOM   4895 C CD2 . LEU B 1 210 ? 6.005   13.87   -5.694  1   34.84  ? 210 LEU B CD2 1 
ATOM   4896 N N   . GLU B 1 211 ? 8.742   11.468  -1.663  1   29.82  ? 211 GLU B N   1 
ATOM   4897 C CA  . GLU B 1 211 ? 8.994   10.542  -0.558  1   34.29  ? 211 GLU B CA  1 
ATOM   4898 C C   . GLU B 1 211 ? 8.379   11.104  0.733   1   33.5   ? 211 GLU B C   1 
ATOM   4899 O O   . GLU B 1 211 ? 7.735   10.347  1.464   1   34.25  ? 211 GLU B O   1 
ATOM   4900 C CB  . GLU B 1 211 ? 10.464  10.159  -0.397  1   41.04  ? 211 GLU B CB  1 
ATOM   4901 C CG  . GLU B 1 211 ? 11.093  9.497   -1.624  1   49.48  ? 211 GLU B CG  1 
ATOM   4902 C CD  . GLU B 1 211 ? 11.579  10.452  -2.733  1   62.86  ? 211 GLU B CD  1 
ATOM   4903 O OE1 . GLU B 1 211 ? 11.195  11.673  -2.855  1   58.4   ? 211 GLU B OE1 1 
ATOM   4904 O OE2 . GLU B 1 211 ? 12.423  9.943   -3.505  1   70.78  ? 211 GLU B OE2 1 
ATOM   4905 N N   . LEU B 1 212 ? 8.568   12.41   1.009   1   30.87  ? 212 LEU B N   1 
ATOM   4906 C CA  . LEU B 1 212 ? 7.971   13.058  2.163   1   31.37  ? 212 LEU B CA  1 
ATOM   4907 C C   . LEU B 1 212 ? 6.463   13.161  2.045   1   28.21  ? 212 LEU B C   1 
ATOM   4908 O O   . LEU B 1 212 ? 5.781   12.995  3.072   1   28.22  ? 212 LEU B O   1 
ATOM   4909 C CB  . LEU B 1 212 ? 8.516   14.451  2.496   1   39.6   ? 212 LEU B CB  1 
ATOM   4910 C CG  . LEU B 1 212 ? 9.886   14.525  3.172   1   51.19  ? 212 LEU B CG  1 
ATOM   4911 C CD1 . LEU B 1 212 ? 10.246  16.001  3.445   1   51.01  ? 212 LEU B CD1 1 
ATOM   4912 C CD2 . LEU B 1 212 ? 9.904   13.716  4.47    1   48.76  ? 212 LEU B CD2 1 
ATOM   4913 N N   . CYS B 1 213 ? 5.95    13.329  0.833   1   26.28  ? 213 CYS B N   1 
ATOM   4914 C CA  . CYS B 1 213 ? 4.528   13.359  0.601   1   25.5   ? 213 CYS B CA  1 
ATOM   4915 C C   . CYS B 1 213 ? 3.933   12.051  1.084   1   26.08  ? 213 CYS B C   1 
ATOM   4916 O O   . CYS B 1 213 ? 3.02    12.026  1.827   1   28.47  ? 213 CYS B O   1 
ATOM   4917 C CB  . CYS B 1 213 ? 4.211   13.515  -0.891  1   25.8   ? 213 CYS B CB  1 
ATOM   4918 S SG  . CYS B 1 213 ? 2.536   13.119  -1.336  1   28.46  ? 213 CYS B SG  1 
ATOM   4919 N N   . ARG B 1 214 ? 4.491   10.963  0.604   1   24.53  ? 214 ARG B N   1 
ATOM   4920 C CA  . ARG B 1 214 ? 4.029   9.641   0.958   1   27.27  ? 214 ARG B CA  1 
ATOM   4921 C C   . ARG B 1 214 ? 4.173   9.33    2.46    1   28.04  ? 214 ARG B C   1 
ATOM   4922 O O   . ARG B 1 214 ? 3.314   8.757   3.042   1   26.26  ? 214 ARG B O   1 
ATOM   4923 C CB  . ARG B 1 214 ? 4.684   8.604   0.072   1   29.69  ? 214 ARG B CB  1 
ATOM   4924 C CG  . ARG B 1 214 ? 4.306   8.81    -1.368  1   31.83  ? 214 ARG B CG  1 
ATOM   4925 C CD  . ARG B 1 214 ? 4.656   7.647   -2.216  1   36.23  ? 214 ARG B CD  1 
ATOM   4926 N NE  . ARG B 1 214 ? 6.024   7.669   -2.609  1   37.9   ? 214 ARG B NE  1 
ATOM   4927 C CZ  . ARG B 1 214 ? 6.466   8.127   -3.758  1   36.25  ? 214 ARG B CZ  1 
ATOM   4928 N NH1 . ARG B 1 214 ? 7.727   8.046   -4.018  1   35.64  ? 214 ARG B NH1 1 
ATOM   4929 N NH2 . ARG B 1 214 ? 5.656   8.643   -4.629  1   34.31  ? 214 ARG B NH2 1 
ATOM   4930 N N   . GLU B 1 215 ? 5.271   9.738   3.049   1   28.5   ? 215 GLU B N   1 
ATOM   4931 C CA  . GLU B 1 215 ? 5.507   9.541   4.462   1   30.92  ? 215 GLU B CA  1 
ATOM   4932 C C   . GLU B 1 215 ? 4.42    10.2    5.324   1   29.48  ? 215 GLU B C   1 
ATOM   4933 O O   . GLU B 1 215 ? 3.913   9.586   6.197   1   27.62  ? 215 GLU B O   1 
ATOM   4934 C CB  . GLU B 1 215 ? 6.88    10.073  4.821   1   34.12  ? 215 GLU B CB  1 
ATOM   4935 C CG  . GLU B 1 215 ? 7.224   9.98    6.289   1   49.67  ? 215 GLU B CG  1 
ATOM   4936 C CD  . GLU B 1 215 ? 8.551   10.632  6.648   1   57.34  ? 215 GLU B CD  1 
ATOM   4937 O OE1 . GLU B 1 215 ? 9.514   10.456  5.909   1   54.51  ? 215 GLU B OE1 1 
ATOM   4938 O OE2 . GLU B 1 215 ? 8.616   11.317  7.671   1   64.42  ? 215 GLU B OE2 1 
ATOM   4939 N N   . TYR B 1 216 ? 4.062   11.444  5.033   1   26.25  ? 216 TYR B N   1 
ATOM   4940 C CA  . TYR B 1 216 ? 3.043   12.163  5.796   1   28.44  ? 216 TYR B CA  1 
ATOM   4941 C C   . TYR B 1 216 ? 1.633   11.618  5.577   1   27.77  ? 216 TYR B C   1 
ATOM   4942 O O   . TYR B 1 216 ? 0.841   11.562  6.528   1   29.1   ? 216 TYR B O   1 
ATOM   4943 C CB  . TYR B 1 216 ? 3.128   13.674  5.575   1   29.25  ? 216 TYR B CB  1 
ATOM   4944 C CG  . TYR B 1 216 ? 4.211   14.319  6.414   1   32.33  ? 216 TYR B CG  1 
ATOM   4945 C CD1 . TYR B 1 216 ? 4.009   14.528  7.777   1   33.89  ? 216 TYR B CD1 1 
ATOM   4946 C CD2 . TYR B 1 216 ? 5.441   14.675  5.864   1   39.56  ? 216 TYR B CD2 1 
ATOM   4947 C CE1 . TYR B 1 216 ? 4.983   15.114  8.563   1   38.39  ? 216 TYR B CE1 1 
ATOM   4948 C CE2 . TYR B 1 216 ? 6.421   15.283  6.633   1   38.31  ? 216 TYR B CE2 1 
ATOM   4949 C CZ  . TYR B 1 216 ? 6.187   15.48   7.986   1   42.47  ? 216 TYR B CZ  1 
ATOM   4950 O OH  . TYR B 1 216 ? 7.113   15.999  8.8     1   47.38  ? 216 TYR B OH  1 
ATOM   4951 N N   . ALA B 1 217 ? 1.314   11.168  4.372   1   26.92  ? 217 ALA B N   1 
ATOM   4952 C CA  . ALA B 1 217 ? 0.028   10.504  4.145   1   27.59  ? 217 ALA B CA  1 
ATOM   4953 C C   . ALA B 1 217 ? -0.038  9.196   4.929   1   27.71  ? 217 ALA B C   1 
ATOM   4954 O O   . ALA B 1 217 ? -1.06   8.917   5.556   1   27.2   ? 217 ALA B O   1 
ATOM   4955 C CB  . ALA B 1 217 ? -0.216  10.307  2.679   1   27.26  ? 217 ALA B CB  1 
ATOM   4956 N N   . GLN B 1 218 ? 1.045   8.405   4.9     1   29.45  ? 218 GLN B N   1 
ATOM   4957 C CA  . GLN B 1 218 ? 1.11    7.165   5.66    1   31.63  ? 218 GLN B CA  1 
ATOM   4958 C C   . GLN B 1 218 ? 0.949   7.416   7.171   1   31.22  ? 218 GLN B C   1 
ATOM   4959 O O   . GLN B 1 218 ? 0.323   6.623   7.868   1   32.15  ? 218 GLN B O   1 
ATOM   4960 C CB  . GLN B 1 218 ? 2.403   6.383   5.407   1   31.89  ? 218 GLN B CB  1 
ATOM   4961 C CG  . GLN B 1 218 ? 2.31    5.479   4.193   1   38.33  ? 218 GLN B CG  1 
ATOM   4962 C CD  . GLN B 1 218 ? 1.316   4.366   4.449   1   43.37  ? 218 GLN B CD  1 
ATOM   4963 O OE1 . GLN B 1 218 ? 1.424   3.594   5.41    1   52.38  ? 218 GLN B OE1 1 
ATOM   4964 N NE2 . GLN B 1 218 ? 0.336   4.278   3.576   1   42.85  ? 218 GLN B NE2 1 
ATOM   4965 N N   . LYS B 1 219 ? 1.525   8.506   7.671   1   28.46  ? 219 LYS B N   1 
ATOM   4966 C CA  . LYS B 1 219 ? 1.367   8.889   9.07    1   34.71  ? 219 LYS B CA  1 
ATOM   4967 C C   . LYS B 1 219 ? -0.103  9.16    9.397   1   33.24  ? 219 LYS B C   1 
ATOM   4968 O O   . LYS B 1 219 ? -0.59   8.732   10.432  1   31.31  ? 219 LYS B O   1 
ATOM   4969 C CB  . LYS B 1 219 ? 2.264   10.102  9.359   1   38.11  ? 219 LYS B CB  1 
ATOM   4970 C CG  . LYS B 1 219 ? 2.656   10.378  10.793  1   49.07  ? 219 LYS B CG  1 
ATOM   4971 C CD  . LYS B 1 219 ? 3.881   11.298  10.947  1   58.47  ? 219 LYS B CD  1 
ATOM   4972 C CE  . LYS B 1 219 ? 5.053   11.01   10.013  1   67.29  ? 219 LYS B CE  1 
ATOM   4973 N NZ  . LYS B 1 219 ? 6.366   11.61   10.295  1   72.91  ? 219 LYS B NZ  1 
ATOM   4974 N N   . ALA B 1 220 ? -0.8    9.895   8.523   1   28.29  ? 220 ALA B N   1 
ATOM   4975 C CA  . ALA B 1 220 ? -2.218  10.178  8.704   1   30.26  ? 220 ALA B CA  1 
ATOM   4976 C C   . ALA B 1 220 ? -3.019  8.871   8.698   1   28.77  ? 220 ALA B C   1 
ATOM   4977 O O   . ALA B 1 220 ? -3.816  8.624   9.583   1   28.91  ? 220 ALA B O   1 
ATOM   4978 C CB  . ALA B 1 220 ? -2.684  11.15   7.636   1   27.94  ? 220 ALA B CB  1 
ATOM   4979 N N   . ILE B 1 221 ? -2.722  7.974   7.758   1   28.37  ? 221 ILE B N   1 
ATOM   4980 C CA  . ILE B 1 221 ? -3.427  6.701   7.644   1   28.63  ? 221 ILE B CA  1 
ATOM   4981 C C   . ILE B 1 221 ? -3.235  5.857   8.903   1   31.65  ? 221 ILE B C   1 
ATOM   4982 O O   . ILE B 1 221 ? -4.212  5.276   9.393   1   34.21  ? 221 ILE B O   1 
ATOM   4983 C CB  . ILE B 1 221 ? -2.985  5.943   6.379   1   32.55  ? 221 ILE B CB  1 
ATOM   4984 C CG1 . ILE B 1 221 ? -3.569  6.625   5.127   1   29.39  ? 221 ILE B CG1 1 
ATOM   4985 C CG2 . ILE B 1 221 ? -3.362  4.447   6.478   1   32.96  ? 221 ILE B CG2 1 
ATOM   4986 C CD1 . ILE B 1 221 ? -2.884  6.283   3.808   1   30.86  ? 221 ILE B CD1 1 
ATOM   4987 N N   . SER B 1 222 ? -2.001  5.824   9.448   1   32.11  ? 222 SER B N   1 
ATOM   4988 C CA  . SER B 1 222 ? -1.677  5.033   10.637  1   34.19  ? 222 SER B CA  1 
ATOM   4989 C C   . SER B 1 222 ? -2.323  5.552   11.908  1   36.24  ? 222 SER B C   1 
ATOM   4990 O O   . SER B 1 222 ? -2.282  4.859   12.894  1   34.87  ? 222 SER B O   1 
ATOM   4991 C CB  . SER B 1 222 ? -0.225  4.969   10.863  1   37.18  ? 222 SER B CB  1 
ATOM   4992 O OG  . SER B 1 222 ? 0.293   4.381   9.69    1   44.21  ? 222 SER B OG  1 
ATOM   4993 N N   . SER B 1 223 ? -2.805  6.789   11.96   1   36.57  ? 223 SER B N   1 
ATOM   4994 C CA  . SER B 1 223 ? -3.266  7.357   13.228  1   38.24  ? 223 SER B CA  1 
ATOM   4995 C C   . SER B 1 223 ? -4.688  7.888   13.152  1   38.24  ? 223 SER B C   1 
ATOM   4996 O O   . SER B 1 223 ? -5.035  8.697   13.996  1   38.7   ? 223 SER B O   1 
ATOM   4997 C CB  . SER B 1 223 ? -2.315  8.455   13.626  1   40.8   ? 223 SER B CB  1 
ATOM   4998 O OG  . SER B 1 223 ? -2.203  9.334   12.52   1   40.94  ? 223 SER B OG  1 
ATOM   4999 N N   . THR B 1 224 ? -5.481  7.549   12.108  1   34.32  ? 224 THR B N   1 
ATOM   5000 C CA  . THR B 1 224 ? -6.849  8.043   11.984  1   34.06  ? 224 THR B CA  1 
ATOM   5001 C C   . THR B 1 224 ? -7.795  6.88    11.695  1   36.05  ? 224 THR B C   1 
ATOM   5002 O O   . THR B 1 224 ? -7.381  5.875   11.12   1   35.2   ? 224 THR B O   1 
ATOM   5003 C CB  . THR B 1 224 ? -6.967  9.112   10.882  1   35.54  ? 224 THR B CB  1 
ATOM   5004 O OG1 . THR B 1 224 ? -8.216  9.776   11.101  1   32.2   ? 224 THR B OG1 1 
ATOM   5005 C CG2 . THR B 1 224 ? -6.977  8.539   9.481   1   34.18  ? 224 THR B CG2 1 
ATOM   5006 N N   . ASP B 1 225 ? -9.08   7.064   12.028  1   35.88  ? 225 ASP B N   1 
ATOM   5007 C CA  . ASP B 1 225 ? -10.159 6.205   11.544  1   41.05  ? 225 ASP B CA  1 
ATOM   5008 C C   . ASP B 1 225 ? -11.263 7.072   10.934  1   37.84  ? 225 ASP B C   1 
ATOM   5009 O O   . ASP B 1 225 ? -12.421 6.65    10.874  1   38.45  ? 225 ASP B O   1 
ATOM   5010 C CB  . ASP B 1 225 ? -10.798 5.361   12.643  1   51.39  ? 225 ASP B CB  1 
ATOM   5011 C CG  . ASP B 1 225 ? -9.895  4.696   13.674  1   65.99  ? 225 ASP B CG  1 
ATOM   5012 O OD1 . ASP B 1 225 ? -9.076  3.82    13.298  1   75.46  ? 225 ASP B OD1 1 
ATOM   5013 O OD2 . ASP B 1 225 ? -10.069 5.031   14.868  1   71.62  ? 225 ASP B OD2 1 
ATOM   5014 N N   . THR B 1 226 ? -10.931 8.305   10.51   1   34.21  ? 226 THR B N   1 
ATOM   5015 C CA  . THR B 1 226 ? -11.897 9.215   9.917   1   32.72  ? 226 THR B CA  1 
ATOM   5016 C C   . THR B 1 226 ? -11.82  9.025   8.409   1   29.45  ? 226 THR B C   1 
ATOM   5017 O O   . THR B 1 226 ? -10.763 9.284   7.836   1   28.45  ? 226 THR B O   1 
ATOM   5018 C CB  . THR B 1 226 ? -11.517 10.643  10.314  1   31.26  ? 226 THR B CB  1 
ATOM   5019 O OG1 . THR B 1 226 ? -11.666 10.607  11.718  1   33.83  ? 226 THR B OG1 1 
ATOM   5020 C CG2 . THR B 1 226 ? -12.409 11.732  9.76    1   31.92  ? 226 THR B CG2 1 
ATOM   5021 N N   . GLN B 1 227 ? -12.953 8.697   7.79    1   30.14  ? 227 GLN B N   1 
ATOM   5022 C CA  . GLN B 1 227 ? -13.024 8.463   6.357   1   32.04  ? 227 GLN B CA  1 
ATOM   5023 C C   . GLN B 1 227 ? -12.369 9.616   5.581   1   29.52  ? 227 GLN B C   1 
ATOM   5024 O O   . GLN B 1 227 ? -11.602 9.383   4.64    1   30.61  ? 227 GLN B O   1 
ATOM   5025 C CB  . GLN B 1 227 ? -14.473 8.279   5.931   1   32.76  ? 227 GLN B CB  1 
ATOM   5026 C CG  . GLN B 1 227 ? -14.676 8.024   4.444   1   33.07  ? 227 GLN B CG  1 
ATOM   5027 C CD  . GLN B 1 227 ? -16.14  8.03    4.035   1   37.7   ? 227 GLN B CD  1 
ATOM   5028 O OE1 . GLN B 1 227 ? -16.99  8.66    4.675   1   38.55  ? 227 GLN B OE1 1 
ATOM   5029 N NE2 . GLN B 1 227 ? -16.448 7.392   2.916   1   34.19  ? 227 GLN B NE2 1 
ATOM   5030 N N   . ARG B 1 228 ? -12.761 10.857  5.885   1   27.59  ? 228 ARG B N   1 
ATOM   5031 C CA  . ARG B 1 228 ? -12.235 12.026  5.175   1   28.91  ? 228 ARG B CA  1 
ATOM   5032 C C   . ARG B 1 228 ? -10.69  12.014  5.082   1   28.16  ? 228 ARG B C   1 
ATOM   5033 O O   . ARG B 1 228 ? -10.147 12.326  4.021   1   25.46  ? 228 ARG B O   1 
ATOM   5034 C CB  . ARG B 1 228 ? -12.811 13.291  5.832   1   28.89  ? 228 ARG B CB  1 
ATOM   5035 C CG  . ARG B 1 228 ? -12.285 14.615  5.26    1   27.53  ? 228 ARG B CG  1 
ATOM   5036 C CD  . ARG B 1 228 ? -11.041 15.097  5.958   1   27.29  ? 228 ARG B CD  1 
ATOM   5037 N NE  . ARG B 1 228 ? -10.548 16.439  5.604   1   29.97  ? 228 ARG B NE  1 
ATOM   5038 C CZ  . ARG B 1 228 ? -11.129 17.595  5.943   1   30.81  ? 228 ARG B CZ  1 
ATOM   5039 N NH1 . ARG B 1 228 ? -12.171 17.641  6.787   1   29.25  ? 228 ARG B NH1 1 
ATOM   5040 N NH2 . ARG B 1 228 ? -10.577 18.715  5.536   1   31.49  ? 228 ARG B NH2 1 
ATOM   5041 N N   . PHE B 1 229 ? -9.972  11.737  6.195   1   26.97  ? 229 PHE B N   1 
ATOM   5042 C CA  . PHE B 1 229 ? -8.518  11.794  6.204   1   28.41  ? 229 PHE B CA  1 
ATOM   5043 C C   . PHE B 1 229 ? -7.925  10.6    5.455   1   28.65  ? 229 PHE B C   1 
ATOM   5044 O O   . PHE B 1 229 ? -6.907  10.768  4.774   1   26.43  ? 229 PHE B O   1 
ATOM   5045 C CB  . PHE B 1 229 ? -7.941  11.89   7.613   1   28.95  ? 229 PHE B CB  1 
ATOM   5046 C CG  . PHE B 1 229 ? -8.382  13.168  8.324   1   28.59  ? 229 PHE B CG  1 
ATOM   5047 C CD1 . PHE B 1 229 ? -8.164  14.402  7.74    1   31.8   ? 229 PHE B CD1 1 
ATOM   5048 C CD2 . PHE B 1 229 ? -9.02   13.13   9.543   1   30.28  ? 229 PHE B CD2 1 
ATOM   5049 C CE1 . PHE B 1 229 ? -8.575  15.575  8.364   1   32.74  ? 229 PHE B CE1 1 
ATOM   5050 C CE2 . PHE B 1 229 ? -9.39   14.306  10.207  1   31.17  ? 229 PHE B CE2 1 
ATOM   5051 C CZ  . PHE B 1 229 ? -9.207  15.515  9.606   1   33.14  ? 229 PHE B CZ  1 
ATOM   5052 N N   . LEU B 1 230 ? -8.578  9.433   5.565   1   27.68  ? 230 LEU B N   1 
ATOM   5053 C CA  . LEU B 1 230 ? -8.159  8.253   4.824   1   26.61  ? 230 LEU B CA  1 
ATOM   5054 C C   . LEU B 1 230 ? -8.296  8.523   3.328   1   28.12  ? 230 LEU B C   1 
ATOM   5055 O O   . LEU B 1 230 ? -7.355  8.242   2.574   1   28.41  ? 230 LEU B O   1 
ATOM   5056 C CB  . LEU B 1 230 ? -8.962  7.026   5.266   1   28.57  ? 230 LEU B CB  1 
ATOM   5057 C CG  . LEU B 1 230 ? -8.703  6.55    6.691   1   30.46  ? 230 LEU B CG  1 
ATOM   5058 C CD1 . LEU B 1 230 ? -9.77   5.508   7.137   1   30.5   ? 230 LEU B CD1 1 
ATOM   5059 C CD2 . LEU B 1 230 ? -7.298  5.972   6.838   1   31.81  ? 230 LEU B CD2 1 
ATOM   5060 N N   . VAL B 1 231 ? -9.44   9.076   2.91    1   25.91  ? 231 VAL B N   1 
ATOM   5061 C CA  . VAL B 1 231 ? -9.695  9.384   1.515   1   26.98  ? 231 VAL B CA  1 
ATOM   5062 C C   . VAL B 1 231 ? -8.606  10.29   0.948   1   27     ? 231 VAL B C   1 
ATOM   5063 O O   . VAL B 1 231 ? -8.034  10.016  -0.101  1   27.44  ? 231 VAL B O   1 
ATOM   5064 C CB  . VAL B 1 231 ? -11.109 9.979   1.35    1   28.72  ? 231 VAL B CB  1 
ATOM   5065 C CG1 . VAL B 1 231 ? -11.28  10.915  0.137   1   30.88  ? 231 VAL B CG1 1 
ATOM   5066 C CG2 . VAL B 1 231 ? -12.154 8.881   1.373   1   32.17  ? 231 VAL B CG2 1 
ATOM   5067 N N   . PHE B 1 232 ? -8.367  11.422  1.608   1   24.92  ? 232 PHE B N   1 
ATOM   5068 C CA  . PHE B 1 232 ? -7.38   12.365  1.104   1   27.76  ? 232 PHE B CA  1 
ATOM   5069 C C   . PHE B 1 232 ? -5.944  11.854  1.167   1   26.14  ? 232 PHE B C   1 
ATOM   5070 O O   . PHE B 1 232 ? -5.137  12.277  0.338   1   25.28  ? 232 PHE B O   1 
ATOM   5071 C CB  . PHE B 1 232 ? -7.587  13.727  1.744   1   23.88  ? 232 PHE B CB  1 
ATOM   5072 C CG  . PHE B 1 232 ? -8.821  14.432  1.214   1   26.6   ? 232 PHE B CG  1 
ATOM   5073 C CD1 . PHE B 1 232 ? -9.093  14.508  -0.137  1   27.13  ? 232 PHE B CD1 1 
ATOM   5074 C CD2 . PHE B 1 232 ? -9.741  14.987  2.083   1   28.8   ? 232 PHE B CD2 1 
ATOM   5075 C CE1 . PHE B 1 232 ? -10.225 15.143  -0.615  1   33.64  ? 232 PHE B CE1 1 
ATOM   5076 C CE2 . PHE B 1 232 ? -10.868 15.648  1.603   1   32.68  ? 232 PHE B CE2 1 
ATOM   5077 C CZ  . PHE B 1 232 ? -11.12  15.704  0.253   1   34.96  ? 232 PHE B CZ  1 
ATOM   5078 N N   . SER B 1 233 ? -5.631  10.961  2.102   1   24.56  ? 233 SER B N   1 
ATOM   5079 C CA  . SER B 1 233 ? -4.305  10.375  2.184   1   24.67  ? 233 SER B CA  1 
ATOM   5080 C C   . SER B 1 233 ? -4.082  9.467   0.982   1   24.61  ? 233 SER B C   1 
ATOM   5081 O O   . SER B 1 233 ? -3.061  9.618   0.331   1   24.96  ? 233 SER B O   1 
ATOM   5082 C CB  . SER B 1 233 ? -4.056  9.661   3.501   1   26.07  ? 233 SER B CB  1 
ATOM   5083 O OG  . SER B 1 233 ? -4.18   10.573  4.592   1   27.21  ? 233 SER B OG  1 
ATOM   5084 N N   . TYR B 1 234 ? -5.019  8.571   0.666   1   24.24  ? 234 TYR B N   1 
ATOM   5085 C CA  . TYR B 1 234 ? -4.842  7.688   -0.475  1   26.24  ? 234 TYR B CA  1 
ATOM   5086 C C   . TYR B 1 234 ? -4.836  8.505   -1.776  1   25.72  ? 234 TYR B C   1 
ATOM   5087 O O   . TYR B 1 234 ? -4.116  8.155   -2.718  1   23.94  ? 234 TYR B O   1 
ATOM   5088 C CB  . TYR B 1 234 ? -5.882  6.551   -0.468  1   25.15  ? 234 TYR B CB  1 
ATOM   5089 C CG  . TYR B 1 234 ? -5.534  5.469   0.53    1   24.98  ? 234 TYR B CG  1 
ATOM   5090 C CD1 . TYR B 1 234 ? -4.395  4.683   0.38    1   24.53  ? 234 TYR B CD1 1 
ATOM   5091 C CD2 . TYR B 1 234 ? -6.303  5.283   1.689   1   25.06  ? 234 TYR B CD2 1 
ATOM   5092 C CE1 . TYR B 1 234 ? -4.112  3.67    1.272   1   25.46  ? 234 TYR B CE1 1 
ATOM   5093 C CE2 . TYR B 1 234 ? -5.975  4.333   2.623   1   26.77  ? 234 TYR B CE2 1 
ATOM   5094 C CZ  . TYR B 1 234 ? -4.885  3.522   2.414   1   27.65  ? 234 TYR B CZ  1 
ATOM   5095 O OH  . TYR B 1 234 ? -4.603  2.585   3.369   1   27.88  ? 234 TYR B OH  1 
ATOM   5096 N N   . LEU B 1 235 ? -5.672  9.551   -1.859  1   23.1   ? 235 LEU B N   1 
ATOM   5097 C CA  . LEU B 1 235 ? -5.705  10.415  -3.041  1   23.58  ? 235 LEU B CA  1 
ATOM   5098 C C   . LEU B 1 235 ? -4.318  11.026  -3.294  1   23.34  ? 235 LEU B C   1 
ATOM   5099 O O   . LEU B 1 235 ? -3.808  10.994  -4.426  1   23.9   ? 235 LEU B O   1 
ATOM   5100 C CB  . LEU B 1 235 ? -6.721  11.546  -2.892  1   23.78  ? 235 LEU B CB  1 
ATOM   5101 C CG  . LEU B 1 235 ? -6.985  12.403  -4.139  1   23.61  ? 235 LEU B CG  1 
ATOM   5102 C CD1 . LEU B 1 235 ? -7.844  11.66   -5.156  1   24.22  ? 235 LEU B CD1 1 
ATOM   5103 C CD2 . LEU B 1 235 ? -7.607  13.737  -3.704  1   24.1   ? 235 LEU B CD2 1 
ATOM   5104 N N   . THR B 1 236 ? -3.721  11.596  -2.24   1   21.9   ? 236 THR B N   1 
ATOM   5105 C CA  . THR B 1 236 ? -2.454  12.299  -2.365  1   21.83  ? 236 THR B CA  1 
ATOM   5106 C C   . THR B 1 236 ? -1.329  11.31   -2.688  1   23.18  ? 236 THR B C   1 
ATOM   5107 O O   . THR B 1 236 ? -0.468  11.607  -3.514  1   24.85  ? 236 THR B O   1 
ATOM   5108 C CB  . THR B 1 236 ? -2.19   13.099  -1.092  1   24.32  ? 236 THR B CB  1 
ATOM   5109 O OG1 . THR B 1 236 ? -3.336  13.88   -0.775  1   24.92  ? 236 THR B OG1 1 
ATOM   5110 C CG2 . THR B 1 236 ? -1.065  14.073  -1.306  1   25.28  ? 236 THR B CG2 1 
ATOM   5111 N N   . ILE B 1 237 ? -1.356  10.096  -2.105  1   24.14  ? 237 ILE B N   1 
ATOM   5112 C CA  . ILE B 1 237 ? -0.36   9.081   -2.475  1   26.19  ? 237 ILE B CA  1 
ATOM   5113 C C   . ILE B 1 237 ? -0.494  8.735   -3.963  1   26.13  ? 237 ILE B C   1 
ATOM   5114 O O   . ILE B 1 237 ? 0.504   8.62    -4.677  1   28.34  ? 237 ILE B O   1 
ATOM   5115 C CB  . ILE B 1 237 ? -0.46   7.838   -1.584  1   27.05  ? 237 ILE B CB  1 
ATOM   5116 C CG1 . ILE B 1 237 ? -0.123  8.158   -0.089  1   28.43  ? 237 ILE B CG1 1 
ATOM   5117 C CG2 . ILE B 1 237 ? 0.432   6.696   -2.087  1   26.52  ? 237 ILE B CG2 1 
ATOM   5118 C CD1 . ILE B 1 237 ? -0.449  6.986   0.839   1   28.54  ? 237 ILE B CD1 1 
ATOM   5119 N N   . GLY B 1 238 ? -1.731  8.522   -4.426  1   25.82  ? 238 GLY B N   1 
ATOM   5120 C CA  . GLY B 1 238 ? -1.99   8.241   -5.845  1   24.66  ? 238 GLY B CA  1 
ATOM   5121 C C   . GLY B 1 238 ? -1.402  9.328   -6.758  1   24.23  ? 238 GLY B C   1 
ATOM   5122 O O   . GLY B 1 238 ? -0.731  9.05    -7.756  1   27.22  ? 238 GLY B O   1 
ATOM   5123 N N   . THR B 1 239 ? -1.655  10.591  -6.419  1   24.5   ? 239 THR B N   1 
ATOM   5124 C CA  . THR B 1 239 ? -1.12   11.707  -7.205  1   26.38  ? 239 THR B CA  1 
ATOM   5125 C C   . THR B 1 239 ? 0.411   11.769  -7.195  1   29.27  ? 239 THR B C   1 
ATOM   5126 O O   . THR B 1 239 ? 1.014   12.162  -8.209  1   28.46  ? 239 THR B O   1 
ATOM   5127 C CB  . THR B 1 239 ? -1.701  13.014  -6.7    1   24.61  ? 239 THR B CB  1 
ATOM   5128 O OG1 . THR B 1 239 ? -3.096  12.837  -6.803  1   26.27  ? 239 THR B OG1 1 
ATOM   5129 C CG2 . THR B 1 239 ? -1.365  14.203  -7.573  1   25.54  ? 239 THR B CG2 1 
ATOM   5130 N N   . SER B 1 240 ? 1.041   11.331  -6.08   1   25.82  ? 240 SER B N   1 
ATOM   5131 C CA  . SER B 1 240 ? 2.481   11.301  -5.985  1   25.26  ? 240 SER B CA  1 
ATOM   5132 C C   . SER B 1 240 ? 3.095   10.38   -7.038  1   27.13  ? 240 SER B C   1 
ATOM   5133 O O   . SER B 1 240 ? 4.257   10.527  -7.336  1   27.45  ? 240 SER B O   1 
ATOM   5134 C CB  . SER B 1 240 ? 2.957   10.959  -4.582  1   26.61  ? 240 SER B CB  1 
ATOM   5135 O OG  . SER B 1 240 ? 3.02    9.562   -4.384  1   24.98  ? 240 SER B OG  1 
ATOM   5136 N N   . TYR B 1 241 ? 2.345   9.423   -7.567  1   26.33  ? 241 TYR B N   1 
ATOM   5137 C CA  . TYR B 1 241 ? 2.863   8.497   -8.574  1   29.29  ? 241 TYR B CA  1 
ATOM   5138 C C   . TYR B 1 241 ? 2.378   8.787   -10.004 1   29.14  ? 241 TYR B C   1 
ATOM   5139 O O   . TYR B 1 241 ? 2.723   8.037   -10.925 1   29.95  ? 241 TYR B O   1 
ATOM   5140 C CB  . TYR B 1 241 ? 2.37    7.1     -8.191  1   27.77  ? 241 TYR B CB  1 
ATOM   5141 C CG  . TYR B 1 241 ? 3.092   6.447   -7.043  1   27.65  ? 241 TYR B CG  1 
ATOM   5142 C CD1 . TYR B 1 241 ? 4.437   6.132   -7.162  1   33.84  ? 241 TYR B CD1 1 
ATOM   5143 C CD2 . TYR B 1 241 ? 2.446   6.169   -5.839  1   30.83  ? 241 TYR B CD2 1 
ATOM   5144 C CE1 . TYR B 1 241 ? 5.129   5.546   -6.114  1   34.78  ? 241 TYR B CE1 1 
ATOM   5145 C CE2 . TYR B 1 241 ? 3.12    5.544   -4.791  1   31.87  ? 241 TYR B CE2 1 
ATOM   5146 C CZ  . TYR B 1 241 ? 4.46    5.219   -4.94   1   33.8   ? 241 TYR B CZ  1 
ATOM   5147 O OH  . TYR B 1 241 ? 5.14    4.58    -3.937  1   32     ? 241 TYR B OH  1 
ATOM   5148 N N   . ILE B 1 242 ? 1.558   9.825   -10.176 1   28.89  ? 242 ILE B N   1 
ATOM   5149 C CA  . ILE B 1 242 ? 0.801   10.066  -11.395 1   34.39  ? 242 ILE B CA  1 
ATOM   5150 C C   . ILE B 1 242 ? 1.73    10.238  -12.61  1   35.47  ? 242 ILE B C   1 
ATOM   5151 O O   . ILE B 1 242 ? 1.371   9.776   -13.71  1   36.55  ? 242 ILE B O   1 
ATOM   5152 C CB  . ILE B 1 242 ? -0.186  11.249  -11.162 1   35.6   ? 242 ILE B CB  1 
ATOM   5153 C CG1 . ILE B 1 242 ? -1.457  11.066  -11.967 1   41.81  ? 242 ILE B CG1 1 
ATOM   5154 C CG2 . ILE B 1 242 ? 0.472   12.622  -11.406 1   36.94  ? 242 ILE B CG2 1 
ATOM   5155 C CD1 . ILE B 1 242 ? -2.548  12.058  -11.632 1   45.35  ? 242 ILE B CD1 1 
ATOM   5156 N N   . PHE B 1 243 ? 2.952   10.769  -12.405 1   34.77  ? 243 PHE B N   1 
ATOM   5157 C CA  . PHE B 1 243 ? 3.908   11.014  -13.48  1   39.38  ? 243 PHE B CA  1 
ATOM   5158 C C   . PHE B 1 243 ? 4.958   9.929   -13.543 1   44.74  ? 243 PHE B C   1 
ATOM   5159 O O   . PHE B 1 243 ? 5.67    9.907   -14.537 1   48.5   ? 243 PHE B O   1 
ATOM   5160 C CB  . PHE B 1 243 ? 4.591   12.402  -13.438 1   36.42  ? 243 PHE B CB  1 
ATOM   5161 C CG  . PHE B 1 243 ? 3.542   13.481  -13.604 1   36.27  ? 243 PHE B CG  1 
ATOM   5162 C CD1 . PHE B 1 243 ? 2.728   13.512  -14.727 1   35.12  ? 243 PHE B CD1 1 
ATOM   5163 C CD2 . PHE B 1 243 ? 3.27    14.394  -12.59  1   41.82  ? 243 PHE B CD2 1 
ATOM   5164 C CE1 . PHE B 1 243 ? 1.715   14.442  -14.864 1   34.83  ? 243 PHE B CE1 1 
ATOM   5165 C CE2 . PHE B 1 243 ? 2.233   15.308  -12.712 1   40.72  ? 243 PHE B CE2 1 
ATOM   5166 C CZ  . PHE B 1 243 ? 1.462   15.34   -13.861 1   43.73  ? 243 PHE B CZ  1 
ATOM   5167 N N   . SER B 1 244 ? 5.041   9.033   -12.544 1   40.05  ? 244 SER B N   1 
ATOM   5168 C CA  . SER B 1 244 ? 6.187   8.138   -12.43  1   39.45  ? 244 SER B CA  1 
ATOM   5169 C C   . SER B 1 244 ? 5.802   6.654   -12.44  1   44.28  ? 244 SER B C   1 
ATOM   5170 O O   . SER B 1 244 ? 6.637   5.842   -12.804 1   42.75  ? 244 SER B O   1 
ATOM   5171 C CB  . SER B 1 244 ? 7.015   8.457   -11.211 1   41.12  ? 244 SER B CB  1 
ATOM   5172 O OG  . SER B 1 244 ? 6.226   8.451   -10.022 1   45.09  ? 244 SER B OG  1 
ATOM   5173 N N   . ASP B 1 245 ? 4.6     6.259   -11.985 1   35.66  ? 245 ASP B N   1 
ATOM   5174 C CA  . ASP B 1 245 ? 4.282   4.842   -11.857 1   33.66  ? 245 ASP B CA  1 
ATOM   5175 C C   . ASP B 1 245 ? 2.782   4.631   -11.97  1   31.62  ? 245 ASP B C   1 
ATOM   5176 O O   . ASP B 1 245 ? 2.045   4.783   -10.982 1   30.78  ? 245 ASP B O   1 
ATOM   5177 C CB  . ASP B 1 245 ? 4.838   4.259   -10.571 1   35.53  ? 245 ASP B CB  1 
ATOM   5178 C CG  . ASP B 1 245 ? 4.763   2.739   -10.417 1   39.77  ? 245 ASP B CG  1 
ATOM   5179 O OD1 . ASP B 1 245 ? 3.804   2.109   -10.91  1   38.75  ? 245 ASP B OD1 1 
ATOM   5180 O OD2 . ASP B 1 245 ? 5.625   2.21    -9.707  1   44.79  ? 245 ASP B OD2 1 
ATOM   5181 N N   . PHE B 1 246 ? 2.355   4.257   -13.174 1   29.41  ? 246 PHE B N   1 
ATOM   5182 C CA  . PHE B 1 246 ? 0.948   4.125   -13.497 1   29.44  ? 246 PHE B CA  1 
ATOM   5183 C C   . PHE B 1 246 ? 0.297   3.153   -12.518 1   29.45  ? 246 PHE B C   1 
ATOM   5184 O O   . PHE B 1 246 ? -0.751  3.461   -11.994 1   29.89  ? 246 PHE B O   1 
ATOM   5185 C CB  . PHE B 1 246 ? 0.729   3.652   -14.942 1   30.82  ? 246 PHE B CB  1 
ATOM   5186 C CG  . PHE B 1 246 ? -0.727  3.374   -15.256 1   31.73  ? 246 PHE B CG  1 
ATOM   5187 C CD1 . PHE B 1 246 ? -1.57   4.41    -15.651 1   31.55  ? 246 PHE B CD1 1 
ATOM   5188 C CD2 . PHE B 1 246 ? -1.256  2.083   -15.163 1   35.07  ? 246 PHE B CD2 1 
ATOM   5189 C CE1 . PHE B 1 246 ? -2.911  4.147   -15.924 1   32.3   ? 246 PHE B CE1 1 
ATOM   5190 C CE2 . PHE B 1 246 ? -2.605  1.828   -15.412 1   35.9   ? 246 PHE B CE2 1 
ATOM   5191 C CZ  . PHE B 1 246 ? -3.436  2.857   -15.793 1   36.65  ? 246 PHE B CZ  1 
ATOM   5192 N N   . ASN B 1 247 ? 0.897   1.978   -12.328 1   31.04  ? 247 ASN B N   1 
ATOM   5193 C CA  . ASN B 1 247 ? 0.287   0.927   -11.524 1   32.77  ? 247 ASN B CA  1 
ATOM   5194 C C   . ASN B 1 247 ? 0.075   1.367   -10.072 1   29.55  ? 247 ASN B C   1 
ATOM   5195 O O   . ASN B 1 247 ? -0.996  1.106   -9.519  1   29.26  ? 247 ASN B O   1 
ATOM   5196 C CB  . ASN B 1 247 ? 1.068   -0.377  -11.598 1   36.91  ? 247 ASN B CB  1 
ATOM   5197 C CG  . ASN B 1 247 ? 0.752   -1.194  -12.833 1   46.22  ? 247 ASN B CG  1 
ATOM   5198 O OD1 . ASN B 1 247 ? -0.198  -0.933  -13.578 1   46.55  ? 247 ASN B OD1 1 
ATOM   5199 N ND2 . ASN B 1 247 ? 1.508   -2.254  -13.02  1   52.09  ? 247 ASN B ND2 1 
ATOM   5200 N N   . LEU B 1 248 ? 1.063   2.051   -9.473  1   29.47  ? 248 LEU B N   1 
ATOM   5201 C CA  . LEU B 1 248 ? 0.937   2.423   -8.065  1   29.66  ? 248 LEU B CA  1 
ATOM   5202 C C   . LEU B 1 248 ? -0.009  3.612   -7.928  1   29.8   ? 248 LEU B C   1 
ATOM   5203 O O   . LEU B 1 248 ? -0.7    3.749   -6.922  1   27.77  ? 248 LEU B O   1 
ATOM   5204 C CB  . LEU B 1 248 ? 2.3     2.685   -7.435  1   29.66  ? 248 LEU B CB  1 
ATOM   5205 C CG  . LEU B 1 248 ? 3.214   1.465   -7.23   1   33.24  ? 248 LEU B CG  1 
ATOM   5206 C CD1 . LEU B 1 248 ? 4.487   1.868   -6.539  1   31.37  ? 248 LEU B CD1 1 
ATOM   5207 C CD2 . LEU B 1 248 ? 2.54    0.326   -6.493  1   37.21  ? 248 LEU B CD2 1 
ATOM   5208 N N   . SER B 1 249 ? -0.019  4.52    -8.912  1   28.68  ? 249 SER B N   1 
ATOM   5209 C CA  . SER B 1 249 ? -0.975  5.618   -8.942  1   25.51  ? 249 SER B CA  1 
ATOM   5210 C C   . SER B 1 249 ? -2.398  5.068   -8.926  1   25.4   ? 249 SER B C   1 
ATOM   5211 O O   . SER B 1 249 ? -3.213  5.4     -8.055  1   24.87  ? 249 SER B O   1 
ATOM   5212 C CB  . SER B 1 249 ? -0.726  6.54    -10.153 1   24.74  ? 249 SER B CB  1 
ATOM   5213 O OG  . SER B 1 249 ? -1.574  7.675   -10.048 1   25.23  ? 249 SER B OG  1 
ATOM   5214 N N   . LYS B 1 250 ? -2.68   4.191   -9.884  1   25.41  ? 250 LYS B N   1 
ATOM   5215 C CA  . LYS B 1 250 ? -3.998  3.615   -10.052 1   28.09  ? 250 LYS B CA  1 
ATOM   5216 C C   . LYS B 1 250 ? -4.381  2.835   -8.797  1   28.22  ? 250 LYS B C   1 
ATOM   5217 O O   . LYS B 1 250 ? -5.518  2.913   -8.364  1   29.67  ? 250 LYS B O   1 
ATOM   5218 C CB  . LYS B 1 250 ? -3.99   2.686   -11.273 1   27.67  ? 250 LYS B CB  1 
ATOM   5219 C CG  . LYS B 1 250 ? -5.216  1.842   -11.473 1   32.53  ? 250 LYS B CG  1 
ATOM   5220 C CD  . LYS B 1 250 ? -5.156  0.886   -12.675 1   36.17  ? 250 LYS B CD  1 
ATOM   5221 C CE  . LYS B 1 250 ? -5.362  -0.562  -12.275 1   43.38  ? 250 LYS B CE  1 
ATOM   5222 N NZ  . LYS B 1 250 ? -6.146  -1.444  -13.143 1   53.5   ? 250 LYS B NZ  1 
ATOM   5223 N N   . GLN B 1 251 ? -3.452  2.029   -8.273  1   29.68  ? 251 GLN B N   1 
ATOM   5224 C CA  . GLN B 1 251 ? -3.742  1.206   -7.104  1   29.98  ? 251 GLN B CA  1 
ATOM   5225 C C   . GLN B 1 251 ? -4.226  2.062   -5.948  1   27.48  ? 251 GLN B C   1 
ATOM   5226 O O   . GLN B 1 251 ? -5.21   1.7     -5.296  1   28.26  ? 251 GLN B O   1 
ATOM   5227 C CB  . GLN B 1 251 ? -2.532  0.368   -6.706  1   32.89  ? 251 GLN B CB  1 
ATOM   5228 C CG  . GLN B 1 251 ? -2.847  -0.642  -5.597  1   44.46  ? 251 GLN B CG  1 
ATOM   5229 C CD  . GLN B 1 251 ? -1.652  -1.387  -5.008  1   44.27  ? 251 GLN B CD  1 
ATOM   5230 O OE1 . GLN B 1 251 ? -0.525  -1.309  -5.519  1   42.89  ? 251 GLN B OE1 1 
ATOM   5231 N NE2 . GLN B 1 251 ? -1.9    -2.091  -3.906  1   38.22  ? 251 GLN B NE2 1 
ATOM   5232 N N   . ASN B 1 252 ? -3.467  3.124   -5.631  1   27.45  ? 252 ASN B N   1 
ATOM   5233 C CA  . ASN B 1 252 ? -3.808  4.013   -4.535  1   27.08  ? 252 ASN B CA  1 
ATOM   5234 C C   . ASN B 1 252 ? -5.128  4.748   -4.774  1   27.41  ? 252 ASN B C   1 
ATOM   5235 O O   . ASN B 1 252 ? -5.882  4.962   -3.821  1   24.62  ? 252 ASN B O   1 
ATOM   5236 C CB  . ASN B 1 252 ? -2.665  4.984   -4.221  1   25.72  ? 252 ASN B CB  1 
ATOM   5237 C CG  . ASN B 1 252 ? -1.622  4.235   -3.433  1   28.79  ? 252 ASN B CG  1 
ATOM   5238 O OD1 . ASN B 1 252 ? -1.769  4.07    -2.223  1   27.51  ? 252 ASN B OD1 1 
ATOM   5239 N ND2 . ASN B 1 252 ? -0.577  3.78    -4.084  1   28.03  ? 252 ASN B ND2 1 
ATOM   5240 N N   . TYR B 1 253 ? -5.406  5.155   -6.026  1   25.1   ? 253 TYR B N   1 
ATOM   5241 C CA  . TYR B 1 253 ? -6.691  5.751   -6.336  1   26.73  ? 253 TYR B CA  1 
ATOM   5242 C C   . TYR B 1 253 ? -7.844  4.752   -6.16   1   26.55  ? 253 TYR B C   1 
ATOM   5243 O O   . TYR B 1 253 ? -8.888  5.148   -5.661  1   26.82  ? 253 TYR B O   1 
ATOM   5244 C CB  . TYR B 1 253 ? -6.723  6.362   -7.745  1   26.21  ? 253 TYR B CB  1 
ATOM   5245 C CG  . TYR B 1 253 ? -5.926  7.622   -7.98   1   24.54  ? 253 TYR B CG  1 
ATOM   5246 C CD1 . TYR B 1 253 ? -5.767  8.607   -7.01   1   25.01  ? 253 TYR B CD1 1 
ATOM   5247 C CD2 . TYR B 1 253 ? -5.292  7.832   -9.206  1   25.75  ? 253 TYR B CD2 1 
ATOM   5248 C CE1 . TYR B 1 253 ? -4.981  9.711   -7.235  1   26.13  ? 253 TYR B CE1 1 
ATOM   5249 C CE2 . TYR B 1 253 ? -4.532  8.954   -9.448  1   27.45  ? 253 TYR B CE2 1 
ATOM   5250 C CZ  . TYR B 1 253 ? -4.397  9.909   -8.473  1   25.78  ? 253 TYR B CZ  1 
ATOM   5251 O OH  . TYR B 1 253 ? -3.717  11.055  -8.712  1   26.47  ? 253 TYR B OH  1 
ATOM   5252 N N   . LEU B 1 254 ? -7.662  3.472   -6.514  1   26.94  ? 254 LEU B N   1 
ATOM   5253 C CA  . LEU B 1 254 ? -8.72   2.472   -6.392  1   28.18  ? 254 LEU B CA  1 
ATOM   5254 C C   . LEU B 1 254 ? -8.986  2.15    -4.919  1   30.41  ? 254 LEU B C   1 
ATOM   5255 O O   . LEU B 1 254 ? -10.149 1.901   -4.555  1   30.4   ? 254 LEU B O   1 
ATOM   5256 C CB  . LEU B 1 254 ? -8.447  1.205   -7.185  1   31.24  ? 254 LEU B CB  1 
ATOM   5257 C CG  . LEU B 1 254 ? -8.461  1.375   -8.712  1   35.54  ? 254 LEU B CG  1 
ATOM   5258 C CD1 . LEU B 1 254 ? -8.082  0.065   -9.399  1   38     ? 254 LEU B CD1 1 
ATOM   5259 C CD2 . LEU B 1 254 ? -9.792  1.936   -9.221  1   38.24  ? 254 LEU B CD2 1 
ATOM   5260 N N   . ILE B 1 255 ? -7.903  2.093   -4.11   1   28.85  ? 255 ILE B N   1 
ATOM   5261 C CA  . ILE B 1 255 ? -8.037  1.953   -2.659  1   29.44  ? 255 ILE B CA  1 
ATOM   5262 C C   . ILE B 1 255 ? -8.88   3.117   -2.141  1   26.5   ? 255 ILE B C   1 
ATOM   5263 O O   . ILE B 1 255 ? -9.852  2.928   -1.431  1   28.58  ? 255 ILE B O   1 
ATOM   5264 C CB  . ILE B 1 255 ? -6.668  1.886   -1.943  1   30.97  ? 255 ILE B CB  1 
ATOM   5265 C CG1 . ILE B 1 255 ? -5.903  0.608   -2.273  1   30.75  ? 255 ILE B CG1 1 
ATOM   5266 C CG2 . ILE B 1 255 ? -6.822  2.039   -0.416  1   28.62  ? 255 ILE B CG2 1 
ATOM   5267 C CD1 . ILE B 1 255 ? -4.395  0.691   -1.97   1   30.96  ? 255 ILE B CD1 1 
ATOM   5268 N N   . GLY B 1 256 ? -8.444  4.337   -2.42   1   27.46  ? 256 GLY B N   1 
ATOM   5269 C CA  . GLY B 1 256 ? -9.119  5.503   -1.911  1   28.4   ? 256 GLY B CA  1 
ATOM   5270 C C   . GLY B 1 256 ? -10.596 5.545   -2.311  1   30.45  ? 256 GLY B C   1 
ATOM   5271 O O   . GLY B 1 256 ? -11.453 5.927   -1.49   1   29.66  ? 256 GLY B O   1 
ATOM   5272 N N   . LEU B 1 257 ? -10.884 5.202   -3.582  1   28.97  ? 257 LEU B N   1 
ATOM   5273 C CA  . LEU B 1 257 ? -12.251 5.108   -4.075  1   31.18  ? 257 LEU B CA  1 
ATOM   5274 C C   . LEU B 1 257 ? -13.084 4.114   -3.256  1   32.13  ? 257 LEU B C   1 
ATOM   5275 O O   . LEU B 1 257 ? -14.221 4.406   -2.919  1   33.38  ? 257 LEU B O   1 
ATOM   5276 C CB  . LEU B 1 257 ? -12.182 4.758   -5.558  1   32.5   ? 257 LEU B CB  1 
ATOM   5277 C CG  . LEU B 1 257 ? -13.503 4.682   -6.316  1   38.21  ? 257 LEU B CG  1 
ATOM   5278 C CD1 . LEU B 1 257 ? -14.296 5.975   -6.178  1   35.06  ? 257 LEU B CD1 1 
ATOM   5279 C CD2 . LEU B 1 257 ? -13.182 4.388   -7.799  1   40.05  ? 257 LEU B CD2 1 
ATOM   5280 N N   . LYS B 1 258 ? -12.492 2.986   -2.853  1   30.59  ? 258 LYS B N   1 
ATOM   5281 C CA  . LYS B 1 258 ? -13.183 2.046   -1.992  1   31.26  ? 258 LYS B CA  1 
ATOM   5282 C C   . LYS B 1 258 ? -13.43  2.663   -0.608  1   30.83  ? 258 LYS B C   1 
ATOM   5283 O O   . LYS B 1 258 ? -14.51  2.456   -0.08   1   33.71  ? 258 LYS B O   1 
ATOM   5284 C CB  . LYS B 1 258 ? -12.469 0.7     -1.816  1   33.19  ? 258 LYS B CB  1 
ATOM   5285 C CG  . LYS B 1 258 ? -12.304 -0.175  -3.026  1   37.35  ? 258 LYS B CG  1 
ATOM   5286 C CD  . LYS B 1 258 ? -13.664 -0.575  -3.579  1   40.69  ? 258 LYS B CD  1 
ATOM   5287 C CE  . LYS B 1 258 ? -13.527 -1.434  -4.781  1   48.1   ? 258 LYS B CE  1 
ATOM   5288 N NZ  . LYS B 1 258 ? -14.829 -1.54   -5.423  1   50.68  ? 258 LYS B NZ  1 
ATOM   5289 N N   . PHE B 1 259 ? -12.485 3.422   -0.025  1   31.89  ? 259 PHE B N   1 
ATOM   5290 C CA  . PHE B 1 259 ? -12.737 4.176   1.206   1   31.73  ? 259 PHE B CA  1 
ATOM   5291 C C   . PHE B 1 259 ? -13.807 5.256   1.009   1   33.22  ? 259 PHE B C   1 
ATOM   5292 O O   . PHE B 1 259 ? -14.53  5.608   1.95    1   31.16  ? 259 PHE B O   1 
ATOM   5293 C CB  . PHE B 1 259 ? -11.485 4.842   1.79    1   29.96  ? 259 PHE B CB  1 
ATOM   5294 C CG  . PHE B 1 259 ? -10.635 3.845   2.55    1   30.25  ? 259 PHE B CG  1 
ATOM   5295 C CD1 . PHE B 1 259 ? -9.739  3.019   1.88    1   29.47  ? 259 PHE B CD1 1 
ATOM   5296 C CD2 . PHE B 1 259 ? -10.835 3.644   3.911   1   32.97  ? 259 PHE B CD2 1 
ATOM   5297 C CE1 . PHE B 1 259 ? -8.988  2.072   2.571   1   32.3   ? 259 PHE B CE1 1 
ATOM   5298 C CE2 . PHE B 1 259 ? -10.101 2.687   4.609   1   32.13  ? 259 PHE B CE2 1 
ATOM   5299 C CZ  . PHE B 1 259 ? -9.174  1.897   3.935   1   31.89  ? 259 PHE B CZ  1 
ATOM   5300 N N   . ALA B 1 260 ? -13.873 5.851   -0.19   1   30.11  ? 260 ALA B N   1 
ATOM   5301 C CA  . ALA B 1 260 ? -14.845 6.898   -0.456  1   30.7   ? 260 ALA B CA  1 
ATOM   5302 C C   . ALA B 1 260 ? -16.276 6.375   -0.657  1   35.36  ? 260 ALA B C   1 
ATOM   5303 O O   . ALA B 1 260 ? -17.18  7.191   -0.709  1   37.41  ? 260 ALA B O   1 
ATOM   5304 C CB  . ALA B 1 260 ? -14.412 7.683   -1.677  1   30.23  ? 260 ALA B CB  1 
ATOM   5305 N N   . LYS B 1 261 ? -16.477 5.07    -0.861  1   38.08  ? 261 LYS B N   1 
ATOM   5306 C CA  . LYS B 1 261 ? -17.727 4.489   -1.327  1   45.22  ? 261 LYS B CA  1 
ATOM   5307 C C   . LYS B 1 261 ? -18.927 5.033   -0.568  1   44.22  ? 261 LYS B C   1 
ATOM   5308 O O   . LYS B 1 261 ? -18.919 5.021   0.644   1   41.06  ? 261 LYS B O   1 
ATOM   5309 C CB  . LYS B 1 261 ? -17.732 2.972   -1.103  1   49.92  ? 261 LYS B CB  1 
ATOM   5310 C CG  . LYS B 1 261 ? -18.953 2.193   -1.6    1   57.94  ? 261 LYS B CG  1 
ATOM   5311 C CD  . LYS B 1 261 ? -19.064 2.176   -3.117  1   64.49  ? 261 LYS B CD  1 
ATOM   5312 C CE  . LYS B 1 261 ? -20.294 1.44    -3.549  1   71.82  ? 261 LYS B CE  1 
ATOM   5313 N NZ  . LYS B 1 261 ? -20.201 1.192   -4.991  1   76.16  ? 261 LYS B NZ  1 
ATOM   5314 N N   . GLY B 1 262 ? -19.942 5.488   -1.316  1   48.83  ? 262 GLY B N   1 
ATOM   5315 C CA  . GLY B 1 262 ? -21.161 6.038   -0.749  1   50.68  ? 262 GLY B CA  1 
ATOM   5316 C C   . GLY B 1 262 ? -21.092 7.51    -0.349  1   49.42  ? 262 GLY B C   1 
ATOM   5317 O O   . GLY B 1 262 ? -21.982 7.969   0.339   1   53.08  ? 262 GLY B O   1 
ATOM   5318 N N   . ASN B 1 263 ? -20.006 8.219   -0.676  1   46.96  ? 263 ASN B N   1 
ATOM   5319 C CA  . ASN B 1 263 ? -19.921 9.665   -0.523  1   44.97  ? 263 ASN B CA  1 
ATOM   5320 C C   . ASN B 1 263 ? -19.52  10.2    -1.9    1   46.22  ? 263 ASN B C   1 
ATOM   5321 O O   . ASN B 1 263 ? -18.346 10.119  -2.272  1   38.14  ? 263 ASN B O   1 
ATOM   5322 C CB  . ASN B 1 263 ? -18.93  10.081  0.552   1   42.36  ? 263 ASN B CB  1 
ATOM   5323 C CG  . ASN B 1 263 ? -18.876 11.57   0.755   1   45.49  ? 263 ASN B CG  1 
ATOM   5324 O OD1 . ASN B 1 263 ? -18.665 12.342  -0.19   1   47.26  ? 263 ASN B OD1 1 
ATOM   5325 N ND2 . ASN B 1 263 ? -19.008 11.996  2.005   1   46.63  ? 263 ASN B ND2 1 
ATOM   5326 N N   . PRO B 1 264 ? -20.48  10.691  -2.712  1   47.06  ? 264 PRO B N   1 
ATOM   5327 C CA  . PRO B 1 264 ? -20.177 11.136  -4.071  1   45.04  ? 264 PRO B CA  1 
ATOM   5328 C C   . PRO B 1 264 ? -19.099 12.2    -4.197  1   38.84  ? 264 PRO B C   1 
ATOM   5329 O O   . PRO B 1 264 ? -18.368 12.17   -5.172  1   36.73  ? 264 PRO B O   1 
ATOM   5330 C CB  . PRO B 1 264 ? -21.536 11.651  -4.554  1   47.81  ? 264 PRO B CB  1 
ATOM   5331 C CG  . PRO B 1 264 ? -22.501 10.745  -3.842  1   50.94  ? 264 PRO B CG  1 
ATOM   5332 C CD  . PRO B 1 264 ? -21.934 10.753  -2.428  1   50.29  ? 264 PRO B CD  1 
ATOM   5333 N N   . GLY B 1 265 ? -19.044 13.149  -3.249  1   37.11  ? 265 GLY B N   1 
ATOM   5334 C CA  . GLY B 1 265 ? -17.999 14.155  -3.214  1   36.97  ? 265 GLY B CA  1 
ATOM   5335 C C   . GLY B 1 265 ? -16.596 13.536  -3.15   1   35.62  ? 265 GLY B C   1 
ATOM   5336 O O   . GLY B 1 265 ? -15.701 13.918  -3.914  1   32.61  ? 265 GLY B O   1 
ATOM   5337 N N   . PHE B 1 266 ? -16.414 12.592  -2.219  1   34.58  ? 266 PHE B N   1 
ATOM   5338 C CA  . PHE B 1 266 ? -15.144 11.898  -2.064  1   34.4   ? 266 PHE B CA  1 
ATOM   5339 C C   . PHE B 1 266 ? -14.854 11.063  -3.317  1   31.5   ? 266 PHE B C   1 
ATOM   5340 O O   . PHE B 1 266 ? -13.736 11.103  -3.826  1   33.65  ? 266 PHE B O   1 
ATOM   5341 C CB  . PHE B 1 266 ? -15.107 11.045  -0.792  1   30.74  ? 266 PHE B CB  1 
ATOM   5342 C CG  . PHE B 1 266 ? -15.142 11.78   0.544   1   31.95  ? 266 PHE B CG  1 
ATOM   5343 C CD1 . PHE B 1 266 ? -14.792 13.119  0.673   1   33.15  ? 266 PHE B CD1 1 
ATOM   5344 C CD2 . PHE B 1 266 ? -15.576 11.117  1.69    1   34.34  ? 266 PHE B CD2 1 
ATOM   5345 C CE1 . PHE B 1 266 ? -14.829 13.756  1.91    1   34.29  ? 266 PHE B CE1 1 
ATOM   5346 C CE2 . PHE B 1 266 ? -15.637 11.765  2.925   1   34.38  ? 266 PHE B CE2 1 
ATOM   5347 C CZ  . PHE B 1 266 ? -15.264 13.082  3.032   1   33.34  ? 266 PHE B CZ  1 
ATOM   5348 N N   . GLU B 1 267 ? -15.853 10.358  -3.836  1   30.75  ? 267 GLU B N   1 
ATOM   5349 C CA  . GLU B 1 267 ? -15.63  9.49    -4.978  1   32.83  ? 267 GLU B CA  1 
ATOM   5350 C C   . GLU B 1 267 ? -15.158 10.281  -6.193  1   31.35  ? 267 GLU B C   1 
ATOM   5351 O O   . GLU B 1 267 ? -14.309 9.817   -6.937  1   29.41  ? 267 GLU B O   1 
ATOM   5352 C CB  . GLU B 1 267 ? -16.883 8.699   -5.33   1   35.05  ? 267 GLU B CB  1 
ATOM   5353 C CG  . GLU B 1 267 ? -17.256 7.664   -4.272  1   35.68  ? 267 GLU B CG  1 
ATOM   5354 C CD  . GLU B 1 267 ? -18.604 7.002   -4.569  1   43.78  ? 267 GLU B CD  1 
ATOM   5355 O OE1 . GLU B 1 267 ? -18.74  5.797   -4.389  1   49.68  ? 267 GLU B OE1 1 
ATOM   5356 O OE2 . GLU B 1 267 ? -19.548 7.664   -5.005  1   54.86  ? 267 GLU B OE2 1 
ATOM   5357 N N   . GLU B 1 268 ? -15.706 11.478  -6.362  1   31.81  ? 268 GLU B N   1 
ATOM   5358 C CA  . GLU B 1 268 ? -15.374 12.331  -7.488  1   34.62  ? 268 GLU B CA  1 
ATOM   5359 C C   . GLU B 1 268 ? -13.886 12.712  -7.592  1   31.9   ? 268 GLU B C   1 
ATOM   5360 O O   . GLU B 1 268 ? -13.388 12.882  -8.7    1   29.57  ? 268 GLU B O   1 
ATOM   5361 C CB  . GLU B 1 268 ? -16.285 13.551  -7.376  1   34.48  ? 268 GLU B CB  1 
ATOM   5362 C CG  . GLU B 1 268 ? -16.046 14.578  -8.472  1   34.87  ? 268 GLU B CG  1 
ATOM   5363 C CD  . GLU B 1 268 ? -17.018 15.719  -8.357  1   41.74  ? 268 GLU B CD  1 
ATOM   5364 O OE1 . GLU B 1 268 ? -17.743 15.986  -9.321  1   39.97  ? 268 GLU B OE1 1 
ATOM   5365 O OE2 . GLU B 1 268 ? -17.07  16.317  -7.27   1   40.03  ? 268 GLU B OE2 1 
ATOM   5366 N N   . PHE B 1 269 ? -13.182 12.941  -6.469  1   29.45  ? 269 PHE B N   1 
ATOM   5367 C CA  . PHE B 1 269 ? -11.756 13.203  -6.486  1   29.2   ? 269 PHE B CA  1 
ATOM   5368 C C   . PHE B 1 269 ? -11.041 12.065  -7.236  1   28.94  ? 269 PHE B C   1 
ATOM   5369 O O   . PHE B 1 269 ? -10.161 12.33   -8.031  1   26.7   ? 269 PHE B O   1 
ATOM   5370 C CB  . PHE B 1 269 ? -11.154 13.367  -5.085  1   29.18  ? 269 PHE B CB  1 
ATOM   5371 C CG  . PHE B 1 269 ? -11.515 14.706  -4.448  1   28.26  ? 269 PHE B CG  1 
ATOM   5372 C CD1 . PHE B 1 269 ? -12.654 14.824  -3.644  1   32.2   ? 269 PHE B CD1 1 
ATOM   5373 C CD2 . PHE B 1 269 ? -10.718 15.819  -4.613  1   29.5   ? 269 PHE B CD2 1 
ATOM   5374 C CE1 . PHE B 1 269 ? -13.011 16.043  -3.064  1   29.34  ? 269 PHE B CE1 1 
ATOM   5375 C CE2 . PHE B 1 269 ? -11.053 17.026  -3.986  1   28.43  ? 269 PHE B CE2 1 
ATOM   5376 C CZ  . PHE B 1 269 ? -12.22  17.135  -3.244  1   26.7   ? 269 PHE B CZ  1 
ATOM   5377 N N   . PHE B 1 270 ? -11.388 10.817  -6.933  1   25.46  ? 270 PHE B N   1 
ATOM   5378 C CA  . PHE B 1 270 ? -10.718 9.664   -7.539  1   27.24  ? 270 PHE B CA  1 
ATOM   5379 C C   . PHE B 1 270 ? -11.064 9.523   -9.015  1   29.24  ? 270 PHE B C   1 
ATOM   5380 O O   . PHE B 1 270 ? -10.19  9.241   -9.834  1   30.63  ? 270 PHE B O   1 
ATOM   5381 C CB  . PHE B 1 270 ? -11.041 8.375   -6.784  1   26.64  ? 270 PHE B CB  1 
ATOM   5382 C CG  . PHE B 1 270 ? -10.521 8.478   -5.366  1   27.74  ? 270 PHE B CG  1 
ATOM   5383 C CD1 . PHE B 1 270 ? -9.161  8.349   -5.102  1   26.87  ? 270 PHE B CD1 1 
ATOM   5384 C CD2 . PHE B 1 270 ? -11.373 8.817   -4.311  1   30.99  ? 270 PHE B CD2 1 
ATOM   5385 C CE1 . PHE B 1 270 ? -8.664  8.488   -3.808  1   26.27  ? 270 PHE B CE1 1 
ATOM   5386 C CE2 . PHE B 1 270 ? -10.869 8.966   -3.022  1   29.37  ? 270 PHE B CE2 1 
ATOM   5387 C CZ  . PHE B 1 270 ? -9.518  8.813   -2.774  1   28.89  ? 270 PHE B CZ  1 
ATOM   5388 N N   . LYS B 1 271 ? -12.343 9.696   -9.358  1   30.7   ? 271 LYS B N   1 
ATOM   5389 C CA  . LYS B 1 271 ? -12.754 9.606   -10.757 1   30.89  ? 271 LYS B CA  1 
ATOM   5390 C C   . LYS B 1 271 ? -12.029 10.652  -11.613 1   28.05  ? 271 LYS B C   1 
ATOM   5391 O O   . LYS B 1 271 ? -11.601 10.346  -12.714 1   29.35  ? 271 LYS B O   1 
ATOM   5392 C CB  . LYS B 1 271 ? -14.271 9.74    -10.857 1   35.23  ? 271 LYS B CB  1 
ATOM   5393 C CG  . LYS B 1 271 ? -15.028 8.545   -10.281 1   40.02  ? 271 LYS B CG  1 
ATOM   5394 C CD  . LYS B 1 271 ? -16.398 8.423   -10.925 1   48.89  ? 271 LYS B CD  1 
ATOM   5395 C CE  . LYS B 1 271 ? -17.226 7.338   -10.325 1   61.31  ? 271 LYS B CE  1 
ATOM   5396 N NZ  . LYS B 1 271 ? -17.684 7.727   -8.988  1   68.75  ? 271 LYS B NZ  1 
ATOM   5397 N N   . ARG B 1 272 ? -11.876 11.856  -11.068 1   28.9   ? 272 ARG B N   1 
ATOM   5398 C CA  . ARG B 1 272 ? -11.174 12.946  -11.744 1   28.86  ? 272 ARG B CA  1 
ATOM   5399 C C   . ARG B 1 272 ? -9.702  12.595  -11.953 1   28.77  ? 272 ARG B C   1 
ATOM   5400 O O   . ARG B 1 272 ? -9.181  12.78   -13.044 1   26.22  ? 272 ARG B O   1 
ATOM   5401 C CB  . ARG B 1 272 ? -11.345 14.228  -10.921 1   30.78  ? 272 ARG B CB  1 
ATOM   5402 C CG  . ARG B 1 272 ? -12.706 14.855  -11.159 1   32.71  ? 272 ARG B CG  1 
ATOM   5403 C CD  . ARG B 1 272 ? -13.019 16.069  -10.335 1   31.42  ? 272 ARG B CD  1 
ATOM   5404 N NE  . ARG B 1 272 ? -14.248 16.716  -10.828 1   31.21  ? 272 ARG B NE  1 
ATOM   5405 C CZ  . ARG B 1 272 ? -14.777 17.8    -10.277 1   31     ? 272 ARG B CZ  1 
ATOM   5406 N NH1 . ARG B 1 272 ? -14.4   18.189  -9.069  1   32.35  ? 272 ARG B NH1 1 
ATOM   5407 N NH2 . ARG B 1 272 ? -15.726 18.452  -10.891 1   32.61  ? 272 ARG B NH2 1 
ATOM   5408 N N   . ASN B 1 273 ? -9.012  12.121  -10.899 1   25.79  ? 273 ASN B N   1 
ATOM   5409 C CA  . ASN B 1 273 ? -7.603  11.826  -11.05  1   26.39  ? 273 ASN B CA  1 
ATOM   5410 C C   . ASN B 1 273 ? -7.361  10.568  -11.873 1   24.33  ? 273 ASN B C   1 
ATOM   5411 O O   . ASN B 1 273 ? -6.351  10.522  -12.574 1   24.45  ? 273 ASN B O   1 
ATOM   5412 C CB  . ASN B 1 273 ? -6.86   11.819  -9.717  1   24.63  ? 273 ASN B CB  1 
ATOM   5413 C CG  . ASN B 1 273 ? -6.658  13.208  -9.171  1   26.9   ? 273 ASN B CG  1 
ATOM   5414 O OD1 . ASN B 1 273 ? -6.861  14.217  -9.881  1   26.46  ? 273 ASN B OD1 1 
ATOM   5415 N ND2 . ASN B 1 273 ? -6.288  13.301  -7.899  1   26.22  ? 273 ASN B ND2 1 
ATOM   5416 N N   . LEU B 1 274 ? -8.248  9.559   -11.764 1   25.35  ? 274 LEU B N   1 
ATOM   5417 C CA  . LEU B 1 274 ? -8.18   8.423   -12.669 1   26.73  ? 274 LEU B CA  1 
ATOM   5418 C C   . LEU B 1 274 ? -8.371  8.838   -14.134 1   29.25  ? 274 LEU B C   1 
ATOM   5419 O O   . LEU B 1 274 ? -7.711  8.26    -15.003 1   27.12  ? 274 LEU B O   1 
ATOM   5420 C CB  . LEU B 1 274 ? -9.159  7.357   -12.213 1   28.99  ? 274 LEU B CB  1 
ATOM   5421 C CG  . LEU B 1 274 ? -8.681  6.567   -10.978 1   28.14  ? 274 LEU B CG  1 
ATOM   5422 C CD1 . LEU B 1 274 ? -9.886  5.926   -10.313 1   32.29  ? 274 LEU B CD1 1 
ATOM   5423 C CD2 . LEU B 1 274 ? -7.688  5.478   -11.422 1   26.53  ? 274 LEU B CD2 1 
ATOM   5424 N N   . SER B 1 275 ? -9.279  9.799   -14.405 1   27.4   ? 275 SER B N   1 
ATOM   5425 C CA  . SER B 1 275 ? -9.464  10.332  -15.75  1   29.12  ? 275 SER B CA  1 
ATOM   5426 C C   . SER B 1 275 ? -8.136  10.896  -16.263 1   28.77  ? 275 SER B C   1 
ATOM   5427 O O   . SER B 1 275 ? -7.731  10.587  -17.385 1   28.26  ? 275 SER B O   1 
ATOM   5428 C CB  . SER B 1 275 ? -10.502 11.441  -15.797 1   28.3   ? 275 SER B CB  1 
ATOM   5429 O OG  . SER B 1 275 ? -11.782 10.916  -15.476 1   31.46  ? 275 SER B OG  1 
ATOM   5430 N N   . PHE B 1 276 ? -7.517  11.757  -15.436 1   27.7   ? 276 PHE B N   1 
ATOM   5431 C CA  . PHE B 1 276 ? -6.269  12.399  -15.783 1   28.19  ? 276 PHE B CA  1 
ATOM   5432 C C   . PHE B 1 276 ? -5.187  11.348  -15.985 1   29     ? 276 PHE B C   1 
ATOM   5433 O O   . PHE B 1 276 ? -4.473  11.387  -16.967 1   25.59  ? 276 PHE B O   1 
ATOM   5434 C CB  . PHE B 1 276 ? -5.852  13.442  -14.754 1   30.29  ? 276 PHE B CB  1 
ATOM   5435 C CG  . PHE B 1 276 ? -4.551  14.117  -15.166 1   31.03  ? 276 PHE B CG  1 
ATOM   5436 C CD1 . PHE B 1 276 ? -4.558  15.159  -16.084 1   32.83  ? 276 PHE B CD1 1 
ATOM   5437 C CD2 . PHE B 1 276 ? -3.326  13.595  -14.734 1   30.06  ? 276 PHE B CD2 1 
ATOM   5438 C CE1 . PHE B 1 276 ? -3.358  15.731  -16.506 1   33.32  ? 276 PHE B CE1 1 
ATOM   5439 C CE2 . PHE B 1 276 ? -2.145  14.138  -15.179 1   33.24  ? 276 PHE B CE2 1 
ATOM   5440 C CZ  . PHE B 1 276 ? -2.165  15.222  -16.054 1   32.84  ? 276 PHE B CZ  1 
ATOM   5441 N N   . LEU B 1 277 ? -5.05   10.403  -15.045 1   26.98  ? 277 LEU B N   1 
ATOM   5442 C CA  . LEU B 1 277 ? -3.996  9.405   -15.135 1   27.32  ? 277 LEU B CA  1 
ATOM   5443 C C   . LEU B 1 277 ? -4.097  8.638   -16.448 1   26.26  ? 277 LEU B C   1 
ATOM   5444 O O   . LEU B 1 277 ? -3.117  8.491   -17.155 1   29.04  ? 277 LEU B O   1 
ATOM   5445 C CB  . LEU B 1 277 ? -4.132  8.468   -13.93  1   27.32  ? 277 LEU B CB  1 
ATOM   5446 C CG  . LEU B 1 277 ? -3.138  7.305   -13.895 1   30.24  ? 277 LEU B CG  1 
ATOM   5447 C CD1 . LEU B 1 277 ? -1.732  7.774   -13.585 1   30.2   ? 277 LEU B CD1 1 
ATOM   5448 C CD2 . LEU B 1 277 ? -3.565  6.227   -12.917 1   32.51  ? 277 LEU B CD2 1 
ATOM   5449 N N   . ASN B 1 278 ? -5.285  8.119   -16.769 1   27.33  ? 278 ASN B N   1 
ATOM   5450 C CA  . ASN B 1 278 ? -5.493  7.359   -17.994 1   29.89  ? 278 ASN B CA  1 
ATOM   5451 C C   . ASN B 1 278 ? -5.235  8.22    -19.252 1   30.18  ? 278 ASN B C   1 
ATOM   5452 O O   . ASN B 1 278 ? -4.596  7.749   -20.213 1   28.82  ? 278 ASN B O   1 
ATOM   5453 C CB  . ASN B 1 278 ? -6.841  6.654   -17.975 1   31.16  ? 278 ASN B CB  1 
ATOM   5454 C CG  . ASN B 1 278 ? -6.793  5.405   -17.115 1   33.91  ? 278 ASN B CG  1 
ATOM   5455 O OD1 . ASN B 1 278 ? -6.168  4.43    -17.55  1   32     ? 278 ASN B OD1 1 
ATOM   5456 N ND2 . ASN B 1 278 ? -7.335  5.44    -15.896 1   30.3   ? 278 ASN B ND2 1 
ATOM   5457 N N   . ASN B 1 279 ? -5.654  9.486   -19.22  1   30.67  ? 279 ASN B N   1 
ATOM   5458 C CA  . ASN B 1 279 ? -5.375  10.364  -20.355 1   30.35  ? 279 ASN B CA  1 
ATOM   5459 C C   . ASN B 1 279 ? -3.867  10.582  -20.513 1   29.84  ? 279 ASN B C   1 
ATOM   5460 O O   . ASN B 1 279 ? -3.344  10.469  -21.631 1   29.93  ? 279 ASN B O   1 
ATOM   5461 C CB  . ASN B 1 279 ? -6.14   11.67   -20.261 1   28.88  ? 279 ASN B CB  1 
ATOM   5462 C CG  . ASN B 1 279 ? -7.6    11.58   -20.593 1   28.73  ? 279 ASN B CG  1 
ATOM   5463 O OD1 . ASN B 1 279 ? -8.025  10.694  -21.341 1   30.6   ? 279 ASN B OD1 1 
ATOM   5464 N ND2 . ASN B 1 279 ? -8.386  12.523  -20.088 1   29.14  ? 279 ASN B ND2 1 
ATOM   5465 N N   . PHE B 1 280 ? -3.174  10.893  -19.408 1   27.28  ? 280 PHE B N   1 
ATOM   5466 C CA  . PHE B 1 280 ? -1.757  11.221  -19.439 1   29.36  ? 280 PHE B CA  1 
ATOM   5467 C C   . PHE B 1 280 ? -0.944  10.018  -19.915 1   31.43  ? 280 PHE B C   1 
ATOM   5468 O O   . PHE B 1 280 ? 0.007   10.221  -20.662 1   32.96  ? 280 PHE B O   1 
ATOM   5469 C CB  . PHE B 1 280 ? -1.241  11.791  -18.111 1   32.13  ? 280 PHE B CB  1 
ATOM   5470 C CG  . PHE B 1 280 ? 0.207   12.252  -18.196 1   32.21  ? 280 PHE B CG  1 
ATOM   5471 C CD1 . PHE B 1 280 ? 0.501   13.517  -18.688 1   32.56  ? 280 PHE B CD1 1 
ATOM   5472 C CD2 . PHE B 1 280 ? 1.265   11.41   -17.841 1   33.48  ? 280 PHE B CD2 1 
ATOM   5473 C CE1 . PHE B 1 280 ? 1.824   13.932  -18.85  1   35.74  ? 280 PHE B CE1 1 
ATOM   5474 C CE2 . PHE B 1 280 ? 2.579   11.858  -17.953 1   37.64  ? 280 PHE B CE2 1 
ATOM   5475 C CZ  . PHE B 1 280 ? 2.854   13.089  -18.471 1   33.9   ? 280 PHE B CZ  1 
ATOM   5476 N N   . TRP B 1 281 ? -1.352  8.783   -19.579 1   30.56  ? 281 TRP B N   1 
ATOM   5477 C CA  . TRP B 1 281 ? -0.612  7.586   -19.981 1   30.67  ? 281 TRP B CA  1 
ATOM   5478 C C   . TRP B 1 281 ? -1.177  6.992   -21.277 1   31.77  ? 281 TRP B C   1 
ATOM   5479 O O   . TRP B 1 281 ? -0.819  5.882   -21.625 1   31.79  ? 281 TRP B O   1 
ATOM   5480 C CB  . TRP B 1 281 ? -0.618  6.563   -18.841 1   32.16  ? 281 TRP B CB  1 
ATOM   5481 C CG  . TRP B 1 281 ? 0.26    6.979   -17.689 1   31.54  ? 281 TRP B CG  1 
ATOM   5482 C CD1 . TRP B 1 281 ? -0.002  7.878   -16.684 1   35.36  ? 281 TRP B CD1 1 
ATOM   5483 C CD2 . TRP B 1 281 ? 1.595   6.491   -17.439 1   31.92  ? 281 TRP B CD2 1 
ATOM   5484 N NE1 . TRP B 1 281 ? 1.082   8.016   -15.858 1   31.97  ? 281 TRP B NE1 1 
ATOM   5485 C CE2 . TRP B 1 281 ? 2.066   7.157   -16.284 1   31.24  ? 281 TRP B CE2 1 
ATOM   5486 C CE3 . TRP B 1 281 ? 2.414   5.537   -18.06  1   34.94  ? 281 TRP B CE3 1 
ATOM   5487 C CZ2 . TRP B 1 281 ? 3.338   6.932   -15.773 1   34.78  ? 281 TRP B CZ2 1 
ATOM   5488 C CZ3 . TRP B 1 281 ? 3.666   5.29    -17.534 1   38.58  ? 281 TRP B CZ3 1 
ATOM   5489 C CH2 . TRP B 1 281 ? 4.121   5.983   -16.402 1   35.64  ? 281 TRP B CH2 1 
ATOM   5490 N N   . ASN B 1 282 ? -2.095  7.696   -21.972 1   33.92  ? 282 ASN B N   1 
ATOM   5491 C CA  . ASN B 1 282 ? -2.625  7.276   -23.276 1   35.52  ? 282 ASN B CA  1 
ATOM   5492 C C   . ASN B 1 282 ? -3.316  5.918   -23.19  1   37.77  ? 282 ASN B C   1 
ATOM   5493 O O   . ASN B 1 282 ? -3.05   5.028   -23.974 1   36.67  ? 282 ASN B O   1 
ATOM   5494 C CB  . ASN B 1 282 ? -1.529  7.345   -24.343 1   36.78  ? 282 ASN B CB  1 
ATOM   5495 C CG  . ASN B 1 282 ? -2.082  7.245   -25.75  1   43.06  ? 282 ASN B CG  1 
ATOM   5496 O OD1 . ASN B 1 282 ? -3.209  7.68    -26.027 1   40.14  ? 282 ASN B OD1 1 
ATOM   5497 N ND2 . ASN B 1 282 ? -1.39   6.511   -26.606 1   43.05  ? 282 ASN B ND2 1 
ATOM   5498 N N   . LYS B 1 283 ? -4.255  5.765   -22.261 1   35.05  ? 283 LYS B N   1 
ATOM   5499 C CA  . LYS B 1 283 ? -5.058  4.558   -22.19  1   37.56  ? 283 LYS B CA  1 
ATOM   5500 C C   . LYS B 1 283 ? -6.497  4.947   -22.459 1   35.97  ? 283 LYS B C   1 
ATOM   5501 O O   . LYS B 1 283 ? -6.857  6.105   -22.232 1   35.68  ? 283 LYS B O   1 
ATOM   5502 C CB  . LYS B 1 283 ? -5.071  3.906   -20.813 1   38.95  ? 283 LYS B CB  1 
ATOM   5503 C CG  . LYS B 1 283 ? -3.805  3.877   -20.051 1   40.05  ? 283 LYS B CG  1 
ATOM   5504 C CD  . LYS B 1 283 ? -2.79   2.872   -20.549 1   45.01  ? 283 LYS B CD  1 
ATOM   5505 C CE  . LYS B 1 283 ? -1.845  2.676   -19.373 1   46.3   ? 283 LYS B CE  1 
ATOM   5506 N NZ  . LYS B 1 283 ? -1.102  1.442   -19.583 1   51.74  ? 283 LYS B NZ  1 
ATOM   5507 N N   . GLU B 1 284 ? -7.301  3.958   -22.833 1   37.54  ? 284 GLU B N   1 
ATOM   5508 C CA  . GLU B 1 284 ? -8.728  4.157   -23.022 1   41.58  ? 284 GLU B CA  1 
ATOM   5509 C C   . GLU B 1 284 ? -9.356  4.46    -21.66  1   40.76  ? 284 GLU B C   1 
ATOM   5510 O O   . GLU B 1 284 ? -9.065  3.778   -20.685 1   35.75  ? 284 GLU B O   1 
ATOM   5511 C CB  . GLU B 1 284 ? -9.445  3.045   -23.797 1   43.2   ? 284 GLU B CB  1 
ATOM   5512 C CG  . GLU B 1 284 ? -10.863 3.453   -24.232 1   45.3   ? 284 GLU B CG  1 
ATOM   5513 C CD  . GLU B 1 284 ? -11.033 4.494   -25.364 1   48.58  ? 284 GLU B CD  1 
ATOM   5514 O OE1 . GLU B 1 284 ? -10.018 4.672   -26.094 1   43.34  ? 284 GLU B OE1 1 
ATOM   5515 O OE2 . GLU B 1 284 ? -12.136 5.107   -25.539 1   44.33  ? 284 GLU B OE2 1 
ATOM   5516 N N   . ASN B 1 285 ? -10.13  5.557   -21.6   1   36.13  ? 285 ASN B N   1 
ATOM   5517 C CA  . ASN B 1 285 ? -10.577 6.115   -20.345 1   33.94  ? 285 ASN B CA  1 
ATOM   5518 C C   . ASN B 1 285 ? -11.975 5.602   -20.06  1   36     ? 285 ASN B C   1 
ATOM   5519 O O   . ASN B 1 285 ? -12.781 5.463   -20.97  1   42.21  ? 285 ASN B O   1 
ATOM   5520 C CB  . ASN B 1 285 ? -10.615 7.626   -20.404 1   35.52  ? 285 ASN B CB  1 
ATOM   5521 C CG  . ASN B 1 285 ? -10.233 8.246   -19.097 1   32.75  ? 285 ASN B CG  1 
ATOM   5522 O OD1 . ASN B 1 285 ? -10.669 7.802   -18.042 1   30.85  ? 285 ASN B OD1 1 
ATOM   5523 N ND2 . ASN B 1 285 ? -9.386  9.255   -19.172 1   35.09  ? 285 ASN B ND2 1 
ATOM   5524 N N   . GLU B 1 286 ? -12.236 5.215   -18.812 1   34.42  ? 286 GLU B N   1 
ATOM   5525 C CA  . GLU B 1 286 ? -13.582 4.853   -18.411 1   35.13  ? 286 GLU B CA  1 
ATOM   5526 C C   . GLU B 1 286 ? -14.115 5.794   -17.342 1   34.34  ? 286 GLU B C   1 
ATOM   5527 O O   . GLU B 1 286 ? -15.149 5.493   -16.772 1   34.52  ? 286 GLU B O   1 
ATOM   5528 C CB  . GLU B 1 286 ? -13.535 3.37    -18.026 1   40.9   ? 286 GLU B CB  1 
ATOM   5529 C CG  . GLU B 1 286 ? -12.893 3.06    -16.673 1   48.75  ? 286 GLU B CG  1 
ATOM   5530 C CD  . GLU B 1 286 ? -12.917 1.524   -16.453 1   57.13  ? 286 GLU B CD  1 
ATOM   5531 O OE1 . GLU B 1 286 ? -13.394 1.144   -15.364 1   60.92  ? 286 GLU B OE1 1 
ATOM   5532 O OE2 . GLU B 1 286 ? -12.578 0.707   -17.365 1   57.9   ? 286 GLU B OE2 1 
ATOM   5533 N N   . TRP B 1 287 ? -13.443 6.918   -17.059 1   30.87  ? 287 TRP B N   1 
ATOM   5534 C CA  . TRP B 1 287 ? -13.702 7.682   -15.83  1   29.79  ? 287 TRP B CA  1 
ATOM   5535 C C   . TRP B 1 287 ? -14.258 9.078   -16.071 1   30.85  ? 287 TRP B C   1 
ATOM   5536 O O   . TRP B 1 287 ? -14.539 9.8     -15.108 1   32.69  ? 287 TRP B O   1 
ATOM   5537 C CB  . TRP B 1 287 ? -12.403 7.803   -15.032 1   29.62  ? 287 TRP B CB  1 
ATOM   5538 C CG  . TRP B 1 287 ? -11.831 6.479   -14.636 1   33.03  ? 287 TRP B CG  1 
ATOM   5539 C CD1 . TRP B 1 287 ? -10.79  5.816   -15.21  1   34.93  ? 287 TRP B CD1 1 
ATOM   5540 C CD2 . TRP B 1 287 ? -12.338 5.644   -13.583 1   34.02  ? 287 TRP B CD2 1 
ATOM   5541 N NE1 . TRP B 1 287 ? -10.613 4.615   -14.571 1   37.91  ? 287 TRP B NE1 1 
ATOM   5542 C CE2 . TRP B 1 287 ? -11.546 4.48    -13.579 1   34.57  ? 287 TRP B CE2 1 
ATOM   5543 C CE3 . TRP B 1 287 ? -13.387 5.767   -12.66  1   35.1   ? 287 TRP B CE3 1 
ATOM   5544 C CZ2 . TRP B 1 287 ? -11.758 3.449   -12.661 1   36.57  ? 287 TRP B CZ2 1 
ATOM   5545 C CZ3 . TRP B 1 287 ? -13.599 4.745   -11.752 1   38.2   ? 287 TRP B CZ3 1 
ATOM   5546 C CH2 . TRP B 1 287 ? -12.773 3.616   -11.743 1   37.54  ? 287 TRP B CH2 1 
ATOM   5547 N N   . ILE B 1 288 ? -14.269 9.534   -17.32  1   31.23  ? 288 ILE B N   1 
ATOM   5548 C CA  . ILE B 1 288 ? -14.513 10.931  -17.648 1   31.74  ? 288 ILE B CA  1 
ATOM   5549 C C   . ILE B 1 288 ? -15.966 11.277  -17.36  1   31     ? 288 ILE B C   1 
ATOM   5550 O O   . ILE B 1 288 ? -16.837 10.452  -17.582 1   32.1   ? 288 ILE B O   1 
ATOM   5551 C CB  . ILE B 1 288 ? -14.14  11.154  -19.125 1   31.78  ? 288 ILE B CB  1 
ATOM   5552 C CG1 . ILE B 1 288 ? -12.632 11.112  -19.294 1   32.38  ? 288 ILE B CG1 1 
ATOM   5553 C CG2 . ILE B 1 288 ? -14.721 12.448  -19.69  1   33.62  ? 288 ILE B CG2 1 
ATOM   5554 C CD1 . ILE B 1 288 ? -12.154 10.894  -20.725 1   32.74  ? 288 ILE B CD1 1 
ATOM   5555 N N   . ASN B 1 289 ? -16.219 12.498  -16.894 1   31.88  ? 289 ASN B N   1 
ATOM   5556 C CA  . ASN B 1 289 ? -17.565 13.03   -16.74  1   34.64  ? 289 ASN B CA  1 
ATOM   5557 C C   . ASN B 1 289 ? -17.872 13.965  -17.925 1   35.11  ? 289 ASN B C   1 
ATOM   5558 O O   . ASN B 1 289 ? -17.435 15.117  -17.946 1   33.23  ? 289 ASN B O   1 
ATOM   5559 C CB  . ASN B 1 289 ? -17.726 13.703  -15.391 1   35.12  ? 289 ASN B CB  1 
ATOM   5560 C CG  . ASN B 1 289 ? -19.161 14.082  -15.117 1   37.4   ? 289 ASN B CG  1 
ATOM   5561 O OD1 . ASN B 1 289 ? -20.022 14.06   -16.001 1   37.06  ? 289 ASN B OD1 1 
ATOM   5562 N ND2 . ASN B 1 289 ? -19.456 14.435  -13.881 1   40.96  ? 289 ASN B ND2 1 
ATOM   5563 N N   . TYR B 1 290 ? -18.61  13.429  -18.913 1   36.47  ? 290 TYR B N   1 
ATOM   5564 C CA  . TYR B 1 290 ? -18.962 14.149  -20.133 1   38.6   ? 290 TYR B CA  1 
ATOM   5565 C C   . TYR B 1 290 ? -20.093 15.155  -19.895 1   40.17  ? 290 TYR B C   1 
ATOM   5566 O O   . TYR B 1 290 ? -20.342 15.967  -20.755 1   40.93  ? 290 TYR B O   1 
ATOM   5567 C CB  . TYR B 1 290 ? -19.397 13.176  -21.229 1   40.21  ? 290 TYR B CB  1 
ATOM   5568 C CG  . TYR B 1 290 ? -18.284 12.191  -21.58  1   40.04  ? 290 TYR B CG  1 
ATOM   5569 C CD1 . TYR B 1 290 ? -17.324 12.505  -22.528 1   39.36  ? 290 TYR B CD1 1 
ATOM   5570 C CD2 . TYR B 1 290 ? -18.189 10.944  -20.94  1   40.96  ? 290 TYR B CD2 1 
ATOM   5571 C CE1 . TYR B 1 290 ? -16.286 11.634  -22.821 1   40.21  ? 290 TYR B CE1 1 
ATOM   5572 C CE2 . TYR B 1 290 ? -17.156 10.066  -21.216 1   39.74  ? 290 TYR B CE2 1 
ATOM   5573 C CZ  . TYR B 1 290 ? -16.209 10.4    -22.177 1   40.3   ? 290 TYR B CZ  1 
ATOM   5574 O OH  . TYR B 1 290 ? -15.175 9.539   -22.434 1   35.5   ? 290 TYR B OH  1 
ATOM   5575 N N   . ASP B 1 291 ? -20.842 15.056  -18.785 1   40.67  ? 291 ASP B N   1 
ATOM   5576 C CA  . ASP B 1 291 ? -21.978 15.926  -18.494 1   45.84  ? 291 ASP B CA  1 
ATOM   5577 C C   . ASP B 1 291 ? -21.6   17.165  -17.688 1   42.26  ? 291 ASP B C   1 
ATOM   5578 O O   . ASP B 1 291 ? -22.344 18.12   -17.672 1   52.64  ? 291 ASP B O   1 
ATOM   5579 C CB  . ASP B 1 291 ? -23.066 15.183  -17.736 1   53.98  ? 291 ASP B CB  1 
ATOM   5580 C CG  . ASP B 1 291 ? -23.54  13.906  -18.415 1   61.97  ? 291 ASP B CG  1 
ATOM   5581 O OD1 . ASP B 1 291 ? -24.002 14.011  -19.557 1   62.16  ? 291 ASP B OD1 1 
ATOM   5582 O OD2 . ASP B 1 291 ? -23.377 12.808  -17.818 1   70.41  ? 291 ASP B OD2 1 
ATOM   5583 N N   . SER B 1 292 ? -20.448 17.189  -17.046 1   39.03  ? 292 SER B N   1 
ATOM   5584 C CA  . SER B 1 292 ? -20.105 18.214  -16.078 1   39.53  ? 292 SER B CA  1 
ATOM   5585 C C   . SER B 1 292 ? -19.67  19.492  -16.798 1   41.7   ? 292 SER B C   1 
ATOM   5586 O O   . SER B 1 292 ? -18.964 19.41   -17.79  1   38.9   ? 292 SER B O   1 
ATOM   5587 C CB  . SER B 1 292 ? -19.02  17.698  -15.202 1   37.39  ? 292 SER B CB  1 
ATOM   5588 O OG  . SER B 1 292 ? -18.46  18.688  -14.371 1   35.41  ? 292 SER B OG  1 
ATOM   5589 N N   . ASP B 1 293 ? -20.018 20.664  -16.257 1   44.36  ? 293 ASP B N   1 
ATOM   5590 C CA  . ASP B 1 293 ? -19.406 21.902  -16.743 1   51.11  ? 293 ASP B CA  1 
ATOM   5591 C C   . ASP B 1 293 ? -18.387 22.45   -15.743 1   45.04  ? 293 ASP B C   1 
ATOM   5592 O O   . ASP B 1 293 ? -18.068 23.629  -15.771 1   46.31  ? 293 ASP B O   1 
ATOM   5593 C CB  . ASP B 1 293 ? -20.412 22.937  -17.229 1   56.71  ? 293 ASP B CB  1 
ATOM   5594 C CG  . ASP B 1 293 ? -21.426 23.38   -16.197 1   65.1   ? 293 ASP B CG  1 
ATOM   5595 O OD1 . ASP B 1 293 ? -21.149 23.206  -14.975 1   63.77  ? 293 ASP B OD1 1 
ATOM   5596 O OD2 . ASP B 1 293 ? -22.529 23.786  -16.637 1   83.4   ? 293 ASP B OD2 1 
ATOM   5597 N N   . ALA B 1 294 ? -17.802 21.593  -14.916 1   37.62  ? 294 ALA B N   1 
ATOM   5598 C CA  . ALA B 1 294 ? -16.592 21.939  -14.189 1   38.41  ? 294 ALA B CA  1 
ATOM   5599 C C   . ALA B 1 294 ? -15.406 21.922  -15.165 1   33.11  ? 294 ALA B C   1 
ATOM   5600 O O   . ALA B 1 294 ? -15.283 21.021  -15.996 1   35.99  ? 294 ALA B O   1 
ATOM   5601 C CB  . ALA B 1 294 ? -16.392 21.003  -13.014 1   36.66  ? 294 ALA B CB  1 
ATOM   5602 N N   . VAL B 1 295 ? -14.575 22.971  -15.113 1   33.75  ? 295 VAL B N   1 
ATOM   5603 C CA  . VAL B 1 295 ? -13.423 23.092  -16     1   32.71  ? 295 VAL B CA  1 
ATOM   5604 C C   . VAL B 1 295 ? -12.538 21.835  -15.929 1   32.16  ? 295 VAL B C   1 
ATOM   5605 O O   . VAL B 1 295 ? -12.102 21.366  -16.968 1   33.61  ? 295 VAL B O   1 
ATOM   5606 C CB  . VAL B 1 295 ? -12.594 24.342  -15.63  1   34.66  ? 295 VAL B CB  1 
ATOM   5607 C CG1 . VAL B 1 295 ? -11.172 24.318  -16.232 1   33.02  ? 295 VAL B CG1 1 
ATOM   5608 C CG2 . VAL B 1 295 ? -13.367 25.616  -15.997 1   36.3   ? 295 VAL B CG2 1 
ATOM   5609 N N   . THR B 1 296 ? -12.272 21.282  -14.735 1   29.78  ? 296 THR B N   1 
ATOM   5610 C CA  . THR B 1 296 ? -11.373 20.128  -14.673 1   30.99  ? 296 THR B CA  1 
ATOM   5611 C C   . THR B 1 296 ? -11.953 18.924  -15.421 1   29.65  ? 296 THR B C   1 
ATOM   5612 O O   . THR B 1 296 ? -11.189 18.15   -16.008 1   31.47  ? 296 THR B O   1 
ATOM   5613 C CB  . THR B 1 296 ? -11.013 19.772  -13.236 1   34.04  ? 296 THR B CB  1 
ATOM   5614 O OG1 . THR B 1 296 ? -10.008 18.764  -13.263 1   34.24  ? 296 THR B OG1 1 
ATOM   5615 C CG2 . THR B 1 296 ? -12.173 19.188  -12.449 1   38.07  ? 296 THR B CG2 1 
ATOM   5616 N N   . ASP B 1 297 ? -13.273 18.737  -15.387 1   29.85  ? 297 ASP B N   1 
ATOM   5617 C CA  . ASP B 1 297 ? -13.919 17.649  -16.121 1   29.32  ? 297 ASP B CA  1 
ATOM   5618 C C   . ASP B 1 297 ? -13.852 17.877  -17.626 1   31.33  ? 297 ASP B C   1 
ATOM   5619 O O   . ASP B 1 297 ? -13.63  16.932  -18.4   1   28.7   ? 297 ASP B O   1 
ATOM   5620 C CB  . ASP B 1 297 ? -15.323 17.4    -15.616 1   31.34  ? 297 ASP B CB  1 
ATOM   5621 C CG  . ASP B 1 297 ? -15.403 17.006  -14.138 1   34.38  ? 297 ASP B CG  1 
ATOM   5622 O OD1 . ASP B 1 297 ? -14.485 16.3    -13.64  1   35.17  ? 297 ASP B OD1 1 
ATOM   5623 O OD2 . ASP B 1 297 ? -16.382 17.382  -13.514 1   33.74  ? 297 ASP B OD2 1 
ATOM   5624 N N   . MET B 1 298 ? -14.087 19.126  -18.034 1   28.3   ? 298 MET B N   1 
ATOM   5625 C CA  . MET B 1 298 ? -14.082 19.474  -19.446 1   31.23  ? 298 MET B CA  1 
ATOM   5626 C C   . MET B 1 298 ? -12.675 19.324  -20.031 1   29.04  ? 298 MET B C   1 
ATOM   5627 O O   . MET B 1 298 ? -12.549 18.937  -21.18  1   28.38  ? 298 MET B O   1 
ATOM   5628 C CB  . MET B 1 298 ? -14.671 20.882  -19.636 1   35.49  ? 298 MET B CB  1 
ATOM   5629 C CG  . MET B 1 298 ? -16.169 20.984  -19.287 1   39.93  ? 298 MET B CG  1 
ATOM   5630 S SD  . MET B 1 298 ? -16.69  22.686  -18.929 1   48.14  ? 298 MET B SD  1 
ATOM   5631 C CE  . MET B 1 298 ? -16.933 23.15   -20.641 1   49.46  ? 298 MET B CE  1 
ATOM   5632 N N   . GLN B 1 299 ? -11.643 19.611  -19.212 1   29.11  ? 299 GLN B N   1 
ATOM   5633 C CA  . GLN B 1 299 ? -10.25  19.362  -19.551 1   29.88  ? 299 GLN B CA  1 
ATOM   5634 C C   . GLN B 1 299 ? -9.979  17.904  -19.886 1   29.31  ? 299 GLN B C   1 
ATOM   5635 O O   . GLN B 1 299 ? -9.266  17.64   -20.841 1   28.06  ? 299 GLN B O   1 
ATOM   5636 C CB  . GLN B 1 299 ? -9.294  19.779  -18.44  1   29.88  ? 299 GLN B CB  1 
ATOM   5637 C CG  . GLN B 1 299 ? -9.161  21.297  -18.342 1   31.72  ? 299 GLN B CG  1 
ATOM   5638 C CD  . GLN B 1 299 ? -8.247  21.737  -17.226 1   31.15  ? 299 GLN B CD  1 
ATOM   5639 O OE1 . GLN B 1 299 ? -7.877  20.959  -16.329 1   30.3   ? 299 GLN B OE1 1 
ATOM   5640 N NE2 . GLN B 1 299 ? -7.832  22.992  -17.324 1   29.74  ? 299 GLN B NE2 1 
ATOM   5641 N N   . GLU B 1 300 ? -10.562 16.958  -19.126 1   30.82  ? 300 GLU B N   1 
ATOM   5642 C CA  . GLU B 1 300 ? -10.35  15.551  -19.42  1   30.02  ? 300 GLU B CA  1 
ATOM   5643 C C   . GLU B 1 300 ? -11.067 15.066  -20.677 1   31.56  ? 300 GLU B C   1 
ATOM   5644 O O   . GLU B 1 300 ? -10.528 14.187  -21.369 1   27.86  ? 300 GLU B O   1 
ATOM   5645 C CB  . GLU B 1 300 ? -10.644 14.707  -18.183 1   33.88  ? 300 GLU B CB  1 
ATOM   5646 C CG  . GLU B 1 300 ? -9.662  14.972  -17.039 1   33.39  ? 300 GLU B CG  1 
ATOM   5647 C CD  . GLU B 1 300 ? -8.197  15.232  -17.393 1   35.76  ? 300 GLU B CD  1 
ATOM   5648 O OE1 . GLU B 1 300 ? -7.579  14.478  -18.177 1   37.57  ? 300 GLU B OE1 1 
ATOM   5649 O OE2 . GLU B 1 300 ? -7.642  16.245  -16.924 1   36.16  ? 300 GLU B OE2 1 
ATOM   5650 N N   . VAL B 1 301 ? -12.244 15.645  -21.003 1   31.53  ? 301 VAL B N   1 
ATOM   5651 C CA  . VAL B 1 301 ? -12.922 15.387  -22.266 1   32.73  ? 301 VAL B CA  1 
ATOM   5652 C C   . VAL B 1 301 ? -11.966 15.761  -23.405 1   31.71  ? 301 VAL B C   1 
ATOM   5653 O O   . VAL B 1 301 ? -11.827 15.022  -24.388 1   31.35  ? 301 VAL B O   1 
ATOM   5654 C CB  . VAL B 1 301 ? -14.279 16.128  -22.369 1   33.18  ? 301 VAL B CB  1 
ATOM   5655 C CG1 . VAL B 1 301 ? -14.926 16.04   -23.742 1   34.7   ? 301 VAL B CG1 1 
ATOM   5656 C CG2 . VAL B 1 301 ? -15.292 15.677  -21.303 1   34.44  ? 301 VAL B CG2 1 
ATOM   5657 N N   . ILE B 1 302 ? -11.336 16.938  -23.263 1   29.7   ? 302 ILE B N   1 
ATOM   5658 C CA  . ILE B 1 302 ? -10.454 17.469  -24.294 1   31.75  ? 302 ILE B CA  1 
ATOM   5659 C C   . ILE B 1 302 ? -9.213  16.593  -24.433 1   29.61  ? 302 ILE B C   1 
ATOM   5660 O O   . ILE B 1 302 ? -8.826  16.25   -25.547 1   30.95  ? 302 ILE B O   1 
ATOM   5661 C CB  . ILE B 1 302 ? -10.107 18.938  -23.985 1   31.17  ? 302 ILE B CB  1 
ATOM   5662 C CG1 . ILE B 1 302 ? -11.318 19.865  -24.221 1   32.8   ? 302 ILE B CG1 1 
ATOM   5663 C CG2 . ILE B 1 302 ? -8.904  19.4    -24.812 1   31.27  ? 302 ILE B CG2 1 
ATOM   5664 C CD1 . ILE B 1 302 ? -11.19  21.197  -23.505 1   31.28  ? 302 ILE B CD1 1 
ATOM   5665 N N   . PHE B 1 303 ? -8.613  16.196  -23.3   1   28.87  ? 303 PHE B N   1 
ATOM   5666 C CA  . PHE B 1 303 ? -7.413  15.382  -23.345 1   28.57  ? 303 PHE B CA  1 
ATOM   5667 C C   . PHE B 1 303 ? -7.689  14.044  -24.022 1   29.15  ? 303 PHE B C   1 
ATOM   5668 O O   . PHE B 1 303 ? -6.884  13.58   -24.841 1   28.79  ? 303 PHE B O   1 
ATOM   5669 C CB  . PHE B 1 303 ? -6.865  15.192  -21.919 1   28.29  ? 303 PHE B CB  1 
ATOM   5670 C CG  . PHE B 1 303 ? -5.382  14.926  -21.769 1   28.25  ? 303 PHE B CG  1 
ATOM   5671 C CD1 . PHE B 1 303 ? -4.578  14.498  -22.836 1   29.93  ? 303 PHE B CD1 1 
ATOM   5672 C CD2 . PHE B 1 303 ? -4.806  14.989  -20.493 1   31.37  ? 303 PHE B CD2 1 
ATOM   5673 C CE1 . PHE B 1 303 ? -3.232  14.228  -22.622 1   30.05  ? 303 PHE B CE1 1 
ATOM   5674 C CE2 . PHE B 1 303 ? -3.462  14.704  -20.302 1   30.77  ? 303 PHE B CE2 1 
ATOM   5675 C CZ  . PHE B 1 303 ? -2.688  14.329  -21.367 1   30.75  ? 303 PHE B CZ  1 
ATOM   5676 N N   . GLU B 1 304 ? -8.847  13.436  -23.717 1   28.72  ? 304 GLU B N   1 
ATOM   5677 C CA  . GLU B 1 304 ? -9.268  12.249  -24.44  1   30.79  ? 304 GLU B CA  1 
ATOM   5678 C C   . GLU B 1 304 ? -9.336  12.503  -25.948 1   31.75  ? 304 GLU B C   1 
ATOM   5679 O O   . GLU B 1 304 ? -8.929  11.649  -26.757 1   32.39  ? 304 GLU B O   1 
ATOM   5680 C CB  . GLU B 1 304 ? -10.578 11.696  -23.888 1   31.5   ? 304 GLU B CB  1 
ATOM   5681 C CG  . GLU B 1 304 ? -11.12  10.519  -24.693 1   32.63  ? 304 GLU B CG  1 
ATOM   5682 C CD  . GLU B 1 304 ? -12.327 9.886   -24.031 1   39.99  ? 304 GLU B CD  1 
ATOM   5683 O OE1 . GLU B 1 304 ? -12.218 8.672   -23.64  1   39.46  ? 304 GLU B OE1 1 
ATOM   5684 O OE2 . GLU B 1 304 ? -13.386 10.579  -24.029 1   35.67  ? 304 GLU B OE2 1 
ATOM   5685 N N   . LEU B 1 305 ? -9.945  13.62   -26.367 1   30.62  ? 305 LEU B N   1 
ATOM   5686 C CA  . LEU B 1 305 ? -10.046 13.883  -27.798 1   31.37  ? 305 LEU B CA  1 
ATOM   5687 C C   . LEU B 1 305 ? -8.651  13.973  -28.432 1   31.88  ? 305 LEU B C   1 
ATOM   5688 O O   . LEU B 1 305 ? -8.459  13.474  -29.551 1   36.54  ? 305 LEU B O   1 
ATOM   5689 C CB  . LEU B 1 305 ? -10.888 15.141  -28.059 1   32.97  ? 305 LEU B CB  1 
ATOM   5690 C CG  . LEU B 1 305 ? -12.392 14.979  -27.85  1   36.49  ? 305 LEU B CG  1 
ATOM   5691 C CD1 . LEU B 1 305 ? -13.126 16.294  -27.73  1   39.93  ? 305 LEU B CD1 1 
ATOM   5692 C CD2 . LEU B 1 305 ? -13.001 14.179  -28.988 1   39.67  ? 305 LEU B CD2 1 
ATOM   5693 N N   . ILE B 1 306 ? -7.699  14.617  -27.736 1   33.34  ? 306 ILE B N   1 
ATOM   5694 C CA  . ILE B 1 306 ? -6.318  14.688  -28.195 1   35.46  ? 306 ILE B CA  1 
ATOM   5695 C C   . ILE B 1 306 ? -5.743  13.281  -28.392 1   35.8   ? 306 ILE B C   1 
ATOM   5696 O O   . ILE B 1 306 ? -5.205  12.988  -29.435 1   35.09  ? 306 ILE B O   1 
ATOM   5697 C CB  . ILE B 1 306 ? -5.435  15.522  -27.27  1   36.28  ? 306 ILE B CB  1 
ATOM   5698 C CG1 . ILE B 1 306 ? -5.912  16.979  -27.194 1   34.28  ? 306 ILE B CG1 1 
ATOM   5699 C CG2 . ILE B 1 306 ? -3.958  15.421  -27.699 1   37.58  ? 306 ILE B CG2 1 
ATOM   5700 C CD1 . ILE B 1 306 ? -5.333  17.713  -26.01  1   35.51  ? 306 ILE B CD1 1 
ATOM   5701 N N   . ASN B 1 307 ? -5.892  12.381  -27.412 1   34.56  ? 307 ASN B N   1 
ATOM   5702 C CA  . ASN B 1 307 ? -5.473  10.993  -27.6   1   35.93  ? 307 ASN B CA  1 
ATOM   5703 C C   . ASN B 1 307 ? -6.205  10.285  -28.737 1   36.38  ? 307 ASN B C   1 
ATOM   5704 O O   . ASN B 1 307 ? -5.622  9.39    -29.338 1   39.91  ? 307 ASN B O   1 
ATOM   5705 C CB  . ASN B 1 307 ? -5.624  10.159  -26.323 1   34.45  ? 307 ASN B CB  1 
ATOM   5706 C CG  . ASN B 1 307 ? -4.716  10.636  -25.22  1   35.54  ? 307 ASN B CG  1 
ATOM   5707 O OD1 . ASN B 1 307 ? -3.736  11.336  -25.474 1   31.55  ? 307 ASN B OD1 1 
ATOM   5708 N ND2 . ASN B 1 307 ? -4.991  10.232  -23.981 1   32.24  ? 307 ASN B ND2 1 
ATOM   5709 N N   . HIS B 1 308 ? -7.474  10.63   -29.018 1   38.36  ? 308 HIS B N   1 
ATOM   5710 C CA  . HIS B 1 308 ? -8.216  10.052  -30.14  1   39.19  ? 308 HIS B CA  1 
ATOM   5711 C C   . HIS B 1 308 ? -8.001  10.817  -31.455 1   41.23  ? 308 HIS B C   1 
ATOM   5712 O O   . HIS B 1 308 ? -8.731  10.567  -32.41  1   40.57  ? 308 HIS B O   1 
ATOM   5713 C CB  . HIS B 1 308 ? -9.714  9.929   -29.808 1   40.56  ? 308 HIS B CB  1 
ATOM   5714 C CG  . HIS B 1 308 ? -10.053 8.936   -28.735 1   47.68  ? 308 HIS B CG  1 
ATOM   5715 N ND1 . HIS B 1 308 ? -11.246 8.974   -28.034 1   46.43  ? 308 HIS B ND1 1 
ATOM   5716 C CD2 . HIS B 1 308 ? -9.4    7.85    -28.276 1   51.63  ? 308 HIS B CD2 1 
ATOM   5717 C CE1 . HIS B 1 308 ? -11.281 7.974   -27.164 1   47.66  ? 308 HIS B CE1 1 
ATOM   5718 N NE2 . HIS B 1 308 ? -10.171 7.285   -27.29  1   47.25  ? 308 HIS B NE2 1 
ATOM   5719 N N   . LYS B 1 309 ? -7.027  11.744  -31.52  1   42.87  ? 309 LYS B N   1 
ATOM   5720 C CA  . LYS B 1 309 ? -6.599  12.4    -32.759 1   46.12  ? 309 LYS B CA  1 
ATOM   5721 C C   . LYS B 1 309 ? -7.663  13.381  -33.269 1   44.41  ? 309 LYS B C   1 
ATOM   5722 O O   . LYS B 1 309 ? -7.625  13.726  -34.437 1   47.14  ? 309 LYS B O   1 
ATOM   5723 C CB  . LYS B 1 309 ? -6.259  11.476  -33.953 1   51.03  ? 309 LYS B CB  1 
ATOM   5724 C CG  . LYS B 1 309 ? -5.363  10.303  -33.703 1   59.87  ? 309 LYS B CG  1 
ATOM   5725 C CD  . LYS B 1 309 ? -3.971  10.711  -33.265 1   59.83  ? 309 LYS B CD  1 
ATOM   5726 C CE  . LYS B 1 309 ? -3.239  9.533   -32.728 1   63.1   ? 309 LYS B CE  1 
ATOM   5727 N NZ  . LYS B 1 309 ? -2.061  9.998   -32     1   64.27  ? 309 LYS B NZ  1 
ATOM   5728 N N   . GLU B 1 310 ? -8.616  13.8    -32.427 1   38.23  ? 310 GLU B N   1 
ATOM   5729 C CA  . GLU B 1 310 ? -9.694  14.686  -32.813 1   41.83  ? 310 GLU B CA  1 
ATOM   5730 C C   . GLU B 1 310 ? -9.285  16.107  -32.412 1   40.73  ? 310 GLU B C   1 
ATOM   5731 O O   . GLU B 1 310 ? -9.892  16.703  -31.53  1   38.8   ? 310 GLU B O   1 
ATOM   5732 C CB  . GLU B 1 310 ? -11.001 14.18   -32.226 1   45.23  ? 310 GLU B CB  1 
ATOM   5733 C CG  . GLU B 1 310 ? -11.505 12.913  -32.918 1   52.74  ? 310 GLU B CG  1 
ATOM   5734 C CD  . GLU B 1 310 ? -12.859 12.513  -32.378 1   58.64  ? 310 GLU B CD  1 
ATOM   5735 O OE1 . GLU B 1 310 ? -13.813 13.281  -32.598 1   63.02  ? 310 GLU B OE1 1 
ATOM   5736 O OE2 . GLU B 1 310 ? -12.954 11.475  -31.699 1   68.27  ? 310 GLU B OE2 1 
ATOM   5737 N N   . LEU B 1 311 ? -8.235  16.611  -33.064 1   40.48  ? 311 LEU B N   1 
ATOM   5738 C CA  . LEU B 1 311 ? -7.584  17.845  -32.639 1   41.77  ? 311 LEU B CA  1 
ATOM   5739 C C   . LEU B 1 311 ? -8.497  19.054  -32.882 1   41.5   ? 311 LEU B C   1 
ATOM   5740 O O   . LEU B 1 311 ? -8.535  19.984  -32.063 1   40.64  ? 311 LEU B O   1 
ATOM   5741 C CB  . LEU B 1 311 ? -6.234  17.98   -33.359 1   44.55  ? 311 LEU B CB  1 
ATOM   5742 C CG  . LEU B 1 311 ? -5.145  16.951  -33.02  1   47.34  ? 311 LEU B CG  1 
ATOM   5743 C CD1 . LEU B 1 311 ? -3.74   17.365  -33.494 1   47.77  ? 311 LEU B CD1 1 
ATOM   5744 C CD2 . LEU B 1 311 ? -5.089  16.675  -31.546 1   46.26  ? 311 LEU B CD2 1 
ATOM   5745 N N   . SER B 1 312 ? -9.215  19.04   -34.011 1   42.17  ? 312 SER B N   1 
ATOM   5746 C CA  . SER B 1 312 ? -10.101 20.121  -34.403 1   44.55  ? 312 SER B CA  1 
ATOM   5747 C C   . SER B 1 312 ? -11.24  20.271  -33.398 1   45.94  ? 312 SER B C   1 
ATOM   5748 O O   . SER B 1 312 ? -11.458 21.387  -32.926 1   45.19  ? 312 SER B O   1 
ATOM   5749 C CB  . SER B 1 312 ? -10.603 19.919  -35.833 1   49.42  ? 312 SER B CB  1 
ATOM   5750 O OG  . SER B 1 312 ? -11.757 20.716  -36.034 1   52.45  ? 312 SER B OG  1 
ATOM   5751 N N   . LYS B 1 313 ? -11.881 19.156  -33     1   42.22  ? 313 LYS B N   1 
ATOM   5752 C CA  . LYS B 1 313 ? -12.908 19.222  -31.978 1   43.78  ? 313 LYS B CA  1 
ATOM   5753 C C   . LYS B 1 313 ? -12.319 19.576  -30.603 1   40.09  ? 313 LYS B C   1 
ATOM   5754 O O   . LYS B 1 313 ? -12.986 20.272  -29.84  1   42.82  ? 313 LYS B O   1 
ATOM   5755 C CB  . LYS B 1 313 ? -13.782 17.973  -31.848 1   50.35  ? 313 LYS B CB  1 
ATOM   5756 C CG  . LYS B 1 313 ? -14.945 18.158  -30.86  1   56.35  ? 313 LYS B CG  1 
ATOM   5757 C CD  . LYS B 1 313 ? -16.161 17.26   -31.034 1   66.85  ? 313 LYS B CD  1 
ATOM   5758 C CE  . LYS B 1 313 ? -15.992 15.92   -30.36  1   75.35  ? 313 LYS B CE  1 
ATOM   5759 N NZ  . LYS B 1 313 ? -16.931 14.886  -30.812 1   80.74  ? 313 LYS B NZ  1 
ATOM   5760 N N   . ALA B 1 314 ? -11.149 19.042  -30.232 1   35.4   ? 314 ALA B N   1 
ATOM   5761 C CA  . ALA B 1 314 ? -10.495 19.382  -28.963 1   32.97  ? 314 ALA B CA  1 
ATOM   5762 C C   . ALA B 1 314 ? -10.251 20.894  -28.886 1   34.29  ? 314 ALA B C   1 
ATOM   5763 O O   . ALA B 1 314 ? -10.522 21.503  -27.864 1   33.63  ? 314 ALA B O   1 
ATOM   5764 C CB  . ALA B 1 314 ? -9.193  18.643  -28.825 1   31.98  ? 314 ALA B CB  1 
ATOM   5765 N N   . LEU B 1 315 ? -9.78   21.486  -29.98  1   36.78  ? 315 LEU B N   1 
ATOM   5766 C CA  . LEU B 1 315 ? -9.501  22.92   -30.024 1   42.15  ? 315 LEU B CA  1 
ATOM   5767 C C   . LEU B 1 315 ? -10.783 23.732  -29.855 1   47.92  ? 315 LEU B C   1 
ATOM   5768 O O   . LEU B 1 315 ? -10.798 24.686  -29.079 1   47.55  ? 315 LEU B O   1 
ATOM   5769 C CB  . LEU B 1 315 ? -8.747  23.34   -31.275 1   45.8   ? 315 LEU B CB  1 
ATOM   5770 C CG  . LEU B 1 315 ? -8.213  24.783  -31.304 1   52.22  ? 315 LEU B CG  1 
ATOM   5771 C CD1 . LEU B 1 315 ? -7.289  25.193  -30.153 1   48.94  ? 315 LEU B CD1 1 
ATOM   5772 C CD2 . LEU B 1 315 ? -7.489  24.952  -32.645 1   55.08  ? 315 LEU B CD2 1 
ATOM   5773 N N   . GLN B 1 316 ? -11.87  23.343  -30.521 1   49.65  ? 316 GLN B N   1 
ATOM   5774 C CA  . GLN B 1 316 ? -13.148 24.026  -30.353 1   53.36  ? 316 GLN B CA  1 
ATOM   5775 C C   . GLN B 1 316 ? -13.613 23.963  -28.892 1   49.43  ? 316 GLN B C   1 
ATOM   5776 O O   . GLN B 1 316 ? -14.075 24.977  -28.376 1   51.34  ? 316 GLN B O   1 
ATOM   5777 C CB  . GLN B 1 316 ? -14.218 23.556  -31.348 1   53.71  ? 316 GLN B CB  1 
ATOM   5778 C CG  . GLN B 1 316 ? -13.839 23.872  -32.8   1   60.06  ? 316 GLN B CG  1 
ATOM   5779 C CD  . GLN B 1 316 ? -14.812 23.339  -33.837 1   65.5   ? 316 GLN B CD  1 
ATOM   5780 O OE1 . GLN B 1 316 ? -15.531 22.359  -33.598 1   70.65  ? 316 GLN B OE1 1 
ATOM   5781 N NE2 . GLN B 1 316 ? -14.816 23.959  -35.012 1   62.9   ? 316 GLN B NE2 1 
ATOM   5782 N N   . LEU B 1 317 ? -13.506 22.812  -28.217 1   44.93  ? 317 LEU B N   1 
ATOM   5783 C CA  . LEU B 1 317 ? -13.888 22.71   -26.806 1   44.99  ? 317 LEU B CA  1 
ATOM   5784 C C   . LEU B 1 317 ? -12.953 23.527  -25.896 1   41.55  ? 317 LEU B C   1 
ATOM   5785 O O   . LEU B 1 317 ? -13.407 24.052  -24.879 1   41.54  ? 317 LEU B O   1 
ATOM   5786 C CB  . LEU B 1 317 ? -14.018 21.275  -26.306 1   45.94  ? 317 LEU B CB  1 
ATOM   5787 C CG  . LEU B 1 317 ? -15.166 20.481  -26.963 1   55.06  ? 317 LEU B CG  1 
ATOM   5788 C CD1 . LEU B 1 317 ? -15.033 19.001  -26.634 1   50.7   ? 317 LEU B CD1 1 
ATOM   5789 C CD2 . LEU B 1 317 ? -16.565 20.98   -26.557 1   57.37  ? 317 LEU B CD2 1 
ATOM   5790 N N   . LEU B 1 318 ? -11.662 23.59   -26.234 1   36.98  ? 318 LEU B N   1 
ATOM   5791 C CA  . LEU B 1 318 ? -10.692 24.313  -25.444 1   36.75  ? 318 LEU B CA  1 
ATOM   5792 C C   . LEU B 1 318 ? -11     25.814  -25.516 1   39.98  ? 318 LEU B C   1 
ATOM   5793 O O   . LEU B 1 318 ? -10.936 26.503  -24.516 1   38.13  ? 318 LEU B O   1 
ATOM   5794 C CB  . LEU B 1 318 ? -9.273  23.972  -25.855 1   36.37  ? 318 LEU B CB  1 
ATOM   5795 C CG  . LEU B 1 318 ? -8.153  24.485  -24.943 1   39.23  ? 318 LEU B CG  1 
ATOM   5796 C CD1 . LEU B 1 318 ? -8.097  23.776  -23.6   1   34.38  ? 318 LEU B CD1 1 
ATOM   5797 C CD2 . LEU B 1 318 ? -6.814  24.354  -25.633 1   43.09  ? 318 LEU B CD2 1 
ATOM   5798 N N   . ASN B 1 319 ? -11.368 26.321  -26.689 1   41.63  ? 319 ASN B N   1 
ATOM   5799 C CA  . ASN B 1 319 ? -11.861 27.692  -26.852 1   48.02  ? 319 ASN B CA  1 
ATOM   5800 C C   . ASN B 1 319 ? -13.066 28.041  -25.978 1   49.76  ? 319 ASN B C   1 
ATOM   5801 O O   . ASN B 1 319 ? -13.086 29.126  -25.434 1   53.81  ? 319 ASN B O   1 
ATOM   5802 C CB  . ASN B 1 319 ? -12.313 27.965  -28.278 1   54.61  ? 319 ASN B CB  1 
ATOM   5803 C CG  . ASN B 1 319 ? -11.158 28.122  -29.231 1   57.53  ? 319 ASN B CG  1 
ATOM   5804 O OD1 . ASN B 1 319 ? -9.995  28.223  -28.797 1   51.2   ? 319 ASN B OD1 1 
ATOM   5805 N ND2 . ASN B 1 319 ? -11.515 28.24   -30.515 1   62.66  ? 319 ASN B ND2 1 
ATOM   5806 N N   . LYS B 1 320 ? -14.028 27.133  -25.809 1   53.85  ? 320 LYS B N   1 
ATOM   5807 C CA  . LYS B 1 320 ? -15.115 27.329  -24.858 1   61.51  ? 320 LYS B CA  1 
ATOM   5808 C C   . LYS B 1 320 ? -14.6   27.521  -23.425 1   56.52  ? 320 LYS B C   1 
ATOM   5809 O O   . LYS B 1 320 ? -15.231 28.258  -22.67  1   52.56  ? 320 LYS B O   1 
ATOM   5810 C CB  . LYS B 1 320 ? -16.139 26.185  -24.897 1   73.78  ? 320 LYS B CB  1 
ATOM   5811 C CG  . LYS B 1 320 ? -16.969 26.092  -26.195 1   82.93  ? 320 LYS B CG  1 
ATOM   5812 C CD  . LYS B 1 320 ? -17.698 24.762  -26.407 1   91.68  ? 320 LYS B CD  1 
ATOM   5813 C CE  . LYS B 1 320 ? -18.575 24.281  -25.281 1   98.12  ? 320 LYS B CE  1 
ATOM   5814 N NZ  . LYS B 1 320 ? -19.643 25.245  -24.994 1   107.11 ? 320 LYS B NZ  1 
ATOM   5815 N N   . LEU B 1 321 ? -13.495 26.85   -23.043 1   49.22  ? 321 LEU B N   1 
ATOM   5816 C CA  . LEU B 1 321 ? -12.918 26.992  -21.717 1   45.88  ? 321 LEU B CA  1 
ATOM   5817 C C   . LEU B 1 321 ? -12.247 28.339  -21.502 1   42.75  ? 321 LEU B C   1 
ATOM   5818 O O   . LEU B 1 321 ? -12.155 28.753  -20.352 1   45.9   ? 321 LEU B O   1 
ATOM   5819 C CB  . LEU B 1 321 ? -11.954 25.856  -21.359 1   42.66  ? 321 LEU B CB  1 
ATOM   5820 C CG  . LEU B 1 321 ? -12.64  24.533  -21.039 1   41.44  ? 321 LEU B CG  1 
ATOM   5821 C CD1 . LEU B 1 321 ? -11.633 23.456  -20.756 1   38.17  ? 321 LEU B CD1 1 
ATOM   5822 C CD2 . LEU B 1 321 ? -13.58  24.703  -19.872 1   45.05  ? 321 LEU B CD2 1 
ATOM   5823 N N   . GLU B 1 322 ? -11.765 29.008  -22.553 1   44.23  ? 322 GLU B N   1 
ATOM   5824 C CA  . GLU B 1 322 ? -11.224 30.362  -22.414 1   50.46  ? 322 GLU B CA  1 
ATOM   5825 C C   . GLU B 1 322 ? -12.251 31.378  -21.901 1   53.71  ? 322 GLU B C   1 
ATOM   5826 O O   . GLU B 1 322 ? -11.878 32.344  -21.253 1   58.85  ? 322 GLU B O   1 
ATOM   5827 C CB  . GLU B 1 322 ? -10.561 30.809  -23.718 1   54.8   ? 322 GLU B CB  1 
ATOM   5828 C CG  . GLU B 1 322 ? -9.386  29.89   -24.044 1   56     ? 322 GLU B CG  1 
ATOM   5829 C CD  . GLU B 1 322 ? -8.177  30.408  -24.803 1   59.96  ? 322 GLU B CD  1 
ATOM   5830 O OE1 . GLU B 1 322 ? -7.102  29.738  -24.73  1   56.75  ? 322 GLU B OE1 1 
ATOM   5831 O OE2 . GLU B 1 322 ? -8.308  31.462  -25.467 1   62.77  ? 322 GLU B OE2 1 
ATOM   5832 N N   . GLU B 1 323 ? -13.541 31.126  -22.117 1   57.37  ? 323 GLU B N   1 
ATOM   5833 C CA  . GLU B 1 323 ? -14.633 31.948  -21.604 1   66.37  ? 323 GLU B CA  1 
ATOM   5834 C C   . GLU B 1 323 ? -14.824 31.752  -20.088 1   63.53  ? 323 GLU B C   1 
ATOM   5835 O O   . GLU B 1 323 ? -15.564 32.524  -19.479 1   63.5   ? 323 GLU B O   1 
ATOM   5836 C CB  . GLU B 1 323 ? -15.916 31.582  -22.376 1   71.27  ? 323 GLU B CB  1 
ATOM   5837 C CG  . GLU B 1 323 ? -17.041 32.62   -22.365 1   86.01  ? 323 GLU B CG  1 
ATOM   5838 C CD  . GLU B 1 323 ? -16.817 33.911  -23.153 1   90.9   ? 323 GLU B CD  1 
ATOM   5839 O OE1 . GLU B 1 323 ? -15.977 33.884  -24.084 1   106.03 ? 323 GLU B OE1 1 
ATOM   5840 O OE2 . GLU B 1 323 ? -17.454 34.954  -22.845 1   74.44  ? 323 GLU B OE2 1 
ATOM   5841 N N   . ARG B 1 324 ? -14.204 30.721  -19.476 1   46.99  ? 324 ARG B N   1 
ATOM   5842 C CA  . ARG B 1 324 ? -14.556 30.304  -18.128 1   45.46  ? 324 ARG B CA  1 
ATOM   5843 C C   . ARG B 1 324 ? -13.527 30.836  -17.137 1   42.83  ? 324 ARG B C   1 
ATOM   5844 O O   . ARG B 1 324 ? -12.361 31.008  -17.462 1   40.07  ? 324 ARG B O   1 
ATOM   5845 C CB  . ARG B 1 324 ? -14.626 28.773  -18.011 1   44.59  ? 324 ARG B CB  1 
ATOM   5846 C CG  . ARG B 1 324 ? -15.748 28.154  -18.842 1   46.97  ? 324 ARG B CG  1 
ATOM   5847 C CD  . ARG B 1 324 ? -17.126 28.483  -18.307 1   46.65  ? 324 ARG B CD  1 
ATOM   5848 N NE  . ARG B 1 324 ? -17.225 27.919  -16.958 1   45.06  ? 324 ARG B NE  1 
ATOM   5849 C CZ  . ARG B 1 324 ? -17.395 26.642  -16.672 1   44.42  ? 324 ARG B CZ  1 
ATOM   5850 N NH1 . ARG B 1 324 ? -17.678 25.763  -17.615 1   41.46  ? 324 ARG B NH1 1 
ATOM   5851 N NH2 . ARG B 1 324 ? -17.262 26.244  -15.43  1   42.29  ? 324 ARG B NH2 1 
ATOM   5852 N N   . ASP B 1 325 ? -13.987 31.038  -15.901 1   42.4   ? 325 ASP B N   1 
ATOM   5853 C CA  . ASP B 1 325 ? -13.15  31.452  -14.794 1   42.44  ? 325 ASP B CA  1 
ATOM   5854 C C   . ASP B 1 325 ? -12.323 30.241  -14.429 1   35.5   ? 325 ASP B C   1 
ATOM   5855 O O   . ASP B 1 325 ? -12.899 29.154  -14.271 1   37.36  ? 325 ASP B O   1 
ATOM   5856 C CB  . ASP B 1 325 ? -13.998 31.897  -13.607 1   46.88  ? 325 ASP B CB  1 
ATOM   5857 C CG  . ASP B 1 325 ? -14.723 33.223  -13.835 1   54.84  ? 325 ASP B CG  1 
ATOM   5858 O OD1 . ASP B 1 325 ? -14.139 34.092  -14.526 1   55.46  ? 325 ASP B OD1 1 
ATOM   5859 O OD2 . ASP B 1 325 ? -15.842 33.408  -13.285 1   72.96  ? 325 ASP B OD2 1 
ATOM   5860 N N   . GLN B 1 326 ? -11.004 30.419  -14.361 1   33.5   ? 326 GLN B N   1 
ATOM   5861 C CA  . GLN B 1 326 ? -10.093 29.344  -13.992 1   34.04  ? 326 GLN B CA  1 
ATOM   5862 C C   . GLN B 1 326 ? -9.049  29.865  -13.036 1   34.71  ? 326 GLN B C   1 
ATOM   5863 O O   . GLN B 1 326 ? -8.603  30.979  -13.239 1   30.85  ? 326 GLN B O   1 
ATOM   5864 C CB  . GLN B 1 326 ? -9.335  28.899  -15.233 1   34.28  ? 326 GLN B CB  1 
ATOM   5865 C CG  . GLN B 1 326 ? -10.255 28.243  -16.24  1   35.63  ? 326 GLN B CG  1 
ATOM   5866 C CD  . GLN B 1 326 ? -9.489  27.662  -17.396 1   35.85  ? 326 GLN B CD  1 
ATOM   5867 O OE1 . GLN B 1 326 ? -8.648  26.776  -17.251 1   34.42  ? 326 GLN B OE1 1 
ATOM   5868 N NE2 . GLN B 1 326 ? -9.785  28.144  -18.581 1   36.76  ? 326 GLN B NE2 1 
ATOM   5869 N N   . ASN B 1 327 ? -8.585  29.002  -12.132 1   34.01  ? 327 ASN B N   1 
ATOM   5870 C CA  . ASN B 1 327 ? -7.44   29.339  -11.287 1   36.17  ? 327 ASN B CA  1 
ATOM   5871 C C   . ASN B 1 327 ? -6.115  29.112  -12.045 1   34.32  ? 327 ASN B C   1 
ATOM   5872 O O   . ASN B 1 327 ? -6.072  28.567  -13.148 1   31     ? 327 ASN B O   1 
ATOM   5873 C CB  . ASN B 1 327 ? -7.557  28.653  -9.933  1   31.32  ? 327 ASN B CB  1 
ATOM   5874 C CG  . ASN B 1 327 ? -7.299  27.176  -9.988  1   30.77  ? 327 ASN B CG  1 
ATOM   5875 O OD1 . ASN B 1 327 ? -6.274  26.755  -10.524 1   31.32  ? 327 ASN B OD1 1 
ATOM   5876 N ND2 . ASN B 1 327 ? -8.15   26.37   -9.355  1   31.44  ? 327 ASN B ND2 1 
ATOM   5877 N N   . GLU B 1 328 ? -5.016  29.587  -11.451 1   30.78  ? 328 GLU B N   1 
ATOM   5878 C CA  . GLU B 1 328 ? -3.71   29.543  -12.071 1   31.63  ? 328 GLU B CA  1 
ATOM   5879 C C   . GLU B 1 328 ? -3.251  28.117  -12.345 1   28.64  ? 328 GLU B C   1 
ATOM   5880 O O   . GLU B 1 328 ? -2.603  27.898  -13.363 1   26.46  ? 328 GLU B O   1 
ATOM   5881 C CB  . GLU B 1 328 ? -2.69   30.333  -11.255 1   32.99  ? 328 GLU B CB  1 
ATOM   5882 C CG  . GLU B 1 328 ? -2.917  31.833  -11.437 1   39.81  ? 328 GLU B CG  1 
ATOM   5883 C CD  . GLU B 1 328 ? -1.871  32.652  -10.702 1   48.97  ? 328 GLU B CD  1 
ATOM   5884 O OE1 . GLU B 1 328 ? -1.286  32.199  -9.679  1   42.68  ? 328 GLU B OE1 1 
ATOM   5885 O OE2 . GLU B 1 328 ? -1.601  33.738  -11.23  1   53.38  ? 328 GLU B OE2 1 
ATOM   5886 N N   . ASN B 1 329 ? -3.529  27.171  -11.438 1   26.34  ? 329 ASN B N   1 
ATOM   5887 C CA  . ASN B 1 329 ? -3.133  25.789  -11.665 1   28.21  ? 329 ASN B CA  1 
ATOM   5888 C C   . ASN B 1 329 ? -3.951  25.194  -12.823 1   28.26  ? 329 ASN B C   1 
ATOM   5889 O O   . ASN B 1 329 ? -3.433  24.507  -13.715 1   26.43  ? 329 ASN B O   1 
ATOM   5890 C CB  . ASN B 1 329 ? -3.32   24.962  -10.402 1   26.65  ? 329 ASN B CB  1 
ATOM   5891 C CG  . ASN B 1 329 ? -2.533  23.69   -10.438 1   26.88  ? 329 ASN B CG  1 
ATOM   5892 O OD1 . ASN B 1 329 ? -3.083  22.61   -10.627 1   27.89  ? 329 ASN B OD1 1 
ATOM   5893 N ND2 . ASN B 1 329 ? -1.223  23.804  -10.345 1   25.99  ? 329 ASN B ND2 1 
ATOM   5894 N N   . GLU B 1 330 ? -5.246  25.501  -12.846 1   27.79  ? 330 GLU B N   1 
ATOM   5895 C CA  . GLU B 1 330 ? -6.121  25.047  -13.931 1   29.17  ? 330 GLU B CA  1 
ATOM   5896 C C   . GLU B 1 330 ? -5.629  25.598  -15.273 1   27.44  ? 330 GLU B C   1 
ATOM   5897 O O   . GLU B 1 330 ? -5.666  24.904  -16.257 1   27.21  ? 330 GLU B O   1 
ATOM   5898 C CB  . GLU B 1 330 ? -7.571  25.464  -13.693 1   30.49  ? 330 GLU B CB  1 
ATOM   5899 C CG  . GLU B 1 330 ? -8.268  24.657  -12.601 1   35.14  ? 330 GLU B CG  1 
ATOM   5900 C CD  . GLU B 1 330 ? -9.665  25.115  -12.2   1   39.55  ? 330 GLU B CD  1 
ATOM   5901 O OE1 . GLU B 1 330 ? -9.97   26.315  -12.39  1   35.22  ? 330 GLU B OE1 1 
ATOM   5902 O OE2 . GLU B 1 330 ? -10.46  24.259  -11.703 1   37.39  ? 330 GLU B OE2 1 
ATOM   5903 N N   . LEU B 1 331 ? -5.193  26.847  -15.311 1   28.89  ? 331 LEU B N   1 
ATOM   5904 C CA  . LEU B 1 331 ? -4.639  27.443  -16.513 1   30.66  ? 331 LEU B CA  1 
ATOM   5905 C C   . LEU B 1 331 ? -3.329  26.765  -16.942 1   30.24  ? 331 LEU B C   1 
ATOM   5906 O O   . LEU B 1 331 ? -3.059  26.669  -18.13  1   29.78  ? 331 LEU B O   1 
ATOM   5907 C CB  . LEU B 1 331 ? -4.46   28.94   -16.282 1   32.29  ? 331 LEU B CB  1 
ATOM   5908 C CG  . LEU B 1 331 ? -5.761  29.743  -16.331 1   33.16  ? 331 LEU B CG  1 
ATOM   5909 C CD1 . LEU B 1 331 ? -5.546  31.134  -15.867 1   34.11  ? 331 LEU B CD1 1 
ATOM   5910 C CD2 . LEU B 1 331 ? -6.411  29.696  -17.769 1   35.61  ? 331 LEU B CD2 1 
ATOM   5911 N N   . GLY B 1 332 ? -2.503  26.295  -16.013 1   27.11  ? 332 GLY B N   1 
ATOM   5912 C CA  . GLY B 1 332 ? -1.379  25.416  -16.349 1   27.73  ? 332 GLY B CA  1 
ATOM   5913 C C   . GLY B 1 332 ? -1.788  24.229  -17.215 1   27.42  ? 332 GLY B C   1 
ATOM   5914 O O   . GLY B 1 332 ? -1.15   23.927  -18.239 1   30.37  ? 332 GLY B O   1 
ATOM   5915 N N   . PHE B 1 333 ? -2.838  23.554  -16.771 1   26.44  ? 333 PHE B N   1 
ATOM   5916 C CA  . PHE B 1 333 ? -3.397  22.417  -17.501 1   28.17  ? 333 PHE B CA  1 
ATOM   5917 C C   . PHE B 1 333 ? -3.957  22.906  -18.833 1   27.64  ? 333 PHE B C   1 
ATOM   5918 O O   . PHE B 1 333 ? -3.695  22.247  -19.841 1   26.38  ? 333 PHE B O   1 
ATOM   5919 C CB  . PHE B 1 333 ? -4.417  21.649  -16.653 1   27.41  ? 333 PHE B CB  1 
ATOM   5920 C CG  . PHE B 1 333 ? -3.731  20.821  -15.586 1   31.74  ? 333 PHE B CG  1 
ATOM   5921 C CD1 . PHE B 1 333 ? -3.116  19.619  -15.905 1   35.82  ? 333 PHE B CD1 1 
ATOM   5922 C CD2 . PHE B 1 333 ? -3.591  21.308  -14.276 1   34.93  ? 333 PHE B CD2 1 
ATOM   5923 C CE1 . PHE B 1 333 ? -2.485  18.86   -14.907 1   33.15  ? 333 PHE B CE1 1 
ATOM   5924 C CE2 . PHE B 1 333 ? -2.917  20.565  -13.311 1   35.17  ? 333 PHE B CE2 1 
ATOM   5925 C CZ  . PHE B 1 333 ? -2.365  19.35   -13.633 1   34.74  ? 333 PHE B CZ  1 
ATOM   5926 N N   . HIS B 1 334 ? -4.717  24.011  -18.824 1   27.15  ? 334 HIS B N   1 
ATOM   5927 C CA  . HIS B 1 334 ? -5.315  24.557  -20.04  1   28.55  ? 334 HIS B CA  1 
ATOM   5928 C C   . HIS B 1 334 ? -4.276  24.728  -21.156 1   31.05  ? 334 HIS B C   1 
ATOM   5929 O O   . HIS B 1 334 ? -4.47   24.286  -22.295 1   29.52  ? 334 HIS B O   1 
ATOM   5930 C CB  . HIS B 1 334 ? -5.951  25.921  -19.743 1   29.32  ? 334 HIS B CB  1 
ATOM   5931 C CG  . HIS B 1 334 ? -6.587  26.559  -20.928 1   31.64  ? 334 HIS B CG  1 
ATOM   5932 N ND1 . HIS B 1 334 ? -7.898  26.301  -21.237 1   32.23  ? 334 HIS B ND1 1 
ATOM   5933 C CD2 . HIS B 1 334 ? -6.132  27.405  -21.852 1   33.5   ? 334 HIS B CD2 1 
ATOM   5934 C CE1 . HIS B 1 334 ? -8.226  27.016  -22.31  1   33.66  ? 334 HIS B CE1 1 
ATOM   5935 N NE2 . HIS B 1 334 ? -7.156  27.678  -22.734 1   31.96  ? 334 HIS B NE2 1 
ATOM   5936 N N   . TYR B 1 335 ? -3.193  25.464  -20.835 1   30.12  ? 335 TYR B N   1 
ATOM   5937 C CA  . TYR B 1 335 ? -2.15   25.778  -21.806 1   30.72  ? 335 TYR B CA  1 
ATOM   5938 C C   . TYR B 1 335 ? -1.339  24.538  -22.213 1   29.43  ? 335 TYR B C   1 
ATOM   5939 O O   . TYR B 1 335 ? -0.885  24.447  -23.361 1   28.37  ? 335 TYR B O   1 
ATOM   5940 C CB  . TYR B 1 335 ? -1.379  27.009  -21.304 1   29.85  ? 335 TYR B CB  1 
ATOM   5941 C CG  . TYR B 1 335 ? -2.146  28.295  -21.581 1   30.03  ? 335 TYR B CG  1 
ATOM   5942 C CD1 . TYR B 1 335 ? -2.235  28.835  -22.868 1   34.15  ? 335 TYR B CD1 1 
ATOM   5943 C CD2 . TYR B 1 335 ? -2.841  28.928  -20.571 1   32.33  ? 335 TYR B CD2 1 
ATOM   5944 C CE1 . TYR B 1 335 ? -2.937  30.007  -23.126 1   34.89  ? 335 TYR B CE1 1 
ATOM   5945 C CE2 . TYR B 1 335 ? -3.515  30.109  -20.793 1   35.4   ? 335 TYR B CE2 1 
ATOM   5946 C CZ  . TYR B 1 335 ? -3.582  30.635  -22.079 1   37.46  ? 335 TYR B CZ  1 
ATOM   5947 O OH  . TYR B 1 335 ? -4.272  31.784  -22.195 1   41.03  ? 335 TYR B OH  1 
ATOM   5948 N N   . TYR B 1 336 ? -1.17   23.564  -21.322 1   29.05  ? 336 TYR B N   1 
ATOM   5949 C CA  . TYR B 1 336 ? -0.552  22.306  -21.689 1   28.19  ? 336 TYR B CA  1 
ATOM   5950 C C   . TYR B 1 336 ? -1.377  21.588  -22.762 1   30.67  ? 336 TYR B C   1 
ATOM   5951 O O   . TYR B 1 336 ? -0.813  21.127  -23.787 1   30.02  ? 336 TYR B O   1 
ATOM   5952 C CB  . TYR B 1 336 ? -0.434  21.378  -20.47  1   27.83  ? 336 TYR B CB  1 
ATOM   5953 C CG  . TYR B 1 336 ? 0.214   20.04   -20.786 1   28.51  ? 336 TYR B CG  1 
ATOM   5954 C CD1 . TYR B 1 336 ? 1.558   19.966  -21.11  1   31.44  ? 336 TYR B CD1 1 
ATOM   5955 C CD2 . TYR B 1 336 ? -0.519  18.862  -20.822 1   29.47  ? 336 TYR B CD2 1 
ATOM   5956 C CE1 . TYR B 1 336 ? 2.14    18.768  -21.495 1   28.97  ? 336 TYR B CE1 1 
ATOM   5957 C CE2 . TYR B 1 336 ? 0.06    17.657  -21.169 1   30.25  ? 336 TYR B CE2 1 
ATOM   5958 C CZ  . TYR B 1 336 ? 1.39    17.611  -21.494 1   30.55  ? 336 TYR B CZ  1 
ATOM   5959 O OH  . TYR B 1 336 ? 2       16.455  -21.803 1   30.87  ? 336 TYR B OH  1 
ATOM   5960 N N   . LEU B 1 337 ? -2.708  21.498  -22.539 1   30.83  ? 337 LEU B N   1 
ATOM   5961 C CA  . LEU B 1 337 ? -3.602  20.915  -23.559 1   32.56  ? 337 LEU B CA  1 
ATOM   5962 C C   . LEU B 1 337 ? -3.505  21.7    -24.861 1   34.99  ? 337 LEU B C   1 
ATOM   5963 O O   . LEU B 1 337 ? -3.422  21.098  -25.928 1   35.84  ? 337 LEU B O   1 
ATOM   5964 C CB  . LEU B 1 337 ? -5.05   20.887  -23.092 1   35.05  ? 337 LEU B CB  1 
ATOM   5965 C CG  . LEU B 1 337 ? -5.343  20.037  -21.851 1   32.95  ? 337 LEU B CG  1 
ATOM   5966 C CD1 . LEU B 1 337 ? -6.763  20.241  -21.383 1   32.5   ? 337 LEU B CD1 1 
ATOM   5967 C CD2 . LEU B 1 337 ? -5.056  18.586  -22.132 1   33.07  ? 337 LEU B CD2 1 
ATOM   5968 N N   . LYS B 1 338 ? -3.502  23.034  -24.756 1   34.18  ? 338 LYS B N   1 
ATOM   5969 C CA  . LYS B 1 338 ? -3.435  23.893  -25.941 1   35.05  ? 338 LYS B CA  1 
ATOM   5970 C C   . LYS B 1 338 ? -2.19   23.597  -26.77  1   33.97  ? 338 LYS B C   1 
ATOM   5971 O O   . LYS B 1 338 ? -2.241  23.536  -27.995 1   34.84  ? 338 LYS B O   1 
ATOM   5972 C CB  . LYS B 1 338 ? -3.447  25.373  -25.575 1   36.8   ? 338 LYS B CB  1 
ATOM   5973 C CG  . LYS B 1 338 ? -3.613  26.327  -26.77  1   37.86  ? 338 LYS B CG  1 
ATOM   5974 C CD  . LYS B 1 338 ? -4.097  27.701  -26.329 1   39.86  ? 338 LYS B CD  1 
ATOM   5975 C CE  . LYS B 1 338 ? -4.735  28.46   -27.486 1   46.15  ? 338 LYS B CE  1 
ATOM   5976 N NZ  . LYS B 1 338 ? -5.138  29.78   -26.985 1   48.86  ? 338 LYS B NZ  1 
ATOM   5977 N N   . GLY B 1 339 ? -1.062  23.464  -26.088 1   33.93  ? 339 GLY B N   1 
ATOM   5978 C CA  . GLY B 1 339 ? 0.212   23.055  -26.652 1   32.45  ? 339 GLY B CA  1 
ATOM   5979 C C   . GLY B 1 339 ? 0.164   21.725  -27.365 1   32.32  ? 339 GLY B C   1 
ATOM   5980 O O   . GLY B 1 339 ? 0.687   21.609  -28.467 1   36.16  ? 339 GLY B O   1 
ATOM   5981 N N   . LEU B 1 340 ? -0.437  20.71   -26.726 1   31.29  ? 340 LEU B N   1 
ATOM   5982 C CA  . LEU B 1 340 ? -0.563  19.402  -27.343 1   32.47  ? 340 LEU B CA  1 
ATOM   5983 C C   . LEU B 1 340 ? -1.395  19.506  -28.625 1   34.22  ? 340 LEU B C   1 
ATOM   5984 O O   . LEU B 1 340 ? -1.034  18.84   -29.588 1   32.88  ? 340 LEU B O   1 
ATOM   5985 C CB  . LEU B 1 340 ? -1.148  18.338  -26.413 1   32.14  ? 340 LEU B CB  1 
ATOM   5986 C CG  . LEU B 1 340 ? -0.306  17.939  -25.2   1   31.47  ? 340 LEU B CG  1 
ATOM   5987 C CD1 . LEU B 1 340 ? -1.105  16.967  -24.333 1   33.23  ? 340 LEU B CD1 1 
ATOM   5988 C CD2 . LEU B 1 340 ? 1.022   17.322  -25.563 1   33.45  ? 340 LEU B CD2 1 
ATOM   5989 N N   . ILE B 1 341 ? -2.442  20.361  -28.64  1   35.79  ? 341 ILE B N   1 
ATOM   5990 C CA  . ILE B 1 341 ? -3.323  20.482  -29.796 1   39.55  ? 341 ILE B CA  1 
ATOM   5991 C C   . ILE B 1 341 ? -2.618  21.262  -30.926 1   43.24  ? 341 ILE B C   1 
ATOM   5992 O O   . ILE B 1 341 ? -2.697  20.837  -32.071 1   44.39  ? 341 ILE B O   1 
ATOM   5993 C CB  . ILE B 1 341 ? -4.659  21.134  -29.394 1   38.44  ? 341 ILE B CB  1 
ATOM   5994 C CG1 . ILE B 1 341 ? -5.448  20.258  -28.433 1   38.47  ? 341 ILE B CG1 1 
ATOM   5995 C CG2 . ILE B 1 341 ? -5.505  21.521  -30.62  1   41.31  ? 341 ILE B CG2 1 
ATOM   5996 C CD1 . ILE B 1 341 ? -6.473  21.005  -27.598 1   40.26  ? 341 ILE B CD1 1 
ATOM   5997 N N   . THR B 1 342 ? -2.013  22.424  -30.604 1   39.83  ? 342 THR B N   1 
ATOM   5998 C CA  . THR B 1 342 ? -1.53   23.393  -31.596 1   40.85  ? 342 THR B CA  1 
ATOM   5999 C C   . THR B 1 342 ? -0.05   23.216  -31.926 1   41.37  ? 342 THR B C   1 
ATOM   6000 O O   . THR B 1 342 ? 0.403   23.75   -32.935 1   39.82  ? 342 THR B O   1 
ATOM   6001 C CB  . THR B 1 342 ? -1.798  24.815  -31.114 1   42     ? 342 THR B CB  1 
ATOM   6002 O OG1 . THR B 1 342 ? -0.995  25.053  -29.944 1   39.49  ? 342 THR B OG1 1 
ATOM   6003 C CG2 . THR B 1 342 ? -3.271  25.07   -30.856 1   39.74  ? 342 THR B CG2 1 
ATOM   6004 N N   . ASN B 1 343 ? 0.715   22.507  -31.096 1   40.23  ? 343 ASN B N   1 
ATOM   6005 C CA  . ASN B 1 343 ? 2.155   22.377  -31.255 1   45.95  ? 343 ASN B CA  1 
ATOM   6006 C C   . ASN B 1 343 ? 2.907   23.722  -31.161 1   47.04  ? 343 ASN B C   1 
ATOM   6007 O O   . ASN B 1 343 ? 4.031   23.826  -31.646 1   45.02  ? 343 ASN B O   1 
ATOM   6008 C CB  . ASN B 1 343 ? 2.497   21.654  -32.548 1   52.16  ? 343 ASN B CB  1 
ATOM   6009 C CG  . ASN B 1 343 ? 3.811   20.934  -32.42  1   59.61  ? 343 ASN B CG  1 
ATOM   6010 O OD1 . ASN B 1 343 ? 4.844   21.409  -32.898 1   74.37  ? 343 ASN B OD1 1 
ATOM   6011 N ND2 . ASN B 1 343 ? 3.794   19.801  -31.748 1   62.44  ? 343 ASN B ND2 1 
ATOM   6012 N N   . GLU B 1 344 ? 2.326   24.722  -30.474 1   44.14  ? 344 GLU B N   1 
ATOM   6013 C CA  . GLU B 1 344 ? 2.931   26.042  -30.288 1   45.48  ? 344 GLU B CA  1 
ATOM   6014 C C   . GLU B 1 344 ? 3.756   26.019  -29.006 1   43.38  ? 344 GLU B C   1 
ATOM   6015 O O   . GLU B 1 344 ? 3.218   25.749  -27.934 1   40.98  ? 344 GLU B O   1 
ATOM   6016 C CB  . GLU B 1 344 ? 1.874   27.149  -30.186 1   44.62  ? 344 GLU B CB  1 
ATOM   6017 C CG  . GLU B 1 344 ? 1.165   27.391  -31.524 1   51.15  ? 344 GLU B CG  1 
ATOM   6018 C CD  . GLU B 1 344 ? 2.038   28.025  -32.611 1   57.07  ? 344 GLU B CD  1 
ATOM   6019 O OE1 . GLU B 1 344 ? 3.104   28.57   -32.264 1   59.24  ? 344 GLU B OE1 1 
ATOM   6020 O OE2 . GLU B 1 344 ? 1.683   27.941  -33.81  1   62.17  ? 344 GLU B OE2 1 
ATOM   6021 N N   . LYS B 1 345 ? 5.051   26.323  -29.105 1   38.57  ? 345 LYS B N   1 
ATOM   6022 C CA  . LYS B 1 345 ? 5.884   26.5    -27.921 1   39.61  ? 345 LYS B CA  1 
ATOM   6023 C C   . LYS B 1 345 ? 5.292   27.547  -26.99  1   39.22  ? 345 LYS B C   1 
ATOM   6024 O O   . LYS B 1 345 ? 5.387   27.342  -25.768 1   35.35  ? 345 LYS B O   1 
ATOM   6025 C CB  . LYS B 1 345 ? 7.289   26.953  -28.274 1   39.49  ? 345 LYS B CB  1 
ATOM   6026 C CG  . LYS B 1 345 ? 8.129   25.858  -28.815 1   40.49  ? 345 LYS B CG  1 
ATOM   6027 C CD  . LYS B 1 345 ? 9.449   26.446  -29.269 1   41.61  ? 345 LYS B CD  1 
ATOM   6028 C CE  . LYS B 1 345 ? 10.368  25.346  -29.524 1   41.15  ? 345 LYS B CE  1 
ATOM   6029 N NZ  . LYS B 1 345 ? 11.584  25.975  -29.995 1   42.23  ? 345 LYS B NZ  1 
ATOM   6030 N N   . GLU B 1 346 ? 4.684   28.626  -27.547 1   35.46  ? 346 GLU B N   1 
ATOM   6031 C CA  . GLU B 1 346 ? 4.072   29.675  -26.738 1   38.97  ? 346 GLU B CA  1 
ATOM   6032 C C   . GLU B 1 346 ? 3.156   29.071  -25.653 1   35.45  ? 346 GLU B C   1 
ATOM   6033 O O   . GLU B 1 346 ? 3.213   29.482  -24.47  1   31.9   ? 346 GLU B O   1 
ATOM   6034 C CB  . GLU B 1 346 ? 3.385   30.745  -27.598 1   38.87  ? 346 GLU B CB  1 
ATOM   6035 C CG  . GLU B 1 346 ? 2.652   31.836  -26.807 1   40.98  ? 346 GLU B CG  1 
ATOM   6036 C CD  . GLU B 1 346 ? 3.49    32.668  -25.826 1   41.92  ? 346 GLU B CD  1 
ATOM   6037 O OE1 . GLU B 1 346 ? 4.703   32.796  -26.044 1   41.72  ? 346 GLU B OE1 1 
ATOM   6038 O OE2 . GLU B 1 346 ? 2.969   33.152  -24.786 1   40.11  ? 346 GLU B OE2 1 
ATOM   6039 N N   . ALA B 1 347 ? 2.284   28.136  -26.062 1   32.49  ? 347 ALA B N   1 
ATOM   6040 C CA  . ALA B 1 347 ? 1.333   27.588  -25.109 1   33.27  ? 347 ALA B CA  1 
ATOM   6041 C C   . ALA B 1 347 ? 2.068   26.808  -24.003 1   32.43  ? 347 ALA B C   1 
ATOM   6042 O O   . ALA B 1 347 ? 1.664   26.862  -22.832 1   32.45  ? 347 ALA B O   1 
ATOM   6043 C CB  . ALA B 1 347 ? 0.314   26.724  -25.836 1   35.95  ? 347 ALA B CB  1 
ATOM   6044 N N   . PHE B 1 348 ? 3.111   26.053  -24.346 1   28.52  ? 348 PHE B N   1 
ATOM   6045 C CA  . PHE B 1 348 ? 3.889   25.363  -23.315 1   28.49  ? 348 PHE B CA  1 
ATOM   6046 C C   . PHE B 1 348 ? 4.631   26.315  -22.38  1   29.69  ? 348 PHE B C   1 
ATOM   6047 O O   . PHE B 1 348 ? 4.66    26.075  -21.161 1   30.14  ? 348 PHE B O   1 
ATOM   6048 C CB  . PHE B 1 348 ? 4.848   24.367  -23.966 1   30.21  ? 348 PHE B CB  1 
ATOM   6049 C CG  . PHE B 1 348 ? 4.161   23.167  -24.61  1   29.49  ? 348 PHE B CG  1 
ATOM   6050 C CD1 . PHE B 1 348 ? 3.274   22.353  -23.888 1   30.26  ? 348 PHE B CD1 1 
ATOM   6051 C CD2 . PHE B 1 348 ? 4.345   22.912  -25.971 1   32.14  ? 348 PHE B CD2 1 
ATOM   6052 C CE1 . PHE B 1 348 ? 2.648   21.282  -24.515 1   31.49  ? 348 PHE B CE1 1 
ATOM   6053 C CE2 . PHE B 1 348 ? 3.716   21.84   -26.586 1   33.36  ? 348 PHE B CE2 1 
ATOM   6054 C CZ  . PHE B 1 348 ? 2.888   21.013  -25.86  1   33.68  ? 348 PHE B CZ  1 
ATOM   6055 N N   . PHE B 1 349 ? 5.145   27.435  -22.902 1   29.35  ? 349 PHE B N   1 
ATOM   6056 C CA  . PHE B 1 349 ? 5.775   28.449  -22.074 1   29.21  ? 349 PHE B CA  1 
ATOM   6057 C C   . PHE B 1 349 ? 4.762   29.015  -21.084 1   31.29  ? 349 PHE B C   1 
ATOM   6058 O O   . PHE B 1 349 ? 5.109   29.179  -19.91  1   30.28  ? 349 PHE B O   1 
ATOM   6059 C CB  . PHE B 1 349 ? 6.374   29.593  -22.898 1   32.57  ? 349 PHE B CB  1 
ATOM   6060 C CG  . PHE B 1 349 ? 7.559   29.228  -23.788 1   34.72  ? 349 PHE B CG  1 
ATOM   6061 C CD1 . PHE B 1 349 ? 8.628   28.479  -23.313 1   35.75  ? 349 PHE B CD1 1 
ATOM   6062 C CD2 . PHE B 1 349 ? 7.688   29.806  -25.052 1   36.27  ? 349 PHE B CD2 1 
ATOM   6063 C CE1 . PHE B 1 349 ? 9.718   28.213  -24.138 1   36.54  ? 349 PHE B CE1 1 
ATOM   6064 C CE2 . PHE B 1 349 ? 8.779   29.541  -25.865 1   37.45  ? 349 PHE B CE2 1 
ATOM   6065 C CZ  . PHE B 1 349 ? 9.776   28.717  -25.417 1   37.43  ? 349 PHE B CZ  1 
ATOM   6066 N N   . LYS B 1 350 ? 3.536   29.347  -21.551 1   30.84  ? 350 LYS B N   1 
ATOM   6067 C CA  . LYS B 1 350 ? 2.479   29.816  -20.661 1   32.97  ? 350 LYS B CA  1 
ATOM   6068 C C   . LYS B 1 350 ? 2.143   28.771  -19.588 1   28.86  ? 350 LYS B C   1 
ATOM   6069 O O   . LYS B 1 350 ? 1.944   29.145  -18.434 1   27.66  ? 350 LYS B O   1 
ATOM   6070 C CB  . LYS B 1 350 ? 1.161   30.133  -21.383 1   37.61  ? 350 LYS B CB  1 
ATOM   6071 C CG  . LYS B 1 350 ? 1.164   31.317  -22.321 1   45.7   ? 350 LYS B CG  1 
ATOM   6072 C CD  . LYS B 1 350 ? 0.395   32.562  -21.877 1   55.05  ? 350 LYS B CD  1 
ATOM   6073 C CE  . LYS B 1 350 ? -0.371  33.274  -22.98  1   60     ? 350 LYS B CE  1 
ATOM   6074 N NZ  . LYS B 1 350 ? 0.084   33.067  -24.363 1   60.86  ? 350 LYS B NZ  1 
ATOM   6075 N N   . SER B 1 351 ? 2.052   27.518  -19.989 1   27.19  ? 351 SER B N   1 
ATOM   6076 C CA  . SER B 1 351 ? 1.791   26.424  -19.053 1   29.55  ? 351 SER B CA  1 
ATOM   6077 C C   . SER B 1 351 ? 2.82    26.398  -17.908 1   28.92  ? 351 SER B C   1 
ATOM   6078 O O   . SER B 1 351 ? 2.447   26.342  -16.725 1   26.94  ? 351 SER B O   1 
ATOM   6079 C CB  . SER B 1 351 ? 1.732   25.118  -19.792 1   27.78  ? 351 SER B CB  1 
ATOM   6080 O OG  . SER B 1 351 ? 1.454   24.04   -18.896 1   26.87  ? 351 SER B OG  1 
ATOM   6081 N N   . VAL B 1 352 ? 4.103   26.546  -18.282 1   28.25  ? 352 VAL B N   1 
ATOM   6082 C CA  . VAL B 1 352 ? 5.223   26.659  -17.345 1   27.03  ? 352 VAL B CA  1 
ATOM   6083 C C   . VAL B 1 352 ? 4.982   27.815  -16.401 1   27.37  ? 352 VAL B C   1 
ATOM   6084 O O   . VAL B 1 352 ? 5.128   27.648  -15.194 1   26.69  ? 352 VAL B O   1 
ATOM   6085 C CB  . VAL B 1 352 ? 6.61    26.719  -18.013 1   28.57  ? 352 VAL B CB  1 
ATOM   6086 C CG1 . VAL B 1 352 ? 7.701   26.95   -16.986 1   30.03  ? 352 VAL B CG1 1 
ATOM   6087 C CG2 . VAL B 1 352 ? 6.923   25.436  -18.775 1   28.04  ? 352 VAL B CG2 1 
ATOM   6088 N N   . GLU B 1 353 ? 4.612   28.983  -16.947 1   27.35  ? 353 GLU B N   1 
ATOM   6089 C CA  . GLU B 1 353 ? 4.488   30.201  -16.152 1   27.29  ? 353 GLU B CA  1 
ATOM   6090 C C   . GLU B 1 353 ? 3.358   30.043  -15.138 1   30.18  ? 353 GLU B C   1 
ATOM   6091 O O   . GLU B 1 353 ? 3.492   30.478  -13.982 1   26.11  ? 353 GLU B O   1 
ATOM   6092 C CB  . GLU B 1 353 ? 4.281   31.419  -17.064 1   27.16  ? 353 GLU B CB  1 
ATOM   6093 C CG  . GLU B 1 353 ? 5.55    31.787  -17.805 1   28.01  ? 353 GLU B CG  1 
ATOM   6094 C CD  . GLU B 1 353 ? 5.367   32.807  -18.916 1   33.35  ? 353 GLU B CD  1 
ATOM   6095 O OE1 . GLU B 1 353 ? 4.374   32.704  -19.687 1   34.12  ? 353 GLU B OE1 1 
ATOM   6096 O OE2 . GLU B 1 353 ? 6.339   33.55   -19.122 1   33.57  ? 353 GLU B OE2 1 
ATOM   6097 N N   . TYR B 1 354 ? 2.242   29.435  -15.574 1   29.55  ? 354 TYR B N   1 
ATOM   6098 C CA  . TYR B 1 354 ? 1.117   29.221  -14.672 1   27.55  ? 354 TYR B CA  1 
ATOM   6099 C C   . TYR B 1 354 ? 1.484   28.252  -13.572 1   26.66  ? 354 TYR B C   1 
ATOM   6100 O O   . TYR B 1 354 ? 1.047   28.469  -12.442 1   28.52  ? 354 TYR B O   1 
ATOM   6101 C CB  . TYR B 1 354 ? -0.156  28.824  -15.41  1   28.89  ? 354 TYR B CB  1 
ATOM   6102 C CG  . TYR B 1 354 ? -0.873  30.004  -16.042 1   31.64  ? 354 TYR B CG  1 
ATOM   6103 C CD1 . TYR B 1 354 ? -1.473  30.967  -15.242 1   32.77  ? 354 TYR B CD1 1 
ATOM   6104 C CD2 . TYR B 1 354 ? -0.945  30.149  -17.423 1   35.12  ? 354 TYR B CD2 1 
ATOM   6105 C CE1 . TYR B 1 354 ? -2.125  32.057  -15.795 1   36.08  ? 354 TYR B CE1 1 
ATOM   6106 C CE2 . TYR B 1 354 ? -1.608  31.224  -17.994 1   35.38  ? 354 TYR B CE2 1 
ATOM   6107 C CZ  . TYR B 1 354 ? -2.195  32.171  -17.177 1   37.46  ? 354 TYR B CZ  1 
ATOM   6108 O OH  . TYR B 1 354 ? -2.828  33.248  -17.7   1   40.89  ? 354 TYR B OH  1 
ATOM   6109 N N   . PHE B 1 355 ? 2.237   27.2    -13.887 1   26.25  ? 355 PHE B N   1 
ATOM   6110 C CA  . PHE B 1 355 ? 2.657   26.268  -12.845 1   25.68  ? 355 PHE B CA  1 
ATOM   6111 C C   . PHE B 1 355 ? 3.65    26.9    -11.881 1   26.75  ? 355 PHE B C   1 
ATOM   6112 O O   . PHE B 1 355 ? 3.559   26.629  -10.687 1   26.67  ? 355 PHE B O   1 
ATOM   6113 C CB  . PHE B 1 355 ? 3.178   24.935  -13.377 1   26.62  ? 355 PHE B CB  1 
ATOM   6114 C CG  . PHE B 1 355 ? 2.079   24.067  -13.973 1   26.81  ? 355 PHE B CG  1 
ATOM   6115 C CD1 . PHE B 1 355 ? 0.913   23.784  -13.274 1   25.55  ? 355 PHE B CD1 1 
ATOM   6116 C CD2 . PHE B 1 355 ? 2.201   23.535  -15.243 1   26.85  ? 355 PHE B CD2 1 
ATOM   6117 C CE1 . PHE B 1 355 ? -0.074  22.963  -13.823 1   26.55  ? 355 PHE B CE1 1 
ATOM   6118 C CE2 . PHE B 1 355 ? 1.206   22.723  -15.78  1   24.9   ? 355 PHE B CE2 1 
ATOM   6119 C CZ  . PHE B 1 355 ? 0.088   22.419  -15.068 1   26.4   ? 355 PHE B CZ  1 
ATOM   6120 N N   . LYS B 1 356 ? 4.528   27.787  -12.355 1   27.6   ? 356 LYS B N   1 
ATOM   6121 C CA  . LYS B 1 356 ? 5.369   28.577  -11.491 1   28.7   ? 356 LYS B CA  1 
ATOM   6122 C C   . LYS B 1 356 ? 4.537   29.475  -10.596 1   30.95  ? 356 LYS B C   1 
ATOM   6123 O O   . LYS B 1 356 ? 4.805   29.574  -9.382  1   28.07  ? 356 LYS B O   1 
ATOM   6124 C CB  . LYS B 1 356 ? 6.309   29.439  -12.353 1   32.96  ? 356 LYS B CB  1 
ATOM   6125 C CG  . LYS B 1 356 ? 7.501   28.663  -12.832 1   33.61  ? 356 LYS B CG  1 
ATOM   6126 C CD  . LYS B 1 356 ? 8.599   28.697  -11.765 1   37.62  ? 356 LYS B CD  1 
ATOM   6127 C CE  . LYS B 1 356 ? 9.614   27.679  -12.097 1   35.37  ? 356 LYS B CE  1 
ATOM   6128 N NZ  . LYS B 1 356 ? 10.79   27.943  -11.274 1   31.74  ? 356 LYS B NZ  1 
ATOM   6129 N N   . ALA B 1 357 ? 3.531   30.128  -11.178 1   28.84  ? 357 ALA B N   1 
ATOM   6130 C CA  . ALA B 1 357 ? 2.711   31.045  -10.39  1   32.06  ? 357 ALA B CA  1 
ATOM   6131 C C   . ALA B 1 357 ? 1.916   30.312  -9.309  1   30.45  ? 357 ALA B C   1 
ATOM   6132 O O   . ALA B 1 357 ? 1.814   30.793  -8.176  1   29.81  ? 357 ALA B O   1 
ATOM   6133 C CB  . ALA B 1 357 ? 1.795   31.834  -11.302 1   32.69  ? 357 ALA B CB  1 
ATOM   6134 N N   . SER B 1 358 ? 1.369   29.13   -9.63   1   26.96  ? 358 SER B N   1 
ATOM   6135 C CA  . SER B 1 358 ? 0.684   28.332  -8.619  1   25.82  ? 358 SER B CA  1 
ATOM   6136 C C   . SER B 1 358 ? 1.636   27.59   -7.657  1   27.63  ? 358 SER B C   1 
ATOM   6137 O O   . SER B 1 358 ? 1.153   27.014  -6.7    1   25.62  ? 358 SER B O   1 
ATOM   6138 C CB  . SER B 1 358 ? -0.278  27.389  -9.275  1   30.08  ? 358 SER B CB  1 
ATOM   6139 O OG  . SER B 1 358 ? 0.349   26.52   -10.175 1   34.27  ? 358 SER B OG  1 
ATOM   6140 N N   . GLN B 1 359 ? 2.959   27.612  -7.888  1   27.34  ? 359 GLN B N   1 
ATOM   6141 C CA  . GLN B 1 359 ? 3.992   26.9    -7.134  1   28.47  ? 359 GLN B CA  1 
ATOM   6142 C C   . GLN B 1 359 ? 3.702   25.398  -7.159  1   32.78  ? 359 GLN B C   1 
ATOM   6143 O O   . GLN B 1 359 ? 3.733   24.702  -6.124  1   25.88  ? 359 GLN B O   1 
ATOM   6144 C CB  . GLN B 1 359 ? 4.26    27.513  -5.758  1   29.32  ? 359 GLN B CB  1 
ATOM   6145 C CG  . GLN B 1 359 ? 5.663   27.232  -5.235  1   30.72  ? 359 GLN B CG  1 
ATOM   6146 C CD  . GLN B 1 359 ? 5.848   27.732  -3.824  1   33.32  ? 359 GLN B CD  1 
ATOM   6147 O OE1 . GLN B 1 359 ? 6.047   28.924  -3.568  1   36.18  ? 359 GLN B OE1 1 
ATOM   6148 N NE2 . GLN B 1 359 ? 5.661   26.843  -2.873  1   35.55  ? 359 GLN B NE2 1 
ATOM   6149 N N   . ASP B 1 360 ? 3.427   24.917  -8.372  1   28.62  ? 360 ASP B N   1 
ATOM   6150 C CA  . ASP B 1 360 ? 3.235   23.507  -8.618  1   28.69  ? 360 ASP B CA  1 
ATOM   6151 C C   . ASP B 1 360 ? 4.514   22.974  -9.255  1   30.31  ? 360 ASP B C   1 
ATOM   6152 O O   . ASP B 1 360 ? 4.655   23.027  -10.459 1   30.73  ? 360 ASP B O   1 
ATOM   6153 C CB  . ASP B 1 360 ? 1.97    23.264  -9.412  1   27.54  ? 360 ASP B CB  1 
ATOM   6154 C CG  . ASP B 1 360 ? 1.595   21.806  -9.644  1   26.71  ? 360 ASP B CG  1 
ATOM   6155 O OD1 . ASP B 1 360 ? 2.419   20.919  -9.321  1   28.08  ? 360 ASP B OD1 1 
ATOM   6156 O OD2 . ASP B 1 360 ? 0.454   21.558  -10.144 1   29.54  ? 360 ASP B OD2 1 
ATOM   6157 N N   . LYS B 1 361 ? 5.358   22.32   -8.456  1   25.6   ? 361 LYS B N   1 
ATOM   6158 C CA  . LYS B 1 361 ? 6.581   21.722  -8.937  1   26.72  ? 361 LYS B CA  1 
ATOM   6159 C C   . LYS B 1 361 ? 6.402   20.305  -9.444  1   26.81  ? 361 LYS B C   1 
ATOM   6160 O O   . LYS B 1 361 ? 7.356   19.73   -9.953  1   30.37  ? 361 LYS B O   1 
ATOM   6161 C CB  . LYS B 1 361 ? 7.64    21.71   -7.835  1   29.54  ? 361 LYS B CB  1 
ATOM   6162 C CG  . LYS B 1 361 ? 8.029   23.074  -7.334  1   35.49  ? 361 LYS B CG  1 
ATOM   6163 C CD  . LYS B 1 361 ? 9.307   22.963  -6.492  1   41.77  ? 361 LYS B CD  1 
ATOM   6164 C CE  . LYS B 1 361 ? 10.13   24.163  -6.413  1   49.58  ? 361 LYS B CE  1 
ATOM   6165 N NZ  . LYS B 1 361 ? 9.409   25.175  -5.627  1   55.55  ? 361 LYS B NZ  1 
ATOM   6166 N N   . LEU B 1 362 ? 5.212   19.717  -9.278  1   25.96  ? 362 LEU B N   1 
ATOM   6167 C CA  . LEU B 1 362 ? 4.942   18.392  -9.808  1   28.86  ? 362 LEU B CA  1 
ATOM   6168 C C   . LEU B 1 362 ? 4.49    18.5    -11.273 1   28.38  ? 362 LEU B C   1 
ATOM   6169 O O   . LEU B 1 362 ? 5.105   17.937  -12.181 1   30.23  ? 362 LEU B O   1 
ATOM   6170 C CB  . LEU B 1 362 ? 3.864   17.8    -8.914  1   28.05  ? 362 LEU B CB  1 
ATOM   6171 C CG  . LEU B 1 362 ? 3.387   16.412  -9.324  1   32.45  ? 362 LEU B CG  1 
ATOM   6172 C CD1 . LEU B 1 362 ? 4.518   15.398  -9.169  1   36.38  ? 362 LEU B CD1 1 
ATOM   6173 C CD2 . LEU B 1 362 ? 2.148   16.032  -8.599  1   35.69  ? 362 LEU B CD2 1 
ATOM   6174 N N   . SER B 1 363 ? 3.419   19.274  -11.498 1   29.04  ? 363 SER B N   1 
ATOM   6175 C CA  . SER B 1 363 ? 2.747   19.309  -12.8   1   28.12  ? 363 SER B CA  1 
ATOM   6176 C C   . SER B 1 363 ? 3.615   19.997  -13.847 1   26.66  ? 363 SER B C   1 
ATOM   6177 O O   . SER B 1 363 ? 3.446   19.708  -15.024 1   26.38  ? 363 SER B O   1 
ATOM   6178 C CB  . SER B 1 363 ? 1.379   19.95   -12.746 1   28.96  ? 363 SER B CB  1 
ATOM   6179 O OG  . SER B 1 363 ? 0.532   19.385  -11.754 1   27.13  ? 363 SER B OG  1 
ATOM   6180 N N   . ILE B 1 364 ? 4.562   20.847  -13.424 1   26.72  ? 364 ILE B N   1 
ATOM   6181 C CA  . ILE B 1 364 ? 5.413   21.628  -14.309 1   26.69  ? 364 ILE B CA  1 
ATOM   6182 C C   . ILE B 1 364 ? 6.245   20.742  -15.231 1   28.04  ? 364 ILE B C   1 
ATOM   6183 O O   . ILE B 1 364 ? 6.618   21.169  -16.313 1   26.78  ? 364 ILE B O   1 
ATOM   6184 C CB  . ILE B 1 364 ? 6.3     22.607  -13.529 1   28.67  ? 364 ILE B CB  1 
ATOM   6185 C CG1 . ILE B 1 364 ? 6.869   23.751  -14.468 1   26.58  ? 364 ILE B CG1 1 
ATOM   6186 C CG2 . ILE B 1 364 ? 7.433   21.917  -12.752 1   28.17  ? 364 ILE B CG2 1 
ATOM   6187 C CD1 . ILE B 1 364 ? 7.543   24.846  -13.68  1   27.06  ? 364 ILE B CD1 1 
ATOM   6188 N N   . LYS B 1 365 ? 6.535   19.51   -14.813 1   27.97  ? 365 LYS B N   1 
ATOM   6189 C CA  . LYS B 1 365 ? 7.269   18.567  -15.628 1   32.84  ? 365 LYS B CA  1 
ATOM   6190 C C   . LYS B 1 365 ? 6.561   18.328  -16.965 1   30.65  ? 365 LYS B C   1 
ATOM   6191 O O   . LYS B 1 365 ? 7.244   18.085  -17.953 1   31.57  ? 365 LYS B O   1 
ATOM   6192 C CB  . LYS B 1 365 ? 7.412   17.191  -14.953 1   41.11  ? 365 LYS B CB  1 
ATOM   6193 C CG  . LYS B 1 365 ? 8.127   17.128  -13.601 1   64.03  ? 365 LYS B CG  1 
ATOM   6194 C CD  . LYS B 1 365 ? 8.001   15.778  -12.871 1   71.37  ? 365 LYS B CD  1 
ATOM   6195 C CE  . LYS B 1 365 ? 7.904   15.935  -11.341 1   72.79  ? 365 LYS B CE  1 
ATOM   6196 N NZ  . LYS B 1 365 ? 8.058   14.711  -10.52  1   60.06  ? 365 LYS B NZ  1 
ATOM   6197 N N   . MET B 1 366 ? 5.22    18.385  -17.017 1   26.81  ? 366 MET B N   1 
ATOM   6198 C CA  . MET B 1 366 ? 4.523   18.059  -18.252 1   30.54  ? 366 MET B CA  1 
ATOM   6199 C C   . MET B 1 366 ? 4.931   19      -19.394 1   31.13  ? 366 MET B C   1 
ATOM   6200 O O   . MET B 1 366 ? 5.433   18.501  -20.409 1   28.85  ? 366 MET B O   1 
ATOM   6201 C CB  . MET B 1 366 ? 3.016   18.068  -18.079 1   31.21  ? 366 MET B CB  1 
ATOM   6202 C CG  . MET B 1 366 ? 2.468   17.066  -17.05  1   33.68  ? 366 MET B CG  1 
ATOM   6203 S SD  . MET B 1 366 ? 0.663   17.139  -17.089 1   38.2   ? 366 MET B SD  1 
ATOM   6204 C CE  . MET B 1 366 ? 0.303   18.889  -16.838 1   43.71  ? 366 MET B CE  1 
ATOM   6205 N N   . PRO B 1 367 ? 4.736   20.347  -19.305 1   25.83  ? 367 PRO B N   1 
ATOM   6206 C CA  . PRO B 1 367 ? 5.149   21.234  -20.393 1   26.68  ? 367 PRO B CA  1 
ATOM   6207 C C   . PRO B 1 367 ? 6.657   21.254  -20.594 1   27.98  ? 367 PRO B C   1 
ATOM   6208 O O   . PRO B 1 367 ? 7.071   21.462  -21.731 1   29.13  ? 367 PRO B O   1 
ATOM   6209 C CB  . PRO B 1 367 ? 4.561   22.592  -20.006 1   26.22  ? 367 PRO B CB  1 
ATOM   6210 C CG  . PRO B 1 367 ? 4.441   22.507  -18.492 1   25.76  ? 367 PRO B CG  1 
ATOM   6211 C CD  . PRO B 1 367 ? 3.98    21.103  -18.283 1   23.71  ? 367 PRO B CD  1 
ATOM   6212 N N   . LEU B 1 368 ? 7.453   21.033  -19.528 1   28.29  ? 368 LEU B N   1 
ATOM   6213 C CA  . LEU B 1 368 ? 8.907   21.002  -19.644 1   29.54  ? 368 LEU B CA  1 
ATOM   6214 C C   . LEU B 1 368 ? 9.376   19.871  -20.553 1   29.44  ? 368 LEU B C   1 
ATOM   6215 O O   . LEU B 1 368 ? 10.251  20.091  -21.396 1   29.16  ? 368 LEU B O   1 
ATOM   6216 C CB  . LEU B 1 368 ? 9.627   20.953  -18.283 1   28.68  ? 368 LEU B CB  1 
ATOM   6217 C CG  . LEU B 1 368 ? 9.485   22.236  -17.456 1   29.08  ? 368 LEU B CG  1 
ATOM   6218 C CD1 . LEU B 1 368 ? 10.074  21.992  -16.078 1   28.44  ? 368 LEU B CD1 1 
ATOM   6219 C CD2 . LEU B 1 368 ? 10.104  23.445  -18.097 1   28     ? 368 LEU B CD2 1 
ATOM   6220 N N   . ILE B 1 369 ? 8.817   18.679  -20.373 1   30.16  ? 369 ILE B N   1 
ATOM   6221 C CA  . ILE B 1 369 ? 9.082   17.549  -21.254 1   34.37  ? 369 ILE B CA  1 
ATOM   6222 C C   . ILE B 1 369 ? 8.796   17.886  -22.718 1   33.03  ? 369 ILE B C   1 
ATOM   6223 O O   . ILE B 1 369 ? 9.615   17.567  -23.576 1   33.49  ? 369 ILE B O   1 
ATOM   6224 C CB  . ILE B 1 369 ? 8.293   16.308  -20.803 1   39.31  ? 369 ILE B CB  1 
ATOM   6225 C CG1 . ILE B 1 369 ? 8.874   15.744  -19.491 1   46.52  ? 369 ILE B CG1 1 
ATOM   6226 C CG2 . ILE B 1 369 ? 8.221   15.219  -21.893 1   38.69  ? 369 ILE B CG2 1 
ATOM   6227 C CD1 . ILE B 1 369 ? 7.941   14.751  -18.786 1   49.41  ? 369 ILE B CD1 1 
ATOM   6228 N N   . GLN B 1 370 ? 7.676   18.569  -22.997 1   31.84  ? 370 GLN B N   1 
ATOM   6229 C CA  . GLN B 1 370 ? 7.307   18.895  -24.364 1   33.08  ? 370 GLN B CA  1 
ATOM   6230 C C   . GLN B 1 370 ? 8.29    19.919  -24.94  1   34.32  ? 370 GLN B C   1 
ATOM   6231 O O   . GLN B 1 370 ? 8.702   19.786  -26.097 1   33.37  ? 370 GLN B O   1 
ATOM   6232 C CB  . GLN B 1 370 ? 5.864   19.374  -24.504 1   33.07  ? 370 GLN B CB  1 
ATOM   6233 C CG  . GLN B 1 370 ? 4.814   18.324  -24.122 1   33.66  ? 370 GLN B CG  1 
ATOM   6234 C CD  . GLN B 1 370 ? 4.928   17.011  -24.879 1   33.81  ? 370 GLN B CD  1 
ATOM   6235 O OE1 . GLN B 1 370 ? 5.028   15.916  -24.309 1   36.69  ? 370 GLN B OE1 1 
ATOM   6236 N NE2 . GLN B 1 370 ? 5.07    17.122  -26.167 1   29.87  ? 370 GLN B NE2 1 
ATOM   6237 N N   . LEU B 1 371 ? 8.691   20.914  -24.128 1   30.65  ? 371 LEU B N   1 
ATOM   6238 C CA  . LEU B 1 371 ? 9.676   21.883  -24.582 1   32.02  ? 371 LEU B CA  1 
ATOM   6239 C C   . LEU B 1 371 ? 11.014  21.223  -24.893 1   30.43  ? 371 LEU B C   1 
ATOM   6240 O O   . LEU B 1 371 ? 11.649  21.611  -25.883 1   35.88  ? 371 LEU B O   1 
ATOM   6241 C CB  . LEU B 1 371 ? 9.818   23.023  -23.574 1   31.82  ? 371 LEU B CB  1 
ATOM   6242 C CG  . LEU B 1 371 ? 8.611   23.96   -23.497 1   31.4   ? 371 LEU B CG  1 
ATOM   6243 C CD1 . LEU B 1 371 ? 8.73    24.83   -22.265 1   30.28  ? 371 LEU B CD1 1 
ATOM   6244 C CD2 . LEU B 1 371 ? 8.465   24.772  -24.795 1   31.92  ? 371 LEU B CD2 1 
ATOM   6245 N N   . GLU B 1 372 ? 11.432  20.241  -24.094 1   31.01  ? 372 GLU B N   1 
ATOM   6246 C CA  . GLU B 1 372 ? 12.668  19.5    -24.344 1   34     ? 372 GLU B CA  1 
ATOM   6247 C C   . GLU B 1 372 ? 12.606  18.773  -25.696 1   35.96  ? 372 GLU B C   1 
ATOM   6248 O O   . GLU B 1 372 ? 13.563  18.797  -26.475 1   35.02  ? 372 GLU B O   1 
ATOM   6249 C CB  . GLU B 1 372 ? 12.961  18.497  -23.23  1   34.51  ? 372 GLU B CB  1 
ATOM   6250 C CG  . GLU B 1 372 ? 14.283  17.741  -23.423 1   45.12  ? 372 GLU B CG  1 
ATOM   6251 C CD  . GLU B 1 372 ? 15.127  17.402  -22.201 1   52.08  ? 372 GLU B CD  1 
ATOM   6252 O OE1 . GLU B 1 372 ? 15.033  18.088  -21.154 1   59.87  ? 372 GLU B OE1 1 
ATOM   6253 O OE2 . GLU B 1 372 ? 15.925  16.458  -22.28  1   62.35  ? 372 GLU B OE2 1 
ATOM   6254 N N   . LYS B 1 373 ? 11.471  18.123  -25.963 1   38.43  ? 373 LYS B N   1 
ATOM   6255 C CA  . LYS B 1 373 ? 11.265  17.437  -27.239 1   41.13  ? 373 LYS B CA  1 
ATOM   6256 C C   . LYS B 1 373 ? 11.261  18.424  -28.412 1   37.49  ? 373 LYS B C   1 
ATOM   6257 O O   . LYS B 1 373 ? 11.599  18.041  -29.522 1   41.43  ? 373 LYS B O   1 
ATOM   6258 C CB  . LYS B 1 373 ? 9.919   16.707  -27.267 1   46.17  ? 373 LYS B CB  1 
ATOM   6259 C CG  . LYS B 1 373 ? 9.733   15.603  -26.265 1   54.35  ? 373 LYS B CG  1 
ATOM   6260 C CD  . LYS B 1 373 ? 8.52    14.707  -26.523 1   59.62  ? 373 LYS B CD  1 
ATOM   6261 C CE  . LYS B 1 373 ? 8.447   13.655  -25.466 1   58.87  ? 373 LYS B CE  1 
ATOM   6262 N NZ  . LYS B 1 373 ? 7.11    13.059  -25.46  1   68.02  ? 373 LYS B NZ  1 
ATOM   6263 N N   . MET B 1 374 ? 10.822  19.667  -28.194 1   38.26  ? 374 MET B N   1 
ATOM   6264 C CA  . MET B 1 374 ? 10.763  20.676  -29.234 1   41.15  ? 374 MET B CA  1 
ATOM   6265 C C   . MET B 1 374 ? 12.068  21.467  -29.374 1   41.52  ? 374 MET B C   1 
ATOM   6266 O O   . MET B 1 374 ? 12.044  22.504  -30.034 1   42.2   ? 374 MET B O   1 
ATOM   6267 C CB  . MET B 1 374 ? 9.569   21.599  -28.963 1   43.3   ? 374 MET B CB  1 
ATOM   6268 C CG  . MET B 1 374 ? 8.237   20.897  -29.078 1   43.07  ? 374 MET B CG  1 
ATOM   6269 S SD  . MET B 1 374 ? 6.976   21.82   -28.183 1   43.19  ? 374 MET B SD  1 
ATOM   6270 C CE  . MET B 1 374 ? 6.191   22.75   -29.498 1   41.74  ? 374 MET B CE  1 
ATOM   6271 N N   . GLY B 1 375 ? 13.186  20.999  -28.778 1   38.19  ? 375 GLY B N   1 
ATOM   6272 C CA  . GLY B 1 375 ? 14.494  21.587  -29.007 1   37.43  ? 375 GLY B CA  1 
ATOM   6273 C C   . GLY B 1 375 ? 14.912  22.667  -27.994 1   37.81  ? 375 GLY B C   1 
ATOM   6274 O O   . GLY B 1 375 ? 15.963  23.252  -28.181 1   36.82  ? 375 GLY B O   1 
ATOM   6275 N N   . GLU B 1 376 ? 14.162  22.941  -26.914 1   36.93  ? 376 GLU B N   1 
ATOM   6276 C CA  . GLU B 1 376 ? 14.628  23.923  -25.927 1   35.72  ? 376 GLU B CA  1 
ATOM   6277 C C   . GLU B 1 376 ? 15.811  23.381  -25.111 1   34.37  ? 376 GLU B C   1 
ATOM   6278 O O   . GLU B 1 376 ? 15.922  22.176  -24.891 1   32.79  ? 376 GLU B O   1 
ATOM   6279 C CB  . GLU B 1 376 ? 13.467  24.422  -25.065 1   35.89  ? 376 GLU B CB  1 
ATOM   6280 C CG  . GLU B 1 376 ? 12.492  25.33   -25.817 1   35.8   ? 376 GLU B CG  1 
ATOM   6281 C CD  . GLU B 1 376 ? 13.011  26.582  -26.488 1   43.88  ? 376 GLU B CD  1 
ATOM   6282 O OE1 . GLU B 1 376 ? 12.694  26.789  -27.687 1   43.79  ? 376 GLU B OE1 1 
ATOM   6283 O OE2 . GLU B 1 376 ? 13.77   27.334  -25.843 1   43.74  ? 376 GLU B OE2 1 
ATOM   6284 N N   . ASN B 1 377 ? 16.681  24.302  -24.641 1   34.42  ? 377 ASN B N   1 
ATOM   6285 C CA  . ASN B 1 377 ? 17.94   23.962  -23.997 1   35.57  ? 377 ASN B CA  1 
ATOM   6286 C C   . ASN B 1 377 ? 17.648  23.115  -22.753 1   35.43  ? 377 ASN B C   1 
ATOM   6287 O O   . ASN B 1 377 ? 17.041  23.631  -21.826 1   36.07  ? 377 ASN B O   1 
ATOM   6288 C CB  . ASN B 1 377 ? 18.724  25.21   -23.59  1   37.1   ? 377 ASN B CB  1 
ATOM   6289 C CG  . ASN B 1 377 ? 20.1    24.892  -23.043 1   39.91  ? 377 ASN B CG  1 
ATOM   6290 O OD1 . ASN B 1 377 ? 20.373  23.792  -22.545 1   43.27  ? 377 ASN B OD1 1 
ATOM   6291 N ND2 . ASN B 1 377 ? 21.005  25.855  -23.134 1   43.33  ? 377 ASN B ND2 1 
ATOM   6292 N N   . PRO B 1 378 ? 18.097  21.839  -22.657 1   37.01  ? 378 PRO B N   1 
ATOM   6293 C CA  . PRO B 1 378 ? 17.792  21.01   -21.486 1   36.81  ? 378 PRO B CA  1 
ATOM   6294 C C   . PRO B 1 378 ? 18.304  21.584  -20.16  1   33.2   ? 378 PRO B C   1 
ATOM   6295 O O   . PRO B 1 378 ? 17.692  21.366  -19.118 1   31.17  ? 378 PRO B O   1 
ATOM   6296 C CB  . PRO B 1 378 ? 18.476  19.664  -21.813 1   40.51  ? 378 PRO B CB  1 
ATOM   6297 C CG  . PRO B 1 378 ? 18.573  19.638  -23.343 1   40.25  ? 378 PRO B CG  1 
ATOM   6298 C CD  . PRO B 1 378 ? 18.873  21.109  -23.689 1   41.73  ? 378 PRO B CD  1 
ATOM   6299 N N   . ARG B 1 379 ? 19.458  22.276  -20.212 1   31.41  ? 379 ARG B N   1 
ATOM   6300 C CA  . ARG B 1 379 ? 20.05   22.805  -18.996 1   31.27  ? 379 ARG B CA  1 
ATOM   6301 C C   . ARG B 1 379 ? 19.119  23.854  -18.391 1   30.38  ? 379 ARG B C   1 
ATOM   6302 O O   . ARG B 1 379 ? 18.925  23.865  -17.176 1   28.75  ? 379 ARG B O   1 
ATOM   6303 C CB  . ARG B 1 379 ? 21.457  23.304  -19.308 1   33.5   ? 379 ARG B CB  1 
ATOM   6304 C CG  . ARG B 1 379 ? 22.244  23.866  -18.129 1   33.18  ? 379 ARG B CG  1 
ATOM   6305 C CD  . ARG B 1 379 ? 22.401  22.833  -17.005 1   33.49  ? 379 ARG B CD  1 
ATOM   6306 N NE  . ARG B 1 379 ? 23.414  23.129  -15.984 1   32.73  ? 379 ARG B NE  1 
ATOM   6307 C CZ  . ARG B 1 379 ? 24.708  23.254  -16.198 1   33.49  ? 379 ARG B CZ  1 
ATOM   6308 N NH1 . ARG B 1 379 ? 25.262  23.042  -17.39  1   37.35  ? 379 ARG B NH1 1 
ATOM   6309 N NH2 . ARG B 1 379 ? 25.5    23.589  -15.215 1   33.98  ? 379 ARG B NH2 1 
ATOM   6310 N N   . LEU B 1 380 ? 18.548  24.732  -19.23  1   29.33  ? 380 LEU B N   1 
ATOM   6311 C CA  . LEU B 1 380 ? 17.605  25.756  -18.798 1   30.18  ? 380 LEU B CA  1 
ATOM   6312 C C   . LEU B 1 380 ? 16.314  25.149  -18.278 1   29.74  ? 380 LEU B C   1 
ATOM   6313 O O   . LEU B 1 380 ? 15.811  25.564  -17.237 1   27.87  ? 380 LEU B O   1 
ATOM   6314 C CB  . LEU B 1 380 ? 17.358  26.797  -19.897 1   32.96  ? 380 LEU B CB  1 
ATOM   6315 C CG  . LEU B 1 380 ? 18.557  27.689  -20.251 1   35.74  ? 380 LEU B CG  1 
ATOM   6316 C CD1 . LEU B 1 380 ? 18.075  28.775  -21.214 1   38.67  ? 380 LEU B CD1 1 
ATOM   6317 C CD2 . LEU B 1 380 ? 19.251  28.32   -19.066 1   36.82  ? 380 LEU B CD2 1 
ATOM   6318 N N   . LEU B 1 381 ? 15.834  24.099  -18.932 1   28.33  ? 381 LEU B N   1 
ATOM   6319 C CA  . LEU B 1 381 ? 14.665  23.377  -18.458 1   29.55  ? 381 LEU B CA  1 
ATOM   6320 C C   . LEU B 1 381 ? 14.913  22.746  -17.081 1   28.05  ? 381 LEU B C   1 
ATOM   6321 O O   . LEU B 1 381 ? 14.036  22.806  -16.202 1   29.57  ? 381 LEU B O   1 
ATOM   6322 C CB  . LEU B 1 381 ? 14.209  22.375  -19.517 1   28.86  ? 381 LEU B CB  1 
ATOM   6323 C CG  . LEU B 1 381 ? 13.889  22.961  -20.896 1   30.37  ? 381 LEU B CG  1 
ATOM   6324 C CD1 . LEU B 1 381 ? 13.561  21.795  -21.835 1   32.41  ? 381 LEU B CD1 1 
ATOM   6325 C CD2 . LEU B 1 381 ? 12.769  23.914  -20.877 1   32.46  ? 381 LEU B CD2 1 
ATOM   6326 N N   . LYS B 1 382 ? 16.118  22.241  -16.857 1   28.5   ? 382 LYS B N   1 
ATOM   6327 C CA  . LYS B 1 382 ? 16.451  21.673  -15.552 1   29.06  ? 382 LYS B CA  1 
ATOM   6328 C C   . LYS B 1 382 ? 16.472  22.772  -14.486 1   27.51  ? 382 LYS B C   1 
ATOM   6329 O O   . LYS B 1 382 ? 15.902  22.614  -13.424 1   28.02  ? 382 LYS B O   1 
ATOM   6330 C CB  . LYS B 1 382 ? 17.801  20.968  -15.644 1   31.5   ? 382 LYS B CB  1 
ATOM   6331 C CG  . LYS B 1 382 ? 18.22   20.237  -14.403 1   38.26  ? 382 LYS B CG  1 
ATOM   6332 C CD  . LYS B 1 382 ? 19.645  19.725  -14.461 1   43.01  ? 382 LYS B CD  1 
ATOM   6333 C CE  . LYS B 1 382 ? 19.954  19.142  -13.104 1   51.4   ? 382 LYS B CE  1 
ATOM   6334 N NZ  . LYS B 1 382 ? 21.391  18.876  -13.002 1   58.77  ? 382 LYS B NZ  1 
ATOM   6335 N N   . ILE B 1 383 ? 17.069  23.918  -14.809 1   26.7   ? 383 ILE B N   1 
ATOM   6336 C CA  . ILE B 1 383 ? 17.169  25.035  -13.886 1   28.39  ? 383 ILE B CA  1 
ATOM   6337 C C   . ILE B 1 383 ? 15.79   25.543  -13.474 1   28.77  ? 383 ILE B C   1 
ATOM   6338 O O   . ILE B 1 383 ? 15.598  25.85   -12.28  1   28.04  ? 383 ILE B O   1 
ATOM   6339 C CB  . ILE B 1 383 ? 18.114  26.111  -14.451 1   29.02  ? 383 ILE B CB  1 
ATOM   6340 C CG1 . ILE B 1 383 ? 19.532  25.626  -14.439 1   29.34  ? 383 ILE B CG1 1 
ATOM   6341 C CG2 . ILE B 1 383 ? 17.99   27.391  -13.614 1   30.13  ? 383 ILE B CG2 1 
ATOM   6342 C CD1 . ILE B 1 383 ? 20.548  26.452  -15.208 1   33.1   ? 383 ILE B CD1 1 
ATOM   6343 N N   . ILE B 1 384 ? 14.816  25.501  -14.401 1   26.07  ? 384 ILE B N   1 
ATOM   6344 C CA  . ILE B 1 384 ? 13.441  25.883  -14.121 1   28     ? 384 ILE B CA  1 
ATOM   6345 C C   . ILE B 1 384 ? 12.785  24.993  -13.049 1   29.48  ? 384 ILE B C   1 
ATOM   6346 O O   . ILE B 1 384 ? 11.916  25.484  -12.341 1   29.28  ? 384 ILE B O   1 
ATOM   6347 C CB  . ILE B 1 384 ? 12.612  25.969  -15.43  1   29.27  ? 384 ILE B CB  1 
ATOM   6348 C CG1 . ILE B 1 384 ? 13.109  27.185  -16.251 1   30.84  ? 384 ILE B CG1 1 
ATOM   6349 C CG2 . ILE B 1 384 ? 11.102  26.037  -15.17  1   29.78  ? 384 ILE B CG2 1 
ATOM   6350 C CD1 . ILE B 1 384 ? 12.547  27.243  -17.667 1   32.64  ? 384 ILE B CD1 1 
ATOM   6351 N N   . THR B 1 385 ? 13.241  23.747  -12.879 1   29.3   ? 385 THR B N   1 
ATOM   6352 C CA  . THR B 1 385 ? 12.688  22.882  -11.828 1   30.31  ? 385 THR B CA  1 
ATOM   6353 C C   . THR B 1 385 ? 13.302  23.151  -10.453 1   33.39  ? 385 THR B C   1 
ATOM   6354 O O   . THR B 1 385 ? 12.755  22.622  -9.48   1   37.08  ? 385 THR B O   1 
ATOM   6355 C CB  . THR B 1 385 ? 12.876  21.41   -12.186 1   29.86  ? 385 THR B CB  1 
ATOM   6356 O OG1 . THR B 1 385 ? 14.264  21.1    -12.069 1   32.08  ? 385 THR B OG1 1 
ATOM   6357 C CG2 . THR B 1 385 ? 12.399  21.059  -13.58  1   32.64  ? 385 THR B CG2 1 
ATOM   6358 N N   . MET B 1 386 ? 14.378  23.958  -10.312 1   37.46  ? 386 MET B N   1 
ATOM   6359 C CA  . MET B 1 386 ? 15.05   24.116  -9.011  1   40.8   ? 386 MET B CA  1 
ATOM   6360 C C   . MET B 1 386 ? 14.215  24.972  -8.011  1   45.56  ? 386 MET B C   1 
ATOM   6361 O O   . MET B 1 386 ? 13.507  25.873  -8.53   1   42.22  ? 386 MET B O   1 
ATOM   6362 C CB  . MET B 1 386 ? 16.411  24.773  -9.179  1   37.83  ? 386 MET B CB  1 
ATOM   6363 C CG  . MET B 1 386 ? 17.359  23.927  -9.982  1   36.94  ? 386 MET B CG  1 
ATOM   6364 S SD  . MET B 1 386 ? 18.896  24.807  -10.204 1   34.6   ? 386 MET B SD  1 
ATOM   6365 C CE  . MET B 1 386 ? 19.853  24.704  -8.68   1   36.49  ? 386 MET B CE  1 
ATOM   6366 N N   . GLY C 2 1   ? 32.292  40.166  -4.139  1   26.63  ? 1   GLY C N   1 
ATOM   6367 C CA  . GLY C 2 1   ? 30.855  40.069  -4.449  1   27.23  ? 1   GLY C CA  1 
ATOM   6368 C C   . GLY C 2 1   ? 30.094  40.935  -3.438  1   25.74  ? 1   GLY C C   1 
ATOM   6369 O O   . GLY C 2 1   ? 30.713  41.756  -2.746  1   29.31  ? 1   GLY C O   1 
ATOM   6370 N N   . VAL C 2 2   ? 28.796  40.756  -3.389  1   25.51  ? 2   VAL C N   1 
ATOM   6371 C CA  . VAL C 2 2   ? 27.907  41.494  -2.53   1   23.87  ? 2   VAL C CA  1 
ATOM   6372 C C   . VAL C 2 2   ? 27.821  40.92   -1.123  1   22.75  ? 2   VAL C C   1 
ATOM   6373 O O   . VAL C 2 2   ? 27.793  39.744  -0.966  1   22.82  ? 2   VAL C O   1 
ATOM   6374 C CB  . VAL C 2 2   ? 26.499  41.494  -3.161  1   27.09  ? 2   VAL C CB  1 
ATOM   6375 C CG1 . VAL C 2 2   ? 25.452  42.118  -2.29   1   28.87  ? 2   VAL C CG1 1 
ATOM   6376 C CG2 . VAL C 2 2   ? 26.516  42.191  -4.486  1   29.63  ? 2   VAL C CG2 1 
ATOM   6377 N N   . VAL C 2 3   ? 27.814  41.786  -0.114  1   19.94  ? 3   VAL C N   1 
ATOM   6378 C CA  . VAL C 2 3   ? 27.632  41.368  1.26    1   21.93  ? 3   VAL C CA  1 
ATOM   6379 C C   . VAL C 2 3   ? 26.331  41.921  1.826   1   22.14  ? 3   VAL C C   1 
ATOM   6380 O O   . VAL C 2 3   ? 25.826  42.857  1.33    1   23.62  ? 3   VAL C O   1 
ATOM   6381 C CB  . VAL C 2 3   ? 28.813  41.736  2.161   1   23.27  ? 3   VAL C CB  1 
ATOM   6382 C CG1 . VAL C 2 3   ? 30.028  40.926  1.782   1   27.86  ? 3   VAL C CG1 1 
ATOM   6383 C CG2 . VAL C 2 3   ? 29.079  43.22   2.128   1   24.25  ? 3   VAL C CG2 1 
ATOM   6384 N N   . ARG C 2 4   ? 25.837  41.304  2.876   1   24.3   ? 4   ARG C N   1 
ATOM   6385 C CA  . ARG C 2 4   ? 24.591  41.676  3.496   1   25.39  ? 4   ARG C CA  1 
ATOM   6386 C C   . ARG C 2 4   ? 24.666  41.533  4.98    1   24.34  ? 4   ARG C C   1 
ATOM   6387 O O   . ARG C 2 4   ? 25.454  40.828  5.46    1   23.64  ? 4   ARG C O   1 
ATOM   6388 C CB  . ARG C 2 4   ? 23.455  40.774  3.026   1   26.09  ? 4   ARG C CB  1 
ATOM   6389 C CG  . ARG C 2 4   ? 23.096  40.825  1.572   1   25.32  ? 4   ARG C CG  1 
ATOM   6390 C CD  . ARG C 2 4   ? 22.955  39.44   1.034   1   29.68  ? 4   ARG C CD  1 
ATOM   6391 N NE  . ARG C 2 4   ? 22.227  39.414  -0.19   1   33.41  ? 4   ARG C NE  1 
ATOM   6392 C CZ  . ARG C 2 4   ? 22.623  38.899  -1.339  1   38.63  ? 4   ARG C CZ  1 
ATOM   6393 N NH1 . ARG C 2 4   ? 21.807  38.971  -2.378  1   45.44  ? 4   ARG C NH1 1 
ATOM   6394 N NH2 . ARG C 2 4   ? 23.782  38.339  -1.476  1   36.01  ? 4   ARG C NH2 1 
ATOM   6395 N N   . GLY C 2 5   ? 23.772  42.215  5.661   1   23.89  ? 5   GLY C N   1 
ATOM   6396 C CA  . GLY C 2 5   ? 23.665  42.147  7.101   1   25.36  ? 5   GLY C CA  1 
ATOM   6397 C C   . GLY C 2 5   ? 22.394  42.784  7.62    1   22.97  ? 5   GLY C C   1 
ATOM   6398 O O   . GLY C 2 5   ? 21.768  43.469  6.915   1   24.03  ? 5   GLY C O   1 
ATOM   6399 N N   . ALA C 2 6   ? 22.025  42.506  8.856   1   25.7   ? 6   ALA C N   1 
ATOM   6400 C CA  . ALA C 2 6   ? 20.859  43.056  9.514   1   28.37  ? 6   ALA C CA  1 
ATOM   6401 C C   . ALA C 2 6   ? 21.192  43.28   10.998  1   29.26  ? 6   ALA C C   1 
ATOM   6402 O O   . ALA C 2 6   ? 22.128  42.57   11.517  1   32.37  ? 6   ALA C O   1 
ATOM   6403 C CB  . ALA C 2 6   ? 19.627  42.106  9.323   1   28.11  ? 6   ALA C CB  1 
ATOM   6404 O OXT . ALA C 2 6   ? 20.494  44.13   11.606  1   31.03  ? 6   ALA C OXT 1 
ATOM   6405 N N   . GLY D 2 1   ? -7.891  18.327  -15.302 1   34.8   ? 1   GLY D N   1 
ATOM   6406 C CA  . GLY D 2 1   ? -6.527  18.351  -14.722 1   30.75  ? 1   GLY D CA  1 
ATOM   6407 C C   . GLY D 2 1   ? -6.551  17.511  -13.432 1   29.21  ? 1   GLY D C   1 
ATOM   6408 O O   . GLY D 2 1   ? -7.547  16.848  -13.171 1   31.53  ? 1   GLY D O   1 
ATOM   6409 N N   . VAL D 2 2   ? -5.528  17.648  -12.617 1   30.59  ? 2   VAL D N   1 
ATOM   6410 C CA  . VAL D 2 2   ? -5.392  16.975  -11.351 1   26.37  ? 2   VAL D CA  1 
ATOM   6411 C C   . VAL D 2 2   ? -6.136  17.721  -10.24  1   27.26  ? 2   VAL D C   1 
ATOM   6412 O O   . VAL D 2 2   ? -6.113  18.899  -10.206 1   26.78  ? 2   VAL D O   1 
ATOM   6413 C CB  . VAL D 2 2   ? -3.904  16.921  -10.994 1   27.96  ? 2   VAL D CB  1 
ATOM   6414 C CG1 . VAL D 2 2   ? -3.661  16.338  -9.626  1   29.51  ? 2   VAL D CG1 1 
ATOM   6415 C CG2 . VAL D 2 2   ? -3.15   16.12   -12.004 1   31.39  ? 2   VAL D CG2 1 
ATOM   6416 N N   . VAL D 2 3   ? -6.818  17.012  -9.358  1   24.03  ? 3   VAL D N   1 
ATOM   6417 C CA  . VAL D 2 3   ? -7.473  17.64   -8.229  1   24.43  ? 3   VAL D CA  1 
ATOM   6418 C C   . VAL D 2 3   ? -6.767  17.195  -6.948  1   25.19  ? 3   VAL D C   1 
ATOM   6419 O O   . VAL D 2 3   ? -6.166  16.167  -6.916  1   25.37  ? 3   VAL D O   1 
ATOM   6420 C CB  . VAL D 2 3   ? -8.988  17.377  -8.154  1   25.29  ? 3   VAL D CB  1 
ATOM   6421 C CG1 . VAL D 2 3   ? -9.717  18.075  -9.286  1   27.87  ? 3   VAL D CG1 1 
ATOM   6422 C CG2 . VAL D 2 3   ? -9.28   15.885  -8.136  1   25.86  ? 3   VAL D CG2 1 
ATOM   6423 N N   . ARG D 2 4   ? -6.853  18.007  -5.919  1   29.11  ? 4   ARG D N   1 
ATOM   6424 C CA  . ARG D 2 4   ? -6.223  17.759  -4.644  1   28.64  ? 4   ARG D CA  1 
ATOM   6425 C C   . ARG D 2 4   ? -7.153  18.065  -3.474  1   29.54  ? 4   ARG D C   1 
ATOM   6426 O O   . ARG D 2 4   ? -8.065  18.826  -3.601  1   28.62  ? 4   ARG D O   1 
ATOM   6427 C CB  . ARG D 2 4   ? -5      18.645  -4.503  1   28.74  ? 4   ARG D CB  1 
ATOM   6428 C CG  . ARG D 2 4   ? -3.84   18.312  -5.383  1   31.07  ? 4   ARG D CG  1 
ATOM   6429 C CD  . ARG D 2 4   ? -3.21   19.577  -5.896  1   32.8   ? 4   ARG D CD  1 
ATOM   6430 N NE  . ARG D 2 4   ? -1.891  19.408  -6.425  1   32.63  ? 4   ARG D NE  1 
ATOM   6431 C CZ  . ARG D 2 4   ? -1.534  19.727  -7.649  1   37.09  ? 4   ARG D CZ  1 
ATOM   6432 N NH1 . ARG D 2 4   ? -2.407  20.213  -8.482  1   35.59  ? 4   ARG D NH1 1 
ATOM   6433 N NH2 . ARG D 2 4   ? -0.295  19.541  -8.023  1   36.96  ? 4   ARG D NH2 1 
ATOM   6434 N N   . GLY D 2 5   ? -6.876  17.46   -2.332  1   24.64  ? 5   GLY D N   1 
ATOM   6435 C CA  . GLY D 2 5   ? -7.642  17.687  -1.133  1   25.88  ? 5   GLY D CA  1 
ATOM   6436 C C   . GLY D 2 5   ? -6.936  17.247  0.138   1   27.92  ? 5   GLY D C   1 
ATOM   6437 O O   . GLY D 2 5   ? -6.069  16.428  0.067   1   25.42  ? 5   GLY D O   1 
ATOM   6438 N N   . ALA D 2 6   ? -7.321  17.833  1.275   1   31.08  ? 6   ALA D N   1 
ATOM   6439 C CA  . ALA D 2 6   ? -6.796  17.499  2.579   1   31.4   ? 6   ALA D CA  1 
ATOM   6440 C C   . ALA D 2 6   ? -7.937  17.546  3.616   1   33.65  ? 6   ALA D C   1 
ATOM   6441 O O   . ALA D 2 6   ? -9.005  18.208  3.352   1   35.91  ? 6   ALA D O   1 
ATOM   6442 C CB  . ALA D 2 6   ? -5.648  18.421  2.923   1   30.43  ? 6   ALA D CB  1 
ATOM   6443 O OXT . ALA D 2 6   ? -7.779  16.838  4.653   1   31.89  ? 6   ALA D OXT 1 
HETATM 6444 C C1  . MPD E 3 .   ? 23.114  22.639  -7.847  1   79.03  ? 401 MPD A C1  1 
HETATM 6445 C C2  . MPD E 3 .   ? 24.511  23.015  -7.372  1   83.58  ? 401 MPD A C2  1 
HETATM 6446 O O2  . MPD E 3 .   ? 24.298  24.133  -6.51   1   74.53  ? 401 MPD A O2  1 
HETATM 6447 C CM  . MPD E 3 .   ? 25.124  21.934  -6.495  1   77.85  ? 401 MPD A CM  1 
HETATM 6448 C C3  . MPD E 3 .   ? 25.444  23.457  -8.516  1   89.54  ? 401 MPD A C3  1 
HETATM 6449 C C4  . MPD E 3 .   ? 26.18   22.385  -9.333  1   87.83  ? 401 MPD A C4  1 
HETATM 6450 O O4  . MPD E 3 .   ? 25.335  21.273  -9.625  1   91.36  ? 401 MPD A O4  1 
HETATM 6451 C C5  . MPD E 3 .   ? 26.752  22.853  -10.642 1   81.74  ? 401 MPD A C5  1 
HETATM 6452 C C   . ACT F 4 .   ? 33.275  25.715  -14.955 1   38.21  ? 402 ACT A C   1 
HETATM 6453 O O   . ACT F 4 .   ? 32.366  26.326  -15.469 1   41.26  ? 402 ACT A O   1 
HETATM 6454 O OXT . ACT F 4 .   ? 33.13   24.906  -14.044 1   86.24  ? 402 ACT A OXT 1 
HETATM 6455 C CH3 . ACT F 4 .   ? 34.674  25.87   -15.456 1   57.75  ? 402 ACT A CH3 1 
HETATM 6456 C C   . ACT G 4 .   ? 18.479  26.124  9.573   1   56.14  ? 403 ACT A C   1 
HETATM 6457 O O   . ACT G 4 .   ? 19.491  25.444  9.314   1   68.42  ? 403 ACT A O   1 
HETATM 6458 O OXT . ACT G 4 .   ? 18.533  27.26   10.117  1   53.61  ? 403 ACT A OXT 1 
HETATM 6459 C CH3 . ACT G 4 .   ? 17.106  25.541  9.222   1   47.27  ? 403 ACT A CH3 1 
HETATM 6460 C C1  . MPD H 3 .   ? -5.98   5.663   -28.383 1   76.25  ? 401 MPD B C1  1 
HETATM 6461 C C2  . MPD H 3 .   ? -6.31   5.197   -26.965 1   65.16  ? 401 MPD B C2  1 
HETATM 6462 O O2  . MPD H 3 .   ? -7.534  4.438   -26.962 1   52.33  ? 401 MPD B O2  1 
HETATM 6463 C CM  . MPD H 3 .   ? -6.552  6.384   -26.044 1   56.93  ? 401 MPD B CM  1 
HETATM 6464 C C3  . MPD H 3 .   ? -5.208  4.296   -26.406 1   62.81  ? 401 MPD B C3  1 
HETATM 6465 C C4  . MPD H 3 .   ? -4.658  3.242   -27.347 1   65.17  ? 401 MPD B C4  1 
HETATM 6466 O O4  . MPD H 3 .   ? -3.727  2.572   -26.578 1   65.63  ? 401 MPD B O4  1 
HETATM 6467 C C5  . MPD H 3 .   ? -5.589  2.216   -27.935 1   64.08  ? 401 MPD B C5  1 
HETATM 6468 C C1  . MPD I 3 .   ? -9.082  0.949   -13.551 1   38.71  ? 402 MPD B C1  1 
HETATM 6469 C C2  . MPD I 3 .   ? -8.681  1.195   -15.004 1   32.71  ? 402 MPD B C2  1 
HETATM 6470 O O2  . MPD I 3 .   ? -8.543  2.582   -15.208 1   42.97  ? 402 MPD B O2  1 
HETATM 6471 C CM  . MPD I 3 .   ? -7.287  0.724   -15.34  1   35.45  ? 402 MPD B CM  1 
HETATM 6472 C C3  . MPD I 3 .   ? -9.728  0.597   -15.963 1   52.32  ? 402 MPD B C3  1 
HETATM 6473 C C4  . MPD I 3 .   ? -9.609  -0.899  -16.367 1   64.12  ? 402 MPD B C4  1 
HETATM 6474 O O4  . MPD I 3 .   ? -9.064  -1.712  -15.312 1   80.72  ? 402 MPD B O4  1 
HETATM 6475 C C5  . MPD I 3 .   ? -10.865 -1.589  -16.825 1   59.13  ? 402 MPD B C5  1 
HETATM 6476 C C   . ACT J 4 .   ? 1.122   34.583  -15.557 1   69.69  ? 403 ACT B C   1 
HETATM 6477 O O   . ACT J 4 .   ? 1.866   33.969  -14.779 1   60.26  ? 403 ACT B O   1 
HETATM 6478 O OXT . ACT J 4 .   ? 1.216   34.494  -16.799 1   70.04  ? 403 ACT B OXT 1 
HETATM 6479 C CH3 . ACT J 4 .   ? 0.027   35.491  -14.957 1   58.09  ? 403 ACT B CH3 1 
HETATM 6480 O O   . HOH K 5 .   ? 3.555   35.663  25.572  1   55.6   ? 501 HOH A O   1 
HETATM 6481 O O   . HOH K 5 .   ? 17.54   56.429  0.827   1   48.44  ? 502 HOH A O   1 
HETATM 6482 O O   . HOH K 5 .   ? 27.289  23.385  -20.541 1   46.22  ? 503 HOH A O   1 
HETATM 6483 O O   . HOH K 5 .   ? 31.278  54.63   14.89   1   42.79  ? 504 HOH A O   1 
HETATM 6484 O O   . HOH K 5 .   ? 21.236  56.325  -12.02  1   42.63  ? 505 HOH A O   1 
HETATM 6485 O O   . HOH K 5 .   ? 26.201  40.016  7.932   1   34.6   ? 506 HOH A O   1 
HETATM 6486 O O   . HOH K 5 .   ? 27.484  36.647  -1.108  1   39.99  ? 507 HOH A O   1 
HETATM 6487 O O   . HOH K 5 .   ? 18.782  59.142  7.801   1   34.7   ? 508 HOH A O   1 
HETATM 6488 O O   . HOH K 5 .   ? 38.158  41.898  6.926   1   45.37  ? 509 HOH A O   1 
HETATM 6489 O O   . HOH K 5 .   ? 22.8    41.1    17.062  1   31.94  ? 510 HOH A O   1 
HETATM 6490 O O   . HOH K 5 .   ? 18.225  51.376  22.41   1   48.41  ? 511 HOH A O   1 
HETATM 6491 O O   . HOH K 5 .   ? 32.091  55.876  -8.663  1   40.46  ? 512 HOH A O   1 
HETATM 6492 O O   . HOH K 5 .   ? 11.817  33.144  0.636   1   46.43  ? 513 HOH A O   1 
HETATM 6493 O O   . HOH K 5 .   ? 12.057  37.549  -9.38   1   39.24  ? 514 HOH A O   1 
HETATM 6494 O O   . HOH K 5 .   ? 27.914  38.517  17.603  1   40.83  ? 515 HOH A O   1 
HETATM 6495 O O   . HOH K 5 .   ? 23.475  39.207  9.459   1   38.72  ? 516 HOH A O   1 
HETATM 6496 O O   . HOH K 5 .   ? 32.445  43.882  7.842   1   28.25  ? 517 HOH A O   1 
HETATM 6497 O O   . HOH K 5 .   ? 30.792  23.924  -9.051  1   44.37  ? 518 HOH A O   1 
HETATM 6498 O O   . HOH K 5 .   ? 13.221  54.174  -6.566  1   44.65  ? 519 HOH A O   1 
HETATM 6499 O O   . HOH K 5 .   ? 19.146  35.957  -26.485 1   37.05  ? 520 HOH A O   1 
HETATM 6500 O O   . HOH K 5 .   ? 36.462  48.213  -12.138 1   44.82  ? 521 HOH A O   1 
HETATM 6501 O O   . HOH K 5 .   ? 15.365  51.525  16.996  1   47.7   ? 522 HOH A O   1 
HETATM 6502 O O   . HOH K 5 .   ? 26.38   59.409  -8.372  1   38.03  ? 523 HOH A O   1 
HETATM 6503 O O   . HOH K 5 .   ? 33.195  26.545  -17.927 1   46.66  ? 524 HOH A O   1 
HETATM 6504 O O   . HOH K 5 .   ? 6.569   37.121  11.728  1   37.47  ? 525 HOH A O   1 
HETATM 6505 O O   . HOH K 5 .   ? 26.28   56.905  13.237  1   46.11  ? 526 HOH A O   1 
HETATM 6506 O O   . HOH K 5 .   ? 17.795  48.459  20.348  1   39.67  ? 527 HOH A O   1 
HETATM 6507 O O   . HOH K 5 .   ? 15.042  34.427  -1.021  1   27.59  ? 528 HOH A O   1 
HETATM 6508 O O   . HOH K 5 .   ? 22.707  53.275  20.702  1   39.79  ? 529 HOH A O   1 
HETATM 6509 O O   . HOH K 5 .   ? 17.326  53.887  18.413  1   43.99  ? 530 HOH A O   1 
HETATM 6510 O O   . HOH K 5 .   ? 42.664  44.787  -9.807  1   26.3   ? 531 HOH A O   1 
HETATM 6511 O O   . HOH K 5 .   ? 27.621  51.106  17.336  1   45.55  ? 532 HOH A O   1 
HETATM 6512 O O   . HOH K 5 .   ? 4.072   33.434  13.714  1   42.8   ? 533 HOH A O   1 
HETATM 6513 O O   . HOH K 5 .   ? 10.883  54.16   32.545  1   42.78  ? 534 HOH A O   1 
HETATM 6514 O O   . HOH K 5 .   ? 35.697  43.998  -1.408  1   24.23  ? 535 HOH A O   1 
HETATM 6515 O O   . HOH K 5 .   ? 14.841  27.86   -2.706  1   41.48  ? 536 HOH A O   1 
HETATM 6516 O O   . HOH K 5 .   ? 35.178  54.852  -6.703  1   33.85  ? 537 HOH A O   1 
HETATM 6517 O O   . HOH K 5 .   ? 15.504  54.325  -10.076 1   44.28  ? 538 HOH A O   1 
HETATM 6518 O O   . HOH K 5 .   ? 19.133  28.791  0.519   1   27.82  ? 539 HOH A O   1 
HETATM 6519 O O   . HOH K 5 .   ? 26.601  33.99   11.486  1   43.35  ? 540 HOH A O   1 
HETATM 6520 O O   . HOH K 5 .   ? 25.403  37.324  2.737   1   38.41  ? 541 HOH A O   1 
HETATM 6521 O O   . HOH K 5 .   ? 7.111   46.379  11.042  1   46.88  ? 542 HOH A O   1 
HETATM 6522 O O   . HOH K 5 .   ? 32.21   33.931  3.646   1   42.56  ? 543 HOH A O   1 
HETATM 6523 O O   . HOH K 5 .   ? 29.109  59.279  -9.49   1   49.55  ? 544 HOH A O   1 
HETATM 6524 O O   . HOH K 5 .   ? 23.41   44.329  1.269   1   22.4   ? 545 HOH A O   1 
HETATM 6525 O O   . HOH K 5 .   ? 14.745  54.761  -2.355  1   48.4   ? 546 HOH A O   1 
HETATM 6526 O O   . HOH K 5 .   ? 40.005  40.489  5.274   1   42.57  ? 547 HOH A O   1 
HETATM 6527 O O   . HOH K 5 .   ? 35.094  24.989  -11.626 1   53.26  ? 548 HOH A O   1 
HETATM 6528 O O   . HOH K 5 .   ? 41.944  40.948  -2.037  1   27.18  ? 549 HOH A O   1 
HETATM 6529 O O   . HOH K 5 .   ? 47.095  37.826  -11.809 1   49.93  ? 550 HOH A O   1 
HETATM 6530 O O   . HOH K 5 .   ? 25.677  40.776  -16.427 1   32.63  ? 551 HOH A O   1 
HETATM 6531 O O   . HOH K 5 .   ? 25.213  58.736  -6.095  1   30.86  ? 552 HOH A O   1 
HETATM 6532 O O   . HOH K 5 .   ? 17.232  44.917  -10.081 1   31.27  ? 553 HOH A O   1 
HETATM 6533 O O   . HOH K 5 .   ? 24.863  50.521  17.285  1   32.57  ? 554 HOH A O   1 
HETATM 6534 O O   . HOH K 5 .   ? 12.92   47.777  29.808  1   35.7   ? 555 HOH A O   1 
HETATM 6535 O O   . HOH K 5 .   ? 9.153   50.958  -1.412  1   39.84  ? 556 HOH A O   1 
HETATM 6536 O O   . HOH K 5 .   ? 15.032  36.157  -9.88   1   37.63  ? 557 HOH A O   1 
HETATM 6537 O O   . HOH K 5 .   ? 30.732  36.776  -3.068  1   30.2   ? 558 HOH A O   1 
HETATM 6538 O O   . HOH K 5 .   ? 30.687  37.012  1.395   1   29.04  ? 559 HOH A O   1 
HETATM 6539 O O   . HOH K 5 .   ? 18.559  33.253  -29.529 1   44.37  ? 560 HOH A O   1 
HETATM 6540 O O   . HOH K 5 .   ? 36.787  48.884  7.31    1   29.85  ? 561 HOH A O   1 
HETATM 6541 O O   . HOH K 5 .   ? 21.971  43.826  3.557   1   22.12  ? 562 HOH A O   1 
HETATM 6542 O O   . HOH K 5 .   ? 35.327  33.197  -5.705  1   28.42  ? 563 HOH A O   1 
HETATM 6543 O O   . HOH K 5 .   ? 30.358  38.448  -0.815  1   27.86  ? 564 HOH A O   1 
HETATM 6544 O O   . HOH K 5 .   ? 42.753  35.525  -6.011  1   30.26  ? 565 HOH A O   1 
HETATM 6545 O O   . HOH K 5 .   ? 23.257  20.913  -13.5   1   41.73  ? 566 HOH A O   1 
HETATM 6546 O O   . HOH K 5 .   ? 18.077  28.835  -24.948 1   41.9   ? 567 HOH A O   1 
HETATM 6547 O O   . HOH K 5 .   ? 12.327  29.472  1.164   1   44.45  ? 568 HOH A O   1 
HETATM 6548 O O   . HOH K 5 .   ? 21.726  65.641  21.599  1   51.45  ? 569 HOH A O   1 
HETATM 6549 O O   . HOH K 5 .   ? 13.553  49.832  22.256  1   44.92  ? 570 HOH A O   1 
HETATM 6550 O O   . HOH K 5 .   ? 15.278  50.024  33.176  1   38.53  ? 571 HOH A O   1 
HETATM 6551 O O   . HOH K 5 .   ? 30.164  58.884  2.961   1   31.06  ? 572 HOH A O   1 
HETATM 6552 O O   . HOH K 5 .   ? 13.902  33.473  2.673   1   30.91  ? 573 HOH A O   1 
HETATM 6553 O O   . HOH K 5 .   ? 24.944  58.875  21.225  1   44.52  ? 574 HOH A O   1 
HETATM 6554 O O   . HOH K 5 .   ? 23.631  34.068  15.076  1   34.17  ? 575 HOH A O   1 
HETATM 6555 O O   . HOH K 5 .   ? 32.786  56.461  7.346   1   48.29  ? 576 HOH A O   1 
HETATM 6556 O O   . HOH K 5 .   ? 27.363  58.897  -11.747 1   49.59  ? 577 HOH A O   1 
HETATM 6557 O O   . HOH K 5 .   ? 34.679  32.168  1.952   1   35.85  ? 578 HOH A O   1 
HETATM 6558 O O   . HOH K 5 .   ? 20.439  51.859  20.796  1   34.26  ? 579 HOH A O   1 
HETATM 6559 O O   . HOH K 5 .   ? 31.696  56.755  25.392  1   48.35  ? 580 HOH A O   1 
HETATM 6560 O O   . HOH K 5 .   ? 29.82   28.545  -24.267 1   43.69  ? 581 HOH A O   1 
HETATM 6561 O O   . HOH K 5 .   ? 27.637  20.854  -15.714 1   42.97  ? 582 HOH A O   1 
HETATM 6562 O O   . HOH K 5 .   ? 30.172  35.645  27.905  1   43.97  ? 583 HOH A O   1 
HETATM 6563 O O   . HOH K 5 .   ? 7.65    33.359  21.005  1   41.56  ? 584 HOH A O   1 
HETATM 6564 O O   . HOH K 5 .   ? 37.703  44.133  3.46    1   29.25  ? 585 HOH A O   1 
HETATM 6565 O O   . HOH K 5 .   ? 23.321  28.319  0.608   1   40.05  ? 586 HOH A O   1 
HETATM 6566 O O   . HOH K 5 .   ? 44.769  37.788  -0.544  1   41.69  ? 587 HOH A O   1 
HETATM 6567 O O   . HOH K 5 .   ? 37.699  30.74   2.604   1   36.86  ? 588 HOH A O   1 
HETATM 6568 O O   . HOH K 5 .   ? 15.421  54.055  23.76   1   42.48  ? 589 HOH A O   1 
HETATM 6569 O O   . HOH K 5 .   ? 14.759  35.791  1.275   1   25.43  ? 590 HOH A O   1 
HETATM 6570 O O   . HOH K 5 .   ? 29.148  48.881  17.549  1   42.88  ? 591 HOH A O   1 
HETATM 6571 O O   . HOH K 5 .   ? 18.637  46.589  -8.429  1   33.08  ? 592 HOH A O   1 
HETATM 6572 O O   . HOH K 5 .   ? 38.251  44.16   -2.656  1   26.1   ? 593 HOH A O   1 
HETATM 6573 O O   . HOH K 5 .   ? 31.756  45.884  -15.719 1   32.42  ? 594 HOH A O   1 
HETATM 6574 O O   . HOH K 5 .   ? 29.173  35.613  24.984  1   47.16  ? 595 HOH A O   1 
HETATM 6575 O O   . HOH K 5 .   ? 6.577   33.939  18.245  1   38.23  ? 596 HOH A O   1 
HETATM 6576 O O   . HOH K 5 .   ? 39.268  51.18   -10.888 1   39.68  ? 597 HOH A O   1 
HETATM 6577 O O   . HOH K 5 .   ? 30.568  52.007  16.714  1   49.55  ? 598 HOH A O   1 
HETATM 6578 O O   . HOH K 5 .   ? 13.21   56.559  6.136   1   31.92  ? 599 HOH A O   1 
HETATM 6579 O O   . HOH K 5 .   ? 34.972  28.513  -17.819 1   43.95  ? 600 HOH A O   1 
HETATM 6580 O O   . HOH K 5 .   ? 21.155  25.103  -0.597  1   45.1   ? 601 HOH A O   1 
HETATM 6581 O O   . HOH K 5 .   ? 5.127   39.827  14.828  1   37.52  ? 602 HOH A O   1 
HETATM 6582 O O   . HOH K 5 .   ? 14.756  37.512  -20.76  1   45.46  ? 603 HOH A O   1 
HETATM 6583 O O   . HOH K 5 .   ? 44.126  47.248  -0.164  1   35.62  ? 604 HOH A O   1 
HETATM 6584 O O   . HOH K 5 .   ? 34.47   36.21   1.734   1   26.06  ? 605 HOH A O   1 
HETATM 6585 O O   . HOH K 5 .   ? 31.799  46.473  23.612  1   43.11  ? 606 HOH A O   1 
HETATM 6586 O O   . HOH K 5 .   ? 26.465  27.762  1.231   1   45.78  ? 607 HOH A O   1 
HETATM 6587 O O   . HOH K 5 .   ? 17.009  36.354  2.839   1   27.63  ? 608 HOH A O   1 
HETATM 6588 O O   . HOH K 5 .   ? 9.142   53.487  11.769  1   38.81  ? 609 HOH A O   1 
HETATM 6589 O O   . HOH K 5 .   ? 29.362  25.994  -0.781  1   41.64  ? 610 HOH A O   1 
HETATM 6590 O O   . HOH K 5 .   ? 36.414  46.518  -0.096  1   26.48  ? 611 HOH A O   1 
HETATM 6591 O O   . HOH K 5 .   ? 34.554  40.11   -19.983 1   41.07  ? 612 HOH A O   1 
HETATM 6592 O O   . HOH K 5 .   ? 30.124  31.995  4.479   1   35.38  ? 613 HOH A O   1 
HETATM 6593 O O   . HOH K 5 .   ? 27.874  44.753  -15.913 1   37.17  ? 614 HOH A O   1 
HETATM 6594 O O   . HOH K 5 .   ? 42.131  38.159  -6.243  1   28.45  ? 615 HOH A O   1 
HETATM 6595 O O   . HOH K 5 .   ? 34.621  47.248  13.995  1   47.84  ? 616 HOH A O   1 
HETATM 6596 O O   . HOH K 5 .   ? 44.274  30.209  -2.537  1   46.12  ? 617 HOH A O   1 
HETATM 6597 O O   . HOH K 5 .   ? 46.138  39.964  -18.285 1   41.35  ? 618 HOH A O   1 
HETATM 6598 O O   . HOH K 5 .   ? 17.036  56.251  -1.779  1   37.23  ? 619 HOH A O   1 
HETATM 6599 O O   . HOH K 5 .   ? 15.595  28.712  -5.562  1   40.64  ? 620 HOH A O   1 
HETATM 6600 O O   . HOH K 5 .   ? 30.044  35.981  5.257   1   43.56  ? 621 HOH A O   1 
HETATM 6601 O O   . HOH K 5 .   ? 39.106  52.797  0.117   1   43.95  ? 622 HOH A O   1 
HETATM 6602 O O   . HOH K 5 .   ? 10.846  44.278  -7.199  1   36.48  ? 623 HOH A O   1 
HETATM 6603 O O   . HOH K 5 .   ? 23.975  54.372  18.026  1   31.45  ? 624 HOH A O   1 
HETATM 6604 O O   . HOH K 5 .   ? 20.007  22.74   -12.227 1   40.73  ? 625 HOH A O   1 
HETATM 6605 O O   . HOH K 5 .   ? 30.384  26.32   -22.051 1   38.96  ? 626 HOH A O   1 
HETATM 6606 O O   . HOH K 5 .   ? 27.206  66.444  27.246  1   45.38  ? 627 HOH A O   1 
HETATM 6607 O O   . HOH K 5 .   ? 33.751  25.735  -0.945  1   48.3   ? 628 HOH A O   1 
HETATM 6608 O O   . HOH K 5 .   ? 32.412  55.576  -5.49   1   33.78  ? 629 HOH A O   1 
HETATM 6609 O O   . HOH K 5 .   ? 48.192  40.248  2.378   1   47.3   ? 630 HOH A O   1 
HETATM 6610 O O   . HOH K 5 .   ? 36.436  34.207  2.596   1   26.24  ? 631 HOH A O   1 
HETATM 6611 O O   . HOH K 5 .   ? 39.618  28.424  2.335   1   41.91  ? 632 HOH A O   1 
HETATM 6612 O O   . HOH K 5 .   ? 30.776  46.729  16.138  1   48.02  ? 633 HOH A O   1 
HETATM 6613 O O   . HOH K 5 .   ? 31.051  46.18   13.8    1   39.06  ? 634 HOH A O   1 
HETATM 6614 O O   . HOH K 5 .   ? 11.738  49.889  13.527  1   43.97  ? 635 HOH A O   1 
HETATM 6615 O O   . HOH K 5 .   ? 22.041  53.909  -13.267 1   37.61  ? 636 HOH A O   1 
HETATM 6616 O O   . HOH K 5 .   ? 31.405  42.815  5.371   1   26.34  ? 637 HOH A O   1 
HETATM 6617 O O   . HOH K 5 .   ? 14.661  46.392  36.567  1   42.42  ? 638 HOH A O   1 
HETATM 6618 O O   . HOH K 5 .   ? 17.329  32.481  -7.46   1   28.94  ? 639 HOH A O   1 
HETATM 6619 O O   . HOH K 5 .   ? 46.988  38.527  0.93    1   36.1   ? 640 HOH A O   1 
HETATM 6620 O O   . HOH K 5 .   ? 25.858  40.132  16.98   1   40.53  ? 641 HOH A O   1 
HETATM 6621 O O   . HOH K 5 .   ? 42.611  43.784  4.721   1   48.47  ? 642 HOH A O   1 
HETATM 6622 O O   . HOH K 5 .   ? 28.1    35.629  1.306   1   30.18  ? 643 HOH A O   1 
HETATM 6623 O O   . HOH K 5 .   ? 6.68    35.054  27.702  1   30     ? 644 HOH A O   1 
HETATM 6624 O O   . HOH K 5 .   ? 18.546  72.014  42.937  1   45.05  ? 645 HOH A O   1 
HETATM 6625 O O   . HOH K 5 .   ? 37.056  51.425  -15.314 1   58.62  ? 646 HOH A O   1 
HETATM 6626 O O   . HOH K 5 .   ? 6.214   44.056  25.86   1   50.13  ? 647 HOH A O   1 
HETATM 6627 O O   . HOH K 5 .   ? 32.17   24.731  -21.399 1   56.61  ? 648 HOH A O   1 
HETATM 6628 O O   . HOH K 5 .   ? 15.286  33.297  -9.379  1   33.48  ? 649 HOH A O   1 
HETATM 6629 O O   . HOH K 5 .   ? 19.225  25.006  5.278   1   42.76  ? 650 HOH A O   1 
HETATM 6630 O O   . HOH K 5 .   ? 42.04   49.459  0.522   1   37.83  ? 651 HOH A O   1 
HETATM 6631 O O   . HOH K 5 .   ? 45.198  39.107  -20.902 1   56.27  ? 652 HOH A O   1 
HETATM 6632 O O   . HOH K 5 .   ? 20.152  52.795  -14.924 1   49.57  ? 653 HOH A O   1 
HETATM 6633 O O   . HOH K 5 .   ? 43.633  46.176  4.13    1   57.12  ? 654 HOH A O   1 
HETATM 6634 O O   . HOH K 5 .   ? 23.839  39.816  14.519  1   45.24  ? 655 HOH A O   1 
HETATM 6635 O O   . HOH K 5 .   ? 25.339  37.743  13.344  1   43.19  ? 656 HOH A O   1 
HETATM 6636 O O   . HOH K 5 .   ? 7.158   34.79   0.326   1   48.73  ? 657 HOH A O   1 
HETATM 6637 O O   . HOH K 5 .   ? 25.315  35.077  13.351  1   39.8   ? 658 HOH A O   1 
HETATM 6638 O O   . HOH K 5 .   ? 16.957  65.415  42.699  1   40.13  ? 659 HOH A O   1 
HETATM 6639 O O   . HOH K 5 .   ? 14.009  47.744  32.28   1   39.67  ? 660 HOH A O   1 
HETATM 6640 O O   . HOH K 5 .   ? 32.19   28.601  3.326   1   53.04  ? 661 HOH A O   1 
HETATM 6641 O O   . HOH K 5 .   ? 26.957  53.172  18.76   1   48.32  ? 662 HOH A O   1 
HETATM 6642 O O   . HOH K 5 .   ? 32.569  26.091  2.619   1   56.99  ? 663 HOH A O   1 
HETATM 6643 O O   . HOH K 5 .   ? 15.82   30.962  -5.83   1   36.79  ? 664 HOH A O   1 
HETATM 6644 O O   . HOH K 5 .   ? 10.261  36.586  -22.994 1   44.87  ? 665 HOH A O   1 
HETATM 6645 O O   . HOH K 5 .   ? 7.618   37.003  -22.297 1   49.75  ? 666 HOH A O   1 
HETATM 6646 O O   . HOH K 5 .   ? 29.92   46.095  -17.765 1   57.89  ? 667 HOH A O   1 
HETATM 6647 O O   . HOH K 5 .   ? 37.89   34.401  4.953   1   41.83  ? 668 HOH A O   1 
HETATM 6648 O O   . HOH K 5 .   ? 30.23   40.23   5.205   1   30.31  ? 669 HOH A O   1 
HETATM 6649 O O   . HOH K 5 .   ? 33.927  37.504  4.046   1   40.63  ? 670 HOH A O   1 
HETATM 6650 O O   . HOH K 5 .   ? 30.379  44.58   11.937  1   44.17  ? 671 HOH A O   1 
HETATM 6651 O O   . HOH K 5 .   ? 36.989  46.438  2.475   1   30.44  ? 672 HOH A O   1 
HETATM 6652 O O   . HOH K 5 .   ? 12.617  26.747  1.699   1   45.41  ? 673 HOH A O   1 
HETATM 6653 O O   . HOH K 5 .   ? 24.017  56.793  14.664  1   48.4   ? 674 HOH A O   1 
HETATM 6654 O O   . HOH K 5 .   ? 9.755   31.517  1.251   1   51.02  ? 675 HOH A O   1 
HETATM 6655 O O   . HOH K 5 .   ? 43.576  39.779  -4.224  1   35.38  ? 676 HOH A O   1 
HETATM 6656 O O   . HOH K 5 .   ? 6.962   39.765  12.863  1   48.65  ? 677 HOH A O   1 
HETATM 6657 O O   . HOH K 5 .   ? 37.501  23.372  -2.149  1   56.9   ? 678 HOH A O   1 
HETATM 6658 O O   . HOH K 5 .   ? 32.79   58.1    -3.847  1   42.18  ? 679 HOH A O   1 
HETATM 6659 O O   . HOH K 5 .   ? 26.662  41.158  10.657  1   38.29  ? 680 HOH A O   1 
HETATM 6660 O O   . HOH K 5 .   ? 25.21   43.3    -16.815 1   38.58  ? 681 HOH A O   1 
HETATM 6661 O O   . HOH K 5 .   ? 31.271  38.089  3.925   1   33.69  ? 682 HOH A O   1 
HETATM 6662 O O   . HOH K 5 .   ? 33.747  24.86   -19.568 1   53.16  ? 683 HOH A O   1 
HETATM 6663 O O   . HOH K 5 .   ? 18.602  58.739  9.837   1   47.99  ? 684 HOH A O   1 
HETATM 6664 O O   . HOH K 5 .   ? 34.884  53.836  27.658  1   48.13  ? 685 HOH A O   1 
HETATM 6665 O O   . HOH K 5 .   ? 24.378  54.853  -14.813 1   48.42  ? 686 HOH A O   1 
HETATM 6666 O O   . HOH K 5 .   ? 45.104  37.798  -3.173  1   39.91  ? 687 HOH A O   1 
HETATM 6667 O O   . HOH K 5 .   ? 33.228  58.94   -1.603  1   52.34  ? 688 HOH A O   1 
HETATM 6668 O O   . HOH K 5 .   ? 17.1    39.317  -17.915 1   56.56  ? 689 HOH A O   1 
HETATM 6669 O O   . HOH K 5 .   ? 45.185  35.573  -4.805  1   47.54  ? 690 HOH A O   1 
HETATM 6670 O O   . HOH K 5 .   ? 23.268  44.945  -16.813 1   50.72  ? 691 HOH A O   1 
HETATM 6671 O O   . HOH L 5 .   ? 10.076  9.484   4.139   1   53.94  ? 501 HOH B O   1 
HETATM 6672 O O   . HOH L 5 .   ? -18.488 39.056  3.492   1   43.43  ? 502 HOH B O   1 
HETATM 6673 O O   . HOH L 5 .   ? 1.246   3.845   1.379   1   46.06  ? 503 HOH B O   1 
HETATM 6674 O O   . HOH L 5 .   ? -0.35   2.9     -0.608  1   41     ? 504 HOH B O   1 
HETATM 6675 O O   . HOH L 5 .   ? -15.758 9.199   11.791  1   47.64  ? 505 HOH B O   1 
HETATM 6676 O O   . HOH L 5 .   ? -11.609 14.506  14.178  1   42.93  ? 506 HOH B O   1 
HETATM 6677 O O   . HOH L 5 .   ? -19.541 17.697  -9.627  1   48.96  ? 507 HOH B O   1 
HETATM 6678 O O   . HOH L 5 .   ? -10.25  19.974  -2.257  1   39.77  ? 508 HOH B O   1 
HETATM 6679 O O   . HOH L 5 .   ? -9.075  12.512  23.306  1   49.93  ? 509 HOH B O   1 
HETATM 6680 O O   . HOH L 5 .   ? 7.643   3.036   -8.441  1   46.72  ? 510 HOH B O   1 
HETATM 6681 O O   . HOH L 5 .   ? 6.994   29.239  -8.123  1   38.86  ? 511 HOH B O   1 
HETATM 6682 O O   . HOH L 5 .   ? -25.382 29.531  11.298  1   45.2   ? 512 HOH B O   1 
HETATM 6683 O O   . HOH L 5 .   ? -11.945 27.011  -0.915  1   35.53  ? 513 HOH B O   1 
HETATM 6684 O O   . HOH L 5 .   ? -12.448 20.695  7.126   1   32.59  ? 514 HOH B O   1 
HETATM 6685 O O   . HOH L 5 .   ? -2.195  30.536  -7.954  1   40.03  ? 515 HOH B O   1 
HETATM 6686 O O   . HOH L 5 .   ? 4.905   28.755  14.545  1   47.53  ? 516 HOH B O   1 
HETATM 6687 O O   . HOH L 5 .   ? -13.48  11.314  15.597  1   44.18  ? 517 HOH B O   1 
HETATM 6688 O O   . HOH L 5 .   ? -7.389  38.19   9.185   1   43.74  ? 518 HOH B O   1 
HETATM 6689 O O   . HOH L 5 .   ? 5.895   35.967  -19.955 1   44.01  ? 519 HOH B O   1 
HETATM 6690 O O   . HOH L 5 .   ? 16.331  26.959  -25.657 1   39.48  ? 520 HOH B O   1 
HETATM 6691 O O   . HOH L 5 .   ? -6.322  1.845   -17.734 1   36.38  ? 521 HOH B O   1 
HETATM 6692 O O   . HOH L 5 .   ? 16.008  19.9    -26.138 1   42.59  ? 522 HOH B O   1 
HETATM 6693 O O   . HOH L 5 .   ? 7.922   7.781   1.822   1   38.38  ? 523 HOH B O   1 
HETATM 6694 O O   . HOH L 5 .   ? 13.676  27.226  -10.741 1   37.61  ? 524 HOH B O   1 
HETATM 6695 O O   . HOH L 5 .   ? -13.844 10.732  13.132  1   32.12  ? 525 HOH B O   1 
HETATM 6696 O O   . HOH L 5 .   ? -28.303 14.265  7.921   1   54.37  ? 526 HOH B O   1 
HETATM 6697 O O   . HOH L 5 .   ? -15.331 16.276  -5.331  1   33.99  ? 527 HOH B O   1 
HETATM 6698 O O   . HOH L 5 .   ? 0.606   14.364  -22.502 1   41.5   ? 528 HOH B O   1 
HETATM 6699 O O   . HOH L 5 .   ? -16.926 14.846  25.6    1   44.31  ? 529 HOH B O   1 
HETATM 6700 O O   . HOH L 5 .   ? -21.22  35.82   5.37    1   48.29  ? 530 HOH B O   1 
HETATM 6701 O O   . HOH L 5 .   ? -17.498 4.629   -17.510 1   47.16  ? 531 HOH B O   1 
HETATM 6702 O O   . HOH L 5 .   ? -26.222 20.656  20.325  1   48.39  ? 532 HOH B O   1 
HETATM 6703 O O   . HOH L 5 .   ? 5.927   29.678  -0.72   1   41.51  ? 533 HOH B O   1 
HETATM 6704 O O   . HOH L 5 .   ? 7.345   3.405   -4.733  1   46.92  ? 534 HOH B O   1 
HETATM 6705 O O   . HOH L 5 .   ? -5.853  1.595   5.463   1   39.84  ? 535 HOH B O   1 
HETATM 6706 O O   . HOH L 5 .   ? -4.262  14.705  -5.339  1   24.9   ? 536 HOH B O   1 
HETATM 6707 O O   . HOH L 5 .   ? 0.852   30.108  -5.49   1   28.09  ? 537 HOH B O   1 
HETATM 6708 O O   . HOH L 5 .   ? -18.014 34.169  7.574   1   43.86  ? 538 HOH B O   1 
HETATM 6709 O O   . HOH L 5 .   ? -2.401  -2.057  -12.615 1   43.19  ? 539 HOH B O   1 
HETATM 6710 O O   . HOH L 5 .   ? 14.411  28.254  -29.088 1   48.13  ? 540 HOH B O   1 
HETATM 6711 O O   . HOH L 5 .   ? -16.275 3.743   -4.476  1   43.61  ? 541 HOH B O   1 
HETATM 6712 O O   . HOH L 5 .   ? -5.706  22.363  -11.011 1   39.09  ? 542 HOH B O   1 
HETATM 6713 O O   . HOH L 5 .   ? 3.781   24.098  12.108  1   38.99  ? 543 HOH B O   1 
HETATM 6714 O O   . HOH L 5 .   ? 5.113   7.602   7.509   1   35.09  ? 544 HOH B O   1 
HETATM 6715 O O   . HOH L 5 .   ? 3.737   3.373   -2.02   1   46.75  ? 545 HOH B O   1 
HETATM 6716 O O   . HOH L 5 .   ? -27.074 31.827  14.968  1   45.66  ? 546 HOH B O   1 
HETATM 6717 O O   . HOH L 5 .   ? -19.067 10.269  4.22    1   43     ? 547 HOH B O   1 
HETATM 6718 O O   . HOH L 5 .   ? -18.478 33.547  10.751  1   36.58  ? 548 HOH B O   1 
HETATM 6719 O O   . HOH L 5 .   ? -4.371  15.69   -2.741  1   25.18  ? 549 HOH B O   1 
HETATM 6720 O O   . HOH L 5 .   ? -8.932  37.694  15.042  1   34.77  ? 550 HOH B O   1 
HETATM 6721 O O   . HOH L 5 .   ? -13.828 35.368  19.359  1   37.94  ? 551 HOH B O   1 
HETATM 6722 O O   . HOH L 5 .   ? -24.071 15.796  7.53    1   40.58  ? 552 HOH B O   1 
HETATM 6723 O O   . HOH L 5 .   ? 10.635  13.306  -4.899  1   44.53  ? 553 HOH B O   1 
HETATM 6724 O O   . HOH L 5 .   ? -11.797 9.26    18.874  1   41.98  ? 554 HOH B O   1 
HETATM 6725 O O   . HOH L 5 .   ? -11.547 27.263  3.9     1   30.73  ? 555 HOH B O   1 
HETATM 6726 O O   . HOH L 5 .   ? -27.529 9.251   19.829  1   44.34  ? 556 HOH B O   1 
HETATM 6727 O O   . HOH L 5 .   ? -9.88   7.384   -23.924 1   34.25  ? 557 HOH B O   1 
HETATM 6728 O O   . HOH L 5 .   ? -12.592 14.683  -14.648 1   32.57  ? 558 HOH B O   1 
HETATM 6729 O O   . HOH L 5 .   ? -19.214 13.392  25.91   1   41.73  ? 559 HOH B O   1 
HETATM 6730 O O   . HOH L 5 .   ? -12.838 11.101  -27.618 1   48.94  ? 560 HOH B O   1 
HETATM 6731 O O   . HOH L 5 .   ? -13.686 13.013  -25.133 1   34.05  ? 561 HOH B O   1 
HETATM 6732 O O   . HOH L 5 .   ? -10.647 8.626   24.999  1   44.76  ? 562 HOH B O   1 
HETATM 6733 O O   . HOH L 5 .   ? -24.842 27.171  10.156  1   44.1   ? 563 HOH B O   1 
HETATM 6734 O O   . HOH L 5 .   ? -13.053 37.942  21.128  1   49.5   ? 564 HOH B O   1 
HETATM 6735 O O   . HOH L 5 .   ? -16.218 35.033  21.421  1   38.65  ? 565 HOH B O   1 
HETATM 6736 O O   . HOH L 5 .   ? 16.276  19.101  -18.712 1   44.99  ? 566 HOH B O   1 
HETATM 6737 O O   . HOH L 5 .   ? -17.271 22.868  3.518   1   42.31  ? 567 HOH B O   1 
HETATM 6738 O O   . HOH L 5 .   ? -19.08  11.025  -7.517  1   43.07  ? 568 HOH B O   1 
HETATM 6739 O O   . HOH L 5 .   ? -9.53   22.123  -10.328 1   35.96  ? 569 HOH B O   1 
HETATM 6740 O O   . HOH L 5 .   ? 6.296   30.763  -5.538  1   39.26  ? 570 HOH B O   1 
HETATM 6741 O O   . HOH L 5 .   ? -8.982  24.844  -19.117 1   33.22  ? 571 HOH B O   1 
HETATM 6742 O O   . HOH L 5 .   ? 11.933  30.367  -11.667 1   30.55  ? 572 HOH B O   1 
HETATM 6743 O O   . HOH L 5 .   ? 4.627   16.011  -21.296 1   32.21  ? 573 HOH B O   1 
HETATM 6744 O O   . HOH L 5 .   ? -17.264 7.835   -18.157 1   41.3   ? 574 HOH B O   1 
HETATM 6745 O O   . HOH L 5 .   ? -7.791  11.535  13.129  1   38.33  ? 575 HOH B O   1 
HETATM 6746 O O   . HOH L 5 .   ? -17.923 3.734   11.87   1   46.08  ? 576 HOH B O   1 
HETATM 6747 O O   . HOH L 5 .   ? -6.467  22.167  -6.577  1   33.92  ? 577 HOH B O   1 
HETATM 6748 O O   . HOH L 5 .   ? -17.288 17.7    -19.081 1   38.67  ? 578 HOH B O   1 
HETATM 6749 O O   . HOH L 5 .   ? 3.511   26.028  -0.024  1   29.56  ? 579 HOH B O   1 
HETATM 6750 O O   . HOH L 5 .   ? -11.506 25.486  -9.509  1   46.23  ? 580 HOH B O   1 
HETATM 6751 O O   . HOH L 5 .   ? -8.053  3.433   10.117  1   44.45  ? 581 HOH B O   1 
HETATM 6752 O O   . HOH L 5 .   ? -15.355 11.423  7.296   1   29.56  ? 582 HOH B O   1 
HETATM 6753 O O   . HOH L 5 .   ? -7.445  8.641   -23.051 1   34.68  ? 583 HOH B O   1 
HETATM 6754 O O   . HOH L 5 .   ? -7.052  21.673  -13.826 1   37.62  ? 584 HOH B O   1 
HETATM 6755 O O   . HOH L 5 .   ? -12.785 16.658  24.133  1   36.41  ? 585 HOH B O   1 
HETATM 6756 O O   . HOH L 5 .   ? -6.724  31.208  0.603   1   43.67  ? 586 HOH B O   1 
HETATM 6757 O O   . HOH L 5 .   ? 4.784   24.195  -3.652  1   26.96  ? 587 HOH B O   1 
HETATM 6758 O O   . HOH L 5 .   ? -12.041 1.044   -6.333  1   39.52  ? 588 HOH B O   1 
HETATM 6759 O O   . HOH L 5 .   ? -12.743 22.882  -12.328 1   35.47  ? 589 HOH B O   1 
HETATM 6760 O O   . HOH L 5 .   ? -18.775 13.021  4.923   1   41.65  ? 590 HOH B O   1 
HETATM 6761 O O   . HOH L 5 .   ? -13.168 33.453  22.673  1   48.85  ? 591 HOH B O   1 
HETATM 6762 O O   . HOH L 5 .   ? -23.632 30.627  5.361   1   47.99  ? 592 HOH B O   1 
HETATM 6763 O O   . HOH L 5 .   ? -8.184  20.21   -11.797 1   32.71  ? 593 HOH B O   1 
HETATM 6764 O O   . HOH L 5 .   ? -1.572  10.973  -23.675 1   34.45  ? 594 HOH B O   1 
HETATM 6765 O O   . HOH L 5 .   ? -6.225  34.301  13.503  1   42.28  ? 595 HOH B O   1 
HETATM 6766 O O   . HOH L 5 .   ? -5.977  25.484  24.135  1   53.67  ? 596 HOH B O   1 
HETATM 6767 O O   . HOH L 5 .   ? -16.272 20.214  6.818   1   35.35  ? 597 HOH B O   1 
HETATM 6768 O O   . HOH L 5 .   ? 0.413   33.46   -7.905  1   43.5   ? 598 HOH B O   1 
HETATM 6769 O O   . HOH L 5 .   ? -16.072 37.261  12.526  1   36.32  ? 599 HOH B O   1 
HETATM 6770 O O   . HOH L 5 .   ? 5.224   -0.524  -9.847  1   46.68  ? 600 HOH B O   1 
HETATM 6771 O O   . HOH L 5 .   ? -25.557 11.481  29.368  1   47.65  ? 601 HOH B O   1 
HETATM 6772 O O   . HOH L 5 .   ? 7.78    34.568  -16.974 1   42.43  ? 602 HOH B O   1 
HETATM 6773 O O   . HOH L 5 .   ? -17.151 15.112  -11.897 1   37.13  ? 603 HOH B O   1 
HETATM 6774 O O   . HOH L 5 .   ? -8.213  40.417  15.328  1   47.84  ? 604 HOH B O   1 
HETATM 6775 O O   . HOH L 5 .   ? -16.551 -3.665  19.723  1   52.93  ? 605 HOH B O   1 
HETATM 6776 O O   . HOH L 5 .   ? -12.772 26.924  -12.581 1   41.43  ? 606 HOH B O   1 
HETATM 6777 O O   . HOH L 5 .   ? -9.765  3.781   -17.955 1   33.02  ? 607 HOH B O   1 
HETATM 6778 O O   . HOH L 5 .   ? 1.252   -0.591  -3.45   1   50.2   ? 608 HOH B O   1 
HETATM 6779 O O   . HOH L 5 .   ? -15.177 7.905   9.334   1   40.63  ? 609 HOH B O   1 
HETATM 6780 O O   . HOH L 5 .   ? 9.821   20.965  -10.588 1   34.62  ? 610 HOH B O   1 
HETATM 6781 O O   . HOH L 5 .   ? -18.124 15.049  0.43    1   44.3   ? 611 HOH B O   1 
HETATM 6782 O O   . HOH L 5 .   ? -14.264 12.284  -13.781 1   33.19  ? 612 HOH B O   1 
HETATM 6783 O O   . HOH L 5 .   ? 4.894   10.952  -10.092 1   32.98  ? 613 HOH B O   1 
HETATM 6784 O O   . HOH L 5 .   ? -14.036 14.309  -16.949 1   32.26  ? 614 HOH B O   1 
HETATM 6785 O O   . HOH L 5 .   ? -10.262 9.108   13.695  1   38.38  ? 615 HOH B O   1 
HETATM 6786 O O   . HOH L 5 .   ? 1.867   12.149  -21.645 1   40.82  ? 616 HOH B O   1 
HETATM 6787 O O   . HOH L 5 .   ? 3.535   23.315  -1.432  1   28.11  ? 617 HOH B O   1 
HETATM 6788 O O   . HOH L 5 .   ? 0.885   23.026  -1.447  1   30     ? 618 HOH B O   1 
HETATM 6789 O O   . HOH L 5 .   ? -22.871 28.208  6.119   1   48.46  ? 619 HOH B O   1 
HETATM 6790 O O   . HOH L 5 .   ? 0       23.587  -35.767 0.5 41.79  ? 620 HOH B O   1 
HETATM 6791 O O   . HOH L 5 .   ? -5.146  3.948   11.754  1   43.85  ? 621 HOH B O   1 
HETATM 6792 O O   . HOH L 5 .   ? -14.969 21.312  5.036   1   34.99  ? 622 HOH B O   1 
HETATM 6793 O O   . HOH L 5 .   ? -2.017  34.79   14.272  1   50.12  ? 623 HOH B O   1 
HETATM 6794 O O   . HOH L 5 .   ? -20.319 11.262  -18.11  1   39.9   ? 624 HOH B O   1 
HETATM 6795 O O   . HOH L 5 .   ? -9.119  41.401  3.701   1   29.66  ? 625 HOH B O   1 
HETATM 6796 O O   . HOH L 5 .   ? -0.007  28.58   16.522  1   38.83  ? 626 HOH B O   1 
HETATM 6797 O O   . HOH L 5 .   ? -12.637 23.051  23.257  1   46.25  ? 627 HOH B O   1 
HETATM 6798 O O   . HOH L 5 .   ? -11.679 16.738  -34.559 1   40.76  ? 628 HOH B O   1 
HETATM 6799 O O   . HOH L 5 .   ? -14.272 8.01    -20.155 1   34.48  ? 629 HOH B O   1 
HETATM 6800 O O   . HOH L 5 .   ? -2.36   29.37   18.151  1   37.55  ? 630 HOH B O   1 
HETATM 6801 O O   . HOH L 5 .   ? 23.216  23.204  -22.567 1   45.96  ? 631 HOH B O   1 
HETATM 6802 O O   . HOH L 5 .   ? -14.88  19.853  -22.65  1   38.63  ? 632 HOH B O   1 
HETATM 6803 O O   . HOH L 5 .   ? -10.271 15.908  -13.746 1   38.01  ? 633 HOH B O   1 
HETATM 6804 O O   . HOH L 5 .   ? -22.85  -1.398  13.754  1   50.19  ? 634 HOH B O   1 
HETATM 6805 O O   . HOH L 5 .   ? -19.266 15.264  2.805   1   53.31  ? 635 HOH B O   1 
HETATM 6806 O O   . HOH L 5 .   ? 3.43    0.891   -13.547 1   43.85  ? 636 HOH B O   1 
HETATM 6807 O O   . HOH L 5 .   ? -22.165 26.972  8.39    1   34.26  ? 637 HOH B O   1 
HETATM 6808 O O   . HOH L 5 .   ? 1.394   2.211   -2.579  1   33.68  ? 638 HOH B O   1 
HETATM 6809 O O   . HOH L 5 .   ? -12.958 16.735  -6.965  1   30.19  ? 639 HOH B O   1 
HETATM 6810 O O   . HOH L 5 .   ? -11.265 34.146  -2.987  1   34.76  ? 640 HOH B O   1 
HETATM 6811 O O   . HOH L 5 .   ? 4.293   3.039   -15.02  1   40.48  ? 641 HOH B O   1 
HETATM 6812 O O   . HOH L 5 .   ? -9.066  13.031  17.502  1   39.23  ? 642 HOH B O   1 
HETATM 6813 O O   . HOH L 5 .   ? 7.432   8.549   -7.331  1   47.91  ? 643 HOH B O   1 
HETATM 6814 O O   . HOH L 5 .   ? -7.288  23.535  -9.247  1   37.03  ? 644 HOH B O   1 
HETATM 6815 O O   . HOH L 5 .   ? -1.897  34.673  -2.435  1   44.14  ? 645 HOH B O   1 
HETATM 6816 O O   . HOH L 5 .   ? -25.646 5.817   10.377  1   44.92  ? 646 HOH B O   1 
HETATM 6817 O O   . HOH L 5 .   ? 3.02    22.038  15.717  1   34.24  ? 647 HOH B O   1 
HETATM 6818 O O   . HOH L 5 .   ? -15.075 24.95   -12.917 1   40.29  ? 648 HOH B O   1 
HETATM 6819 O O   . HOH L 5 .   ? -12.034 22.979  1.836   1   35.8   ? 649 HOH B O   1 
HETATM 6820 O O   . HOH L 5 .   ? -14.653 11.038  31.104  1   42.01  ? 650 HOH B O   1 
HETATM 6821 O O   . HOH L 5 .   ? -17.955 6.549   -15.932 1   50.39  ? 651 HOH B O   1 
HETATM 6822 O O   . HOH L 5 .   ? -5.7    18.29   -18.245 1   44.27  ? 652 HOH B O   1 
HETATM 6823 O O   . HOH L 5 .   ? -27.578 24.116  23.721  1   47.19  ? 653 HOH B O   1 
HETATM 6824 O O   . HOH L 5 .   ? 24.368  22.407  -20.318 1   42.61  ? 654 HOH B O   1 
HETATM 6825 O O   . HOH L 5 .   ? -10.79  27.625  -8.242  1   43.76  ? 655 HOH B O   1 
HETATM 6826 O O   . HOH L 5 .   ? -15.875 30.741  27.225  1   45.74  ? 656 HOH B O   1 
HETATM 6827 O O   . HOH L 5 .   ? -8.562  17.055  -36.357 1   44.06  ? 657 HOH B O   1 
HETATM 6828 O O   . HOH L 5 .   ? -16.279 39.781  17.413  1   48.33  ? 658 HOH B O   1 
HETATM 6829 O O   . HOH L 5 .   ? 6.859   25.337  -10.284 1   36.07  ? 659 HOH B O   1 
HETATM 6830 O O   . HOH L 5 .   ? -12.343 2.963   18.925  1   52.91  ? 660 HOH B O   1 
HETATM 6831 O O   . HOH L 5 .   ? -18.857 36.366  18.106  1   37.15  ? 661 HOH B O   1 
HETATM 6832 O O   . HOH L 5 .   ? 9.456   24.166  -10.56  1   38.24  ? 662 HOH B O   1 
HETATM 6833 O O   . HOH L 5 .   ? 3.084   33.001  -0.816  1   45.93  ? 663 HOH B O   1 
HETATM 6834 O O   . HOH L 5 .   ? 4.707   3.100   6.076   1   42.65  ? 664 HOH B O   1 
HETATM 6835 O O   . HOH L 5 .   ? -12.02  25.972  1.642   1   37.36  ? 665 HOH B O   1 
HETATM 6836 O O   . HOH L 5 .   ? -15.092 17      25.341  1   42.38  ? 666 HOH B O   1 
HETATM 6837 O O   . HOH L 5 .   ? 5.979   6.322   3.05    1   45.23  ? 667 HOH B O   1 
HETATM 6838 O O   . HOH L 5 .   ? 7.345   26.59   -8.091  1   44.06  ? 668 HOH B O   1 
HETATM 6839 O O   . HOH L 5 .   ? 7.057   8.211   9.384   1   53.1   ? 669 HOH B O   1 
HETATM 6840 O O   . HOH L 5 .   ? 3.623   5.966   9.17    1   38.05  ? 670 HOH B O   1 
HETATM 6841 O O   . HOH L 5 .   ? 13.483  19.285  -16.861 1   50.53  ? 671 HOH B O   1 
HETATM 6842 O O   . HOH L 5 .   ? -17.449 36.226  10.588  1   39.99  ? 672 HOH B O   1 
HETATM 6843 O O   . HOH L 5 .   ? -7.903  12.141  21.136  1   48.61  ? 673 HOH B O   1 
HETATM 6844 O O   . HOH L 5 .   ? -6.497  38.512  11.61   1   42.9   ? 674 HOH B O   1 
HETATM 6845 O O   . HOH L 5 .   ? -15.109 0.398   -12.153 1   46.48  ? 675 HOH B O   1 
HETATM 6846 O O   . HOH L 5 .   ? 7.37    26.628  0.452   1   53.06  ? 676 HOH B O   1 
HETATM 6847 O O   . HOH L 5 .   ? 18.675  17.858  -18.134 1   55.26  ? 677 HOH B O   1 
HETATM 6848 O O   . HOH L 5 .   ? -11.689 19.414  -6.642  1   39.07  ? 678 HOH B O   1 
HETATM 6849 O O   . HOH L 5 .   ? -25.222 15.597  26.473  1   42.21  ? 679 HOH B O   1 
HETATM 6850 O O   . HOH L 5 .   ? 25.388  19.145  -17.478 1   59.22  ? 680 HOH B O   1 
HETATM 6851 O O   . HOH L 5 .   ? -6.790  40.485  4.398   1   39.15  ? 681 HOH B O   1 
HETATM 6852 O O   . HOH L 5 .   ? -11.888 19.367  -0.353  1   43.68  ? 682 HOH B O   1 
HETATM 6853 O O   . HOH L 5 .   ? -5.094  36.914  1.937   1   61.41  ? 683 HOH B O   1 
HETATM 6854 O O   . HOH L 5 .   ? -17.382 18.539  -21.608 1   40.15  ? 684 HOH B O   1 
HETATM 6855 O O   . HOH L 5 .   ? -16.143 12.679  -12.175 1   37.32  ? 685 HOH B O   1 
HETATM 6856 O O   . HOH L 5 .   ? -6.587  40.652  13.206  1   51.44  ? 686 HOH B O   1 
HETATM 6857 O O   . HOH L 5 .   ? 0.475   35.249  4.712   1   56.34  ? 687 HOH B O   1 
HETATM 6858 O O   . HOH L 5 .   ? -11.512 21.25   -8.627  1   35.52  ? 688 HOH B O   1 
HETATM 6859 O O   . HOH L 5 .   ? 5.841   1.557   -0.961  1   53.81  ? 689 HOH B O   1 
HETATM 6860 O O   . HOH L 5 .   ? -6.659  36.562  14.207  1   45.29  ? 690 HOH B O   1 
HETATM 6861 O O   . HOH L 5 .   ? 5.678   32.927  -1.154  1   46.34  ? 691 HOH B O   1 
HETATM 6862 O O   . HOH L 5 .   ? 5.901   5.533   5.802   1   39.31  ? 692 HOH B O   1 
HETATM 6863 O O   . HOH L 5 .   ? 0.715   13.387  -24.949 1   49.69  ? 693 HOH B O   1 
HETATM 6864 O O   . HOH L 5 .   ? -15.977 13.702  -26.339 1   38.05  ? 694 HOH B O   1 
HETATM 6865 O O   . HOH L 5 .   ? -23.487 11.546  5.358   1   65.58  ? 695 HOH B O   1 
HETATM 6866 O O   . HOH L 5 .   ? 3.832   0       0       0.5 47.08  ? 696 HOH B O   1 
HETATM 6867 O O   . HOH M 5 .   ? 25.207  38.234  0.126   1   37.35  ? 101 HOH C O   1 
HETATM 6868 O O   . HOH M 5 .   ? 24.08   40.823  11.47   1   44.49  ? 102 HOH C O   1 
HETATM 6869 O O   . HOH M 5 .   ? 18.333  43.056  12.67   1   25.9   ? 103 HOH C O   1 
HETATM 6870 O O   . HOH M 5 .   ? 27.429  39.196  4.244   1   34.71  ? 104 HOH C O   1 
HETATM 6871 O O   . HOH M 5 .   ? 33.213  43.066  -2.169  1   28.41  ? 105 HOH C O   1 
HETATM 6872 O O   . HOH N 5 .   ? -9.992  20.003  1.836   1   44.9   ? 101 HOH D O   1 
HETATM 6873 O O   . HOH N 5 .   ? -6.536  18.207  6.503   1   28.22  ? 102 HOH D O   1 
HETATM 6874 O O   . HOH N 5 .   ? -4.977  20.451  -7.981  1   40.64  ? 103 HOH D O   1 
HETATM 6875 O O   . HOH N 5 .   ? -8.426  20.223  -6.072  1   37.15  ? 104 HOH D 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   . MET A 1   ? 1.2244 1.1858 0.6798 0.0951  -0.1751 -0.2528 1   MET A N   
2    C CA  . MET A 1   ? 1.1775 1.1328 0.6552 0.0889  -0.1606 -0.2634 1   MET A CA  
3    C C   . MET A 1   ? 1.0577 1.021  0.5849 0.0836  -0.1591 -0.258  1   MET A C   
4    O O   . MET A 1   ? 1.0082 0.9829 0.5584 0.0799  -0.1745 -0.2628 1   MET A O   
5    C CB  . MET A 1   ? 1.2442 1.1965 0.7131 0.0848  -0.1692 -0.2868 1   MET A CB  
6    C CG  . MET A 1   ? 1.2559 1.2002 0.7487 0.0788  -0.1566 -0.2991 1   MET A CG  
7    S SD  . MET A 1   ? 1.3079 1.2371 0.7834 0.083   -0.1293 -0.296  1   MET A SD  
8    C CE  . MET A 1   ? 1.2021 1.1193 0.6838 0.078   -0.1261 -0.3214 1   MET A CE  
9    N N   . GLU A 2   ? 0.9489 0.907  0.4935 0.0826  -0.1403 -0.2498 2   GLU A N   
10   C CA  . GLU A 2   ? 0.9264 0.8917 0.5136 0.0785  -0.1386 -0.2418 2   GLU A CA  
11   C C   . GLU A 2   ? 0.8731 0.8372 0.4886 0.0711  -0.1396 -0.2572 2   GLU A C   
12   O O   . GLU A 2   ? 0.9076 0.8614 0.5125 0.0699  -0.1334 -0.2711 2   GLU A O   
13   C CB  . GLU A 2   ? 0.9394 0.9025 0.5371 0.0801  -0.1216 -0.2245 2   GLU A CB  
14   C CG  . GLU A 2   ? 0.9877 0.9406 0.5609 0.0834  -0.1035 -0.2229 2   GLU A CG  
15   C CD  . GLU A 2   ? 0.9879 0.9367 0.5189 0.089   -0.1034 -0.2161 2   GLU A CD  
16   O OE1 . GLU A 2   ? 0.9358 0.8888 0.4665 0.091   -0.1099 -0.2025 2   GLU A OE1 
17   O OE2 . GLU A 2   ? 1.0514 0.9925 0.5507 0.0915  -0.0978 -0.2241 2   GLU A OE2 
18   N N   . LEU A 3   ? 0.8242 0.7979 0.4753 0.0663  -0.1463 -0.2541 3   LEU A N   
19   C CA  . LEU A 3   ? 0.8588 0.8318 0.5393 0.0582  -0.1485 -0.2666 3   LEU A CA  
20   C C   . LEU A 3   ? 0.9076 0.8668 0.5974 0.0571  -0.1302 -0.2688 3   LEU A C   
21   O O   . LEU A 3   ? 0.8559 0.8064 0.5522 0.0523  -0.1298 -0.284  3   LEU A O   
22   C CB  . LEU A 3   ? 0.8031 0.7893 0.5193 0.0537  -0.1562 -0.2596 3   LEU A CB  
23   C CG  . LEU A 3   ? 0.9333 0.9356 0.6522 0.0524  -0.177  -0.264  3   LEU A CG  
24   C CD1 . LEU A 3   ? 1.0215 1.0311 0.7128 0.0611  -0.1869 -0.2555 3   LEU A CD1 
25   C CD2 . LEU A 3   ? 0.8787 0.8931 0.6383 0.0468  -0.1804 -0.2588 3   LEU A CD2 
26   N N   . ILE A 4   ? 0.8718 0.8293 0.564  0.0614  -0.1156 -0.2538 4   ILE A N   
27   C CA  . ILE A 4   ? 0.8475 0.7949 0.5515 0.0617  -0.0988 -0.2543 4   ILE A CA  
28   C C   . ILE A 4   ? 0.8751 0.81   0.5536 0.0645  -0.0924 -0.269  4   ILE A C   
29   O O   . ILE A 4   ? 0.8558 0.7801 0.5466 0.0622  -0.0868 -0.2797 4   ILE A O   
30   C CB  . ILE A 4   ? 0.8058 0.7565 0.5169 0.0655  -0.0855 -0.2359 4   ILE A CB  
31   C CG1 . ILE A 4   ? 0.801  0.7439 0.5301 0.0661  -0.0699 -0.2365 4   ILE A CG1 
32   C CG2 . ILE A 4   ? 0.7754 0.7269 0.4535 0.0716  -0.0804 -0.2283 4   ILE A CG2 
33   C CD1 . ILE A 4   ? 0.797  0.7344 0.5548 0.0603  -0.0727 -0.2444 4   ILE A CD1 
34   N N   . ARG A 5   ? 0.8507 0.7853 0.493  0.0694  -0.0935 -0.27   5   ARG A N   
35   C CA  . ARG A 5   ? 0.9052 0.8284 0.5195 0.0724  -0.0873 -0.284  5   ARG A CA  
36   C C   . ARG A 5   ? 0.9086 0.8246 0.524  0.067   -0.0982 -0.3048 5   ARG A C   
37   O O   . ARG A 5   ? 0.8352 0.7377 0.4474 0.0674  -0.0895 -0.3177 5   ARG A O   
38   C CB  . ARG A 5   ? 0.9986 0.9233 0.5724 0.0781  -0.0872 -0.2797 5   ARG A CB  
39   C CG  . ARG A 5   ? 0.9808 0.9089 0.5505 0.0826  -0.0722 -0.2618 5   ARG A CG  
40   C CD  . ARG A 5   ? 1.018  0.9475 0.5497 0.0867  -0.0749 -0.2543 5   ARG A CD  
41   N NE  . ARG A 5   ? 1.0883 1.0088 0.5827 0.0903  -0.0687 -0.2657 5   ARG A NE  
42   C CZ  . ARG A 5   ? 1.1023 1.0208 0.5565 0.0937  -0.073  -0.2642 5   ARG A CZ  
43   N NH1 . ARG A 5   ? 1.133  1.0427 0.5546 0.0965  -0.0671 -0.2764 5   ARG A NH1 
44   N NH2 . ARG A 5   ? 1.0688 0.9926 0.5134 0.0949  -0.083  -0.2504 5   ARG A NH2 
45   N N   . ILE A 6   ? 0.9136 0.8386 0.5357 0.0616  -0.1168 -0.308  6   ILE A N   
46   C CA  . ILE A 6   ? 1.0245 0.9452 0.649  0.0546  -0.129  -0.3277 6   ILE A CA  
47   C C   . ILE A 6   ? 0.9874 0.8987 0.6458 0.0484  -0.1225 -0.3334 6   ILE A C   
48   O O   . ILE A 6   ? 0.9243 0.821  0.5781 0.0453  -0.1209 -0.3506 6   ILE A O   
49   C CB  . ILE A 6   ? 1.0751 1.012  0.7013 0.0508  -0.1507 -0.3283 6   ILE A CB  
50   C CG1 . ILE A 6   ? 1.0912 1.0326 0.6756 0.0577  -0.1584 -0.3268 6   ILE A CG1 
51   C CG2 . ILE A 6   ? 1.111  1.0471 0.7523 0.0406  -0.1634 -0.3474 6   ILE A CG2 
52   C CD1 . ILE A 6   ? 1.0672 1.0266 0.6527 0.0576  -0.1786 -0.3218 6   ILE A CD1 
53   N N   . ALA A 7   ? 0.9381 0.856  0.6288 0.0464  -0.119  -0.3193 7   ALA A N   
54   C CA  . ALA A 7   ? 0.938  0.8467 0.6607 0.0404  -0.1135 -0.3224 7   ALA A CA  
55   C C   . ALA A 7   ? 0.9332 0.8231 0.6511 0.0454  -0.0962 -0.3273 7   ALA A C   
56   O O   . ALA A 7   ? 0.9009 0.7749 0.6278 0.041   -0.094  -0.3404 7   ALA A O   
57   C CB  . ALA A 7   ? 0.8893 0.809  0.6422 0.0388  -0.1121 -0.3049 7   ALA A CB  
58   N N   . MET A 8   ? 0.9229 0.8145 0.6255 0.0546  -0.0841 -0.3172 8   MET A N   
59   C CA  . MET A 8   ? 0.9437 0.8218 0.6418 0.0614  -0.067  -0.3202 8   MET A CA  
60   C C   . MET A 8   ? 0.9603 0.8223 0.6342 0.062   -0.0668 -0.3416 8   MET A C   
61   O O   . MET A 8   ? 0.9294 0.7745 0.6105 0.0632  -0.058  -0.3509 8   MET A O   
62   C CB  . MET A 8   ? 0.9026 0.7901 0.5899 0.0699  -0.0551 -0.305  8   MET A CB  
63   C CG  . MET A 8   ? 0.8799 0.7794 0.595  0.0689  -0.0532 -0.2854 8   MET A CG  
64   S SD  . MET A 8   ? 0.8257 0.7369 0.5375 0.0761  -0.0389 -0.2661 8   MET A SD  
65   C CE  . MET A 8   ? 0.9492 0.8634 0.6226 0.0831  -0.0297 -0.2649 8   MET A CE  
66   N N   . LYS A 9   ? 1.0243 0.8903 0.6675 0.0618  -0.0762 -0.3494 9   LYS A N   
67   C CA  . LYS A 9   ? 0.9651 0.8161 0.5828 0.0613  -0.078  -0.3711 9   LYS A CA  
68   C C   . LYS A 9   ? 0.9435 0.7823 0.5787 0.0514  -0.0869 -0.3869 9   LYS A C   
69   O O   . LYS A 9   ? 0.9601 0.7788 0.5903 0.052   -0.0796 -0.4017 9   LYS A O   
70   C CB  . LYS A 9   ? 1.0701 0.9306 0.6526 0.0624  -0.0891 -0.3738 9   LYS A CB  
71   C CG  . LYS A 9   ? 1.128  0.988  0.6776 0.0722  -0.0763 -0.37   9   LYS A CG  
72   C CD  . LYS A 9   ? 1.1572 1.0333 0.6882 0.0747  -0.0831 -0.3553 9   LYS A CD  
73   C CE  . LYS A 9   ? 1.2204 1.0928 0.7111 0.0822  -0.073  -0.3566 9   LYS A CE  
74   N NZ  . LYS A 9   ? 1.2205 1.1054 0.6916 0.0841  -0.0805 -0.3424 9   LYS A NZ  
75   N N   . LYS A 10  ? 0.9658 0.8163 0.6196 0.042   -0.1026 -0.385  10  LYS A N   
76   C CA  . LYS A 10  ? 1.0242 0.8662 0.7001 0.0304  -0.111  -0.3974 10  LYS A CA  
77   C C   . LYS A 10  ? 1.0412 0.8633 0.7393 0.0308  -0.0963 -0.3974 10  LYS A C   
78   O O   . LYS A 10  ? 1.0791 0.8804 0.7747 0.0265  -0.0949 -0.4146 10  LYS A O   
79   C CB  . LYS A 10  ? 1.1007 0.9632 0.8019 0.0222  -0.1254 -0.3882 10  LYS A CB  
80   C CG  . LYS A 10  ? 1.1485 1.0078 0.8793 0.0084  -0.1337 -0.3972 10  LYS A CG  
81   C CD  . LYS A 10  ? 1.248  1.1121 0.9712 -0.002  -0.1519 -0.4163 10  LYS A CD  
82   C CE  . LYS A 10  ? 1.2803 1.1211 1.0011 -0.0106 -0.1515 -0.4384 10  LYS A CE  
83   N NZ  . LYS A 10  ? 1.3676 1.1841 1.0638 -0.0019 -0.1369 -0.446  10  LYS A NZ  
84   N N   . ASP A 11  ? 0.9923 0.8198 0.7101 0.0364  -0.0855 -0.3782 11  ASP A N   
85   C CA  . ASP A 11  ? 0.9763 0.787  0.7157 0.0385  -0.0723 -0.375  11  ASP A CA  
86   C C   . ASP A 11  ? 1.0159 0.8078 0.7362 0.0487  -0.0577 -0.3841 11  ASP A C   
87   O O   . ASP A 11  ? 1.0486 0.8177 0.7763 0.0479  -0.0517 -0.3941 11  ASP A O   
88   C CB  . ASP A 11  ? 0.9406 0.7648 0.7048 0.0414  -0.0668 -0.3523 11  ASP A CB  
89   C CG  . ASP A 11  ? 0.9376 0.7732 0.7288 0.0308  -0.0775 -0.3448 11  ASP A CG  
90   O OD1 . ASP A 11  ? 0.9556 0.7832 0.7554 0.0201  -0.0859 -0.3573 11  ASP A OD1 
91   O OD2 . ASP A 11  ? 0.8824 0.7346 0.686  0.0327  -0.0771 -0.3272 11  ASP A OD2 
92   N N   . LEU A 12  ? 1.0376 0.8387 0.7335 0.0584  -0.0515 -0.3806 12  LEU A N   
93   C CA  . LEU A 12  ? 1.0966 0.8842 0.7734 0.0692  -0.0366 -0.3886 12  LEU A CA  
94   C C   . LEU A 12  ? 1.1844 0.9504 0.839  0.0666  -0.0392 -0.4135 12  LEU A C   
95   O O   . LEU A 12  ? 1.1343 0.8814 0.7826 0.0741  -0.0264 -0.4229 12  LEU A O   
96   C CB  . LEU A 12  ? 1.1376 0.9433 0.7931 0.0774  -0.031  -0.3784 12  LEU A CB  
97   C CG  . LEU A 12  ? 1.2394 1.0381 0.8759 0.0895  -0.0135 -0.3832 12  LEU A CG  
98   C CD1 . LEU A 12  ? 1.2034 1.0025 0.8675 0.097   0.0006  -0.3708 12  LEU A CD1 
99   C CD2 . LEU A 12  ? 1.233  1.0473 0.8402 0.0941  -0.0109 -0.3778 12  LEU A CD2 
100  N N   . GLU A 13  ? 1.2177 0.9867 0.8614 0.0561  -0.0561 -0.4245 13  GLU A N   
101  C CA  . GLU A 13  ? 1.2467 0.9968 0.873  0.0494  -0.0631 -0.449  13  GLU A CA  
102  C C   . GLU A 13  ? 1.2813 1.0038 0.9265 0.0474  -0.0552 -0.4579 13  GLU A C   
103  O O   . GLU A 13  ? 1.2661 0.9655 0.8937 0.0508  -0.0483 -0.4754 13  GLU A O   
104  C CB  . GLU A 13  ? 1.2092 0.973  0.8381 0.036   -0.0846 -0.4535 13  GLU A CB  
105  C CG  . GLU A 13  ? 1.2552 1.0127 0.857  0.0288  -0.0977 -0.4766 13  GLU A CG  
106  C CD  . GLU A 13  ? 1.2371 1.0152 0.8427 0.0172  -0.1201 -0.4788 13  GLU A CD  
107  O OE1 . GLU A 13  ? 1.1386 0.9411 0.7474 0.0204  -0.1255 -0.4612 13  GLU A OE1 
108  O OE2 . GLU A 13  ? 1.2    0.9706 0.8038 0.005   -0.1331 -0.4989 13  GLU A OE2 
109  N N   . ASN A 14  ? 1.251  0.9749 0.9309 0.0423  -0.0557 -0.4453 14  ASN A N   
110  C CA  . ASN A 14  ? 1.2946 0.9921 0.9947 0.0382  -0.0503 -0.4513 14  ASN A CA  
111  C C   . ASN A 14  ? 1.2164 0.9021 0.9273 0.052   -0.0319 -0.441  14  ASN A C   
112  O O   . ASN A 14  ? 1.2099 0.8694 0.9326 0.0512  -0.026  -0.4468 14  ASN A O   
113  C CB  . ASN A 14  ? 1.2866 0.9905 1.0166 0.0237  -0.0614 -0.445  14  ASN A CB  
114  C CG  . ASN A 14  ? 1.2728 0.9909 0.9956 0.0105  -0.0803 -0.4557 14  ASN A CG  
115  O OD1 . ASN A 14  ? 1.2888 0.9917 0.9981 0.0025  -0.0867 -0.477  14  ASN A OD1 
116  N ND2 . ASN A 14  ? 1.216  0.9637 0.947  0.0083  -0.0898 -0.4417 14  ASN A ND2 
117  N N   . ASP A 15  ? 1.1546 0.8586 0.8624 0.0643  -0.0229 -0.426  15  ASP A N   
118  C CA  . ASP A 15  ? 1.0942 0.7935 0.8177 0.0768  -0.0074 -0.4139 15  ASP A CA  
119  C C   . ASP A 15  ? 1.0651 0.7848 0.7754 0.0896  0.0023  -0.4044 15  ASP A C   
120  O O   . ASP A 15  ? 1.0022 0.7465 0.7216 0.0895  0.0004  -0.3866 15  ASP A O   
121  C CB  . ASP A 15  ? 1.0222 0.726  0.7794 0.0714  -0.01   -0.3967 15  ASP A CB  
122  C CG  . ASP A 15  ? 0.981  0.6787 0.758  0.0828  0.0034  -0.3835 15  ASP A CG  
123  O OD1 . ASP A 15  ? 0.9842 0.6727 0.7513 0.0961  0.0159  -0.3885 15  ASP A OD1 
124  O OD2 . ASP A 15  ? 0.9235 0.6264 0.7258 0.0782  0.0008  -0.3685 15  ASP A OD2 
125  N N   . ASN A 16  ? 1.1085 0.8172 0.7992 0.1007  0.0144  -0.4157 16  ASN A N   
126  C CA  . ASN A 16  ? 1.1355 0.8623 0.812  0.1122  0.0255  -0.409  16  ASN A CA  
127  C C   . ASN A 16  ? 1.1174 0.8547 0.819  0.1229  0.038   -0.3913 16  ASN A C   
128  O O   . ASN A 16  ? 1.0684 0.8258 0.7648 0.1305  0.0469  -0.3821 16  ASN A O   
129  C CB  . ASN A 16  ? 1.2395 0.9525 0.8846 0.1196  0.034   -0.4287 16  ASN A CB  
130  C CG  . ASN A 16  ? 1.2545 0.9893 0.8734 0.1225  0.0361  -0.4252 16  ASN A CG  
131  O OD1 . ASN A 16  ? 1.267  1.0236 0.8948 0.1277  0.0431  -0.4079 16  ASN A OD1 
132  N ND2 . ASN A 16  ? 1.276  1.0059 0.8626 0.1179  0.0292  -0.4404 16  ASN A ND2 
133  N N   . SER A 17  ? 1.0416 0.7654 0.7702 0.1231  0.0388  -0.3863 17  SER A N   
134  C CA  . SER A 17  ? 0.984  0.7192 0.7384 0.1316  0.0472  -0.3683 17  SER A CA  
135  C C   . SER A 17  ? 0.9189 0.683  0.6847 0.1251  0.0404  -0.3486 17  SER A C   
136  O O   . SER A 17  ? 0.8995 0.6811 0.6785 0.1325  0.0483  -0.3342 17  SER A O   
137  C CB  . SER A 17  ? 0.9364 0.6481 0.7134 0.1332  0.0486  -0.3675 17  SER A CB  
138  O OG  . SER A 17  ? 0.9031 0.6125 0.6954 0.1194  0.0361  -0.3609 17  SER A OG  
139  N N   . LEU A 18  ? 0.9115 0.6808 0.6728 0.1116  0.0259  -0.3485 18  LEU A N   
140  C CA  . LEU A 18  ? 0.8957 0.69   0.6663 0.1053  0.0185  -0.3311 18  LEU A CA  
141  C C   . LEU A 18  ? 0.884  0.7008 0.6417 0.1119  0.0261  -0.3224 18  LEU A C   
142  O O   . LEU A 18  ? 0.9051 0.7409 0.6764 0.1117  0.0268  -0.3052 18  LEU A O   
143  C CB  . LEU A 18  ? 0.8912 0.6877 0.6558 0.0915  0.0019  -0.3353 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.9346 0.7162 0.7192 0.0814  -0.0068 -0.3382 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.9582 0.7437 0.7341 0.0685  -0.0229 -0.3467 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.8884 0.6783 0.703  0.0805  -0.0056 -0.3191 18  LEU A CD2 
147  N N   . MET A 19  ? 0.9408 0.7548 0.6712 0.1171  0.0321  -0.3346 19  MET A N   
148  C CA  . MET A 19  ? 0.985  0.8179 0.6994 0.1227  0.0407  -0.3282 19  MET A CA  
149  C C   . MET A 19  ? 0.9728 0.8199 0.7087 0.1316  0.0541  -0.3141 19  MET A C   
150  O O   . MET A 19  ? 0.8716 0.7396 0.6129 0.1297  0.0549  -0.2985 19  MET A O   
151  C CB  . MET A 19  ? 1.06   0.8824 0.7416 0.1273  0.0463  -0.3466 19  MET A CB  
152  C CG  . MET A 19  ? 1.1119 0.9512 0.7711 0.1314  0.055   -0.342  19  MET A CG  
153  S SD  . MET A 19  ? 1.1312 0.991  0.7835 0.1216  0.0428  -0.3251 19  MET A SD  
154  C CE  . MET A 19  ? 1.1141 0.9925 0.7679 0.131   0.0635  -0.3138 19  MET A CE  
155  N N   . ASN A 20  ? 0.9753 0.8108 0.7242 0.1412  0.064   -0.3196 20  ASN A N   
156  C CA  . ASN A 20  ? 0.9625 0.812  0.7342 0.1506  0.0756  -0.3075 20  ASN A CA  
157  C C   . ASN A 20  ? 0.84   0.7004 0.6397 0.1453  0.0688  -0.2893 20  ASN A C   
158  O O   . ASN A 20  ? 0.7752 0.6565 0.5878 0.1485  0.075   -0.2758 20  ASN A O   
159  C CB  . ASN A 20  ? 1.0502 0.8834 0.8305 0.1633  0.0861  -0.3175 20  ASN A CB  
160  C CG  . ASN A 20  ? 1.1017 0.9441 0.8682 0.1745  0.1018  -0.3244 20  ASN A CG  
161  O OD1 . ASN A 20  ? 1.149  1.0168 0.9214 0.1769  0.1092  -0.3128 20  ASN A OD1 
162  N ND2 . ASN A 20  ? 1.1457 0.9684 0.8941 0.1807  0.1075  -0.343  20  ASN A ND2 
163  N N   . LYS A 21  ? 0.829  0.6752 0.6378 0.137   0.0566  -0.2895 21  LYS A N   
164  C CA  . LYS A 21  ? 0.8335 0.6873 0.6666 0.1312  0.0498  -0.2736 21  LYS A CA  
165  C C   . LYS A 21  ? 0.7889 0.6661 0.6174 0.1243  0.0454  -0.261  21  LYS A C   
166  O O   . LYS A 21  ? 0.6902 0.5837 0.5354 0.1251  0.048   -0.246  21  LYS A O   
167  C CB  . LYS A 21  ? 0.8636 0.696  0.7045 0.123   0.0391  -0.2788 21  LYS A CB  
168  C CG  . LYS A 21  ? 0.9195 0.7575 0.784  0.1161  0.0319  -0.2635 21  LYS A CG  
169  C CD  . LYS A 21  ? 1.0273 0.8426 0.9006 0.1084  0.0242  -0.2692 21  LYS A CD  
170  C CE  . LYS A 21  ? 1.0838 0.898  0.9476 0.0952  0.0115  -0.2761 21  LYS A CE  
171  N NZ  . LYS A 21  ? 1.075  0.9034 0.9537 0.0863  0.0033  -0.2622 21  LYS A NZ  
172  N N   . TRP A 22  ? 0.7929 0.6709 0.5968 0.1183  0.0394  -0.2677 22  TRP A N   
173  C CA  . TRP A 22  ? 0.7781 0.674  0.5735 0.1119  0.0341  -0.2568 22  TRP A CA  
174  C C   . TRP A 22  ? 0.7388 0.6532 0.5302 0.1178  0.0467  -0.248  22  TRP A C   
175  O O   . TRP A 22  ? 0.6955 0.6256 0.496  0.1141  0.0458  -0.2331 22  TRP A O   
176  C CB  . TRP A 22  ? 0.7985 0.6888 0.5667 0.1059  0.0241  -0.2673 22  TRP A CB  
177  C CG  . TRP A 22  ? 0.7532 0.6312 0.5275 0.0973  0.0098  -0.274  22  TRP A CG  
178  C CD1 . TRP A 22  ? 0.7377 0.6128 0.5382 0.0921  0.0038  -0.2677 22  TRP A CD1 
179  C CD2 . TRP A 22  ? 0.7523 0.621  0.5057 0.0921  -0.0005 -0.2888 22  TRP A CD2 
180  N NE1 . TRP A 22  ? 0.7322 0.597  0.5311 0.0837  -0.0084 -0.2777 22  TRP A NE1 
181  C CE2 . TRP A 22  ? 0.7411 0.6025 0.5121 0.0834  -0.012  -0.2908 22  TRP A CE2 
182  C CE3 . TRP A 22  ? 0.7785 0.6447 0.4994 0.0937  -0.001  -0.3005 22  TRP A CE3 
183  C CZ2 . TRP A 22  ? 0.7639 0.6174 0.5237 0.0759  -0.0244 -0.3047 22  TRP A CZ2 
184  C CZ3 . TRP A 22  ? 0.7835 0.6408 0.4911 0.0869  -0.014  -0.3143 22  TRP A CZ3 
185  C CH2 . TRP A 22  ? 0.7779 0.6297 0.5058 0.078   -0.0257 -0.3166 22  TRP A CH2 
186  N N   . ALA A 23  ? 0.7494 0.6619 0.5275 0.1263  0.0588  -0.2578 23  ALA A N   
187  C CA  . ALA A 23  ? 0.7692 0.6999 0.545  0.1319  0.0727  -0.2513 23  ALA A CA  
188  C C   . ALA A 23  ? 0.8039 0.7487 0.6112 0.1347  0.0776  -0.2376 23  ALA A C   
189  O O   . ALA A 23  ? 0.8372 0.8006 0.6487 0.1314  0.0805  -0.2247 23  ALA A O   
190  C CB  . ALA A 23  ? 0.8448 0.7697 0.605  0.1412  0.0851  -0.2657 23  ALA A CB  
191  N N   . THR A 24  ? 0.8061 0.741  0.6352 0.1399  0.0771  -0.2397 24  THR A N   
192  C CA  . THR A 24  ? 0.8032 0.7513 0.6614 0.1435  0.0805  -0.227  24  THR A CA  
193  C C   . THR A 24  ? 0.707  0.6625 0.5754 0.133   0.0699  -0.2126 24  THR A C   
194  O O   . THR A 24  ? 0.687  0.6619 0.5666 0.1321  0.0738  -0.2005 24  THR A O   
195  C CB  . THR A 24  ? 0.8488 0.7829 0.726  0.1525  0.0821  -0.2314 24  THR A CB  
196  O OG1 . THR A 24  ? 1.005  0.9185 0.8822 0.1453  0.0698  -0.2344 24  THR A OG1 
197  C CG2 . THR A 24  ? 0.8351 0.7606 0.7039 0.1646  0.0934  -0.246  24  THR A CG2 
198  N N   . VAL A 25  ? 0.7102 0.651  0.576  0.1253  0.0572  -0.2146 25  VAL A N   
199  C CA  . VAL A 25  ? 0.6874 0.6334 0.5614 0.1153  0.0466  -0.2027 25  VAL A CA  
200  C C   . VAL A 25  ? 0.6329 0.596  0.4948 0.1103  0.0474  -0.1938 25  VAL A C   
201  O O   . VAL A 25  ? 0.5518 0.5263 0.4257 0.1056  0.045   -0.1805 25  VAL A O   
202  C CB  . VAL A 25  ? 0.7686 0.6968 0.6373 0.1083  0.0341  -0.2104 25  VAL A CB  
203  C CG1 . VAL A 25  ? 0.8001 0.7346 0.6671 0.0981  0.023   -0.2024 25  VAL A CG1 
204  C CG2 . VAL A 25  ? 0.8569 0.769  0.7445 0.11    0.0321  -0.2129 25  VAL A CG2 
205  N N   . ALA A 26  ? 0.6833 0.646  0.519  0.1109  0.0507  -0.2013 26  ALA A N   
206  C CA  . ALA A 26  ? 0.6701 0.645  0.4894 0.1062  0.0519  -0.1933 26  ALA A CA  
207  C C   . ALA A 26  ? 0.705  0.6978 0.5295 0.1095  0.0659  -0.1859 26  ALA A C   
208  O O   . ALA A 26  ? 0.7232 0.7251 0.534  0.1052  0.0689  -0.1787 26  ALA A O   
209  C CB  . ALA A 26  ? 0.6792 0.6453 0.4666 0.1055  0.0495  -0.204  26  ALA A CB  
210  N N   . GLY A 27  ? 0.7572 0.7548 0.6002 0.1175  0.075   -0.1883 27  GLY A N   
211  C CA  . GLY A 27  ? 0.7255 0.7435 0.5789 0.1209  0.0879  -0.1819 27  GLY A CA  
212  C C   . GLY A 27  ? 0.7398 0.7625 0.5703 0.124   0.1002  -0.189  27  GLY A C   
213  O O   . GLY A 27  ? 0.7336 0.774  0.5649 0.1225  0.1103  -0.1823 27  GLY A O   
214  N N   . LEU A 28  ? 0.8002 0.807  0.6098 0.1278  0.0997  -0.203  28  LEU A N   
215  C CA  . LEU A 28  ? 0.8397 0.8486 0.6236 0.1309  0.1112  -0.211  28  LEU A CA  
216  C C   . LEU A 28  ? 0.892  0.908  0.6891 0.1425  0.1256  -0.2189 28  LEU A C   
217  O O   . LEU A 28  ? 0.8729 0.882  0.6901 0.1493  0.1233  -0.2233 28  LEU A O   
218  C CB  . LEU A 28  ? 0.8164 0.8045 0.5711 0.1294  0.1026  -0.2231 28  LEU A CB  
219  C CG  . LEU A 28  ? 0.7781 0.7594 0.5203 0.1196  0.0869  -0.2167 28  LEU A CG  
220  C CD1 . LEU A 28  ? 0.8013 0.7649 0.5137 0.1192  0.0792  -0.2307 28  LEU A CD1 
221  C CD2 . LEU A 28  ? 0.7405 0.7347 0.4732 0.1129  0.0896  -0.2024 28  LEU A CD2 
222  N N   . LYS A 29  ? 0.9379 0.9673 0.7229 0.1449  0.1407  -0.2207 29  LYS A N   
223  C CA  . LYS A 29  ? 1.0321 1.0707 0.8275 0.1567  0.156   -0.2293 29  LYS A CA  
224  C C   . LYS A 29  ? 1.1184 1.1345 0.8955 0.1645  0.1561  -0.2474 29  LYS A C   
225  O O   . LYS A 29  ? 1.1757 1.1869 0.9692 0.1754  0.1598  -0.2555 29  LYS A O   
226  C CB  . LYS A 29  ? 1.1286 1.1878 0.9137 0.1558  0.1731  -0.2269 29  LYS A CB  
227  C CG  . LYS A 29  ? 1.1396 1.2199 0.9341 0.1456  0.1756  -0.2103 29  LYS A CG  
228  C CD  . LYS A 29  ? 1.2313 1.3279 1.01   0.1439  0.194   -0.2103 29  LYS A CD  
229  C CE  . LYS A 29  ? 1.2708 1.3731 1.0343 0.1303  0.1943  -0.1968 29  LYS A CE  
230  N NZ  . LYS A 29  ? 1.2043 1.3238 0.997  0.1234  0.1914  -0.1826 29  LYS A NZ  
231  N N   . ASN A 30  ? 1.1185 1.1206 0.8606 0.1591  0.1518  -0.2538 30  ASN A N   
232  C CA  . ASN A 30  ? 1.1616 1.1416 0.8805 0.1642  0.1508  -0.2718 30  ASN A CA  
233  C C   . ASN A 30  ? 1.1301 1.092  0.8291 0.1546  0.1324  -0.2731 30  ASN A C   
234  O O   . ASN A 30  ? 1.0737 1.0416 0.7741 0.1452  0.123   -0.2599 30  ASN A O   
235  C CB  . ASN A 30  ? 1.1702 1.1563 0.864  0.1693  0.168   -0.2806 30  ASN A CB  
236  C CG  . ASN A 30  ? 1.1694 1.1632 0.8351 0.1598  0.1696  -0.2724 30  ASN A CG  
237  O OD1 . ASN A 30  ? 1.2135 1.2184 0.8881 0.1512  0.1646  -0.2566 30  ASN A OD1 
238  N ND2 . ASN A 30  ? 1.2835 1.27   0.9131 0.1611  0.1767  -0.2828 30  ASN A ND2 
239  N N   . PRO A 31  ? 1.1319 1.0713 0.8137 0.1566  0.1263  -0.2893 31  PRO A N   
240  C CA  . PRO A 31  ? 1.0985 1.0239 0.7585 0.1475  0.1094  -0.2924 31  PRO A CA  
241  C C   . PRO A 31  ? 1.0514 0.9794 0.6747 0.1414  0.107   -0.2905 31  PRO A C   
242  O O   . PRO A 31  ? 1.0245 0.9431 0.6349 0.1345  0.091   -0.2916 31  PRO A O   
243  C CB  . PRO A 31  ? 1.1547 1.0565 0.8074 0.1523  0.1066  -0.3124 31  PRO A CB  
244  C CG  . PRO A 31  ? 1.2321 1.1364 0.8845 0.1644  0.1258  -0.3212 31  PRO A CG  
245  C CD  . PRO A 31  ? 1.1956 1.1214 0.8822 0.1675  0.1334  -0.3053 31  PRO A CD  
246  N N   . ASN A 32  ? 1.0488 0.9894 0.6559 0.1438  0.1222  -0.287  32  ASN A N   
247  C CA  . ASN A 32  ? 1.0875 1.0258 0.6533 0.1397  0.1217  -0.2876 32  ASN A CA  
248  C C   . ASN A 32  ? 1.0437 0.9845 0.6032 0.13    0.1069  -0.2731 32  ASN A C   
249  O O   . ASN A 32  ? 1.0006 0.9303 0.5316 0.1267  0.0949  -0.2783 32  ASN A O   
250  C CB  . ASN A 32  ? 1.1103 1.0617 0.6607 0.1433  0.1426  -0.2855 32  ASN A CB  
251  C CG  . ASN A 32  ? 1.2122 1.156  0.7483 0.1527  0.1555  -0.3041 32  ASN A CG  
252  O OD1 . ASN A 32  ? 1.2423 1.1886 0.8051 0.1608  0.1638  -0.31   32  ASN A OD1 
253  N ND2 . ASN A 32  ? 1.2747 1.2082 0.7685 0.1527  0.157   -0.314  32  ASN A ND2 
254  N N   . PRO A 33  ? 1.0195 0.9743 0.6039 0.1256  0.1067  -0.2555 33  PRO A N   
255  C CA  . PRO A 33  ? 1.0347 0.9896 0.6162 0.1174  0.0916  -0.2425 33  PRO A CA  
256  C C   . PRO A 33  ? 0.9946 0.9364 0.5777 0.1144  0.0709  -0.2492 33  PRO A C   
257  O O   . PRO A 33  ? 0.9647 0.9031 0.5294 0.1098  0.0582  -0.245  33  PRO A O   
258  C CB  . PRO A 33  ? 0.9772 0.9475 0.5938 0.1143  0.0952  -0.2259 33  PRO A CB  
259  C CG  . PRO A 33  ? 0.9835 0.9658 0.617  0.1206  0.1142  -0.2283 33  PRO A CG  
260  C CD  . PRO A 33  ? 0.9967 0.9685 0.613  0.1285  0.1206  -0.2473 33  PRO A CD  
261  N N   . LEU A 34  ? 0.985  0.9195 0.5903 0.1172  0.068   -0.2597 34  LEU A N   
262  C CA  . LEU A 34  ? 0.958  0.8808 0.5698 0.1134  0.0501  -0.2669 34  LEU A CA  
263  C C   . LEU A 34  ? 0.9708 0.8801 0.5482 0.1135  0.0429  -0.2835 34  LEU A C   
264  O O   . LEU A 34  ? 0.9332 0.838  0.5036 0.1081  0.0258  -0.2856 34  LEU A O   
265  C CB  . LEU A 34  ? 1.0023 0.9209 0.6483 0.1165  0.0529  -0.2713 34  LEU A CB  
266  C CG  . LEU A 34  ? 1.0769 0.9862 0.7434 0.1112  0.0372  -0.2741 34  LEU A CG  
267  C CD1 . LEU A 34  ? 1.0087 0.9265 0.6845 0.1034  0.0241  -0.2602 34  LEU A CD1 
268  C CD2 . LEU A 34  ? 1.0825 0.989  0.7825 0.1153  0.0436  -0.2736 34  LEU A CD2 
269  N N   . TYR A 35  ? 1.0026 0.9062 0.5594 0.1197  0.0555  -0.2959 35  TYR A N   
270  C CA  . TYR A 35  ? 1.0812 0.9729 0.5995 0.1201  0.0504  -0.3112 35  TYR A CA  
271  C C   . TYR A 35  ? 1.1312 1.0282 0.6187 0.1162  0.043   -0.3018 35  TYR A C   
272  O O   . TYR A 35  ? 1.0944 0.9849 0.5638 0.1124  0.0261  -0.3079 35  TYR A O   
273  C CB  . TYR A 35  ? 1.0807 0.9665 0.5806 0.1282  0.0681  -0.3247 35  TYR A CB  
274  C CG  . TYR A 35  ? 1.0444 0.9202 0.5669 0.1341  0.0753  -0.3378 35  TYR A CG  
275  C CD1 . TYR A 35  ? 1.0358 0.8989 0.5786 0.1309  0.0626  -0.3454 35  TYR A CD1 
276  C CD2 . TYR A 35  ? 1.0672 0.9461 0.5911 0.1433  0.0957  -0.342  35  TYR A CD2 
277  C CE1 . TYR A 35  ? 1.0616 0.9124 0.6228 0.1369  0.0697  -0.3565 35  TYR A CE1 
278  C CE2 . TYR A 35  ? 1.0899 0.9583 0.6332 0.1506  0.1027  -0.3536 35  TYR A CE2 
279  C CZ  . TYR A 35  ? 1.0601 0.9132 0.6217 0.1474  0.0895  -0.3603 35  TYR A CZ  
280  O OH  . TYR A 35  ? 1.0588 0.8986 0.6376 0.1549  0.0967  -0.3709 35  TYR A OH  
281  N N   . ASP A 36  ? 1.0779 0.9868 0.5618 0.1169  0.055   -0.2863 36  ASP A N   
282  C CA  . ASP A 36  ? 1.0888 1.0012 0.5443 0.1138  0.0506  -0.2744 36  ASP A CA  
283  C C   . ASP A 36  ? 0.9756 0.8896 0.4433 0.108   0.0299  -0.2653 36  ASP A C   
284  O O   . ASP A 36  ? 0.92   0.8303 0.3614 0.1063  0.0162  -0.2649 36  ASP A O   
285  C CB  . ASP A 36  ? 1.1188 1.0432 0.5763 0.1142  0.0689  -0.2592 36  ASP A CB  
286  C CG  . ASP A 36  ? 1.1974 1.1206 0.6123 0.1138  0.0751  -0.2528 36  ASP A CG  
287  O OD1 . ASP A 36  ? 1.1765 1.0897 0.5569 0.1138  0.0638  -0.2591 36  ASP A OD1 
288  O OD2 . ASP A 36  ? 1.2628 1.1955 0.6796 0.113   0.0915  -0.2413 36  ASP A OD2 
289  N N   . PHE A 37  ? 0.9571 0.8775 0.4655 0.1056  0.0275  -0.2577 37  PHE A N   
290  C CA  . PHE A 37  ? 0.8935 0.8169 0.4181 0.1005  0.01    -0.249  37  PHE A CA  
291  C C   . PHE A 37  ? 0.9094 0.8248 0.4269 0.0984  -0.0087 -0.2634 37  PHE A C   
292  O O   . PHE A 37  ? 0.9775 0.8953 0.4884 0.0956  -0.0245 -0.2585 37  PHE A O   
293  C CB  . PHE A 37  ? 0.8494 0.7798 0.4187 0.0985  0.0124  -0.2409 37  PHE A CB  
294  C CG  . PHE A 37  ? 0.8126 0.7458 0.4009 0.0933  -0.0048 -0.234  37  PHE A CG  
295  C CD1 . PHE A 37  ? 0.8486 0.7883 0.4318 0.0912  -0.0093 -0.2179 37  PHE A CD1 
296  C CD2 . PHE A 37  ? 0.7876 0.7168 0.3989 0.0905  -0.0158 -0.2431 37  PHE A CD2 
297  C CE1 . PHE A 37  ? 0.8112 0.7544 0.4121 0.0874  -0.0241 -0.2116 37  PHE A CE1 
298  C CE2 . PHE A 37  ? 0.7807 0.7146 0.4096 0.0856  -0.0304 -0.2365 37  PHE A CE2 
299  C CZ  . PHE A 37  ? 0.7929 0.7346 0.4179 0.0846  -0.0342 -0.2207 37  PHE A CZ  
300  N N   . LEU A 38  ? 0.9001 0.8064 0.4227 0.0996  -0.0073 -0.2809 38  LEU A N   
301  C CA  . LEU A 38  ? 0.9164 0.8152 0.4373 0.0958  -0.0245 -0.2958 38  LEU A CA  
302  C C   . LEU A 38  ? 0.9474 0.842  0.4247 0.0967  -0.0334 -0.3042 38  LEU A C   
303  O O   . LEU A 38  ? 0.954  0.8497 0.4272 0.0928  -0.0523 -0.3085 38  LEU A O   
304  C CB  . LEU A 38  ? 0.9449 0.8321 0.4822 0.0964  -0.0195 -0.3121 38  LEU A CB  
305  C CG  . LEU A 38  ? 0.9251 0.8139 0.5071 0.0939  -0.0184 -0.3062 38  LEU A CG  
306  C CD1 . LEU A 38  ? 0.9592 0.8332 0.5533 0.096   -0.0113 -0.3215 38  LEU A CD1 
307  C CD2 . LEU A 38  ? 0.9216 0.8156 0.5214 0.0862  -0.0371 -0.302  38  LEU A CD2 
308  N N   . ASN A 39  ? 0.976  0.8669 0.4215 0.1018  -0.0197 -0.3062 39  ASN A N   
309  C CA  . ASN A 39  ? 1.0682 0.9514 0.4697 0.1035  -0.0254 -0.3187 39  ASN A CA  
310  C C   . ASN A 39  ? 1.1278 1.0157 0.4958 0.1048  -0.0293 -0.3051 39  ASN A C   
311  O O   . ASN A 39  ? 1.1744 1.0569 0.5055 0.1057  -0.0394 -0.3139 39  ASN A O   
312  C CB  . ASN A 39  ? 1.1177 0.991  0.5026 0.1085  -0.0076 -0.3329 39  ASN A CB  
313  C CG  . ASN A 39  ? 1.1231 0.9866 0.5325 0.1079  -0.0068 -0.3498 39  ASN A CG  
314  O OD1 . ASN A 39  ? 1.1586 1.0201 0.5895 0.1022  -0.0225 -0.355  39  ASN A OD1 
315  N ND2 . ASN A 39  ? 1.1187 0.9752 0.5247 0.1138  0.0116  -0.3587 39  ASN A ND2 
316  N N   . HIS A 40  ? 1.0414 0.9375 0.4182 0.1052  -0.0208 -0.2847 40  HIS A N   
317  C CA  . HIS A 40  ? 1.1162 1.0129 0.4581 0.107   -0.0204 -0.2713 40  HIS A CA  
318  C C   . HIS A 40  ? 1.0884 0.9932 0.45   0.1045  -0.0299 -0.2522 40  HIS A C   
319  O O   . HIS A 40  ? 0.9841 0.8956 0.3805 0.1024  -0.0216 -0.242  40  HIS A O   
320  C CB  . HIS A 40  ? 1.1433 1.0397 0.4693 0.1097  0.0041  -0.2648 40  HIS A CB  
321  C CG  . HIS A 40  ? 1.1853 1.0743 0.4922 0.1133  0.0161  -0.2828 40  HIS A CG  
322  N ND1 . HIS A 40  ? 1.2527 1.1324 0.5359 0.1142  0.0042  -0.3014 40  HIS A ND1 
323  C CD2 . HIS A 40  ? 1.2168 1.1067 0.5232 0.1163  0.0385  -0.2857 40  HIS A CD2 
324  C CE1 . HIS A 40  ? 1.2959 1.1691 0.5638 0.1179  0.0197  -0.3152 40  HIS A CE1 
325  N NE2 . HIS A 40  ? 1.2874 1.1674 0.5697 0.1197  0.0409  -0.3057 40  HIS A NE2 
326  N N   . ASP A 41  ? 1.1341 1.038  0.4715 0.1054  -0.0472 -0.2477 41  ASP A N   
327  C CA  . ASP A 41  ? 1.1563 1.0662 0.5067 0.1045  -0.0583 -0.2306 41  ASP A CA  
328  C C   . ASP A 41  ? 1.0919 1.0023 0.4431 0.1043  -0.0415 -0.2111 41  ASP A C   
329  O O   . ASP A 41  ? 1.0666 0.9715 0.3892 0.1058  -0.0259 -0.2082 41  ASP A O   
330  C CB  . ASP A 41  ? 1.2544 1.1621 0.5716 0.1077  -0.0779 -0.2293 41  ASP A CB  
331  C CG  . ASP A 41  ? 1.2705 1.1797 0.585  0.1071  -0.0973 -0.2485 41  ASP A CG  
332  O OD1 . ASP A 41  ? 1.2432 1.1587 0.5962 0.1027  -0.1036 -0.2569 41  ASP A OD1 
333  O OD2 . ASP A 41  ? 1.4704 1.3741 0.7437 0.1104  -0.1052 -0.2553 41  ASP A OD2 
334  N N   . GLY A 42  ? 1.1075 1.0247 0.4932 0.1017  -0.0439 -0.1987 42  GLY A N   
335  C CA  . GLY A 42  ? 1.1294 1.0471 0.5182 0.1003  -0.0307 -0.1799 42  GLY A CA  
336  C C   . GLY A 42  ? 1.085  1.0067 0.4924 0.0978  -0.0082 -0.1798 42  GLY A C   
337  O O   . GLY A 42  ? 1.0223 0.9455 0.4316 0.0956  0.0044  -0.1656 42  GLY A O   
338  N N   . LYS A 43  ? 1.0562 0.98   0.4781 0.0983  -0.0031 -0.1956 43  LYS A N   
339  C CA  . LYS A 43  ? 1.0738 1.0033 0.516  0.0975  0.0172  -0.1951 43  LYS A CA  
340  C C   . LYS A 43  ? 1.0036 0.9417 0.4925 0.0942  0.0144  -0.1884 43  LYS A C   
341  O O   . LYS A 43  ? 0.9578 0.8964 0.4694 0.0937  0.0023  -0.1965 43  LYS A O   
342  C CB  . LYS A 43  ? 1.204  1.1309 0.6406 0.1008  0.0263  -0.2134 43  LYS A CB  
343  C CG  . LYS A 43  ? 1.3581 1.2932 0.8182 0.1014  0.0472  -0.2124 43  LYS A CG  
344  C CD  . LYS A 43  ? 1.4262 1.3688 0.8839 0.099   0.064   -0.1966 43  LYS A CD  
345  C CE  . LYS A 43  ? 1.4095 1.3631 0.8941 0.1005  0.0826  -0.1994 43  LYS A CE  
346  N NZ  . LYS A 43  ? 1.3769 1.3394 0.8582 0.0972  0.0998  -0.1862 43  LYS A NZ  
347  N N   . THR A 44  ? 0.933  0.8769 0.434  0.0913  0.0249  -0.173  44  THR A N   
348  C CA  . THR A 44  ? 0.857  0.8093 0.3997 0.088   0.0241  -0.1656 44  THR A CA  
349  C C   . THR A 44  ? 0.8146 0.7753 0.3788 0.0885  0.0419  -0.1685 44  THR A C   
350  O O   . THR A 44  ? 0.8153 0.7775 0.3614 0.0899  0.0572  -0.1698 44  THR A O   
351  C CB  . THR A 44  ? 0.8505 0.8032 0.3921 0.0844  0.0222  -0.1473 44  THR A CB  
352  O OG1 . THR A 44  ? 0.8816 0.8338 0.4015 0.083   0.0385  -0.1395 44  THR A OG1 
353  C CG2 . THR A 44  ? 0.8556 0.8004 0.3762 0.0858  0.0042  -0.1442 44  THR A CG2 
354  N N   . PHE A 45  ? 0.7453 0.712  0.3477 0.0878  0.0399  -0.1693 45  PHE A N   
355  C CA  . PHE A 45  ? 0.737  0.7142 0.3644 0.0884  0.0552  -0.1681 45  PHE A CA  
356  C C   . PHE A 45  ? 0.7018 0.6875 0.3313 0.0836  0.0651  -0.152  45  PHE A C   
357  O O   . PHE A 45  ? 0.7238 0.7062 0.3475 0.0795  0.0573  -0.141  45  PHE A O   
358  C CB  . PHE A 45  ? 0.7348 0.7146 0.4002 0.0888  0.0488  -0.171  45  PHE A CB  
359  C CG  . PHE A 45  ? 0.7438 0.7137 0.4091 0.0923  0.0404  -0.1873 45  PHE A CG  
360  C CD1 . PHE A 45  ? 0.787  0.7541 0.4477 0.098   0.0504  -0.2005 45  PHE A CD1 
361  C CD2 . PHE A 45  ? 0.7357 0.699  0.4055 0.0896  0.0229  -0.19   45  PHE A CD2 
362  C CE1 . PHE A 45  ? 0.8006 0.7561 0.4599 0.1004  0.0429  -0.2161 45  PHE A CE1 
363  C CE2 . PHE A 45  ? 0.7653 0.7192 0.435  0.0911  0.0154  -0.2055 45  PHE A CE2 
364  C CZ  . PHE A 45  ? 0.7904 0.7392 0.4546 0.0963  0.0254  -0.2184 45  PHE A CZ  
365  N N   . ASN A 46  ? 0.7314 0.7285 0.3719 0.0841  0.0821  -0.151  46  ASN A N   
366  C CA  . ASN A 46  ? 0.7781 0.7855 0.4248 0.0783  0.0932  -0.1373 46  ASN A CA  
367  C C   . ASN A 46  ? 0.7008 0.7122 0.3764 0.0737  0.0846  -0.127  46  ASN A C   
368  O O   . ASN A 46  ? 0.7411 0.753  0.4123 0.0674  0.0862  -0.1143 46  ASN A O   
369  C CB  . ASN A 46  ? 0.8222 0.8453 0.4828 0.08    0.112   -0.1401 46  ASN A CB  
370  C CG  . ASN A 46  ? 0.969  0.9902 0.5988 0.0831  0.1249  -0.1477 46  ASN A CG  
371  O OD1 . ASN A 46  ? 1.0477 1.0555 0.6419 0.0829  0.1205  -0.1486 46  ASN A OD1 
372  N ND2 . ASN A 46  ? 1.0152 1.0504 0.6577 0.0867  0.1409  -0.1534 46  ASN A ND2 
373  N N   . GLU A 47  ? 0.6763 0.6888 0.379  0.0766  0.0762  -0.1325 47  GLU A N   
374  C CA  . GLU A 47  ? 0.6939 0.7095 0.4234 0.0727  0.0678  -0.1239 47  GLU A CA  
375  C C   . GLU A 47  ? 0.6404 0.6454 0.3739 0.0745  0.0508  -0.1296 47  GLU A C   
376  O O   . GLU A 47  ? 0.5967 0.5969 0.3322 0.0792  0.0475  -0.1419 47  GLU A O   
377  C CB  . GLU A 47  ? 0.6737 0.7045 0.4353 0.0734  0.0771  -0.1226 47  GLU A CB  
378  C CG  . GLU A 47  ? 0.7148 0.7592 0.478  0.0684  0.0914  -0.1136 47  GLU A CG  
379  C CD  . GLU A 47  ? 0.7513 0.7946 0.5123 0.0595  0.0887  -0.0995 47  GLU A CD  
380  O OE1 . GLU A 47  ? 0.6689 0.7033 0.4339 0.0578  0.0752  -0.0954 47  GLU A OE1 
381  O OE2 . GLU A 47  ? 0.7378 0.7884 0.4919 0.054   0.1009  -0.0928 47  GLU A OE2 
382  N N   . PHE A 48  ? 0.6006 0.6025 0.3379 0.0702  0.0406  -0.1204 48  PHE A N   
383  C CA  . PHE A 48  ? 0.5814 0.5755 0.3221 0.0706  0.0245  -0.1242 48  PHE A CA  
384  C C   . PHE A 48  ? 0.5919 0.5878 0.3628 0.0718  0.0208  -0.1301 48  PHE A C   
385  O O   . PHE A 48  ? 0.6199 0.6091 0.3927 0.0727  0.0098  -0.138  48  PHE A O   
386  C CB  . PHE A 48  ? 0.5982 0.5905 0.3375 0.0663  0.0174  -0.1117 48  PHE A CB  
387  C CG  . PHE A 48  ? 0.5715 0.557  0.3068 0.0672  0.0009  -0.1145 48  PHE A CG  
388  C CD1 . PHE A 48  ? 0.6054 0.5837 0.3108 0.07    -0.0055 -0.1188 48  PHE A CD1 
389  C CD2 . PHE A 48  ? 0.542  0.5294 0.3027 0.0654  -0.008  -0.1135 48  PHE A CD2 
390  C CE1 . PHE A 48  ? 0.5946 0.5695 0.2978 0.0711  -0.0215 -0.1218 48  PHE A CE1 
391  C CE2 . PHE A 48  ? 0.5704 0.5542 0.3289 0.066   -0.0227 -0.1165 48  PHE A CE2 
392  C CZ  . PHE A 48  ? 0.5925 0.571  0.3231 0.0689  -0.0298 -0.1207 48  PHE A CZ  
393  N N   . SER A 49  ? 0.5398 0.5448 0.3332 0.0718  0.0299  -0.1265 49  SER A N   
394  C CA  . SER A 49  ? 0.5658 0.5718 0.3857 0.0744  0.0294  -0.1314 49  SER A CA  
395  C C   . SER A 49  ? 0.5785 0.5753 0.392  0.0795  0.0278  -0.1466 49  SER A C   
396  O O   . SER A 49  ? 0.6129 0.6034 0.442  0.0801  0.0214  -0.1519 49  SER A O   
397  C CB  . SER A 49  ? 0.5257 0.5448 0.3637 0.0755  0.0416  -0.1261 49  SER A CB  
398  O OG  . SER A 49  ? 0.5469 0.5715 0.3687 0.0779  0.0538  -0.1288 49  SER A OG  
399  N N   . SER A 50  ? 0.5768 0.5715 0.3663 0.0827  0.0338  -0.1536 50  SER A N   
400  C CA  . SER A 50  ? 0.6436 0.6285 0.4234 0.0876  0.0335  -0.1691 50  SER A CA  
401  C C   . SER A 50  ? 0.6589 0.6325 0.4352 0.0849  0.018   -0.1762 50  SER A C   
402  O O   . SER A 50  ? 0.6679 0.6336 0.4567 0.0862  0.0147  -0.1854 50  SER A O   
403  C CB  . SER A 50  ? 0.663  0.6475 0.4135 0.0906  0.0421  -0.1747 50  SER A CB  
404  O OG  . SER A 50  ? 0.6817 0.6772 0.4396 0.094   0.0579  -0.1722 50  SER A OG  
405  N N   . ILE A 51  ? 0.649  0.622  0.4091 0.0811  0.0085  -0.1719 51  ILE A N   
406  C CA  . ILE A 51  ? 0.6329 0.599  0.3908 0.0785  -0.0067 -0.1788 51  ILE A CA  
407  C C   . ILE A 51  ? 0.6111 0.5788 0.3993 0.0744  -0.0136 -0.1738 51  ILE A C   
408  O O   . ILE A 51  ? 0.5858 0.5471 0.3833 0.0726  -0.0215 -0.1829 51  ILE A O   
409  C CB  . ILE A 51  ? 0.6925 0.6583 0.4228 0.0775  -0.0152 -0.1764 51  ILE A CB  
410  C CG1 . ILE A 51  ? 0.7239 0.6849 0.4514 0.0755  -0.0314 -0.1865 51  ILE A CG1 
411  C CG2 . ILE A 51  ? 0.6776 0.65   0.4103 0.0749  -0.016  -0.1598 51  ILE A CG2 
412  C CD1 . ILE A 51  ? 0.7492 0.7012 0.4718 0.0768  -0.0319 -0.2042 51  ILE A CD1 
413  N N   . VAL A 52  ? 0.5595 0.5351 0.3628 0.0725  -0.0102 -0.1599 52  VAL A N   
414  C CA  . VAL A 52  ? 0.5533 0.5304 0.3836 0.0687  -0.0159 -0.1548 52  VAL A CA  
415  C C   . VAL A 52  ? 0.5445 0.5158 0.3942 0.0703  -0.012  -0.1617 52  VAL A C   
416  O O   . VAL A 52  ? 0.5786 0.5446 0.4426 0.067   -0.0194 -0.1654 52  VAL A O   
417  C CB  . VAL A 52  ? 0.537  0.5228 0.3781 0.0665  -0.0118 -0.1394 52  VAL A CB  
418  C CG1 . VAL A 52  ? 0.526  0.5128 0.3941 0.063   -0.016  -0.1345 52  VAL A CG1 
419  C CG2 . VAL A 52  ? 0.5619 0.5501 0.3843 0.0649  -0.0159 -0.1314 52  VAL A CG2 
420  N N   . ASN A 53  ? 0.5643 0.5366 0.4144 0.0754  -0.0001 -0.1631 53  ASN A N   
421  C CA  . ASN A 53  ? 0.5477 0.5136 0.4155 0.0788  0.0043  -0.1682 53  ASN A CA  
422  C C   . ASN A 53  ? 0.5589 0.5103 0.42   0.0791  -0.0007 -0.1836 53  ASN A C   
423  O O   . ASN A 53  ? 0.5828 0.5248 0.4603 0.0782  -0.0029 -0.1872 53  ASN A O   
424  C CB  . ASN A 53  ? 0.5393 0.5115 0.4097 0.0857  0.0179  -0.1669 53  ASN A CB  
425  C CG  . ASN A 53  ? 0.5334 0.5202 0.4166 0.0844  0.0228  -0.1524 53  ASN A CG  
426  O OD1 . ASN A 53  ? 0.5147 0.5047 0.4062 0.0788  0.0166  -0.1432 53  ASN A OD1 
427  N ND2 . ASN A 53  ? 0.5844 0.581  0.4682 0.0893  0.0344  -0.1509 53  ASN A ND2 
428  N N   . ILE A 54  ? 0.5161 0.4648 0.3521 0.0799  -0.0026 -0.1927 54  ILE A N   
429  C CA  . ILE A 54  ? 0.5748 0.5099 0.4024 0.0791  -0.0085 -0.2086 54  ILE A CA  
430  C C   . ILE A 54  ? 0.5625 0.4948 0.4016 0.0711  -0.0221 -0.2097 54  ILE A C   
431  O O   . ILE A 54  ? 0.5893 0.5093 0.4373 0.0687  -0.0252 -0.2196 54  ILE A O   
432  C CB  . ILE A 54  ? 0.593  0.5267 0.3888 0.0814  -0.0086 -0.2178 54  ILE A CB  
433  C CG1 . ILE A 54  ? 0.6259 0.5606 0.4118 0.0894  0.0067  -0.22   54  ILE A CG1 
434  C CG2 . ILE A 54  ? 0.6293 0.5501 0.4163 0.0784  -0.0181 -0.2344 54  ILE A CG2 
435  C CD1 . ILE A 54  ? 0.6773 0.6135 0.4297 0.0918  0.0096  -0.2251 54  ILE A CD1 
436  N N   . VAL A 55  ? 0.5543 0.4974 0.3911 0.0672  -0.0299 -0.2007 55  VAL A N   
437  C CA  . VAL A 55  ? 0.565  0.5091 0.4106 0.0603  -0.0431 -0.2026 55  VAL A CA  
438  C C   . VAL A 55  ? 0.5961 0.5373 0.4709 0.0567  -0.0419 -0.1978 55  VAL A C   
439  O O   . VAL A 55  ? 0.6028 0.5369 0.4883 0.0512  -0.0481 -0.2059 55  VAL A O   
440  C CB  . VAL A 55  ? 0.6169 0.5732 0.4533 0.0591  -0.0508 -0.1933 55  VAL A CB  
441  C CG1 . VAL A 55  ? 0.6558 0.6169 0.5086 0.0527  -0.063  -0.1927 55  VAL A CG1 
442  C CG2 . VAL A 55  ? 0.6317 0.5881 0.4367 0.0621  -0.0544 -0.1998 55  VAL A CG2 
443  N N   . LYS A 56  ? 0.5586 0.5049 0.4451 0.0592  -0.0336 -0.185  56  LYS A N   
444  C CA  . LYS A 56  ? 0.5963 0.5398 0.5078 0.0566  -0.0318 -0.1788 56  LYS A CA  
445  C C   . LYS A 56  ? 0.5971 0.5246 0.5162 0.0582  -0.0272 -0.1877 56  LYS A C   
446  O O   . LYS A 56  ? 0.6446 0.565  0.5806 0.0534  -0.0296 -0.1874 56  LYS A O   
447  C CB  . LYS A 56  ? 0.5974 0.5503 0.5171 0.0595  -0.0243 -0.164  56  LYS A CB  
448  C CG  . LYS A 56  ? 0.6206 0.5856 0.5397 0.056   -0.0294 -0.1534 56  LYS A CG  
449  C CD  . LYS A 56  ? 0.6231 0.5962 0.5512 0.0575  -0.0221 -0.1398 56  LYS A CD  
450  C CE  . LYS A 56  ? 0.625  0.6064 0.5559 0.0534  -0.027  -0.1296 56  LYS A CE  
451  N NZ  . LYS A 56  ? 0.5902 0.5696 0.5395 0.0483  -0.0326 -0.128  56  LYS A NZ  
452  N N   . SER A 57  ? 0.5772 0.4986 0.4836 0.0651  -0.02   -0.1953 57  SER A N   
453  C CA  . SER A 57  ? 0.6334 0.5379 0.545  0.0686  -0.0145 -0.2039 57  SER A CA  
454  C C   . SER A 57  ? 0.7027 0.593  0.6089 0.0626  -0.0221 -0.2193 57  SER A C   
455  O O   . SER A 57  ? 0.6748 0.5501 0.5937 0.0591  -0.0226 -0.2234 57  SER A O   
456  C CB  . SER A 57  ? 0.61   0.5143 0.5099 0.0788  -0.0037 -0.2074 57  SER A CB  
457  O OG  . SER A 57  ? 0.7309 0.6166 0.626  0.0826  -0.0003 -0.2214 57  SER A OG  
458  N N   . GLN A 58  ? 0.7176 0.6114 0.603  0.0617  -0.0273 -0.2284 58  GLN A N   
459  C CA  . GLN A 58  ? 0.7    0.5817 0.5769 0.0564  -0.0346 -0.2451 58  GLN A CA  
460  C C   . GLN A 58  ? 0.6928 0.5808 0.5797 0.0456  -0.0477 -0.2456 58  GLN A C   
461  O O   . GLN A 58  ? 0.6847 0.5613 0.5762 0.0385  -0.0532 -0.2576 58  GLN A O   
462  C CB  . GLN A 58  ? 0.7507 0.6338 0.5988 0.0609  -0.0346 -0.255  58  GLN A CB  
463  C CG  . GLN A 58  ? 0.7971 0.6656 0.6328 0.0568  -0.0406 -0.2745 58  GLN A CG  
464  C CD  . GLN A 58  ? 0.8474 0.6931 0.6895 0.0591  -0.0328 -0.2842 58  GLN A CD  
465  O OE1 . GLN A 58  ? 0.7652 0.606  0.6079 0.0686  -0.0206 -0.2808 58  GLN A OE1 
466  N NE2 . GLN A 58  ? 0.8882 0.7194 0.7342 0.0508  -0.0395 -0.2971 58  GLN A NE2 
467  N N   . TYR A 59  ? 0.6733 0.5796 0.5627 0.0442  -0.0529 -0.234  59  TYR A N   
468  C CA  . TYR A 59  ? 0.6797 0.5957 0.5755 0.0358  -0.0659 -0.2356 59  TYR A CA  
469  C C   . TYR A 59  ? 0.6562 0.5838 0.5721 0.0333  -0.0664 -0.2201 59  TYR A C   
470  O O   . TYR A 59  ? 0.6484 0.5907 0.5628 0.032   -0.0741 -0.215  59  TYR A O   
471  C CB  . TYR A 59  ? 0.7041 0.6311 0.5767 0.0376  -0.0747 -0.2396 59  TYR A CB  
472  C CG  . TYR A 59  ? 0.6922 0.6086 0.5412 0.0401  -0.0747 -0.2553 59  TYR A CG  
473  C CD1 . TYR A 59  ? 0.7409 0.6473 0.5914 0.0332  -0.0816 -0.2718 59  TYR A CD1 
474  C CD2 . TYR A 59  ? 0.7397 0.6554 0.5652 0.0487  -0.067  -0.2542 59  TYR A CD2 
475  C CE1 . TYR A 59  ? 0.744  0.6392 0.5716 0.0353  -0.0814 -0.2873 59  TYR A CE1 
476  C CE2 . TYR A 59  ? 0.7493 0.6545 0.5519 0.0513  -0.066  -0.2693 59  TYR A CE2 
477  C CZ  . TYR A 59  ? 0.7625 0.657  0.5656 0.0448  -0.0735 -0.286  59  TYR A CZ  
478  O OH  . TYR A 59  ? 0.7853 0.6683 0.5647 0.0474  -0.072  -0.3014 59  TYR A OH  
479  N N   . PRO A 60  ? 0.6764 0.5974 0.6114 0.0325  -0.0588 -0.2125 60  PRO A N   
480  C CA  . PRO A 60  ? 0.6981 0.6303 0.6489 0.0311  -0.0582 -0.1973 60  PRO A CA  
481  C C   . PRO A 60  ? 0.7226 0.6662 0.6844 0.0232  -0.069  -0.1977 60  PRO A C   
482  O O   . PRO A 60  ? 0.6402 0.5975 0.6051 0.0239  -0.0717 -0.1875 60  PRO A O   
483  C CB  . PRO A 60  ? 0.6683 0.5875 0.635  0.0312  -0.0491 -0.1926 60  PRO A CB  
484  C CG  . PRO A 60  ? 0.6779 0.5786 0.6431 0.0283  -0.0492 -0.2075 60  PRO A CG  
485  C CD  . PRO A 60  ? 0.6854 0.5868 0.6266 0.0331  -0.0513 -0.2184 60  PRO A CD  
486  N N   . ASP A 61  ? 0.7459 0.6844 0.7134 0.0156  -0.0755 -0.2105 61  ASP A N   
487  C CA  . ASP A 61  ? 0.7367 0.6879 0.7171 0.0076  -0.0861 -0.2134 61  ASP A CA  
488  C C   . ASP A 61  ? 0.6437 0.6108 0.609  0.0108  -0.0971 -0.216  61  ASP A C   
489  O O   . ASP A 61  ? 0.6772 0.6591 0.6541 0.0072  -0.1052 -0.214  61  ASP A O   
490  C CB  . ASP A 61  ? 0.8624 0.8027 0.8549 -0.0024 -0.0886 -0.2266 61  ASP A CB  
491  C CG  . ASP A 61  ? 0.9624 0.8889 0.9379 -0.0023 -0.0901 -0.2429 61  ASP A CG  
492  O OD1 . ASP A 61  ? 1.0045 0.9182 0.9656 0.0056  -0.0816 -0.2425 61  ASP A OD1 
493  O OD2 . ASP A 61  ? 1.2395 1.1684 1.2166 -0.0101 -0.0997 -0.2564 61  ASP A OD2 
494  N N   . ARG A 62  ? 0.6281 0.5925 0.5677 0.0177  -0.0974 -0.2201 62  ARG A N   
495  C CA  . ARG A 62  ? 0.6887 0.6654 0.61   0.0212  -0.108  -0.2224 62  ARG A CA  
496  C C   . ARG A 62  ? 0.6713 0.6534 0.5771 0.0302  -0.1034 -0.2082 62  ARG A C   
497  O O   . ARG A 62  ? 0.6971 0.684  0.5806 0.035   -0.1093 -0.2092 62  ARG A O   
498  C CB  . ARG A 62  ? 0.7459 0.7154 0.6456 0.0214  -0.1132 -0.2388 62  ARG A CB  
499  C CG  . ARG A 62  ? 0.7785 0.7422 0.6867 0.0121  -0.12   -0.2562 62  ARG A CG  
500  C CD  . ARG A 62  ? 0.826  0.7799 0.7085 0.0135  -0.1232 -0.2722 62  ARG A CD  
501  N NE  . ARG A 62  ? 0.8111 0.7771 0.6709 0.0171  -0.1355 -0.2764 62  ARG A NE  
502  C CZ  . ARG A 62  ? 0.9259 0.8855 0.7569 0.0203  -0.1385 -0.2878 62  ARG A CZ  
503  N NH1 . ARG A 62  ? 1.0061 0.9468 0.8279 0.0198  -0.1305 -0.2992 62  ARG A NH1 
504  N NH2 . ARG A 62  ? 0.9395 0.9106 0.7487 0.0247  -0.1495 -0.2883 62  ARG A NH2 
505  N N   . GLU A 63  ? 0.5982 0.579  0.5144 0.0321  -0.0932 -0.1947 63  GLU A N   
506  C CA  . GLU A 63  ? 0.6041 0.5869 0.5046 0.0394  -0.0865 -0.183  63  GLU A CA  
507  C C   . GLU A 63  ? 0.5431 0.5373 0.4314 0.0424  -0.0958 -0.1775 63  GLU A C   
508  O O   . GLU A 63  ? 0.5618 0.555  0.4245 0.0476  -0.0966 -0.1777 63  GLU A O   
509  C CB  . GLU A 63  ? 0.5358 0.5169 0.4512 0.0398  -0.0754 -0.1705 63  GLU A CB  
510  C CG  . GLU A 63  ? 0.5719 0.5552 0.472  0.0458  -0.0678 -0.1595 63  GLU A CG  
511  C CD  . GLU A 63  ? 0.6091 0.5924 0.5232 0.0461  -0.0577 -0.1478 63  GLU A CD  
512  O OE1 . GLU A 63  ? 0.6004 0.5797 0.5341 0.0429  -0.055  -0.1481 63  GLU A OE1 
513  O OE2 . GLU A 63  ? 0.5712 0.5584 0.4757 0.0491  -0.0527 -0.1381 63  GLU A OE2 
514  N N   . TYR A 64  ? 0.6111 0.6154 0.5173 0.0394  -0.1028 -0.1732 64  TYR A N   
515  C CA  . TYR A 64  ? 0.6162 0.6306 0.5136 0.0437  -0.1113 -0.1664 64  TYR A CA  
516  C C   . TYR A 64  ? 0.6802 0.6972 0.5554 0.0467  -0.1226 -0.1759 64  TYR A C   
517  O O   . TYR A 64  ? 0.627  0.6425 0.4768 0.0532  -0.1232 -0.1704 64  TYR A O   
518  C CB  . TYR A 64  ? 0.6393 0.6646 0.5625 0.0404  -0.1161 -0.1616 64  TYR A CB  
519  C CG  . TYR A 64  ? 0.6398 0.6744 0.554  0.0465  -0.1243 -0.1541 64  TYR A CG  
520  C CD1 . TYR A 64  ? 0.6543 0.6858 0.5618 0.0509  -0.1176 -0.14   64  TYR A CD1 
521  C CD2 . TYR A 64  ? 0.6733 0.7186 0.584  0.0483  -0.139  -0.1613 64  TYR A CD2 
522  C CE1 . TYR A 64  ? 0.6704 0.707  0.5681 0.0571  -0.1246 -0.1327 64  TYR A CE1 
523  C CE2 . TYR A 64  ? 0.6919 0.7441 0.5925 0.0557  -0.1469 -0.1539 64  TYR A CE2 
524  C CZ  . TYR A 64  ? 0.7028 0.7492 0.5963 0.0603  -0.1393 -0.1393 64  TYR A CZ  
525  O OH  . TYR A 64  ? 0.7255 0.7762 0.6092 0.0679  -0.1468 -0.1319 64  TYR A OH  
526  N N   . GLU A 65  ? 0.7043 0.7239 0.5875 0.0414  -0.131  -0.1905 65  GLU A N   
527  C CA  . GLU A 65  ? 0.6566 0.6799 0.5208 0.0431  -0.1434 -0.2016 65  GLU A CA  
528  C C   . GLU A 65  ? 0.6964 0.7085 0.5267 0.049   -0.1377 -0.2022 65  GLU A C   
529  O O   . GLU A 65  ? 0.6629 0.6777 0.4682 0.0549  -0.1449 -0.2006 65  GLU A O   
530  C CB  . GLU A 65  ? 0.7299 0.7535 0.6086 0.0344  -0.1494 -0.2185 65  GLU A CB  
531  C CG  . GLU A 65  ? 0.8098 0.8356 0.668  0.0346  -0.1621 -0.2333 65  GLU A CG  
532  C CD  . GLU A 65  ? 0.8047 0.8193 0.6617 0.0277  -0.161  -0.2507 65  GLU A CD  
533  O OE1 . GLU A 65  ? 0.8509 0.8578 0.7299 0.0208  -0.1531 -0.2531 65  GLU A OE1 
534  O OE2 . GLU A 65  ? 0.8452 0.8571 0.678  0.0292  -0.168  -0.262  65  GLU A OE2 
535  N N   . LEU A 66  ? 0.6599 0.6592 0.4888 0.0476  -0.1248 -0.2052 66  LEU A N   
536  C CA  . LEU A 66  ? 0.6716 0.6612 0.47   0.0525  -0.1187 -0.2086 66  LEU A CA  
537  C C   . LEU A 66  ? 0.6196 0.6092 0.4008 0.059   -0.1116 -0.1932 66  LEU A C   
538  O O   . LEU A 66  ? 0.6542 0.641  0.4048 0.0639  -0.1129 -0.1938 66  LEU A O   
539  C CB  . LEU A 66  ? 0.7071 0.6841 0.5113 0.0503  -0.1068 -0.2164 66  LEU A CB  
540  C CG  . LEU A 66  ? 0.7596 0.7322 0.575  0.0435  -0.1133 -0.2333 66  LEU A CG  
541  C CD1 . LEU A 66  ? 0.7516 0.7098 0.5792 0.0414  -0.1011 -0.2383 66  LEU A CD1 
542  C CD2 . LEU A 66  ? 0.7806 0.7525 0.569  0.0446  -0.1236 -0.2471 66  LEU A CD2 
543  N N   . MET A 67  ? 0.6408 0.6323 0.4404 0.0584  -0.1037 -0.1801 67  MET A N   
544  C CA  . MET A 67  ? 0.6302 0.6206 0.416  0.0628  -0.0955 -0.1657 67  MET A CA  
545  C C   . MET A 67  ? 0.6447 0.6403 0.416  0.0669  -0.1062 -0.1584 67  MET A C   
546  O O   . MET A 67  ? 0.613  0.6038 0.3576 0.0714  -0.1027 -0.1515 67  MET A O   
547  C CB  . MET A 67  ? 0.5825 0.5734 0.3921 0.0604  -0.0847 -0.1552 67  MET A CB  
548  C CG  . MET A 67  ? 0.5783 0.5628 0.3964 0.059   -0.0728 -0.1604 67  MET A CG  
549  S SD  . MET A 67  ? 0.6217 0.5995 0.4096 0.0639  -0.0619 -0.1638 67  MET A SD  
550  C CE  . MET A 67  ? 0.6663 0.6475 0.4457 0.0657  -0.0534 -0.1457 67  MET A CE  
551  N N   . LYS A 68  ? 0.6807 0.6857 0.4689 0.0656  -0.1189 -0.1598 68  LYS A N   
552  C CA  . LYS A 68  ? 0.6428 0.6537 0.4179 0.0709  -0.1317 -0.1551 68  LYS A CA  
553  C C   . LYS A 68  ? 0.6753 0.6823 0.4153 0.0757  -0.1381 -0.1612 68  LYS A C   
554  O O   . LYS A 68  ? 0.6576 0.6596 0.3712 0.0817  -0.1381 -0.1519 68  LYS A O   
555  C CB  . LYS A 68  ? 0.6945 0.7191 0.4969 0.0684  -0.1445 -0.1597 68  LYS A CB  
556  C CG  . LYS A 68  ? 0.7711 0.8043 0.5616 0.0751  -0.1602 -0.158  68  LYS A CG  
557  C CD  . LYS A 68  ? 0.8177 0.8648 0.6365 0.0752  -0.1681 -0.1542 68  LYS A CD  
558  C CE  . LYS A 68  ? 0.8253 0.8799 0.6275 0.084   -0.1837 -0.1526 68  LYS A CE  
559  N NZ  . LYS A 68  ? 0.8399 0.914  0.6698 0.0828  -0.1971 -0.1593 68  LYS A NZ  
560  N N   . ASP A 69  ? 0.6706 0.6782 0.4085 0.0726  -0.1433 -0.1771 69  ASP A N   
561  C CA  . ASP A 69  ? 0.7036 0.7075 0.4074 0.0766  -0.1501 -0.1848 69  ASP A CA  
562  C C   . ASP A 69  ? 0.7263 0.7171 0.4014 0.0796  -0.1352 -0.1795 69  ASP A C   
563  O O   . ASP A 69  ? 0.7294 0.7157 0.371  0.0852  -0.138  -0.176  69  ASP A O   
564  C CB  . ASP A 69  ? 0.7479 0.754  0.4576 0.0713  -0.1575 -0.204  69  ASP A CB  
565  C CG  . ASP A 69  ? 0.8242 0.8244 0.4967 0.0747  -0.1624 -0.2141 69  ASP A CG  
566  O OD1 . ASP A 69  ? 0.8509 0.8579 0.5065 0.079   -0.1778 -0.2154 69  ASP A OD1 
567  O OD2 . ASP A 69  ? 0.8769 0.8657 0.5365 0.0737  -0.1504 -0.2201 69  ASP A OD2 
568  N N   . TYR A 70  ? 0.7095 0.6946 0.3973 0.0761  -0.1192 -0.1791 70  TYR A N   
569  C CA  . TYR A 70  ? 0.7272 0.7028 0.3919 0.0785  -0.1039 -0.175  70  TYR A CA  
570  C C   . TYR A 70  ? 0.6884 0.6619 0.3388 0.0821  -0.0995 -0.1574 70  TYR A C   
571  O O   . TYR A 70  ? 0.7061 0.673  0.3232 0.0859  -0.0964 -0.1541 70  TYR A O   
572  C CB  . TYR A 70  ? 0.7335 0.7062 0.4193 0.0749  -0.0886 -0.1773 70  TYR A CB  
573  C CG  . TYR A 70  ? 0.7523 0.7184 0.4169 0.0775  -0.0723 -0.1741 70  TYR A CG  
574  C CD1 . TYR A 70  ? 0.7624 0.7223 0.3981 0.0801  -0.0703 -0.1848 70  TYR A CD1 
575  C CD2 . TYR A 70  ? 0.7327 0.6998 0.4063 0.0769  -0.0589 -0.1611 70  TYR A CD2 
576  C CE1 . TYR A 70  ? 0.8219 0.7773 0.4378 0.0825  -0.0547 -0.1821 70  TYR A CE1 
577  C CE2 . TYR A 70  ? 0.7773 0.741  0.433  0.0786  -0.0438 -0.1585 70  TYR A CE2 
578  C CZ  . TYR A 70  ? 0.7934 0.7515 0.4208 0.0816  -0.0411 -0.1689 70  TYR A CZ  
579  O OH  . TYR A 70  ? 0.83   0.7862 0.4407 0.0831  -0.025  -0.1667 70  TYR A OH  
580  N N   . CYS A 71  ? 0.7266 0.7045 0.4016 0.0804  -0.0986 -0.1464 71  CYS A N   
581  C CA  . CYS A 71  ? 0.7561 0.73   0.4215 0.0824  -0.0924 -0.1297 71  CYS A CA  
582  C C   . CYS A 71  ? 0.7629 0.7335 0.4001 0.0887  -0.104  -0.1241 71  CYS A C   
583  O O   . CYS A 71  ? 0.8146 0.776  0.4245 0.0912  -0.097  -0.1144 71  CYS A O   
584  C CB  . CYS A 71  ? 0.7284 0.707  0.4256 0.0793  -0.0901 -0.1205 71  CYS A CB  
585  S SG  . CYS A 71  ? 0.7283 0.7096 0.4577 0.0729  -0.076  -0.1228 71  CYS A SG  
586  N N   . LEU A 72  ? 0.8256 0.8041 0.4686 0.0911  -0.1216 -0.1307 72  LEU A N   
587  C CA  . LEU A 72  ? 0.8907 0.8683 0.5094 0.0986  -0.1357 -0.1264 72  LEU A CA  
588  C C   . LEU A 72  ? 0.8963 0.866  0.4735 0.1023  -0.137  -0.1314 72  LEU A C   
589  O O   . LEU A 72  ? 0.9036 0.8682 0.4526 0.1092  -0.1451 -0.1243 72  LEU A O   
590  C CB  . LEU A 72  ? 1.0403 1.0325 0.68   0.0999  -0.1545 -0.1343 72  LEU A CB  
591  C CG  . LEU A 72  ? 1.1503 1.1496 0.814  0.1023  -0.1606 -0.1246 72  LEU A CG  
592  C CD1 . LEU A 72  ? 1.0793 1.0802 0.7769 0.0961  -0.1487 -0.1194 72  LEU A CD1 
593  C CD2 . LEU A 72  ? 1.2817 1.2975 0.9594 0.1043  -0.1804 -0.1353 72  LEU A CD2 
594  N N   . ASN A 73  ? 0.8439 0.8117 0.4163 0.0984  -0.1294 -0.1435 73  ASN A N   
595  C CA  . ASN A 73  ? 0.851  0.8102 0.383  0.1013  -0.1275 -0.1488 73  ASN A CA  
596  C C   . ASN A 73  ? 0.8547 0.8025 0.3662 0.1005  -0.1072 -0.1398 73  ASN A C   
597  O O   . ASN A 73  ? 0.8124 0.7523 0.2878 0.103   -0.1036 -0.1428 73  ASN A O   
598  C CB  . ASN A 73  ? 0.8783 0.8413 0.4129 0.0984  -0.1319 -0.1687 73  ASN A CB  
599  C CG  . ASN A 73  ? 0.9278 0.8972 0.4496 0.1021  -0.1536 -0.177  73  ASN A CG  
600  O OD1 . ASN A 73  ? 0.9097 0.8731 0.3924 0.1078  -0.1591 -0.1758 73  ASN A OD1 
601  N ND2 . ASN A 73  ? 0.9396 0.9218 0.494  0.099   -0.1662 -0.1843 73  ASN A ND2 
602  N N   . LEU A 74  ? 0.7962 0.7436 0.3286 0.097   -0.0943 -0.1286 74  LEU A N   
603  C CA  . LEU A 74  ? 0.827  0.766  0.3429 0.0951  -0.075  -0.12   74  LEU A CA  
604  C C   . LEU A 74  ? 0.8518 0.7791 0.3306 0.0996  -0.076  -0.1065 74  LEU A C   
605  O O   . LEU A 74  ? 0.8586 0.7847 0.337  0.1036  -0.0887 -0.0988 74  LEU A O   
606  C CB  . LEU A 74  ? 0.7369 0.6801 0.2863 0.0895  -0.062  -0.1128 74  LEU A CB  
607  C CG  . LEU A 74  ? 0.7362 0.6879 0.3174 0.0855  -0.0568 -0.1246 74  LEU A CG  
608  C CD1 . LEU A 74  ? 0.6815 0.6381 0.2958 0.081   -0.0489 -0.1159 74  LEU A CD1 
609  C CD2 . LEU A 74  ? 0.7753 0.725  0.3427 0.0853  -0.0439 -0.1346 74  LEU A CD2 
610  N N   . ASP A 75  ? 0.9019 0.8202 0.3489 0.0992  -0.0623 -0.104  75  ASP A N   
611  C CA  . ASP A 75  ? 0.937  0.8414 0.3505 0.101   -0.0565 -0.0886 75  ASP A CA  
612  C C   . ASP A 75  ? 0.9381 0.8414 0.3751 0.096   -0.0468 -0.0748 75  ASP A C   
613  O O   . ASP A 75  ? 0.8516 0.7605 0.309  0.0896  -0.0314 -0.0754 75  ASP A O   
614  C CB  . ASP A 75  ? 0.9865 0.8835 0.3655 0.0999  -0.0415 -0.0908 75  ASP A CB  
615  C CG  . ASP A 75  ? 1.0335 0.9144 0.3751 0.1     -0.0317 -0.0748 75  ASP A CG  
616  O OD1 . ASP A 75  ? 1.0116 0.8851 0.3554 0.1004  -0.0347 -0.0604 75  ASP A OD1 
617  O OD2 . ASP A 75  ? 1.0631 0.938  0.3737 0.0993  -0.0198 -0.0767 75  ASP A OD2 
618  N N   . VAL A 76  ? 0.9387 0.8345 0.3714 0.0995  -0.056  -0.0625 76  VAL A N   
619  C CA  . VAL A 76  ? 0.9242 0.8195 0.3832 0.0953  -0.0506 -0.0516 76  VAL A CA  
620  C C   . VAL A 76  ? 0.9326 0.8174 0.3774 0.0888  -0.0305 -0.04   76  VAL A C   
621  O O   . VAL A 76  ? 0.9749 0.8606 0.4425 0.0831  -0.0228 -0.0328 76  VAL A O   
622  C CB  . VAL A 76  ? 0.9276 0.8183 0.3887 0.1019  -0.0669 -0.0437 76  VAL A CB  
623  C CG1 . VAL A 76  ? 0.9113 0.8173 0.3954 0.1062  -0.0852 -0.0563 76  VAL A CG1 
624  C CG2 . VAL A 76  ? 0.9934 0.8658 0.4104 0.1089  -0.0717 -0.0325 76  VAL A CG2 
625  N N   . LYS A 77  ? 0.9626 0.839  0.3712 0.0886  -0.021  -0.0393 77  LYS A N   
626  C CA  . LYS A 77  ? 0.9765 0.8444 0.3706 0.0813  -0.0005 -0.0296 77  LYS A CA  
627  C C   . LYS A 77  ? 0.8846 0.7681 0.3042 0.074   0.0155  -0.038  77  LYS A C   
628  O O   . LYS A 77  ? 0.9309 0.8119 0.346  0.0667  0.0331  -0.0309 77  LYS A O   
629  C CB  . LYS A 77  ? 1.0924 0.9445 0.4347 0.0847  0.0028  -0.0252 77  LYS A CB  
630  C CG  . LYS A 77  ? 1.1614 0.9961 0.4742 0.0933  -0.0127 -0.0149 77  LYS A CG  
631  C CD  . LYS A 77  ? 1.2422 1.0583 0.5005 0.0967  -0.009  -0.0082 77  LYS A CD  
632  C CE  . LYS A 77  ? 1.2657 1.0886 0.5053 0.102   -0.0161 -0.0224 77  LYS A CE  
633  N NZ  . LYS A 77  ? 1.3925 1.1956 0.577  0.1065  -0.0151 -0.0141 77  LYS A NZ  
634  N N   . THR A 78  ? 0.8408 0.7398 0.2879 0.0756  0.0098  -0.0525 78  THR A N   
635  C CA  . THR A 78  ? 0.8048 0.7177 0.2728 0.0711  0.0239  -0.0616 78  THR A CA  
636  C C   . THR A 78  ? 0.7571 0.6818 0.2694 0.0656  0.0278  -0.0595 78  THR A C   
637  O O   . THR A 78  ? 0.7379 0.6628 0.2703 0.0661  0.0166  -0.0558 78  THR A O   
638  C CB  . THR A 78  ? 0.7994 0.7197 0.2696 0.0763  0.0167  -0.0789 78  THR A CB  
639  O OG1 . THR A 78  ? 0.7432 0.6694 0.2418 0.0786  0.0001  -0.0839 78  THR A OG1 
640  C CG2 . THR A 78  ? 0.8537 0.7637 0.2796 0.0816  0.013   -0.0831 78  THR A CG2 
641  N N   . LYS A 79  ? 0.7271 0.663  0.2547 0.061   0.0437  -0.0631 79  LYS A N   
642  C CA  . LYS A 79  ? 0.7258 0.6759 0.2952 0.057   0.0475  -0.0648 79  LYS A CA  
643  C C   . LYS A 79  ? 0.7101 0.666  0.305  0.0615  0.0325  -0.0745 79  LYS A C   
644  O O   . LYS A 79  ? 0.6588 0.6202 0.284  0.0592  0.028   -0.0716 79  LYS A O   
645  C CB  . LYS A 79  ? 0.7596 0.7222 0.3365 0.0546  0.0652  -0.0708 79  LYS A CB  
646  C CG  . LYS A 79  ? 0.7259 0.7043 0.3445 0.0507  0.0706  -0.0711 79  LYS A CG  
647  C CD  . LYS A 79  ? 0.7696 0.7626 0.3981 0.0504  0.0868  -0.078  79  LYS A CD  
648  C CE  . LYS A 79  ? 0.7472 0.7556 0.4165 0.0488  0.0883  -0.0792 79  LYS A CE  
649  N NZ  . LYS A 79  ? 0.7955 0.8196 0.4764 0.0495  0.1038  -0.0852 79  LYS A NZ  
650  N N   . ALA A 80  ? 0.6748 0.629  0.2569 0.0673  0.0251  -0.0865 80  ALA A N   
651  C CA  . ALA A 80  ? 0.6613 0.6196 0.2654 0.0704  0.0111  -0.0964 80  ALA A CA  
652  C C   . ALA A 80  ? 0.6599 0.6148 0.2729 0.0707  -0.0037 -0.0892 80  ALA A C   
653  O O   . ALA A 80  ? 0.6206 0.5822 0.2651 0.0694  -0.0092 -0.0912 80  ALA A O   
654  C CB  . ALA A 80  ? 0.7115 0.6668 0.2961 0.0755  0.0054  -0.1102 80  ALA A CB  
655  N N   . ALA A 81  ? 0.7095 0.6538 0.2945 0.0729  -0.0097 -0.0809 81  ALA A N   
656  C CA  . ALA A 81  ? 0.6822 0.6229 0.2729 0.075   -0.0239 -0.0742 81  ALA A CA  
657  C C   . ALA A 81  ? 0.6518 0.5938 0.2658 0.0698  -0.0183 -0.0633 81  ALA A C   
658  O O   . ALA A 81  ? 0.6221 0.5678 0.2595 0.0702  -0.0278 -0.0626 81  ALA A O   
659  C CB  . ALA A 81  ? 0.7075 0.6351 0.2602 0.0799  -0.0306 -0.0672 81  ALA A CB  
660  N N   . ARG A 82  ? 0.6715 0.6107 0.2786 0.0645  -0.0027 -0.0553 82  ARG A N   
661  C CA  . ARG A 82  ? 0.6382 0.5798 0.2681 0.0583  0.0038  -0.0464 82  ARG A CA  
662  C C   . ARG A 82  ? 0.5886 0.5446 0.2573 0.0561  0.0037  -0.0533 82  ARG A C   
663  O O   . ARG A 82  ? 0.5649 0.5225 0.2552 0.0542  -0.0011 -0.049  82  ARG A O   
664  C CB  . ARG A 82  ? 0.6669 0.6045 0.2818 0.0519  0.021   -0.0383 82  ARG A CB  
665  C CG  . ARG A 82  ? 0.6973 0.6164 0.2749 0.0536  0.0199  -0.0281 82  ARG A CG  
666  C CD  . ARG A 82  ? 0.7534 0.6671 0.3184 0.0452  0.0374  -0.0186 82  ARG A CD  
667  N NE  . ARG A 82  ? 0.7748 0.6971 0.3325 0.0424  0.0518  -0.0244 82  ARG A NE  
668  C CZ  . ARG A 82  ? 0.8337 0.7485 0.3572 0.0453  0.0558  -0.0258 82  ARG A CZ  
669  N NH1 . ARG A 82  ? 0.8568 0.7807 0.3769 0.0422  0.0708  -0.0307 82  ARG A NH1 
670  N NH2 . ARG A 82  ? 0.864  0.7627 0.3561 0.0517  0.0452  -0.0221 82  ARG A NH2 
671  N N   . SER A 83  ? 0.5925 0.5573 0.2684 0.057   0.0086  -0.0639 83  SER A N   
672  C CA  . SER A 83  ? 0.5882 0.5644 0.298  0.0563  0.0079  -0.0709 83  SER A CA  
673  C C   . SER A 83  ? 0.5457 0.5216 0.2694 0.0594  -0.0079 -0.0759 83  SER A C   
674  O O   . SER A 83  ? 0.5169 0.4983 0.2681 0.0572  -0.0103 -0.0752 83  SER A O   
675  C CB  . SER A 83  ? 0.6119 0.5948 0.3232 0.058   0.0164  -0.0813 83  SER A CB  
676  O OG  . SER A 83  ? 0.6335 0.619  0.3328 0.0551  0.0318  -0.0772 83  SER A OG  
677  N N   . ALA A 84  ? 0.5588 0.5293 0.2631 0.0641  -0.0185 -0.0811 84  ALA A N   
678  C CA  . ALA A 84  ? 0.5464 0.5182 0.2619 0.0667  -0.0341 -0.0865 84  ALA A CA  
679  C C   . ALA A 84  ? 0.5344 0.5052 0.2615 0.0659  -0.0403 -0.0766 84  ALA A C   
680  O O   . ALA A 84  ? 0.5074 0.4839 0.2591 0.0653  -0.0476 -0.0795 84  ALA A O   
681  C CB  . ALA A 84  ? 0.5951 0.5622 0.2831 0.0719  -0.0437 -0.0933 84  ALA A CB  
682  N N   . LEU A 85  ? 0.5295 0.4922 0.2395 0.0655  -0.0361 -0.0649 85  LEU A N   
683  C CA  . LEU A 85  ? 0.5372 0.4967 0.2563 0.0652  -0.0405 -0.0554 85  LEU A CA  
684  C C   . LEU A 85  ? 0.5049 0.4712 0.2547 0.0593  -0.034  -0.0534 85  LEU A C   
685  O O   . LEU A 85  ? 0.4837 0.4534 0.2536 0.0595  -0.041  -0.053  85  LEU A O   
686  C CB  . LEU A 85  ? 0.5716 0.5176 0.2625 0.0657  -0.0362 -0.0436 85  LEU A CB  
687  C CG  . LEU A 85  ? 0.5995 0.5382 0.2957 0.0655  -0.0386 -0.033  85  LEU A CG  
688  C CD1 . LEU A 85  ? 0.6141 0.557  0.3229 0.0715  -0.0539 -0.0363 85  LEU A CD1 
689  C CD2 . LEU A 85  ? 0.6455 0.5671 0.3086 0.0668  -0.0347 -0.022  85  LEU A CD2 
690  N N   . GLU A 86  ? 0.5054 0.4753 0.2593 0.0545  -0.0209 -0.0528 86  GLU A N   
691  C CA  . GLU A 86  ? 0.4722 0.4501 0.2545 0.0496  -0.0156 -0.0518 86  GLU A CA  
692  C C   . GLU A 86  ? 0.4741 0.4596 0.28   0.0511  -0.0226 -0.0611 86  GLU A C   
693  O O   . GLU A 86  ? 0.4795 0.4683 0.307  0.049   -0.0251 -0.0592 86  GLU A O   
694  C CB  . GLU A 86  ? 0.4761 0.4588 0.2585 0.0451  -0.0012 -0.05   86  GLU A CB  
695  C CG  . GLU A 86  ? 0.4304 0.4235 0.2422 0.0413  0.0033  -0.0504 86  GLU A CG  
696  C CD  . GLU A 86  ? 0.4195 0.4114 0.2455 0.0375  0.0007  -0.0429 86  GLU A CD  
697  O OE1 . GLU A 86  ? 0.4196 0.4018 0.2328 0.0374  -0.0029 -0.0365 86  GLU A OE1 
698  O OE2 . GLU A 86  ? 0.4313 0.4313 0.2801 0.035   0.0026  -0.0436 86  GLU A OE2 
699  N N   . TYR A 87  ? 0.488  0.4753 0.2891 0.0543  -0.0248 -0.0714 87  TYR A N   
700  C CA  . TYR A 87  ? 0.472  0.4638 0.2928 0.055   -0.0313 -0.081  87  TYR A CA  
701  C C   . TYR A 87  ? 0.4523 0.4443 0.283  0.0556  -0.0432 -0.0799 87  TYR A C   
702  O O   . TYR A 87  ? 0.4323 0.4284 0.2871 0.053   -0.0448 -0.0805 87  TYR A O   
703  C CB  . TYR A 87  ? 0.4847 0.475  0.292  0.0583  -0.0326 -0.0926 87  TYR A CB  
704  C CG  . TYR A 87  ? 0.4966 0.4886 0.3194 0.0586  -0.0414 -0.1034 87  TYR A CG  
705  C CD1 . TYR A 87  ? 0.5068 0.5009 0.3514 0.0569  -0.037  -0.1082 87  TYR A CD1 
706  C CD2 . TYR A 87  ? 0.5132 0.5047 0.329  0.0605  -0.0543 -0.1088 87  TYR A CD2 
707  C CE1 . TYR A 87  ? 0.5223 0.5157 0.3808 0.0559  -0.0442 -0.1176 87  TYR A CE1 
708  C CE2 . TYR A 87  ? 0.5027 0.4964 0.3342 0.059   -0.0621 -0.1191 87  TYR A CE2 
709  C CZ  . TYR A 87  ? 0.5368 0.5303 0.389  0.0563  -0.0565 -0.1235 87  TYR A CZ  
710  O OH  . TYR A 87  ? 0.5461 0.5395 0.4126 0.0538  -0.0631 -0.1335 87  TYR A OH  
711  N N   . ALA A 88  ? 0.4934 0.4815 0.3052 0.0593  -0.0514 -0.0785 88  ALA A N   
712  C CA  . ALA A 88  ? 0.4848 0.4754 0.3054 0.0613  -0.0635 -0.0787 88  ALA A CA  
713  C C   . ALA A 88  ? 0.4588 0.4494 0.2949 0.0589  -0.0607 -0.0691 88  ALA A C   
714  O O   . ALA A 88  ? 0.4649 0.4612 0.323  0.0575  -0.0652 -0.071  88  ALA A O   
715  C CB  . ALA A 88  ? 0.5007 0.4871 0.2956 0.0672  -0.0725 -0.0781 88  ALA A CB  
716  N N   . ASP A 89  ? 0.456  0.4401 0.2809 0.0574  -0.0523 -0.0591 89  ASP A N   
717  C CA  . ASP A 89  ? 0.4478 0.4305 0.2856 0.0547  -0.0497 -0.0509 89  ASP A CA  
718  C C   . ASP A 89  ? 0.4287 0.4184 0.2924 0.0495  -0.0444 -0.0525 89  ASP A C   
719  O O   . ASP A 89  ? 0.4325 0.4245 0.3132 0.0482  -0.047  -0.0508 89  ASP A O   
720  C CB  . ASP A 89  ? 0.4858 0.4586 0.3047 0.0533  -0.0422 -0.0406 89  ASP A CB  
721  C CG  . ASP A 89  ? 0.5007 0.4695 0.3291 0.0509  -0.0406 -0.0327 89  ASP A CG  
722  O OD1 . ASP A 89  ? 0.4405 0.4134 0.2844 0.045   -0.0334 -0.0314 89  ASP A OD1 
723  O OD2 . ASP A 89  ? 0.5273 0.4891 0.3472 0.0558  -0.0472 -0.0286 89  ASP A OD2 
724  N N   . ALA A 90  ? 0.4158 0.4086 0.2819 0.047   -0.0367 -0.0558 90  ALA A N   
725  C CA  . ALA A 90  ? 0.3856 0.3842 0.2741 0.0432  -0.0318 -0.057  90  ALA A CA  
726  C C   . ALA A 90  ? 0.3997 0.402  0.3067 0.0436  -0.0393 -0.0637 90  ALA A C   
727  O O   . ALA A 90  ? 0.3838 0.3885 0.3091 0.0407  -0.0383 -0.0616 90  ALA A O   
728  C CB  . ALA A 90  ? 0.4214 0.423  0.3075 0.0429  -0.0236 -0.0605 90  ALA A CB  
729  N N   . ASN A 91  ? 0.395  0.3974 0.2961 0.0467  -0.0465 -0.072  91  ASN A N   
730  C CA  . ASN A 91  ? 0.442  0.448  0.3605 0.0458  -0.0534 -0.0796 91  ASN A CA  
731  C C   . ASN A 91  ? 0.4552 0.4644 0.3804 0.0466  -0.0619 -0.0776 91  ASN A C   
732  O O   . ASN A 91  ? 0.5047 0.5188 0.4463 0.0449  -0.0672 -0.0835 91  ASN A O   
733  C CB  . ASN A 91  ? 0.4247 0.4303 0.3359 0.0476  -0.0578 -0.0909 91  ASN A CB  
734  C CG  . ASN A 91  ? 0.4308 0.4339 0.3447 0.0468  -0.0494 -0.095  91  ASN A CG  
735  O OD1 . ASN A 91  ? 0.4269 0.4297 0.3584 0.0443  -0.0484 -0.0988 91  ASN A OD1 
736  N ND2 . ASN A 91  ? 0.4359 0.4368 0.3323 0.0492  -0.0434 -0.0949 91  ASN A ND2 
737  N N   . MET A 92  ? 0.4543 0.4607 0.3667 0.0495  -0.063  -0.0699 92  MET A N   
738  C CA  . MET A 92  ? 0.4607 0.4697 0.3765 0.0526  -0.0713 -0.0679 92  MET A CA  
739  C C   . MET A 92  ? 0.5042 0.5195 0.4191 0.0559  -0.0827 -0.0771 92  MET A C   
740  O O   . MET A 92  ? 0.5205 0.5439 0.4513 0.0564  -0.0897 -0.0801 92  MET A O   
741  C CB  . MET A 92  ? 0.453  0.4657 0.3916 0.0491  -0.0689 -0.065  92  MET A CB  
742  C CG  . MET A 92  ? 0.4551 0.4618 0.3922 0.046   -0.0591 -0.0559 92  MET A CG  
743  S SD  . MET A 92  ? 0.4851 0.4952 0.4453 0.0423  -0.0566 -0.0527 92  MET A SD  
744  C CE  . MET A 92  ? 0.5563 0.5582 0.5069 0.0391  -0.0468 -0.0428 92  MET A CE  
745  N N   . PHE A 93  ? 0.4801 0.4925 0.3757 0.0581  -0.0845 -0.0818 93  PHE A N   
746  C CA  . PHE A 93  ? 0.5198 0.5372 0.4083 0.0619  -0.0964 -0.0901 93  PHE A CA  
747  C C   . PHE A 93  ? 0.5018 0.5158 0.3698 0.0692  -0.1024 -0.0831 93  PHE A C   
748  O O   . PHE A 93  ? 0.5691 0.5761 0.4105 0.0727  -0.1027 -0.082  93  PHE A O   
749  C CB  . PHE A 93  ? 0.5442 0.5584 0.4202 0.0606  -0.0945 -0.0989 93  PHE A CB  
750  C CG  . PHE A 93  ? 0.4895 0.5047 0.3843 0.0546  -0.0893 -0.1065 93  PHE A CG  
751  C CD1 . PHE A 93  ? 0.4979 0.5185 0.4201 0.0499  -0.0898 -0.108  93  PHE A CD1 
752  C CD2 . PHE A 93  ? 0.5366 0.5463 0.4204 0.0541  -0.0839 -0.1128 93  PHE A CD2 
753  C CE1 . PHE A 93  ? 0.498  0.5165 0.4348 0.0448  -0.085  -0.1143 93  PHE A CE1 
754  C CE2 . PHE A 93  ? 0.5025 0.5107 0.4021 0.0498  -0.0794 -0.1196 93  PHE A CE2 
755  C CZ  . PHE A 93  ? 0.5503 0.562  0.4757 0.0452  -0.0802 -0.1201 93  PHE A CZ  
756  N N   . PHE A 94  ? 0.528  0.5461 0.4077 0.072   -0.1068 -0.0782 94  PHE A N   
757  C CA  . PHE A 94  ? 0.5429 0.555  0.4052 0.0798  -0.1112 -0.0695 94  PHE A CA  
758  C C   . PHE A 94  ? 0.5795 0.5934 0.4214 0.0872  -0.1236 -0.0734 94  PHE A C   
759  O O   . PHE A 94  ? 0.6021 0.6045 0.4169 0.0929  -0.1239 -0.0657 94  PHE A O   
760  C CB  . PHE A 94  ? 0.5752 0.5932 0.4583 0.0819  -0.1139 -0.0658 94  PHE A CB  
761  C CG  . PHE A 94  ? 0.5779 0.593  0.4778 0.0754  -0.1024 -0.061  94  PHE A CG  
762  C CD1 . PHE A 94  ? 0.6077 0.6107 0.4961 0.0711  -0.0905 -0.0541 94  PHE A CD1 
763  C CD2 . PHE A 94  ? 0.6435 0.6693 0.5714 0.0729  -0.1033 -0.0639 94  PHE A CD2 
764  C CE1 . PHE A 94  ? 0.5502 0.5518 0.4535 0.0654  -0.0815 -0.0502 94  PHE A CE1 
765  C CE2 . PHE A 94  ? 0.6458 0.6686 0.5869 0.0671  -0.0931 -0.0595 94  PHE A CE2 
766  C CZ  . PHE A 94  ? 0.5829 0.5935 0.5111 0.0637  -0.083  -0.0527 94  PHE A CZ  
767  N N   . GLU A 95  ? 0.6167 0.6436 0.4691 0.0867  -0.1337 -0.0852 95  GLU A N   
768  C CA  . GLU A 95  ? 0.6778 0.7075 0.5097 0.0934  -0.1466 -0.0898 95  GLU A CA  
769  C C   . GLU A 95  ? 0.6562 0.6731 0.4562 0.0933  -0.1412 -0.0896 95  GLU A C   
770  O O   . GLU A 95  ? 0.6338 0.6443 0.4058 0.1005  -0.147  -0.0857 95  GLU A O   
771  C CB  . GLU A 95  ? 0.7702 0.8168 0.6195 0.091   -0.1582 -0.1042 95  GLU A CB  
772  C CG  . GLU A 95  ? 0.8163 0.8792 0.701  0.0891  -0.163  -0.1073 95  GLU A CG  
773  C CD  . GLU A 95  ? 0.8556 0.9373 0.7532 0.0891  -0.1783 -0.1203 95  GLU A CD  
774  O OE1 . GLU A 95  ? 0.9395 1.0219 0.818  0.091   -0.187  -0.1276 95  GLU A OE1 
775  O OE2 . GLU A 95  ? 0.8534 0.9499 0.7814 0.0867  -0.1812 -0.1233 95  GLU A OE2 
776  N N   . ILE A 96  ? 0.622  0.6352 0.4257 0.0856  -0.1299 -0.0936 96  ILE A N   
777  C CA  . ILE A 96  ? 0.6071 0.6094 0.3825 0.0854  -0.1228 -0.0937 96  ILE A CA  
778  C C   . ILE A 96  ? 0.5906 0.5792 0.3457 0.0878  -0.1137 -0.0793 96  ILE A C   
779  O O   . ILE A 96  ? 0.6352 0.6144 0.3583 0.0922  -0.1141 -0.0755 96  ILE A O   
780  C CB  . ILE A 96  ? 0.6133 0.6154 0.3989 0.078   -0.1125 -0.1016 96  ILE A CB  
781  C CG1 . ILE A 96  ? 0.579  0.5914 0.384  0.0744  -0.1206 -0.1162 96  ILE A CG1 
782  C CG2 . ILE A 96  ? 0.626  0.6182 0.381  0.079   -0.1048 -0.1021 96  ILE A CG2 
783  C CD1 . ILE A 96  ? 0.5897 0.5999 0.409  0.0678  -0.1101 -0.1226 96  ILE A CD1 
784  N N   . GLU A 97  ? 0.5589 0.5457 0.3315 0.084   -0.1049 -0.0717 97  GLU A N   
785  C CA  . GLU A 97  ? 0.5635 0.537  0.3204 0.084   -0.0949 -0.0589 97  GLU A CA  
786  C C   . GLU A 97  ? 0.5612 0.5254 0.2948 0.0925  -0.1025 -0.0504 97  GLU A C   
787  O O   . GLU A 97  ? 0.6057 0.5564 0.31   0.094   -0.0973 -0.0432 97  GLU A O   
788  C CB  . GLU A 97  ? 0.5453 0.5212 0.3292 0.0787  -0.0879 -0.0545 97  GLU A CB  
789  C CG  . GLU A 97  ? 0.5714 0.534  0.343  0.0779  -0.0791 -0.0418 97  GLU A CG  
790  C CD  . GLU A 97  ? 0.5494 0.5141 0.3448 0.0713  -0.0707 -0.0386 97  GLU A CD  
791  O OE1 . GLU A 97  ? 0.5281 0.5035 0.3501 0.069   -0.0731 -0.0441 97  GLU A OE1 
792  O OE2 . GLU A 97  ? 0.5701 0.5238 0.3535 0.0684  -0.0616 -0.0297 97  GLU A OE2 
793  N N   . ASP A 98  ? 0.604  0.5751 0.3506 0.0982  -0.1144 -0.0507 98  ASP A N   
794  C CA  . ASP A 98  ? 0.6379 0.6004 0.3651 0.1081  -0.1226 -0.0423 98  ASP A CA  
795  C C   . ASP A 98  ? 0.6807 0.639  0.3754 0.1147  -0.1311 -0.044  98  ASP A C   
796  O O   . ASP A 98  ? 0.6977 0.6403 0.3634 0.1209  -0.1314 -0.0338 98  ASP A O   
797  C CB  . ASP A 98  ? 0.7129 0.6872 0.4651 0.1135  -0.1333 -0.0437 98  ASP A CB  
798  C CG  . ASP A 98  ? 0.6578 0.6327 0.4363 0.1087  -0.1249 -0.0398 98  ASP A CG  
799  O OD1 . ASP A 98  ? 0.6453 0.6082 0.419  0.1023  -0.1113 -0.0332 98  ASP A OD1 
800  O OD2 . ASP A 98  ? 0.7125 0.7011 0.5168 0.1107  -0.1317 -0.0441 98  ASP A OD2 
801  N N   . ALA A 99  ? 0.7204 0.6906 0.4174 0.1129  -0.1372 -0.0567 99  ALA A N   
802  C CA  . ALA A 99  ? 0.7479 0.7144 0.4123 0.1183  -0.145  -0.0598 99  ALA A CA  
803  C C   . ALA A 99  ? 0.7505 0.7002 0.3842 0.1148  -0.1307 -0.0538 99  ALA A C   
804  O O   . ALA A 99  ? 0.7422 0.6791 0.3407 0.1208  -0.1327 -0.0473 99  ALA A O   
805  C CB  . ALA A 99  ? 0.7732 0.7558 0.4493 0.1157  -0.1539 -0.0761 99  ALA A CB  
806  N N   . LEU A 100 ? 0.7255 0.6754 0.3725 0.1053  -0.1158 -0.0559 100 LEU A N   
807  C CA  . LEU A 100 ? 0.714  0.6514 0.3378 0.1009  -0.1003 -0.0506 100 LEU A CA  
808  C C   . LEU A 100 ? 0.7025 0.6229 0.3099 0.1023  -0.0937 -0.0347 100 LEU A C   
809  O O   . LEU A 100 ? 0.7763 0.6825 0.3495 0.1039  -0.0889 -0.0279 100 LEU A O   
810  C CB  . LEU A 100 ? 0.684  0.6282 0.3309 0.0914  -0.0867 -0.056  100 LEU A CB  
811  C CG  . LEU A 100 ? 0.7188 0.6733 0.3733 0.0891  -0.0882 -0.0711 100 LEU A CG  
812  C CD1 . LEU A 100 ? 0.7124 0.6727 0.3948 0.0813  -0.0757 -0.0736 100 LEU A CD1 
813  C CD2 . LEU A 100 ? 0.7544 0.7023 0.3736 0.0914  -0.086  -0.0749 100 LEU A CD2 
814  N N   . ILE A 101 ? 0.7007 0.6215 0.3313 0.1012  -0.0929 -0.0289 101 ILE A N   
815  C CA  . ILE A 101 ? 0.6914 0.5942 0.3073 0.1024  -0.0873 -0.0145 101 ILE A CA  
816  C C   . ILE A 101 ? 0.7431 0.6321 0.3243 0.1132  -0.0972 -0.0074 101 ILE A C   
817  O O   . ILE A 101 ? 0.7851 0.655  0.3349 0.113   -0.0894 0.0027  101 ILE A O   
818  C CB  . ILE A 101 ? 0.6572 0.5634 0.3035 0.1014  -0.0881 -0.0115 101 ILE A CB  
819  C CG1 . ILE A 101 ? 0.6192 0.5329 0.2915 0.09    -0.075  -0.0143 101 ILE A CG1 
820  C CG2 . ILE A 101 ? 0.6886 0.5744 0.3169 0.1062  -0.0871 0.0023  101 ILE A CG2 
821  C CD1 . ILE A 101 ? 0.616  0.5365 0.3203 0.0885  -0.0764 -0.0143 101 ILE A CD1 
822  N N   . ASP A 102 ? 0.8098 0.7089 0.397  0.1225  -0.1146 -0.0126 102 ASP A N   
823  C CA  . ASP A 102 ? 0.8665 0.7548 0.4242 0.1349  -0.1269 -0.0058 102 ASP A CA  
824  C C   . ASP A 102 ? 0.8667 0.7448 0.3836 0.1359  -0.125  -0.0051 102 ASP A C   
825  O O   . ASP A 102 ? 0.9087 0.7661 0.3907 0.1414  -0.1241 0.0067  102 ASP A O   
826  C CB  . ASP A 102 ? 0.8982 0.8049 0.4783 0.1436  -0.1456 -0.0131 102 ASP A CB  
827  C CG  . ASP A 102 ? 1.0748 0.9733 0.6348 0.1584  -0.16   -0.0051 102 ASP A CG  
828  O OD1 . ASP A 102 ? 1.1512 1.0332 0.7063 0.1623  -0.1559 0.007   102 ASP A OD1 
829  O OD2 . ASP A 102 ? 1.1091 1.0177 0.6585 0.1661  -0.1755 -0.0114 102 ASP A OD2 
830  N N   . SER A 103 ? 0.8819 0.7717 0.4005 0.1302  -0.1226 -0.017  103 SER A N   
831  C CA  . SER A 103 ? 0.9289 0.8086 0.4074 0.131   -0.1193 -0.0168 103 SER A CA  
832  C C   . SER A 103 ? 0.9201 0.7847 0.3825 0.1218  -0.0977 -0.0087 103 SER A C   
833  O O   . SER A 103 ? 0.8655 0.7151 0.2889 0.1232  -0.0926 -0.003  103 SER A O   
834  C CB  . SER A 103 ? 0.9459 0.8419 0.4268 0.1306  -0.1271 -0.0331 103 SER A CB  
835  O OG  . SER A 103 ? 0.9919 0.9032 0.5087 0.1215  -0.1204 -0.0439 103 SER A OG  
836  N N   . MET A 104 ? 0.8542 0.7229 0.3458 0.1123  -0.0848 -0.0079 104 MET A N   
837  C CA  . MET A 104 ? 0.8912 0.7488 0.3717 0.1028  -0.0646 -0.0008 104 MET A CA  
838  C C   . MET A 104 ? 0.8983 0.7319 0.3557 0.1042  -0.06   0.0159  104 MET A C   
839  O O   . MET A 104 ? 0.9144 0.7324 0.342  0.1001  -0.0475 0.0237  104 MET A O   
840  C CB  . MET A 104 ? 0.8293 0.7014 0.3484 0.0925  -0.0538 -0.0066 104 MET A CB  
841  C CG  . MET A 104 ? 0.8793 0.7684 0.4099 0.0902  -0.0531 -0.0215 104 MET A CG  
842  S SD  . MET A 104 ? 0.8253 0.7331 0.4037 0.0814  -0.0454 -0.03   104 MET A SD  
843  C CE  . MET A 104 ? 0.7875 0.6867 0.3536 0.072   -0.0232 -0.0207 104 MET A CE  
844  N N   . ILE A 105 ? 0.9274 0.757  0.3977 0.1101  -0.0696 0.0213  105 ILE A N   
845  C CA  . ILE A 105 ? 0.9681 0.7724 0.4163 0.1131  -0.0668 0.0367  105 ILE A CA  
846  C C   . ILE A 105 ? 1.0913 0.8766 0.4912 0.1213  -0.0709 0.0444  105 ILE A C   
847  O O   . ILE A 105 ? 1.1961 0.9573 0.5682 0.1183  -0.06   0.0571  105 ILE A O   
848  C CB  . ILE A 105 ? 0.9863 0.7924 0.4591 0.1199  -0.0778 0.0387  105 ILE A CB  
849  C CG1 . ILE A 105 ? 0.9888 0.8048 0.4997 0.109   -0.0677 0.0356  105 ILE A CG1 
850  C CG2 . ILE A 105 ? 1.0591 0.8377 0.5039 0.1284  -0.0807 0.0536  105 ILE A CG2 
851  C CD1 . ILE A 105 ? 0.9877 0.8122 0.5293 0.1146  -0.078  0.0335  105 ILE A CD1 
852  N N   . SER A 106 ? 1.115  0.9106 0.5042 0.1306  -0.0861 0.0367  106 SER A N   
853  C CA  . SER A 106 ? 1.1883 0.9676 0.5307 0.14    -0.0929 0.0432  106 SER A CA  
854  C C   . SER A 106 ? 1.196  0.9702 0.5077 0.1331  -0.0799 0.0418  106 SER A C   
855  O O   . SER A 106 ? 1.2066 0.9636 0.4753 0.1395  -0.0826 0.0491  106 SER A O   
856  C CB  . SER A 106 ? 1.1917 0.9858 0.5359 0.1529  -0.116  0.0349  106 SER A CB  
857  O OG  . SER A 106 ? 1.1694 0.9659 0.5359 0.1614  -0.128  0.0383  106 SER A OG  
858  N N   . CYS A 107 ? 1.1485 0.9379 0.4804 0.1215  -0.0668 0.032   107 CYS A N   
859  C CA  . CYS A 107 ? 1.1562 0.9436 0.4603 0.1165  -0.0551 0.0287  107 CYS A CA  
860  C C   . CYS A 107 ? 1.2144 0.9798 0.4939 0.1079  -0.0346 0.0426  107 CYS A C   
861  O O   . CYS A 107 ? 1.1407 0.8953 0.4316 0.1036  -0.0284 0.0525  107 CYS A O   
862  C CB  . CYS A 107 ? 1.1269 0.9389 0.4609 0.1093  -0.0499 0.0122  107 CYS A CB  
863  S SG  . CYS A 107 ? 1.067  0.887  0.4387 0.0944  -0.029  0.0128  107 CYS A SG  
864  N N   . SER A 108 ? 1.1954 0.9552 0.4423 0.1045  -0.0234 0.0422  108 SER A N   
865  C CA  . SER A 108 ? 1.253  0.9922 0.4711 0.0959  -0.0032 0.0549  108 SER A CA  
866  C C   . SER A 108 ? 1.238  0.9915 0.4817 0.081   0.018   0.0496  108 SER A C   
867  O O   . SER A 108 ? 1.2953 1.0362 0.5186 0.0719  0.0367  0.0581  108 SER A O   
868  C CB  . SER A 108 ? 1.3418 1.0658 0.5066 0.1015  -0.0032 0.0585  108 SER A CB  
869  O OG  . SER A 108 ? 1.381  1.1247 0.5471 0.1023  -0.0048 0.0425  108 SER A OG  
870  N N   . ASN A 109 ? 1.1344 0.9141 0.4225 0.0783  0.0158  0.0361  109 ASN A N   
871  C CA  . ASN A 109 ? 1.0493 0.8439 0.3649 0.0657  0.0343  0.0316  109 ASN A CA  
872  C C   . ASN A 109 ? 1.033  0.8253 0.3777 0.0589  0.0376  0.0392  109 ASN A C   
873  O O   . ASN A 109 ? 0.9716 0.7704 0.343  0.0639  0.0235  0.0363  109 ASN A O   
874  C CB  . ASN A 109 ? 1.0021 0.8235 0.3481 0.0669  0.0305  0.0139  109 ASN A CB  
875  C CG  . ASN A 109 ? 0.971  0.8088 0.345  0.0557  0.0488  0.0093  109 ASN A CG  
876  O OD1 . ASN A 109 ? 0.92   0.7658 0.3284 0.0496  0.0517  0.0108  109 ASN A OD1 
877  N ND2 . ASN A 109 ? 0.9575 0.8015 0.3171 0.0534  0.0611  0.003   109 ASN A ND2 
878  N N   . MET A 110 ? 1.0479 0.8319 0.3881 0.0469  0.0564  0.0479  110 MET A N   
879  C CA  . MET A 110 ? 1.0703 0.8466 0.43   0.0398  0.0599  0.0565  110 MET A CA  
880  C C   . MET A 110 ? 0.9593 0.7609 0.3699 0.0357  0.0581  0.0467  110 MET A C   
881  O O   . MET A 110 ? 0.9179 0.7154 0.3471 0.0363  0.0507  0.0502  110 MET A O   
882  C CB  . MET A 110 ? 1.1601 0.9224 0.5036 0.0261  0.081   0.0673  110 MET A CB  
883  C CG  . MET A 110 ? 1.3179 1.0472 0.6103 0.0287  0.0835  0.0815  110 MET A CG  
884  S SD  . MET A 110 ? 1.4604 1.1615 0.7382 0.0408  0.0649  0.0929  110 MET A SD  
885  C CE  . MET A 110 ? 1.3479 1.0499 0.6002 0.0599  0.0439  0.0877  110 MET A CE  
886  N N   . LYS A 111 ? 0.9289 0.7545 0.3596 0.0326  0.0644  0.0349  111 LYS A N   
887  C CA  . LYS A 111 ? 0.9086 0.7575 0.3854 0.0301  0.062   0.0257  111 LYS A CA  
888  C C   . LYS A 111 ? 0.8626 0.717  0.3557 0.0409  0.0417  0.019   111 LYS A C   
889  O O   . LYS A 111 ? 0.803  0.6625 0.3251 0.0398  0.036   0.019   111 LYS A O   
890  C CB  . LYS A 111 ? 0.9193 0.7914 0.4131 0.0258  0.0734  0.0149  111 LYS A CB  
891  C CG  . LYS A 111 ? 0.9878 0.8591 0.4714 0.0139  0.0946  0.0208  111 LYS A CG  
892  C CD  . LYS A 111 ? 1.0432 0.9389 0.5636 0.0048  0.1067  0.0153  111 LYS A CD  
893  C CE  . LYS A 111 ? 1.0314 0.9504 0.5723 0.0099  0.1065  0.0011  111 LYS A CE  
894  N NZ  . LYS A 111 ? 1.0847 1.007  0.6036 0.0087  0.1209  -0.0018 111 LYS A NZ  
895  N N   . SER A 112 ? 0.8371 0.6914 0.312  0.0506  0.0312  0.0128  112 SER A N   
896  C CA  . SER A 112 ? 0.8143 0.6745 0.3033 0.0603  0.0118  0.0062  112 SER A CA  
897  C C   . SER A 112 ? 0.7953 0.6401 0.2811 0.0647  0.0015  0.0164  112 SER A C   
898  O O   . SER A 112 ? 0.7684 0.6214 0.2821 0.0677  -0.009  0.0131  112 SER A O   
899  C CB  . SER A 112 ? 0.8528 0.7146 0.3194 0.0689  0.0025  -0.0021 112 SER A CB  
900  O OG  . SER A 112 ? 0.8868 0.7651 0.3649 0.066   0.01    -0.0145 112 SER A OG  
901  N N   . LYS A 113 ? 0.8324 0.6541 0.2839 0.0653  0.0053  0.029   113 LYS A N   
902  C CA  . LYS A 113 ? 0.9048 0.7092 0.3516 0.0702  -0.0031 0.0393  113 LYS A CA  
903  C C   . LYS A 113 ? 0.8437 0.6515 0.3233 0.0619  0.0029  0.0416  113 LYS A C   
904  O O   . LYS A 113 ? 0.8237 0.6322 0.3221 0.0671  -0.0081 0.0416  113 LYS A O   
905  C CB  . LYS A 113 ? 0.9831 0.7591 0.3847 0.0712  0.0027  0.0531  113 LYS A CB  
906  C CG  . LYS A 113 ? 1.1332 0.8873 0.5204 0.0804  -0.0084 0.064   113 LYS A CG  
907  C CD  . LYS A 113 ? 1.2981 1.0203 0.6461 0.077   0.0028  0.0798  113 LYS A CD  
908  C CE  . LYS A 113 ? 1.3776 1.0766 0.6853 0.0905  -0.0085 0.0892  113 LYS A CE  
909  N NZ  . LYS A 113 ? 1.4437 1.1445 0.72   0.0938  -0.0087 0.0863  113 LYS A NZ  
910  N N   . GLU A 114 ? 0.8404 0.6507 0.3264 0.049   0.0203  0.0433  114 GLU A N   
911  C CA  . GLU A 114 ? 0.8056 0.6198 0.3211 0.0399  0.0264  0.045   114 GLU A CA  
912  C C   . GLU A 114 ? 0.723  0.56   0.2781 0.0426  0.0168  0.0342  114 GLU A C   
913  O O   . GLU A 114 ? 0.7185 0.5541 0.2929 0.043   0.0115  0.0358  114 GLU A O   
914  C CB  . GLU A 114 ? 0.8339 0.6522 0.3505 0.0257  0.0459  0.0468  114 GLU A CB  
915  C CG  . GLU A 114 ? 0.7995 0.6243 0.3466 0.0151  0.0522  0.0475  114 GLU A CG  
916  C CD  . GLU A 114 ? 0.8354 0.664  0.3827 0.0006  0.071   0.0501  114 GLU A CD  
917  O OE1 . GLU A 114 ? 0.8572 0.6654 0.3743 -0.0046 0.0806  0.0596  114 GLU A OE1 
918  O OE2 . GLU A 114 ? 0.8111 0.6631 0.3893 -0.006  0.0763  0.043   114 GLU A OE2 
919  N N   . TYR A 115 ? 0.7043 0.5615 0.2713 0.0441  0.0156  0.0229  115 TYR A N   
920  C CA  . TYR A 115 ? 0.658  0.535  0.2606 0.0464  0.0072  0.0127  115 TYR A CA  
921  C C   . TYR A 115 ? 0.6501 0.523  0.2558 0.0566  -0.0098 0.0126  115 TYR A C   
922  O O   . TYR A 115 ? 0.5919 0.4712 0.2242 0.0565  -0.0148 0.011   115 TYR A O   
923  C CB  . TYR A 115 ? 0.6551 0.55   0.2655 0.048   0.0073  0.0006  115 TYR A CB  
924  C CG  . TYR A 115 ? 0.624  0.5328 0.2484 0.0395  0.022   -0.0036 115 TYR A CG  
925  C CD1 . TYR A 115 ? 0.665  0.5687 0.277  0.0309  0.0375  0.0033  115 TYR A CD1 
926  C CD2 . TYR A 115 ? 0.6327 0.5602 0.2833 0.0404  0.0204  -0.0148 115 TYR A CD2 
927  C CE1 . TYR A 115 ? 0.649  0.5687 0.2756 0.024   0.0507  -0.0011 115 TYR A CE1 
928  C CE2 . TYR A 115 ? 0.6323 0.5734 0.2959 0.0347  0.0331  -0.0189 115 TYR A CE2 
929  C CZ  . TYR A 115 ? 0.6624 0.601  0.3142 0.0269  0.0481  -0.0124 115 TYR A CZ  
930  O OH  . TYR A 115 ? 0.6742 0.6292 0.3404 0.0225  0.0601  -0.0174 115 TYR A OH  
931  N N   . GLY A 116 ? 0.6974 0.5607 0.2758 0.0658  -0.019  0.0141  116 GLY A N   
932  C CA  . GLY A 116 ? 0.7091 0.5719 0.292  0.0764  -0.036  0.0131  116 GLY A CA  
933  C C   . GLY A 116 ? 0.6934 0.5432 0.2819 0.0773  -0.0373 0.0225  116 GLY A C   
934  O O   . GLY A 116 ? 0.6901 0.5485 0.3032 0.0809  -0.0461 0.0189  116 GLY A O   
935  N N   . LYS A 117 ? 0.7354 0.5641 0.3015 0.0731  -0.0274 0.0339  117 LYS A N   
936  C CA  . LYS A 117 ? 0.7413 0.553  0.3078 0.0738  -0.0272 0.043   117 LYS A CA  
937  C C   . LYS A 117 ? 0.6817 0.5042 0.2833 0.0652  -0.0219 0.0397  117 LYS A C   
938  O O   . LYS A 117 ? 0.656  0.4765 0.2725 0.0693  -0.0282 0.0406  117 LYS A O   
939  C CB  . LYS A 117 ? 0.8162 0.6018 0.3491 0.0686  -0.0153 0.0553  117 LYS A CB  
940  C CG  . LYS A 117 ? 0.9472 0.7143 0.4395 0.0784  -0.021  0.0622  117 LYS A CG  
941  C CD  . LYS A 117 ? 1.0341 0.7796 0.5131 0.0896  -0.0305 0.0715  117 LYS A CD  
942  C CE  . LYS A 117 ? 1.1619 0.8761 0.5966 0.0909  -0.0247 0.0849  117 LYS A CE  
943  N NZ  . LYS A 117 ? 1.1533 0.8681 0.5584 0.0949  -0.0266 0.0843  117 LYS A NZ  
944  N N   . VAL A 118 ? 0.6897 0.5253 0.3052 0.054   -0.0106 0.0353  118 VAL A N   
945  C CA  . VAL A 118 ? 0.6339 0.4793 0.2796 0.0453  -0.0051 0.0329  118 VAL A CA  
946  C C   . VAL A 118 ? 0.5989 0.4645 0.2756 0.0501  -0.0155 0.0232  118 VAL A C   
947  O O   . VAL A 118 ? 0.5755 0.4424 0.2716 0.049   -0.0173 0.0234  118 VAL A O   
948  C CB  . VAL A 118 ? 0.6272 0.48   0.2765 0.0324  0.01    0.0323  118 VAL A CB  
949  C CG1 . VAL A 118 ? 0.5717 0.4376 0.2531 0.0243  0.0138  0.0289  118 VAL A CG1 
950  C CG2 . VAL A 118 ? 0.651  0.4815 0.2714 0.026   0.0209  0.043   118 VAL A CG2 
951  N N   . TYR A 119 ? 0.5754 0.4559 0.2564 0.0547  -0.0216 0.0147  119 TYR A N   
952  C CA  . TYR A 119 ? 0.5325 0.43   0.2407 0.059   -0.0317 0.0056  119 TYR A CA  
953  C C   . TYR A 119 ? 0.5537 0.4452 0.2624 0.0686  -0.0439 0.008   119 TYR A C   
954  O O   . TYR A 119 ? 0.5342 0.4352 0.2685 0.0694  -0.0484 0.0043  119 TYR A O   
955  C CB  . TYR A 119 ? 0.5684 0.4798 0.2776 0.0615  -0.0356 -0.0043 119 TYR A CB  
956  C CG  . TYR A 119 ? 0.5142 0.4383 0.2377 0.0535  -0.0255 -0.0099 119 TYR A CG  
957  C CD1 . TYR A 119 ? 0.5152 0.4544 0.2694 0.051   -0.0266 -0.017  119 TYR A CD1 
958  C CD2 . TYR A 119 ? 0.5498 0.4709 0.2554 0.0491  -0.0144 -0.0081 119 TYR A CD2 
959  C CE1 . TYR A 119 ? 0.507  0.4569 0.2736 0.0452  -0.0176 -0.0213 119 TYR A CE1 
960  C CE2 . TYR A 119 ? 0.5258 0.4598 0.2456 0.0429  -0.0049 -0.0132 119 TYR A CE2 
961  C CZ  . TYR A 119 ? 0.5055 0.4537 0.2556 0.0417  -0.0071 -0.0198 119 TYR A CZ  
962  O OH  . TYR A 119 ? 0.5028 0.4629 0.2651 0.0371  0.0022  -0.0242 119 TYR A OH  
963  N N   . LYS A 120 ? 0.5956 0.4708 0.2758 0.076   -0.0483 0.0148  120 LYS A N   
964  C CA  . LYS A 120 ? 0.6365 0.5052 0.3155 0.0868  -0.0597 0.018   120 LYS A CA  
965  C C   . LYS A 120 ? 0.6013 0.4605 0.2921 0.0841  -0.055  0.0235  120 LYS A C   
966  O O   . LYS A 120 ? 0.6263 0.4917 0.3354 0.0903  -0.0629 0.0211  120 LYS A O   
967  C CB  . LYS A 120 ? 0.6687 0.5202 0.3124 0.0964  -0.0657 0.0251  120 LYS A CB  
968  C CG  . LYS A 120 ? 0.7252 0.5787 0.3736 0.1101  -0.0812 0.0249  120 LYS A CG  
969  C CD  . LYS A 120 ? 0.7934 0.6349 0.4092 0.1224  -0.0913 0.0302  120 LYS A CD  
970  C CE  . LYS A 120 ? 0.8147 0.6635 0.4432 0.1357  -0.1066 0.0287  120 LYS A CE  
971  N NZ  . LYS A 120 ? 0.924  0.7635 0.5228 0.1489  -0.1184 0.0336  120 LYS A NZ  
972  N N   . ILE A 121 ? 0.627  0.4724 0.3085 0.0746  -0.042  0.03    121 ILE A N   
973  C CA  . ILE A 121 ? 0.6376 0.4735 0.3298 0.0703  -0.0368 0.0341  121 ILE A CA  
974  C C   . ILE A 121 ? 0.5733 0.4305 0.3009 0.0668  -0.0382 0.0256  121 ILE A C   
975  O O   . ILE A 121 ? 0.5798 0.437  0.3217 0.071   -0.0424 0.0251  121 ILE A O   
976  C CB  . ILE A 121 ? 0.6498 0.4689 0.3266 0.0586  -0.0225 0.0414  121 ILE A CB  
977  C CG1 . ILE A 121 ? 0.7193 0.5122 0.3587 0.063   -0.0212 0.0514  121 ILE A CG1 
978  C CG2 . ILE A 121 ? 0.6283 0.4412 0.32   0.0519  -0.0169 0.0429  121 ILE A CG2 
979  C CD1 . ILE A 121 ? 0.7329 0.5122 0.3538 0.0501  -0.0062 0.0577  121 ILE A CD1 
980  N N   . HIS A 122 ? 0.5773 0.4523 0.3182 0.06    -0.0348 0.0189  122 HIS A N   
981  C CA  . HIS A 122 ? 0.5252 0.4193 0.2975 0.0566  -0.0358 0.0113  122 HIS A CA  
982  C C   . HIS A 122 ? 0.5236 0.4279 0.3108 0.0663  -0.0481 0.0059  122 HIS A C   
983  O O   . HIS A 122 ? 0.5121 0.4237 0.3215 0.0655  -0.0491 0.0033  122 HIS A O   
984  C CB  . HIS A 122 ? 0.5235 0.4326 0.3042 0.0497  -0.0305 0.0054  122 HIS A CB  
985  C CG  . HIS A 122 ? 0.5009 0.4281 0.3106 0.0481  -0.0331 -0.0024 122 HIS A CG  
986  N ND1 . HIS A 122 ? 0.4946 0.4244 0.323  0.044   -0.0308 -0.002  122 HIS A ND1 
987  C CD2 . HIS A 122 ? 0.5707 0.5124 0.3922 0.0498  -0.0376 -0.0106 122 HIS A CD2 
988  C CE1 . HIS A 122 ? 0.5407 0.4861 0.3913 0.0435  -0.0337 -0.0091 122 HIS A CE1 
989  N NE2 . HIS A 122 ? 0.549  0.5013 0.3963 0.047   -0.0379 -0.0146 122 HIS A NE2 
990  N N   . ARG A 123 ? 0.5065 0.4143 0.2833 0.0742  -0.057  0.0032  123 ARG A N   
991  C CA  . ARG A 123 ? 0.5094 0.4301 0.3012 0.0827  -0.0694 -0.0029 123 ARG A CA  
992  C C   . ARG A 123 ? 0.5071 0.4191 0.3001 0.0907  -0.0739 0.0021  123 ARG A C   
993  O O   . ARG A 123 ? 0.5064 0.4304 0.3237 0.0926  -0.0778 -0.0024 123 ARG A O   
994  C CB  . ARG A 123 ? 0.5361 0.4611 0.3127 0.0895  -0.0788 -0.0067 123 ARG A CB  
995  C CG  . ARG A 123 ? 0.5371 0.4751 0.3208 0.0829  -0.0761 -0.0152 123 ARG A CG  
996  C CD  . ARG A 123 ? 0.5373 0.4944 0.3533 0.0805  -0.0801 -0.0248 123 ARG A CD  
997  N NE  . ARG A 123 ? 0.5754 0.5432 0.3987 0.0886  -0.0939 -0.0305 123 ARG A NE  
998  C CZ  . ARG A 123 ? 0.5877 0.5674 0.436  0.0907  -0.0998 -0.0344 123 ARG A CZ  
999  N NH1 . ARG A 123 ? 0.5966 0.5793 0.4659 0.0851  -0.0931 -0.0339 123 ARG A NH1 
1000 N NH2 . ARG A 123 ? 0.6361 0.6263 0.4884 0.0983  -0.1126 -0.0392 123 ARG A NH2 
1001 N N   . GLU A 124 ? 0.5256 0.4161 0.2924 0.0949  -0.0723 0.0113  124 GLU A N   
1002 C CA  . GLU A 124 ? 0.5741 0.4525 0.3389 0.1035  -0.0756 0.0168  124 GLU A CA  
1003 C C   . GLU A 124 ? 0.573  0.4503 0.3572 0.097   -0.0676 0.0167  124 GLU A C   
1004 O O   . GLU A 124 ? 0.564  0.4469 0.3647 0.1036  -0.0723 0.0145  124 GLU A O   
1005 C CB  . GLU A 124 ? 0.6254 0.4772 0.3556 0.1085  -0.0741 0.0273  124 GLU A CB  
1006 C CG  . GLU A 124 ? 0.7069 0.5599 0.4178 0.1192  -0.0854 0.0277  124 GLU A CG  
1007 C CD  . GLU A 124 ? 0.8217 0.646  0.4955 0.1247  -0.0839 0.0394  124 GLU A CD  
1008 O OE1 . GLU A 124 ? 0.8895 0.6922 0.5528 0.1188  -0.073  0.0469  124 GLU A OE1 
1009 O OE2 . GLU A 124 ? 0.8627 0.6855 0.5173 0.1349  -0.0939 0.041   124 GLU A OE2 
1010 N N   . LEU A 125 ? 0.5632 0.4355 0.3462 0.0843  -0.056  0.0182  125 LEU A N   
1011 C CA  . LEU A 125 ? 0.5472 0.418  0.3458 0.0773  -0.0487 0.018   125 LEU A CA  
1012 C C   . LEU A 125 ? 0.5244 0.4188 0.3541 0.0765  -0.0521 0.0093  125 LEU A C   
1013 O O   . LEU A 125 ? 0.5475 0.4433 0.3915 0.0786  -0.0521 0.0081  125 LEU A O   
1014 C CB  . LEU A 125 ? 0.5307 0.3946 0.3224 0.0637  -0.0368 0.0208  125 LEU A CB  
1015 C CG  . LEU A 125 ? 0.5191 0.3814 0.3245 0.0551  -0.0294 0.0204  125 LEU A CG  
1016 C CD1 . LEU A 125 ? 0.5255 0.3686 0.3238 0.0612  -0.0297 0.0246  125 LEU A CD1 
1017 C CD2 . LEU A 125 ? 0.5311 0.388  0.3273 0.0422  -0.0192 0.0233  125 LEU A CD2 
1018 N N   . SER A 126 ? 0.5117 0.4232 0.3511 0.0731  -0.0542 0.0033  126 SER A N   
1019 C CA  . SER A 126 ? 0.5183 0.4496 0.3856 0.0708  -0.0561 -0.0044 126 SER A CA  
1020 C C   . SER A 126 ? 0.5089 0.4498 0.3895 0.0809  -0.0659 -0.0081 126 SER A C   
1021 O O   . SER A 126 ? 0.5287 0.4801 0.4314 0.0795  -0.0652 -0.012  126 SER A O   
1022 C CB  . SER A 126 ? 0.5247 0.4692 0.3979 0.0652  -0.0558 -0.01   126 SER A CB  
1023 O OG  . SER A 126 ? 0.6259 0.574  0.4893 0.0717  -0.0639 -0.0128 126 SER A OG  
1024 N N   . LYS A 127 ? 0.5401 0.4785 0.4078 0.0911  -0.0748 -0.007  127 LYS A N   
1025 C CA  . LYS A 127 ? 0.5598 0.5092 0.4408 0.1018  -0.0848 -0.0104 127 LYS A CA  
1026 C C   . LYS A 127 ? 0.6231 0.5603 0.5026 0.109   -0.0834 -0.0051 127 LYS A C   
1027 O O   . LYS A 127 ? 0.6539 0.602  0.5479 0.1181  -0.0905 -0.0082 127 LYS A O   
1028 C CB  . LYS A 127 ? 0.6027 0.5549 0.4695 0.1112  -0.0965 -0.0111 127 LYS A CB  
1029 C CG  . LYS A 127 ? 0.6378 0.6053 0.5095 0.1061  -0.1003 -0.0191 127 LYS A CG  
1030 C CD  . LYS A 127 ? 0.7009 0.6608 0.5443 0.1108  -0.106  -0.017  127 LYS A CD  
1031 C CE  . LYS A 127 ? 0.6985 0.6679 0.5406 0.1221  -0.1203 -0.02   127 LYS A CE  
1032 N NZ  . LYS A 127 ? 0.8428 0.7964 0.6502 0.1285  -0.1239 -0.0136 127 LYS A NZ  
1033 N N   . GLY A 128 ? 0.653  0.5677 0.515  0.1056  -0.0746 0.0023  128 GLY A N   
1034 C CA  . GLY A 128 ? 0.6429 0.5423 0.5009 0.1124  -0.0726 0.007   128 GLY A CA  
1035 C C   . GLY A 128 ? 0.6991 0.5851 0.5368 0.1267  -0.0806 0.0127  128 GLY A C   
1036 O O   . GLY A 128 ? 0.7588 0.636  0.5972 0.1361  -0.0817 0.0152  128 GLY A O   
1037 N N   . GLU A 129 ? 0.6677 0.5502 0.4854 0.1287  -0.0857 0.0153  129 GLU A N   
1038 C CA  . GLU A 129 ? 0.7274 0.592  0.5189 0.1413  -0.0922 0.0228  129 GLU A CA  
1039 C C   . GLU A 129 ? 0.7386 0.5699 0.5032 0.1381  -0.0822 0.0329  129 GLU A C   
1040 O O   . GLU A 129 ? 0.767  0.578  0.5118 0.1496  -0.0857 0.0402  129 GLU A O   
1041 C CB  . GLU A 129 ? 0.6985 0.5705 0.4759 0.1439  -0.1007 0.0219  129 GLU A CB  
1042 C CG  . GLU A 129 ? 0.7328 0.6359 0.5356 0.1485  -0.1124 0.0116  129 GLU A CG  
1043 C CD  . GLU A 129 ? 0.8179 0.731  0.6096 0.1481  -0.12   0.008   129 GLU A CD  
1044 O OE1 . GLU A 129 ? 0.8792 0.8175 0.6921 0.1487  -0.1285 -0.0016 129 GLU A OE1 
1045 O OE2 . GLU A 129 ? 0.7901 0.6855 0.552  0.146   -0.1166 0.0142  129 GLU A OE2 
1046 N N   . ILE A 130 ? 0.6865 0.512  0.4496 0.1226  -0.0702 0.0333  130 ILE A N   
1047 C CA  . ILE A 130 ? 0.679  0.4752 0.4217 0.1165  -0.0595 0.0411  130 ILE A CA  
1048 C C   . ILE A 130 ? 0.6646 0.4662 0.4271 0.1041  -0.05   0.0368  130 ILE A C   
1049 O O   . ILE A 130 ? 0.6376 0.464  0.4245 0.0989  -0.0508 0.0291  130 ILE A O   
1050 C CB  . ILE A 130 ? 0.71   0.4923 0.4252 0.1088  -0.0541 0.0472  130 ILE A CB  
1051 C CG1 . ILE A 130 ? 0.6656 0.4687 0.3935 0.0948  -0.049  0.0411  130 ILE A CG1 
1052 C CG2 . ILE A 130 ? 0.7558 0.5297 0.4469 0.1217  -0.0635 0.0525  130 ILE A CG2 
1053 C CD1 . ILE A 130 ? 0.6564 0.4499 0.3594 0.0879  -0.0433 0.0459  130 ILE A CD1 
1054 N N   . ASP A 131 ? 0.6748 0.4516 0.4245 0.0992  -0.0412 0.0419  131 ASP A N   
1055 C CA  . ASP A 131 ? 0.6869 0.4655 0.4497 0.0859  -0.0318 0.0384  131 ASP A CA  
1056 C C   . ASP A 131 ? 0.6289 0.4014 0.3787 0.0707  -0.023  0.0414  131 ASP A C   
1057 O O   . ASP A 131 ? 0.6475 0.4112 0.3768 0.0708  -0.0229 0.0465  131 ASP A O   
1058 C CB  . ASP A 131 ? 0.7362 0.4949 0.4971 0.0898  -0.0282 0.0398  131 ASP A CB  
1059 C CG  . ASP A 131 ? 0.8999 0.6217 0.6308 0.0902  -0.0229 0.0485  131 ASP A CG  
1060 O OD1 . ASP A 131 ? 0.9954 0.705  0.7056 0.0831  -0.0189 0.0542  131 ASP A OD1 
1061 O OD2 . ASP A 131 ? 1.0796 0.7837 0.8074 0.0981  -0.0222 0.0496  131 ASP A OD2 
1062 N N   . VAL A 132 ? 0.6831 0.4598 0.4444 0.0577  -0.0153 0.0382  132 VAL A N   
1063 C CA  . VAL A 132 ? 0.7241 0.5025 0.4809 0.0424  -0.0071 0.039   132 VAL A CA  
1064 C C   . VAL A 132 ? 0.7569 0.5055 0.4854 0.0372  0.0001  0.0472  132 VAL A C   
1065 O O   . VAL A 132 ? 0.7356 0.4843 0.4532 0.0291  0.0049  0.0499  132 VAL A O   
1066 C CB  . VAL A 132 ? 0.7724 0.5649 0.5502 0.0314  -0.0025 0.0332  132 VAL A CB  
1067 C CG1 . VAL A 132 ? 0.7994 0.5718 0.5726 0.0278  0.0026  0.0341  132 VAL A CG1 
1068 C CG2 . VAL A 132 ? 0.7347 0.5399 0.5156 0.0179  0.0033  0.0324  132 VAL A CG2 
1069 N N   . PHE A 133 ? 0.7994 0.5215 0.5147 0.0426  0.001   0.0512  133 PHE A N   
1070 C CA  . PHE A 133 ? 0.8607 0.5502 0.5471 0.0379  0.008   0.0594  133 PHE A CA  
1071 C C   . PHE A 133 ? 0.826  0.5069 0.49   0.0461  0.0044  0.0664  133 PHE A C   
1072 O O   . PHE A 133 ? 0.8543 0.5217 0.4982 0.0372  0.0117  0.0721  133 PHE A O   
1073 C CB  . PHE A 133 ? 0.9896 0.6504 0.6669 0.0421  0.0102  0.0615  133 PHE A CB  
1074 C CG  . PHE A 133 ? 1.1    0.7682 0.7963 0.0326  0.0144  0.0543  133 PHE A CG  
1075 C CD1 . PHE A 133 ? 1.1917 0.8561 0.8863 0.0139  0.0237  0.0533  133 PHE A CD1 
1076 C CD2 . PHE A 133 ? 1.1486 0.8309 0.8655 0.0419  0.009   0.0479  133 PHE A CD2 
1077 C CE1 . PHE A 133 ? 1.2066 0.8794 0.9174 0.0055  0.0265  0.0464  133 PHE A CE1 
1078 C CE2 . PHE A 133 ? 1.1263 0.8162 0.8587 0.0331  0.013   0.0414  133 PHE A CE2 
1079 C CZ  . PHE A 133 ? 1.1715 0.8562 0.9    0.0152  0.0212  0.0407  133 PHE A CZ  
1080 N N   . GLU A 134 ? 0.814  0.503  0.4806 0.0629  -0.0067 0.0659  134 GLU A N   
1081 C CA  . GLU A 134 ? 0.8633 0.5476 0.5089 0.0713  -0.0118 0.0715  134 GLU A CA  
1082 C C   . GLU A 134 ? 0.7719 0.4792 0.4221 0.0621  -0.0097 0.0683  134 GLU A C   
1083 O O   . GLU A 134 ? 0.8097 0.506  0.4361 0.0599  -0.0064 0.0742  134 GLU A O   
1084 C CB  . GLU A 134 ? 0.9228 0.6164 0.5729 0.0909  -0.0258 0.0703  134 GLU A CB  
1085 C CG  . GLU A 134 ? 1.0529 0.7279 0.7007 0.1044  -0.0299 0.0729  134 GLU A CG  
1086 C CD  . GLU A 134 ? 1.0538 0.7506 0.7189 0.1215  -0.0439 0.0681  134 GLU A CD  
1087 O OE1 . GLU A 134 ? 1.1806 0.8734 0.8282 0.133   -0.0523 0.0729  134 GLU A OE1 
1088 O OE2 . GLU A 134 ? 0.8617 0.5806 0.5568 0.1222  -0.0461 0.0597  134 GLU A OE2 
1089 N N   . ALA A 135 ? 0.7317 0.4696 0.4113 0.0576  -0.0114 0.059   135 ALA A N   
1090 C CA  . ALA A 135 ? 0.6851 0.4441 0.3706 0.0493  -0.0086 0.0553  135 ALA A CA  
1091 C C   . ALA A 135 ? 0.7018 0.4495 0.3739 0.0336  0.0045  0.0596  135 ALA A C   
1092 O O   . ALA A 135 ? 0.673  0.4201 0.3292 0.0307  0.0081  0.0625  135 ALA A O   
1093 C CB  . ALA A 135 ? 0.6558 0.4445 0.3742 0.0467  -0.0115 0.0456  135 ALA A CB  
1094 N N   . SER A 136 ? 0.7746 0.5128 0.4519 0.0233  0.0119  0.06    136 SER A N   
1095 C CA  . SER A 136 ? 0.8087 0.536  0.4747 0.0072  0.0244  0.0638  136 SER A CA  
1096 C C   . SER A 136 ? 0.7858 0.4835 0.417  0.0081  0.029   0.0738  136 SER A C   
1097 O O   . SER A 136 ? 0.7658 0.4648 0.3861 -0.0015 0.0373  0.0764  136 SER A O   
1098 C CB  . SER A 136 ? 0.7899 0.5099 0.4654 -0.0036 0.0302  0.062   136 SER A CB  
1099 O OG  . SER A 136 ? 0.7832 0.5325 0.4854 -0.0123 0.0315  0.0544  136 SER A OG  
1100 N N   . ALA A 137 ? 0.8769 0.5478 0.4908 0.0193  0.0245  0.0796  137 ALA A N   
1101 C CA  . ALA A 137 ? 0.933  0.5724 0.5109 0.0223  0.0279  0.0903  137 ALA A CA  
1102 C C   . ALA A 137 ? 0.9098 0.5595 0.4746 0.0289  0.024   0.0921  137 ALA A C   
1103 O O   . ALA A 137 ? 0.9225 0.5573 0.4618 0.0227  0.032   0.0991  137 ALA A O   
1104 C CB  . ALA A 137 ? 0.965  0.5763 0.5289 0.0367  0.0215  0.0957  137 ALA A CB  
1105 N N   . ASN A 138 ? 0.851  0.526  0.4327 0.0407  0.0121  0.0855  138 ASN A N   
1106 C CA  . ASN A 138 ? 0.8607 0.5469 0.4308 0.047   0.0074  0.0855  138 ASN A CA  
1107 C C   . ASN A 138 ? 0.8252 0.5282 0.3989 0.0326  0.0178  0.0823  138 ASN A C   
1108 O O   . ASN A 138 ? 0.842  0.5402 0.3926 0.0328  0.0208  0.0863  138 ASN A O   
1109 C CB  . ASN A 138 ? 0.892  0.6022 0.4817 0.0611  -0.0075 0.0777  138 ASN A CB  
1110 C CG  . ASN A 138 ? 0.9719 0.6667 0.553  0.0781  -0.0186 0.0818  138 ASN A CG  
1111 O OD1 . ASN A 138 ? 0.9333 0.5968 0.4915 0.0807  -0.0155 0.091   138 ASN A OD1 
1112 N ND2 . ASN A 138 ? 0.9798 0.6964 0.5803 0.0897  -0.0315 0.0748  138 ASN A ND2 
1113 N N   . ILE A 139 ? 0.7663 0.4897 0.3684 0.021   0.0231  0.0752  139 ILE A N   
1114 C CA  . ILE A 139 ? 0.7429 0.4834 0.3512 0.0077  0.0334  0.0721  139 ILE A CA  
1115 C C   . ILE A 139 ? 0.7971 0.5138 0.3786 -0.0038 0.0469  0.0811  139 ILE A C   
1116 O O   . ILE A 139 ? 0.8146 0.5339 0.3809 -0.007  0.0531  0.083   139 ILE A O   
1117 C CB  . ILE A 139 ? 0.7006 0.4656 0.3439 -0.0014 0.0355  0.0637  139 ILE A CB  
1118 C CG1 . ILE A 139 ? 0.6737 0.4642 0.3423 0.0088  0.0237  0.0546  139 ILE A CG1 
1119 C CG2 . ILE A 139 ? 0.695  0.4737 0.3438 -0.0167 0.0481  0.0621  139 ILE A CG2 
1120 C CD1 . ILE A 139 ? 0.6354 0.4422 0.3347 0.0028  0.0237  0.0483  139 ILE A CD1 
1121 N N   . GLY A 140 ? 0.8927 0.5852 0.4676 -0.01   0.0517  0.0863  140 GLY A N   
1122 C CA  . GLY A 140 ? 0.9328 0.5992 0.4821 -0.0224 0.0651  0.0951  140 GLY A CA  
1123 C C   . GLY A 140 ? 0.9817 0.6254 0.4932 -0.0146 0.0657  0.1046  140 GLY A C   
1124 O O   . GLY A 140 ? 1.0273 0.6672 0.5215 -0.0243 0.0771  0.1087  140 GLY A O   
1125 N N   . LYS A 141 ? 1.0462 0.6766 0.5453 0.0035  0.0529  0.1077  141 LYS A N   
1126 C CA  . LYS A 141 ? 1.0884 0.6976 0.5507 0.0138  0.0504  0.1168  141 LYS A CA  
1127 C C   . LYS A 141 ? 1.0615 0.6928 0.519  0.0149  0.0506  0.1133  141 LYS A C   
1128 O O   . LYS A 141 ? 1.0792 0.6928 0.503  0.0167  0.0544  0.1213  141 LYS A O   
1129 C CB  . LYS A 141 ? 1.2018 0.8008 0.6579 0.0349  0.034   0.1188  141 LYS A CB  
1130 C CG  . LYS A 141 ? 1.3101 0.8764 0.7569 0.0389  0.0334  0.1256  141 LYS A CG  
1131 C CD  . LYS A 141 ? 1.376  0.942  0.8278 0.0603  0.0165  0.1247  141 LYS A CD  
1132 C CE  . LYS A 141 ? 1.5093 1.0689 0.9338 0.076   0.0068  0.1305  141 LYS A CE  
1133 N NZ  . LYS A 141 ? 1.611  1.1682 1.0396 0.0967  -0.0091 0.1305  141 LYS A NZ  
1134 N N   . GLN A 142 ? 0.9972 0.6649 0.4861 0.0148  0.0462  0.1016  142 GLN A N   
1135 C CA  . GLN A 142 ? 1.0011 0.6895 0.4865 0.0176  0.0452  0.0966  142 GLN A CA  
1136 C C   . GLN A 142 ? 1.0414 0.7315 0.5156 0.0022  0.0626  0.0988  142 GLN A C   
1137 O O   . GLN A 142 ? 0.9855 0.6801 0.4412 0.0053  0.0643  0.0987  142 GLN A O   
1138 C CB  . GLN A 142 ? 0.9808 0.7045 0.5035 0.0217  0.0361  0.0835  142 GLN A CB  
1139 C CG  . GLN A 142 ? 0.9747 0.7192 0.4955 0.0269  0.0325  0.0766  142 GLN A CG  
1140 C CD  . GLN A 142 ? 0.9433 0.6732 0.4318 0.0409  0.0229  0.0813  142 GLN A CD  
1141 O OE1 . GLN A 142 ? 0.9691 0.6866 0.4513 0.0531  0.0108  0.0848  142 GLN A OE1 
1142 N NE2 . GLN A 142 ? 0.9524 0.6845 0.4197 0.0395  0.0285  0.0813  142 GLN A NE2 
1143 N N   . ARG A 143 ? 1.033  0.7213 0.5188 -0.0142 0.0754  0.0999  143 ARG A N   
1144 C CA  . ARG A 143 ? 1.1138 0.8053 0.5912 -0.0299 0.0928  0.1019  143 ARG A CA  
1145 C C   . ARG A 143 ? 1.0608 0.7868 0.5542 -0.0288 0.0935  0.0919  143 ARG A C   
1146 O O   . ARG A 143 ? 0.9985 0.7245 0.4699 -0.0265 0.0979  0.0932  143 ARG A O   
1147 C CB  . ARG A 143 ? 1.2405 0.897  0.6726 -0.0314 0.101   0.1149  143 ARG A CB  
1148 C CG  . ARG A 143 ? 1.3079 0.9268 0.7228 -0.0344 0.1031  0.1253  143 ARG A CG  
1149 C CD  . ARG A 143 ? 1.425  1.0276 0.8261 -0.0549 0.123   0.1321  143 ARG A CD  
1150 N NE  . ARG A 143 ? 1.5257 1.1175 0.8921 -0.0573 0.1334  0.1393  143 ARG A NE  
1151 C CZ  . ARG A 143 ? 1.6806 1.2373 1.0104 -0.0653 0.1457  0.1519  143 ARG A CZ  
1152 N NH1 . ARG A 143 ? 1.6743 1.2233 0.9717 -0.0651 0.1536  0.1578  143 ARG A NH1 
1153 N NH2 . ARG A 143 ? 1.7882 1.3154 1.1117 -0.0737 0.1504  0.1586  143 ARG A NH2 
1154 N N   . ILE A 144 ? 0.9524 0.7069 0.4841 -0.0294 0.0886  0.0815  144 ILE A N   
1155 C CA  . ILE A 144 ? 0.8899 0.6769 0.442  -0.0264 0.087   0.0708  144 ILE A CA  
1156 C C   . ILE A 144 ? 0.8819 0.6815 0.433  -0.0394 0.1043  0.0701  144 ILE A C   
1157 O O   . ILE A 144 ? 0.9189 0.7182 0.4787 -0.0538 0.1151  0.0727  144 ILE A O   
1158 C CB  . ILE A 144 ? 0.8286 0.6372 0.4206 -0.0256 0.0789  0.0622  144 ILE A CB  
1159 C CG1 . ILE A 144 ? 0.8479 0.6471 0.4411 -0.0115 0.0622  0.062   144 ILE A CG1 
1160 C CG2 . ILE A 144 ? 0.7819 0.6238 0.4001 -0.0257 0.0799  0.0514  144 ILE A CG2 
1161 C CD1 . ILE A 144 ? 0.8139 0.629  0.4422 -0.0116 0.0554  0.0554  144 ILE A CD1 
1162 N N   . LYS A 145 ? 0.8887 0.7013 0.4315 -0.0349 0.1069  0.0655  145 LYS A N   
1163 C CA  . LYS A 145 ? 0.9375 0.7643 0.4798 -0.0459 0.124   0.0641  145 LYS A CA  
1164 C C   . LYS A 145 ? 0.8558 0.719  0.4326 -0.0452 0.1246  0.0516  145 LYS A C   
1165 O O   . LYS A 145 ? 0.8398 0.7197 0.427  -0.0558 0.1389  0.0496  145 LYS A O   
1166 C CB  . LYS A 145 ? 1.0709 0.8843 0.5739 -0.0426 0.1307  0.0685  145 LYS A CB  
1167 C CG  . LYS A 145 ? 1.2098 0.9847 0.6706 -0.041  0.1305  0.0818  145 LYS A CG  
1168 C CD  . LYS A 145 ? 1.3451 1.11   0.7671 -0.0356 0.1352  0.0848  145 LYS A CD  
1169 C CE  . LYS A 145 ? 1.4649 1.2005 0.8496 -0.0219 0.1226  0.0927  145 LYS A CE  
1170 N NZ  . LYS A 145 ? 1.5601 1.2599 0.9104 -0.0279 0.1307  0.1076  145 LYS A NZ  
1171 N N   . THR A 146 ? 0.7719 0.6472 0.3649 -0.0327 0.1103  0.0434  146 THR A N   
1172 C CA  . THR A 146 ? 0.7625 0.6687 0.3854 -0.0308 0.1108  0.0321  146 THR A CA  
1173 C C   . THR A 146 ? 0.6924 0.6148 0.3528 -0.0366 0.1085  0.029   146 THR A C   
1174 O O   . THR A 146 ? 0.6672 0.5791 0.3342 -0.0357 0.0992  0.0319  146 THR A O   
1175 C CB  . THR A 146 ? 0.7506 0.6612 0.3722 -0.016  0.0977  0.0242  146 THR A CB  
1176 O OG1 . THR A 146 ? 0.6877 0.5918 0.3194 -0.0086 0.0817  0.0239  146 THR A OG1 
1177 C CG2 . THR A 146 ? 0.7737 0.6696 0.3569 -0.0102 0.0993  0.0264  146 THR A CG2 
1178 N N   . ALA A 147 ? 0.6822 0.6317 0.3679 -0.0409 0.1161  0.0222  147 ALA A N   
1179 C CA  . ALA A 147 ? 0.6807 0.6487 0.4022 -0.0446 0.1126  0.0183  147 ALA A CA  
1180 C C   . ALA A 147 ? 0.6565 0.6246 0.3915 -0.033  0.0961  0.0136  147 ALA A C   
1181 O O   . ALA A 147 ? 0.6319 0.6003 0.3839 -0.0352 0.0898  0.0145  147 ALA A O   
1182 C CB  . ALA A 147 ? 0.6667 0.6644 0.4113 -0.0484 0.1228  0.0117  147 ALA A CB  
1183 N N   . GLU A 148 ? 0.6275 0.5949 0.3537 -0.0213 0.0894  0.0084  148 GLU A N   
1184 C CA  . GLU A 148 ? 0.6116 0.5801 0.3499 -0.0108 0.0746  0.003   148 GLU A CA  
1185 C C   . GLU A 148 ? 0.5643 0.5136 0.2959 -0.0088 0.0641  0.0088  148 GLU A C   
1186 O O   . GLU A 148 ? 0.4978 0.4516 0.2504 -0.0071 0.056   0.0068  148 GLU A O   
1187 C CB  . GLU A 148 ? 0.7284 0.6922 0.4483 0       0.0691  -0.0021 148 GLU A CB  
1188 C CG  . GLU A 148 ? 0.7557 0.7356 0.4783 0.002   0.0771  -0.01   148 GLU A CG  
1189 C CD  . GLU A 148 ? 0.7587 0.7321 0.4531 -0.0023 0.0899  -0.006  148 GLU A CD  
1190 O OE1 . GLU A 148 ? 0.7723 0.7351 0.4391 0.0038  0.0886  -0.0072 148 GLU A OE1 
1191 O OE2 . GLU A 148 ? 0.7006 0.6794 0.4015 -0.0127 0.1012  -0.0012 148 GLU A OE2 
1192 N N   . MET A 149 ? 0.5659 0.4929 0.267  -0.0079 0.0642  0.0161  149 MET A N   
1193 C CA  . MET A 149 ? 0.5784 0.4862 0.2714 -0.0038 0.0541  0.0215  149 MET A CA  
1194 C C   . MET A 149 ? 0.5693 0.4697 0.2699 -0.014  0.0588  0.0277  149 MET A C   
1195 O O   . MET A 149 ? 0.5552 0.4478 0.2635 -0.0111 0.0504  0.0291  149 MET A O   
1196 C CB  . MET A 149 ? 0.6094 0.4963 0.2669 0.0031  0.0509  0.0267  149 MET A CB  
1197 C CG  . MET A 149 ? 0.6252 0.5195 0.2775 0.0142  0.0421  0.0191  149 MET A CG  
1198 S SD  . MET A 149 ? 0.5935 0.5011 0.2761 0.0228  0.0261  0.0102  149 MET A SD  
1199 C CE  . MET A 149 ? 0.5759 0.5101 0.2867 0.0199  0.0317  -0.0006 149 MET A CE  
1200 N N   . ASN A 150 ? 0.5943 0.499  0.2954 -0.0262 0.0723  0.0303  150 ASN A N   
1201 C CA  . ASN A 150 ? 0.5908 0.4927 0.3034 -0.0375 0.0768  0.0339  150 ASN A CA  
1202 C C   . ASN A 150 ? 0.5397 0.4601 0.2854 -0.0359 0.0692  0.0274  150 ASN A C   
1203 O O   . ASN A 150 ? 0.5467 0.4581 0.2986 -0.0369 0.0637  0.0293  150 ASN A O   
1204 C CB  . ASN A 150 ? 0.6602 0.5676 0.3699 -0.0515 0.0925  0.0365  150 ASN A CB  
1205 C CG  . ASN A 150 ? 0.7518 0.6594 0.4762 -0.0644 0.0964  0.0385  150 ASN A CG  
1206 O OD1 . ASN A 150 ? 0.7832 0.6681 0.4971 -0.0659 0.093   0.0438  150 ASN A OD1 
1207 N ND2 . ASN A 150 ? 0.7777 0.7112 0.5278 -0.0726 0.102   0.0336  150 ASN A ND2 
1208 N N   . ILE A 151 ? 0.5074 0.4522 0.2728 -0.0327 0.0688  0.0197  151 ILE A N   
1209 C CA  . ILE A 151 ? 0.4739 0.4353 0.2686 -0.0301 0.0616  0.0139  151 ILE A CA  
1210 C C   . ILE A 151 ? 0.4651 0.4171 0.2604 -0.0194 0.0483  0.0125  151 ILE A C   
1211 O O   . ILE A 151 ? 0.4207 0.3733 0.2309 -0.0201 0.0429  0.0122  151 ILE A O   
1212 C CB  . ILE A 151 ? 0.4444 0.4311 0.2574 -0.028  0.065   0.0066  151 ILE A CB  
1213 C CG1 . ILE A 151 ? 0.4777 0.4785 0.2982 -0.0394 0.0774  0.0076  151 ILE A CG1 
1214 C CG2 . ILE A 151 ? 0.4063 0.4062 0.2451 -0.022  0.0558  0.0008  151 ILE A CG2 
1215 C CD1 . ILE A 151 ? 0.4805 0.503  0.3105 -0.0365 0.084   0.0014  151 ILE A CD1 
1216 N N   . PHE A 152 ? 0.4701 0.4153 0.2501 -0.0097 0.043   0.011   152 PHE A N   
1217 C CA  . PHE A 152 ? 0.464  0.403  0.2453 0.0003  0.0304  0.009   152 PHE A CA  
1218 C C   . PHE A 152 ? 0.4558 0.3758 0.2291 -0.0003 0.0269  0.0156  152 PHE A C   
1219 O O   . PHE A 152 ? 0.4711 0.3916 0.2575 0.004   0.0188  0.0137  152 PHE A O   
1220 C CB  . PHE A 152 ? 0.4886 0.4242 0.2534 0.01    0.0247  0.0059  152 PHE A CB  
1221 C CG  . PHE A 152 ? 0.494  0.4322 0.2702 0.0191  0.0116  0.0009  152 PHE A CG  
1222 C CD1 . PHE A 152 ? 0.5841 0.5389 0.385  0.0205  0.0086  -0.0068 152 PHE A CD1 
1223 C CD2 . PHE A 152 ? 0.5648 0.4893 0.3293 0.0259  0.0027  0.0041  152 PHE A CD2 
1224 C CE1 . PHE A 152 ? 0.5269 0.4846 0.3405 0.0268  -0.0022 -0.0113 152 PHE A CE1 
1225 C CE2 . PHE A 152 ? 0.545  0.4751 0.3236 0.0331  -0.0086 -0.0011 152 PHE A CE2 
1226 C CZ  . PHE A 152 ? 0.5594 0.506  0.3626 0.0327  -0.0106 -0.0088 152 PHE A CZ  
1227 N N   . SER A 153 ? 0.4993 0.4022 0.2514 -0.006  0.0339  0.0231  153 SER A N   
1228 C CA  . SER A 153 ? 0.5133 0.3952 0.256  -0.0065 0.0317  0.0294  153 SER A CA  
1229 C C   . SER A 153 ? 0.5245 0.4126 0.2897 -0.0135 0.0323  0.0278  153 SER A C   
1230 O O   . SER A 153 ? 0.5296 0.407  0.2968 -0.0099 0.0266  0.0291  153 SER A O   
1231 C CB  . SER A 153 ? 0.5684 0.4285 0.283  -0.0119 0.0399  0.0379  153 SER A CB  
1232 O OG  . SER A 153 ? 0.6067 0.4715 0.3265 -0.0263 0.0518  0.0392  153 SER A OG  
1233 N N   . LYS A 154 ? 0.4947 0.4012 0.2771 -0.0224 0.0387  0.0246  154 LYS A N   
1234 C CA  . LYS A 154 ? 0.4644 0.3795 0.268  -0.0286 0.0383  0.0225  154 LYS A CA  
1235 C C   . LYS A 154 ? 0.4441 0.372  0.2677 -0.0201 0.0289  0.0166  154 LYS A C   
1236 O O   . LYS A 154 ? 0.4156 0.3395 0.2476 -0.0195 0.0244  0.0164  154 LYS A O   
1237 C CB  . LYS A 154 ? 0.4911 0.4226 0.306  -0.0404 0.0474  0.0212  154 LYS A CB  
1238 C CG  . LYS A 154 ? 0.5664 0.4826 0.3613 -0.0511 0.0577  0.0275  154 LYS A CG  
1239 C CD  . LYS A 154 ? 0.6367 0.5732 0.4424 -0.0618 0.0676  0.0256  154 LYS A CD  
1240 C CE  . LYS A 154 ? 0.6954 0.6197 0.4808 -0.0719 0.0792  0.0312  154 LYS A CE  
1241 N NZ  . LYS A 154 ? 0.7061 0.6037 0.4769 -0.078  0.0799  0.0367  154 LYS A NZ  
1242 N N   . MET A 155 ? 0.4087 0.3498 0.2379 -0.0135 0.0261  0.0119  155 MET A N   
1243 C CA  . MET A 155 ? 0.4213 0.3733 0.2689 -0.0064 0.0179  0.0064  155 MET A CA  
1244 C C   . MET A 155 ? 0.4024 0.3415 0.2452 0.0014  0.0094  0.0072  155 MET A C   
1245 O O   . MET A 155 ? 0.3728 0.317  0.2317 0.0031  0.0048  0.0047  155 MET A O   
1246 C CB  . MET A 155 ? 0.4494 0.4152 0.3019 -0.0011 0.017   0.0006  155 MET A CB  
1247 C CG  . MET A 155 ? 0.4771 0.4596 0.3412 -0.007  0.0246  -0.0015 155 MET A CG  
1248 S SD  . MET A 155 ? 0.5146 0.5116 0.385  0.0001  0.0244  -0.0091 155 MET A SD  
1249 C CE  . MET A 155 ? 0.621  0.6058 0.4639 0.0055  0.0242  -0.009  155 MET A CE  
1250 N N   . LEU A 156 ? 0.4375 0.3615 0.2591 0.0067  0.0072  0.0107  156 LEU A N   
1251 C CA  . LEU A 156 ? 0.431  0.3464 0.2509 0.0157  -0.0018 0.0108  156 LEU A CA  
1252 C C   . LEU A 156 ? 0.4324 0.3376 0.2563 0.0128  -0.001  0.0139  156 LEU A C   
1253 O O   . LEU A 156 ? 0.4188 0.3255 0.2537 0.0185  -0.0073 0.0116  156 LEU A O   
1254 C CB  . LEU A 156 ? 0.4781 0.3809 0.2745 0.0236  -0.0057 0.0138  156 LEU A CB  
1255 C CG  . LEU A 156 ? 0.5066 0.3871 0.2775 0.0207  0       0.0224  156 LEU A CG  
1256 C CD1 . LEU A 156 ? 0.5233 0.386  0.2886 0.0254  -0.0038 0.0268  156 LEU A CD1 
1257 C CD2 . LEU A 156 ? 0.5486 0.4227 0.2952 0.0247  0.0003  0.0247  156 LEU A CD2 
1258 N N   . LEU A 157 ? 0.448  0.3434 0.2636 0.0034  0.0071  0.0185  157 LEU A N   
1259 C CA  . LEU A 157 ? 0.4554 0.3406 0.2739 -0.001  0.0088  0.0204  157 LEU A CA  
1260 C C   . LEU A 157 ? 0.3958 0.2981 0.2386 -0.0045 0.0078  0.0153  157 LEU A C   
1261 O O   . LEU A 157 ? 0.4279 0.3262 0.2776 -0.0025 0.005   0.0144  157 LEU A O   
1262 C CB  . LEU A 157 ? 0.5008 0.3717 0.3039 -0.0118 0.0179  0.0256  157 LEU A CB  
1263 C CG  . LEU A 157 ? 0.5568 0.4051 0.3323 -0.0088 0.0199  0.0323  157 LEU A CG  
1264 C CD1 . LEU A 157 ? 0.604  0.4401 0.3667 -0.0221 0.0305  0.0369  157 LEU A CD1 
1265 C CD2 . LEU A 157 ? 0.598  0.4271 0.3646 0.0013  0.0138  0.0349  157 LEU A CD2 
1266 N N   . MET A 158 ? 0.4212 0.3421 0.2762 -0.0089 0.0101  0.0122  158 MET A N   
1267 C CA  . MET A 158 ? 0.4011 0.3382 0.2776 -0.0115 0.0089  0.0082  158 MET A CA  
1268 C C   . MET A 158 ? 0.3541 0.2967 0.2425 -0.0025 0.0014  0.0043  158 MET A C   
1269 O O   . MET A 158 ? 0.3426 0.2873 0.2421 -0.0034 -0.0001 0.003   158 MET A O   
1270 C CB  . MET A 158 ? 0.3982 0.3537 0.2848 -0.0159 0.0125  0.0058  158 MET A CB  
1271 C CG  . MET A 158 ? 0.4202 0.3754 0.3002 -0.0265 0.0205  0.0087  158 MET A CG  
1272 S SD  . MET A 158 ? 0.4413 0.4187 0.331  -0.0295 0.0257  0.0061  158 MET A SD  
1273 C CE  . MET A 158 ? 0.4215 0.417  0.3363 -0.0296 0.0216  0.0024  158 MET A CE  
1274 N N   . TYR A 159 ? 0.3635 0.3077 0.2486 0.0056  -0.0032 0.0024  159 TYR A N   
1275 C CA  . TYR A 159 ? 0.354  0.3044 0.2513 0.0131  -0.0103 -0.0019 159 TYR A CA  
1276 C C   . TYR A 159 ? 0.3657 0.3055 0.2621 0.0168  -0.0131 -0.0004 159 TYR A C   
1277 O O   . TYR A 159 ? 0.3622 0.3084 0.2736 0.0181  -0.0154 -0.0032 159 TYR A O   
1278 C CB  . TYR A 159 ? 0.3876 0.3405 0.2787 0.0203  -0.0152 -0.0046 159 TYR A CB  
1279 C CG  . TYR A 159 ? 0.3516 0.3166 0.2474 0.0188  -0.0133 -0.0085 159 TYR A CG  
1280 C CD1 . TYR A 159 ? 0.3626 0.3401 0.2773 0.0171  -0.0132 -0.0125 159 TYR A CD1 
1281 C CD2 . TYR A 159 ? 0.4155 0.3783 0.2957 0.02    -0.0114 -0.0081 159 TYR A CD2 
1282 C CE1 . TYR A 159 ? 0.3608 0.3479 0.2799 0.017   -0.0113 -0.0163 159 TYR A CE1 
1283 C CE2 . TYR A 159 ? 0.4039 0.3776 0.2884 0.0196  -0.0091 -0.0125 159 TYR A CE2 
1284 C CZ  . TYR A 159 ? 0.3681 0.3538 0.2726 0.0184  -0.0091 -0.0167 159 TYR A CZ  
1285 O OH  . TYR A 159 ? 0.3639 0.3588 0.2726 0.0189  -0.0065 -0.0211 159 TYR A OH  
1286 N N   . ASP A 160 ? 0.3963 0.3197 0.2748 0.0187  -0.0123 0.0042  160 ASP A N   
1287 C CA  . ASP A 160 ? 0.4298 0.341  0.3053 0.0235  -0.0144 0.0059  160 ASP A CA  
1288 C C   . ASP A 160 ? 0.3997 0.3085 0.2825 0.0168  -0.0098 0.0059  160 ASP A C   
1289 O O   . ASP A 160 ? 0.3948 0.3053 0.288  0.0207  -0.012  0.0036  160 ASP A O   
1290 C CB  . ASP A 160 ? 0.455  0.3457 0.3071 0.0269  -0.0138 0.0116  160 ASP A CB  
1291 C CG  . ASP A 160 ? 0.536  0.4139 0.3853 0.0351  -0.0169 0.013   160 ASP A CG  
1292 O OD1 . ASP A 160 ? 0.5202 0.4076 0.3808 0.044   -0.0238 0.0096  160 ASP A OD1 
1293 O OD2 . ASP A 160 ? 0.5702 0.4295 0.4074 0.0321  -0.0121 0.017   160 ASP A OD2 
1294 N N   . CYS A 161 ? 0.4208 0.3269 0.2986 0.0066  -0.0035 0.008   161 CYS A N   
1295 C CA  . CYS A 161 ? 0.4142 0.3197 0.2982 -0.0009 0.0002  0.0072  161 CYS A CA  
1296 C C   . CYS A 161 ? 0.4002 0.3224 0.3043 0.0001  -0.0024 0.0029  161 CYS A C   
1297 O O   . CYS A 161 ? 0.3611 0.2806 0.2701 0.0004  -0.0021 0.0016  161 CYS A O   
1298 C CB  . CYS A 161 ? 0.4131 0.3213 0.294  -0.0125 0.0059  0.0086  161 CYS A CB  
1299 S SG  . CYS A 161 ? 0.4811 0.3662 0.338  -0.0179 0.0115  0.014   161 CYS A SG  
1300 N N   . LEU A 162 ? 0.3655 0.3035 0.2799 0.0009  -0.0044 0.0007  162 LEU A N   
1301 C CA  . LEU A 162 ? 0.3555 0.3069 0.2874 0.0016  -0.0064 -0.0027 162 LEU A CA  
1302 C C   . LEU A 162 ? 0.3707 0.3215 0.3096 0.0092  -0.0103 -0.0051 162 LEU A C   
1303 O O   . LEU A 162 ? 0.348  0.3018 0.2964 0.0083  -0.0095 -0.0065 162 LEU A O   
1304 C CB  . LEU A 162 ? 0.3578 0.3227 0.2972 0.0017  -0.0075 -0.0046 162 LEU A CB  
1305 C CG  . LEU A 162 ? 0.3356 0.3127 0.2918 0.002   -0.009  -0.0075 162 LEU A CG  
1306 C CD1 . LEU A 162 ? 0.3265 0.3061 0.2872 -0.0044 -0.0062 -0.006  162 LEU A CD1 
1307 C CD2 . LEU A 162 ? 0.364  0.3509 0.3247 0.0034  -0.0097 -0.0096 162 LEU A CD2 
1308 N N   . ASN A 163 ? 0.3462 0.2944 0.2808 0.0167  -0.0145 -0.0056 163 ASN A N   
1309 C CA  . ASN A 163 ? 0.3998 0.3501 0.3426 0.0243  -0.0188 -0.0082 163 ASN A CA  
1310 C C   . ASN A 163 ? 0.4058 0.3449 0.3449 0.0261  -0.0165 -0.0068 163 ASN A C   
1311 O O   . ASN A 163 ? 0.3844 0.329  0.3355 0.03    -0.0177 -0.0097 163 ASN A O   
1312 C CB  . ASN A 163 ? 0.4515 0.4009 0.3883 0.0328  -0.0249 -0.0088 163 ASN A CB  
1313 C CG  . ASN A 163 ? 0.5209 0.4797 0.4589 0.0323  -0.0275 -0.0113 163 ASN A CG  
1314 O OD1 . ASN A 163 ? 0.6289 0.5971 0.5772 0.0271  -0.0254 -0.0134 163 ASN A OD1 
1315 N ND2 . ASN A 163 ? 0.5707 0.5259 0.4965 0.0378  -0.0318 -0.0107 163 ASN A ND2 
1316 N N   . LYS A 164 ? 0.391  0.314  0.3139 0.0234  -0.0128 -0.0029 164 LYS A N   
1317 C CA  . LYS A 164 ? 0.4018 0.3114 0.3195 0.0259  -0.0104 -0.0022 164 LYS A CA  
1318 C C   . LYS A 164 ? 0.4058 0.313  0.3248 0.0172  -0.0047 -0.0028 164 LYS A C   
1319 O O   . LYS A 164 ? 0.4078 0.3011 0.3192 0.0174  -0.0014 -0.0025 164 LYS A O   
1320 C CB  . LYS A 164 ? 0.4636 0.3528 0.3606 0.029   -0.0099 0.0023  164 LYS A CB  
1321 C CG  . LYS A 164 ? 0.5631 0.4514 0.4545 0.0393  -0.0162 0.0037  164 LYS A CG  
1322 C CD  . LYS A 164 ? 0.6788 0.5791 0.5848 0.0503  -0.0229 -0.0001 164 LYS A CD  
1323 C CE  . LYS A 164 ? 0.6741 0.5784 0.5753 0.0586  -0.0307 0.0004  164 LYS A CE  
1324 N NZ  . LYS A 164 ? 0.7126 0.5958 0.5889 0.0612  -0.0301 0.0068  164 LYS A NZ  
1325 N N   . GLY A 165 ? 0.3906 0.3101 0.3176 0.0097  -0.0035 -0.0037 165 GLY A N   
1326 C CA  . GLY A 165 ? 0.4201 0.3395 0.3483 0.002   0.0006  -0.0044 165 GLY A CA  
1327 C C   . GLY A 165 ? 0.437  0.3425 0.3496 -0.006  0.0044  -0.0022 165 GLY A C   
1328 O O   . GLY A 165 ? 0.4707 0.3685 0.379  -0.0102 0.0076  -0.0034 165 GLY A O   
1329 N N   . ASN A 166 ? 0.406  0.3058 0.3086 -0.0077 0.0045  0.0006  166 ASN A N   
1330 C CA  . ASN A 166 ? 0.3846 0.2711 0.2728 -0.0166 0.0088  0.0027  166 ASN A CA  
1331 C C   . ASN A 166 ? 0.3874 0.2881 0.2798 -0.025  0.0095  0.0035  166 ASN A C   
1332 O O   . ASN A 166 ? 0.389  0.2897 0.2759 -0.0252 0.0101  0.0058  166 ASN A O   
1333 C CB  . ASN A 166 ? 0.4395 0.3055 0.3111 -0.0121 0.0097  0.0059  166 ASN A CB  
1334 C CG  . ASN A 166 ? 0.4753 0.3246 0.331  -0.0225 0.015   0.0082  166 ASN A CG  
1335 O OD1 . ASN A 166 ? 0.4892 0.3394 0.3458 -0.0324 0.0178  0.0061  166 ASN A OD1 
1336 N ND2 . ASN A 166 ? 0.5194 0.3552 0.3607 -0.0218 0.0165  0.0124  166 ASN A ND2 
1337 N N   . PHE A 167 ? 0.3849 0.2982 0.2866 -0.0314 0.0097  0.0015  167 PHE A N   
1338 C CA  . PHE A 167 ? 0.3803 0.3118 0.2909 -0.0363 0.0092  0.0017  167 PHE A CA  
1339 C C   . PHE A 167 ? 0.4135 0.3436 0.3167 -0.0473 0.0131  0.003   167 PHE A C   
1340 O O   . PHE A 167 ? 0.3955 0.3388 0.3039 -0.0497 0.0138  0.0037  167 PHE A O   
1341 C CB  . PHE A 167 ? 0.3398 0.2867 0.2643 -0.036  0.0066  -0.0002 167 PHE A CB  
1342 C CG  . PHE A 167 ? 0.3623 0.311  0.2948 -0.0267 0.004   -0.0015 167 PHE A CG  
1343 C CD1 . PHE A 167 ? 0.3452 0.2936 0.2799 -0.0185 0.0019  -0.0016 167 PHE A CD1 
1344 C CD2 . PHE A 167 ? 0.3372 0.289  0.2755 -0.0269 0.0036  -0.0029 167 PHE A CD2 
1345 C CE1 . PHE A 167 ? 0.3196 0.2715 0.2637 -0.0113 -0.0006 -0.0036 167 PHE A CE1 
1346 C CE2 . PHE A 167 ? 0.3778 0.3321 0.3247 -0.0197 0.0022  -0.0042 167 PHE A CE2 
1347 C CZ  . PHE A 167 ? 0.3643 0.3192 0.3151 -0.0123 0.0001  -0.0048 167 PHE A CZ  
1348 N N   . ALA A 168 ? 0.4022 0.3161 0.2934 -0.0543 0.0162  0.0029  168 ALA A N   
1349 C CA  . ALA A 168 ? 0.4654 0.3798 0.3519 -0.0672 0.0199  0.0031  168 ALA A CA  
1350 C C   . ALA A 168 ? 0.4477 0.3629 0.3297 -0.0696 0.0234  0.0061  168 ALA A C   
1351 O O   . ALA A 168 ? 0.428  0.3586 0.3168 -0.0776 0.0253  0.0057  168 ALA A O   
1352 C CB  . ALA A 168 ? 0.5462 0.4387 0.4184 -0.0743 0.0229  0.0021  168 ALA A CB  
1353 N N   . PRO A 169 ? 0.4286 0.3285 0.299  -0.0625 0.0245  0.0091  169 PRO A N   
1354 C CA  . PRO A 169 ? 0.4173 0.3165 0.2802 -0.0656 0.0288  0.0123  169 PRO A CA  
1355 C C   . PRO A 169 ? 0.3913 0.3152 0.268  -0.0625 0.0276  0.0113  169 PRO A C   
1356 O O   . PRO A 169 ? 0.3891 0.3173 0.2622 -0.0671 0.0324  0.013   169 PRO A O   
1357 C CB  . PRO A 169 ? 0.4698 0.3458 0.3156 -0.0569 0.0288  0.0159  169 PRO A CB  
1358 C CG  . PRO A 169 ? 0.4776 0.3394 0.3211 -0.0518 0.026   0.0144  169 PRO A CG  
1359 C CD  . PRO A 169 ? 0.4328 0.3146 0.295  -0.052  0.0222  0.0099  169 PRO A CD  
1360 N N   . MET A 170 ? 0.3844 0.3227 0.2757 -0.0544 0.022   0.0087  170 MET A N   
1361 C CA  . MET A 170 ? 0.3676 0.3236 0.2691 -0.0485 0.0206  0.0076  170 MET A CA  
1362 C C   . MET A 170 ? 0.3434 0.3183 0.2539 -0.0566 0.0244  0.0069  170 MET A C   
1363 O O   . MET A 170 ? 0.3584 0.3401 0.268  -0.0552 0.0274  0.0072  170 MET A O   
1364 C CB  . MET A 170 ? 0.3708 0.3356 0.2855 -0.0395 0.0144  0.0049  170 MET A CB  
1365 C CG  . MET A 170 ? 0.3924 0.3431 0.3005 -0.03   0.0108  0.0051  170 MET A CG  
1366 S SD  . MET A 170 ? 0.3661 0.3288 0.2915 -0.0216 0.0049  0.0016  170 MET A SD  
1367 C CE  . MET A 170 ? 0.4003 0.3782 0.333  -0.0173 0.0041  -0.0003 170 MET A CE  
1368 N N   . MET A 171 ? 0.3328 0.3182 0.2529 -0.0643 0.024   0.0053  171 MET A N   
1369 C CA  . MET A 171 ? 0.342  0.3489 0.2737 -0.0717 0.0268  0.0042  171 MET A CA  
1370 C C   . MET A 171 ? 0.3536 0.3555 0.275  -0.0818 0.0347  0.0061  171 MET A C   
1371 O O   . MET A 171 ? 0.3423 0.3607 0.2707 -0.0842 0.039   0.0056  171 MET A O   
1372 C CB  . MET A 171 ? 0.356  0.3743 0.2983 -0.0781 0.0234  0.0022  171 MET A CB  
1373 C CG  . MET A 171 ? 0.3826 0.427  0.34   -0.0842 0.0248  0.0007  171 MET A CG  
1374 S SD  . MET A 171 ? 0.3981 0.4651 0.3711 -0.0737 0.0247  -0.0003 171 MET A SD  
1375 C CE  . MET A 171 ? 0.4298 0.5162 0.4209 -0.0695 0.0167  -0.0018 171 MET A CE  
1376 N N   . LEU A 172 ? 0.3616 0.3395 0.2657 -0.0869 0.0374  0.0083  172 LEU A N   
1377 C CA  . LEU A 172 ? 0.4123 0.3803 0.3037 -0.097  0.0455  0.0109  172 LEU A CA  
1378 C C   . LEU A 172 ? 0.4117 0.3774 0.2945 -0.0903 0.0492  0.0135  172 LEU A C   
1379 O O   . LEU A 172 ? 0.4081 0.3844 0.292  -0.0971 0.0563  0.0141  172 LEU A O   
1380 C CB  . LEU A 172 ? 0.5032 0.4414 0.376  -0.1026 0.0473  0.013   172 LEU A CB  
1381 C CG  . LEU A 172 ? 0.5154 0.4529 0.3931 -0.1104 0.0444  0.0097  172 LEU A CG  
1382 C CD1 . LEU A 172 ? 0.5653 0.4714 0.423  -0.117  0.0478  0.0112  172 LEU A CD1 
1383 C CD2 . LEU A 172 ? 0.5614 0.5245 0.4551 -0.1226 0.0456  0.0065  172 LEU A CD2 
1384 N N   . LEU A 173 ? 0.4156 0.3692 0.2907 -0.0775 0.0444  0.0146  173 LEU A N   
1385 C CA  . LEU A 173 ? 0.4206 0.373  0.2871 -0.0697 0.0461  0.0162  173 LEU A CA  
1386 C C   . LEU A 173 ? 0.3846 0.3642 0.2677 -0.0672 0.0471  0.0127  173 LEU A C   
1387 O O   . LEU A 173 ? 0.3735 0.357  0.2503 -0.0683 0.0533  0.0136  173 LEU A O   
1388 C CB  . LEU A 173 ? 0.4387 0.3762 0.2969 -0.0565 0.039   0.0169  173 LEU A CB  
1389 C CG  . LEU A 173 ? 0.4839 0.3921 0.3216 -0.0565 0.0394  0.0213  173 LEU A CG  
1390 C CD1 . LEU A 173 ? 0.5103 0.4114 0.3497 -0.0443 0.0309  0.0201  173 LEU A CD1 
1391 C CD2 . LEU A 173 ? 0.5198 0.4135 0.3359 -0.0567 0.0449  0.0262  173 LEU A CD2 
1392 N N   . PHE A 174 ? 0.3672 0.3642 0.27   -0.0633 0.0414  0.0088  174 PHE A N   
1393 C CA  . PHE A 174 ? 0.352  0.3738 0.2714 -0.06   0.0421  0.0054  174 PHE A CA  
1394 C C   . PHE A 174 ? 0.3516 0.3883 0.2756 -0.0707 0.0508  0.0055  174 PHE A C   
1395 O O   . PHE A 174 ? 0.3289 0.3785 0.2562 -0.0681 0.0555  0.004   174 PHE A O   
1396 C CB  . PHE A 174 ? 0.3637 0.3992 0.3024 -0.0561 0.035   0.0025  174 PHE A CB  
1397 C CG  . PHE A 174 ? 0.3625 0.4236 0.3196 -0.0529 0.0358  -0.0007 174 PHE A CG  
1398 C CD1 . PHE A 174 ? 0.3879 0.453  0.3474 -0.0422 0.0349  -0.0031 174 PHE A CD1 
1399 C CD2 . PHE A 174 ? 0.3597 0.4408 0.3315 -0.0603 0.0375  -0.0016 174 PHE A CD2 
1400 C CE1 . PHE A 174 ? 0.4019 0.4887 0.3781 -0.0381 0.036   -0.0062 174 PHE A CE1 
1401 C CE2 . PHE A 174 ? 0.4105 0.5156 0.3997 -0.0561 0.0384  -0.0043 174 PHE A CE2 
1402 C CZ  . PHE A 174 ? 0.4146 0.5216 0.4054 -0.0445 0.0382  -0.0066 174 PHE A CZ  
1403 N N   . GLN A 175 ? 0.3506 0.3876 0.2765 -0.0833 0.0531  0.0064  175 GLN A N   
1404 C CA  . GLN A 175 ? 0.3563 0.4101 0.2895 -0.0952 0.0611  0.0059  175 GLN A CA  
1405 C C   . GLN A 175 ? 0.3747 0.4184 0.2907 -0.0991 0.0711  0.0089  175 GLN A C   
1406 O O   . GLN A 175 ? 0.3816 0.4427 0.3051 -0.1064 0.079   0.0079  175 GLN A O   
1407 C CB  . GLN A 175 ? 0.3655 0.4183 0.3016 -0.1091 0.0612  0.0058  175 GLN A CB  
1408 C CG  . GLN A 175 ? 0.3619 0.4276 0.3144 -0.1067 0.052   0.0028  175 GLN A CG  
1409 C CD  . GLN A 175 ? 0.3661 0.4648 0.3425 -0.1026 0.0502  -0.0005 175 GLN A CD  
1410 O OE1 . GLN A 175 ? 0.4083 0.5255 0.3933 -0.1064 0.0569  -0.0016 175 GLN A OE1 
1411 N NE2 . GLN A 175 ? 0.3897 0.4958 0.377  -0.0942 0.0414  -0.0019 175 GLN A NE2 
1412 N N   . GLN A 176 ? 0.4207 0.4369 0.3136 -0.0947 0.0711  0.0127  176 GLN A N   
1413 C CA  . GLN A 176 ? 0.4645 0.4681 0.3371 -0.0974 0.0801  0.0165  176 GLN A CA  
1414 C C   . GLN A 176 ? 0.4891 0.5036 0.3615 -0.0866 0.0815  0.0145  176 GLN A C   
1415 O O   . GLN A 176 ? 0.5209 0.5289 0.3771 -0.0889 0.0899  0.0172  176 GLN A O   
1416 C CB  . GLN A 176 ? 0.5141 0.4828 0.3606 -0.0957 0.0784  0.0219  176 GLN A CB  
1417 C CG  . GLN A 176 ? 0.5155 0.4687 0.3587 -0.1063 0.0781  0.0236  176 GLN A CG  
1418 C CD  . GLN A 176 ? 0.5885 0.5079 0.409  -0.1005 0.0744  0.0281  176 GLN A CD  
1419 O OE1 . GLN A 176 ? 0.6057 0.5108 0.4087 -0.0913 0.0739  0.0316  176 GLN A OE1 
1420 N NE2 . GLN A 176 ? 0.6529 0.5586 0.4724 -0.1055 0.0718  0.028   176 GLN A NE2 
1421 N N   . ILE A 177 ? 0.4488 0.4783 0.3373 -0.0754 0.074   0.0099  177 ILE A N   
1422 C CA  . ILE A 177 ? 0.4443 0.481  0.3312 -0.0647 0.0747  0.0069  177 ILE A CA  
1423 C C   . ILE A 177 ? 0.4803 0.5464 0.3863 -0.0671 0.0816  0.0028  177 ILE A C   
1424 O O   . ILE A 177 ? 0.4338 0.5191 0.3628 -0.0682 0.0783  0       177 ILE A O   
1425 C CB  . ILE A 177 ? 0.4355 0.4699 0.3284 -0.0513 0.0633  0.0038  177 ILE A CB  
1426 C CG1 . ILE A 177 ? 0.4268 0.4342 0.301  -0.0476 0.0571  0.0075  177 ILE A CG1 
1427 C CG2 . ILE A 177 ? 0.4265 0.4719 0.3224 -0.0411 0.0637  -0.0011 177 ILE A CG2 
1428 C CD1 . ILE A 177 ? 0.4478 0.4534 0.3307 -0.0374 0.0461  0.0046  177 ILE A CD1 
1429 N N   . ASP A 178 ? 0.4978 0.5673 0.3941 -0.0655 0.0901  0.002   178 ASP A N   
1430 C CA  . ASP A 178 ? 0.5068 0.6041 0.4206 -0.0644 0.097   -0.0028 178 ASP A CA  
1431 C C   . ASP A 178 ? 0.5215 0.6162 0.4246 -0.0522 0.0979  -0.0064 178 ASP A C   
1432 O O   . ASP A 178 ? 0.4746 0.5599 0.3563 -0.0537 0.1061  -0.0046 178 ASP A O   
1433 C CB  . ASP A 178 ? 0.5471 0.6537 0.4608 -0.0791 0.1098  -0.0005 178 ASP A CB  
1434 C CG  . ASP A 178 ? 0.5642 0.7021 0.4966 -0.08   0.1194  -0.0052 178 ASP A CG  
1435 O OD1 . ASP A 178 ? 0.6016 0.7551 0.5494 -0.0679 0.1156  -0.0108 178 ASP A OD1 
1436 O OD2 . ASP A 178 ? 0.6242 0.77   0.5559 -0.0927 0.1311  -0.0035 178 ASP A OD2 
1437 N N   . LEU A 179 ? 0.4912 0.5943 0.4088 -0.0404 0.09    -0.0117 179 LEU A N   
1438 C CA  . LEU A 179 ? 0.5283 0.6277 0.4371 -0.0285 0.089   -0.0166 179 LEU A CA  
1439 C C   . LEU A 179 ? 0.5499 0.6648 0.458  -0.0284 0.1016  -0.0202 179 LEU A C   
1440 O O   . LEU A 179 ? 0.558  0.6641 0.4479 -0.0221 0.1041  -0.0228 179 LEU A O   
1441 C CB  . LEU A 179 ? 0.5601 0.6645 0.4861 -0.0175 0.0788  -0.0217 179 LEU A CB  
1442 C CG  . LEU A 179 ? 0.5197 0.608  0.4448 -0.0158 0.0666  -0.0191 179 LEU A CG  
1443 C CD1 . LEU A 179 ? 0.5507 0.6444 0.4929 -0.006  0.0584  -0.024  179 LEU A CD1 
1444 C CD2 . LEU A 179 ? 0.5372 0.6013 0.436  -0.0143 0.0633  -0.0165 179 LEU A CD2 
1445 N N   . SER A 180 ? 0.5017 0.6396 0.4282 -0.036  0.1099  -0.0203 180 SER A N   
1446 C CA  . SER A 180 ? 0.5303 0.6858 0.4586 -0.0368 0.1235  -0.0238 180 SER A CA  
1447 C C   . SER A 180 ? 0.5736 0.7129 0.4715 -0.0435 0.1335  -0.0197 180 SER A C   
1448 O O   . SER A 180 ? 0.6084 0.758  0.5017 -0.0425 0.145   -0.0229 180 SER A O   
1449 C CB  . SER A 180 ? 0.5365 0.722  0.4926 -0.0448 0.1298  -0.0245 180 SER A CB  
1450 O OG  . SER A 180 ? 0.5718 0.7539 0.5206 -0.061  0.1367  -0.0185 180 SER A OG  
1451 N N   . GLU A 181 ? 0.5789 0.6932 0.4559 -0.0501 0.13    -0.0125 181 GLU A N   
1452 C CA  . GLU A 181 ? 0.6111 0.7058 0.456  -0.0552 0.1382  -0.0074 181 GLU A CA  
1453 C C   . GLU A 181 ? 0.6237 0.7021 0.4445 -0.0429 0.1342  -0.01   181 GLU A C   
1454 O O   . GLU A 181 ? 0.612  0.6773 0.4052 -0.0454 0.1421  -0.0066 181 GLU A O   
1455 C CB  . GLU A 181 ? 0.6806 0.7513 0.5101 -0.0646 0.135   0.0013  181 GLU A CB  
1456 C CG  . GLU A 181 ? 0.8142 0.897  0.6599 -0.0802 0.1419  0.0041  181 GLU A CG  
1457 C CD  . GLU A 181 ? 1.0268 1.0815 0.854  -0.0893 0.1394  0.0123  181 GLU A CD  
1458 O OE1 . GLU A 181 ? 1.1443 1.1996 0.9866 -0.0932 0.1318  0.0128  181 GLU A OE1 
1459 O OE2 . GLU A 181 ? 1.146  1.1769 0.9423 -0.0915 0.1448  0.0182  181 GLU A OE2 
1460 N N   . ILE A 182 ? 0.5843 0.6623 0.4138 -0.0307 0.122   -0.0155 182 ILE A N   
1461 C CA  . ILE A 182 ? 0.6213 0.686  0.4304 -0.0195 0.1169  -0.0195 182 ILE A CA  
1462 C C   . ILE A 182 ? 0.635  0.7167 0.447  -0.0142 0.1269  -0.0275 182 ILE A C   
1463 O O   . ILE A 182 ? 0.6485 0.7488 0.4861 -0.0086 0.1259  -0.0342 182 ILE A O   
1464 C CB  . ILE A 182 ? 0.5676 0.6253 0.3861 -0.01   0.1005  -0.0228 182 ILE A CB  
1465 C CG1 . ILE A 182 ? 0.5871 0.6301 0.4051 -0.0149 0.0918  -0.0155 182 ILE A CG1 
1466 C CG2 . ILE A 182 ? 0.5873 0.6322 0.3852 0.0004  0.0946  -0.0279 182 ILE A CG2 
1467 C CD1 . ILE A 182 ? 0.541  0.5785 0.3697 -0.0071 0.077   -0.0182 182 ILE A CD1 
1468 N N   . LYS A 183 ? 0.744  0.818  0.5286 -0.015  0.1365  -0.027  183 LYS A N   
1469 C CA  . LYS A 183 ? 0.7959 0.8859 0.5812 -0.011  0.1485  -0.0345 183 LYS A CA  
1470 C C   . LYS A 183 ? 0.8371 0.915  0.5996 0.0005  0.1445  -0.0414 183 LYS A C   
1471 O O   . LYS A 183 ? 0.8173 0.9083 0.5866 0.0074  0.1503  -0.0505 183 LYS A O   
1472 C CB  . LYS A 183 ? 0.8705 0.9646 0.6412 -0.0217 0.1664  -0.0298 183 LYS A CB  
1473 C CG  . LYS A 183 ? 0.9405 1.0434 0.7258 -0.0365 0.1732  -0.0223 183 LYS A CG  
1474 C CD  . LYS A 183 ? 0.8789 1.0116 0.7058 -0.0384 0.1737  -0.0262 183 LYS A CD  
1475 C CE  . LYS A 183 ? 0.9027 1.0452 0.7377 -0.0549 0.1843  -0.0199 183 LYS A CE  
1476 N NZ  . LYS A 183 ? 0.8936 1.065  0.7683 -0.057  0.1825  -0.0232 183 LYS A NZ  
1477 N N   . GLU A 184 ? 0.8848 0.938  0.6184 0.0023  0.1358  -0.0375 184 GLU A N   
1478 C CA  . GLU A 184 ? 0.9876 1.0293 0.694  0.0112  0.1336  -0.0436 184 GLU A CA  
1479 C C   . GLU A 184 ? 0.8496 0.8944 0.5723 0.0222  0.1211  -0.054  184 GLU A C   
1480 O O   . GLU A 184 ? 0.8877 0.9367 0.6059 0.0296  0.1242  -0.064  184 GLU A O   
1481 C CB  . GLU A 184 ? 1.1085 1.1246 0.7789 0.0087  0.1289  -0.0346 184 GLU A CB  
1482 C CG  . GLU A 184 ? 1.2572 1.2565 0.9019 0.0187  0.1165  -0.039  184 GLU A CG  
1483 C CD  . GLU A 184 ? 1.3815 1.3589 1.008  0.0202  0.1021  -0.0313 184 GLU A CD  
1484 O OE1 . GLU A 184 ? 1.527  1.5    1.1657 0.0152  0.0975  -0.0233 184 GLU A OE1 
1485 O OE2 . GLU A 184 ? 1.2143 1.179  0.8135 0.0272  0.0946  -0.0339 184 GLU A OE2 
1486 N N   . ASN A 185 ? 0.7239 0.7665 0.4662 0.0228  0.1081  -0.0521 185 ASN A N   
1487 C CA  . ASN A 185 ? 0.6763 0.7117 0.4229 0.0314  0.0931  -0.0588 185 ASN A CA  
1488 C C   . ASN A 185 ? 0.6563 0.7051 0.4397 0.0332  0.0887  -0.0621 185 ASN A C   
1489 O O   . ASN A 185 ? 0.6308 0.6781 0.4287 0.0297  0.0813  -0.0563 185 ASN A O   
1490 C CB  . ASN A 185 ? 0.6866 0.7021 0.4135 0.0308  0.081   -0.0522 185 ASN A CB  
1491 C CG  . ASN A 185 ? 0.6195 0.6276 0.3468 0.0388  0.0657  -0.0594 185 ASN A CG  
1492 O OD1 . ASN A 185 ? 0.57   0.5866 0.3196 0.0429  0.0624  -0.0675 185 ASN A OD1 
1493 N ND2 . ASN A 185 ? 0.6466 0.6391 0.3501 0.0409  0.0561  -0.0565 185 ASN A ND2 
1494 N N   . ARG A 186 ? 0.5742 0.6341 0.3709 0.0397  0.0927  -0.0717 186 ARG A N   
1495 C CA  . ARG A 186 ? 0.6021 0.6738 0.4317 0.0428  0.0894  -0.0746 186 ARG A CA  
1496 C C   . ARG A 186 ? 0.5875 0.6477 0.4245 0.0458  0.0737  -0.0758 186 ARG A C   
1497 O O   . ARG A 186 ? 0.4861 0.5521 0.347  0.0445  0.0693  -0.0726 186 ARG A O   
1498 C CB  . ARG A 186 ? 0.653  0.7356 0.4922 0.051   0.0968  -0.0852 186 ARG A CB  
1499 C CG  . ARG A 186 ? 0.7788 0.882  0.6502 0.0525  0.1023  -0.0853 186 ARG A CG  
1500 C CD  . ARG A 186 ? 0.8979 1.0182 0.7693 0.0539  0.1189  -0.0893 186 ARG A CD  
1501 N NE  . ARG A 186 ? 0.9942 1.1067 0.8463 0.0618  0.1232  -0.0997 186 ARG A NE  
1502 C CZ  . ARG A 186 ? 1.073  1.1947 0.9342 0.0708  0.1306  -0.1093 186 ARG A CZ  
1503 N NH1 . ARG A 186 ? 1.097  1.2414 0.9852 0.0728  0.1388  -0.109  186 ARG A NH1 
1504 N NH2 . ARG A 186 ? 1.0558 1.1642 0.8974 0.0778  0.1303  -0.1194 186 ARG A NH2 
1505 N N   . TYR A 187 ? 0.5591 0.6043 0.376  0.0498  0.0658  -0.0808 187 TYR A N   
1506 C CA  . TYR A 187 ? 0.5475 0.5828 0.3706 0.0518  0.0512  -0.0824 187 TYR A CA  
1507 C C   . TYR A 187 ? 0.5115 0.5441 0.3406 0.0455  0.0456  -0.0717 187 TYR A C   
1508 O O   . TYR A 187 ? 0.4526 0.4865 0.3023 0.0451  0.0389  -0.0703 187 TYR A O   
1509 C CB  . TYR A 187 ? 0.5548 0.5763 0.3537 0.0554  0.0428  -0.0885 187 TYR A CB  
1510 C CG  . TYR A 187 ? 0.5301 0.5442 0.3383 0.056   0.0281  -0.0895 187 TYR A CG  
1511 C CD1 . TYR A 187 ? 0.5198 0.5348 0.3486 0.0591  0.0235  -0.0969 187 TYR A CD1 
1512 C CD2 . TYR A 187 ? 0.5348 0.5415 0.3336 0.0533  0.0197  -0.0823 187 TYR A CD2 
1513 C CE1 . TYR A 187 ? 0.5043 0.5141 0.3436 0.0583  0.0116  -0.0974 187 TYR A CE1 
1514 C CE2 . TYR A 187 ? 0.5109 0.5138 0.321  0.0537  0.0073  -0.0834 187 TYR A CE2 
1515 C CZ  . TYR A 187 ? 0.5087 0.5136 0.339  0.0557  0.0035  -0.0911 187 TYR A CZ  
1516 O OH  . TYR A 187 ? 0.5286 0.5308 0.3716 0.055   -0.0073 -0.0921 187 TYR A OH  
1517 N N   . LEU A 188 ? 0.5039 0.5309 0.3128 0.0407  0.0487  -0.064  188 LEU A N   
1518 C CA  . LEU A 188 ? 0.515  0.5366 0.3265 0.0352  0.0439  -0.0542 188 LEU A CA  
1519 C C   . LEU A 188 ? 0.4701 0.5042 0.3056 0.0295  0.0497  -0.0493 188 LEU A C   
1520 O O   . LEU A 188 ? 0.4649 0.4979 0.315  0.0274  0.043   -0.0456 188 LEU A O   
1521 C CB  . LEU A 188 ? 0.5581 0.5679 0.3398 0.0322  0.0465  -0.0475 188 LEU A CB  
1522 C CG  . LEU A 188 ? 0.5785 0.5787 0.3583 0.0274  0.0418  -0.0374 188 LEU A CG  
1523 C CD1 . LEU A 188 ? 0.6041 0.587  0.3534 0.0295  0.0369  -0.0329 188 LEU A CD1 
1524 C CD2 . LEU A 188 ? 0.6388 0.6451 0.4256 0.0182  0.0529  -0.0301 188 LEU A CD2 
1525 N N   . LYS A 189 ? 0.4717 0.519  0.3122 0.0271  0.0618  -0.0498 189 LYS A N   
1526 C CA  . LYS A 189 ? 0.4806 0.5426 0.3447 0.0217  0.0665  -0.0459 189 LYS A CA  
1527 C C   . LYS A 189 ? 0.4481 0.5154 0.3373 0.0262  0.0585  -0.0492 189 LYS A C   
1528 O O   . LYS A 189 ? 0.4431 0.5129 0.3467 0.0221  0.0547  -0.0442 189 LYS A O   
1529 C CB  . LYS A 189 ? 0.527  0.6064 0.3968 0.0203  0.0802  -0.0481 189 LYS A CB  
1530 C CG  . LYS A 189 ? 0.5349 0.6313 0.4263 0.013   0.0855  -0.0434 189 LYS A CG  
1531 C CD  . LYS A 189 ? 0.5896 0.7067 0.4898 0.013   0.0987  -0.0471 189 LYS A CD  
1532 C CE  . LYS A 189 ? 0.609  0.7449 0.5322 0.0056  0.1023  -0.0429 189 LYS A CE  
1533 N NZ  . LYS A 189 ? 0.7215 0.8817 0.6639 0.0103  0.111   -0.0488 189 LYS A NZ  
1534 N N   . ASN A 190 ? 0.4198 0.4869 0.312  0.0346  0.0563  -0.0578 190 ASN A N   
1535 C CA  . ASN A 190 ? 0.4582 0.527  0.3712 0.0396  0.0494  -0.0614 190 ASN A CA  
1536 C C   . ASN A 190 ? 0.4207 0.4776 0.3357 0.0379  0.0378  -0.0582 190 ASN A C   
1537 O O   . ASN A 190 ? 0.3708 0.431  0.3042 0.0372  0.0338  -0.0557 190 ASN A O   
1538 C CB  . ASN A 190 ? 0.5356 0.6001 0.4454 0.0482  0.0487  -0.0718 190 ASN A CB  
1539 C CG  . ASN A 190 ? 0.6864 0.7631 0.6171 0.0536  0.0534  -0.0756 190 ASN A CG  
1540 O OD1 . ASN A 190 ? 0.6663 0.743  0.6149 0.0552  0.0475  -0.0743 190 ASN A OD1 
1541 N ND2 . ASN A 190 ? 0.6762 0.7631 0.6038 0.0566  0.064   -0.0797 190 ASN A ND2 
1542 N N   . SER A 191 ? 0.4098 0.4535 0.3057 0.0381  0.0323  -0.0588 191 SER A N   
1543 C CA  . SER A 191 ? 0.3768 0.4107 0.2738 0.0368  0.0218  -0.0561 191 SER A CA  
1544 C C   . SER A 191 ? 0.384  0.4191 0.2864 0.03    0.0224  -0.0466 191 SER A C   
1545 O O   . SER A 191 ? 0.3569 0.3907 0.2727 0.029   0.0165  -0.0446 191 SER A O   
1546 C CB  . SER A 191 ? 0.3773 0.3996 0.2517 0.0388  0.0163  -0.058  191 SER A CB  
1547 O OG  . SER A 191 ? 0.3915 0.407  0.2707 0.039   0.0059  -0.0571 191 SER A OG  
1548 N N   . PHE A 192 ? 0.3759 0.4121 0.2664 0.0249  0.0297  -0.0412 192 PHE A N   
1549 C CA  . PHE A 192 ? 0.3836 0.4205 0.2787 0.0173  0.0315  -0.0331 192 PHE A CA  
1550 C C   . PHE A 192 ? 0.3563 0.4073 0.2758 0.0152  0.0332  -0.0326 192 PHE A C   
1551 O O   . PHE A 192 ? 0.3699 0.4192 0.297  0.0108  0.0299  -0.0279 192 PHE A O   
1552 C CB  . PHE A 192 ? 0.3852 0.4204 0.2633 0.0112  0.0406  -0.0281 192 PHE A CB  
1553 C CG  . PHE A 192 ? 0.4138 0.4314 0.2656 0.0117  0.0379  -0.0246 192 PHE A CG  
1554 C CD1 . PHE A 192 ? 0.418  0.4256 0.261  0.0189  0.0281  -0.028  192 PHE A CD1 
1555 C CD2 . PHE A 192 ? 0.4495 0.4601 0.2857 0.0045  0.0449  -0.0174 192 PHE A CD2 
1556 C CE1 . PHE A 192 ? 0.4865 0.4789 0.3051 0.0203  0.0249  -0.0241 192 PHE A CE1 
1557 C CE2 . PHE A 192 ? 0.5203 0.5127 0.3302 0.0058  0.0426  -0.0131 192 PHE A CE2 
1558 C CZ  . PHE A 192 ? 0.5237 0.5076 0.3245 0.0144  0.0323  -0.0164 192 PHE A CZ  
1559 N N   . GLU A 193 ? 0.3489 0.4132 0.2798 0.0187  0.0381  -0.0373 193 GLU A N   
1560 C CA  . GLU A 193 ? 0.3564 0.4346 0.3104 0.0184  0.0385  -0.0366 193 GLU A CA  
1561 C C   . GLU A 193 ? 0.323  0.3941 0.2871 0.0215  0.0289  -0.0368 193 GLU A C   
1562 O O   . GLU A 193 ? 0.3026 0.377  0.2778 0.0178  0.0263  -0.0325 193 GLU A O   
1563 C CB  . GLU A 193 ? 0.4151 0.5083 0.3801 0.0242  0.0447  -0.042  193 GLU A CB  
1564 C CG  . GLU A 193 ? 0.5224 0.6313 0.4883 0.0193  0.0555  -0.0406 193 GLU A CG  
1565 C CD  . GLU A 193 ? 0.6485 0.7698 0.6163 0.0249  0.0646  -0.0468 193 GLU A CD  
1566 O OE1 . GLU A 193 ? 0.7326 0.8486 0.6971 0.0339  0.0638  -0.0537 193 GLU A OE1 
1567 O OE2 . GLU A 193 ? 0.6794 0.816  0.6511 0.0194  0.0737  -0.0448 193 GLU A OE2 
1568 N N   . THR A 194 ? 0.3164 0.3773 0.276  0.0275  0.0238  -0.0422 194 THR A N   
1569 C CA  . THR A 194 ? 0.3002 0.3538 0.2689 0.0292  0.0157  -0.0424 194 THR A CA  
1570 C C   . THR A 194 ? 0.3286 0.3746 0.2924 0.0235  0.0114  -0.0365 194 THR A C   
1571 O O   . THR A 194 ? 0.3015 0.3473 0.2759 0.0217  0.0081  -0.0335 194 THR A O   
1572 C CB  . THR A 194 ? 0.3457 0.3902 0.3106 0.0349  0.0112  -0.0498 194 THR A CB  
1573 O OG1 . THR A 194 ? 0.3536 0.4038 0.3219 0.0404  0.0161  -0.0555 194 THR A OG1 
1574 C CG2 . THR A 194 ? 0.3548 0.3937 0.3323 0.0359  0.0047  -0.0503 194 THR A CG2 
1575 N N   . ARG A 195 ? 0.3517 0.3897 0.2979 0.0217  0.0113  -0.035  195 ARG A N   
1576 C CA  . ARG A 195 ? 0.3464 0.3758 0.287  0.0176  0.0078  -0.0296 195 ARG A CA  
1577 C C   . ARG A 195 ? 0.2998 0.3347 0.2488 0.011   0.0109  -0.0239 195 ARG A C   
1578 O O   . ARG A 195 ? 0.3039 0.3344 0.2579 0.0088  0.007   -0.0211 195 ARG A O   
1579 C CB  . ARG A 195 ? 0.3436 0.3634 0.2625 0.0165  0.0088  -0.027  195 ARG A CB  
1580 C CG  . ARG A 195 ? 0.381  0.3936 0.2885 0.0227  0.0032  -0.0318 195 ARG A CG  
1581 C CD  . ARG A 195 ? 0.3962 0.3989 0.2804 0.022   0.0045  -0.0277 195 ARG A CD  
1582 N NE  . ARG A 195 ? 0.4025 0.399  0.2734 0.0282  -0.0019 -0.0319 195 ARG A NE  
1583 C CZ  . ARG A 195 ? 0.4201 0.4091 0.2871 0.0315  -0.0105 -0.0313 195 ARG A CZ  
1584 N NH1 . ARG A 195 ? 0.3986 0.3861 0.2777 0.03    -0.0138 -0.0282 195 ARG A NH1 
1585 N NH2 . ARG A 195 ? 0.4742 0.4585 0.3265 0.0369  -0.0165 -0.0346 195 ARG A NH2 
1586 N N   . ILE A 196 ? 0.3169 0.3619 0.267  0.0075  0.018   -0.0227 196 ILE A N   
1587 C CA  . ILE A 196 ? 0.3295 0.3815 0.2865 0       0.021   -0.0181 196 ILE A CA  
1588 C C   . ILE A 196 ? 0.2998 0.3609 0.2758 0.0015  0.0176  -0.0185 196 ILE A C   
1589 O O   . ILE A 196 ? 0.2799 0.3404 0.2598 -0.0035 0.0157  -0.015  196 ILE A O   
1590 C CB  . ILE A 196 ? 0.3725 0.4346 0.3262 -0.0049 0.0299  -0.0172 196 ILE A CB  
1591 C CG1 . ILE A 196 ? 0.4493 0.4978 0.3811 -0.0088 0.0332  -0.0142 196 ILE A CG1 
1592 C CG2 . ILE A 196 ? 0.425  0.5017 0.3927 -0.012  0.0326  -0.0148 196 ILE A CG2 
1593 C CD1 . ILE A 196 ? 0.5437 0.5803 0.4688 -0.016  0.0318  -0.0086 196 ILE A CD1 
1594 N N   . ASN A 197 ? 0.292  0.3591 0.2779 0.0086  0.0166  -0.0228 197 ASN A N   
1595 C CA  . ASN A 197 ? 0.2986 0.3707 0.3    0.0111  0.0128  -0.0224 197 ASN A CA  
1596 C C   . ASN A 197 ? 0.3149 0.3749 0.3154 0.0099  0.0068  -0.0203 197 ASN A C   
1597 O O   . ASN A 197 ? 0.287  0.3496 0.2944 0.007   0.0048  -0.0169 197 ASN A O   
1598 C CB  . ASN A 197 ? 0.3291 0.4052 0.3393 0.0197  0.0128  -0.0272 197 ASN A CB  
1599 C CG  . ASN A 197 ? 0.3619 0.4542 0.3786 0.0218  0.019   -0.029  197 ASN A CG  
1600 O OD1 . ASN A 197 ? 0.3276 0.4325 0.3484 0.0165  0.0224  -0.026  197 ASN A OD1 
1601 N ND2 . ASN A 197 ? 0.3589 0.4518 0.3777 0.0296  0.0208  -0.0345 197 ASN A ND2 
1602 N N   . VAL A 198 ? 0.3115 0.3594 0.3036 0.0122  0.0039  -0.0226 198 VAL A N   
1603 C CA  . VAL A 198 ? 0.3022 0.3405 0.2953 0.0118  -0.0011 -0.0216 198 VAL A CA  
1604 C C   . VAL A 198 ? 0.288  0.3218 0.2739 0.0054  -0.0007 -0.0168 198 VAL A C   
1605 O O   . VAL A 198 ? 0.2631 0.2947 0.2537 0.0031  -0.0027 -0.0143 198 VAL A O   
1606 C CB  . VAL A 198 ? 0.3217 0.3517 0.3106 0.0163  -0.0048 -0.0264 198 VAL A CB  
1607 C CG1 . VAL A 198 ? 0.3463 0.3696 0.3399 0.0157  -0.0093 -0.0257 198 VAL A CG1 
1608 C CG2 . VAL A 198 ? 0.3194 0.3523 0.3149 0.0217  -0.0047 -0.0318 198 VAL A CG2 
1609 N N   . LEU A 199 ? 0.2747 0.3058 0.2481 0.0026  0.0025  -0.0154 199 LEU A N   
1610 C CA  . LEU A 199 ? 0.2977 0.3225 0.2633 -0.004  0.0038  -0.0109 199 LEU A CA  
1611 C C   . LEU A 199 ? 0.2874 0.3213 0.2616 -0.01   0.0056  -0.0085 199 LEU A C   
1612 O O   . LEU A 199 ? 0.3053 0.3341 0.2791 -0.0138 0.0041  -0.0063 199 LEU A O   
1613 C CB  . LEU A 199 ? 0.2956 0.3142 0.2452 -0.0065 0.0078  -0.0092 199 LEU A CB  
1614 C CG  . LEU A 199 ? 0.3087 0.3144 0.2454 -0.0013 0.0045  -0.0099 199 LEU A CG  
1615 C CD1 . LEU A 199 ? 0.3412 0.3427 0.2615 -0.002  0.0087  -0.0087 199 LEU A CD1 
1616 C CD2 . LEU A 199 ? 0.3482 0.342  0.2809 -0.0021 0.0014  -0.0072 199 LEU A CD2 
1617 N N   . LEU A 200 ? 0.2849 0.3332 0.2669 -0.0106 0.0086  -0.0093 200 LEU A N   
1618 C CA  . LEU A 200 ? 0.3001 0.3603 0.2913 -0.016  0.0093  -0.0074 200 LEU A CA  
1619 C C   . LEU A 200 ? 0.2746 0.335  0.2748 -0.0131 0.0042  -0.0069 200 LEU A C   
1620 O O   . LEU A 200 ? 0.2736 0.336  0.2755 -0.0183 0.0027  -0.0046 200 LEU A O   
1621 C CB  . LEU A 200 ? 0.3201 0.398  0.3193 -0.0161 0.0137  -0.0088 200 LEU A CB  
1622 C CG  . LEU A 200 ? 0.3501 0.4435 0.3586 -0.0231 0.0145  -0.0072 200 LEU A CG  
1623 C CD1 . LEU A 200 ? 0.333  0.4209 0.3325 -0.0344 0.0167  -0.0048 200 LEU A CD1 
1624 C CD2 . LEU A 200 ? 0.369  0.4821 0.3879 -0.0214 0.0191  -0.0092 200 LEU A CD2 
1625 N N   . SER A 201 ? 0.2696 0.3275 0.275  -0.0054 0.0016  -0.009  201 SER A N   
1626 C CA  . SER A 201 ? 0.2578 0.3132 0.27   -0.003  -0.0024 -0.0079 201 SER A CA  
1627 C C   . SER A 201 ? 0.2605 0.3047 0.2657 -0.0074 -0.0039 -0.0059 201 SER A C   
1628 O O   . SER A 201 ? 0.281  0.3264 0.2886 -0.0099 -0.0055 -0.0036 201 SER A O   
1629 C CB  . SER A 201 ? 0.2676 0.3184 0.2847 0.0046  -0.0041 -0.0109 201 SER A CB  
1630 O OG  . SER A 201 ? 0.2929 0.3391 0.3153 0.0061  -0.007  -0.0093 201 SER A OG  
1631 N N   . ASN A 202 ? 0.2469 0.2804 0.2431 -0.0076 -0.0034 -0.0069 202 ASN A N   
1632 C CA  . ASN A 202 ? 0.2484 0.271  0.2377 -0.0106 -0.004  -0.0055 202 ASN A CA  
1633 C C   . ASN A 202 ? 0.2553 0.278  0.2386 -0.0186 -0.002  -0.0031 202 ASN A C   
1634 O O   . ASN A 202 ? 0.264  0.2815 0.2452 -0.0215 -0.0028 -0.002  202 ASN A O   
1635 C CB  . ASN A 202 ? 0.2554 0.2676 0.2367 -0.0076 -0.0045 -0.0071 202 ASN A CB  
1636 C CG  . ASN A 202 ? 0.2622 0.2727 0.2506 -0.0017 -0.0076 -0.0099 202 ASN A CG  
1637 O OD1 . ASN A 202 ? 0.3009 0.3067 0.2919 -0.0013 -0.0088 -0.0099 202 ASN A OD1 
1638 N ND2 . ASN A 202 ? 0.3094 0.3239 0.3012 0.0026  -0.0085 -0.013  202 ASN A ND2 
1639 N N   . ILE A 203 ? 0.264  0.2922 0.2439 -0.0226 0.001   -0.0028 203 ILE A N   
1640 C CA  . ILE A 203 ? 0.2868 0.3155 0.2617 -0.0318 0.0032  -0.0012 203 ILE A CA  
1641 C C   . ILE A 203 ? 0.3001 0.3392 0.2834 -0.0345 0.0005  -0.0006 203 ILE A C   
1642 O O   . ILE A 203 ? 0.2695 0.3029 0.2474 -0.0401 -0.0001 0       203 ILE A O   
1643 C CB  . ILE A 203 ? 0.2769 0.3112 0.2485 -0.0365 0.0078  -0.001  203 ILE A CB  
1644 C CG1 . ILE A 203 ? 0.2956 0.3147 0.2533 -0.0351 0.0103  -0.0004 203 ILE A CG1 
1645 C CG2 . ILE A 203 ? 0.2775 0.3185 0.2494 -0.0472 0.0097  -0.0003 203 ILE A CG2 
1646 C CD1 . ILE A 203 ? 0.3131 0.3376 0.2667 -0.0378 0.0155  -0.0002 203 ILE A CD1 
1647 N N   . TYR A 204 ? 0.2591 0.3122 0.2545 -0.0296 -0.0013 -0.0008 204 TYR A N   
1648 C CA  . TYR A 204 ? 0.2646 0.3282 0.2673 -0.0306 -0.0048 0.0005  204 TYR A CA  
1649 C C   . TYR A 204 ? 0.2612 0.3144 0.2611 -0.0283 -0.0075 0.0017  204 TYR A C   
1650 O O   . TYR A 204 ? 0.2701 0.3261 0.2685 -0.0323 -0.0098 0.003   204 TYR A O   
1651 C CB  . TYR A 204 ? 0.2793 0.3597 0.2951 -0.0249 -0.0057 0.0003  204 TYR A CB  
1652 C CG  . TYR A 204 ? 0.3188 0.415  0.3396 -0.0292 -0.0027 -0.0008 204 TYR A CG  
1653 C CD1 . TYR A 204 ? 0.3505 0.4538 0.3699 -0.0395 -0.0023 -0.0006 204 TYR A CD1 
1654 C CD2 . TYR A 204 ? 0.2873 0.3917 0.3145 -0.0236 0.0004  -0.0027 204 TYR A CD2 
1655 C CE1 . TYR A 204 ? 0.3619 0.4812 0.3876 -0.0446 0.0013  -0.0018 204 TYR A CE1 
1656 C CE2 . TYR A 204 ? 0.349  0.4698 0.3821 -0.0276 0.0043  -0.0038 204 TYR A CE2 
1657 C CZ  . TYR A 204 ? 0.4064 0.5353 0.4396 -0.0383 0.0048  -0.0032 204 TYR A CZ  
1658 O OH  . TYR A 204 ? 0.4194 0.5657 0.4599 -0.0433 0.0092  -0.0046 204 TYR A OH  
1659 N N   . LEU A 205 ? 0.2604 0.3032 0.2597 -0.0223 -0.0073 0.0009  205 LEU A N   
1660 C CA  . LEU A 205 ? 0.3034 0.3366 0.3009 -0.0206 -0.0085 0.0018  205 LEU A CA  
1661 C C   . LEU A 205 ? 0.2738 0.2981 0.2607 -0.0271 -0.0073 0.0019  205 LEU A C   
1662 O O   . LEU A 205 ? 0.2865 0.3099 0.2707 -0.0294 -0.0084 0.0032  205 LEU A O   
1663 C CB  . LEU A 205 ? 0.2769 0.302  0.2765 -0.0148 -0.0079 -0.0001 205 LEU A CB  
1664 C CG  . LEU A 205 ? 0.3161 0.3316 0.3148 -0.0137 -0.0076 -0.0001 205 LEU A CG  
1665 C CD1 . LEU A 205 ? 0.337  0.3548 0.3417 -0.0115 -0.0088 0.0021  205 LEU A CD1 
1666 C CD2 . LEU A 205 ? 0.3697 0.3789 0.3701 -0.0099 -0.0072 -0.003  205 LEU A CD2 
1667 N N   . ASN A 206 ? 0.2668 0.284  0.2464 -0.0298 -0.0049 0.0005  206 ASN A N   
1668 C CA  . ASN A 206 ? 0.2955 0.3006 0.264  -0.0349 -0.0031 0       206 ASN A CA  
1669 C C   . ASN A 206 ? 0.3235 0.3336 0.2879 -0.0437 -0.0035 0.0002  206 ASN A C   
1670 O O   . ASN A 206 ? 0.3384 0.3389 0.2936 -0.0483 -0.0027 -0.0006 206 ASN A O   
1671 C CB  . ASN A 206 ? 0.3035 0.297  0.2648 -0.0334 -0.0007 -0.0009 206 ASN A CB  
1672 C CG  . ASN A 206 ? 0.3353 0.3248 0.3007 -0.025  -0.0016 -0.0019 206 ASN A CG  
1673 O OD1 . ASN A 206 ? 0.3261 0.3163 0.2975 -0.0218 -0.0026 -0.0023 206 ASN A OD1 
1674 N ND2 . ASN A 206 ? 0.3274 0.3124 0.289  -0.0218 -0.0012 -0.0023 206 ASN A ND2 
1675 N N   . GLU A 207 ? 0.3153 0.3406 0.2865 -0.0463 -0.0046 0.0007  207 GLU A N   
1676 C CA  A GLU A 207 ? 0.3046 0.3395 0.2754 -0.0548 -0.0063 0.0004  207 GLU A CA  
1677 C CA  B GLU A 207 ? 0.3101 0.345  0.2809 -0.0548 -0.0063 0.0004  207 GLU A CA  
1678 C C   . GLU A 207 ? 0.2895 0.334  0.2653 -0.0524 -0.0111 0.0019  207 GLU A C   
1679 O O   . GLU A 207 ? 0.3037 0.3583 0.2798 -0.0583 -0.014  0.0016  207 GLU A O   
1680 C CB  A GLU A 207 ? 0.3031 0.3531 0.281  -0.0589 -0.0052 0       207 GLU A CB  
1681 C CB  B GLU A 207 ? 0.3156 0.3658 0.2937 -0.0587 -0.0052 0       207 GLU A CB  
1682 C CG  A GLU A 207 ? 0.3395 0.3796 0.3094 -0.0639 0.0002  -0.0008 207 GLU A CG  
1683 C CG  B GLU A 207 ? 0.3681 0.4083 0.3373 -0.0655 0       -0.001  207 GLU A CG  
1684 C CD  A GLU A 207 ? 0.3707 0.4262 0.348  -0.0676 0.0029  -0.0011 207 GLU A CD  
1685 C CD  B GLU A 207 ? 0.4081 0.4375 0.3658 -0.0759 0.0008  -0.0025 207 GLU A CD  
1686 O OE1 A GLU A 207 ? 0.3634 0.4384 0.3542 -0.0639 0.0003  -0.001  207 GLU A OE1 
1687 O OE1 B GLU A 207 ? 0.4545 0.4651 0.4014 -0.0743 0.0016  -0.0029 207 GLU A OE1 
1688 O OE2 A GLU A 207 ? 0.3709 0.4193 0.3404 -0.0746 0.0079  -0.0013 207 GLU A OE2 
1689 O OE2 B GLU A 207 ? 0.4822 0.5228 0.4425 -0.0856 0.0005  -0.0039 207 GLU A OE2 
1690 N N   . ASN A 208 ? 0.2968 0.3375 0.2757 -0.0441 -0.012  0.0036  208 ASN A N   
1691 C CA  . ASN A 208 ? 0.3204 0.3677 0.3018 -0.0414 -0.0162 0.0061  208 ASN A CA  
1692 C C   . ASN A 208 ? 0.3257 0.3929 0.3185 -0.0393 -0.0202 0.0076  208 ASN A C   
1693 O O   . ASN A 208 ? 0.2885 0.3647 0.2814 -0.04   -0.025  0.0094  208 ASN A O   
1694 C CB  . ASN A 208 ? 0.373  0.4141 0.3425 -0.0474 -0.0174 0.0058  208 ASN A CB  
1695 C CG  . ASN A 208 ? 0.3898 0.4318 0.3579 -0.0432 -0.0205 0.0092  208 ASN A CG  
1696 O OD1 . ASN A 208 ? 0.3495 0.3884 0.3228 -0.0358 -0.0198 0.0116  208 ASN A OD1 
1697 N ND2 . ASN A 208 ? 0.3912 0.4367 0.3513 -0.048  -0.0242 0.0096  208 ASN A ND2 
1698 N N   . ASN A 209 ? 0.2933 0.3683 0.2953 -0.0364 -0.0183 0.0065  209 ASN A N   
1699 C CA  A ASN A 209 ? 0.279  0.3729 0.2939 -0.0318 -0.0211 0.0075  209 ASN A CA  
1700 C CA  B ASN A 209 ? 0.2867 0.3806 0.3017 -0.032  -0.0208 0.0073  209 ASN A CA  
1701 C C   . ASN A 209 ? 0.2845 0.3736 0.3053 -0.0211 -0.0205 0.0087  209 ASN A C   
1702 O O   . ASN A 209 ? 0.2781 0.3665 0.3031 -0.0176 -0.0172 0.0066  209 ASN A O   
1703 C CB  A ASN A 209 ? 0.2898 0.3977 0.3119 -0.0356 -0.0186 0.0051  209 ASN A CB  
1704 C CB  B ASN A 209 ? 0.3123 0.4168 0.3319 -0.0372 -0.0174 0.0046  209 ASN A CB  
1705 C CG  A ASN A 209 ? 0.2814 0.4119 0.3184 -0.0306 -0.0219 0.0058  209 ASN A CG  
1706 C CG  B ASN A 209 ? 0.3374 0.4477 0.3527 -0.0493 -0.0179 0.003   209 ASN A CG  
1707 O OD1 A ASN A 209 ? 0.2318 0.365  0.2747 -0.021  -0.0253 0.0083  209 ASN A OD1 
1708 O OD1 B ASN A 209 ? 0.325  0.4398 0.338  -0.0527 -0.0228 0.0037  209 ASN A OD1 
1709 N ND2 A ASN A 209 ? 0.312  0.4589 0.3555 -0.0372 -0.0204 0.0036  209 ASN A ND2 
1710 N ND2 B ASN A 209 ? 0.3499 0.4596 0.3631 -0.0566 -0.0129 0.0008  209 ASN A ND2 
1711 N N   . LEU A 210 ? 0.2699 0.3534 0.289  -0.0167 -0.0234 0.0119  210 LEU A N   
1712 C CA  . LEU A 210 ? 0.3121 0.3849 0.3337 -0.0087 -0.0221 0.0128  210 LEU A CA  
1713 C C   . LEU A 210 ? 0.3168 0.3995 0.3503 -0.0001 -0.0231 0.0129  210 LEU A C   
1714 O O   . LEU A 210 ? 0.2988 0.3741 0.3354 0.0048  -0.0204 0.011   210 LEU A O   
1715 C CB  . LEU A 210 ? 0.3164 0.3787 0.3306 -0.0082 -0.0237 0.0166  210 LEU A CB  
1716 C CG  . LEU A 210 ? 0.359  0.4101 0.3614 -0.0156 -0.0214 0.0155  210 LEU A CG  
1717 C CD1 . LEU A 210 ? 0.3955 0.4361 0.391  -0.0143 -0.0215 0.0192  210 LEU A CD1 
1718 C CD2 . LEU A 210 ? 0.3619 0.404  0.3633 -0.0172 -0.0168 0.0115  210 LEU A CD2 
1719 N N   . GLU A 211 ? 0.3123 0.4125 0.3528 0.0014  -0.0267 0.0143  211 GLU A N   
1720 C CA  . GLU A 211 ? 0.3302 0.4421 0.3832 0.0104  -0.0273 0.014   211 GLU A CA  
1721 C C   . GLU A 211 ? 0.3084 0.4243 0.3658 0.0098  -0.0219 0.009   211 GLU A C   
1722 O O   . GLU A 211 ? 0.265  0.3771 0.3271 0.0174  -0.0198 0.0072  211 GLU A O   
1723 C CB  . GLU A 211 ? 0.4123 0.545  0.4734 0.0129  -0.0328 0.0164  211 GLU A CB  
1724 C CG  . GLU A 211 ? 0.5757 0.7037 0.6307 0.0157  -0.0389 0.0222  211 GLU A CG  
1725 C CD  . GLU A 211 ? 0.831  0.9549 0.8732 0.0054  -0.041  0.0232  211 GLU A CD  
1726 O OE1 . GLU A 211 ? 0.6801 0.8002 0.7164 -0.0047 -0.0373 0.0195  211 GLU A OE1 
1727 O OE2 . GLU A 211 ? 0.8536 0.9765 0.8904 0.0084  -0.0464 0.0281  211 GLU A OE2 
1728 N N   . LEU A 212 ? 0.2663 0.3882 0.3209 0.0007  -0.0195 0.0066  212 LEU A N   
1729 C CA  . LEU A 212 ? 0.2888 0.4136 0.3449 -0.0005 -0.0139 0.0026  212 LEU A CA  
1730 C C   . LEU A 212 ? 0.2485 0.3534 0.2955 0.0004  -0.0109 0.0008  212 LEU A C   
1731 O O   . LEU A 212 ? 0.2429 0.3472 0.2911 0.004   -0.0074 -0.0025 212 LEU A O   
1732 C CB  . LEU A 212 ? 0.3089 0.4446 0.3637 -0.0111 -0.0117 0.0014  212 LEU A CB  
1733 C CG  . LEU A 212 ? 0.3558 0.517  0.4235 -0.0125 -0.0136 0.0014  212 LEU A CG  
1734 C CD1 . LEU A 212 ? 0.398  0.5671 0.4633 -0.0255 -0.0102 -0.0004 212 LEU A CD1 
1735 C CD2 . LEU A 212 ? 0.409  0.5846 0.4902 -0.0028 -0.0112 -0.0005 212 LEU A CD2 
1736 N N   . CYS A 213 ? 0.2607 0.3502 0.2984 -0.003  -0.0123 0.0022  213 CYS A N   
1737 C CA  . CYS A 213 ? 0.2963 0.3692 0.3284 -0.001  -0.0107 0.0004  213 CYS A CA  
1738 C C   . CYS A 213 ? 0.2964 0.3664 0.3352 0.0081  -0.0109 -0.001  213 CYS A C   
1739 O O   . CYS A 213 ? 0.2768 0.3425 0.3149 0.011   -0.0088 -0.0049 213 CYS A O   
1740 C CB  . CYS A 213 ? 0.3047 0.3648 0.3295 -0.0043 -0.0121 0.0025  213 CYS A CB  
1741 S SG  . CYS A 213 ? 0.3027 0.3467 0.3258 -0.0007 -0.0111 0.0002  213 CYS A SG  
1742 N N   . ARG A 214 ? 0.258  0.329  0.3019 0.0126  -0.0137 0.002   214 ARG A N   
1743 C CA  . ARG A 214 ? 0.2875 0.3525 0.3369 0.021   -0.0139 0.001   214 ARG A CA  
1744 C C   . ARG A 214 ? 0.2774 0.3529 0.3339 0.0268  -0.0118 -0.0026 214 ARG A C   
1745 O O   . ARG A 214 ? 0.2858 0.3539 0.343  0.0314  -0.0098 -0.0068 214 ARG A O   
1746 C CB  . ARG A 214 ? 0.3182 0.3804 0.3694 0.0247  -0.0172 0.0064  214 ARG A CB  
1747 C CG  . ARG A 214 ? 0.3193 0.367  0.3631 0.0204  -0.0176 0.0092  214 ARG A CG  
1748 C CD  . ARG A 214 ? 0.3145 0.3621 0.3573 0.0236  -0.0211 0.0157  214 ARG A CD  
1749 N NE  . ARG A 214 ? 0.3942 0.4353 0.4277 0.016   -0.0207 0.0177  214 ARG A NE  
1750 C CZ  . ARG A 214 ? 0.3953 0.4374 0.4225 0.0137  -0.0232 0.0222  214 ARG A CZ  
1751 N NH1 . ARG A 214 ? 0.3444 0.3971 0.3737 0.0179  -0.0278 0.026   214 ARG A NH1 
1752 N NH2 . ARG A 214 ? 0.4477 0.4802 0.4664 0.0074  -0.021  0.0224  214 ARG A NH2 
1753 N N   . GLU A 215 ? 0.2673 0.361  0.329  0.0259  -0.0117 -0.0018 215 GLU A N   
1754 C CA  . GLU A 215 ? 0.2388 0.3455 0.3082 0.031   -0.0085 -0.0053 215 GLU A CA  
1755 C C   . GLU A 215 ? 0.2558 0.356  0.319  0.0299  -0.0039 -0.0107 215 GLU A C   
1756 O O   . GLU A 215 ? 0.2517 0.3519 0.3183 0.037   -0.0014 -0.0148 215 GLU A O   
1757 C CB  . GLU A 215 ? 0.2408 0.3702 0.317  0.027   -0.0083 -0.0041 215 GLU A CB  
1758 C CG  . GLU A 215 ? 0.2651 0.4102 0.3499 0.0313  -0.0033 -0.0083 215 GLU A CG  
1759 C CD  . GLU A 215 ? 0.2592 0.4098 0.3553 0.0441  -0.0043 -0.009  215 GLU A CD  
1760 O OE1 . GLU A 215 ? 0.2726 0.4195 0.3715 0.049   -0.0098 -0.0047 215 GLU A OE1 
1761 O OE2 . GLU A 215 ? 0.2666 0.4254 0.3681 0.0491  0.0007  -0.0134 215 GLU A OE2 
1762 N N   . TYR A 216 ? 0.2466 0.3427 0.3003 0.0214  -0.0026 -0.0107 216 TYR A N   
1763 C CA  . TYR A 216 ? 0.2587 0.3505 0.3045 0.02    0.0014  -0.0148 216 TYR A CA  
1764 C C   . TYR A 216 ? 0.2507 0.3254 0.2911 0.0235  -0.0001 -0.018  216 TYR A C   
1765 O O   . TYR A 216 ? 0.2505 0.3229 0.2876 0.027   0.0022  -0.0228 216 TYR A O   
1766 C CB  . TYR A 216 ? 0.2743 0.3679 0.3117 0.0104  0.0034  -0.0131 216 TYR A CB  
1767 C CG  . TYR A 216 ? 0.2789 0.3918 0.3228 0.0072  0.0071  -0.0127 216 TYR A CG  
1768 C CD1 . TYR A 216 ? 0.2786 0.3996 0.323  0.0093  0.0128  -0.0161 216 TYR A CD1 
1769 C CD2 . TYR A 216 ? 0.2693 0.3935 0.3191 0.0018  0.0049  -0.0094 216 TYR A CD2 
1770 C CE1 . TYR A 216 ? 0.2989 0.4397 0.3513 0.0061  0.0171  -0.0162 216 TYR A CE1 
1771 C CE2 . TYR A 216 ? 0.3166 0.461  0.3749 -0.0017 0.008   -0.0097 216 TYR A CE2 
1772 C CZ  . TYR A 216 ? 0.3258 0.4791 0.3861 0.0002  0.0145  -0.013  216 TYR A CZ  
1773 O OH  . TYR A 216 ? 0.3593 0.5344 0.4296 -0.004  0.0183  -0.0136 216 TYR A OH  
1774 N N   . ALA A 217 ? 0.2366 0.3005 0.2768 0.0226  -0.0038 -0.0159 217 ALA A N   
1775 C CA  . ALA A 217 ? 0.2639 0.3138 0.302  0.0252  -0.0053 -0.0193 217 ALA A CA  
1776 C C   . ALA A 217 ? 0.2863 0.334  0.3311 0.0331  -0.0049 -0.0227 217 ALA A C   
1777 O O   . ALA A 217 ? 0.2583 0.2994 0.3006 0.0359  -0.0043 -0.0286 217 ALA A O   
1778 C CB  . ALA A 217 ? 0.2523 0.2933 0.29   0.0216  -0.0081 -0.0161 217 ALA A CB  
1779 N N   . GLN A 218 ? 0.242  0.2946 0.2947 0.037   -0.0055 -0.0192 218 GLN A N   
1780 C CA  . GLN A 218 ? 0.2621 0.3112 0.3211 0.0457  -0.0049 -0.0217 218 GLN A CA  
1781 C C   . GLN A 218 ? 0.2868 0.3445 0.3466 0.0505  -0.0009 -0.0273 218 GLN A C   
1782 O O   . GLN A 218 ? 0.3147 0.3644 0.3748 0.0564  0.0004  -0.0329 218 GLN A O   
1783 C CB  . GLN A 218 ? 0.2752 0.3277 0.3415 0.0502  -0.007  -0.0157 218 GLN A CB  
1784 C CG  . GLN A 218 ? 0.3252 0.3649 0.3887 0.0465  -0.0099 -0.0108 218 GLN A CG  
1785 C CD  . GLN A 218 ? 0.4118 0.4561 0.4785 0.0493  -0.0128 -0.0034 218 GLN A CD  
1786 O OE1 . GLN A 218 ? 0.4733 0.5345 0.5441 0.0505  -0.0139 -0.0011 218 GLN A OE1 
1787 N NE2 . GLN A 218 ? 0.5155 0.5447 0.5807 0.0513  -0.014  0.0001  218 GLN A NE2 
1788 N N   . LYS A 219 ? 0.2535 0.3268 0.3129 0.0474  0.0016  -0.0264 219 LYS A N   
1789 C CA  . LYS A 219 ? 0.2595 0.3418 0.3179 0.0503  0.0067  -0.0315 219 LYS A CA  
1790 C C   . LYS A 219 ? 0.2994 0.3696 0.346  0.0492  0.0078  -0.0376 219 LYS A C   
1791 O O   . LYS A 219 ? 0.3307 0.3994 0.3762 0.0553  0.0108  -0.0439 219 LYS A O   
1792 C CB  . LYS A 219 ? 0.2459 0.3461 0.3049 0.0446  0.0099  -0.0289 219 LYS A CB  
1793 C CG  . LYS A 219 ? 0.2491 0.3626 0.3098 0.0479  0.0167  -0.0334 219 LYS A CG  
1794 C CD  . LYS A 219 ? 0.2728 0.4055 0.3364 0.0407  0.0206  -0.0306 219 LYS A CD  
1795 C CE  . LYS A 219 ? 0.2735 0.4195 0.3501 0.0398  0.0167  -0.0254 219 LYS A CE  
1796 N NZ  . LYS A 219 ? 0.2743 0.4273 0.3648 0.0514  0.0151  -0.0261 219 LYS A NZ  
1797 N N   . ALA A 220 ? 0.2878 0.3506 0.3254 0.0421  0.0053  -0.0361 220 ALA A N   
1798 C CA  . ALA A 220 ? 0.3021 0.3544 0.3284 0.0412  0.0045  -0.0414 220 ALA A CA  
1799 C C   . ALA A 220 ? 0.3153 0.3552 0.3444 0.0461  0.0021  -0.047  220 ALA A C   
1800 O O   . ALA A 220 ? 0.3365 0.3726 0.3603 0.0498  0.0035  -0.0541 220 ALA A O   
1801 C CB  . ALA A 220 ? 0.3121 0.3594 0.3311 0.0341  0.0013  -0.0379 220 ALA A CB  
1802 N N   . ILE A 221 ? 0.3137 0.3471 0.3511 0.0462  -0.0009 -0.0438 221 ILE A N   
1803 C CA  . ILE A 221 ? 0.3267 0.3462 0.367  0.049   -0.0028 -0.0484 221 ILE A CA  
1804 C C   . ILE A 221 ? 0.407  0.4254 0.4502 0.0576  0.0006  -0.0536 221 ILE A C   
1805 O O   . ILE A 221 ? 0.3758 0.3835 0.4158 0.0597  0.0004  -0.0612 221 ILE A O   
1806 C CB  . ILE A 221 ? 0.3369 0.3493 0.3844 0.047   -0.0053 -0.0426 221 ILE A CB  
1807 C CG1 . ILE A 221 ? 0.3148 0.3256 0.3596 0.0391  -0.0081 -0.0395 221 ILE A CG1 
1808 C CG2 . ILE A 221 ? 0.3729 0.37   0.4246 0.0508  -0.0055 -0.0465 221 ILE A CG2 
1809 C CD1 . ILE A 221 ? 0.3497 0.3578 0.3993 0.0364  -0.0091 -0.0321 221 ILE A CD1 
1810 N N   . SER A 222 ? 0.3426 0.3724 0.3926 0.0626  0.0036  -0.05   222 SER A N   
1811 C CA  . SER A 222 ? 0.3324 0.3626 0.3873 0.0724  0.0071  -0.0541 222 SER A CA  
1812 C C   . SER A 222 ? 0.3846 0.4132 0.4306 0.0747  0.0107  -0.0637 222 SER A C   
1813 O O   . SER A 222 ? 0.4231 0.4413 0.4696 0.0813  0.0123  -0.0703 222 SER A O   
1814 C CB  . SER A 222 ? 0.31   0.3582 0.3741 0.0769  0.0096  -0.0492 222 SER A CB  
1815 O OG  . SER A 222 ? 0.3958 0.442  0.4668 0.0881  0.0121  -0.0523 222 SER A OG  
1816 N N   . SER A 223 ? 0.3643 0.4021 0.4013 0.0698  0.0124  -0.0645 223 SER A N   
1817 C CA  . SER A 223 ? 0.4222 0.4598 0.4491 0.0727  0.0165  -0.073  223 SER A CA  
1818 C C   . SER A 223 ? 0.476  0.5047 0.488  0.0671  0.013   -0.0775 223 SER A C   
1819 O O   . SER A 223 ? 0.499  0.5278 0.5    0.0694  0.0163  -0.0842 223 SER A O   
1820 C CB  . SER A 223 ? 0.4107 0.4669 0.4374 0.0736  0.0231  -0.0712 223 SER A CB  
1821 O OG  . SER A 223 ? 0.4446 0.5065 0.4669 0.0646  0.0211  -0.0645 223 SER A OG  
1822 N N   . THR A 224 ? 0.3672 0.3897 0.3784 0.0605  0.0068  -0.0741 224 THR A N   
1823 C CA  . THR A 224 ? 0.3862 0.4025 0.3845 0.0564  0.0027  -0.0783 224 THR A CA  
1824 C C   . THR A 224 ? 0.4442 0.4463 0.4441 0.0569  -0.0019 -0.0861 224 THR A C   
1825 O O   . THR A 224 ? 0.4204 0.4151 0.4317 0.0576  -0.0029 -0.0852 224 THR A O   
1826 C CB  . THR A 224 ? 0.4098 0.429  0.4067 0.0495  -0.0012 -0.0708 224 THR A CB  
1827 O OG1 . THR A 224 ? 0.426  0.442  0.4087 0.0475  -0.0046 -0.0744 224 THR A OG1 
1828 C CG2 . THR A 224 ? 0.4033 0.4161 0.4111 0.0463  -0.006  -0.0677 224 THR A CG2 
1829 N N   . ASP A 225 ? 0.5015 0.4994 0.4891 0.0558  -0.0051 -0.0934 225 ASP A N   
1830 C CA  . ASP A 225 ? 0.5462 0.5327 0.5347 0.0535  -0.0111 -0.1011 225 ASP A CA  
1831 C C   . ASP A 225 ? 0.5122 0.5011 0.495  0.0481  -0.0184 -0.1005 225 ASP A C   
1832 O O   . ASP A 225 ? 0.5084 0.4916 0.4886 0.0462  -0.024  -0.1087 225 ASP A O   
1833 C CB  . ASP A 225 ? 0.6163 0.5955 0.5955 0.058   -0.0095 -0.1129 225 ASP A CB  
1834 C CG  . ASP A 225 ? 0.7188 0.6932 0.7054 0.0648  -0.0028 -0.1148 225 ASP A CG  
1835 O OD1 . ASP A 225 ? 0.6345 0.601  0.6342 0.0645  -0.0033 -0.1123 225 ASP A OD1 
1836 O OD2 . ASP A 225 ? 0.8115 0.7901 0.7906 0.0707  0.0033  -0.1183 225 ASP A OD2 
1837 N N   . THR A 226 ? 0.3991 0.3963 0.379  0.046   -0.0183 -0.0917 226 THR A N   
1838 C CA  . THR A 226 ? 0.4391 0.4384 0.412  0.0429  -0.0248 -0.0905 226 THR A CA  
1839 C C   . THR A 226 ? 0.4009 0.4001 0.3887 0.0384  -0.0281 -0.0857 226 THR A C   
1840 O O   . THR A 226 ? 0.3632 0.3654 0.3578 0.0373  -0.0243 -0.0774 226 THR A O   
1841 C CB  . THR A 226 ? 0.4133 0.4187 0.3731 0.0434  -0.0218 -0.0836 226 THR A CB  
1842 O OG1 . THR A 226 ? 0.5087 0.5139 0.4558 0.0473  -0.0175 -0.0891 226 THR A OG1 
1843 C CG2 . THR A 226 ? 0.4099 0.4158 0.3603 0.0419  -0.0282 -0.0813 226 THR A CG2 
1844 N N   . GLN A 227 ? 0.3809 0.3782 0.3731 0.0357  -0.0349 -0.0909 227 GLN A N   
1845 C CA  . GLN A 227 ? 0.3796 0.3776 0.3866 0.0311  -0.0373 -0.0874 227 GLN A CA  
1846 C C   . GLN A 227 ? 0.3364 0.3399 0.3429 0.0303  -0.0357 -0.0771 227 GLN A C   
1847 O O   . GLN A 227 ? 0.3164 0.3195 0.3335 0.0277  -0.0329 -0.0714 227 GLN A O   
1848 C CB  . GLN A 227 ? 0.392  0.3921 0.4021 0.0286  -0.0455 -0.0945 227 GLN A CB  
1849 C CG  . GLN A 227 ? 0.3772 0.3799 0.4039 0.0235  -0.0473 -0.092  227 GLN A CG  
1850 C CD  . GLN A 227 ? 0.4158 0.4234 0.4485 0.0208  -0.0555 -0.1005 227 GLN A CD  
1851 O OE1 . GLN A 227 ? 0.397  0.4096 0.4193 0.0237  -0.0618 -0.1043 227 GLN A OE1 
1852 N NE2 . GLN A 227 ? 0.3975 0.4047 0.447  0.0149  -0.0556 -0.1031 227 GLN A NE2 
1853 N N   . ARG A 228 ? 0.3053 0.3122 0.2985 0.0323  -0.0377 -0.0749 228 ARG A N   
1854 C CA  . ARG A 228 ? 0.3203 0.3298 0.3114 0.0313  -0.0365 -0.0659 228 ARG A CA  
1855 C C   . ARG A 228 ? 0.3113 0.3212 0.3063 0.0298  -0.0292 -0.0588 228 ARG A C   
1856 O O   . ARG A 228 ? 0.2962 0.3069 0.2976 0.0271  -0.0281 -0.0529 228 ARG A O   
1857 C CB  . ARG A 228 ? 0.3261 0.3358 0.2991 0.0343  -0.0391 -0.065  228 ARG A CB  
1858 C CG  . ARG A 228 ? 0.3747 0.3839 0.3423 0.0335  -0.0372 -0.0559 228 ARG A CG  
1859 C CD  . ARG A 228 ? 0.3957 0.4044 0.3559 0.0321  -0.0294 -0.0501 228 ARG A CD  
1860 N NE  . ARG A 228 ? 0.3848 0.3907 0.3366 0.0304  -0.0271 -0.0422 228 ARG A NE  
1861 C CZ  . ARG A 228 ? 0.4358 0.4367 0.3711 0.0325  -0.0291 -0.0396 228 ARG A CZ  
1862 N NH1 . ARG A 228 ? 0.4633 0.4626 0.3861 0.0366  -0.0332 -0.0438 228 ARG A NH1 
1863 N NH2 . ARG A 228 ? 0.4351 0.431  0.3645 0.0304  -0.0266 -0.0326 228 ARG A NH2 
1864 N N   . PHE A 229 ? 0.3441 0.3547 0.335  0.0319  -0.0244 -0.0596 229 PHE A N   
1865 C CA  . PHE A 229 ? 0.3337 0.3479 0.3287 0.0311  -0.0183 -0.0535 229 PHE A CA  
1866 C C   . PHE A 229 ? 0.3224 0.3344 0.3322 0.0304  -0.0177 -0.0528 229 PHE A C   
1867 O O   . PHE A 229 ? 0.3037 0.3182 0.3188 0.0283  -0.0155 -0.0464 229 PHE A O   
1868 C CB  . PHE A 229 ? 0.3591 0.3772 0.3464 0.034   -0.0131 -0.0549 229 PHE A CB  
1869 C CG  . PHE A 229 ? 0.3472 0.3662 0.3177 0.0337  -0.0122 -0.0535 229 PHE A CG  
1870 C CD1 . PHE A 229 ? 0.3804 0.3989 0.3455 0.0301  -0.0125 -0.0466 229 PHE A CD1 
1871 C CD2 . PHE A 229 ? 0.3991 0.4171 0.3574 0.037   -0.0114 -0.0593 229 PHE A CD2 
1872 C CE1 . PHE A 229 ? 0.3678 0.3839 0.3156 0.03    -0.0116 -0.0447 229 PHE A CE1 
1873 C CE2 . PHE A 229 ? 0.4074 0.4244 0.348  0.0367  -0.0103 -0.0573 229 PHE A CE2 
1874 C CZ  . PHE A 229 ? 0.4035 0.4189 0.3387 0.0333  -0.0105 -0.0497 229 PHE A CZ  
1875 N N   . LEU A 230 ? 0.324  0.3305 0.3393 0.0318  -0.0195 -0.0594 230 LEU A N   
1876 C CA  . LEU A 230 ? 0.3384 0.3394 0.3662 0.0306  -0.0189 -0.0583 230 LEU A CA  
1877 C C   . LEU A 230 ? 0.3078 0.309  0.3415 0.0257  -0.0207 -0.0535 230 LEU A C   
1878 O O   . LEU A 230 ? 0.3075 0.3081 0.3465 0.0243  -0.0183 -0.0474 230 LEU A O   
1879 C CB  . LEU A 230 ? 0.3519 0.3443 0.3836 0.0315  -0.0204 -0.0668 230 LEU A CB  
1880 C CG  . LEU A 230 ? 0.4025 0.3926 0.4298 0.0373  -0.0173 -0.0718 230 LEU A CG  
1881 C CD1 . LEU A 230 ? 0.4506 0.4307 0.4779 0.0374  -0.0197 -0.0824 230 LEU A CD1 
1882 C CD2 . LEU A 230 ? 0.3931 0.3827 0.4268 0.041   -0.0126 -0.0664 230 LEU A CD2 
1883 N N   . VAL A 231 ? 0.285  0.2876 0.3169 0.0237  -0.0249 -0.0564 231 VAL A N   
1884 C CA  . VAL A 231 ? 0.3247 0.3284 0.3633 0.0198  -0.0262 -0.0531 231 VAL A CA  
1885 C C   . VAL A 231 ? 0.3013 0.3078 0.3362 0.0188  -0.0232 -0.0446 231 VAL A C   
1886 O O   . VAL A 231 ? 0.2675 0.2726 0.3086 0.0161  -0.021  -0.0401 231 VAL A O   
1887 C CB  . VAL A 231 ? 0.3293 0.3364 0.3667 0.0197  -0.032  -0.0582 231 VAL A CB  
1888 C CG1 . VAL A 231 ? 0.3876 0.3985 0.4273 0.0181  -0.033  -0.0539 231 VAL A CG1 
1889 C CG2 . VAL A 231 ? 0.3671 0.3719 0.4134 0.0178  -0.0351 -0.0668 231 VAL A CG2 
1890 N N   . PHE A 232 ? 0.2786 0.2883 0.3026 0.0204  -0.0229 -0.0426 232 PHE A N   
1891 C CA  . PHE A 232 ? 0.2797 0.2909 0.3001 0.0181  -0.0204 -0.0354 232 PHE A CA  
1892 C C   . PHE A 232 ? 0.275  0.2882 0.2983 0.0174  -0.0165 -0.031  232 PHE A C   
1893 O O   . PHE A 232 ? 0.2886 0.3024 0.3124 0.0144  -0.015  -0.0258 232 PHE A O   
1894 C CB  . PHE A 232 ? 0.3043 0.3162 0.3115 0.0189  -0.0207 -0.0339 232 PHE A CB  
1895 C CG  . PHE A 232 ? 0.3148 0.3248 0.3194 0.0204  -0.0253 -0.0362 232 PHE A CG  
1896 C CD1 . PHE A 232 ? 0.3134 0.3227 0.3246 0.0189  -0.0262 -0.0346 232 PHE A CD1 
1897 C CD2 . PHE A 232 ? 0.3501 0.3595 0.3446 0.0239  -0.0287 -0.0397 232 PHE A CD2 
1898 C CE1 . PHE A 232 ? 0.3346 0.3443 0.3458 0.0214  -0.0308 -0.0369 232 PHE A CE1 
1899 C CE2 . PHE A 232 ? 0.3632 0.3722 0.3556 0.0263  -0.0341 -0.0414 232 PHE A CE2 
1900 C CZ  . PHE A 232 ? 0.3619 0.3719 0.3641 0.0254  -0.0353 -0.0403 232 PHE A CZ  
1901 N N   . SER A 233 ? 0.2538 0.2683 0.2791 0.0205  -0.0151 -0.0334 233 SER A N   
1902 C CA  . SER A 233 ? 0.276  0.2937 0.306  0.0212  -0.0125 -0.0293 233 SER A CA  
1903 C C   . SER A 233 ? 0.278  0.2902 0.316  0.0199  -0.0129 -0.0267 233 SER A C   
1904 O O   . SER A 233 ? 0.2943 0.3084 0.333  0.018   -0.0119 -0.021  233 SER A O   
1905 C CB  . SER A 233 ? 0.2559 0.2766 0.2869 0.0263  -0.0106 -0.0327 233 SER A CB  
1906 O OG  . SER A 233 ? 0.2763 0.3021 0.2986 0.0271  -0.0091 -0.035  233 SER A OG  
1907 N N   . TYR A 234 ? 0.2791 0.2838 0.3222 0.0202  -0.014  -0.0309 234 TYR A N   
1908 C CA  . TYR A 234 ? 0.2637 0.2616 0.3131 0.0179  -0.0132 -0.0278 234 TYR A CA  
1909 C C   . TYR A 234 ? 0.2851 0.2841 0.3337 0.013   -0.0129 -0.024  234 TYR A C   
1910 O O   . TYR A 234 ? 0.2715 0.2678 0.3211 0.0111  -0.0111 -0.0186 234 TYR A O   
1911 C CB  . TYR A 234 ? 0.2603 0.2496 0.3157 0.0178  -0.0138 -0.0338 234 TYR A CB  
1912 C CG  . TYR A 234 ? 0.2783 0.2618 0.3352 0.0228  -0.0127 -0.0357 234 TYR A CG  
1913 C CD1 . TYR A 234 ? 0.3235 0.302  0.3824 0.0251  -0.0107 -0.0297 234 TYR A CD1 
1914 C CD2 . TYR A 234 ? 0.3214 0.304  0.3763 0.0263  -0.0136 -0.0433 234 TYR A CD2 
1915 C CE1 . TYR A 234 ? 0.3419 0.314  0.4023 0.0312  -0.0096 -0.0311 234 TYR A CE1 
1916 C CE2 . TYR A 234 ? 0.3475 0.3235 0.4037 0.0317  -0.0119 -0.0455 234 TYR A CE2 
1917 C CZ  . TYR A 234 ? 0.3784 0.3492 0.4379 0.0345  -0.0099 -0.0392 234 TYR A CZ  
1918 O OH  . TYR A 234 ? 0.3989 0.3621 0.4599 0.0412  -0.0082 -0.041  234 TYR A OH  
1919 N N   . LEU A 235 ? 0.2786 0.2808 0.3244 0.0117  -0.0146 -0.0266 235 LEU A N   
1920 C CA  . LEU A 235 ? 0.2666 0.2696 0.3114 0.0082  -0.0139 -0.0236 235 LEU A CA  
1921 C C   . LEU A 235 ? 0.2584 0.2635 0.2966 0.0069  -0.012  -0.0174 235 LEU A C   
1922 O O   . LEU A 235 ? 0.2531 0.2561 0.2911 0.004   -0.0102 -0.0136 235 LEU A O   
1923 C CB  . LEU A 235 ? 0.2792 0.2849 0.3209 0.0091  -0.0166 -0.0273 235 LEU A CB  
1924 C CG  . LEU A 235 ? 0.2541 0.2601 0.2958 0.007   -0.0158 -0.0255 235 LEU A CG  
1925 C CD1 . LEU A 235 ? 0.2562 0.2622 0.3097 0.005   -0.0155 -0.0286 235 LEU A CD1 
1926 C CD2 . LEU A 235 ? 0.2744 0.2818 0.3086 0.0096  -0.0185 -0.0268 235 LEU A CD2 
1927 N N   . THR A 236 ? 0.2563 0.2662 0.2888 0.0085  -0.0123 -0.0167 236 THR A N   
1928 C CA  . THR A 236 ? 0.2571 0.2707 0.284  0.006   -0.0111 -0.0119 236 THR A CA  
1929 C C   . THR A 236 ? 0.2735 0.2883 0.304  0.0063  -0.0107 -0.0079 236 THR A C   
1930 O O   . THR A 236 ? 0.2641 0.2793 0.2912 0.0031  -0.0102 -0.0037 236 THR A O   
1931 C CB  . THR A 236 ? 0.2658 0.2852 0.2871 0.0066  -0.0108 -0.0127 236 THR A CB  
1932 O OG1 . THR A 236 ? 0.2521 0.2683 0.2684 0.0074  -0.0117 -0.016  236 THR A OG1 
1933 C CG2 . THR A 236 ? 0.2914 0.3148 0.3073 0.0021  -0.0095 -0.0087 236 THR A CG2 
1934 N N   . ILE A 237 ? 0.2816 0.2952 0.318  0.0105  -0.011  -0.0091 237 ILE A N   
1935 C CA  . ILE A 237 ? 0.2525 0.2652 0.2916 0.0122  -0.0111 -0.0046 237 ILE A CA  
1936 C C   . ILE A 237 ? 0.2461 0.2503 0.2841 0.0088  -0.0099 -0.0014 237 ILE A C   
1937 O O   . ILE A 237 ? 0.2989 0.303  0.3335 0.0077  -0.01   0.004   237 ILE A O   
1938 C CB  . ILE A 237 ? 0.2619 0.272  0.3068 0.0185  -0.0112 -0.0068 237 ILE A CB  
1939 C CG1 . ILE A 237 ? 0.3104 0.3304 0.3561 0.0222  -0.0113 -0.0094 237 ILE A CG1 
1940 C CG2 . ILE A 237 ? 0.2821 0.288  0.3285 0.0212  -0.0116 -0.0009 237 ILE A CG2 
1941 C CD1 . ILE A 237 ? 0.3109 0.3266 0.3615 0.0289  -0.0107 -0.0135 237 ILE A CD1 
1942 N N   . GLY A 238 ? 0.2782 0.2761 0.3196 0.007   -0.0087 -0.0048 238 GLY A N   
1943 C CA  . GLY A 238 ? 0.2932 0.2841 0.3351 0.0033  -0.0062 -0.0025 238 GLY A CA  
1944 C C   . GLY A 238 ? 0.2756 0.2692 0.3104 -0.0005 -0.0052 0.0002  238 GLY A C   
1945 O O   . GLY A 238 ? 0.2912 0.2811 0.3218 -0.0027 -0.0033 0.0047  238 GLY A O   
1946 N N   . THR A 239 ? 0.2635 0.2624 0.2953 -0.0011 -0.0063 -0.0024 239 THR A N   
1947 C CA  . THR A 239 ? 0.2919 0.2913 0.3158 -0.0047 -0.0051 -0.0005 239 THR A CA  
1948 C C   . THR A 239 ? 0.3031 0.3057 0.3204 -0.0059 -0.0062 0.0043  239 THR A C   
1949 O O   . THR A 239 ? 0.2979 0.2978 0.3083 -0.0093 -0.0047 0.0067  239 THR A O   
1950 C CB  . THR A 239 ? 0.285  0.2866 0.3059 -0.0046 -0.006  -0.0038 239 THR A CB  
1951 O OG1 . THR A 239 ? 0.2771 0.2773 0.3049 -0.0027 -0.0062 -0.0081 239 THR A OG1 
1952 C CG2 . THR A 239 ? 0.2956 0.2943 0.3082 -0.008  -0.0041 -0.0028 239 THR A CG2 
1953 N N   . SER A 240 ? 0.2978 0.3066 0.3173 -0.003  -0.0087 0.005   240 SER A N   
1954 C CA  . SER A 240 ? 0.2839 0.2992 0.2999 -0.0035 -0.0109 0.009   240 SER A CA  
1955 C C   . SER A 240 ? 0.2972 0.3075 0.3102 -0.0031 -0.011  0.0141  240 SER A C   
1956 O O   . SER A 240 ? 0.3031 0.3178 0.3101 -0.0048 -0.0132 0.0175  240 SER A O   
1957 C CB  . SER A 240 ? 0.2855 0.3106 0.3074 0.0007  -0.0132 0.0085  240 SER A CB  
1958 O OG  . SER A 240 ? 0.2813 0.3039 0.3089 0.0066  -0.014  0.0104  240 SER A OG  
1959 N N   . TYR A 241 ? 0.2994 0.3003 0.3154 -0.0018 -0.0086 0.0146  241 TYR A N   
1960 C CA  . TYR A 241 ? 0.2951 0.2883 0.3065 -0.0017 -0.0076 0.0201  241 TYR A CA  
1961 C C   . TYR A 241 ? 0.3045 0.2901 0.3105 -0.0068 -0.0029 0.0204  241 TYR A C   
1962 O O   . TYR A 241 ? 0.3303 0.3084 0.3303 -0.0075 -0.001  0.0253  241 TYR A O   
1963 C CB  . TYR A 241 ? 0.34   0.3258 0.3582 0.003   -0.007  0.0208  241 TYR A CB  
1964 C CG  . TYR A 241 ? 0.3177 0.309  0.3396 0.0098  -0.0111 0.0225  241 TYR A CG  
1965 C CD1 . TYR A 241 ? 0.3491 0.3445 0.3653 0.0125  -0.0147 0.0285  241 TYR A CD1 
1966 C CD2 . TYR A 241 ? 0.3127 0.3056 0.3433 0.014   -0.0115 0.0177  241 TYR A CD2 
1967 C CE1 . TYR A 241 ? 0.3851 0.3872 0.4064 0.0199  -0.0185 0.03    241 TYR A CE1 
1968 C CE2 . TYR A 241 ? 0.3723 0.3706 0.4068 0.0211  -0.0143 0.0188  241 TYR A CE2 
1969 C CZ  . TYR A 241 ? 0.3792 0.383  0.4102 0.0243  -0.0178 0.025   241 TYR A CZ  
1970 O OH  . TYR A 241 ? 0.3783 0.3889 0.4149 0.0324  -0.0206 0.026   241 TYR A OH  
1971 N N   . ILE A 242 ? 0.2876 0.2747 0.295  -0.0097 -0.0008 0.0156  242 ILE A N   
1972 C CA  . ILE A 242 ? 0.3576 0.3389 0.3643 -0.0133 0.0045  0.0143  242 ILE A CA  
1973 C C   . ILE A 242 ? 0.4421 0.4196 0.4358 -0.0166 0.0068  0.0185  242 ILE A C   
1974 O O   . ILE A 242 ? 0.4873 0.4582 0.4792 -0.0189 0.0121  0.0201  242 ILE A O   
1975 C CB  . ILE A 242 ? 0.4273 0.4122 0.4388 -0.0136 0.0051  0.0082  242 ILE A CB  
1976 C CG1 . ILE A 242 ? 0.5088 0.4914 0.5285 -0.0148 0.0095  0.005   242 ILE A CG1 
1977 C CG2 . ILE A 242 ? 0.4949 0.4816 0.4967 -0.0158 0.0046  0.0075  242 ILE A CG2 
1978 C CD1 . ILE A 242 ? 0.5037 0.4908 0.5292 -0.0132 0.0083  -0.0008 242 ILE A CD1 
1979 N N   . PHE A 243 ? 0.3774 0.3593 0.3617 -0.0173 0.0029  0.0204  243 PHE A N   
1980 C CA  . PHE A 243 ? 0.4916 0.4703 0.4615 -0.0208 0.0041  0.0233  243 PHE A CA  
1981 C C   . PHE A 243 ? 0.5034 0.4815 0.4667 -0.0186 0.0004  0.0301  243 PHE A C   
1982 O O   . PHE A 243 ? 0.7101 0.6843 0.6598 -0.0211 0.0012  0.0333  243 PHE A O   
1983 C CB  . PHE A 243 ? 0.4577 0.4406 0.4196 -0.0243 0.0022  0.0201  243 PHE A CB  
1984 C CG  . PHE A 243 ? 0.563  0.5441 0.5295 -0.0251 0.0058  0.0143  243 PHE A CG  
1985 C CD1 . PHE A 243 ? 0.5667 0.5416 0.5334 -0.0259 0.0123  0.0125  243 PHE A CD1 
1986 C CD2 . PHE A 243 ? 0.6131 0.5986 0.5842 -0.0245 0.0031  0.0108  243 PHE A CD2 
1987 C CE1 . PHE A 243 ? 0.5264 0.5005 0.4984 -0.0251 0.0149  0.0074  243 PHE A CE1 
1988 C CE2 . PHE A 243 ? 0.6288 0.6113 0.6031 -0.0239 0.0058  0.0063  243 PHE A CE2 
1989 C CZ  . PHE A 243 ? 0.5645 0.5416 0.5394 -0.0237 0.0113  0.0045  243 PHE A CZ  
1990 N N   . SER A 244 ? 0.4577 0.4387 0.4293 -0.0135 -0.0034 0.0323  244 SER A N   
1991 C CA  . SER A 244 ? 0.444  0.4257 0.4101 -0.0096 -0.0083 0.0388  244 SER A CA  
1992 C C   . SER A 244 ? 0.4929 0.4637 0.4621 -0.0052 -0.0063 0.0435  244 SER A C   
1993 O O   . SER A 244 ? 0.5038 0.4695 0.4637 -0.0023 -0.0084 0.0505  244 SER A O   
1994 C CB  . SER A 244 ? 0.4793 0.4749 0.4513 -0.0064 -0.0152 0.0376  244 SER A CB  
1995 O OG  . SER A 244 ? 0.4661 0.465  0.4521 -0.0032 -0.0148 0.0336  244 SER A OG  
1996 N N   . ASP A 245 ? 0.4129 0.3793 0.3942 -0.0044 -0.0027 0.0398  245 ASP A N   
1997 C CA  . ASP A 245 ? 0.4176 0.3723 0.4021 -0.0007 -0.0011 0.0436  245 ASP A CA  
1998 C C   . ASP A 245 ? 0.3981 0.3466 0.3932 -0.0041 0.0048  0.0383  245 ASP A C   
1999 O O   . ASP A 245 ? 0.362  0.3152 0.3686 -0.0022 0.0034  0.0325  245 ASP A O   
2000 C CB  . ASP A 245 ? 0.4037 0.363  0.3943 0.0074  -0.0071 0.0448  245 ASP A CB  
2001 C CG  . ASP A 245 ? 0.45   0.3943 0.4405 0.0127  -0.006  0.05    245 ASP A CG  
2002 O OD1 . ASP A 245 ? 0.4534 0.3838 0.4458 0.0091  0.0002  0.0495  245 ASP A OD1 
2003 O OD2 . ASP A 245 ? 0.4841 0.431  0.4745 0.0206  -0.0113 0.0538  245 ASP A OD2 
2004 N N   . PHE A 246 ? 0.3897 0.3286 0.3804 -0.0092 0.0115  0.0404  246 PHE A N   
2005 C CA  . PHE A 246 ? 0.3472 0.2821 0.3486 -0.0138 0.0175  0.0354  246 PHE A CA  
2006 C C   . PHE A 246 ? 0.3361 0.2653 0.3485 -0.0109 0.0163  0.0331  246 PHE A C   
2007 O O   . PHE A 246 ? 0.3409 0.2753 0.3654 -0.0121 0.0162  0.0256  246 PHE A O   
2008 C CB  . PHE A 246 ? 0.3676 0.2925 0.362  -0.0198 0.0257  0.0394  246 PHE A CB  
2009 C CG  . PHE A 246 ? 0.3949 0.317  0.4029 -0.0252 0.0322  0.0343  246 PHE A CG  
2010 C CD1 . PHE A 246 ? 0.3665 0.3004 0.3857 -0.028  0.0337  0.0263  246 PHE A CD1 
2011 C CD2 . PHE A 246 ? 0.4462 0.3542 0.457  -0.0271 0.036   0.0371  246 PHE A CD2 
2012 C CE1 . PHE A 246 ? 0.4004 0.3347 0.434  -0.0329 0.0387  0.0212  246 PHE A CE1 
2013 C CE2 . PHE A 246 ? 0.4575 0.3643 0.4823 -0.0335 0.0419  0.0317  246 PHE A CE2 
2014 C CZ  . PHE A 246 ? 0.4055 0.3271 0.4425 -0.0364 0.0429  0.0235  246 PHE A CZ  
2015 N N   . ASN A 247 ? 0.342  0.2589 0.3489 -0.0069 0.0156  0.0395  247 ASN A N   
2016 C CA  . ASN A 247 ? 0.3599 0.2669 0.3755 -0.0045 0.0158  0.0374  247 ASN A CA  
2017 C C   . ASN A 247 ? 0.3536 0.2713 0.3782 0.0013  0.0097  0.0308  247 ASN A C   
2018 O O   . ASN A 247 ? 0.3236 0.2396 0.3587 0.0004  0.0104  0.0238  247 ASN A O   
2019 C CB  . ASN A 247 ? 0.3825 0.2718 0.3879 -0.0007 0.0167  0.0467  247 ASN A CB  
2020 C CG  . ASN A 247 ? 0.4248 0.3016 0.4214 -0.008  0.0245  0.0523  247 ASN A CG  
2021 O OD1 . ASN A 247 ? 0.4641 0.3339 0.4682 -0.0154 0.0312  0.0489  247 ASN A OD1 
2022 N ND2 . ASN A 247 ? 0.4581 0.3333 0.4388 -0.007  0.0241  0.0604  247 ASN A ND2 
2023 N N   . LEU A 248 ? 0.3647 0.2945 0.3855 0.0066  0.0041  0.0323  248 LEU A N   
2024 C CA  . LEU A 248 ? 0.3314 0.2722 0.36   0.0117  -0.0004 0.0264  248 LEU A CA  
2025 C C   . LEU A 248 ? 0.3088 0.2603 0.3436 0.007   0       0.0185  248 LEU A C   
2026 O O   . LEU A 248 ? 0.3129 0.2681 0.355  0.0091  -0.0015 0.0121  248 LEU A O   
2027 C CB  . LEU A 248 ? 0.3564 0.3084 0.3812 0.0181  -0.0059 0.0301  248 LEU A CB  
2028 C CG  . LEU A 248 ? 0.4216 0.3656 0.4431 0.0264  -0.0083 0.0368  248 LEU A CG  
2029 C CD1 . LEU A 248 ? 0.4457 0.4057 0.4658 0.032   -0.0144 0.0396  248 LEU A CD1 
2030 C CD2 . LEU A 248 ? 0.4807 0.4155 0.5102 0.0319  -0.0074 0.0328  248 LEU A CD2 
2031 N N   . SER A 249 ? 0.3237 0.2796 0.3546 0.0014  0.002   0.0189  249 SER A N   
2032 C CA  . SER A 249 ? 0.2938 0.2579 0.33   -0.0021 0.0024  0.0121  249 SER A CA  
2033 C C   . SER A 249 ? 0.3022 0.2613 0.3487 -0.0045 0.0048  0.0063  249 SER A C   
2034 O O   . SER A 249 ? 0.2759 0.2401 0.329  -0.0031 0.0022  -0.0004 249 SER A O   
2035 C CB  . SER A 249 ? 0.2887 0.256  0.3184 -0.0067 0.0049  0.0138  249 SER A CB  
2036 O OG  . SER A 249 ? 0.2834 0.258  0.3177 -0.0083 0.0047  0.0077  249 SER A OG  
2037 N N   . LYS A 250 ? 0.2848 0.2333 0.3323 -0.0085 0.0096  0.0088  250 LYS A N   
2038 C CA  . LYS A 250 ? 0.302  0.2464 0.3604 -0.0127 0.0122  0.003   250 LYS A CA  
2039 C C   . LYS A 250 ? 0.2839 0.2231 0.347  -0.0087 0.009   -0.0011 250 LYS A C   
2040 O O   . LYS A 250 ? 0.3042 0.2471 0.376  -0.0101 0.0075  -0.009  250 LYS A O   
2041 C CB  . LYS A 250 ? 0.3094 0.2423 0.367  -0.0187 0.0191  0.0075  250 LYS A CB  
2042 C CG  . LYS A 250 ? 0.3635 0.292  0.4338 -0.0247 0.0225  0.0014  250 LYS A CG  
2043 C CD  . LYS A 250 ? 0.4192 0.338  0.4873 -0.0319 0.031   0.0068  250 LYS A CD  
2044 C CE  . LYS A 250 ? 0.5466 0.4549 0.6242 -0.0386 0.0355  0.0037  250 LYS A CE  
2045 N NZ  . LYS A 250 ? 0.5879 0.4883 0.662  -0.046  0.0448  0.0096  250 LYS A NZ  
2046 N N   . GLN A 251 ? 0.3137 0.2443 0.3707 -0.0033 0.008   0.004   251 GLN A N   
2047 C CA  . GLN A 251 ? 0.3434 0.268  0.4039 0.0018  0.0056  0       251 GLN A CA  
2048 C C   . GLN A 251 ? 0.32   0.2577 0.3845 0.0047  0.0013  -0.008  251 GLN A C   
2049 O O   . GLN A 251 ? 0.3362 0.2712 0.4067 0.0042  0.0004  -0.0157 251 GLN A O   
2050 C CB  . GLN A 251 ? 0.3551 0.2723 0.4082 0.0094  0.0044  0.0074  251 GLN A CB  
2051 C CG  . GLN A 251 ? 0.3907 0.3016 0.4467 0.0167  0.0025  0.0034  251 GLN A CG  
2052 C CD  . GLN A 251 ? 0.4276 0.3381 0.478  0.0262  0       0.0105  251 GLN A CD  
2053 O OE1 . GLN A 251 ? 0.5099 0.4299 0.5625 0.0333  -0.003  0.0077  251 GLN A OE1 
2054 N NE2 . GLN A 251 ? 0.4095 0.3101 0.4525 0.0265  0.0014  0.0197  251 GLN A NE2 
2055 N N   . ASN A 252 ? 0.2846 0.2351 0.3444 0.0075  -0.0014 -0.0058 252 ASN A N   
2056 C CA  . ASN A 252 ? 0.2933 0.2554 0.354  0.0102  -0.0048 -0.0117 252 ASN A CA  
2057 C C   . ASN A 252 ? 0.2798 0.2472 0.3451 0.0055  -0.0054 -0.0183 252 ASN A C   
2058 O O   . ASN A 252 ? 0.2838 0.254  0.3512 0.0072  -0.0079 -0.0251 252 ASN A O   
2059 C CB  . ASN A 252 ? 0.279  0.2522 0.3335 0.0129  -0.0065 -0.0072 252 ASN A CB  
2060 C CG  . ASN A 252 ? 0.3327 0.3054 0.3861 0.0198  -0.0076 -0.0039 252 ASN A CG  
2061 O OD1 . ASN A 252 ? 0.3247 0.3009 0.3803 0.0245  -0.0087 -0.0085 252 ASN A OD1 
2062 N ND2 . ASN A 252 ? 0.3135 0.2827 0.363  0.0211  -0.0074 0.0038  252 ASN A ND2 
2063 N N   . TYR A 253 ? 0.2759 0.2444 0.3429 0       -0.0031 -0.0165 253 TYR A N   
2064 C CA  . TYR A 253 ? 0.2833 0.258  0.3568 -0.0033 -0.0042 -0.0229 253 TYR A CA  
2065 C C   . TYR A 253 ? 0.2966 0.2656 0.3794 -0.006  -0.0043 -0.0297 253 TYR A C   
2066 O O   . TYR A 253 ? 0.2673 0.2426 0.3546 -0.0061 -0.0079 -0.0371 253 TYR A O   
2067 C CB  . TYR A 253 ? 0.2511 0.2292 0.3257 -0.0078 -0.0009 -0.02   253 TYR A CB  
2068 C CG  . TYR A 253 ? 0.2845 0.2683 0.35   -0.0063 -0.0011 -0.0156 253 TYR A CG  
2069 C CD1 . TYR A 253 ? 0.2787 0.2691 0.3391 -0.0026 -0.005  -0.0174 253 TYR A CD1 
2070 C CD2 . TYR A 253 ? 0.3074 0.2893 0.3689 -0.0094 0.0031  -0.0104 253 TYR A CD2 
2071 C CE1 . TYR A 253 ? 0.264  0.2577 0.316  -0.0024 -0.0048 -0.0138 253 TYR A CE1 
2072 C CE2 . TYR A 253 ? 0.3079 0.2939 0.3608 -0.0088 0.0029  -0.0077 253 TYR A CE2 
2073 C CZ  . TYR A 253 ? 0.2887 0.2801 0.3372 -0.0056 -0.0011 -0.0095 253 TYR A CZ  
2074 O OH  . TYR A 253 ? 0.2558 0.2493 0.2956 -0.006  -0.001  -0.0073 253 TYR A OH  
2075 N N   . LEU A 254 ? 0.3119 0.2681 0.3966 -0.0083 -0.0007 -0.0274 254 LEU A N   
2076 C CA  . LEU A 254 ? 0.2922 0.2413 0.3858 -0.0127 -0.0001 -0.0342 254 LEU A CA  
2077 C C   . LEU A 254 ? 0.3398 0.2855 0.4317 -0.0079 -0.0041 -0.0406 254 LEU A C   
2078 O O   . LEU A 254 ? 0.3287 0.2753 0.4273 -0.0109 -0.0065 -0.0496 254 LEU A O   
2079 C CB  . LEU A 254 ? 0.3298 0.263  0.4245 -0.0175 0.0059  -0.0294 254 LEU A CB  
2080 C CG  . LEU A 254 ? 0.3411 0.2762 0.4394 -0.0246 0.0115  -0.0252 254 LEU A CG  
2081 C CD1 . LEU A 254 ? 0.3816 0.2984 0.4791 -0.03   0.0183  -0.0201 254 LEU A CD1 
2082 C CD2 . LEU A 254 ? 0.3617 0.3104 0.4727 -0.03   0.0105  -0.033  254 LEU A CD2 
2083 N N   . ILE A 255 ? 0.3241 0.2665 0.4076 -0.0005 -0.0046 -0.0365 255 ILE A N   
2084 C CA  . ILE A 255 ? 0.3611 0.3028 0.4419 0.0053  -0.0076 -0.0426 255 ILE A CA  
2085 C C   . ILE A 255 ? 0.3299 0.2858 0.4097 0.0058  -0.0121 -0.0488 255 ILE A C   
2086 O O   . ILE A 255 ? 0.3021 0.2576 0.3832 0.0057  -0.015  -0.0577 255 ILE A O   
2087 C CB  . ILE A 255 ? 0.3611 0.3002 0.435  0.0135  -0.0068 -0.0369 255 ILE A CB  
2088 C CG1 . ILE A 255 ? 0.3996 0.3216 0.4735 0.0146  -0.0032 -0.0314 255 ILE A CG1 
2089 C CG2 . ILE A 255 ? 0.3821 0.3244 0.453  0.02    -0.0089 -0.0436 255 ILE A CG2 
2090 C CD1 . ILE A 255 ? 0.4175 0.3403 0.4858 0.0229  -0.0031 -0.0234 255 ILE A CD1 
2091 N N   . GLY A 256 ? 0.3535 0.3206 0.4296 0.0066  -0.0128 -0.0442 256 GLY A N   
2092 C CA  . GLY A 256 ? 0.3162 0.2946 0.3894 0.0076  -0.0169 -0.0485 256 GLY A CA  
2093 C C   . GLY A 256 ? 0.3149 0.2969 0.3959 0.0031  -0.0202 -0.056  256 GLY A C   
2094 O O   . GLY A 256 ? 0.3234 0.3099 0.4016 0.0051  -0.0248 -0.0629 256 GLY A O   
2095 N N   . LEU A 257 ? 0.305  0.2861 0.3954 -0.0029 -0.0177 -0.0547 257 LEU A N   
2096 C CA  . LEU A 257 ? 0.3183 0.3054 0.4197 -0.0079 -0.0203 -0.0617 257 LEU A CA  
2097 C C   . LEU A 257 ? 0.3392 0.3203 0.444  -0.0097 -0.023  -0.0711 257 LEU A C   
2098 O O   . LEU A 257 ? 0.3426 0.3318 0.451  -0.0105 -0.0288 -0.0793 257 LEU A O   
2099 C CB  . LEU A 257 ? 0.3404 0.3268 0.4516 -0.0145 -0.0149 -0.0579 257 LEU A CB  
2100 C CG  . LEU A 257 ? 0.3566 0.3527 0.4827 -0.0205 -0.0166 -0.0648 257 LEU A CG  
2101 C CD1 . LEU A 257 ? 0.3229 0.3346 0.4497 -0.0164 -0.0229 -0.0683 257 LEU A CD1 
2102 C CD2 . LEU A 257 ? 0.3717 0.3666 0.5068 -0.0273 -0.0093 -0.0607 257 LEU A CD2 
2103 N N   . LYS A 258 ? 0.3432 0.3095 0.4456 -0.0096 -0.0193 -0.07   258 LYS A N   
2104 C CA  . LYS A 258 ? 0.3835 0.3406 0.4867 -0.0106 -0.0212 -0.0791 258 LYS A CA  
2105 C C   . LYS A 258 ? 0.3638 0.3266 0.4572 -0.0041 -0.0266 -0.085  258 LYS A C   
2106 O O   . LYS A 258 ? 0.3548 0.3195 0.45   -0.0062 -0.0313 -0.0949 258 LYS A O   
2107 C CB  . LYS A 258 ? 0.428  0.366  0.5289 -0.0099 -0.0157 -0.0757 258 LYS A CB  
2108 C CG  . LYS A 258 ? 0.5324 0.4563 0.6344 -0.0118 -0.0163 -0.0855 258 LYS A CG  
2109 C CD  . LYS A 258 ? 0.658  0.5631 0.7532 -0.0061 -0.0119 -0.082  258 LYS A CD  
2110 C CE  . LYS A 258 ? 0.7706 0.6777 0.8551 0.0048  -0.0133 -0.0832 258 LYS A CE  
2111 N NZ  . LYS A 258 ? 0.8052 0.7265 0.8844 0.0108  -0.0136 -0.0749 258 LYS A NZ  
2112 N N   . PHE A 259 ? 0.3296 0.2961 0.4124 0.0031  -0.0259 -0.0792 259 PHE A N   
2113 C CA  . PHE A 259 ? 0.3267 0.2992 0.3987 0.0087  -0.0299 -0.0839 259 PHE A CA  
2114 C C   . PHE A 259 ? 0.3382 0.3241 0.4098 0.0078  -0.0361 -0.0867 259 PHE A C   
2115 O O   . PHE A 259 ? 0.3408 0.3302 0.4043 0.0105  -0.041  -0.0934 259 PHE A O   
2116 C CB  . PHE A 259 ? 0.3344 0.3087 0.3962 0.0155  -0.0268 -0.077  259 PHE A CB  
2117 C CG  . PHE A 259 ? 0.3697 0.3331 0.4298 0.0197  -0.0225 -0.0768 259 PHE A CG  
2118 C CD1 . PHE A 259 ? 0.4287 0.3849 0.4847 0.0225  -0.0232 -0.0861 259 PHE A CD1 
2119 C CD2 . PHE A 259 ? 0.3445 0.3048 0.4067 0.0217  -0.0181 -0.0677 259 PHE A CD2 
2120 C CE1 . PHE A 259 ? 0.4442 0.3898 0.499  0.0278  -0.0189 -0.086  259 PHE A CE1 
2121 C CE2 . PHE A 259 ? 0.3727 0.3232 0.4342 0.0271  -0.0148 -0.0673 259 PHE A CE2 
2122 C CZ  . PHE A 259 ? 0.4137 0.3568 0.472  0.0306  -0.0149 -0.0764 259 PHE A CZ  
2123 N N   . ALA A 260 ? 0.2981 0.2912 0.377  0.0047  -0.0359 -0.0818 260 ALA A N   
2124 C CA  . ALA A 260 ? 0.3263 0.3319 0.4065 0.005   -0.0419 -0.0843 260 ALA A CA  
2125 C C   . ALA A 260 ? 0.3493 0.36   0.4401 0.0005  -0.0479 -0.0947 260 ALA A C   
2126 O O   . ALA A 260 ? 0.3431 0.3656 0.4352 0.0019  -0.0543 -0.0976 260 ALA A O   
2127 C CB  . ALA A 260 ? 0.3332 0.3447 0.4185 0.0039  -0.0393 -0.0764 260 ALA A CB  
2128 N N   . LYS A 261 ? 0.3946 0.3972 0.4945 -0.0056 -0.0456 -0.0997 261 LYS A N   
2129 C CA  . LYS A 261 ? 0.4898 0.4974 0.6035 -0.0126 -0.0499 -0.1095 261 LYS A CA  
2130 C C   . LYS A 261 ? 0.4443 0.4632 0.5539 -0.0099 -0.06   -0.1183 261 LYS A C   
2131 O O   . LYS A 261 ? 0.4515 0.4655 0.546  -0.0049 -0.0626 -0.1214 261 LYS A O   
2132 C CB  . LYS A 261 ? 0.636  0.6281 0.7512 -0.0174 -0.0474 -0.1161 261 LYS A CB  
2133 C CG  . LYS A 261 ? 0.8371 0.8206 0.9657 -0.0258 -0.0404 -0.1135 261 LYS A CG  
2134 C CD  . LYS A 261 ? 0.8615 0.8537 1.0079 -0.0358 -0.0435 -0.1224 261 LYS A CD  
2135 C CE  . LYS A 261 ? 1.0078 0.9854 1.1635 -0.0448 -0.035  -0.1202 261 LYS A CE  
2136 N NZ  . LYS A 261 ? 1.0699 1.0551 1.2447 -0.0565 -0.036  -0.1285 261 LYS A NZ  
2137 N N   . GLY A 262 ? 0.4906 0.5253 0.6131 -0.0126 -0.0656 -0.1218 262 GLY A N   
2138 C CA  . GLY A 262 ? 0.5636 0.6107 0.6833 -0.0098 -0.0767 -0.1303 262 GLY A CA  
2139 C C   . GLY A 262 ? 0.5558 0.6111 0.6625 0.0001  -0.0811 -0.1242 262 GLY A C   
2140 O O   . GLY A 262 ? 0.4871 0.5528 0.5897 0.0038  -0.091  -0.1297 262 GLY A O   
2141 N N   . ASN A 263 ? 0.42   0.4702 0.5197 0.0042  -0.0743 -0.1128 263 ASN A N   
2142 C CA  . ASN A 263 ? 0.3907 0.4455 0.478  0.0125  -0.0772 -0.1063 263 ASN A CA  
2143 C C   . ASN A 263 ? 0.4015 0.4619 0.5008 0.0119  -0.0727 -0.099  263 ASN A C   
2144 O O   . ASN A 263 ? 0.3255 0.3772 0.423  0.0105  -0.064  -0.0913 263 ASN A O   
2145 C CB  . ASN A 263 ? 0.4021 0.445  0.4678 0.0175  -0.073  -0.1004 263 ASN A CB  
2146 C CG  . ASN A 263 ? 0.4593 0.5048 0.5108 0.025   -0.0757 -0.0938 263 ASN A CG  
2147 O OD1 . ASN A 263 ? 0.404  0.4537 0.4611 0.0264  -0.0744 -0.0878 263 ASN A OD1 
2148 N ND2 . ASN A 263 ? 0.4499 0.4914 0.4814 0.0299  -0.0787 -0.0946 263 ASN A ND2 
2149 N N   . PRO A 264 ? 0.4075 0.4829 0.5193 0.0133  -0.0784 -0.1017 264 PRO A N   
2150 C CA  . PRO A 264 ? 0.3752 0.4564 0.4997 0.0126  -0.0733 -0.0961 264 PRO A CA  
2151 C C   . PRO A 264 ? 0.3741 0.4468 0.4845 0.0181  -0.0678 -0.0854 264 PRO A C   
2152 O O   . PRO A 264 ? 0.3118 0.3822 0.4289 0.0151  -0.06   -0.0802 264 PRO A O   
2153 C CB  . PRO A 264 ? 0.3913 0.4916 0.5296 0.0157  -0.0821 -0.1019 264 PRO A CB  
2154 C CG  . PRO A 264 ? 0.431  0.5361 0.572  0.0121  -0.0903 -0.1129 264 PRO A CG  
2155 C CD  . PRO A 264 ? 0.4265 0.5155 0.5427 0.0151  -0.0902 -0.1111 264 PRO A CD  
2156 N N   . GLY A 265 ? 0.3588 0.4264 0.4493 0.0254  -0.0719 -0.0825 265 GLY A N   
2157 C CA  . GLY A 265 ? 0.3597 0.4178 0.4354 0.0294  -0.0668 -0.0729 265 GLY A CA  
2158 C C   . GLY A 265 ? 0.3354 0.3822 0.407  0.0243  -0.0575 -0.0679 265 GLY A C   
2159 O O   . GLY A 265 ? 0.3532 0.3958 0.4241 0.0234  -0.0511 -0.0612 265 GLY A O   
2160 N N   . PHE A 266 ? 0.2874 0.3291 0.3556 0.0214  -0.0569 -0.0713 266 PHE A N   
2161 C CA  . PHE A 266 ? 0.3023 0.3347 0.3677 0.0179  -0.0492 -0.0669 266 PHE A CA  
2162 C C   . PHE A 266 ? 0.2791 0.3117 0.3606 0.0117  -0.0439 -0.0662 266 PHE A C   
2163 O O   . PHE A 266 ? 0.3053 0.3323 0.3847 0.0101  -0.0375 -0.0594 266 PHE A O   
2164 C CB  . PHE A 266 ? 0.2933 0.3202 0.352  0.0177  -0.0499 -0.0715 266 PHE A CB  
2165 C CG  . PHE A 266 ? 0.3249 0.3494 0.3644 0.0231  -0.0525 -0.0713 266 PHE A CG  
2166 C CD1 . PHE A 266 ? 0.3439 0.3672 0.3707 0.0269  -0.0517 -0.0645 266 PHE A CD1 
2167 C CD2 . PHE A 266 ? 0.3831 0.4053 0.4165 0.024   -0.055  -0.0782 266 PHE A CD2 
2168 C CE1 . PHE A 266 ? 0.4153 0.4355 0.4239 0.0309  -0.0529 -0.064  266 PHE A CE1 
2169 C CE2 . PHE A 266 ? 0.3705 0.3906 0.3854 0.0287  -0.0563 -0.0782 266 PHE A CE2 
2170 C CZ  . PHE A 266 ? 0.3834 0.4026 0.386  0.0319  -0.0552 -0.0709 266 PHE A CZ  
2171 N N   . GLU A 267 ? 0.2742 0.3132 0.3709 0.0078  -0.0465 -0.0731 267 GLU A N   
2172 C CA  . GLU A 267 ? 0.3007 0.3392 0.4121 0.001   -0.0404 -0.0721 267 GLU A CA  
2173 C C   . GLU A 267 ? 0.2786 0.3205 0.3925 0.0017  -0.0359 -0.0656 267 GLU A C   
2174 O O   . GLU A 267 ? 0.2811 0.3172 0.3969 -0.0023 -0.0286 -0.0607 267 GLU A O   
2175 C CB  . GLU A 267 ? 0.3053 0.3522 0.4341 -0.0044 -0.0437 -0.0811 267 GLU A CB  
2176 C CG  . GLU A 267 ? 0.3304 0.3702 0.4569 -0.007  -0.0464 -0.088  267 GLU A CG  
2177 C CD  . GLU A 267 ? 0.4457 0.4947 0.589  -0.0132 -0.0512 -0.0986 267 GLU A CD  
2178 O OE1 . GLU A 267 ? 0.4801 0.5204 0.6274 -0.0192 -0.0493 -0.1032 267 GLU A OE1 
2179 O OE2 . GLU A 267 ? 0.4876 0.5523 0.6398 -0.0116 -0.0571 -0.1024 267 GLU A OE2 
2180 N N   . GLU A 268 ? 0.2626 0.3125 0.3746 0.0074  -0.0402 -0.0656 268 GLU A N   
2181 C CA  . GLU A 268 ? 0.2855 0.3382 0.3998 0.009   -0.0361 -0.0609 268 GLU A CA  
2182 C C   . GLU A 268 ? 0.2938 0.3348 0.3941 0.009   -0.0296 -0.0523 268 GLU A C   
2183 O O   . GLU A 268 ? 0.2806 0.321  0.3842 0.007   -0.0236 -0.0488 268 GLU A O   
2184 C CB  . GLU A 268 ? 0.2799 0.3419 0.394  0.0166  -0.0432 -0.0631 268 GLU A CB  
2185 C CG  . GLU A 268 ? 0.2681 0.3306 0.3818 0.0203  -0.0391 -0.0583 268 GLU A CG  
2186 C CD  . GLU A 268 ? 0.3521 0.4222 0.465  0.0295  -0.0466 -0.0601 268 GLU A CD  
2187 O OE1 . GLU A 268 ? 0.3434 0.4252 0.471  0.032   -0.0469 -0.0627 268 GLU A OE1 
2188 O OE2 . GLU A 268 ? 0.386  0.4494 0.4822 0.0344  -0.0518 -0.0585 268 GLU A OE2 
2189 N N   . PHE A 269 ? 0.2804 0.3134 0.365  0.0113  -0.0308 -0.0494 269 PHE A N   
2190 C CA  . PHE A 269 ? 0.2678 0.2918 0.341  0.0101  -0.0254 -0.0422 269 PHE A CA  
2191 C C   . PHE A 269 ? 0.2894 0.3098 0.3693 0.0043  -0.0194 -0.04   269 PHE A C   
2192 O O   . PHE A 269 ? 0.2406 0.2576 0.317  0.0026  -0.0145 -0.0349 269 PHE A O   
2193 C CB  . PHE A 269 ? 0.285  0.3037 0.3443 0.0123  -0.027  -0.0406 269 PHE A CB  
2194 C CG  . PHE A 269 ? 0.2907 0.3091 0.3379 0.0175  -0.0308 -0.0398 269 PHE A CG  
2195 C CD1 . PHE A 269 ? 0.3168 0.3299 0.3532 0.0182  -0.0279 -0.0341 269 PHE A CD1 
2196 C CD2 . PHE A 269 ? 0.2847 0.3068 0.3299 0.0215  -0.0373 -0.0447 269 PHE A CD2 
2197 C CE1 . PHE A 269 ? 0.336  0.3458 0.3596 0.0228  -0.0308 -0.0327 269 PHE A CE1 
2198 C CE2 . PHE A 269 ? 0.2917 0.3115 0.3234 0.0267  -0.0407 -0.043  269 PHE A CE2 
2199 C CZ  . PHE A 269 ? 0.3095 0.3224 0.3304 0.0274  -0.0372 -0.0367 269 PHE A CZ  
2200 N N   . PHE A 270 ? 0.2589 0.2784 0.3466 0.0013  -0.0198 -0.0437 270 PHE A N   
2201 C CA  . PHE A 270 ? 0.2674 0.2802 0.3589 -0.0038 -0.0142 -0.0407 270 PHE A CA  
2202 C C   . PHE A 270 ? 0.25   0.2664 0.3526 -0.0083 -0.0094 -0.0406 270 PHE A C   
2203 O O   . PHE A 270 ? 0.2596 0.2705 0.3588 -0.011  -0.0035 -0.0348 270 PHE A O   
2204 C CB  . PHE A 270 ? 0.2831 0.291  0.3791 -0.0057 -0.0154 -0.0449 270 PHE A CB  
2205 C CG  . PHE A 270 ? 0.2999 0.3038 0.3845 -0.001  -0.0182 -0.0446 270 PHE A CG  
2206 C CD1 . PHE A 270 ? 0.2633 0.2612 0.3394 0.0004  -0.0151 -0.038  270 PHE A CD1 
2207 C CD2 . PHE A 270 ? 0.3294 0.3371 0.4113 0.0024  -0.024  -0.0508 270 PHE A CD2 
2208 C CE1 . PHE A 270 ? 0.2977 0.2948 0.3652 0.0048  -0.0169 -0.0379 270 PHE A CE1 
2209 C CE2 . PHE A 270 ? 0.3013 0.3062 0.3723 0.0066  -0.0251 -0.0504 270 PHE A CE2 
2210 C CZ  . PHE A 270 ? 0.2779 0.2782 0.3429 0.0077  -0.0212 -0.0442 270 PHE A CZ  
2211 N N   . LYS A 271 ? 0.2621 0.2887 0.3774 -0.0088 -0.0119 -0.0467 271 LYS A N   
2212 C CA  . LYS A 271 ? 0.2888 0.3222 0.417  -0.0128 -0.0067 -0.0474 271 LYS A CA  
2213 C C   . LYS A 271 ? 0.2701 0.3026 0.3903 -0.0104 -0.0023 -0.0418 271 LYS A C   
2214 O O   . LYS A 271 ? 0.2322 0.2627 0.3545 -0.0146 0.0052  -0.0388 271 LYS A O   
2215 C CB  . LYS A 271 ? 0.2818 0.33   0.4263 -0.0125 -0.0115 -0.0557 271 LYS A CB  
2216 C CG  . LYS A 271 ? 0.3629 0.4124 0.5172 -0.0171 -0.0152 -0.0626 271 LYS A CG  
2217 C CD  . LYS A 271 ? 0.3986 0.4659 0.5692 -0.0163 -0.0214 -0.0711 271 LYS A CD  
2218 C CE  . LYS A 271 ? 0.5981 0.6714 0.7875 -0.0254 -0.0194 -0.0774 271 LYS A CE  
2219 N NZ  . LYS A 271 ? 0.6639 0.728  0.8505 -0.0291 -0.023  -0.0818 271 LYS A NZ  
2220 N N   . ARG A 272 ? 0.2513 0.2841 0.3611 -0.0038 -0.0066 -0.0408 272 ARG A N   
2221 C CA  . ARG A 272 ? 0.2482 0.2779 0.3486 -0.0014 -0.003  -0.0364 272 ARG A CA  
2222 C C   . ARG A 272 ? 0.2451 0.2639 0.3332 -0.005  0.0022  -0.0297 272 ARG A C   
2223 O O   . ARG A 272 ? 0.258  0.2747 0.3439 -0.0072 0.0084  -0.027  272 ARG A O   
2224 C CB  . ARG A 272 ? 0.2673 0.2965 0.3574 0.0056  -0.0089 -0.0365 272 ARG A CB  
2225 C CG  . ARG A 272 ? 0.2797 0.3198 0.3806 0.0107  -0.0131 -0.0416 272 ARG A CG  
2226 C CD  . ARG A 272 ? 0.278  0.3158 0.3677 0.0183  -0.0191 -0.0412 272 ARG A CD  
2227 N NE  . ARG A 272 ? 0.2642 0.3132 0.3652 0.0245  -0.0231 -0.0455 272 ARG A NE  
2228 C CZ  . ARG A 272 ? 0.3009 0.3486 0.3935 0.0327  -0.0291 -0.0453 272 ARG A CZ  
2229 N NH1 . ARG A 272 ? 0.3034 0.3417 0.3788 0.0346  -0.0328 -0.0425 272 ARG A NH1 
2230 N NH2 . ARG A 272 ? 0.2872 0.3437 0.389  0.0394  -0.0315 -0.0479 272 ARG A NH2 
2231 N N   . ASN A 273 ? 0.2505 0.2633 0.3307 -0.0052 -0.0004 -0.0274 273 ASN A N   
2232 C CA  . ASN A 273 ? 0.2698 0.2745 0.3389 -0.0075 0.0029  -0.0211 273 ASN A CA  
2233 C C   . ASN A 273 ? 0.2836 0.2841 0.3576 -0.0127 0.0083  -0.0189 273 ASN A C   
2234 O O   . ASN A 273 ? 0.2557 0.2509 0.3211 -0.0148 0.0126  -0.0136 273 ASN A O   
2235 C CB  . ASN A 273 ? 0.2557 0.2573 0.3155 -0.0052 -0.0012 -0.0192 273 ASN A CB  
2236 C CG  . ASN A 273 ? 0.2875 0.2899 0.3374 -0.002  -0.0037 -0.0187 273 ASN A CG  
2237 O OD1 . ASN A 273 ? 0.2848 0.2873 0.3324 -0.0012 -0.0023 -0.019  273 ASN A OD1 
2238 N ND2 . ASN A 273 ? 0.252  0.2541 0.296  -0.0001 -0.0071 -0.0184 273 ASN A ND2 
2239 N N   . LEU A 274 ? 0.2371 0.2391 0.3234 -0.0151 0.0081  -0.0228 274 LEU A N   
2240 C CA  . LEU A 274 ? 0.2808 0.2774 0.3723 -0.0209 0.0143  -0.0207 274 LEU A CA  
2241 C C   . LEU A 274 ? 0.2687 0.2694 0.3641 -0.0241 0.0212  -0.0202 274 LEU A C   
2242 O O   . LEU A 274 ? 0.2968 0.2902 0.3867 -0.0281 0.0277  -0.0151 274 LEU A O   
2243 C CB  . LEU A 274 ? 0.2659 0.2627 0.3702 -0.0237 0.0126  -0.0262 274 LEU A CB  
2244 C CG  . LEU A 274 ? 0.2975 0.2853 0.3956 -0.0213 0.0087  -0.0252 274 LEU A CG  
2245 C CD1 . LEU A 274 ? 0.2951 0.285  0.4046 -0.0227 0.0051  -0.0333 274 LEU A CD1 
2246 C CD2 . LEU A 274 ? 0.2983 0.2726 0.3893 -0.0236 0.0136  -0.018  274 LEU A CD2 
2247 N N   . SER A 275 ? 0.2352 0.247  0.3388 -0.0218 0.0202  -0.0252 275 SER A N   
2248 C CA  . SER A 275 ? 0.2538 0.2705 0.3609 -0.0232 0.0271  -0.0253 275 SER A CA  
2249 C C   . SER A 275 ? 0.2497 0.2579 0.3386 -0.0223 0.0306  -0.0193 275 SER A C   
2250 O O   . SER A 275 ? 0.2762 0.2812 0.3618 -0.0263 0.0386  -0.0164 275 SER A O   
2251 C CB  . SER A 275 ? 0.2576 0.2874 0.3753 -0.0182 0.0245  -0.0314 275 SER A CB  
2252 O OG  . SER A 275 ? 0.3694 0.4095 0.5041 -0.0187 0.0197  -0.0379 275 SER A OG  
2253 N N   . PHE A 276 ? 0.2457 0.251  0.3228 -0.0176 0.0248  -0.018  276 PHE A N   
2254 C CA  . PHE A 276 ? 0.2628 0.2607 0.3226 -0.0175 0.0269  -0.0133 276 PHE A CA  
2255 C C   . PHE A 276 ? 0.2906 0.2799 0.3411 -0.0216 0.0295  -0.0071 276 PHE A C   
2256 O O   . PHE A 276 ? 0.2764 0.2612 0.3177 -0.0243 0.0352  -0.0038 276 PHE A O   
2257 C CB  . PHE A 276 ? 0.2843 0.2807 0.3342 -0.0131 0.0206  -0.0133 276 PHE A CB  
2258 C CG  . PHE A 276 ? 0.332  0.3215 0.3654 -0.0144 0.0232  -0.0098 276 PHE A CG  
2259 C CD1 . PHE A 276 ? 0.38   0.3644 0.4022 -0.0169 0.0218  -0.0048 276 PHE A CD1 
2260 C CD2 . PHE A 276 ? 0.3987 0.3871 0.4286 -0.0134 0.0278  -0.0119 276 PHE A CD2 
2261 C CE1 . PHE A 276 ? 0.3635 0.3426 0.3705 -0.019  0.0237  -0.0023 276 PHE A CE1 
2262 C CE2 . PHE A 276 ? 0.4219 0.4029 0.4358 -0.0156 0.0306  -0.0096 276 PHE A CE2 
2263 C CZ  . PHE A 276 ? 0.3683 0.345  0.3706 -0.0188 0.0281  -0.005  276 PHE A CZ  
2264 N N   . LEU A 277 ? 0.2851 0.2718 0.3374 -0.0215 0.0254  -0.0055 277 LEU A N   
2265 C CA  . LEU A 277 ? 0.3059 0.2837 0.3494 -0.0237 0.0268  0.0009  277 LEU A CA  
2266 C C   . LEU A 277 ? 0.2915 0.2643 0.3355 -0.029  0.0354  0.0036  277 LEU A C   
2267 O O   . LEU A 277 ? 0.3111 0.2771 0.3412 -0.0307 0.0388  0.0093  277 LEU A O   
2268 C CB  . LEU A 277 ? 0.2892 0.2646 0.3374 -0.0217 0.0218  0.0009  277 LEU A CB  
2269 C CG  . LEU A 277 ? 0.3293 0.2943 0.3697 -0.0224 0.0228  0.0078  277 LEU A CG  
2270 C CD1 . LEU A 277 ? 0.3356 0.3001 0.3617 -0.0196 0.0191  0.0129  277 LEU A CD1 
2271 C CD2 . LEU A 277 ? 0.3698 0.3312 0.4183 -0.0207 0.0198  0.0061  277 LEU A CD2 
2272 N N   . ASN A 278 ? 0.2895 0.266  0.3491 -0.032  0.0389  -0.0006 278 ASN A N   
2273 C CA  . ASN A 278 ? 0.295  0.2674 0.3574 -0.0384 0.0482  0.0015  278 ASN A CA  
2274 C C   . ASN A 278 ? 0.3257 0.3012 0.3821 -0.0396 0.0553  0.0017  278 ASN A C   
2275 O O   . ASN A 278 ? 0.3471 0.3146 0.3927 -0.0436 0.0626  0.007   278 ASN A O   
2276 C CB  . ASN A 278 ? 0.3062 0.283  0.3883 -0.0425 0.0499  -0.0038 278 ASN A CB  
2277 C CG  . ASN A 278 ? 0.3443 0.3115 0.4274 -0.0429 0.0459  -0.0024 278 ASN A CG  
2278 O OD1 . ASN A 278 ? 0.3438 0.297  0.4175 -0.0454 0.0495  0.0043  278 ASN A OD1 
2279 N ND2 . ASN A 278 ? 0.3496 0.3225 0.4426 -0.04   0.0386  -0.0086 278 ASN A ND2 
2280 N N   . ASN A 279 ? 0.3038 0.2887 0.3636 -0.0356 0.0532  -0.0034 279 ASN A N   
2281 C CA  . ASN A 279 ? 0.3229 0.3089 0.3752 -0.0356 0.0598  -0.0038 279 ASN A CA  
2282 C C   . ASN A 279 ? 0.3525 0.3278 0.3811 -0.0355 0.0592  0.0023  279 ASN A C   
2283 O O   . ASN A 279 ? 0.3425 0.3128 0.3603 -0.0388 0.067   0.0052  279 ASN A O   
2284 C CB  . ASN A 279 ? 0.3007 0.2969 0.3612 -0.0301 0.0573  -0.0106 279 ASN A CB  
2285 C CG  . ASN A 279 ? 0.3242 0.3338 0.4081 -0.0305 0.0601  -0.0169 279 ASN A CG  
2286 O OD1 . ASN A 279 ? 0.3049 0.3171 0.3981 -0.0364 0.0678  -0.0168 279 ASN A OD1 
2287 N ND2 . ASN A 279 ? 0.2927 0.3116 0.3865 -0.0244 0.0543  -0.0224 279 ASN A ND2 
2288 N N   . PHE A 280 ? 0.3412 0.3143 0.3621 -0.032  0.0503  0.0038  280 PHE A N   
2289 C CA  . PHE A 280 ? 0.339  0.3051 0.3395 -0.032  0.048   0.0083  280 PHE A CA  
2290 C C   . PHE A 280 ? 0.3792 0.3363 0.3687 -0.0354 0.0511  0.0158  280 PHE A C   
2291 O O   . PHE A 280 ? 0.3808 0.3325 0.3531 -0.0371 0.0537  0.0191  280 PHE A O   
2292 C CB  . PHE A 280 ? 0.363  0.3311 0.3609 -0.0283 0.0383  0.008   280 PHE A CB  
2293 C CG  . PHE A 280 ? 0.3699 0.3338 0.3487 -0.0292 0.0356  0.0113  280 PHE A CG  
2294 C CD1 . PHE A 280 ? 0.3979 0.3605 0.3673 -0.0297 0.0374  0.0081  280 PHE A CD1 
2295 C CD2 . PHE A 280 ? 0.4216 0.3824 0.3918 -0.0294 0.0313  0.0174  280 PHE A CD2 
2296 C CE1 . PHE A 280 ? 0.449  0.4078 0.4007 -0.0318 0.0348  0.0102  280 PHE A CE1 
2297 C CE2 . PHE A 280 ? 0.4267 0.3857 0.3801 -0.0306 0.0281  0.0199  280 PHE A CE2 
2298 C CZ  . PHE A 280 ? 0.4271 0.3854 0.3714 -0.0325 0.0297  0.0159  280 PHE A CZ  
2299 N N   . TRP A 281 ? 0.3379 0.292  0.3361 -0.0366 0.0514  0.0184  281 TRP A N   
2300 C CA  . TRP A 281 ? 0.4005 0.3433 0.3872 -0.039  0.0541  0.0264  281 TRP A CA  
2301 C C   . TRP A 281 ? 0.3939 0.3322 0.3825 -0.0449 0.0658  0.0276  281 TRP A C   
2302 O O   . TRP A 281 ? 0.4362 0.363  0.4153 -0.0475 0.0694  0.0348  281 TRP A O   
2303 C CB  . TRP A 281 ? 0.3697 0.3084 0.3619 -0.0363 0.0478  0.0292  281 TRP A CB  
2304 C CG  . TRP A 281 ? 0.3801 0.3223 0.3664 -0.0308 0.0377  0.0302  281 TRP A CG  
2305 C CD1 . TRP A 281 ? 0.3846 0.3362 0.3797 -0.0275 0.0315  0.0246  281 TRP A CD1 
2306 C CD2 . TRP A 281 ? 0.3879 0.3254 0.3584 -0.0282 0.033   0.0372  281 TRP A CD2 
2307 N NE1 . TRP A 281 ? 0.3947 0.3484 0.3817 -0.024  0.0243  0.0273  281 TRP A NE1 
2308 C CE2 . TRP A 281 ? 0.3881 0.3344 0.3609 -0.0241 0.0244  0.0347  281 TRP A CE2 
2309 C CE3 . TRP A 281 ? 0.4655 0.3923 0.42   -0.0289 0.035   0.0456  281 TRP A CE3 
2310 C CZ2 . TRP A 281 ? 0.4487 0.3964 0.411  -0.0207 0.0175  0.0395  281 TRP A CZ2 
2311 C CZ3 . TRP A 281 ? 0.5467 0.474  0.4892 -0.0246 0.0272  0.0507  281 TRP A CZ3 
2312 C CH2 . TRP A 281 ? 0.4789 0.4177 0.4263 -0.0208 0.0185  0.0474  281 TRP A CH2 
2313 N N   . ASN A 282 ? 0.3877 0.3353 0.3891 -0.0469 0.0719  0.0209  282 ASN A N   
2314 C CA  . ASN A 282 ? 0.4155 0.363  0.4223 -0.053  0.0841  0.0205  282 ASN A CA  
2315 C C   . ASN A 282 ? 0.4678 0.4091 0.4849 -0.0579 0.0872  0.0231  282 ASN A C   
2316 O O   . ASN A 282 ? 0.4306 0.3611 0.4386 -0.0632 0.0954  0.0292  282 ASN A O   
2317 C CB  . ASN A 282 ? 0.4904 0.4303 0.475  -0.0552 0.0915  0.0252  282 ASN A CB  
2318 C CG  . ASN A 282 ? 0.548  0.4915 0.5391 -0.0609 0.1054  0.0229  282 ASN A CG  
2319 O OD1 . ASN A 282 ? 0.4976 0.4523 0.5122 -0.0628 0.109   0.0167  282 ASN A OD1 
2320 N ND2 . ASN A 282 ? 0.5978 0.5325 0.5683 -0.0639 0.1136  0.0278  282 ASN A ND2 
2321 N N   . LYS A 283 ? 0.4333 0.3804 0.4683 -0.0564 0.0807  0.0183  283 LYS A N   
2322 C CA  . LYS A 283 ? 0.4686 0.4095 0.5147 -0.0613 0.0827  0.019   283 LYS A CA  
2323 C C   . LYS A 283 ? 0.5092 0.4655 0.5811 -0.0649 0.0854  0.0095  283 LYS A C   
2324 O O   . LYS A 283 ? 0.4439 0.4151 0.5246 -0.0608 0.0825  0.003   283 LYS A O   
2325 C CB  . LYS A 283 ? 0.5197 0.4545 0.5655 -0.0563 0.0721  0.02    283 LYS A CB  
2326 C CG  . LYS A 283 ? 0.5425 0.4658 0.5671 -0.0509 0.0664  0.0283  283 LYS A CG  
2327 C CD  . LYS A 283 ? 0.6443 0.5509 0.65   -0.0537 0.0725  0.0385  283 LYS A CD  
2328 C CE  . LYS A 283 ? 0.7624 0.6599 0.7521 -0.0466 0.064   0.0457  283 LYS A CE  
2329 N NZ  . LYS A 283 ? 0.8672 0.7519 0.8605 -0.045  0.0615  0.0487  283 LYS A NZ  
2330 N N   . GLU A 284 ? 0.519  0.4707 0.6026 -0.072  0.0898  0.0089  284 GLU A N   
2331 C CA  . GLU A 284 ? 0.5835 0.5505 0.6934 -0.0767 0.0914  -0.0005 284 GLU A CA  
2332 C C   . GLU A 284 ? 0.4671 0.444  0.5867 -0.0696 0.0783  -0.0074 284 GLU A C   
2333 O O   . GLU A 284 ? 0.4154 0.3828 0.526  -0.0648 0.07    -0.0051 284 GLU A O   
2334 C CB  . GLU A 284 ? 0.6624 0.6196 0.78   -0.0877 0.1     0.001   284 GLU A CB  
2335 C CG  . GLU A 284 ? 0.8761 0.849  1.0226 -0.0941 0.1002  -0.0094 284 GLU A CG  
2336 C CD  . GLU A 284 ? 0.9878 0.9597 1.1429 -0.0918 0.0887  -0.015  284 GLU A CD  
2337 O OE1 . GLU A 284 ? 0.9966 0.9529 1.1359 -0.0859 0.0819  -0.0102 284 GLU A OE1 
2338 O OE2 . GLU A 284 ? 0.8219 0.8101 1.0003 -0.0955 0.0864  -0.0249 284 GLU A OE2 
2339 N N   . ASN A 285 ? 0.3917 0.3886 0.5287 -0.0679 0.0768  -0.0158 285 ASN A N   
2340 C CA  . ASN A 285 ? 0.338  0.3452 0.4795 -0.0595 0.0651  -0.0214 285 ASN A CA  
2341 C C   . ASN A 285 ? 0.3201 0.3441 0.4869 -0.0619 0.0618  -0.0313 285 ASN A C   
2342 O O   . ASN A 285 ? 0.2994 0.3407 0.4799 -0.0607 0.0639  -0.0365 285 ASN A O   
2343 C CB  . ASN A 285 ? 0.3193 0.3331 0.4525 -0.0525 0.065   -0.021  285 ASN A CB  
2344 C CG  . ASN A 285 ? 0.3066 0.3247 0.4366 -0.0435 0.0534  -0.0238 285 ASN A CG  
2345 O OD1 . ASN A 285 ? 0.2697 0.289  0.4057 -0.042  0.0453  -0.0272 285 ASN A OD1 
2346 N ND2 . ASN A 285 ? 0.318  0.335  0.435  -0.038  0.0531  -0.0217 285 ASN A ND2 
2347 N N   . GLU A 286 ? 0.2951 0.315  0.4672 -0.0636 0.0553  -0.0346 286 GLU A N   
2348 C CA  . GLU A 286 ? 0.3219 0.3575 0.5166 -0.0664 0.0507  -0.0446 286 GLU A CA  
2349 C C   . GLU A 286 ? 0.2519 0.2997 0.4481 -0.0563 0.0387  -0.0498 286 GLU A C   
2350 O O   . GLU A 286 ? 0.2504 0.3112 0.4631 -0.0573 0.0326  -0.0583 286 GLU A O   
2351 C CB  . GLU A 286 ? 0.3454 0.3689 0.5438 -0.0739 0.0499  -0.0464 286 GLU A CB  
2352 C CG  . GLU A 286 ? 0.4215 0.4328 0.6062 -0.0673 0.0403  -0.0456 286 GLU A CG  
2353 C CD  . GLU A 286 ? 0.5638 0.5611 0.7516 -0.0741 0.0401  -0.0481 286 GLU A CD  
2354 O OE1 . GLU A 286 ? 0.5346 0.5377 0.7313 -0.0739 0.0322  -0.0567 286 GLU A OE1 
2355 O OE2 . GLU A 286 ? 0.6659 0.645  0.8451 -0.0791 0.0478  -0.0412 286 GLU A OE2 
2356 N N   . TRP A 287 ? 0.2562 0.3001 0.4356 -0.0473 0.0355  -0.0452 287 TRP A N   
2357 C CA  . TRP A 287 ? 0.2655 0.3142 0.4409 -0.0385 0.0243  -0.0484 287 TRP A CA  
2358 C C   . TRP A 287 ? 0.2532 0.317  0.434  -0.0311 0.0217  -0.0515 287 TRP A C   
2359 O O   . TRP A 287 ? 0.2668 0.3336 0.4424 -0.0233 0.0129  -0.0533 287 TRP A O   
2360 C CB  . TRP A 287 ? 0.2551 0.2877 0.408  -0.034  0.0217  -0.0415 287 TRP A CB  
2361 C CG  . TRP A 287 ? 0.2884 0.306  0.4359 -0.0387 0.0231  -0.0385 287 TRP A CG  
2362 C CD1 . TRP A 287 ? 0.3383 0.3419 0.4756 -0.0425 0.0303  -0.0308 287 TRP A CD1 
2363 C CD2 . TRP A 287 ? 0.2953 0.3093 0.4468 -0.0397 0.0173  -0.0432 287 TRP A CD2 
2364 N NE1 . TRP A 287 ? 0.3623 0.3531 0.4973 -0.045  0.0293  -0.03   287 TRP A NE1 
2365 C CE2 . TRP A 287 ? 0.3079 0.3044 0.4517 -0.0436 0.0218  -0.038  287 TRP A CE2 
2366 C CE3 . TRP A 287 ? 0.2961 0.319  0.4557 -0.0375 0.0089  -0.0515 287 TRP A CE3 
2367 C CZ2 . TRP A 287 ? 0.362  0.3491 0.5067 -0.0449 0.0184  -0.0412 287 TRP A CZ2 
2368 C CZ3 . TRP A 287 ? 0.3404 0.3546 0.4999 -0.0394 0.0055  -0.0551 287 TRP A CZ3 
2369 C CH2 . TRP A 287 ? 0.3282 0.3246 0.4811 -0.0431 0.0105  -0.0503 287 TRP A CH2 
2370 N N   . ILE A 288 ? 0.2205 0.2917 0.4087 -0.0329 0.03    -0.0511 288 ILE A N   
2371 C CA  . ILE A 288 ? 0.2209 0.3016 0.4098 -0.0247 0.0298  -0.0523 288 ILE A CA  
2372 C C   . ILE A 288 ? 0.2147 0.3148 0.4225 -0.0199 0.0214  -0.0605 288 ILE A C   
2373 O O   . ILE A 288 ? 0.1953 0.3078 0.423  -0.0259 0.0213  -0.0664 288 ILE A O   
2374 C CB  . ILE A 288 ? 0.2318 0.3148 0.4237 -0.0281 0.0424  -0.0503 288 ILE A CB  
2375 C CG1 . ILE A 288 ? 0.3044 0.3675 0.4724 -0.0301 0.0477  -0.0417 288 ILE A CG1 
2376 C CG2 . ILE A 288 ? 0.2202 0.3158 0.4182 -0.0191 0.0425  -0.0536 288 ILE A CG2 
2377 C CD1 . ILE A 288 ? 0.3389 0.3999 0.5044 -0.035  0.0606  -0.0388 288 ILE A CD1 
2378 N N   . ASN A 289 ? 0.2048 0.3077 0.4062 -0.0092 0.0148  -0.0609 289 ASN A N   
2379 C CA  . ASN A 289 ? 0.2116 0.333  0.4289 -0.0024 0.0062  -0.0678 289 ASN A CA  
2380 C C   . ASN A 289 ? 0.2086 0.3421 0.4359 0.0038  0.0113  -0.0693 289 ASN A C   
2381 O O   . ASN A 289 ? 0.234  0.3596 0.4471 0.0129  0.0105  -0.066  289 ASN A O   
2382 C CB  . ASN A 289 ? 0.2414 0.3562 0.4438 0.0054  -0.0055 -0.0672 289 ASN A CB  
2383 C CG  . ASN A 289 ? 0.2488 0.3824 0.4664 0.0118  -0.0159 -0.0743 289 ASN A CG  
2384 O OD1 . ASN A 289 ? 0.2254 0.3777 0.4637 0.0135  -0.0146 -0.0791 289 ASN A OD1 
2385 N ND2 . ASN A 289 ? 0.3002 0.4298 0.5072 0.0162  -0.0264 -0.0751 289 ASN A ND2 
2386 N N   . TYR A 290 ? 0.1769 0.3292 0.4292 -0.0012 0.017   -0.0747 290 TYR A N   
2387 C CA  . TYR A 290 ? 0.2024 0.3685 0.4677 0.004   0.024   -0.0769 290 TYR A CA  
2388 C C   . TYR A 290 ? 0.236  0.4194 0.5133 0.0168  0.0136  -0.0821 290 TYR A C   
2389 O O   . TYR A 290 ? 0.2658 0.456  0.5479 0.0253  0.0177  -0.0828 290 TYR A O   
2390 C CB  . TYR A 290 ? 0.2161 0.3987 0.506  -0.0067 0.0343  -0.0812 290 TYR A CB  
2391 C CG  . TYR A 290 ? 0.2281 0.3925 0.5049 -0.0187 0.0457  -0.0752 290 TYR A CG  
2392 C CD1 . TYR A 290 ? 0.2242 0.3787 0.4884 -0.0188 0.0578  -0.0702 290 TYR A CD1 
2393 C CD2 . TYR A 290 ? 0.2469 0.4031 0.5229 -0.0294 0.0444  -0.0745 290 TYR A CD2 
2394 C CE1 . TYR A 290 ? 0.2528 0.3902 0.5029 -0.0288 0.0674  -0.064  290 TYR A CE1 
2395 C CE2 . TYR A 290 ? 0.2425 0.381  0.5058 -0.0392 0.0545  -0.0682 290 TYR A CE2 
2396 C CZ  . TYR A 290 ? 0.2628 0.3928 0.5134 -0.039  0.0659  -0.0628 290 TYR A CZ  
2397 O OH  . TYR A 290 ? 0.2448 0.3563 0.4797 -0.0473 0.0742  -0.0558 290 TYR A OH  
2398 N N   . ASP A 291 ? 0.2723 0.4624 0.5538 0.0188  0.0005  -0.0857 291 ASP A N   
2399 C CA  . ASP A 291 ? 0.3222 0.529  0.6139 0.0315  -0.011  -0.0902 291 ASP A CA  
2400 C C   . ASP A 291 ? 0.3129 0.5021 0.5788 0.0443  -0.0181 -0.0847 291 ASP A C   
2401 O O   . ASP A 291 ? 0.3515 0.5506 0.6228 0.0572  -0.0241 -0.0864 291 ASP A O   
2402 C CB  . ASP A 291 ? 0.321  0.5431 0.6269 0.028   -0.0227 -0.0971 291 ASP A CB  
2403 C CG  . ASP A 291 ? 0.398  0.6396 0.7323 0.0149  -0.0174 -0.104  291 ASP A CG  
2404 O OD1 . ASP A 291 ? 0.3767 0.6378 0.7332 0.0155  -0.0104 -0.1075 291 ASP A OD1 
2405 O OD2 . ASP A 291 ? 0.5714 0.8072 0.9044 0.004   -0.0194 -0.1059 291 ASP A OD2 
2406 N N   . SER A 292 ? 0.2919 0.4567 0.5317 0.0408  -0.0177 -0.0783 292 SER A N   
2407 C CA  . SER A 292 ? 0.3147 0.4616 0.5291 0.05    -0.0244 -0.0731 292 SER A CA  
2408 C C   . SER A 292 ? 0.3407 0.4792 0.5461 0.0599  -0.0193 -0.0696 292 SER A C   
2409 O O   . SER A 292 ? 0.2771 0.412  0.4836 0.0562  -0.0077 -0.0683 292 SER A O   
2410 C CB  . SER A 292 ? 0.2917 0.4173 0.4843 0.0422  -0.0224 -0.0676 292 SER A CB  
2411 O OG  . SER A 292 ? 0.2934 0.4008 0.4607 0.0489  -0.0267 -0.0621 292 SER A OG  
2412 N N   . ASP A 293 ? 0.3074 0.4399 0.501  0.0723  -0.0277 -0.0676 293 ASP A N   
2413 C CA  . ASP A 293 ? 0.3458 0.4632 0.5248 0.0815  -0.0233 -0.0635 293 ASP A CA  
2414 C C   . ASP A 293 ? 0.3033 0.3928 0.4511 0.0797  -0.0232 -0.0563 293 ASP A C   
2415 O O   . ASP A 293 ? 0.3661 0.4399 0.4982 0.0878  -0.0221 -0.0527 293 ASP A O   
2416 C CB  . ASP A 293 ? 0.3926 0.5224 0.582  0.0971  -0.0309 -0.0663 293 ASP A CB  
2417 C CG  . ASP A 293 ? 0.5193 0.6472 0.6983 0.1049  -0.0454 -0.065  293 ASP A CG  
2418 O OD1 . ASP A 293 ? 0.477  0.5943 0.641  0.0979  -0.049  -0.0624 293 ASP A OD1 
2419 O OD2 . ASP A 293 ? 0.7115 0.8483 0.8966 0.119   -0.0532 -0.0663 293 ASP A OD2 
2420 N N   . ALA A 294 ? 0.2805 0.3633 0.4193 0.0694  -0.024  -0.0543 294 ALA A N   
2421 C CA  . ALA A 294 ? 0.3065 0.3658 0.4189 0.0659  -0.022  -0.0479 294 ALA A CA  
2422 C C   . ALA A 294 ? 0.3136 0.3627 0.4203 0.0596  -0.0101 -0.0456 294 ALA A C   
2423 O O   . ALA A 294 ? 0.2507 0.3091 0.3708 0.0525  -0.0034 -0.0479 294 ALA A O   
2424 C CB  . ALA A 294 ? 0.2845 0.3418 0.3907 0.0583  -0.0265 -0.047  294 ALA A CB  
2425 N N   . VAL A 295 ? 0.3057 0.3351 0.3917 0.0622  -0.0071 -0.0414 295 VAL A N   
2426 C CA  . VAL A 295 ? 0.3134 0.3318 0.3907 0.0562  0.0032  -0.0397 295 VAL A CA  
2427 C C   . VAL A 295 ? 0.2855 0.3048 0.3626 0.0437  0.0071  -0.0382 295 VAL A C   
2428 O O   . VAL A 295 ? 0.2537 0.2762 0.3365 0.0387  0.0153  -0.0392 295 VAL A O   
2429 C CB  . VAL A 295 ? 0.3643 0.3595 0.4171 0.0586  0.0044  -0.0355 295 VAL A CB  
2430 C CG1 . VAL A 295 ? 0.3751 0.3591 0.4168 0.0503  0.0137  -0.0342 295 VAL A CG1 
2431 C CG2 . VAL A 295 ? 0.351  0.3424 0.4036 0.0719  0.0027  -0.0368 295 VAL A CG2 
2432 N N   . THR A 296 ? 0.2602 0.2773 0.3311 0.0393  0.0015  -0.0359 296 THR A N   
2433 C CA  . THR A 296 ? 0.2692 0.2856 0.3389 0.0289  0.0049  -0.0339 296 THR A CA  
2434 C C   . THR A 296 ? 0.2812 0.3125 0.3714 0.0245  0.0082  -0.0374 296 THR A C   
2435 O O   . THR A 296 ? 0.2643 0.2933 0.3537 0.0171  0.0146  -0.0356 296 THR A O   
2436 C CB  . THR A 296 ? 0.281  0.293  0.3417 0.0262  -0.0012 -0.0314 296 THR A CB  
2437 O OG1 . THR A 296 ? 0.301  0.3099 0.3582 0.0177  0.0026  -0.0288 296 THR A OG1 
2438 C CG2 . THR A 296 ? 0.2847 0.3082 0.3572 0.0287  -0.0088 -0.0349 296 THR A CG2 
2439 N N   . ASP A 297 ? 0.2438 0.2902 0.3521 0.0288  0.0036  -0.0423 297 ASP A N   
2440 C CA  . ASP A 297 ? 0.2499 0.3115 0.3794 0.0237  0.0067  -0.0463 297 ASP A CA  
2441 C C   . ASP A 297 ? 0.229  0.2954 0.3666 0.0235  0.0167  -0.0477 297 ASP A C   
2442 O O   . ASP A 297 ? 0.2291 0.2995 0.3748 0.0156  0.0242  -0.0479 297 ASP A O   
2443 C CB  . ASP A 297 ? 0.2384 0.3157 0.3843 0.0276  -0.0022 -0.0518 297 ASP A CB  
2444 C CG  . ASP A 297 ? 0.2433 0.3158 0.3806 0.0266  -0.011  -0.0513 297 ASP A CG  
2445 O OD1 . ASP A 297 ? 0.2373 0.2998 0.3651 0.0197  -0.0087 -0.048  297 ASP A OD1 
2446 O OD2 . ASP A 297 ? 0.2384 0.3187 0.3796 0.0329  -0.0201 -0.0546 297 ASP A OD2 
2447 N N   . MET A 298 ? 0.2386 0.3038 0.3734 0.0325  0.0172  -0.0486 298 MET A N   
2448 C CA  . MET A 298 ? 0.2355 0.3056 0.3779 0.0344  0.027   -0.0508 298 MET A CA  
2449 C C   . MET A 298 ? 0.2413 0.2962 0.3664 0.0269  0.0366  -0.0466 298 MET A C   
2450 O O   . MET A 298 ? 0.2708 0.3311 0.4031 0.0227  0.0466  -0.048  298 MET A O   
2451 C CB  . MET A 298 ? 0.2255 0.2951 0.3668 0.0475  0.0245  -0.0527 298 MET A CB  
2452 C CG  . MET A 298 ? 0.2763 0.3632 0.4355 0.0556  0.0144  -0.0569 298 MET A CG  
2453 S SD  . MET A 298 ? 0.3437 0.4247 0.4958 0.0729  0.0084  -0.0569 298 MET A SD  
2454 C CE  . MET A 298 ? 0.3474 0.4364 0.5126 0.0789  0.0202  -0.0611 298 MET A CE  
2455 N N   . GLN A 299 ? 0.2808 0.3184 0.3839 0.0249  0.0334  -0.0418 299 GLN A N   
2456 C CA  . GLN A 299 ? 0.2903 0.3142 0.3757 0.0174  0.0395  -0.0376 299 GLN A CA  
2457 C C   . GLN A 299 ? 0.3083 0.3371 0.4004 0.0078  0.0441  -0.036  299 GLN A C   
2458 O O   . GLN A 299 ? 0.2601 0.2845 0.3458 0.0031  0.0529  -0.0345 299 GLN A O   
2459 C CB  . GLN A 299 ? 0.2813 0.2899 0.346  0.0162  0.0339  -0.0332 299 GLN A CB  
2460 C CG  . GLN A 299 ? 0.2985 0.2956 0.3501 0.0232  0.0324  -0.0335 299 GLN A CG  
2461 C CD  . GLN A 299 ? 0.3023 0.2855 0.3348 0.0207  0.0272  -0.0294 299 GLN A CD  
2462 O OE1 . GLN A 299 ? 0.343  0.3277 0.3742 0.0157  0.023   -0.0267 299 GLN A OE1 
2463 N NE2 . GLN A 299 ? 0.3368 0.3059 0.3543 0.0239  0.028   -0.0291 299 GLN A NE2 
2464 N N   . GLU A 300 ? 0.2719 0.3091 0.3765 0.0051  0.0387  -0.0366 300 GLU A N   
2465 C CA  . GLU A 300 ? 0.2743 0.3128 0.3841 -0.004  0.043   -0.0348 300 GLU A CA  
2466 C C   . GLU A 300 ? 0.281  0.3317 0.4082 -0.0072 0.0523  -0.0381 300 GLU A C   
2467 O O   . GLU A 300 ? 0.2741 0.3201 0.3977 -0.015  0.0602  -0.0349 300 GLU A O   
2468 C CB  . GLU A 300 ? 0.3063 0.347  0.4221 -0.0062 0.0349  -0.0349 300 GLU A CB  
2469 C CG  . GLU A 300 ? 0.3546 0.3836 0.4526 -0.0042 0.0278  -0.031  300 GLU A CG  
2470 C CD  . GLU A 300 ? 0.4354 0.4507 0.5129 -0.0071 0.0316  -0.0253 300 GLU A CD  
2471 O OE1 . GLU A 300 ? 0.4421 0.4534 0.5161 -0.013  0.038   -0.0221 300 GLU A OE1 
2472 O OE2 . GLU A 300 ? 0.4838 0.4921 0.5477 -0.0034 0.0283  -0.024  300 GLU A OE2 
2473 N N   . VAL A 301 ? 0.2495 0.3156 0.395  -0.0013 0.0518  -0.0442 301 VAL A N   
2474 C CA  . VAL A 301 ? 0.2512 0.3316 0.415  -0.0036 0.0615  -0.0481 301 VAL A CA  
2475 C C   . VAL A 301 ? 0.2554 0.3257 0.4038 -0.0046 0.0728  -0.0455 301 VAL A C   
2476 O O   . VAL A 301 ? 0.2505 0.323  0.4024 -0.012  0.0835  -0.0447 301 VAL A O   
2477 C CB  . VAL A 301 ? 0.2541 0.3544 0.4401 0.0052  0.0579  -0.0552 301 VAL A CB  
2478 C CG1 . VAL A 301 ? 0.2501 0.368  0.4573 0.003   0.0689  -0.0599 301 VAL A CG1 
2479 C CG2 . VAL A 301 ? 0.2606 0.3708 0.4595 0.0062  0.0455  -0.0583 301 VAL A CG2 
2480 N N   . ILE A 302 ? 0.2514 0.3101 0.3821 0.0024  0.0706  -0.0445 302 ILE A N   
2481 C CA  . ILE A 302 ? 0.2734 0.3208 0.3867 0.0021  0.0802  -0.0431 302 ILE A CA  
2482 C C   . ILE A 302 ? 0.2469 0.2809 0.3419 -0.0078 0.084   -0.0367 302 ILE A C   
2483 O O   . ILE A 302 ? 0.2825 0.3148 0.3725 -0.0126 0.0951  -0.0358 302 ILE A O   
2484 C CB  . ILE A 302 ? 0.2963 0.3318 0.394  0.011   0.0757  -0.0437 302 ILE A CB  
2485 C CG1 . ILE A 302 ? 0.288  0.3353 0.402  0.0222  0.0747  -0.0496 302 ILE A CG1 
2486 C CG2 . ILE A 302 ? 0.3265 0.3459 0.4005 0.0085  0.0836  -0.0419 302 ILE A CG2 
2487 C CD1 . ILE A 302 ? 0.3135 0.3483 0.4143 0.0312  0.0668  -0.0493 302 ILE A CD1 
2488 N N   . PHE A 303 ? 0.2598 0.2854 0.3452 -0.0103 0.0753  -0.0323 303 PHE A N   
2489 C CA  . PHE A 303 ? 0.2922 0.3053 0.36   -0.0178 0.077   -0.0258 303 PHE A CA  
2490 C C   . PHE A 303 ? 0.3191 0.337  0.3968 -0.0256 0.0848  -0.0241 303 PHE A C   
2491 O O   . PHE A 303 ? 0.3038 0.3131 0.3673 -0.0309 0.0926  -0.0199 303 PHE A O   
2492 C CB  . PHE A 303 ? 0.3156 0.3214 0.3746 -0.0178 0.0659  -0.022  303 PHE A CB  
2493 C CG  . PHE A 303 ? 0.3493 0.3413 0.3854 -0.0219 0.065   -0.0158 303 PHE A CG  
2494 C CD1 . PHE A 303 ? 0.3641 0.3494 0.3869 -0.0268 0.0734  -0.0125 303 PHE A CD1 
2495 C CD2 . PHE A 303 ? 0.388  0.3749 0.4159 -0.0208 0.0555  -0.0131 303 PHE A CD2 
2496 C CE1 . PHE A 303 ? 0.3608 0.3351 0.363  -0.0299 0.0707  -0.0068 303 PHE A CE1 
2497 C CE2 . PHE A 303 ? 0.3715 0.3491 0.3811 -0.0241 0.0537  -0.0078 303 PHE A CE2 
2498 C CZ  . PHE A 303 ? 0.3449 0.3164 0.3418 -0.0284 0.0606  -0.0045 303 PHE A CZ  
2499 N N   . GLU A 304 ? 0.3058 0.3369 0.407  -0.0268 0.0832  -0.0275 304 GLU A N   
2500 C CA  . GLU A 304 ? 0.2971 0.333  0.4099 -0.0353 0.0921  -0.0268 304 GLU A CA  
2501 C C   . GLU A 304 ? 0.3075 0.3476 0.4208 -0.0373 0.1061  -0.0283 304 GLU A C   
2502 O O   . GLU A 304 ? 0.3066 0.34   0.4123 -0.0451 0.1156  -0.0239 304 GLU A O   
2503 C CB  . GLU A 304 ? 0.2804 0.3309 0.4194 -0.0368 0.0874  -0.0318 304 GLU A CB  
2504 C CG  . GLU A 304 ? 0.3051 0.3605 0.4579 -0.047  0.0971  -0.0317 304 GLU A CG  
2505 C CD  . GLU A 304 ? 0.3617 0.4319 0.5408 -0.0495 0.0915  -0.0379 304 GLU A CD  
2506 O OE1 . GLU A 304 ? 0.3689 0.431  0.5484 -0.0563 0.0891  -0.0356 304 GLU A OE1 
2507 O OE2 . GLU A 304 ? 0.3133 0.4029 0.5123 -0.0446 0.0895  -0.0453 304 GLU A OE2 
2508 N N   . LEU A 305 ? 0.2762 0.3272 0.3987 -0.03   0.1081  -0.0345 305 LEU A N   
2509 C CA  . LEU A 305 ? 0.3211 0.3771 0.4446 -0.0305 0.122   -0.037  305 LEU A CA  
2510 C C   . LEU A 305 ? 0.3343 0.3711 0.4266 -0.033  0.1282  -0.0316 305 LEU A C   
2511 O O   . LEU A 305 ? 0.3391 0.3745 0.4259 -0.0387 0.1412  -0.0302 305 LEU A O   
2512 C CB  . LEU A 305 ? 0.3011 0.3708 0.4391 -0.0198 0.1213  -0.0447 305 LEU A CB  
2513 C CG  . LEU A 305 ? 0.3216 0.4154 0.4934 -0.0179 0.1184  -0.051  305 LEU A CG  
2514 C CD1 . LEU A 305 ? 0.2873 0.3915 0.4695 -0.0045 0.1133  -0.0573 305 LEU A CD1 
2515 C CD2 . LEU A 305 ? 0.3228 0.4311 0.513  -0.0264 0.1321  -0.0532 305 LEU A CD2 
2516 N N   . ILE A 306 ? 0.3352 0.358  0.407  -0.0291 0.1189  -0.0289 306 ILE A N   
2517 C CA  . ILE A 306 ? 0.3806 0.386  0.4224 -0.0316 0.1219  -0.0242 306 ILE A CA  
2518 C C   . ILE A 306 ? 0.4156 0.413  0.4474 -0.0409 0.1256  -0.0166 306 ILE A C   
2519 O O   . ILE A 306 ? 0.4262 0.4172 0.4432 -0.0449 0.1361  -0.0143 306 ILE A O   
2520 C CB  . ILE A 306 ? 0.3585 0.3527 0.3835 -0.027  0.1103  -0.0232 306 ILE A CB  
2521 C CG1 . ILE A 306 ? 0.3391 0.3361 0.3684 -0.0179 0.1091  -0.03   306 ILE A CG1 
2522 C CG2 . ILE A 306 ? 0.4115 0.3894 0.4064 -0.0316 0.1116  -0.0178 306 ILE A CG2 
2523 C CD1 . ILE A 306 ? 0.3562 0.3435 0.3737 -0.014  0.0971  -0.0292 306 ILE A CD1 
2524 N N   . ASN A 307 ? 0.3816 0.3794 0.4224 -0.0438 0.1184  -0.0131 307 ASN A N   
2525 C CA  . ASN A 307 ? 0.4255 0.4143 0.4584 -0.0518 0.1221  -0.0056 307 ASN A CA  
2526 C C   . ASN A 307 ? 0.4409 0.4358 0.4845 -0.0588 0.137   -0.0062 307 ASN A C   
2527 O O   . ASN A 307 ? 0.444  0.4273 0.4721 -0.0652 0.144   0.0007  307 ASN A O   
2528 C CB  . ASN A 307 ? 0.4171 0.4042 0.4585 -0.0526 0.1115  -0.0028 307 ASN A CB  
2529 C CG  . ASN A 307 ? 0.4128 0.392  0.4396 -0.0475 0.0988  -0.0004 307 ASN A CG  
2530 O OD1 . ASN A 307 ? 0.4213 0.3924 0.427  -0.0459 0.0981  0.0018  307 ASN A OD1 
2531 N ND2 . ASN A 307 ? 0.3673 0.3491 0.4047 -0.0453 0.0887  -0.0011 307 ASN A ND2 
2532 N N   . HIS A 308 ? 0.394  0.407  0.4632 -0.0575 0.142   -0.0139 308 HIS A N   
2533 C CA  . HIS A 308 ? 0.4554 0.4777 0.5377 -0.0644 0.1572  -0.0156 308 HIS A CA  
2534 C C   . HIS A 308 ? 0.4667 0.4887 0.536  -0.0628 0.1698  -0.0176 308 HIS A C   
2535 O O   . HIS A 308 ? 0.4496 0.4812 0.5301 -0.0677 0.1837  -0.0198 308 HIS A O   
2536 C CB  . HIS A 308 ? 0.4849 0.5296 0.6034 -0.0643 0.1557  -0.0235 308 HIS A CB  
2537 C CG  . HIS A 308 ? 0.517  0.5601 0.6468 -0.0699 0.1484  -0.0213 308 HIS A CG  
2538 N ND1 . HIS A 308 ? 0.6654 0.7113 0.8077 -0.081  0.1584  -0.0202 308 HIS A ND1 
2539 C CD2 . HIS A 308 ? 0.5552 0.5932 0.6852 -0.0673 0.1345  -0.0203 308 HIS A CD2 
2540 C CE1 . HIS A 308 ? 0.6118 0.653  0.7611 -0.0848 0.1501  -0.0189 308 HIS A CE1 
2541 N NE2 . HIS A 308 ? 0.6091 0.6463 0.7513 -0.0761 0.1355  -0.0191 308 HIS A NE2 
2542 N N   . LYS A 309 ? 0.4654 0.4772 0.5124 -0.0562 0.1654  -0.0176 309 LYS A N   
2543 C CA  . LYS A 309 ? 0.5598 0.5682 0.5906 -0.0538 0.176   -0.0204 309 LYS A CA  
2544 C C   . LYS A 309 ? 0.5409 0.5687 0.596  -0.0478 0.1831  -0.0302 309 LYS A C   
2545 O O   . LYS A 309 ? 0.5406 0.5705 0.5904 -0.0477 0.197   -0.0333 309 LYS A O   
2546 C CB  . LYS A 309 ? 0.6746 0.6709 0.6835 -0.0627 0.1883  -0.0134 309 LYS A CB  
2547 C CG  . LYS A 309 ? 0.7682 0.7451 0.7521 -0.066  0.1786  -0.0035 309 LYS A CG  
2548 C CD  . LYS A 309 ? 0.8956 0.8632 0.872  -0.0756 0.1855  0.0056  309 LYS A CD  
2549 C CE  . LYS A 309 ? 1.0432 0.995  0.9858 -0.0793 0.1944  0.0116  309 LYS A CE  
2550 N NZ  . LYS A 309 ? 1.0913 1.0286 1.0058 -0.0753 0.1819  0.016   309 LYS A NZ  
2551 N N   . GLU A 310 ? 0.4392 0.4809 0.5194 -0.0416 0.1732  -0.0352 310 GLU A N   
2552 C CA  . GLU A 310 ? 0.4149 0.4771 0.5212 -0.034  0.1772  -0.0443 310 GLU A CA  
2553 C C   . GLU A 310 ? 0.4224 0.4771 0.5175 -0.0221 0.169   -0.048  310 GLU A C   
2554 O O   . GLU A 310 ? 0.3719 0.4333 0.4809 -0.0144 0.1572  -0.051  310 GLU A O   
2555 C CB  . GLU A 310 ? 0.42   0.5013 0.5592 -0.0356 0.1705  -0.0468 310 GLU A CB  
2556 C CG  . GLU A 310 ? 0.4848 0.5743 0.638  -0.0482 0.1808  -0.0446 310 GLU A CG  
2557 C CD  . GLU A 310 ? 0.5553 0.6622 0.7252 -0.051  0.1985  -0.0497 310 GLU A CD  
2558 O OE1 . GLU A 310 ? 0.586  0.702  0.7605 -0.0417 0.2037  -0.0561 310 GLU A OE1 
2559 O OE2 . GLU A 310 ? 0.6477 0.7582 0.8258 -0.0631 0.208   -0.047  310 GLU A OE2 
2560 N N   . LEU A 311 ? 0.4101 0.4486 0.4773 -0.0213 0.1748  -0.0474 311 LEU A N   
2561 C CA  . LEU A 311 ? 0.4261 0.4509 0.4759 -0.0128 0.1669  -0.0495 311 LEU A CA  
2562 C C   . LEU A 311 ? 0.4297 0.466  0.4978 -0.0005 0.1683  -0.0581 311 LEU A C   
2563 O O   . LEU A 311 ? 0.4387 0.469  0.5047 0.0077  0.1574  -0.0597 311 LEU A O   
2564 C CB  . LEU A 311 ? 0.4809 0.4854 0.4955 -0.0167 0.1729  -0.0472 311 LEU A CB  
2565 C CG  . LEU A 311 ? 0.502  0.4932 0.4954 -0.0265 0.168   -0.038  311 LEU A CG  
2566 C CD1 . LEU A 311 ? 0.5674 0.5389 0.5248 -0.0287 0.17    -0.0366 311 LEU A CD1 
2567 C CD2 . LEU A 311 ? 0.4739 0.4638 0.4728 -0.0263 0.1516  -0.0338 311 LEU A CD2 
2568 N N   . SER A 312 ? 0.4429 0.4953 0.5283 0.0012  0.1819  -0.0634 312 SER A N   
2569 C CA  . SER A 312 ? 0.4755 0.541  0.5802 0.014   0.1843  -0.0717 312 SER A CA  
2570 C C   . SER A 312 ? 0.4393 0.5214 0.5722 0.0202  0.1708  -0.073  312 SER A C   
2571 O O   . SER A 312 ? 0.4164 0.4951 0.5505 0.0318  0.1622  -0.0758 312 SER A O   
2572 C CB  . SER A 312 ? 0.5117 0.5932 0.6302 0.0135  0.2024  -0.0769 312 SER A CB  
2573 O OG  . SER A 312 ? 0.6151 0.7099 0.7535 0.0277  0.2034  -0.0849 312 SER A OG  
2574 N N   . LYS A 313 ? 0.4106 0.5082 0.5638 0.0121  0.1684  -0.0707 313 LYS A N   
2575 C CA  . LYS A 313 ? 0.4235 0.5347 0.5993 0.016   0.1542  -0.0716 313 LYS A CA  
2576 C C   . LYS A 313 ? 0.3589 0.4508 0.5152 0.019   0.1382  -0.067  313 LYS A C   
2577 O O   . LYS A 313 ? 0.3757 0.473  0.5424 0.0287  0.1273  -0.0693 313 LYS A O   
2578 C CB  . LYS A 313 ? 0.4288 0.555  0.6244 0.0041  0.1544  -0.0697 313 LYS A CB  
2579 C CG  . LYS A 313 ? 0.4843 0.6398 0.7138 0.0036  0.1647  -0.0764 313 LYS A CG  
2580 C CD  . LYS A 313 ? 0.5038 0.6742 0.7556 -0.0076 0.1613  -0.0756 313 LYS A CD  
2581 C CE  . LYS A 313 ? 0.5412 0.7086 0.7889 -0.0226 0.1759  -0.072  313 LYS A CE  
2582 N NZ  . LYS A 313 ? 0.5318 0.7244 0.806  -0.0246 0.191   -0.0784 313 LYS A NZ  
2583 N N   . ALA A 314 ? 0.3483 0.4196 0.4778 0.0104  0.1366  -0.0603 314 ALA A N   
2584 C CA  . ALA A 314 ? 0.3597 0.4138 0.4708 0.012   0.1231  -0.0561 314 ALA A CA  
2585 C C   . ALA A 314 ? 0.3742 0.417  0.4735 0.0234  0.1203  -0.0593 314 ALA A C   
2586 O O   . ALA A 314 ? 0.3327 0.3723 0.4326 0.0297  0.1087  -0.0588 314 ALA A O   
2587 C CB  . ALA A 314 ? 0.3801 0.4161 0.4652 0.0017  0.1236  -0.0492 314 ALA A CB  
2588 N N   . LEU A 315 ? 0.3828 0.4186 0.4708 0.026   0.1317  -0.0626 315 LEU A N   
2589 C CA  . LEU A 315 ? 0.426  0.4475 0.5007 0.0365  0.1307  -0.0661 315 LEU A CA  
2590 C C   . LEU A 315 ? 0.4169 0.4527 0.5155 0.0501  0.1259  -0.0708 315 LEU A C   
2591 O O   . LEU A 315 ? 0.4404 0.4639 0.5306 0.0581  0.1169  -0.0704 315 LEU A O   
2592 C CB  . LEU A 315 ? 0.4298 0.4404 0.487  0.0366  0.1446  -0.0699 315 LEU A CB  
2593 C CG  . LEU A 315 ? 0.4937 0.4836 0.532  0.0459  0.1439  -0.0736 315 LEU A CG  
2594 C CD1 . LEU A 315 ? 0.5416 0.509  0.5558 0.0426  0.1321  -0.0692 315 LEU A CD1 
2595 C CD2 . LEU A 315 ? 0.5761 0.5566 0.5976 0.0449  0.1586  -0.0782 315 LEU A CD2 
2596 N N   . GLN A 316 ? 0.4279 0.4893 0.5558 0.0526  0.1314  -0.0749 316 GLN A N   
2597 C CA  . GLN A 316 ? 0.4722 0.5504 0.6247 0.0663  0.1258  -0.0796 316 GLN A CA  
2598 C C   . GLN A 316 ? 0.3912 0.4695 0.5471 0.0681  0.1087  -0.0758 316 GLN A C   
2599 O O   . GLN A 316 ? 0.377  0.4499 0.5316 0.0804  0.1005  -0.0766 316 GLN A O   
2600 C CB  . GLN A 316 ? 0.5014 0.6112 0.6881 0.0676  0.134   -0.0852 316 GLN A CB  
2601 C CG  . GLN A 316 ? 0.6075 0.7206 0.7951 0.0709  0.1513  -0.0907 316 GLN A CG  
2602 C CD  . GLN A 316 ? 0.7486 0.8956 0.9742 0.0774  0.1575  -0.0977 316 GLN A CD  
2603 O OE1 . GLN A 316 ? 0.8071 0.9775 1.06   0.0768  0.1494  -0.0985 316 GLN A OE1 
2604 N NE2 . GLN A 316 ? 0.7919 0.9433 1.0205 0.0835  0.1724  -0.1035 316 GLN A NE2 
2605 N N   . LEU A 317 ? 0.3495 0.4308 0.5064 0.0562  0.1034  -0.0713 317 LEU A N   
2606 C CA  . LEU A 317 ? 0.3512 0.4318 0.5091 0.0574  0.088   -0.0682 317 LEU A CA  
2607 C C   . LEU A 317 ? 0.3548 0.4078 0.4829 0.0591  0.0812  -0.0636 317 LEU A C   
2608 O O   . LEU A 317 ? 0.3828 0.4327 0.5099 0.0662  0.0698  -0.0623 317 LEU A O   
2609 C CB  . LEU A 317 ? 0.3358 0.4261 0.503  0.0445  0.0855  -0.0655 317 LEU A CB  
2610 C CG  . LEU A 317 ? 0.3734 0.4927 0.5736 0.0421  0.0899  -0.0706 317 LEU A CG  
2611 C CD1 . LEU A 317 ? 0.3635 0.485  0.5666 0.0274  0.0902  -0.0673 317 LEU A CD1 
2612 C CD2 . LEU A 317 ? 0.3777 0.5171 0.6018 0.0533  0.0794  -0.0753 317 LEU A CD2 
2613 N N   . LEU A 318 ? 0.378  0.4116 0.4816 0.0518  0.0877  -0.061  318 LEU A N   
2614 C CA  . LEU A 318 ? 0.394  0.4028 0.4703 0.0514  0.0822  -0.0572 318 LEU A CA  
2615 C C   . LEU A 318 ? 0.3935 0.3914 0.4642 0.0648  0.0809  -0.0601 318 LEU A C   
2616 O O   . LEU A 318 ? 0.3793 0.3636 0.438  0.0682  0.0719  -0.0572 318 LEU A O   
2617 C CB  . LEU A 318 ? 0.4329 0.4255 0.4853 0.0409  0.089   -0.0548 318 LEU A CB  
2618 C CG  . LEU A 318 ? 0.4709 0.4421 0.4981 0.037   0.0817  -0.0506 318 LEU A CG  
2619 C CD1 . LEU A 318 ? 0.4798 0.4541 0.5089 0.0317  0.0711  -0.0454 318 LEU A CD1 
2620 C CD2 . LEU A 318 ? 0.6085 0.5656 0.6131 0.0284  0.0883  -0.0497 318 LEU A CD2 
2621 N N   . ASN A 319 ? 0.4265 0.4292 0.505  0.0724  0.0906  -0.0657 319 ASN A N   
2622 C CA  . ASN A 319 ? 0.4618 0.454  0.5366 0.087   0.0904  -0.0689 319 ASN A CA  
2623 C C   . ASN A 319 ? 0.4684 0.4699 0.558  0.0983  0.0784  -0.068  319 ASN A C   
2624 O O   . ASN A 319 ? 0.4724 0.4554 0.5481 0.107   0.0733  -0.0666 319 ASN A O   
2625 C CB  . ASN A 319 ? 0.5155 0.5168 0.602  0.0948  0.103   -0.0757 319 ASN A CB  
2626 C CG  . ASN A 319 ? 0.5306 0.5158 0.5955 0.0874  0.1153  -0.0776 319 ASN A CG  
2627 O OD1 . ASN A 319 ? 0.5956 0.5591 0.6342 0.0786  0.1133  -0.0741 319 ASN A OD1 
2628 N ND2 . ASN A 319 ? 0.5742 0.5715 0.6506 0.0907  0.1281  -0.0833 319 ASN A ND2 
2629 N N   . LYS A 320 ? 0.446  0.4745 0.5619 0.0979  0.0738  -0.0688 320 LYS A N   
2630 C CA  . LYS A 320 ? 0.4681 0.5059 0.5957 0.107   0.0607  -0.0677 320 LYS A CA  
2631 C C   . LYS A 320 ? 0.4497 0.4678 0.5552 0.1032  0.0501  -0.0612 320 LYS A C   
2632 O O   . LYS A 320 ? 0.4862 0.4996 0.5893 0.1137  0.0407  -0.0595 320 LYS A O   
2633 C CB  . LYS A 320 ? 0.4491 0.5196 0.6078 0.1038  0.0579  -0.0705 320 LYS A CB  
2634 C CG  . LYS A 320 ? 0.5142 0.6098 0.701  0.1108  0.0663  -0.0775 320 LYS A CG  
2635 C CD  . LYS A 320 ? 0.6148 0.7421 0.8317 0.1033  0.0646  -0.0804 320 LYS A CD  
2636 C CE  . LYS A 320 ? 0.6978 0.851  0.9421 0.1033  0.0762  -0.087  320 LYS A CE  
2637 N NZ  . LYS A 320 ? 0.7803 0.9469 1.0415 0.1216  0.0743  -0.092  320 LYS A NZ  
2638 N N   . LEU A 321 ? 0.4069 0.4152 0.4974 0.0886  0.0514  -0.0575 321 LEU A N   
2639 C CA  . LEU A 321 ? 0.4291 0.4204 0.4998 0.084   0.0428  -0.0517 321 LEU A CA  
2640 C C   . LEU A 321 ? 0.4514 0.4136 0.4959 0.088   0.0439  -0.0497 321 LEU A C   
2641 O O   . LEU A 321 ? 0.4156 0.3646 0.4462 0.0883  0.0363  -0.0454 321 LEU A O   
2642 C CB  . LEU A 321 ? 0.4114 0.4027 0.4758 0.0684  0.0436  -0.0485 321 LEU A CB  
2643 C CG  . LEU A 321 ? 0.3871 0.402  0.4737 0.0635  0.0402  -0.0493 321 LEU A CG  
2644 C CD1 . LEU A 321 ? 0.3749 0.3875 0.4547 0.0495  0.0425  -0.0461 321 LEU A CD1 
2645 C CD2 . LEU A 321 ? 0.4326 0.4538 0.5254 0.0698  0.0279  -0.0484 321 LEU A CD2 
2646 N N   . GLU A 322 ? 0.4694 0.4209 0.5067 0.0912  0.0535  -0.0532 322 GLU A N   
2647 C CA  . GLU A 322 ? 0.5631 0.4851 0.5758 0.0951  0.0549  -0.0523 322 GLU A CA  
2648 C C   . GLU A 322 ? 0.6008 0.5158 0.6139 0.1107  0.0479  -0.0511 322 GLU A C   
2649 O O   . GLU A 322 ? 0.6643 0.5527 0.6555 0.1129  0.0471  -0.0487 322 GLU A O   
2650 C CB  . GLU A 322 ? 0.6202 0.5316 0.6245 0.0951  0.0673  -0.0574 322 GLU A CB  
2651 C CG  . GLU A 322 ? 0.6679 0.5824 0.6659 0.0794  0.0733  -0.0574 322 GLU A CG  
2652 C CD  . GLU A 322 ? 0.7437 0.6343 0.7154 0.072   0.0802  -0.0589 322 GLU A CD  
2653 O OE1 . GLU A 322 ? 0.6737 0.5659 0.6375 0.0587  0.0816  -0.0571 322 GLU A OE1 
2654 O OE2 . GLU A 322 ? 0.8431 0.7136 0.8019 0.0792  0.0837  -0.0619 322 GLU A OE2 
2655 N N   . GLU A 323 ? 0.5865 0.5244 0.6237 0.1215  0.0433  -0.053  323 GLU A N   
2656 C CA  . GLU A 323 ? 0.6592 0.5926 0.6968 0.1368  0.0345  -0.051  323 GLU A CA  
2657 C C   . GLU A 323 ? 0.579  0.513  0.6112 0.1334  0.0224  -0.0451 323 GLU A C   
2658 O O   . GLU A 323 ? 0.5882 0.516  0.6164 0.1454  0.0144  -0.0423 323 GLU A O   
2659 C CB  . GLU A 323 ? 0.7207 0.6808 0.7875 0.15    0.0349  -0.0564 323 GLU A CB  
2660 C CG  . GLU A 323 ? 0.8577 0.8095 0.9236 0.1569  0.0472  -0.0618 323 GLU A CG  
2661 C CD  . GLU A 323 ? 0.9544 0.9365 1.0518 0.1661  0.0519  -0.0686 323 GLU A CD  
2662 O OE1 . GLU A 323 ? 1.097  1.0697 1.1917 0.1747  0.0614  -0.0729 323 GLU A OE1 
2663 O OE2 . GLU A 323 ? 0.8752 0.8888 0.9989 0.1644  0.047   -0.0701 323 GLU A OE2 
2664 N N   . ARG A 324 ? 0.4823 0.424  0.5144 0.1184  0.0211  -0.0433 324 ARG A N   
2665 C CA  . ARG A 324 ? 0.4694 0.4166 0.5005 0.1159  0.0103  -0.0392 324 ARG A CA  
2666 C C   . ARG A 324 ? 0.4887 0.4098 0.4918 0.108   0.0093  -0.0333 324 ARG A C   
2667 O O   . ARG A 324 ? 0.4443 0.3521 0.4346 0.0979  0.0165  -0.0332 324 ARG A O   
2668 C CB  . ARG A 324 ? 0.4438 0.416  0.4935 0.1052  0.0091  -0.0411 324 ARG A CB  
2669 C CG  . ARG A 324 ? 0.3841 0.3854 0.4641 0.111   0.0092  -0.047  324 ARG A CG  
2670 C CD  . ARG A 324 ? 0.4013 0.4155 0.4931 0.1247  -0.0023 -0.0476 324 ARG A CD  
2671 N NE  . ARG A 324 ? 0.4009 0.4166 0.4867 0.1192  -0.012  -0.0444 324 ARG A NE  
2672 C CZ  . ARG A 324 ? 0.3774 0.4112 0.4769 0.1092  -0.0142 -0.0466 324 ARG A CZ  
2673 N NH1 . ARG A 324 ? 0.3635 0.4197 0.4877 0.1053  -0.0096 -0.052  324 ARG A NH1 
2674 N NH2 . ARG A 324 ? 0.3598 0.3891 0.4485 0.1033  -0.0209 -0.0435 324 ARG A NH2 
2675 N N   . ASP A 325 ? 0.4865 0.4032 0.4815 0.1116  0       -0.0289 325 ASP A N   
2676 C CA  . ASP A 325 ? 0.492  0.3877 0.4629 0.1037  -0.0011 -0.0233 325 ASP A CA  
2677 C C   . ASP A 325 ? 0.4442 0.352  0.4194 0.0884  -0.0002 -0.0233 325 ASP A C   
2678 O O   . ASP A 325 ? 0.4045 0.3351 0.398  0.0873  -0.0043 -0.0255 325 ASP A O   
2679 C CB  . ASP A 325 ? 0.5408 0.4304 0.5018 0.1114  -0.0106 -0.0184 325 ASP A CB  
2680 C CG  . ASP A 325 ? 0.6814 0.5562 0.6349 0.128   -0.0132 -0.0167 325 ASP A CG  
2681 O OD1 . ASP A 325 ? 0.6441 0.5042 0.5928 0.1322  -0.0062 -0.0183 325 ASP A OD1 
2682 O OD2 . ASP A 325 ? 0.8479 0.7272 0.8012 0.1376  -0.0226 -0.014  325 ASP A OD2 
2683 N N   . GLN A 326 ? 0.4323 0.3246 0.3914 0.0772  0.0052  -0.0214 326 GLN A N   
2684 C CA  . GLN A 326 ? 0.4035 0.3052 0.365  0.0635  0.0065  -0.0211 326 GLN A CA  
2685 C C   . GLN A 326 ? 0.401  0.2848 0.3414 0.0548  0.007   -0.0168 326 GLN A C   
2686 O O   . GLN A 326 ? 0.4403 0.3024 0.3643 0.0554  0.0106  -0.0158 326 GLN A O   
2687 C CB  . GLN A 326 ? 0.373  0.2782 0.3395 0.0571  0.0146  -0.0246 326 GLN A CB  
2688 C CG  . GLN A 326 ? 0.3851 0.3096 0.3737 0.0634  0.0162  -0.0292 326 GLN A CG  
2689 C CD  . GLN A 326 ? 0.3819 0.3101 0.374  0.0564  0.0248  -0.0321 326 GLN A CD  
2690 O OE1 . GLN A 326 ? 0.3667 0.2988 0.3571 0.0456  0.0261  -0.0308 326 GLN A OE1 
2691 N NE2 . GLN A 326 ? 0.4478 0.376  0.4453 0.0634  0.0307  -0.0361 326 GLN A NE2 
2692 N N   . ASN A 327 ? 0.3597 0.2531 0.3016 0.0464  0.0042  -0.0149 327 ASN A N   
2693 C CA  . ASN A 327 ? 0.4266 0.3078 0.352  0.0364  0.0056  -0.0115 327 ASN A CA  
2694 C C   . ASN A 327 ? 0.4238 0.3029 0.3464 0.026   0.0117  -0.0133 327 ASN A C   
2695 O O   . ASN A 327 ? 0.3968 0.284  0.3292 0.0264  0.0149  -0.0167 327 ASN A O   
2696 C CB  . ASN A 327 ? 0.4156 0.307  0.3428 0.0333  0.0006  -0.009  327 ASN A CB  
2697 C CG  . ASN A 327 ? 0.4408 0.3524 0.3835 0.0276  -0.0001 -0.011  327 ASN A CG  
2698 O OD1 . ASN A 327 ? 0.3494 0.2632 0.2934 0.0197  0.0039  -0.0118 327 ASN A OD1 
2699 N ND2 . ASN A 327 ? 0.3972 0.3224 0.35   0.0311  -0.0055 -0.0115 327 ASN A ND2 
2700 N N   . GLU A 328 ? 0.4415 0.3091 0.3494 0.0164  0.0134  -0.0111 328 GLU A N   
2701 C CA  . GLU A 328 ? 0.4471 0.3104 0.349  0.0068  0.0182  -0.0131 328 GLU A CA  
2702 C C   . GLU A 328 ? 0.404  0.2877 0.3193 0.0017  0.0175  -0.0141 328 GLU A C   
2703 O O   . GLU A 328 ? 0.406  0.2901 0.3205 -0.0022 0.0212  -0.0165 328 GLU A O   
2704 C CB  . GLU A 328 ? 0.5164 0.3653 0.4017 -0.0031 0.0196  -0.0112 328 GLU A CB  
2705 C CG  . GLU A 328 ? 0.6176 0.4401 0.4863 0.0003  0.0226  -0.011  328 GLU A CG  
2706 C CD  . GLU A 328 ? 0.7312 0.5389 0.5837 -0.0115 0.0247  -0.0093 328 GLU A CD  
2707 O OE1 . GLU A 328 ? 0.6479 0.4665 0.5025 -0.0198 0.0229  -0.007  328 GLU A OE1 
2708 O OE2 . GLU A 328 ? 0.8398 0.6243 0.6777 -0.0124 0.0288  -0.0108 328 GLU A OE2 
2709 N N   . ASN A 329 ? 0.3727 0.2713 0.2976 0.0012  0.0131  -0.012  329 ASN A N   
2710 C CA  . ASN A 329 ? 0.3529 0.2684 0.2899 -0.0025 0.0125  -0.0124 329 ASN A CA  
2711 C C   . ASN A 329 ? 0.3606 0.284  0.3105 0.0034  0.0143  -0.0151 329 ASN A C   
2712 O O   . ASN A 329 ? 0.3206 0.2486 0.2736 -0.0002 0.0176  -0.0161 329 ASN A O   
2713 C CB  . ASN A 329 ? 0.343  0.2702 0.2869 -0.0032 0.0079  -0.0102 329 ASN A CB  
2714 C CG  . ASN A 329 ? 0.3511 0.2911 0.3029 -0.0085 0.0075  -0.0097 329 ASN A CG  
2715 O OD1 . ASN A 329 ? 0.3453 0.2962 0.31   -0.0057 0.0064  -0.0104 329 ASN A OD1 
2716 N ND2 . ASN A 329 ? 0.3596 0.2979 0.3035 -0.0164 0.0085  -0.0086 329 ASN A ND2 
2717 N N   . GLU A 330 ? 0.3415 0.2657 0.2982 0.0128  0.0126  -0.0164 330 GLU A N   
2718 C CA  . GLU A 330 ? 0.3668 0.3006 0.3381 0.0182  0.0148  -0.0196 330 GLU A CA  
2719 C C   . GLU A 330 ? 0.3504 0.2751 0.3151 0.0175  0.0219  -0.022  330 GLU A C   
2720 O O   . GLU A 330 ? 0.3148 0.2478 0.2883 0.0168  0.0261  -0.024  330 GLU A O   
2721 C CB  . GLU A 330 ? 0.3633 0.301  0.3433 0.0291  0.0108  -0.021  330 GLU A CB  
2722 C CG  . GLU A 330 ? 0.3712 0.3196 0.3584 0.03    0.0038  -0.0199 330 GLU A CG  
2723 C CD  . GLU A 330 ? 0.3923 0.3446 0.3854 0.0406  -0.0021 -0.0211 330 GLU A CD  
2724 O OE1 . GLU A 330 ? 0.3957 0.3365 0.3806 0.0477  -0.0019 -0.0207 330 GLU A OE1 
2725 O OE2 . GLU A 330 ? 0.3569 0.3233 0.3624 0.0422  -0.0072 -0.0228 330 GLU A OE2 
2726 N N   . LEU A 331 ? 0.338  0.2448 0.2866 0.0178  0.0237  -0.022  331 LEU A N   
2727 C CA  . LEU A 331 ? 0.3706 0.2657 0.3094 0.0165  0.0305  -0.025  331 LEU A CA  
2728 C C   . LEU A 331 ? 0.3732 0.2708 0.3064 0.0059  0.0335  -0.025  331 LEU A C   
2729 O O   . LEU A 331 ? 0.3736 0.2703 0.3055 0.0055  0.0396  -0.028  331 LEU A O   
2730 C CB  . LEU A 331 ? 0.3933 0.266  0.3148 0.0184  0.0313  -0.025  331 LEU A CB  
2731 C CG  . LEU A 331 ? 0.3994 0.2671 0.3252 0.032   0.0304  -0.0258 331 LEU A CG  
2732 C CD1 . LEU A 331 ? 0.4522 0.2944 0.3586 0.0337  0.0307  -0.0244 331 LEU A CD1 
2733 C CD2 . LEU A 331 ? 0.4223 0.2958 0.3591 0.0401  0.0356  -0.0304 331 LEU A CD2 
2734 N N   . GLY A 332 ? 0.3601 0.2615 0.2899 -0.0021 0.0293  -0.0217 332 GLY A N   
2735 C CA  . GLY A 332 ? 0.3989 0.306  0.3256 -0.0105 0.0305  -0.021  332 GLY A CA  
2736 C C   . GLY A 332 ? 0.3802 0.3006 0.32   -0.0087 0.0332  -0.0213 332 GLY A C   
2737 O O   . GLY A 332 ? 0.3523 0.272  0.2866 -0.0125 0.0377  -0.0221 332 GLY A O   
2738 N N   . PHE A 333 ? 0.3481 0.2805 0.3047 -0.0037 0.0304  -0.0204 333 PHE A N   
2739 C CA  . PHE A 333 ? 0.3172 0.2616 0.2878 -0.0026 0.0336  -0.0209 333 PHE A CA  
2740 C C   . PHE A 333 ? 0.3089 0.2512 0.282  0.0022  0.0408  -0.025  333 PHE A C   
2741 O O   . PHE A 333 ? 0.3492 0.2956 0.3242 -0.0006 0.0468  -0.0255 333 PHE A O   
2742 C CB  . PHE A 333 ? 0.3439 0.3008 0.3317 0.0009  0.0285  -0.0202 333 PHE A CB  
2743 C CG  . PHE A 333 ? 0.3447 0.305  0.331  -0.0041 0.0233  -0.0164 333 PHE A CG  
2744 C CD1 . PHE A 333 ? 0.389  0.3548 0.3784 -0.0088 0.0246  -0.0141 333 PHE A CD1 
2745 C CD2 . PHE A 333 ? 0.3804 0.3379 0.3617 -0.0036 0.0178  -0.0151 333 PHE A CD2 
2746 C CE1 . PHE A 333 ? 0.3844 0.353  0.3723 -0.0122 0.0199  -0.0107 333 PHE A CE1 
2747 C CE2 . PHE A 333 ? 0.378  0.34   0.3589 -0.0077 0.0139  -0.0121 333 PHE A CE2 
2748 C CZ  . PHE A 333 ? 0.3622 0.3298 0.3465 -0.0115 0.0147  -0.0101 333 PHE A CZ  
2749 N N   . HIS A 334 ? 0.3132 0.2493 0.2862 0.0099  0.0407  -0.0278 334 HIS A N   
2750 C CA  . HIS A 334 ? 0.3368 0.2719 0.3139 0.0164  0.0476  -0.0322 334 HIS A CA  
2751 C C   . HIS A 334 ? 0.3719 0.2975 0.3341 0.0111  0.0556  -0.034  334 HIS A C   
2752 O O   . HIS A 334 ? 0.3438 0.2759 0.312  0.0115  0.0631  -0.0364 334 HIS A O   
2753 C CB  . HIS A 334 ? 0.3428 0.2672 0.3162 0.0257  0.0457  -0.034  334 HIS A CB  
2754 C CG  . HIS A 334 ? 0.3557 0.279  0.334  0.0342  0.0524  -0.0388 334 HIS A CG  
2755 N ND1 . HIS A 334 ? 0.3631 0.3031 0.3632 0.0424  0.0523  -0.0411 334 HIS A ND1 
2756 C CD2 . HIS A 334 ? 0.4207 0.3306 0.387  0.0358  0.0599  -0.0424 334 HIS A CD2 
2757 C CE1 . HIS A 334 ? 0.3852 0.3227 0.3874 0.0498  0.0593  -0.0457 334 HIS A CE1 
2758 N NE2 . HIS A 334 ? 0.4073 0.3255 0.3883 0.0462  0.0645  -0.0467 334 HIS A NE2 
2759 N N   . TYR A 335 ? 0.3635 0.2737 0.3059 0.0061  0.0542  -0.0334 335 TYR A N   
2760 C CA  . TYR A 335 ? 0.3813 0.2804 0.3062 0.0009  0.0604  -0.0359 335 TYR A CA  
2761 C C   . TYR A 335 ? 0.3793 0.2866 0.3016 -0.0075 0.0616  -0.0331 335 TYR A C   
2762 O O   . TYR A 335 ? 0.399  0.3029 0.3122 -0.0099 0.0687  -0.0354 335 TYR A O   
2763 C CB  . TYR A 335 ? 0.3883 0.2683 0.2936 -0.0025 0.058   -0.037  335 TYR A CB  
2764 C CG  . TYR A 335 ? 0.4152 0.2811 0.3178 0.0067  0.0608  -0.0407 335 TYR A CG  
2765 C CD1 . TYR A 335 ? 0.4727 0.33   0.3694 0.0109  0.0694  -0.0463 335 TYR A CD1 
2766 C CD2 . TYR A 335 ? 0.4214 0.2828 0.3274 0.0122  0.0552  -0.0386 335 TYR A CD2 
2767 C CE1 . TYR A 335 ? 0.5027 0.3471 0.398  0.0213  0.0722  -0.0497 335 TYR A CE1 
2768 C CE2 . TYR A 335 ? 0.4699 0.3173 0.3727 0.022   0.0574  -0.0413 335 TYR A CE2 
2769 C CZ  . TYR A 335 ? 0.5012 0.3393 0.3984 0.0266  0.0658  -0.0469 335 TYR A CZ  
2770 O OH  . TYR A 335 ? 0.5269 0.3502 0.421  0.0375  0.0679  -0.0494 335 TYR A OH  
2771 N N   . TYR A 336 ? 0.3629 0.2807 0.293  -0.011  0.0553  -0.0283 336 TYR A N   
2772 C CA  . TYR A 336 ? 0.36   0.2852 0.2895 -0.0169 0.0565  -0.0248 336 TYR A CA  
2773 C C   . TYR A 336 ? 0.4136 0.347  0.3547 -0.0142 0.0648  -0.0261 336 TYR A C   
2774 O O   . TYR A 336 ? 0.3962 0.3274 0.3275 -0.0182 0.0713  -0.026  336 TYR A O   
2775 C CB  . TYR A 336 ? 0.3442 0.2785 0.2819 -0.0194 0.0485  -0.0196 336 TYR A CB  
2776 C CG  . TYR A 336 ? 0.3524 0.2921 0.2886 -0.0243 0.0493  -0.0153 336 TYR A CG  
2777 C CD1 . TYR A 336 ? 0.392  0.3261 0.3098 -0.0303 0.0489  -0.0135 336 TYR A CD1 
2778 C CD2 . TYR A 336 ? 0.3987 0.3482 0.3509 -0.0231 0.0506  -0.013  336 TYR A CD2 
2779 C CE1 . TYR A 336 ? 0.389  0.3263 0.3032 -0.0337 0.05    -0.0088 336 TYR A CE1 
2780 C CE2 . TYR A 336 ? 0.3924 0.3436 0.3414 -0.0273 0.052   -0.0083 336 TYR A CE2 
2781 C CZ  . TYR A 336 ? 0.4403 0.3852 0.3699 -0.032  0.0516  -0.0057 336 TYR A CZ  
2782 O OH  . TYR A 336 ? 0.4629 0.4085 0.3884 -0.035  0.0523  -0.0002 336 TYR A OH  
2783 N N   . LEU A 337 ? 0.3946 0.3376 0.356  -0.0077 0.0648  -0.0277 337 LEU A N   
2784 C CA  . LEU A 337 ? 0.3775 0.3309 0.3536 -0.0055 0.0728  -0.0299 337 LEU A CA  
2785 C C   . LEU A 337 ? 0.3781 0.3245 0.3449 -0.0031 0.0827  -0.0347 337 LEU A C   
2786 O O   . LEU A 337 ? 0.3808 0.3305 0.347  -0.006  0.0917  -0.0352 337 LEU A O   
2787 C CB  . LEU A 337 ? 0.3621 0.3287 0.3622 0.0013  0.0698  -0.0319 337 LEU A CB  
2788 C CG  . LEU A 337 ? 0.3662 0.3402 0.3761 -0.0012 0.0612  -0.0281 337 LEU A CG  
2789 C CD1 . LEU A 337 ? 0.4216 0.4072 0.4521 0.0062  0.0568  -0.0312 337 LEU A CD1 
2790 C CD2 . LEU A 337 ? 0.4023 0.3814 0.4156 -0.0084 0.0641  -0.0244 337 LEU A CD2 
2791 N N   . LYS A 338 ? 0.3613 0.2967 0.32   0.0022  0.0815  -0.0384 338 LYS A N   
2792 C CA  . LYS A 338 ? 0.4024 0.3288 0.3515 0.0057  0.0908  -0.044  338 LYS A CA  
2793 C C   . LYS A 338 ? 0.4149 0.3324 0.342  -0.0027 0.0965  -0.0436 338 LYS A C   
2794 O O   . LYS A 338 ? 0.4724 0.3899 0.396  -0.002  0.1072  -0.0472 338 LYS A O   
2795 C CB  . LYS A 338 ? 0.423  0.3338 0.3622 0.0116  0.0877  -0.0472 338 LYS A CB  
2796 C CG  . LYS A 338 ? 0.4711 0.373  0.4044 0.0181  0.0978  -0.054  338 LYS A CG  
2797 C CD  . LYS A 338 ? 0.5498 0.4362 0.4776 0.0265  0.0951  -0.057  338 LYS A CD  
2798 C CE  . LYS A 338 ? 0.6522 0.5362 0.5834 0.0364  0.1053  -0.0638 338 LYS A CE  
2799 N NZ  . LYS A 338 ? 0.7235 0.5948 0.6545 0.0475  0.102   -0.0656 338 LYS A NZ  
2800 N N   . GLY A 339 ? 0.4354 0.3458 0.3472 -0.01   0.0892  -0.0398 339 GLY A N   
2801 C CA  . GLY A 339 ? 0.4616 0.3657 0.3523 -0.0184 0.0915  -0.0384 339 GLY A CA  
2802 C C   . GLY A 339 ? 0.4611 0.375  0.3559 -0.0217 0.0978  -0.0348 339 GLY A C   
2803 O O   . GLY A 339 ? 0.4531 0.3617 0.3325 -0.0247 0.106   -0.0363 339 GLY A O   
2804 N N   . LEU A 340 ? 0.4356 0.3622 0.3493 -0.0217 0.094   -0.03   340 LEU A N   
2805 C CA  . LEU A 340 ? 0.434  0.3686 0.3534 -0.0253 0.1002  -0.0261 340 LEU A CA  
2806 C C   . LEU A 340 ? 0.4581 0.3979 0.386  -0.0222 0.1134  -0.0309 340 LEU A C   
2807 O O   . LEU A 340 ? 0.4928 0.433  0.4139 -0.0267 0.1222  -0.0289 340 LEU A O   
2808 C CB  . LEU A 340 ? 0.4296 0.3753 0.3688 -0.0258 0.0939  -0.0212 340 LEU A CB  
2809 C CG  . LEU A 340 ? 0.4455 0.3889 0.379  -0.0289 0.0821  -0.0156 340 LEU A CG  
2810 C CD1 . LEU A 340 ? 0.4179 0.3718 0.3729 -0.028  0.0776  -0.0127 340 LEU A CD1 
2811 C CD2 . LEU A 340 ? 0.4767 0.4131 0.3888 -0.0351 0.0821  -0.0103 340 LEU A CD2 
2812 N N   . ILE A 341 ? 0.4439 0.3881 0.3867 -0.0142 0.1153  -0.037  341 ILE A N   
2813 C CA  . ILE A 341 ? 0.4336 0.3862 0.3889 -0.0097 0.1275  -0.0423 341 ILE A CA  
2814 C C   . ILE A 341 ? 0.4887 0.4282 0.4211 -0.0095 0.137   -0.0471 341 ILE A C   
2815 O O   . ILE A 341 ? 0.4734 0.4166 0.404  -0.0115 0.1493  -0.0484 341 ILE A O   
2816 C CB  . ILE A 341 ? 0.4466 0.4097 0.4265 0.0003  0.1247  -0.047  341 ILE A CB  
2817 C CG1 . ILE A 341 ? 0.4159 0.3939 0.4189 -0.0009 0.1169  -0.0432 341 ILE A CG1 
2818 C CG2 . ILE A 341 ? 0.4856 0.4576 0.4779 0.0069  0.1374  -0.0538 341 ILE A CG2 
2819 C CD1 . ILE A 341 ? 0.4232 0.4076 0.4431 0.0082  0.1083  -0.046  341 ILE A CD1 
2820 N N   . THR A 342 ? 0.4757 0.4    0.3912 -0.0071 0.132   -0.0501 342 THR A N   
2821 C CA  . THR A 342 ? 0.506  0.4161 0.4015 -0.0051 0.1402  -0.0568 342 THR A CA  
2822 C C   . THR A 342 ? 0.5193 0.416  0.3837 -0.0145 0.1401  -0.0549 342 THR A C   
2823 O O   . THR A 342 ? 0.5958 0.4815 0.4413 -0.0145 0.1486  -0.0605 342 THR A O   
2824 C CB  . THR A 342 ? 0.5258 0.4248 0.4204 0.0028  0.1353  -0.0618 342 THR A CB  
2825 O OG1 . THR A 342 ? 0.5224 0.4116 0.405  -0.0025 0.1229  -0.058  342 THR A OG1 
2826 C CG2 . THR A 342 ? 0.5272 0.439  0.4505 0.0136  0.1347  -0.0638 342 THR A CG2 
2827 N N   . ASN A 343 ? 0.5141 0.4112 0.3721 -0.0217 0.1303  -0.0477 343 ASN A N   
2828 C CA  . ASN A 343 ? 0.6146 0.5004 0.4439 -0.0298 0.127   -0.0458 343 ASN A CA  
2829 C C   . ASN A 343 ? 0.6594 0.528  0.4681 -0.0304 0.1237  -0.0524 343 ASN A C   
2830 O O   . ASN A 343 ? 0.6911 0.5494 0.4736 -0.0364 0.1246  -0.054  343 ASN A O   
2831 C CB  . ASN A 343 ? 0.6665 0.5522 0.482  -0.0337 0.1386  -0.0449 343 ASN A CB  
2832 C CG  . ASN A 343 ? 0.7147 0.5943 0.5053 -0.042  0.1328  -0.0393 343 ASN A CG  
2833 O OD1 . ASN A 343 ? 0.835  0.7057 0.6011 -0.0453 0.1397  -0.0416 343 ASN A OD1 
2834 N ND2 . ASN A 343 ? 0.757  0.6415 0.5526 -0.045  0.1206  -0.032  343 ASN A ND2 
2835 N N   . GLU A 344 ? 0.6278 0.4922 0.447  -0.0246 0.1197  -0.056  344 GLU A N   
2836 C CA  . GLU A 344 ? 0.6335 0.4795 0.4348 -0.0254 0.117   -0.0622 344 GLU A CA  
2837 C C   . GLU A 344 ? 0.6141 0.4591 0.4114 -0.0324 0.1031  -0.0576 344 GLU A C   
2838 O O   . GLU A 344 ? 0.526  0.3806 0.3424 -0.0301 0.0959  -0.0527 344 GLU A O   
2839 C CB  . GLU A 344 ? 0.6647 0.5045 0.4781 -0.0151 0.12    -0.0676 344 GLU A CB  
2840 C CG  . GLU A 344 ? 0.7673 0.6076 0.5852 -0.0069 0.134   -0.0738 344 GLU A CG  
2841 C CD  . GLU A 344 ? 0.9701 0.7934 0.7606 -0.0093 0.143   -0.0815 344 GLU A CD  
2842 O OE1 . GLU A 344 ? 0.9918 0.8007 0.7579 -0.0179 0.1375  -0.0829 344 GLU A OE1 
2843 O OE2 . GLU A 344 ? 1.0541 0.8796 0.8485 -0.0026 0.1558  -0.0866 344 GLU A OE2 
2844 N N   . LYS A 345 ? 0.5858 0.42   0.3585 -0.0408 0.0996  -0.0599 345 LYS A N   
2845 C CA  . LYS A 345 ? 0.6033 0.437  0.3719 -0.048  0.0871  -0.0571 345 LYS A CA  
2846 C C   . LYS A 345 ? 0.5299 0.3572 0.3096 -0.0442 0.0833  -0.0586 345 LYS A C   
2847 O O   . LYS A 345 ? 0.5091 0.344  0.2989 -0.0466 0.0742  -0.0536 345 LYS A O   
2848 C CB  . LYS A 345 ? 0.6423 0.4638 0.383  -0.0576 0.0841  -0.062  345 LYS A CB  
2849 C CG  . LYS A 345 ? 0.7447 0.5716 0.4691 -0.0634 0.0836  -0.0595 345 LYS A CG  
2850 C CD  . LYS A 345 ? 0.7925 0.6047 0.4883 -0.0719 0.0817  -0.0672 345 LYS A CD  
2851 C CE  . LYS A 345 ? 0.9121 0.7252 0.5855 -0.0768 0.0827  -0.067  345 LYS A CE  
2852 N NZ  . LYS A 345 ? 0.9925 0.8202 0.6662 -0.0821 0.0707  -0.0589 345 LYS A NZ  
2853 N N   . GLU A 346 ? 0.525  0.3376 0.3018 -0.0379 0.0906  -0.0653 346 GLU A N   
2854 C CA  . GLU A 346 ? 0.5525 0.3551 0.3361 -0.0336 0.0876  -0.0664 346 GLU A CA  
2855 C C   . GLU A 346 ? 0.5186 0.3376 0.3276 -0.0281 0.0819  -0.0591 346 GLU A C   
2856 O O   . GLU A 346 ? 0.4797 0.2965 0.2927 -0.0297 0.0746  -0.0563 346 GLU A O   
2857 C CB  . GLU A 346 ? 0.6076 0.3927 0.3856 -0.0249 0.0973  -0.074  346 GLU A CB  
2858 C CG  . GLU A 346 ? 0.6095 0.381  0.3923 -0.0187 0.0949  -0.0746 346 GLU A CG  
2859 C CD  . GLU A 346 ? 0.6177 0.3745 0.3871 -0.0283 0.0875  -0.0746 346 GLU A CD  
2860 O OE1 . GLU A 346 ? 0.6177 0.3685 0.3688 -0.04   0.0858  -0.0777 346 GLU A OE1 
2861 O OE2 . GLU A 346 ? 0.5978 0.3505 0.3757 -0.0247 0.0831  -0.0711 346 GLU A OE2 
2862 N N   . ALA A 347 ? 0.4968 0.3316 0.3231 -0.0217 0.0859  -0.0565 347 ALA A N   
2863 C CA  . ALA A 347 ? 0.4873 0.3369 0.3371 -0.0165 0.0805  -0.0509 347 ALA A CA  
2864 C C   . ALA A 347 ? 0.4411 0.3003 0.2927 -0.0245 0.0706  -0.0445 347 ALA A C   
2865 O O   . ALA A 347 ? 0.4265 0.2896 0.2886 -0.023  0.0639  -0.0411 347 ALA A O   
2866 C CB  . ALA A 347 ? 0.475  0.3403 0.3436 -0.0097 0.0868  -0.0502 347 ALA A CB  
2867 N N   . PHE A 348 ? 0.4386 0.3017 0.2792 -0.0326 0.0695  -0.0427 348 PHE A N   
2868 C CA  . PHE A 348 ? 0.4266 0.2994 0.2689 -0.0392 0.0602  -0.037  348 PHE A CA  
2869 C C   . PHE A 348 ? 0.4401 0.3038 0.273  -0.045  0.0537  -0.0384 348 PHE A C   
2870 O O   . PHE A 348 ? 0.3996 0.2716 0.2423 -0.0464 0.0466  -0.0342 348 PHE A O   
2871 C CB  . PHE A 348 ? 0.4702 0.3486 0.302  -0.045  0.0605  -0.0345 348 PHE A CB  
2872 C CG  . PHE A 348 ? 0.4304 0.3194 0.2731 -0.0411 0.066   -0.0309 348 PHE A CG  
2873 C CD1 . PHE A 348 ? 0.4471 0.3488 0.3115 -0.0372 0.0633  -0.0261 348 PHE A CD1 
2874 C CD2 . PHE A 348 ? 0.4729 0.358  0.3036 -0.0419 0.0748  -0.0329 348 PHE A CD2 
2875 C CE1 . PHE A 348 ? 0.4417 0.3517 0.3163 -0.0349 0.0692  -0.0234 348 PHE A CE1 
2876 C CE2 . PHE A 348 ? 0.4886 0.3825 0.3288 -0.0397 0.0811  -0.0295 348 PHE A CE2 
2877 C CZ  . PHE A 348 ? 0.4569 0.3631 0.3193 -0.0367 0.0782  -0.0247 348 PHE A CZ  
2878 N N   . PHE A 349 ? 0.4468 0.2933 0.2615 -0.0485 0.0569  -0.0448 349 PHE A N   
2879 C CA  . PHE A 349 ? 0.4897 0.3254 0.2957 -0.055  0.0521  -0.0467 349 PHE A CA  
2880 C C   . PHE A 349 ? 0.4719 0.3044 0.2906 -0.0489 0.0506  -0.0446 349 PHE A C   
2881 O O   . PHE A 349 ? 0.431  0.2667 0.2526 -0.0539 0.0444  -0.0417 349 PHE A O   
2882 C CB  . PHE A 349 ? 0.4875 0.3015 0.2717 -0.0594 0.0566  -0.0548 349 PHE A CB  
2883 C CG  . PHE A 349 ? 0.5119 0.3254 0.2776 -0.0676 0.0568  -0.0583 349 PHE A CG  
2884 C CD1 . PHE A 349 ? 0.5182 0.3466 0.2825 -0.0756 0.0487  -0.0545 349 PHE A CD1 
2885 C CD2 . PHE A 349 ? 0.6002 0.3981 0.349  -0.0665 0.065   -0.0656 349 PHE A CD2 
2886 C CE1 . PHE A 349 ? 0.5718 0.3995 0.3172 -0.0825 0.0478  -0.0577 349 PHE A CE1 
2887 C CE2 . PHE A 349 ? 0.6025 0.3992 0.3314 -0.0741 0.0649  -0.0692 349 PHE A CE2 
2888 C CZ  . PHE A 349 ? 0.5644 0.3757 0.2912 -0.0822 0.0559  -0.0651 349 PHE A CZ  
2889 N N   . LYS A 350 ? 0.4646 0.2915 0.2905 -0.038  0.0564  -0.0461 350 LYS A N   
2890 C CA  . LYS A 350 ? 0.4559 0.2804 0.2929 -0.0306 0.0543  -0.0435 350 LYS A CA  
2891 C C   . LYS A 350 ? 0.4113 0.2564 0.2662 -0.0299 0.0478  -0.0369 350 LYS A C   
2892 O O   . LYS A 350 ? 0.3958 0.2394 0.2535 -0.0302 0.0434  -0.0342 350 LYS A O   
2893 C CB  . LYS A 350 ? 0.4843 0.3041 0.3287 -0.0177 0.0606  -0.0461 350 LYS A CB  
2894 C CG  . LYS A 350 ? 0.5478 0.3434 0.3757 -0.0151 0.0673  -0.0527 350 LYS A CG  
2895 C CD  . LYS A 350 ? 0.5914 0.3843 0.4302 -0.0001 0.0718  -0.0543 350 LYS A CD  
2896 C CE  . LYS A 350 ? 0.6759 0.443  0.5    0.0052  0.0779  -0.0602 350 LYS A CE  
2897 N NZ  . LYS A 350 ? 0.6834 0.4469 0.4981 0.0042  0.0864  -0.0668 350 LYS A NZ  
2898 N N   . SER A 351 ? 0.3994 0.2617 0.265  -0.0289 0.048   -0.0346 351 SER A N   
2899 C CA  . SER A 351 ? 0.4008 0.2809 0.2821 -0.0285 0.0422  -0.0291 351 SER A CA  
2900 C C   . SER A 351 ? 0.4001 0.2829 0.2767 -0.0371 0.0353  -0.0263 351 SER A C   
2901 O O   . SER A 351 ? 0.3537 0.2416 0.2388 -0.0356 0.031   -0.0233 351 SER A O   
2902 C CB  . SER A 351 ? 0.3886 0.2819 0.2777 -0.028  0.0444  -0.0273 351 SER A CB  
2903 O OG  . SER A 351 ? 0.3756 0.2839 0.2791 -0.0276 0.0391  -0.0224 351 SER A OG  
2904 N N   . VAL A 352 ? 0.3986 0.278  0.2609 -0.046  0.0347  -0.028  352 VAL A N   
2905 C CA  . VAL A 352 ? 0.3892 0.2728 0.247  -0.0551 0.0286  -0.0267 352 VAL A CA  
2906 C C   . VAL A 352 ? 0.3741 0.2465 0.229  -0.0568 0.028   -0.0275 352 VAL A C   
2907 O O   . VAL A 352 ? 0.3755 0.2569 0.2378 -0.0591 0.0235  -0.0241 352 VAL A O   
2908 C CB  . VAL A 352 ? 0.4123 0.2937 0.2541 -0.0644 0.0277  -0.0296 352 VAL A CB  
2909 C CG1 . VAL A 352 ? 0.4125 0.2996 0.2516 -0.0744 0.0211  -0.0292 352 VAL A CG1 
2910 C CG2 . VAL A 352 ? 0.4293 0.3229 0.2729 -0.063  0.0272  -0.0268 352 VAL A CG2 
2911 N N   . GLU A 353 ? 0.3925 0.2449 0.2366 -0.0549 0.033   -0.0317 353 GLU A N   
2912 C CA  . GLU A 353 ? 0.4035 0.2405 0.2413 -0.0568 0.0333  -0.0321 353 GLU A CA  
2913 C C   . GLU A 353 ? 0.4054 0.2479 0.2562 -0.0488 0.0313  -0.0273 353 GLU A C   
2914 O O   . GLU A 353 ? 0.4189 0.259  0.2683 -0.053  0.029   -0.025  353 GLU A O   
2915 C CB  . GLU A 353 ? 0.4661 0.2779 0.2884 -0.0552 0.0394  -0.0376 353 GLU A CB  
2916 C CG  . GLU A 353 ? 0.4751 0.279  0.2808 -0.0662 0.0405  -0.0433 353 GLU A CG  
2917 C CD  . GLU A 353 ? 0.5385 0.3184 0.3287 -0.0635 0.0475  -0.0499 353 GLU A CD  
2918 O OE1 . GLU A 353 ? 0.5435 0.3194 0.3384 -0.0515 0.0523  -0.0505 353 GLU A OE1 
2919 O OE2 . GLU A 353 ? 0.5572 0.3241 0.3308 -0.074  0.0481  -0.0551 353 GLU A OE2 
2920 N N   . TYR A 354 ? 0.3976 0.2465 0.2598 -0.0377 0.0325  -0.0263 354 TYR A N   
2921 C CA  . TYR A 354 ? 0.3926 0.2476 0.2667 -0.0298 0.0297  -0.0225 354 TYR A CA  
2922 C C   . TYR A 354 ? 0.3732 0.2469 0.2573 -0.034  0.0243  -0.0185 354 TYR A C   
2923 O O   . TYR A 354 ? 0.3575 0.2317 0.2439 -0.0327 0.0219  -0.0157 354 TYR A O   
2924 C CB  . TYR A 354 ? 0.3546 0.2145 0.2403 -0.0178 0.0316  -0.0233 354 TYR A CB  
2925 C CG  . TYR A 354 ? 0.4069 0.2485 0.2855 -0.0099 0.0359  -0.0263 354 TYR A CG  
2926 C CD1 . TYR A 354 ? 0.4202 0.2478 0.2928 -0.0053 0.0345  -0.0244 354 TYR A CD1 
2927 C CD2 . TYR A 354 ? 0.4137 0.2505 0.29   -0.0066 0.0419  -0.0309 354 TYR A CD2 
2928 C CE1 . TYR A 354 ? 0.4724 0.2817 0.3381 0.0036  0.0381  -0.0266 354 TYR A CE1 
2929 C CE2 . TYR A 354 ? 0.446  0.2657 0.3163 0.0021  0.0461  -0.0339 354 TYR A CE2 
2930 C CZ  . TYR A 354 ? 0.4885 0.2949 0.3544 0.0079  0.0437  -0.0316 354 TYR A CZ  
2931 O OH  . TYR A 354 ? 0.5423 0.3306 0.4019 0.0178  0.0474  -0.0339 354 TYR A OH  
2932 N N   . PHE A 355 ? 0.3667 0.2547 0.2557 -0.0383 0.0228  -0.0182 355 PHE A N   
2933 C CA  . PHE A 355 ? 0.3808 0.2856 0.279  -0.0416 0.0179  -0.0147 355 PHE A CA  
2934 C C   . PHE A 355 ? 0.3796 0.2826 0.2704 -0.051  0.016   -0.0142 355 PHE A C   
2935 O O   . PHE A 355 ? 0.3561 0.2677 0.2536 -0.0514 0.0135  -0.0115 355 PHE A O   
2936 C CB  . PHE A 355 ? 0.3551 0.274  0.2597 -0.0426 0.0165  -0.0136 355 PHE A CB  
2937 C CG  . PHE A 355 ? 0.3353 0.2601 0.2518 -0.0343 0.018   -0.0129 355 PHE A CG  
2938 C CD1 . PHE A 355 ? 0.3336 0.2638 0.2622 -0.0274 0.0164  -0.0117 355 PHE A CD1 
2939 C CD2 . PHE A 355 ? 0.3233 0.2485 0.2384 -0.0338 0.0216  -0.014  355 PHE A CD2 
2940 C CE1 . PHE A 355 ? 0.3308 0.2676 0.2715 -0.0212 0.0176  -0.0119 355 PHE A CE1 
2941 C CE2 . PHE A 355 ? 0.3282 0.2595 0.2551 -0.0277 0.0239  -0.0136 355 PHE A CE2 
2942 C CZ  . PHE A 355 ? 0.3397 0.2776 0.2806 -0.0217 0.0216  -0.0127 355 PHE A CZ  
2943 N N   . LYS A 356 ? 0.3708 0.262  0.2479 -0.0589 0.0179  -0.0175 356 LYS A N   
2944 C CA  . LYS A 356 ? 0.3701 0.2574 0.2401 -0.0691 0.0172  -0.0179 356 LYS A CA  
2945 C C   . LYS A 356 ? 0.4099 0.2847 0.2769 -0.0664 0.0193  -0.016  356 LYS A C   
2946 O O   . LYS A 356 ? 0.4026 0.2836 0.2722 -0.0712 0.0181  -0.0136 356 LYS A O   
2947 C CB  . LYS A 356 ? 0.4203 0.2942 0.2748 -0.0784 0.0192  -0.0228 356 LYS A CB  
2948 C CG  . LYS A 356 ? 0.4559 0.3457 0.3117 -0.0843 0.0151  -0.024  356 LYS A CG  
2949 C CD  . LYS A 356 ? 0.4744 0.3821 0.3372 -0.0931 0.0101  -0.0225 356 LYS A CD  
2950 C CE  . LYS A 356 ? 0.4705 0.3916 0.3321 -0.0979 0.0055  -0.0238 356 LYS A CE  
2951 N NZ  . LYS A 356 ? 0.4593 0.3996 0.3288 -0.1057 0.0002  -0.023  356 LYS A NZ  
2952 N N   . ALA A 357 ? 0.429  0.2863 0.29   -0.0583 0.0226  -0.0168 357 ALA A N   
2953 C CA  . ALA A 357 ? 0.4401 0.283  0.2953 -0.0547 0.0241  -0.0143 357 ALA A CA  
2954 C C   . ALA A 357 ? 0.4193 0.2774 0.2868 -0.0485 0.0208  -0.0099 357 ALA A C   
2955 O O   . ALA A 357 ? 0.409  0.2628 0.2721 -0.0508 0.0211  -0.007  357 ALA A O   
2956 C CB  . ALA A 357 ? 0.4596 0.2817 0.3065 -0.0458 0.0276  -0.016  357 ALA A CB  
2957 N N   . SER A 358 ? 0.3788 0.2533 0.2604 -0.0411 0.0181  -0.0096 358 SER A N   
2958 C CA  . SER A 358 ? 0.3963 0.285  0.289  -0.0358 0.0147  -0.0067 358 SER A CA  
2959 C C   . SER A 358 ? 0.3793 0.2854 0.2788 -0.0434 0.0126  -0.0053 358 SER A C   
2960 O O   . SER A 358 ? 0.3702 0.2869 0.2773 -0.0399 0.0106  -0.0034 358 SER A O   
2961 C CB  . SER A 358 ? 0.4188 0.3171 0.3241 -0.0261 0.0129  -0.0074 358 SER A CB  
2962 O OG  . SER A 358 ? 0.4466 0.3545 0.3579 -0.0289 0.0131  -0.0091 358 SER A OG  
2963 N N   . GLN A 359 ? 0.3797 0.2896 0.2766 -0.0532 0.0129  -0.0067 359 GLN A N   
2964 C CA  . GLN A 359 ? 0.3728 0.3012 0.2775 -0.0599 0.0105  -0.006  359 GLN A CA  
2965 C C   . GLN A 359 ? 0.3716 0.3172 0.2907 -0.0529 0.0071  -0.0049 359 GLN A C   
2966 O O   . GLN A 359 ? 0.3416 0.3013 0.2699 -0.052  0.0052  -0.0033 359 GLN A O   
2967 C CB  . GLN A 359 ? 0.3704 0.3    0.2727 -0.066  0.012   -0.0044 359 GLN A CB  
2968 C CG  . GLN A 359 ? 0.4803 0.4265 0.388  -0.0763 0.0105  -0.0052 359 GLN A CG  
2969 C CD  . GLN A 359 ? 0.5107 0.4615 0.4188 -0.0824 0.0131  -0.0038 359 GLN A CD  
2970 O OE1 . GLN A 359 ? 0.5597 0.4962 0.4563 -0.0906 0.017   -0.0041 359 GLN A OE1 
2971 N NE2 . GLN A 359 ? 0.473  0.4412 0.393  -0.0779 0.0118  -0.0021 359 GLN A NE2 
2972 N N   . ASP A 360 ? 0.3223 0.2658 0.2428 -0.0485 0.007   -0.0059 360 ASP A N   
2973 C CA  . ASP A 360 ? 0.3361 0.293  0.2687 -0.0433 0.0046  -0.0047 360 ASP A CA  
2974 C C   . ASP A 360 ? 0.3576 0.3218 0.2887 -0.049  0.0028  -0.0047 360 ASP A C   
2975 O O   . ASP A 360 ? 0.3539 0.311  0.2782 -0.05   0.0045  -0.0062 360 ASP A O   
2976 C CB  . ASP A 360 ? 0.323  0.2745 0.2593 -0.0351 0.0061  -0.0055 360 ASP A CB  
2977 C CG  . ASP A 360 ? 0.3085 0.2713 0.2573 -0.0304 0.0044  -0.0044 360 ASP A CG  
2978 O OD1 . ASP A 360 ? 0.3348 0.3087 0.2882 -0.0328 0.0019  -0.0025 360 ASP A OD1 
2979 O OD2 . ASP A 360 ? 0.3291 0.2897 0.2834 -0.0243 0.0057  -0.0055 360 ASP A OD2 
2980 N N   . LYS A 361 ? 0.3409 0.32   0.2785 -0.0519 -0.0006 -0.0031 361 LYS A N   
2981 C CA  . LYS A 361 ? 0.3572 0.3455 0.2938 -0.0564 -0.0038 -0.0026 361 LYS A CA  
2982 C C   . LYS A 361 ? 0.3429 0.3378 0.2865 -0.0499 -0.0057 0.0002  361 LYS A C   
2983 O O   . LYS A 361 ? 0.3441 0.3455 0.2855 -0.052  -0.0087 0.0016  361 LYS A O   
2984 C CB  . LYS A 361 ? 0.3601 0.3631 0.3018 -0.062  -0.0069 -0.0022 361 LYS A CB  
2985 C CG  . LYS A 361 ? 0.3879 0.3847 0.3223 -0.0708 -0.0045 -0.0047 361 LYS A CG  
2986 C CD  . LYS A 361 ? 0.4671 0.4822 0.408  -0.0781 -0.0077 -0.005  361 LYS A CD  
2987 C CE  . LYS A 361 ? 0.6667 0.6768 0.5992 -0.0901 -0.0061 -0.0081 361 LYS A CE  
2988 N NZ  . LYS A 361 ? 0.7645 0.7599 0.6916 -0.0913 -0.0003 -0.0082 361 LYS A NZ  
2989 N N   . LEU A 362 ? 0.3522 0.3451 0.3034 -0.0424 -0.0041 0.0011  362 LEU A N   
2990 C CA  . LEU A 362 ? 0.3296 0.3253 0.287  -0.037  -0.0046 0.0035  362 LEU A CA  
2991 C C   . LEU A 362 ? 0.3264 0.3113 0.2775 -0.0364 -0.0005 0.0026  362 LEU A C   
2992 O O   . LEU A 362 ? 0.3269 0.3112 0.2727 -0.0376 -0.0005 0.0044  362 LEU A O   
2993 C CB  . LEU A 362 ? 0.3552 0.3547 0.3246 -0.0306 -0.0048 0.0038  362 LEU A CB  
2994 C CG  . LEU A 362 ? 0.3931 0.394  0.3698 -0.0257 -0.005  0.0061  362 LEU A CG  
2995 C CD1 . LEU A 362 ? 0.4353 0.4437 0.412  -0.0258 -0.0085 0.01    362 LEU A CD1 
2996 C CD2 . LEU A 362 ? 0.4171 0.4202 0.4043 -0.0204 -0.0053 0.005   362 LEU A CD2 
2997 N N   . SER A 363 ? 0.3187 0.295  0.2701 -0.0339 0.0031  -0.0001 363 SER A N   
2998 C CA  . SER A 363 ? 0.3242 0.2928 0.2738 -0.0318 0.0078  -0.0015 363 SER A CA  
2999 C C   . SER A 363 ? 0.3376 0.2984 0.2727 -0.0367 0.0103  -0.003  363 SER A C   
3000 O O   . SER A 363 ? 0.3367 0.2934 0.2688 -0.0359 0.0146  -0.0034 363 SER A O   
3001 C CB  . SER A 363 ? 0.3494 0.3128 0.304  -0.0269 0.0101  -0.0044 363 SER A CB  
3002 O OG  . SER A 363 ? 0.3541 0.3246 0.3208 -0.0226 0.0073  -0.0037 363 SER A OG  
3003 N N   . ILE A 364 ? 0.3491 0.3079 0.2749 -0.0424 0.0082  -0.0043 364 ILE A N   
3004 C CA  . ILE A 364 ? 0.3538 0.3041 0.2641 -0.0483 0.01    -0.007  364 ILE A CA  
3005 C C   . ILE A 364 ? 0.4044 0.3585 0.3086 -0.0501 0.0093  -0.0048 364 ILE A C   
3006 O O   . ILE A 364 ? 0.3715 0.3171 0.2625 -0.0531 0.0124  -0.0073 364 ILE A O   
3007 C CB  . ILE A 364 ? 0.3314 0.281  0.2353 -0.0555 0.007   -0.0087 364 ILE A CB  
3008 C CG1 . ILE A 364 ? 0.3783 0.314  0.2651 -0.0618 0.0097  -0.0134 364 ILE A CG1 
3009 C CG2 . ILE A 364 ? 0.3461 0.3114 0.2545 -0.0593 0.0006  -0.0059 364 ILE A CG2 
3010 C CD1 . ILE A 364 ? 0.3798 0.3132 0.2607 -0.0705 0.0074  -0.0157 364 ILE A CD1 
3011 N N   . LYS A 365 ? 0.397  0.3623 0.3095 -0.0478 0.0054  -0.0001 365 LYS A N   
3012 C CA  . LYS A 365 ? 0.4384 0.4063 0.3445 -0.0482 0.0042  0.0035  365 LYS A CA  
3013 C C   . LYS A 365 ? 0.4244 0.3832 0.3258 -0.0461 0.0116  0.003   365 LYS A C   
3014 O O   . LYS A 365 ? 0.4439 0.3994 0.332  -0.0487 0.0127  0.004   365 LYS A O   
3015 C CB  . LYS A 365 ? 0.4814 0.4598 0.3983 -0.044  -0.0002 0.0091  365 LYS A CB  
3016 C CG  . LYS A 365 ? 0.7021 0.6932 0.6248 -0.0454 -0.0074 0.0099  365 LYS A CG  
3017 C CD  . LYS A 365 ? 0.7929 0.7933 0.7297 -0.0392 -0.0106 0.014   365 LYS A CD  
3018 C CE  . LYS A 365 ? 0.7564 0.7694 0.7027 -0.0396 -0.0152 0.0132  365 LYS A CE  
3019 N NZ  . LYS A 365 ? 0.5527 0.5755 0.5108 -0.0331 -0.0188 0.017   365 LYS A NZ  
3020 N N   . MET A 366 ? 0.391  0.3468 0.3031 -0.0416 0.0166  0.0014  366 MET A N   
3021 C CA  . MET A 366 ? 0.4338 0.3842 0.3451 -0.0397 0.0243  0.0009  366 MET A CA  
3022 C C   . MET A 366 ? 0.4246 0.3652 0.3195 -0.0429 0.0292  -0.0033 366 MET A C   
3023 O O   . MET A 366 ? 0.4116 0.3492 0.2952 -0.0448 0.0326  -0.0017 366 MET A O   
3024 C CB  . MET A 366 ? 0.4494 0.4011 0.3771 -0.0344 0.0279  -0.0012 366 MET A CB  
3025 C CG  . MET A 366 ? 0.4948 0.4546 0.4381 -0.0313 0.0237  0.0016  366 MET A CG  
3026 S SD  . MET A 366 ? 0.4819 0.4437 0.4425 -0.026  0.0276  -0.0023 366 MET A SD  
3027 C CE  . MET A 366 ? 0.4515 0.4074 0.4077 -0.0238 0.0275  -0.0074 366 MET A CE  
3028 N N   . PRO A 367 ? 0.3653 0.2988 0.2562 -0.0434 0.0304  -0.0087 367 PRO A N   
3029 C CA  . PRO A 367 ? 0.4005 0.3226 0.2744 -0.0463 0.0355  -0.0135 367 PRO A CA  
3030 C C   . PRO A 367 ? 0.4148 0.3358 0.2707 -0.0535 0.0312  -0.0131 367 PRO A C   
3031 O O   . PRO A 367 ? 0.4392 0.3526 0.2794 -0.0558 0.0358  -0.0157 367 PRO A O   
3032 C CB  . PRO A 367 ? 0.3762 0.2894 0.2507 -0.0446 0.0367  -0.0186 367 PRO A CB  
3033 C CG  . PRO A 367 ? 0.3553 0.2763 0.2419 -0.0441 0.0296  -0.0156 367 PRO A CG  
3034 C CD  . PRO A 367 ? 0.3681 0.3013 0.2691 -0.0405 0.0283  -0.0107 367 PRO A CD  
3035 N N   . LEU A 368 ? 0.4118 0.3415 0.2702 -0.0567 0.0225  -0.0102 368 LEU A N   
3036 C CA  . LEU A 368 ? 0.4404 0.3722 0.2832 -0.0634 0.0169  -0.0102 368 LEU A CA  
3037 C C   . LEU A 368 ? 0.4688 0.4032 0.3036 -0.0624 0.0174  -0.0052 368 LEU A C   
3038 O O   . LEU A 368 ? 0.4576 0.3874 0.2736 -0.0666 0.0173  -0.0069 368 LEU A O   
3039 C CB  . LEU A 368 ? 0.4179 0.3618 0.2687 -0.0664 0.0077  -0.0082 368 LEU A CB  
3040 C CG  . LEU A 368 ? 0.3983 0.3383 0.2526 -0.0698 0.0072  -0.0128 368 LEU A CG  
3041 C CD1 . LEU A 368 ? 0.4218 0.3764 0.2871 -0.0719 -0.0002 -0.0101 368 LEU A CD1 
3042 C CD2 . LEU A 368 ? 0.4368 0.3643 0.2731 -0.0772 0.0089  -0.0194 368 LEU A CD2 
3043 N N   . ILE A 369 ? 0.4368 0.3773 0.2842 -0.057  0.0179  0.0008  369 ILE A N   
3044 C CA  . ILE A 369 ? 0.4717 0.4112 0.3111 -0.0556 0.0203  0.0062  369 ILE A CA  
3045 C C   . ILE A 369 ? 0.4877 0.4157 0.3129 -0.0568 0.0304  0.0028  369 ILE A C   
3046 O O   . ILE A 369 ? 0.488  0.4123 0.2944 -0.0593 0.031   0.0048  369 ILE A O   
3047 C CB  . ILE A 369 ? 0.484  0.4285 0.3408 -0.0501 0.0211  0.0122  369 ILE A CB  
3048 C CG1 . ILE A 369 ? 0.5007 0.4561 0.3666 -0.0485 0.0111  0.0164  369 ILE A CG1 
3049 C CG2 . ILE A 369 ? 0.5532 0.4922 0.4019 -0.0491 0.0273  0.0175  369 ILE A CG2 
3050 C CD1 . ILE A 369 ? 0.5265 0.486  0.4117 -0.043  0.0113  0.02    369 ILE A CD1 
3051 N N   . GLN A 370 ? 0.4473 0.3702 0.2808 -0.0545 0.0383  -0.0024 370 GLN A N   
3052 C CA  . GLN A 370 ? 0.4612 0.3749 0.2838 -0.0545 0.0489  -0.0062 370 GLN A CA  
3053 C C   . GLN A 370 ? 0.494  0.3985 0.2936 -0.0597 0.0485  -0.0122 370 GLN A C   
3054 O O   . GLN A 370 ? 0.5085 0.4061 0.2894 -0.0618 0.0543  -0.0135 370 GLN A O   
3055 C CB  . GLN A 370 ? 0.4717 0.3843 0.3109 -0.0495 0.0567  -0.0106 370 GLN A CB  
3056 C CG  . GLN A 370 ? 0.435  0.3566 0.2963 -0.0453 0.058   -0.006  370 GLN A CG  
3057 C CD  . GLN A 370 ? 0.481  0.4032 0.3385 -0.0465 0.0633  -0.0002 370 GLN A CD  
3058 O OE1 . GLN A 370 ? 0.5317 0.4586 0.3962 -0.0462 0.0592  0.0063  370 GLN A OE1 
3059 N NE2 . GLN A 370 ? 0.4462 0.3622 0.2909 -0.0479 0.0727  -0.0025 370 GLN A NE2 
3060 N N   . LEU A 371 ? 0.4608 0.3645 0.2603 -0.0626 0.0418  -0.0162 371 LEU A N   
3061 C CA  . LEU A 371 ? 0.4739 0.3683 0.251  -0.0691 0.0406  -0.0224 371 LEU A CA  
3062 C C   . LEU A 371 ? 0.4741 0.373  0.2337 -0.074  0.0338  -0.0188 371 LEU A C   
3063 O O   . LEU A 371 ? 0.533  0.4234 0.2699 -0.078  0.0363  -0.023  371 LEU A O   
3064 C CB  . LEU A 371 ? 0.4549 0.3469 0.2367 -0.0723 0.0354  -0.0271 371 LEU A CB  
3065 C CG  . LEU A 371 ? 0.4477 0.3305 0.2397 -0.0673 0.0422  -0.0316 371 LEU A CG  
3066 C CD1 . LEU A 371 ? 0.4458 0.3273 0.244  -0.0703 0.0363  -0.0334 371 LEU A CD1 
3067 C CD2 . LEU A 371 ? 0.5036 0.3706 0.2796 -0.0671 0.0513  -0.0389 371 LEU A CD2 
3068 N N   . GLU A 372 ? 0.5224 0.4345 0.2914 -0.0729 0.0252  -0.0112 372 GLU A N   
3069 C CA  . GLU A 372 ? 0.6112 0.5283 0.3642 -0.0755 0.0181  -0.0065 372 GLU A CA  
3070 C C   . GLU A 372 ? 0.6511 0.5603 0.388  -0.0736 0.0264  -0.0032 372 GLU A C   
3071 O O   . GLU A 372 ? 0.5847 0.49   0.2975 -0.0773 0.0246  -0.0037 372 GLU A O   
3072 C CB  . GLU A 372 ? 0.6421 0.574  0.4107 -0.0723 0.0087  0.0015  372 GLU A CB  
3073 C CG  . GLU A 372 ? 0.7478 0.6869 0.5009 -0.0743 -0.0015 0.0059  372 GLU A CG  
3074 C CD  . GLU A 372 ? 0.8775 0.8302 0.6457 -0.069  -0.0098 0.0146  372 GLU A CD  
3075 O OE1 . GLU A 372 ? 0.9738 0.9401 0.7491 -0.0707 -0.0203 0.0142  372 GLU A OE1 
3076 O OE2 . GLU A 372 ? 1.036  0.9852 0.8087 -0.0631 -0.0051 0.0216  372 GLU A OE2 
3077 N N   . LYS A 373 ? 0.6226 0.5298 0.3725 -0.0684 0.0358  -0.0001 373 LYS A N   
3078 C CA  . LYS A 373 ? 0.6946 0.5941 0.4316 -0.0673 0.0462  0.0027  373 LYS A CA  
3079 C C   . LYS A 373 ? 0.6254 0.5132 0.3439 -0.0702 0.0555  -0.0059 373 LYS A C   
3080 O O   . LYS A 373 ? 0.7055 0.5868 0.4041 -0.0714 0.0618  -0.0044 373 LYS A O   
3081 C CB  . LYS A 373 ? 0.6963 0.5976 0.4547 -0.0624 0.055   0.0065  373 LYS A CB  
3082 C CG  . LYS A 373 ? 0.8392 0.7484 0.6104 -0.0595 0.048   0.0159  373 LYS A CG  
3083 C CD  . LYS A 373 ? 0.9394 0.85   0.7311 -0.0559 0.0555  0.0197  373 LYS A CD  
3084 C CE  . LYS A 373 ? 1.0609 0.9717 0.8515 -0.0543 0.0521  0.0301  373 LYS A CE  
3085 N NZ  . LYS A 373 ? 1.1314 1.0468 0.9476 -0.051  0.053   0.0326  373 LYS A NZ  
3086 N N   . MET A 374 ? 0.5921 0.4759 0.316  -0.0709 0.0568  -0.0148 374 MET A N   
3087 C CA  . MET A 374 ? 0.6351 0.506  0.3416 -0.0728 0.0655  -0.0241 374 MET A CA  
3088 C C   . MET A 374 ? 0.6577 0.523  0.3391 -0.0801 0.0577  -0.0295 374 MET A C   
3089 O O   . MET A 374 ? 0.6617 0.5144 0.3284 -0.0824 0.0634  -0.0388 374 MET A O   
3090 C CB  . MET A 374 ? 0.6207 0.4875 0.3446 -0.0687 0.0715  -0.0309 374 MET A CB  
3091 C CG  . MET A 374 ? 0.6901 0.5636 0.4377 -0.0618 0.0798  -0.0271 374 MET A CG  
3092 S SD  . MET A 374 ? 0.7259 0.5992 0.4982 -0.0555 0.0818  -0.0326 374 MET A SD  
3093 C CE  . MET A 374 ? 0.7314 0.592  0.4933 -0.0521 0.0966  -0.0423 374 MET A CE  
3094 N N   . GLY A 375 ? 0.6266 0.5012 0.3031 -0.0836 0.0448  -0.0242 375 GLY A N   
3095 C CA  . GLY A 375 ? 0.6334 0.5055 0.2857 -0.0912 0.0364  -0.029  375 GLY A CA  
3096 C C   . GLY A 375 ? 0.6326 0.506  0.2911 -0.097  0.0281  -0.0362 375 GLY A C   
3097 O O   . GLY A 375 ? 0.6184 0.4886 0.2571 -0.1047 0.0221  -0.0423 375 GLY A O   
3098 N N   . GLU A 376 ? 0.5508 0.4286 0.2351 -0.0944 0.0275  -0.0356 376 GLU A N   
3099 C CA  . GLU A 376 ? 0.5713 0.4504 0.2604 -0.101  0.0198  -0.0412 376 GLU A CA  
3100 C C   . GLU A 376 ? 0.5917 0.4893 0.2843 -0.105  0.0054  -0.0362 376 GLU A C   
3101 O O   . GLU A 376 ? 0.5286 0.4383 0.2291 -0.0996 0.0016  -0.0268 376 GLU A O   
3102 C CB  . GLU A 376 ? 0.5452 0.4227 0.2585 -0.0964 0.0241  -0.0413 376 GLU A CB  
3103 C CG  . GLU A 376 ? 0.5538 0.413  0.2633 -0.0925 0.0368  -0.0479 376 GLU A CG  
3104 C CD  . GLU A 376 ? 0.6458 0.4873 0.3342 -0.0993 0.0392  -0.0587 376 GLU A CD  
3105 O OE1 . GLU A 376 ? 0.7267 0.5542 0.4004 -0.0971 0.049   -0.0642 376 GLU A OE1 
3106 O OE2 . GLU A 376 ? 0.7514 0.5929 0.4384 -0.1073 0.0315  -0.0621 376 GLU A OE2 
3107 N N   . ASN A 377 ? 0.6281 0.5274 0.3149 -0.1145 -0.0024 -0.0428 377 ASN A N   
3108 C CA  . ASN A 377 ? 0.6018 0.52   0.2897 -0.1196 -0.0165 -0.0404 377 ASN A CA  
3109 C C   . ASN A 377 ? 0.5457 0.4818 0.2617 -0.1136 -0.0213 -0.0317 377 ASN A C   
3110 O O   . ASN A 377 ? 0.553  0.4897 0.2869 -0.1143 -0.0195 -0.0332 377 ASN A O   
3111 C CB  . ASN A 377 ? 0.6026 0.5198 0.2832 -0.1322 -0.0225 -0.0504 377 ASN A CB  
3112 C CG  . ASN A 377 ? 0.639  0.5789 0.3213 -0.1378 -0.0377 -0.0486 377 ASN A CG  
3113 O OD1 . ASN A 377 ? 0.657  0.6145 0.351  -0.1309 -0.0441 -0.0393 377 ASN A OD1 
3114 N ND2 . ASN A 377 ? 0.6647 0.6053 0.3349 -0.1499 -0.0442 -0.0578 377 ASN A ND2 
3115 N N   . PRO A 378 ? 0.5302 0.4803 0.2498 -0.1076 -0.0276 -0.0224 378 PRO A N   
3116 C CA  . PRO A 378 ? 0.5271 0.4928 0.2726 -0.1011 -0.0315 -0.0147 378 PRO A CA  
3117 C C   . PRO A 378 ? 0.4788 0.4603 0.2403 -0.1071 -0.0399 -0.0177 378 PRO A C   
3118 O O   . PRO A 378 ? 0.4937 0.483  0.2775 -0.1029 -0.0393 -0.0144 378 PRO A O   
3119 C CB  . PRO A 378 ? 0.5824 0.5571 0.3213 -0.0948 -0.0379 -0.0054 378 PRO A CB  
3120 C CG  . PRO A 378 ? 0.6102 0.5686 0.322  -0.0955 -0.0315 -0.0067 378 PRO A CG  
3121 C CD  . PRO A 378 ? 0.6067 0.5562 0.3044 -0.1057 -0.0303 -0.0184 378 PRO A CD  
3122 N N   . ARG A 379 ? 0.4903 0.4775 0.2405 -0.117  -0.0476 -0.024  379 ARG A N   
3123 C CA  . ARG A 379 ? 0.4951 0.4985 0.2603 -0.1246 -0.0549 -0.0276 379 ARG A CA  
3124 C C   . ARG A 379 ? 0.47   0.4617 0.2462 -0.1282 -0.0462 -0.0323 379 ARG A C   
3125 O O   . ARG A 379 ? 0.4634 0.4679 0.2604 -0.1282 -0.048  -0.0305 379 ARG A O   
3126 C CB  . ARG A 379 ? 0.5138 0.5243 0.2634 -0.136  -0.0644 -0.0348 379 ARG A CB  
3127 C CG  . ARG A 379 ? 0.5149 0.5473 0.2809 -0.145  -0.0735 -0.0385 379 ARG A CG  
3128 C CD  . ARG A 379 ? 0.5384 0.5963 0.3293 -0.1366 -0.0801 -0.0299 379 ARG A CD  
3129 N NE  . ARG A 379 ? 0.5317 0.616  0.3388 -0.1447 -0.0898 -0.0333 379 ARG A NE  
3130 C CZ  . ARG A 379 ? 0.5141 0.6151 0.3146 -0.1517 -0.1016 -0.0371 379 ARG A CZ  
3131 N NH1 . ARG A 379 ? 0.5535 0.6489 0.3296 -0.1507 -0.1068 -0.0372 379 ARG A NH1 
3132 N NH2 . ARG A 379 ? 0.5357 0.6616 0.355  -0.1595 -0.1087 -0.0406 379 ARG A NH2 
3133 N N   . LEU A 380 ? 0.5107 0.4782 0.2715 -0.131  -0.037  -0.0385 380 LEU A N   
3134 C CA  . LEU A 380 ? 0.5131 0.466  0.2811 -0.1328 -0.0285 -0.0423 380 LEU A CA  
3135 C C   . LEU A 380 ? 0.4965 0.45   0.2829 -0.1212 -0.0229 -0.035  380 LEU A C   
3136 O O   . LEU A 380 ? 0.4589 0.4151 0.2607 -0.1219 -0.0216 -0.0345 380 LEU A O   
3137 C CB  . LEU A 380 ? 0.5586 0.4847 0.306  -0.1368 -0.0201 -0.0505 380 LEU A CB  
3138 C CG  . LEU A 380 ? 0.6089 0.5303 0.3365 -0.15   -0.0247 -0.0598 380 LEU A CG  
3139 C CD1 . LEU A 380 ? 0.6668 0.5596 0.3743 -0.1512 -0.0149 -0.0676 380 LEU A CD1 
3140 C CD2 . LEU A 380 ? 0.6412 0.5727 0.378  -0.1622 -0.031  -0.064  380 LEU A CD2 
3141 N N   . LEU A 381 ? 0.435  0.3879 0.2205 -0.1113 -0.0202 -0.0291 381 LEU A N   
3142 C CA  . LEU A 381 ? 0.4476 0.4026 0.2511 -0.1009 -0.0157 -0.0226 381 LEU A CA  
3143 C C   . LEU A 381 ? 0.4493 0.4254 0.2732 -0.0989 -0.023  -0.0173 381 LEU A C   
3144 O O   . LEU A 381 ? 0.4408 0.4183 0.2808 -0.0949 -0.0201 -0.0154 381 LEU A O   
3145 C CB  . LEU A 381 ? 0.4547 0.4044 0.2522 -0.0927 -0.0109 -0.0179 381 LEU A CB  
3146 C CG  . LEU A 381 ? 0.5049 0.4353 0.2829 -0.0939 -0.0024 -0.0233 381 LEU A CG  
3147 C CD1 . LEU A 381 ? 0.5461 0.4746 0.3183 -0.0871 0.0021  -0.0179 381 LEU A CD1 
3148 C CD2 . LEU A 381 ? 0.5071 0.4221 0.2881 -0.0928 0.0063  -0.0285 381 LEU A CD2 
3149 N N   . LYS A 382 ? 0.4291 0.4224 0.2524 -0.1018 -0.0328 -0.0156 382 LYS A N   
3150 C CA  . LYS A 382 ? 0.4339 0.4487 0.277  -0.0996 -0.0395 -0.0114 382 LYS A CA  
3151 C C   . LYS A 382 ? 0.3781 0.3973 0.2315 -0.1077 -0.0393 -0.0164 382 LYS A C   
3152 O O   . LYS A 382 ? 0.4118 0.4381 0.2827 -0.1037 -0.0377 -0.0136 382 LYS A O   
3153 C CB  . LYS A 382 ? 0.4689 0.5016 0.3083 -0.1002 -0.0506 -0.0089 382 LYS A CB  
3154 C CG  . LYS A 382 ? 0.5199 0.5771 0.38   -0.0961 -0.0582 -0.0044 382 LYS A CG  
3155 C CD  . LYS A 382 ? 0.6955 0.7686 0.548  -0.0962 -0.0699 -0.0023 382 LYS A CD  
3156 C CE  . LYS A 382 ? 0.7986 0.9    0.6705 -0.096  -0.0793 -0.0012 382 LYS A CE  
3157 N NZ  . LYS A 382 ? 0.7872 0.8958 0.6788 -0.0846 -0.0775 0.0053  382 LYS A NZ  
3158 N N   . ILE A 383 ? 0.3921 0.4038 0.2331 -0.1191 -0.0393 -0.0239 383 ILE A N   
3159 C CA  . ILE A 383 ? 0.3999 0.4124 0.2481 -0.1286 -0.0379 -0.0286 383 ILE A CA  
3160 C C   . ILE A 383 ? 0.4076 0.4038 0.2615 -0.1236 -0.0282 -0.0274 383 ILE A C   
3161 O O   . ILE A 383 ? 0.4217 0.4249 0.2893 -0.1254 -0.0271 -0.0266 383 ILE A O   
3162 C CB  . ILE A 383 ? 0.4012 0.4051 0.2325 -0.1425 -0.0394 -0.0374 383 ILE A CB  
3163 C CG1 . ILE A 383 ? 0.4116 0.4371 0.2412 -0.1479 -0.0508 -0.0386 383 ILE A CG1 
3164 C CG2 . ILE A 383 ? 0.4221 0.4184 0.2578 -0.1526 -0.0348 -0.0421 383 ILE A CG2 
3165 C CD1 . ILE A 383 ? 0.4328 0.4496 0.2428 -0.1611 -0.0533 -0.0478 383 ILE A CD1 
3166 N N   . ILE A 384 ? 0.4276 0.4042 0.2718 -0.1168 -0.0214 -0.0271 384 ILE A N   
3167 C CA  . ILE A 384 ? 0.427  0.3887 0.2759 -0.1107 -0.0133 -0.026  384 ILE A CA  
3168 C C   . ILE A 384 ? 0.4306 0.4059 0.2991 -0.1016 -0.014  -0.0195 384 ILE A C   
3169 O O   . ILE A 384 ? 0.4301 0.3995 0.3055 -0.0994 -0.0098 -0.0189 384 ILE A O   
3170 C CB  . ILE A 384 ? 0.4295 0.3707 0.2652 -0.1052 -0.0063 -0.0278 384 ILE A CB  
3171 C CG1 . ILE A 384 ? 0.4604 0.384  0.2764 -0.1145 -0.004  -0.0357 384 ILE A CG1 
3172 C CG2 . ILE A 384 ? 0.4443 0.3753 0.2884 -0.096  0.0004  -0.0255 384 ILE A CG2 
3173 C CD1 . ILE A 384 ? 0.4832 0.3882 0.2847 -0.1096 0.003   -0.0385 384 ILE A CD1 
3174 N N   . THR A 385 ? 0.4269 0.4198 0.3036 -0.0966 -0.0197 -0.0147 385 THR A N   
3175 C CA  . THR A 385 ? 0.4353 0.4404 0.3299 -0.0882 -0.0205 -0.0094 385 THR A CA  
3176 C C   . THR A 385 ? 0.4634 0.485  0.371  -0.0928 -0.0238 -0.0097 385 THR A C   
3177 O O   . THR A 385 ? 0.4978 0.5261 0.4188 -0.0863 -0.0227 -0.0065 385 THR A O   
3178 C CB  . THR A 385 ? 0.4532 0.4676 0.3508 -0.0802 -0.0245 -0.0039 385 THR A CB  
3179 O OG1 . THR A 385 ? 0.534  0.5653 0.4315 -0.0846 -0.0328 -0.0036 385 THR A OG1 
3180 C CG2 . THR A 385 ? 0.4475 0.4466 0.3321 -0.0767 -0.0202 -0.0033 385 THR A CG2 
3181 N N   . MET A 386 ? 0.4787 0.5072 0.3831 -0.104  -0.0271 -0.0138 386 MET A N   
3182 C CA  . MET A 386 ? 0.4844 0.5338 0.4035 -0.1088 -0.0304 -0.014  386 MET A CA  
3183 C C   . MET A 386 ? 0.5132 0.5569 0.4389 -0.1102 -0.0237 -0.0143 386 MET A C   
3184 O O   . MET A 386 ? 0.611  0.6315 0.5246 -0.1128 -0.0176 -0.0166 386 MET A O   
3185 C CB  . MET A 386 ? 0.4702 0.5285 0.3842 -0.1222 -0.0355 -0.0192 386 MET A CB  
3186 C CG  . MET A 386 ? 0.4473 0.5186 0.3569 -0.1213 -0.0445 -0.0187 386 MET A CG  
3187 S SD  . MET A 386 ? 0.456  0.5358 0.3579 -0.139  -0.0506 -0.0268 386 MET A SD  
3188 C CE  . MET A 386 ? 0.4964 0.6111 0.4245 -0.1429 -0.0555 -0.0264 386 MET A CE  
3189 N N   . MET B 1   ? 1.0162 1.0476 1.0992 -0.1397 0.3272  -0.007  1   MET B N   
3190 C CA  . MET B 1   ? 0.9949 0.9914 1.0386 -0.138  0.3196  0.0034  1   MET B CA  
3191 C C   . MET B 1   ? 0.8925 0.8889 0.9479 -0.1352 0.299   0.0045  1   MET B C   
3192 O O   . MET B 1   ? 0.8668 0.8815 0.9534 -0.1423 0.2956  0.0002  1   MET B O   
3193 C CB  . MET B 1   ? 0.987  0.9609 1.0069 -0.152  0.3361  0.0108  1   MET B CB  
3194 C CG  . MET B 1   ? 1.0395 0.9765 1.0126 -0.1472 0.3327  0.022   1   MET B CG  
3195 S SD  . MET B 1   ? 1.2958 1.2038 1.231  -0.1584 0.3558  0.0313  1   MET B SD  
3196 C CE  . MET B 1   ? 1.2722 1.1666 1.2133 -0.1771 0.3635  0.0357  1   MET B CE  
3197 N N   . GLU B 2   ? 0.8804 0.8562 0.9099 -0.1252 0.2852  0.0102  2   GLU B N   
3198 C CA  . GLU B 2   ? 0.8441 0.8179 0.8813 -0.1219 0.266   0.0115  2   GLU B CA  
3199 C C   . GLU B 2   ? 0.8071 0.7609 0.8328 -0.1337 0.2687  0.018   2   GLU B C   
3200 O O   . GLU B 2   ? 0.774  0.7076 0.7754 -0.1406 0.2828  0.024   2   GLU B O   
3201 C CB  . GLU B 2   ? 0.8763 0.8412 0.8961 -0.1069 0.2504  0.0132  2   GLU B CB  
3202 C CG  . GLU B 2   ? 0.9126 0.8559 0.8932 -0.1008 0.2551  0.0187  2   GLU B CG  
3203 C CD  . GLU B 2   ? 0.8555 0.8078 0.8326 -0.0963 0.2658  0.0137  2   GLU B CD  
3204 O OE1 . GLU B 2   ? 0.9045 0.855  0.8758 -0.1045 0.2835  0.0145  2   GLU B OE1 
3205 O OE2 . GLU B 2   ? 0.7827 0.7417 0.7603 -0.0858 0.2581  0.0092  2   GLU B OE2 
3206 N N   . LEU B 3   ? 0.7404 0.6998 0.7843 -0.1365 0.2562  0.0165  3   LEU B N   
3207 C CA  . LEU B 3   ? 0.7728 0.717  0.813  -0.1491 0.2588  0.0202  3   LEU B CA  
3208 C C   . LEU B 3   ? 0.7984 0.7049 0.7966 -0.1463 0.2591  0.0309  3   LEU B C   
3209 O O   . LEU B 3   ? 0.8424 0.7287 0.8263 -0.1572 0.2704  0.0358  3   LEU B O   
3210 C CB  . LEU B 3   ? 0.7549 0.7128 0.8206 -0.1507 0.2431  0.0157  3   LEU B CB  
3211 C CG  . LEU B 3   ? 0.7565 0.7521 0.8657 -0.1554 0.2422  0.0057  3   LEU B CG  
3212 C CD1 . LEU B 3   ? 0.7475 0.7548 0.8757 -0.1526 0.2229  0.0024  3   LEU B CD1 
3213 C CD2 . LEU B 3   ? 0.7917 0.7953 0.9151 -0.1735 0.2597  0.0026  3   LEU B CD2 
3214 N N   . ILE B 4   ? 0.7541 0.6513 0.733  -0.1317 0.2469  0.0344  4   ILE B N   
3215 C CA  . ILE B 4   ? 0.7683 0.6333 0.7083 -0.126  0.2451  0.0444  4   ILE B CA  
3216 C C   . ILE B 4   ? 0.8027 0.6501 0.7157 -0.1302 0.2635  0.0505  4   ILE B C   
3217 O O   . ILE B 4   ? 0.8435 0.6631 0.7321 -0.1345 0.2695  0.0588  4   ILE B O   
3218 C CB  . ILE B 4   ? 0.7389 0.603  0.6665 -0.1097 0.2285  0.0456  4   ILE B CB  
3219 C CG1 . ILE B 4   ? 0.7453 0.5791 0.6354 -0.103  0.2249  0.0558  4   ILE B CG1 
3220 C CG2 . ILE B 4   ? 0.7401 0.6196 0.6685 -0.1017 0.2303  0.0412  4   ILE B CG2 
3221 C CD1 . ILE B 4   ? 0.8127 0.6257 0.6968 -0.1097 0.2246  0.0609  4   ILE B CD1 
3222 N N   . ARG B 5   ? 0.7981 0.6603 0.7149 -0.1291 0.273   0.0465  5   ARG B N   
3223 C CA  . ARG B 5   ? 0.8814 0.7288 0.7723 -0.133  0.2912  0.0517  5   ARG B CA  
3224 C C   . ARG B 5   ? 0.8798 0.7193 0.7757 -0.1504 0.3082  0.0532  5   ARG B C   
3225 O O   . ARG B 5   ? 0.8632 0.6749 0.7273 -0.154  0.3197  0.0623  5   ARG B O   
3226 C CB  . ARG B 5   ? 0.9051 0.7717 0.8005 -0.1278 0.2974  0.0455  5   ARG B CB  
3227 C CG  . ARG B 5   ? 0.918  0.7782 0.7896 -0.1121 0.285   0.0477  5   ARG B CG  
3228 C CD  . ARG B 5   ? 0.9118 0.7931 0.7931 -0.1056 0.2867  0.0393  5   ARG B CD  
3229 N NE  . ARG B 5   ? 0.9071 0.7826 0.7683 -0.1092 0.3053  0.0407  5   ARG B NE  
3230 C CZ  . ARG B 5   ? 0.9476 0.8419 0.825  -0.1127 0.3186  0.0329  5   ARG B CZ  
3231 N NH1 . ARG B 5   ? 0.9025 0.7873 0.7574 -0.1174 0.3365  0.0358  5   ARG B NH1 
3232 N NH2 . ARG B 5   ? 0.8979 0.82   0.813  -0.1113 0.3148  0.0227  5   ARG B NH2 
3233 N N   . ILE B 6   ? 0.8874 0.7504 0.8217 -0.1608 0.3091  0.0448  6   ILE B N   
3234 C CA  . ILE B 6   ? 0.9078 0.7675 0.852  -0.1793 0.3247  0.0442  6   ILE B CA  
3235 C C   . ILE B 6   ? 0.9243 0.7499 0.8454 -0.1838 0.3226  0.0528  6   ILE B C   
3236 O O   . ILE B 6   ? 0.9243 0.7251 0.8238 -0.194  0.3389  0.0593  6   ILE B O   
3237 C CB  . ILE B 6   ? 0.9135 0.8101 0.9061 -0.1884 0.3233  0.0324  6   ILE B CB  
3238 C CG1 . ILE B 6   ? 0.9227 0.8512 0.9376 -0.1851 0.33    0.0242  6   ILE B CG1 
3239 C CG2 . ILE B 6   ? 0.9351 0.827  0.938  -0.2091 0.3367  0.0313  6   ILE B CG2 
3240 C CD1 . ILE B 6   ? 0.9013 0.8697 0.9644 -0.1872 0.3228  0.0128  6   ILE B CD1 
3241 N N   . ALA B 7   ? 0.8599 0.6838 0.7858 -0.1765 0.3036  0.0526  7   ALA B N   
3242 C CA  . ALA B 7   ? 0.8625 0.6556 0.7696 -0.1797 0.3005  0.0594  7   ALA B CA  
3243 C C   . ALA B 7   ? 0.8963 0.6518 0.7565 -0.1719 0.306   0.0723  7   ALA B C   
3244 O O   . ALA B 7   ? 0.8863 0.6115 0.7261 -0.1804 0.3167  0.0793  7   ALA B O   
3245 C CB  . ALA B 7   ? 0.8467 0.6482 0.7677 -0.1715 0.2791  0.056   7   ALA B CB  
3246 N N   . MET B 8   ? 0.8846 0.6422 0.7276 -0.156  0.2989  0.0754  8   MET B N   
3247 C CA  . MET B 8   ? 0.9101 0.6364 0.709  -0.1462 0.3014  0.0874  8   MET B CA  
3248 C C   . MET B 8   ? 0.9548 0.6623 0.7315 -0.156  0.3239  0.0937  8   MET B C   
3249 O O   . MET B 8   ? 0.9373 0.6099 0.681  -0.1557 0.3302  0.1047  8   MET B O   
3250 C CB  . MET B 8   ? 0.9134 0.6508 0.7014 -0.1287 0.2891  0.0875  8   MET B CB  
3251 C CG  . MET B 8   ? 0.8991 0.6438 0.6966 -0.1173 0.2669  0.0852  8   MET B CG  
3252 S SD  . MET B 8   ? 0.8954 0.6527 0.6803 -0.0984 0.2524  0.0844  8   MET B SD  
3253 C CE  . MET B 8   ? 1.0119 0.8018 0.8256 -0.1044 0.261   0.073   8   MET B CE  
3254 N N   . LYS B 9   ? 0.9715 0.7011 0.7662 -0.1647 0.3365  0.0868  9   LYS B N   
3255 C CA  . LYS B 9   ? 1.0292 0.7437 0.8064 -0.1764 0.3598  0.0915  9   LYS B CA  
3256 C C   . LYS B 9   ? 1.0215 0.7144 0.7991 -0.1936 0.3719  0.0944  9   LYS B C   
3257 O O   . LYS B 9   ? 1.1747 0.8328 0.9175 -0.1969 0.3848  0.1053  9   LYS B O   
3258 C CB  . LYS B 9   ? 1.042  0.7901 0.8456 -0.1824 0.37    0.0813  9   LYS B CB  
3259 C CG  . LYS B 9   ? 1.0471 0.8072 0.8395 -0.1669 0.3636  0.0802  9   LYS B CG  
3260 C CD  . LYS B 9   ? 1.083  0.8779 0.9058 -0.1716 0.3723  0.0687  9   LYS B CD  
3261 C CE  . LYS B 9   ? 1.1209 0.9247 0.9303 -0.157  0.3671  0.067   9   LYS B CE  
3262 N NZ  . LYS B 9   ? 1.1877 1.0147 1.013  -0.1619 0.3821  0.0587  9   LYS B NZ  
3263 N N   . LYS B 10  ? 1.0295 0.743  0.8459 -0.2049 0.3682  0.0844  10  LYS B N   
3264 C CA  . LYS B 10  ? 1.1146 0.8107 0.9363 -0.2219 0.3762  0.0846  10  LYS B CA  
3265 C C   . LYS B 10  ? 1.1325 0.7833 0.9154 -0.2157 0.3733  0.0972  10  LYS B C   
3266 O O   . LYS B 10  ? 1.1932 0.8113 0.9524 -0.2262 0.3901  0.1047  10  LYS B O   
3267 C CB  . LYS B 10  ? 1.1393 0.8639 1.0044 -0.2287 0.3637  0.0726  10  LYS B CB  
3268 C CG  . LYS B 10  ? 1.1725 0.9323 1.0791 -0.2458 0.3734  0.0604  10  LYS B CG  
3269 C CD  . LYS B 10  ? 1.2405 0.9878 1.1551 -0.2684 0.3863  0.0582  10  LYS B CD  
3270 C CE  . LYS B 10  ? 1.2526 1.0266 1.1937 -0.2856 0.4044  0.05    10  LYS B CE  
3271 N NZ  . LYS B 10  ? 1.281  1.0472 1.2334 -0.3093 0.417   0.0461  10  LYS B NZ  
3272 N N   . ASP B 11  ? 1.0853 0.7345 0.862  -0.1982 0.3526  0.0993  11  ASP B N   
3273 C CA  . ASP B 11  ? 1.1028 0.7139 0.8479 -0.1897 0.3466  0.1098  11  ASP B CA  
3274 C C   . ASP B 11  ? 1.1413 0.7209 0.8398 -0.18   0.3555  0.1239  11  ASP B C   
3275 O O   . ASP B 11  ? 1.1465 0.6864 0.8156 -0.1813 0.3631  0.1342  11  ASP B O   
3276 C CB  . ASP B 11  ? 1.0821 0.705  0.8376 -0.1748 0.3226  0.1067  11  ASP B CB  
3277 C CG  . ASP B 11  ? 1.0815 0.7243 0.8745 -0.1841 0.3132  0.0955  11  ASP B CG  
3278 O OD1 . ASP B 11  ? 1.1399 0.7809 0.9478 -0.2028 0.3247  0.0908  11  ASP B OD1 
3279 O OD2 . ASP B 11  ? 0.9836 0.6453 0.7911 -0.173  0.2944  0.0909  11  ASP B OD2 
3280 N N   . LEU B 12  ? 1.1147 0.711  0.8059 -0.1704 0.3551  0.1244  12  LEU B N   
3281 C CA  . LEU B 12  ? 1.1787 0.7495 0.8254 -0.1603 0.362   0.1371  12  LEU B CA  
3282 C C   . LEU B 12  ? 1.2838 0.829  0.9102 -0.1755 0.3876  0.1437  12  LEU B C   
3283 O O   . LEU B 12  ? 1.323  0.8322 0.9067 -0.1691 0.3943  0.1575  12  LEU B O   
3284 C CB  . LEU B 12  ? 1.1464 0.7457 0.7947 -0.1477 0.3539  0.1331  12  LEU B CB  
3285 C CG  . LEU B 12  ? 1.181  0.7615 0.7848 -0.1353 0.3578  0.1445  12  LEU B CG  
3286 C CD1 . LEU B 12  ? 1.1904 0.7437 0.7619 -0.1186 0.345   0.1562  12  LEU B CD1 
3287 C CD2 . LEU B 12  ? 1.1621 0.7754 0.7748 -0.1273 0.3515  0.1368  12  LEU B CD2 
3288 N N   . GLU B 13  ? 1.3267 0.8896 0.9813 -0.1951 0.4022  0.1347  13  GLU B N   
3289 C CA  . GLU B 13  ? 1.4313 0.9697 1.0665 -0.211  0.4277  0.1408  13  GLU B CA  
3290 C C   . GLU B 13  ? 1.4781 0.9734 1.0939 -0.2187 0.4344  0.1491  13  GLU B C   
3291 O O   . GLU B 13  ? 1.5998 1.061  1.1831 -0.2253 0.4529  0.1596  13  GLU B O   
3292 C CB  . GLU B 13  ? 1.4894 1.0587 1.1583 -0.23   0.4435  0.1291  13  GLU B CB  
3293 C CG  . GLU B 13  ? 1.5296 1.1254 1.2468 -0.2442 0.4388  0.1155  13  GLU B CG  
3294 C CD  . GLU B 13  ? 1.5349 1.1619 1.288  -0.2641 0.4547  0.1039  13  GLU B CD  
3295 O OE1 . GLU B 13  ? 1.4434 1.1123 1.2399 -0.2648 0.4438  0.0907  13  GLU B OE1 
3296 O OE2 . GLU B 13  ? 1.5602 1.1697 1.2981 -0.2788 0.4779  0.108   13  GLU B OE2 
3297 N N   . ASN B 14  ? 1.523  1.0182 1.1568 -0.2176 0.4198  0.1448  14  ASN B N   
3298 C CA  . ASN B 14  ? 1.5241 0.9775 1.1391 -0.2221 0.4234  0.152   14  ASN B CA  
3299 C C   . ASN B 14  ? 1.52   0.9374 1.0919 -0.2003 0.4141  0.1669  14  ASN B C   
3300 O O   . ASN B 14  ? 1.5193 0.8937 1.0654 -0.2029 0.4221  0.176   14  ASN B O   
3301 C CB  . ASN B 14  ? 1.4953 0.9642 1.146  -0.2282 0.4102  0.1406  14  ASN B CB  
3302 C CG  . ASN B 14  ? 1.4967 0.9916 1.1866 -0.2525 0.4213  0.1273  14  ASN B CG  
3303 O OD1 . ASN B 14  ? 1.5833 1.0542 1.2702 -0.2709 0.4363  0.1275  14  ASN B OD1 
3304 N ND2 . ASN B 14  ? 1.4265 0.9687 1.1509 -0.2531 0.4159  0.1162  14  ASN B ND2 
3305 N N   . ASP B 15  ? 1.4237 0.8593 0.9896 -0.1792 0.3968  0.1685  15  ASP B N   
3306 C CA  . ASP B 15  ? 1.3671 0.779  0.9017 -0.1571 0.3831  0.1797  15  ASP B CA  
3307 C C   . ASP B 15  ? 1.3393 0.7703 0.8596 -0.1385 0.3726  0.1828  15  ASP B C   
3308 O O   . ASP B 15  ? 1.3242 0.7899 0.8689 -0.1297 0.3547  0.1739  15  ASP B O   
3309 C CB  . ASP B 15  ? 1.3    0.7168 0.8564 -0.153  0.3658  0.1735  15  ASP B CB  
3310 C CG  . ASP B 15  ? 1.2763 0.6684 0.8044 -0.1312 0.3521  0.184   15  ASP B CG  
3311 O OD1 . ASP B 15  ? 1.3365 0.7029 0.8246 -0.119  0.3565  0.1978  15  ASP B OD1 
3312 O OD2 . ASP B 15  ? 1.2125 0.6123 0.7584 -0.126  0.337   0.1784  15  ASP B OD2 
3313 N N   . ASN B 16  ? 1.3605 0.7668 0.8393 -0.1323 0.3834  0.1958  16  ASN B N   
3314 C CA  . ASN B 16  ? 1.3875 0.8091 0.8476 -0.1159 0.3754  0.1992  16  ASN B CA  
3315 C C   . ASN B 16  ? 1.3386 0.7578 0.7835 -0.0922 0.3534  0.205   16  ASN B C   
3316 O O   . ASN B 16  ? 1.2438 0.686  0.684  -0.079  0.3418  0.2035  16  ASN B O   
3317 C CB  . ASN B 16  ? 1.4504 0.848  0.8709 -0.1182 0.3945  0.2107  16  ASN B CB  
3318 C CG  . ASN B 16  ? 1.5142 0.9321 0.9536 -0.1371 0.4122  0.2019  16  ASN B CG  
3319 O OD1 . ASN B 16  ? 1.5606 1.0123 1.0443 -0.1484 0.4102  0.187   16  ASN B OD1 
3320 N ND2 . ASN B 16  ? 1.5408 0.9398 0.9467 -0.1402 0.4298  0.211   16  ASN B ND2 
3321 N N   . SER B 17  ? 1.3221 0.715  0.7605 -0.0872 0.3481  0.2105  17  SER B N   
3322 C CA  . SER B 17  ? 1.3218 0.7172 0.7548 -0.0663 0.3267  0.2133  17  SER B CA  
3323 C C   . SER B 17  ? 1.2221 0.6638 0.6948 -0.0634 0.3079  0.1984  17  SER B C   
3324 O O   . SER B 17  ? 1.2487 0.7023 0.7151 -0.0455 0.2907  0.1997  17  SER B O   
3325 C CB  . SER B 17  ? 1.3247 0.6843 0.7481 -0.0636 0.3264  0.22    17  SER B CB  
3326 O OG  . SER B 17  ? 1.2732 0.6453 0.7346 -0.0749 0.3216  0.2077  17  SER B OG  
3327 N N   . LEU B 18  ? 1.1877 0.6543 0.7002 -0.0805 0.3112  0.1846  18  LEU B N   
3328 C CA  . LEU B 18  ? 1.156  0.6641 0.7068 -0.0788 0.2947  0.1707  18  LEU B CA  
3329 C C   . LEU B 18  ? 1.1348 0.6705 0.682  -0.0671 0.2853  0.1681  18  LEU B C   
3330 O O   . LEU B 18  ? 1.0913 0.6516 0.6562 -0.0579 0.2675  0.1613  18  LEU B O   
3331 C CB  . LEU B 18  ? 1.1004 0.63   0.6919 -0.0988 0.3014  0.1575  18  LEU B CB  
3332 C CG  . LEU B 18  ? 1.109  0.6232 0.7157 -0.1099 0.3034  0.155   18  LEU B CG  
3333 C CD1 . LEU B 18  ? 1.0906 0.6261 0.7341 -0.1309 0.3125  0.1429  18  LEU B CD1 
3334 C CD2 . LEU B 18  ? 1.0462 0.567  0.6637 -0.0978 0.2829  0.152   18  LEU B CD2 
3335 N N   . MET B 19  ? 1.1689 0.6999 0.693  -0.0682 0.2975  0.1731  19  MET B N   
3336 C CA  . MET B 19  ? 1.1781 0.7313 0.6931 -0.0574 0.2901  0.171   19  MET B CA  
3337 C C   . MET B 19  ? 1.1413 0.6942 0.6381 -0.0367 0.2709  0.1764  19  MET B C   
3338 O O   . MET B 19  ? 1.0726 0.655  0.5864 -0.0301 0.2562  0.1677  19  MET B O   
3339 C CB  . MET B 19  ? 1.2471 0.7873 0.7306 -0.0602 0.3069  0.1782  19  MET B CB  
3340 C CG  . MET B 19  ? 1.2883 0.8542 0.7934 -0.073  0.3178  0.1672  19  MET B CG  
3341 S SD  . MET B 19  ? 1.3172 0.9265 0.8436 -0.0636 0.3005  0.1539  19  MET B SD  
3342 C CE  . MET B 19  ? 1.3062 0.9342 0.8623 -0.0835 0.32    0.1429  19  MET B CE  
3343 N N   . ASN B 20  ? 1.1467 0.6669 0.6099 -0.0264 0.2711  0.1904  20  ASN B N   
3344 C CA  . ASN B 20  ? 1.1598 0.6812 0.6064 -0.006  0.253   0.1958  20  ASN B CA  
3345 C C   . ASN B 20  ? 1.0811 0.618  0.5581 -0.0022 0.2365  0.1879  20  ASN B C   
3346 O O   . ASN B 20  ? 1.0395 0.5968 0.5192 0.0108  0.2195  0.185   20  ASN B O   
3347 C CB  . ASN B 20  ? 1.215  0.6977 0.6184 0.0057  0.2572  0.2133  20  ASN B CB  
3348 C CG  . ASN B 20  ? 1.2785 0.7497 0.647  0.006   0.2697  0.2217  20  ASN B CG  
3349 O OD1 . ASN B 20  ? 1.3577 0.8542 0.7251 0.0081  0.2659  0.2162  20  ASN B OD1 
3350 N ND2 . ASN B 20  ? 1.3056 0.7376 0.6453 0.0029  0.2856  0.2345  20  ASN B ND2 
3351 N N   . LYS B 21  ? 1.0942 0.6217 0.5933 -0.0141 0.2417  0.1842  21  LYS B N   
3352 C CA  . LYS B 21  ? 1.0619 0.6036 0.5903 -0.0125 0.2276  0.176   21  LYS B CA  
3353 C C   . LYS B 21  ? 1.0292 0.6128 0.5892 -0.015  0.2172  0.162   21  LYS B C   
3354 O O   . LYS B 21  ? 0.9844 0.5862 0.5547 -0.0048 0.2005  0.1578  21  LYS B O   
3355 C CB  . LYS B 21  ? 1.0587 0.581  0.602  -0.0265 0.2368  0.1744  21  LYS B CB  
3356 C CG  . LYS B 21  ? 0.994  0.5312 0.5679 -0.0264 0.2229  0.1652  21  LYS B CG  
3357 C CD  . LYS B 21  ? 1.0147 0.5313 0.6    -0.0382 0.2296  0.1636  21  LYS B CD  
3358 C CE  . LYS B 21  ? 1.0472 0.5191 0.5995 -0.0319 0.2369  0.1767  21  LYS B CE  
3359 N NZ  . LYS B 21  ? 1.0039 0.4725 0.5425 -0.011  0.222   0.182   21  LYS B NZ  
3360 N N   . TRP B 22  ? 1.0092 0.6076 0.5833 -0.028  0.2276  0.1552  22  TRP B N   
3361 C CA  . TRP B 22  ? 0.9465 0.582  0.5524 -0.0311 0.2193  0.1416  22  TRP B CA  
3362 C C   . TRP B 22  ? 0.8927 0.5452 0.4848 -0.018  0.2088  0.1409  22  TRP B C   
3363 O O   . TRP B 22  ? 0.8395 0.5158 0.4509 -0.0132 0.1944  0.1327  22  TRP B O   
3364 C CB  . TRP B 22  ? 0.9434 0.5897 0.5692 -0.0477 0.234   0.1344  22  TRP B CB  
3365 C CG  . TRP B 22  ? 0.9318 0.5715 0.5808 -0.0625 0.2415  0.131   22  TRP B CG  
3366 C CD1 . TRP B 22  ? 0.9076 0.5408 0.5701 -0.0636 0.2339  0.1299  22  TRP B CD1 
3367 C CD2 . TRP B 22  ? 0.9267 0.5675 0.5885 -0.0795 0.259   0.1276  22  TRP B CD2 
3368 N NE1 . TRP B 22  ? 0.8987 0.5288 0.5809 -0.0804 0.2449  0.1256  22  TRP B NE1 
3369 C CE2 . TRP B 22  ? 0.8982 0.5339 0.5815 -0.0905 0.2602  0.1241  22  TRP B CE2 
3370 C CE3 . TRP B 22  ? 0.9548 0.6017 0.6124 -0.0866 0.2738  0.1264  22  TRP B CE3 
3371 C CZ2 . TRP B 22  ? 0.9195 0.5577 0.6213 -0.1088 0.2752  0.1193  22  TRP B CZ2 
3372 C CZ3 . TRP B 22  ? 0.955  0.6047 0.632  -0.1042 0.2892  0.1219  22  TRP B CZ3 
3373 C CH2 . TRP B 22  ? 0.937  0.5834 0.6366 -0.1153 0.2895  0.1182  22  TRP B CH2 
3374 N N   . ALA B 23  ? 0.921  0.5599 0.4786 -0.0127 0.2161  0.1497  23  ALA B N   
3375 C CA  . ALA B 23  ? 0.9343 0.5858 0.4722 0.0002  0.2063  0.1505  23  ALA B CA  
3376 C C   . ALA B 23  ? 0.9185 0.576  0.4555 0.0148  0.1872  0.1517  23  ALA B C   
3377 O O   . ALA B 23  ? 0.8791 0.5628 0.4286 0.0196  0.1743  0.1433  23  ALA B O   
3378 C CB  . ALA B 23  ? 0.9937 0.6239 0.4908 0.0042  0.2171  0.1621  23  ALA B CB  
3379 N N   . THR B 24  ? 0.9408 0.5741 0.4653 0.021   0.1859  0.1614  24  THR B N   
3380 C CA  . THR B 24  ? 0.9244 0.5623 0.4478 0.0355  0.1691  0.1632  24  THR B CA  
3381 C C   . THR B 24  ? 0.8933 0.5551 0.4553 0.0307  0.1584  0.1506  24  THR B C   
3382 O O   . THR B 24  ? 0.9085 0.5925 0.4768 0.0392  0.1439  0.1455  24  THR B O   
3383 C CB  . THR B 24  ? 0.9627 0.5672 0.4665 0.0425  0.172   0.1757  24  THR B CB  
3384 O OG1 . THR B 24  ? 0.9857 0.5666 0.4547 0.0442  0.1844  0.1871  24  THR B OG1 
3385 C CG2 . THR B 24  ? 0.971  0.5804 0.4699 0.0598  0.1553  0.1786  24  THR B CG2 
3386 N N   . VAL B 25  ? 0.8891 0.5453 0.4749 0.0176  0.1655  0.1462  25  VAL B N   
3387 C CA  . VAL B 25  ? 0.8816 0.5582 0.5037 0.0118  0.1567  0.1348  25  VAL B CA  
3388 C C   . VAL B 25  ? 0.8338 0.5427 0.4736 0.0104  0.1498  0.1238  25  VAL B C   
3389 O O   . VAL B 25  ? 0.776  0.504  0.4345 0.0136  0.1369  0.1166  25  VAL B O   
3390 C CB  . VAL B 25  ? 0.9361 0.6023 0.5775 -0.0042 0.1685  0.132   25  VAL B CB  
3391 C CG1 . VAL B 25  ? 0.9736 0.6647 0.6531 -0.0135 0.1631  0.1193  25  VAL B CG1 
3392 C CG2 . VAL B 25  ? 1.026  0.6626 0.6573 -0.0032 0.1715  0.1396  25  VAL B CG2 
3393 N N   . ALA B 26  ? 0.8734 0.5869 0.5069 0.0051  0.1596  0.1223  26  ALA B N   
3394 C CA  . ALA B 26  ? 0.8943 0.6349 0.5428 0.0029  0.1558  0.1116  26  ALA B CA  
3395 C C   . ALA B 26  ? 0.9152 0.6677 0.5454 0.0152  0.1447  0.1115  26  ALA B C   
3396 O O   . ALA B 26  ? 0.9265 0.6999 0.5668 0.0138  0.141   0.1023  26  ALA B O   
3397 C CB  . ALA B 26  ? 0.9219 0.6618 0.5705 -0.0076 0.172   0.1097  26  ALA B CB  
3398 N N   . GLY B 27  ? 0.9249 0.6641 0.5273 0.027   0.1398  0.1216  27  GLY B N   
3399 C CA  . GLY B 27  ? 0.8969 0.6499 0.483  0.0389  0.1278  0.1213  27  GLY B CA  
3400 C C   . GLY B 27  ? 0.9416 0.6973 0.505  0.0386  0.1347  0.1216  27  GLY B C   
3401 O O   . GLY B 27  ? 1.0144 0.7882 0.5714 0.0439  0.1259  0.1165  27  GLY B O   
3402 N N   . LEU B 28  ? 0.9548 0.6916 0.5045 0.0322  0.1509  0.1276  28  LEU B N   
3403 C CA  . LEU B 28  ? 1.0179 0.7548 0.5442 0.031   0.1596  0.1283  28  LEU B CA  
3404 C C   . LEU B 28  ? 1.1673 0.8892 0.6531 0.044   0.157   0.1413  28  LEU B C   
3405 O O   . LEU B 28  ? 1.1845 0.8869 0.6598 0.0509  0.1554  0.1519  28  LEU B O   
3406 C CB  . LEU B 28  ? 0.9873 0.7119 0.5189 0.0175  0.1792  0.1286  28  LEU B CB  
3407 C CG  . LEU B 28  ? 0.9329 0.6718 0.5056 0.0051  0.1825  0.117   28  LEU B CG  
3408 C CD1 . LEU B 28  ? 0.9338 0.6629 0.5097 -0.0078 0.2023  0.1175  28  LEU B CD1 
3409 C CD2 . LEU B 28  ? 0.9029 0.6702 0.4954 0.005   0.1736  0.1034  28  LEU B CD2 
3410 N N   . LYS B 29  ? 1.2489 0.9788 0.7111 0.0475  0.1572  0.1404  29  LYS B N   
3411 C CA  . LYS B 29  ? 1.3515 1.0687 0.7724 0.0598  0.1552  0.1528  29  LYS B CA  
3412 C C   . LYS B 29  ? 1.4604 1.1453 0.8582 0.0556  0.1735  0.1652  29  LYS B C   
3413 O O   . LYS B 29  ? 1.5821 1.2439 0.9547 0.0653  0.1735  0.1792  29  LYS B O   
3414 C CB  . LYS B 29  ? 1.4401 1.1752 0.8404 0.0632  0.1511  0.1477  29  LYS B CB  
3415 C CG  . LYS B 29  ? 1.4913 1.2587 0.9134 0.0606  0.1398  0.1313  29  LYS B CG  
3416 C CD  . LYS B 29  ? 1.5624 1.3497 0.9745 0.0729  0.1207  0.1295  29  LYS B CD  
3417 C CE  . LYS B 29  ? 1.614  1.4275 1.035  0.0673  0.1161  0.1138  29  LYS B CE  
3418 N NZ  . LYS B 29  ? 1.6627 1.5001 1.0919 0.0744  0.0971  0.1074  29  LYS B NZ  
3419 N N   . ASN B 30  ? 1.3824 1.0658 0.7885 0.0414  0.1896  0.1599  30  ASN B N   
3420 C CA  . ASN B 30  ? 1.3564 1.0122 0.7438 0.034   0.2094  0.1694  30  ASN B CA  
3421 C C   . ASN B 30  ? 1.32   0.978  0.7431 0.017   0.2219  0.161   30  ASN B C   
3422 O O   . ASN B 30  ? 1.1983 0.8799 0.6568 0.0125  0.2147  0.1482  30  ASN B O   
3423 C CB  . ASN B 30  ? 1.3643 1.0183 0.7164 0.0356  0.2171  0.1724  30  ASN B CB  
3424 C CG  . ASN B 30  ? 1.3502 1.0311 0.7185 0.0275  0.2191  0.1569  30  ASN B CG  
3425 O OD1 . ASN B 30  ? 1.2982 1.004  0.6962 0.027   0.2075  0.1443  30  ASN B OD1 
3426 N ND2 . ASN B 30  ? 1.4929 1.1681 0.841  0.0213  0.2345  0.1573  30  ASN B ND2 
3427 N N   . PRO B 31  ? 1.3299 0.9636 0.746  0.007   0.2406  0.168   31  PRO B N   
3428 C CA  . PRO B 31  ? 1.3277 0.968  0.7777 -0.01   0.2533  0.1589  31  PRO B CA  
3429 C C   . PRO B 31  ? 1.2691 0.9327 0.7355 -0.0194 0.2618  0.1462  31  PRO B C   
3430 O O   . PRO B 31  ? 1.1459 0.8173 0.6436 -0.0321 0.2706  0.1387  31  PRO B O   
3431 C CB  . PRO B 31  ? 1.3899 0.9958 0.821  -0.0175 0.2717  0.1711  31  PRO B CB  
3432 C CG  . PRO B 31  ? 1.4001 0.9806 0.798  -0.0028 0.2637  0.186   31  PRO B CG  
3433 C CD  . PRO B 31  ? 1.3665 0.9647 0.7451 0.0116  0.2493  0.185   31  PRO B CD  
3434 N N   . ASN B 32  ? 1.2976 0.9729 0.7441 -0.0135 0.2593  0.1432  32  ASN B N   
3435 C CA  . ASN B 32  ? 1.2567 0.9481 0.7118 -0.0223 0.271   0.1327  32  ASN B CA  
3436 C C   . ASN B 32  ? 1.1539 0.8731 0.6554 -0.0284 0.2663  0.1168  32  ASN B C   
3437 O O   . ASN B 32  ? 1.1227 0.8488 0.6444 -0.0398 0.2807  0.1103  32  ASN B O   
3438 C CB  . ASN B 32  ? 1.2666 0.9634 0.6884 -0.0147 0.269   0.1322  32  ASN B CB  
3439 C CG  . ASN B 32  ? 1.3453 1.017  0.7274 -0.0167 0.2859  0.1444  32  ASN B CG  
3440 O OD1 . ASN B 32  ? 1.4213 1.0932 0.8053 -0.0277 0.3041  0.1406  32  ASN B OD1 
3441 N ND2 . ASN B 32  ? 1.3782 1.0266 0.7264 -0.0071 0.2816  0.1594  32  ASN B ND2 
3442 N N   . PRO B 33  ? 1.0734 0.8097 0.5934 -0.0212 0.2472  0.1101  33  PRO B N   
3443 C CA  . PRO B 33  ? 1.0196 0.7787 0.5835 -0.0268 0.2431  0.0968  33  PRO B CA  
3444 C C   . PRO B 33  ? 1.0274 0.7831 0.6213 -0.0377 0.2517  0.0965  33  PRO B C   
3445 O O   . PRO B 33  ? 0.9827 0.7559 0.6082 -0.0452 0.2566  0.0862  33  PRO B O   
3446 C CB  . PRO B 33  ? 0.9822 0.753  0.5542 -0.0168 0.2211  0.0935  33  PRO B CB  
3447 C CG  . PRO B 33  ? 1.0029 0.7659 0.5342 -0.0058 0.2146  0.101   33  PRO B CG  
3448 C CD  . PRO B 33  ? 1.0363 0.7725 0.5365 -0.0074 0.229   0.1147  33  PRO B CD  
3449 N N   . LEU B 34  ? 1.0525 0.7854 0.6354 -0.0387 0.254   0.1079  34  LEU B N   
3450 C CA  . LEU B 34  ? 1.0442 0.7715 0.6522 -0.0497 0.2614  0.1082  34  LEU B CA  
3451 C C   . LEU B 34  ? 1.0197 0.7424 0.6279 -0.0628 0.2839  0.1081  34  LEU B C   
3452 O O   . LEU B 34  ? 0.923  0.6573 0.5644 -0.0737 0.2905  0.1011  34  LEU B O   
3453 C CB  . LEU B 34  ? 1.0806 0.7827 0.6715 -0.0448 0.2557  0.1202  34  LEU B CB  
3454 C CG  . LEU B 34  ? 1.1166 0.8108 0.7315 -0.0538 0.2577  0.1206  34  LEU B CG  
3455 C CD1 . LEU B 34  ? 1.0648 0.7846 0.7223 -0.0571 0.2473  0.1085  34  LEU B CD1 
3456 C CD2 . LEU B 34  ? 1.1449 0.8132 0.7368 -0.0452 0.2504  0.1323  34  LEU B CD2 
3457 N N   . TYR B 35  ? 1.1488 0.8551 0.72   -0.0617 0.2955  0.1159  35  TYR B N   
3458 C CA  . TYR B 35  ? 1.2041 0.9086 0.772  -0.0733 0.3175  0.1148  35  TYR B CA  
3459 C C   . TYR B 35  ? 1.1436 0.8793 0.7424 -0.0771 0.3199  0.0996  35  TYR B C   
3460 O O   . TYR B 35  ? 1.1067 0.8528 0.7329 -0.089  0.3326  0.0936  35  TYR B O   
3461 C CB  . TYR B 35  ? 1.3186 1.0032 0.8387 -0.0695 0.3277  0.1247  35  TYR B CB  
3462 C CG  . TYR B 35  ? 1.4674 1.1167 0.9586 -0.0722 0.3374  0.1401  35  TYR B CG  
3463 C CD1 . TYR B 35  ? 1.5234 1.153  0.9924 -0.0605 0.3242  0.1511  35  TYR B CD1 
3464 C CD2 . TYR B 35  ? 1.5856 1.2209 1.0724 -0.0865 0.3602  0.1436  35  TYR B CD2 
3465 C CE1 . TYR B 35  ? 1.6274 1.2218 1.0696 -0.062  0.3332  0.1655  35  TYR B CE1 
3466 C CE2 . TYR B 35  ? 1.723  1.3229 1.1825 -0.0896 0.3698  0.1579  35  TYR B CE2 
3467 C CZ  . TYR B 35  ? 1.7265 1.3047 1.163  -0.0769 0.3562  0.169   35  TYR B CZ  
3468 O OH  . TYR B 35  ? 1.8348 1.3754 1.2428 -0.0783 0.3655  0.1836  35  TYR B OH  
3469 N N   . ASP B 36  ? 1.1502 0.9005 0.744  -0.0668 0.308   0.0935  36  ASP B N   
3470 C CA  . ASP B 36  ? 1.1086 0.8858 0.7275 -0.0681 0.3095  0.0792  36  ASP B CA  
3471 C C   . ASP B 36  ? 1.0374 0.8337 0.704  -0.0727 0.3036  0.0704  36  ASP B C   
3472 O O   . ASP B 36  ? 0.9638 0.7773 0.6578 -0.0799 0.3139  0.0614  36  ASP B O   
3473 C CB  . ASP B 36  ? 1.1316 0.9176 0.7348 -0.0566 0.2961  0.0744  36  ASP B CB  
3474 C CG  . ASP B 36  ? 1.2571 1.0332 0.8174 -0.0528 0.3033  0.0783  36  ASP B CG  
3475 O OD1 . ASP B 36  ? 1.3639 1.1245 0.9036 -0.059  0.3206  0.0855  36  ASP B OD1 
3476 O OD2 . ASP B 36  ? 1.3304 1.1145 0.8777 -0.0441 0.2917  0.0738  36  ASP B OD2 
3477 N N   . PHE B 37  ? 0.9983 0.7917 0.6746 -0.0683 0.2873  0.0733  37  PHE B N   
3478 C CA  . PHE B 37  ? 0.9391 0.7493 0.6577 -0.072  0.2801  0.066   37  PHE B CA  
3479 C C   . PHE B 37  ? 0.9496 0.7605 0.6898 -0.0859 0.2952  0.0658  37  PHE B C   
3480 O O   . PHE B 37  ? 0.8864 0.7192 0.6634 -0.0907 0.2961  0.0564  37  PHE B O   
3481 C CB  . PHE B 37  ? 0.9326 0.7352 0.651  -0.0653 0.2615  0.0708  37  PHE B CB  
3482 C CG  . PHE B 37  ? 0.8881 0.7058 0.6469 -0.0695 0.2539  0.0644  37  PHE B CG  
3483 C CD1 . PHE B 37  ? 0.9059 0.7466 0.6907 -0.0654 0.2443  0.0538  37  PHE B CD1 
3484 C CD2 . PHE B 37  ? 0.8876 0.6956 0.6572 -0.0774 0.2561  0.0687  37  PHE B CD2 
3485 C CE1 . PHE B 37  ? 0.8444 0.6989 0.6642 -0.0682 0.2364  0.0485  37  PHE B CE1 
3486 C CE2 . PHE B 37  ? 0.8384 0.6618 0.6438 -0.081  0.2482  0.0623  37  PHE B CE2 
3487 C CZ  . PHE B 37  ? 0.8279 0.6748 0.658  -0.0761 0.2381  0.0527  37  PHE B CZ  
3488 N N   . LEU B 38  ? 1.0183 0.8051 0.7363 -0.0922 0.3061  0.0762  38  LEU B N   
3489 C CA  . LEU B 38  ? 1.061  0.8463 0.7973 -0.1072 0.321   0.0763  38  LEU B CA  
3490 C C   . LEU B 38  ? 1.062  0.862  0.8084 -0.1157 0.3402  0.0697  38  LEU B C   
3491 O O   . LEU B 38  ? 1.0616 0.8788 0.8423 -0.126  0.3475  0.0628  38  LEU B O   
3492 C CB  . LEU B 38  ? 1.1061 0.8581 0.8137 -0.1119 0.3282  0.0894  38  LEU B CB  
3493 C CG  . LEU B 38  ? 1.1435 0.8817 0.8513 -0.1076 0.3129  0.0947  38  LEU B CG  
3494 C CD1 . LEU B 38  ? 1.1779 0.8796 0.8525 -0.1108 0.322   0.1083  38  LEU B CD1 
3495 C CD2 . LEU B 38  ? 1.1605 0.9174 0.9118 -0.1155 0.3071  0.0861  38  LEU B CD2 
3496 N N   . ASN B 39  ? 1.0587 0.8538 0.7764 -0.111  0.3479  0.0711  39  ASN B N   
3497 C CA  . ASN B 39  ? 1.1521 0.954  0.8697 -0.1198 0.3696  0.0674  39  ASN B CA  
3498 C C   . ASN B 39  ? 1.1197 0.9506 0.8596 -0.1156 0.3701  0.0539  39  ASN B C   
3499 O O   . ASN B 39  ? 1.1187 0.9617 0.8706 -0.1236 0.3878  0.0483  39  ASN B O   
3500 C CB  . ASN B 39  ? 1.2117 0.9864 0.8798 -0.119  0.3813  0.0783  39  ASN B CB  
3501 C CG  . ASN B 39  ? 1.2595 1.0028 0.9053 -0.1249 0.3863  0.0919  39  ASN B CG  
3502 O OD1 . ASN B 39  ? 1.2318 0.9748 0.9019 -0.1346 0.388   0.0917  39  ASN B OD1 
3503 N ND2 . ASN B 39  ? 1.3538 1.07   0.9525 -0.119  0.3888  0.1038  39  ASN B ND2 
3504 N N   . HIS B 40  ? 1.0873 0.9285 0.8314 -0.1032 0.3522  0.0486  40  HIS B N   
3505 C CA  . HIS B 40  ? 1.0756 0.9392 0.8347 -0.0979 0.3526  0.0364  40  HIS B CA  
3506 C C   . HIS B 40  ? 1.0366 0.9202 0.8336 -0.0926 0.3357  0.0283  40  HIS B C   
3507 O O   . HIS B 40  ? 1.0227 0.8997 0.8134 -0.0852 0.3174  0.0315  40  HIS B O   
3508 C CB  . HIS B 40  ? 1.0777 0.9318 0.799  -0.0879 0.3483  0.0372  40  HIS B CB  
3509 C CG  . HIS B 40  ? 1.2191 1.0526 0.8994 -0.0917 0.3637  0.0459  40  HIS B CG  
3510 N ND1 . HIS B 40  ? 1.2466 1.0772 0.9291 -0.1038 0.3853  0.048   40  HIS B ND1 
3511 C CD2 . HIS B 40  ? 1.2736 1.0889 0.9097 -0.0853 0.3609  0.0533  40  HIS B CD2 
3512 C CE1 . HIS B 40  ? 1.2978 1.1069 0.9372 -0.1046 0.3956  0.0569  40  HIS B CE1 
3513 N NE2 . HIS B 40  ? 1.3497 1.1497 0.9602 -0.0929 0.3806  0.0604  40  HIS B NE2 
3514 N N   . ASP B 41  ? 1.0197 0.9277 0.8551 -0.0963 0.3422  0.0182  41  ASP B N   
3515 C CA  . ASP B 41  ? 0.9831 0.9114 0.8562 -0.0915 0.328   0.0107  41  ASP B CA  
3516 C C   . ASP B 41  ? 0.9475 0.8758 0.8103 -0.0787 0.3133  0.0063  41  ASP B C   
3517 O O   . ASP B 41  ? 0.8887 0.8136 0.7294 -0.0745 0.3192  0.0033  41  ASP B O   
3518 C CB  . ASP B 41  ? 1.0036 0.9589 0.9157 -0.0951 0.3389  0.0003  41  ASP B CB  
3519 C CG  . ASP B 41  ? 1.0162 0.9787 0.9471 -0.109  0.3538  0.0017  41  ASP B CG  
3520 O OD1 . ASP B 41  ? 1.0388 0.997  0.9789 -0.115  0.347   0.0067  41  ASP B OD1 
3521 O OD2 . ASP B 41  ? 1.122  1.095  1.059  -0.1144 0.3725  -0.003  41  ASP B OD2 
3522 N N   . GLY B 42  ? 0.8947 0.8261 0.7719 -0.0732 0.2944  0.0062  42  GLY B N   
3523 C CA  . GLY B 42  ? 0.8934 0.8262 0.7654 -0.0625 0.2803  0.0014  42  GLY B CA  
3524 C C   . GLY B 42  ? 0.9296 0.8428 0.7607 -0.0576 0.2726  0.0078  42  GLY B C   
3525 O O   . GLY B 42  ? 0.9794 0.894  0.804  -0.0499 0.2616  0.0033  42  GLY B O   
3526 N N   . LYS B 43  ? 0.9134 0.8087 0.7174 -0.0616 0.2772  0.0184  43  LYS B N   
3527 C CA  . LYS B 43  ? 0.9708 0.8498 0.7386 -0.0551 0.2673  0.0251  43  LYS B CA  
3528 C C   . LYS B 43  ? 0.8749 0.7515 0.6521 -0.0513 0.2486  0.0289  43  LYS B C   
3529 O O   . LYS B 43  ? 0.8708 0.7431 0.6602 -0.0564 0.2485  0.0342  43  LYS B O   
3530 C CB  . LYS B 43  ? 1.1208 0.9799 0.8531 -0.0587 0.2788  0.0356  43  LYS B CB  
3531 C CG  . LYS B 43  ? 1.2438 1.0873 0.9379 -0.0506 0.2676  0.0434  43  LYS B CG  
3532 C CD  . LYS B 43  ? 1.2943 1.1455 0.9768 -0.0417 0.2555  0.0365  43  LYS B CD  
3533 C CE  . LYS B 43  ? 1.3601 1.2202 1.0373 -0.0421 0.2659  0.0266  43  LYS B CE  
3534 N NZ  . LYS B 43  ? 1.4038 1.2547 1.0588 -0.0474 0.285   0.0306  43  LYS B NZ  
3535 N N   . THR B 44  ? 0.8257 0.7059 0.5986 -0.0432 0.2336  0.0252  44  THR B N   
3536 C CA  . THR B 44  ? 0.7672 0.6458 0.547  -0.039  0.216   0.0284  44  THR B CA  
3537 C C   . THR B 44  ? 0.7971 0.6611 0.5409 -0.033  0.2084  0.0366  44  THR B C   
3538 O O   . THR B 44  ? 0.8339 0.6942 0.5505 -0.0303 0.2124  0.0365  44  THR B O   
3539 C CB  . THR B 44  ? 0.7169 0.6107 0.5196 -0.0346 0.205   0.0183  44  THR B CB  
3540 O OG1 . THR B 44  ? 0.6848 0.5797 0.4676 -0.0298 0.2039  0.0129  44  THR B OG1 
3541 C CG2 . THR B 44  ? 0.6665 0.5755 0.5042 -0.0384 0.2121  0.0106  44  THR B CG2 
3542 N N   . PHE B 45  ? 0.7743 0.6307 0.5181 -0.0307 0.1973  0.0435  45  PHE B N   
3543 C CA  . PHE B 45  ? 0.7979 0.6445 0.5127 -0.0229 0.187   0.0503  45  PHE B CA  
3544 C C   . PHE B 45  ? 0.8022 0.6621 0.5184 -0.0166 0.1737  0.0421  45  PHE B C   
3545 O O   . PHE B 45  ? 0.7675 0.6401 0.5111 -0.018  0.1693  0.0336  45  PHE B O   
3546 C CB  . PHE B 45  ? 0.792  0.6276 0.5094 -0.0217 0.1794  0.0588  45  PHE B CB  
3547 C CG  . PHE B 45  ? 0.809  0.6283 0.5226 -0.0287 0.1926  0.067   45  PHE B CG  
3548 C CD1 . PHE B 45  ? 0.8576 0.6581 0.5372 -0.0273 0.201   0.0769  45  PHE B CD1 
3549 C CD2 . PHE B 45  ? 0.7794 0.6019 0.5226 -0.037  0.1963  0.0649  45  PHE B CD2 
3550 C CE1 . PHE B 45  ? 0.852  0.6349 0.5271 -0.0346 0.2139  0.0846  45  PHE B CE1 
3551 C CE2 . PHE B 45  ? 0.8215 0.6289 0.5615 -0.0451 0.2089  0.0715  45  PHE B CE2 
3552 C CZ  . PHE B 45  ? 0.8123 0.5988 0.5182 -0.0442 0.218   0.0814  45  PHE B CZ  
3553 N N   . ASN B 46  ? 0.7958 0.6523 0.4821 -0.0099 0.1674  0.045   46  ASN B N   
3554 C CA  . ASN B 46  ? 0.8127 0.6811 0.4963 -0.0047 0.1543  0.0378  46  ASN B CA  
3555 C C   . ASN B 46  ? 0.7398 0.6146 0.4462 -0.0028 0.1403  0.0362  46  ASN B C   
3556 O O   . ASN B 46  ? 0.6799 0.5667 0.3989 -0.0024 0.133   0.0269  46  ASN B O   
3557 C CB  . ASN B 46  ? 0.9055 0.7702 0.5535 0.0024  0.1483  0.0429  46  ASN B CB  
3558 C CG  . ASN B 46  ? 1.104  0.9666 0.7268 0.0012  0.1593  0.0411  46  ASN B CG  
3559 O OD1 . ASN B 46  ? 1.1873 1.0522 0.8199 -0.0049 0.1718  0.0347  46  ASN B OD1 
3560 N ND2 . ASN B 46  ? 1.2084 1.0678 0.7982 0.0076  0.1546  0.0464  46  ASN B ND2 
3561 N N   . GLU B 47  ? 0.7293 0.5947 0.439  -0.0019 0.1373  0.0451  47  GLU B N   
3562 C CA  . GLU B 47  ? 0.7176 0.5877 0.4474 -0.0003 0.125   0.0442  47  GLU B CA  
3563 C C   . GLU B 47  ? 0.7242 0.5886 0.4764 -0.0064 0.1306  0.047   47  GLU B C   
3564 O O   . GLU B 47  ? 0.7384 0.5894 0.4819 -0.0091 0.1397  0.0546  47  GLU B O   
3565 C CB  . GLU B 47  ? 0.7563 0.6235 0.4676 0.0081  0.113   0.0505  47  GLU B CB  
3566 C CG  . GLU B 47  ? 0.7639 0.6445 0.4645 0.0127  0.1033  0.0439  47  GLU B CG  
3567 C CD  . GLU B 47  ? 0.7912 0.6863 0.5153 0.0102  0.0954  0.033   47  GLU B CD  
3568 O OE1 . GLU B 47  ? 0.7087 0.6049 0.4584 0.0069  0.0936  0.0313  47  GLU B OE1 
3569 O OE2 . GLU B 47  ? 0.7512 0.6562 0.4671 0.011   0.0916  0.0256  47  GLU B OE2 
3570 N N   . PHE B 48  ? 0.6331 0.5077 0.4136 -0.0089 0.1249  0.0405  48  PHE B N   
3571 C CA  . PHE B 48  ? 0.6326 0.5064 0.4373 -0.0152 0.1292  0.041   48  PHE B CA  
3572 C C   . PHE B 48  ? 0.664  0.5247 0.4645 -0.0149 0.1258  0.0497  48  PHE B C   
3573 O O   . PHE B 48  ? 0.6277 0.4834 0.441  -0.0214 0.1322  0.0518  48  PHE B O   
3574 C CB  . PHE B 48  ? 0.6082 0.4962 0.4401 -0.0157 0.121   0.0326  48  PHE B CB  
3575 C CG  . PHE B 48  ? 0.5651 0.4578 0.4248 -0.0222 0.1259  0.0306  48  PHE B CG  
3576 C CD1 . PHE B 48  ? 0.5746 0.4735 0.4447 -0.0266 0.1381  0.0265  48  PHE B CD1 
3577 C CD2 . PHE B 48  ? 0.5263 0.4193 0.402  -0.0237 0.118   0.032   48  PHE B CD2 
3578 C CE1 . PHE B 48  ? 0.5617 0.4684 0.4591 -0.0323 0.142   0.0242  48  PHE B CE1 
3579 C CE2 . PHE B 48  ? 0.5299 0.43   0.4315 -0.0297 0.1215  0.0295  48  PHE B CE2 
3580 C CZ  . PHE B 48  ? 0.5137 0.4214 0.4266 -0.0339 0.1332  0.0258  48  PHE B CZ  
3581 N N   . SER B 49  ? 0.6425 0.4987 0.4262 -0.0073 0.1157  0.0539  49  SER B N   
3582 C CA  . SER B 49  ? 0.676  0.5175 0.4503 -0.0047 0.1129  0.0625  49  SER B CA  
3583 C C   . SER B 49  ? 0.6649 0.488  0.424  -0.0084 0.1264  0.0707  49  SER B C   
3584 O O   . SER B 49  ? 0.6647 0.4748 0.4267 -0.0114 0.1287  0.0755  49  SER B O   
3585 C CB  . SER B 49  ? 0.676  0.5179 0.4318 0.0057  0.1015  0.0656  49  SER B CB  
3586 O OG  . SER B 49  ? 0.6975 0.5422 0.4317 0.0096  0.1037  0.0656  49  SER B OG  
3587 N N   . SER B 50  ? 0.6574 0.4786 0.4005 -0.0094 0.1364  0.0715  50  SER B N   
3588 C CA  . SER B 50  ? 0.6918 0.4952 0.4196 -0.0141 0.151   0.079   50  SER B CA  
3589 C C   . SER B 50  ? 0.6918 0.4924 0.443  -0.0255 0.1599  0.0775  50  SER B C   
3590 O O   . SER B 50  ? 0.6859 0.4681 0.4301 -0.0287 0.1652  0.0846  50  SER B O   
3591 C CB  . SER B 50  ? 0.724  0.5292 0.4345 -0.0144 0.1606  0.0782  50  SER B CB  
3592 O OG  . SER B 50  ? 0.7303 0.5353 0.4146 -0.004  0.1525  0.0812  50  SER B OG  
3593 N N   . ILE B 51  ? 0.6704 0.4894 0.4492 -0.0316 0.1616  0.0681  51  ILE B N   
3594 C CA  . ILE B 51  ? 0.6928 0.5141 0.4961 -0.0426 0.1696  0.0656  51  ILE B CA  
3595 C C   . ILE B 51  ? 0.6574 0.4778 0.4773 -0.0437 0.1595  0.0653  51  ILE B C   
3596 O O   . ILE B 51  ? 0.6651 0.4759 0.4914 -0.0519 0.1657  0.0678  51  ILE B O   
3597 C CB  . ILE B 51  ? 0.7314 0.5738 0.5585 -0.0473 0.1752  0.056   51  ILE B CB  
3598 C CG1 . ILE B 51  ? 0.7139 0.5611 0.5656 -0.0591 0.1851  0.0536  51  ILE B CG1 
3599 C CG2 . ILE B 51  ? 0.6939 0.5545 0.5389 -0.0416 0.1619  0.048   51  ILE B CG2 
3600 C CD1 . ILE B 51  ? 0.7736 0.6024 0.6094 -0.067  0.2003  0.0606  51  ILE B CD1 
3601 N N   . VAL B 52  ? 0.5992 0.4283 0.4246 -0.0364 0.1447  0.0624  52  VAL B N   
3602 C CA  . VAL B 52  ? 0.638  0.4662 0.4776 -0.0372 0.135   0.0619  52  VAL B CA  
3603 C C   . VAL B 52  ? 0.6301 0.4342 0.4489 -0.0358 0.1367  0.071   52  VAL B C   
3604 O O   . VAL B 52  ? 0.628  0.4245 0.4565 -0.0422 0.1379  0.0716  52  VAL B O   
3605 C CB  . VAL B 52  ? 0.6343 0.4754 0.4817 -0.0297 0.1196  0.0573  52  VAL B CB  
3606 C CG1 . VAL B 52  ? 0.6337 0.4721 0.4923 -0.0304 0.1104  0.0574  52  VAL B CG1 
3607 C CG2 . VAL B 52  ? 0.6332 0.495  0.501  -0.0306 0.1179  0.0485  52  VAL B CG2 
3608 N N   . ASN B 53  ? 0.6399 0.4325 0.4301 -0.0269 0.1361  0.0777  53  ASN B N   
3609 C CA  . ASN B 53  ? 0.6895 0.4581 0.4577 -0.0227 0.137   0.0871  53  ASN B CA  
3610 C C   . ASN B 53  ? 0.712  0.4613 0.4748 -0.0327 0.1524  0.0919  53  ASN B C   
3611 O O   . ASN B 53  ? 0.7181 0.4487 0.4766 -0.0347 0.1538  0.0962  53  ASN B O   
3612 C CB  . ASN B 53  ? 0.7249 0.4872 0.4633 -0.0099 0.1329  0.0937  53  ASN B CB  
3613 C CG  . ASN B 53  ? 0.7447 0.5233 0.4877 -0.0004 0.117   0.0896  53  ASN B CG  
3614 O OD1 . ASN B 53  ? 0.6973 0.4898 0.464  -0.0031 0.1093  0.0824  53  ASN B OD1 
3615 N ND2 . ASN B 53  ? 0.7955 0.5737 0.5156 0.0105  0.1119  0.094   53  ASN B ND2 
3616 N N   . ILE B 54  ? 0.6928 0.4455 0.455  -0.0393 0.1646  0.0909  54  ILE B N   
3617 C CA  . ILE B 54  ? 0.7299 0.4667 0.4896 -0.0509 0.1806  0.0943  54  ILE B CA  
3618 C C   . ILE B 54  ? 0.7305 0.4739 0.5205 -0.0628 0.1809  0.0878  54  ILE B C   
3619 O O   . ILE B 54  ? 0.7611 0.4844 0.546  -0.0698 0.1879  0.0918  54  ILE B O   
3620 C CB  . ILE B 54  ? 0.7495 0.4916 0.504  -0.0558 0.194   0.0935  54  ILE B CB  
3621 C CG1 . ILE B 54  ? 0.7944 0.524  0.5125 -0.0451 0.1954  0.1018  54  ILE B CG1 
3622 C CG2 . ILE B 54  ? 0.7936 0.5248 0.5538 -0.0708 0.2109  0.0946  54  ILE B CG2 
3623 C CD1 . ILE B 54  ? 0.8317 0.5703 0.5426 -0.0474 0.2059  0.0997  54  ILE B CD1 
3624 N N   . VAL B 55  ? 0.6824 0.453  0.5022 -0.0653 0.1742  0.078   55  VAL B N   
3625 C CA  . VAL B 55  ? 0.7275 0.5091 0.5775 -0.0762 0.1735  0.0711  55  VAL B CA  
3626 C C   . VAL B 55  ? 0.7393 0.5077 0.5875 -0.0748 0.1645  0.073   55  VAL B C   
3627 O O   . VAL B 55  ? 0.779  0.5375 0.6338 -0.0854 0.1702  0.0726  55  VAL B O   
3628 C CB  . VAL B 55  ? 0.6999 0.5129 0.5796 -0.0758 0.1662  0.0613  55  VAL B CB  
3629 C CG1 . VAL B 55  ? 0.6939 0.5204 0.6039 -0.0843 0.1613  0.0545  55  VAL B CG1 
3630 C CG2 . VAL B 55  ? 0.7475 0.573  0.6326 -0.0794 0.1777  0.0582  55  VAL B CG2 
3631 N N   . LYS B 56  ? 0.6934 0.4619 0.5326 -0.0624 0.1512  0.0745  56  LYS B N   
3632 C CA  . LYS B 56  ? 0.7203 0.4775 0.5571 -0.0593 0.1422  0.0759  56  LYS B CA  
3633 C C   . LYS B 56  ? 0.7414 0.466  0.5532 -0.0598 0.1507  0.0847  56  LYS B C   
3634 O O   . LYS B 56  ? 0.7567 0.4692 0.5716 -0.0641 0.1496  0.0842  56  LYS B O   
3635 C CB  . LYS B 56  ? 0.7133 0.4777 0.5433 -0.0452 0.1279  0.0762  56  LYS B CB  
3636 C CG  . LYS B 56  ? 0.7248 0.5163 0.5801 -0.0448 0.117   0.0675  56  LYS B CG  
3637 C CD  . LYS B 56  ? 0.7263 0.5229 0.5752 -0.0329 0.1035  0.0676  56  LYS B CD  
3638 C CE  . LYS B 56  ? 0.7693 0.5887 0.6417 -0.0333 0.0933  0.0595  56  LYS B CE  
3639 N NZ  . LYS B 56  ? 0.7039 0.5248 0.5935 -0.0395 0.0885  0.0558  56  LYS B NZ  
3640 N N   . SER B 57  ? 0.7265 0.4358 0.5119 -0.0546 0.1588  0.0928  57  SER B N   
3641 C CA  . SER B 57  ? 0.8154 0.4912 0.5736 -0.0527 0.1667  0.1026  57  SER B CA  
3642 C C   . SER B 57  ? 0.8649 0.5259 0.6257 -0.069  0.183   0.1029  57  SER B C   
3643 O O   . SER B 57  ? 0.8809 0.5174 0.6342 -0.0738 0.1879  0.1059  57  SER B O   
3644 C CB  . SER B 57  ? 0.8737 0.539  0.6009 -0.0397 0.1678  0.1118  57  SER B CB  
3645 O OG  . SER B 57  ? 0.8977 0.569  0.6204 -0.0444 0.1782  0.1123  57  SER B OG  
3646 N N   . GLN B 58  ? 0.8565 0.5317 0.6276 -0.0778 0.1924  0.0996  58  GLN B N   
3647 C CA  . GLN B 58  ? 0.8675 0.5311 0.6412 -0.094  0.2093  0.0997  58  GLN B CA  
3648 C C   . GLN B 58  ? 0.7991 0.4804 0.6076 -0.1086 0.2084  0.089   58  GLN B C   
3649 O O   . GLN B 58  ? 0.8151 0.4812 0.6249 -0.1222 0.2195  0.0889  58  GLN B O   
3650 C CB  . GLN B 58  ? 0.9272 0.5985 0.695  -0.0965 0.221   0.101   58  GLN B CB  
3651 C CG  . GLN B 58  ? 0.9814 0.6371 0.7453 -0.1124 0.241   0.1031  58  GLN B CG  
3652 C CD  . GLN B 58  ? 1.0665 0.6803 0.798  -0.1133 0.2511  0.1143  58  GLN B CD  
3653 O OE1 . GLN B 58  ? 1.1418 0.7405 0.8746 -0.1289 0.2659  0.1144  58  GLN B OE1 
3654 N NE2 . GLN B 58  ? 1.0489 0.6429 0.7513 -0.0971 0.2443  0.1237  58  GLN B NE2 
3655 N N   . TYR B 59  ? 0.7522 0.4655 0.5881 -0.1063 0.196   0.0802  59  TYR B N   
3656 C CA  . TYR B 59  ? 0.7457 0.4813 0.616  -0.1194 0.1949  0.07    59  TYR B CA  
3657 C C   . TYR B 59  ? 0.6983 0.4487 0.5847 -0.1134 0.1771  0.0644  59  TYR B C   
3658 O O   . TYR B 59  ? 0.7019 0.4812 0.615  -0.1148 0.1701  0.0566  59  TYR B O   
3659 C CB  . TYR B 59  ? 0.7236 0.4876 0.6155 -0.1246 0.2008  0.064   59  TYR B CB  
3660 C CG  . TYR B 59  ? 0.7602 0.5115 0.6359 -0.1307 0.2194  0.069   59  TYR B CG  
3661 C CD1 . TYR B 59  ? 0.794  0.5313 0.6701 -0.1467 0.2342  0.0695  59  TYR B CD1 
3662 C CD2 . TYR B 59  ? 0.7621 0.5148 0.621  -0.121  0.2223  0.0731  59  TYR B CD2 
3663 C CE1 . TYR B 59  ? 0.8533 0.5776 0.7131 -0.1528 0.2522  0.0745  59  TYR B CE1 
3664 C CE2 . TYR B 59  ? 0.8237 0.5637 0.6651 -0.1263 0.2395  0.0781  59  TYR B CE2 
3665 C CZ  . TYR B 59  ? 0.8419 0.5677 0.6839 -0.1422 0.2548  0.0791  59  TYR B CZ  
3666 O OH  . TYR B 59  ? 0.8751 0.5883 0.6986 -0.1471 0.2722  0.0844  59  TYR B OH  
3667 N N   . PRO B 60  ? 0.7201 0.451  0.5912 -0.1068 0.1696  0.0681  60  PRO B N   
3668 C CA  . PRO B 60  ? 0.7472 0.4915 0.63   -0.0995 0.1529  0.0636  60  PRO B CA  
3669 C C   . PRO B 60  ? 0.7435 0.5109 0.6585 -0.1104 0.1477  0.0536  60  PRO B C   
3670 O O   . PRO B 60  ? 0.7213 0.5115 0.6529 -0.105  0.1354  0.0487  60  PRO B O   
3671 C CB  . PRO B 60  ? 0.7588 0.4734 0.6183 -0.0937 0.1506  0.0695  60  PRO B CB  
3672 C CG  . PRO B 60  ? 0.8087 0.4958 0.6539 -0.1042 0.1668  0.074   60  PRO B CG  
3673 C CD  . PRO B 60  ? 0.797  0.4911 0.6395 -0.1064 0.1776  0.0766  60  PRO B CD  
3674 N N   . ASP B 61  ? 0.7692 0.5311 0.6927 -0.126  0.1576  0.0507  61  ASP B N   
3675 C CA  . ASP B 61  ? 0.795  0.5786 0.7482 -0.1374 0.1529  0.0411  61  ASP B CA  
3676 C C   . ASP B 61  ? 0.7277 0.5454 0.7079 -0.1398 0.1528  0.0353  61  ASP B C   
3677 O O   . ASP B 61  ? 0.7372 0.5783 0.7429 -0.1442 0.1446  0.0278  61  ASP B O   
3678 C CB  . ASP B 61  ? 0.8434 0.6099 0.7962 -0.1539 0.1629  0.039   61  ASP B CB  
3679 C CG  . ASP B 61  ? 0.9301 0.6631 0.8589 -0.1512 0.1617  0.0432  61  ASP B CG  
3680 O OD1 . ASP B 61  ? 0.9531 0.6874 0.8787 -0.1403 0.1483  0.0431  61  ASP B OD1 
3681 O OD2 . ASP B 61  ? 0.9913 0.6968 0.9048 -0.16   0.1747  0.0465  61  ASP B OD2 
3682 N N   . ARG B 62  ? 0.7169 0.538  0.6917 -0.1363 0.1617  0.0386  62  ARG B N   
3683 C CA  . ARG B 62  ? 0.6829 0.5348 0.683  -0.1383 0.1636  0.0329  62  ARG B CA  
3684 C C   . ARG B 62  ? 0.6891 0.5524 0.6859 -0.1228 0.1562  0.0342  62  ARG B C   
3685 O O   . ARG B 62  ? 0.6845 0.5663 0.6939 -0.1222 0.1612  0.0313  62  ARG B O   
3686 C CB  . ARG B 62  ? 0.7399 0.5867 0.7379 -0.1497 0.1826  0.0341  62  ARG B CB  
3687 C CG  . ARG B 62  ? 0.7465 0.5818 0.7483 -0.1675 0.1927  0.0321  62  ARG B CG  
3688 C CD  . ARG B 62  ? 0.7645 0.5923 0.7599 -0.1777 0.2128  0.0345  62  ARG B CD  
3689 N NE  . ARG B 62  ? 0.7671 0.6277 0.7881 -0.1797 0.2175  0.0286  62  ARG B NE  
3690 C CZ  . ARG B 62  ? 0.8235 0.6843 0.8407 -0.1849 0.2342  0.0302  62  ARG B CZ  
3691 N NH1 . ARG B 62  ? 0.8306 0.6594 0.8171 -0.1882 0.2479  0.0385  62  ARG B NH1 
3692 N NH2 . ARG B 62  ? 0.8414 0.7341 0.8846 -0.186  0.2375  0.0237  62  ARG B NH2 
3693 N N   . GLU B 63  ? 0.7017 0.5554 0.6831 -0.1106 0.1443  0.0376  63  GLU B N   
3694 C CA  . GLU B 63  ? 0.6368 0.4977 0.6111 -0.0971 0.1384  0.0389  63  GLU B CA  
3695 C C   . GLU B 63  ? 0.5914 0.4826 0.5938 -0.0957 0.1337  0.0317  63  GLU B C   
3696 O O   . GLU B 63  ? 0.6039 0.504  0.6073 -0.0923 0.1397  0.0309  63  GLU B O   
3697 C CB  . GLU B 63  ? 0.6212 0.4711 0.5792 -0.0859 0.1257  0.0423  63  GLU B CB  
3698 C CG  . GLU B 63  ? 0.585  0.4412 0.5339 -0.0734 0.1204  0.0433  63  GLU B CG  
3699 C CD  . GLU B 63  ? 0.6002 0.4503 0.5369 -0.0632 0.1076  0.0454  63  GLU B CD  
3700 O OE1 . GLU B 63  ? 0.6197 0.4545 0.5475 -0.064  0.1049  0.0482  63  GLU B OE1 
3701 O OE2 . GLU B 63  ? 0.5584 0.4183 0.4935 -0.0545 0.101   0.044   63  GLU B OE2 
3702 N N   . TYR B 64  ? 0.5338 0.4402 0.5583 -0.0984 0.1238  0.0264  64  TYR B N   
3703 C CA  . TYR B 64  ? 0.5557 0.4892 0.6053 -0.0946 0.1175  0.0205  64  TYR B CA  
3704 C C   . TYR B 64  ? 0.5733 0.5235 0.6403 -0.1004 0.1297  0.0169  64  TYR B C   
3705 O O   . TYR B 64  ? 0.544  0.5047 0.6148 -0.0933 0.132   0.0153  64  TYR B O   
3706 C CB  . TYR B 64  ? 0.5396 0.4845 0.6067 -0.0963 0.1043  0.0165  64  TYR B CB  
3707 C CG  . TYR B 64  ? 0.543  0.5139 0.6339 -0.0904 0.0973  0.0116  64  TYR B CG  
3708 C CD1 . TYR B 64  ? 0.5402 0.5119 0.6255 -0.0782 0.0884  0.0124  64  TYR B CD1 
3709 C CD2 . TYR B 64  ? 0.5328 0.5273 0.6515 -0.0966 0.1005  0.0062  64  TYR B CD2 
3710 C CE1 . TYR B 64  ? 0.5252 0.5171 0.6304 -0.0722 0.0829  0.0085  64  TYR B CE1 
3711 C CE2 . TYR B 64  ? 0.54   0.5574 0.6801 -0.0895 0.0943  0.0023  64  TYR B CE2 
3712 C CZ  . TYR B 64  ? 0.531  0.5453 0.6632 -0.0771 0.0856  0.0038  64  TYR B CZ  
3713 O OH  . TYR B 64  ? 0.5388 0.572  0.69   -0.0696 0.0805  0.0006  64  TYR B OH  
3714 N N   . GLU B 65  ? 0.5856 0.5367 0.6617 -0.1138 0.1386  0.0153  65  GLU B N   
3715 C CA  . GLU B 65  ? 0.568  0.5365 0.6631 -0.1217 0.1514  0.0112  65  GLU B CA  
3716 C C   . GLU B 65  ? 0.5786 0.5391 0.6567 -0.1168 0.1633  0.0145  65  GLU B C   
3717 O O   . GLU B 65  ? 0.5956 0.5755 0.689  -0.1136 0.1677  0.0105  65  GLU B O   
3718 C CB  . GLU B 65  ? 0.6213 0.5835 0.72   -0.1382 0.1602  0.0103  65  GLU B CB  
3719 C CG  . GLU B 65  ? 0.6828 0.6591 0.7977 -0.1497 0.1765  0.0067  65  GLU B CG  
3720 C CD  . GLU B 65  ? 0.7174 0.6737 0.8209 -0.1656 0.1903  0.0088  65  GLU B CD  
3721 O OE1 . GLU B 65  ? 0.7712 0.7025 0.8559 -0.1685 0.187   0.0126  65  GLU B OE1 
3722 O OE2 . GLU B 65  ? 0.7704 0.7348 0.8826 -0.1753 0.2059  0.0068  65  GLU B OE2 
3723 N N   . LEU B 66  ? 0.5512 0.4834 0.5974 -0.1159 0.1685  0.0218  66  LEU B N   
3724 C CA  . LEU B 66  ? 0.5817 0.505  0.6086 -0.1126 0.1805  0.0254  66  LEU B CA  
3725 C C   . LEU B 66  ? 0.5845 0.5144 0.6063 -0.0984 0.1728  0.0245  66  LEU B C   
3726 O O   . LEU B 66  ? 0.5918 0.5293 0.6137 -0.096  0.1816  0.0226  66  LEU B O   
3727 C CB  . LEU B 66  ? 0.6015 0.4923 0.5946 -0.1147 0.1875  0.0341  66  LEU B CB  
3728 C CG  . LEU B 66  ? 0.6387 0.5187 0.6334 -0.1303 0.1991  0.0351  66  LEU B CG  
3729 C CD1 . LEU B 66  ? 0.7019 0.5459 0.661  -0.1297 0.2035  0.0447  66  LEU B CD1 
3730 C CD2 . LEU B 66  ? 0.6487 0.5417 0.6568 -0.1405 0.2158  0.0317  66  LEU B CD2 
3731 N N   . MET B 67  ? 0.5814 0.5069 0.597  -0.0895 0.1576  0.0256  67  MET B N   
3732 C CA  . MET B 67  ? 0.5665 0.4959 0.5753 -0.0773 0.1504  0.0246  67  MET B CA  
3733 C C   . MET B 67  ? 0.5615 0.5166 0.5988 -0.0743 0.1477  0.017   67  MET B C   
3734 O O   . MET B 67  ? 0.5756 0.5355 0.6097 -0.0676 0.1506  0.0147  67  MET B O   
3735 C CB  . MET B 67  ? 0.5488 0.4666 0.5433 -0.0699 0.136   0.0279  67  MET B CB  
3736 C CG  . MET B 67  ? 0.5804 0.4731 0.543  -0.0685 0.1389  0.0357  67  MET B CG  
3737 S SD  . MET B 67  ? 0.6261 0.5102 0.5625 -0.0639 0.1502  0.0391  67  MET B SD  
3738 C CE  . MET B 67  ? 0.6302 0.5272 0.5681 -0.0523 0.1388  0.0341  67  MET B CE  
3739 N N   . LYS B 68  ? 0.5729 0.544  0.6373 -0.0789 0.1425  0.0131  68  LYS B N   
3740 C CA  . LYS B 68  ? 0.592  0.5885 0.6854 -0.0759 0.1409  0.0065  68  LYS B CA  
3741 C C   . LYS B 68  ? 0.5906 0.5975 0.6913 -0.0781 0.1565  0.0034  68  LYS B C   
3742 O O   . LYS B 68  ? 0.5272 0.5435 0.6336 -0.0702 0.1582  -0.0003 68  LYS B O   
3743 C CB  . LYS B 68  ? 0.6286 0.641  0.7483 -0.0827 0.1345  0.0034  68  LYS B CB  
3744 C CG  . LYS B 68  ? 0.6381 0.6785 0.789  -0.0785 0.1322  -0.0029 68  LYS B CG  
3745 C CD  . LYS B 68  ? 0.7003 0.7539 0.8707 -0.0795 0.1183  -0.0048 68  LYS B CD  
3746 C CE  . LYS B 68  ? 0.7545 0.8317 0.9504 -0.0707 0.1115  -0.0092 68  LYS B CE  
3747 N NZ  . LYS B 68  ? 0.7514 0.8553 0.9783 -0.0778 0.113   -0.014  68  LYS B NZ  
3748 N N   . ASP B 69  ? 0.5727 0.5765 0.6724 -0.0894 0.169   0.0046  69  ASP B N   
3749 C CA  . ASP B 69  ? 0.5765 0.5891 0.6817 -0.0932 0.1856  0.002   69  ASP B CA  
3750 C C   . ASP B 69  ? 0.5558 0.5531 0.6327 -0.0861 0.1921  0.0046  69  ASP B C   
3751 O O   . ASP B 69  ? 0.567  0.5759 0.6509 -0.0825 0.2003  0.0001  69  ASP B O   
3752 C CB  . ASP B 69  ? 0.6078 0.617  0.7149 -0.1083 0.1976  0.0034  69  ASP B CB  
3753 C CG  . ASP B 69  ? 0.6142 0.6307 0.7243 -0.1136 0.2166  0.0012  69  ASP B CG  
3754 O OD1 . ASP B 69  ? 0.6107 0.6548 0.752  -0.1152 0.2204  -0.0058 69  ASP B OD1 
3755 O OD2 . ASP B 69  ? 0.6431 0.6383 0.7239 -0.1149 0.2268  0.0065  69  ASP B OD2 
3756 N N   . TYR B 70  ? 0.543  0.5152 0.5878 -0.0841 0.189   0.0115  70  TYR B N   
3757 C CA  . TYR B 70  ? 0.5602 0.519  0.5766 -0.0776 0.194   0.0139  70  TYR B CA  
3758 C C   . TYR B 70  ? 0.588  0.5567 0.6099 -0.0661 0.1853  0.0087  70  TYR B C   
3759 O O   . TYR B 70  ? 0.5601 0.5331 0.5781 -0.0625 0.1937  0.005   70  TYR B O   
3760 C CB  . TYR B 70  ? 0.5749 0.5075 0.5574 -0.0759 0.1899  0.0224  70  TYR B CB  
3761 C CG  . TYR B 70  ? 0.6154 0.5364 0.5679 -0.0687 0.1934  0.0248  70  TYR B CG  
3762 C CD1 . TYR B 70  ? 0.6329 0.5495 0.5719 -0.0726 0.2097  0.0259  70  TYR B CD1 
3763 C CD2 . TYR B 70  ? 0.6207 0.5363 0.5582 -0.0587 0.1807  0.0254  70  TYR B CD2 
3764 C CE1 . TYR B 70  ? 0.6791 0.5859 0.5893 -0.0664 0.2127  0.0278  70  TYR B CE1 
3765 C CE2 . TYR B 70  ? 0.6596 0.5666 0.5698 -0.053  0.1834  0.0268  70  TYR B CE2 
3766 C CZ  . TYR B 70  ? 0.6725 0.5751 0.5686 -0.0566 0.1991  0.028   70  TYR B CZ  
3767 O OH  . TYR B 70  ? 0.7119 0.6068 0.5799 -0.0512 0.2014  0.0291  70  TYR B OH  
3768 N N   . CYS B 71  ? 0.5288 0.5    0.5588 -0.0607 0.1693  0.0081  71  CYS B N   
3769 C CA  . CYS B 71  ? 0.5506 0.5263 0.5819 -0.0504 0.1606  0.004   71  CYS B CA  
3770 C C   . CYS B 71  ? 0.5471 0.543  0.6043 -0.0474 0.1659  -0.0036 71  CYS B C   
3771 O O   . CYS B 71  ? 0.5481 0.5441 0.5991 -0.0408 0.169   -0.0076 71  CYS B O   
3772 C CB  . CYS B 71  ? 0.5103 0.4844 0.5458 -0.0464 0.1436  0.0051  71  CYS B CB  
3773 S SG  . CYS B 71  ? 0.5865 0.5376 0.5909 -0.0464 0.136   0.0131  71  CYS B SG  
3774 N N   . LEU B 72  ? 0.5734 0.5866 0.6592 -0.0523 0.1679  -0.0059 72  LEU B N   
3775 C CA  . LEU B 72  ? 0.6386 0.6735 0.7523 -0.0483 0.172   -0.0128 72  LEU B CA  
3776 C C   . LEU B 72  ? 0.6333 0.6735 0.7466 -0.0514 0.1905  -0.0159 72  LEU B C   
3777 O O   . LEU B 72  ? 0.6653 0.7228 0.7999 -0.0466 0.1955  -0.0221 72  LEU B O   
3778 C CB  . LEU B 72  ? 0.7062 0.7597 0.8507 -0.0513 0.1644  -0.014  72  LEU B CB  
3779 C CG  . LEU B 72  ? 0.6873 0.7345 0.8298 -0.0478 0.1462  -0.0111 72  LEU B CG  
3780 C CD1 . LEU B 72  ? 0.7163 0.7854 0.8907 -0.0479 0.1378  -0.0137 72  LEU B CD1 
3781 C CD2 . LEU B 72  ? 0.6868 0.7212 0.8126 -0.0371 0.1372  -0.0108 72  LEU B CD2 
3782 N N   . ASN B 73  ? 0.6065 0.6309 0.6939 -0.0578 0.2006  -0.0117 73  ASN B N   
3783 C CA  . ASN B 73  ? 0.6085 0.6327 0.6864 -0.0595 0.218   -0.014  73  ASN B CA  
3784 C C   . ASN B 73  ? 0.5673 0.5757 0.6148 -0.0523 0.2187  -0.0142 73  ASN B C   
3785 O O   . ASN B 73  ? 0.5685 0.5774 0.6075 -0.0527 0.2327  -0.0172 73  ASN B O   
3786 C CB  . ASN B 73  ? 0.63   0.6473 0.6983 -0.072  0.2308  -0.0093 73  ASN B CB  
3787 C CG  . ASN B 73  ? 0.6814 0.7225 0.7826 -0.0792 0.2413  -0.0143 73  ASN B CG  
3788 O OD1 . ASN B 73  ? 0.7267 0.7793 0.8354 -0.0783 0.2546  -0.0195 73  ASN B OD1 
3789 N ND2 . ASN B 73  ? 0.7073 0.758  0.8294 -0.086  0.2352  -0.0136 73  ASN B ND2 
3790 N N   . LEU B 74  ? 0.5671 0.5628 0.5984 -0.0463 0.2044  -0.0117 74  LEU B N   
3791 C CA  . LEU B 74  ? 0.5759 0.5578 0.5779 -0.0407 0.2039  -0.0122 74  LEU B CA  
3792 C C   . LEU B 74  ? 0.5766 0.5677 0.5885 -0.0334 0.2078  -0.0213 74  LEU B C   
3793 O O   . LEU B 74  ? 0.5729 0.5778 0.6127 -0.0291 0.2035  -0.0258 74  LEU B O   
3794 C CB  . LEU B 74  ? 0.5908 0.5602 0.577  -0.0366 0.1873  -0.0082 74  LEU B CB  
3795 C CG  . LEU B 74  ? 0.5989 0.5536 0.5654 -0.0412 0.1836  0.0009  74  LEU B CG  
3796 C CD1 . LEU B 74  ? 0.5906 0.5395 0.5521 -0.0363 0.1664  0.0029  74  LEU B CD1 
3797 C CD2 . LEU B 74  ? 0.637  0.5772 0.5697 -0.0426 0.1929  0.0051  74  LEU B CD2 
3798 N N   . ASP B 75  ? 0.5779 0.5603 0.5652 -0.0317 0.2158  -0.0238 75  ASP B N   
3799 C CA  . ASP B 75  ? 0.6014 0.5858 0.5886 -0.0245 0.2177  -0.0324 75  ASP B CA  
3800 C C   . ASP B 75  ? 0.5897 0.5668 0.5717 -0.0187 0.2009  -0.0329 75  ASP B C   
3801 O O   . ASP B 75  ? 0.5931 0.5576 0.5493 -0.0193 0.1938  -0.029  75  ASP B O   
3802 C CB  . ASP B 75  ? 0.618  0.594  0.5768 -0.0256 0.2303  -0.0348 75  ASP B CB  
3803 C CG  . ASP B 75  ? 0.6451 0.6205 0.5992 -0.0193 0.2343  -0.0448 75  ASP B CG  
3804 O OD1 . ASP B 75  ? 0.5913 0.5691 0.5601 -0.013  0.2255  -0.0495 75  ASP B OD1 
3805 O OD2 . ASP B 75  ? 0.6817 0.6524 0.6147 -0.0208 0.2465  -0.0477 75  ASP B OD2 
3806 N N   . VAL B 76  ? 0.5903 0.5755 0.5962 -0.0127 0.1955  -0.038  76  VAL B N   
3807 C CA  . VAL B 76  ? 0.5677 0.547  0.5736 -0.0083 0.1797  -0.0376 76  VAL B CA  
3808 C C   . VAL B 76  ? 0.5617 0.5286 0.5429 -0.0052 0.1779  -0.0427 76  VAL B C   
3809 O O   . VAL B 76  ? 0.5496 0.5097 0.5243 -0.0035 0.1654  -0.0419 76  VAL B O   
3810 C CB  . VAL B 76  ? 0.5809 0.5715 0.619  -0.0028 0.1743  -0.0401 76  VAL B CB  
3811 C CG1 . VAL B 76  ? 0.5874 0.5911 0.6479 -0.007  0.173   -0.0349 76  VAL B CG1 
3812 C CG2 . VAL B 76  ? 0.5868 0.5836 0.6385 0.0038  0.1841  -0.0486 76  VAL B CG2 
3813 N N   . LYS B 77  ? 0.5723 0.5366 0.5384 -0.0056 0.1905  -0.048  77  LYS B N   
3814 C CA  . LYS B 77  ? 0.5757 0.5291 0.516  -0.0043 0.1899  -0.0536 77  LYS B CA  
3815 C C   . LYS B 77  ? 0.5935 0.5385 0.5033 -0.0084 0.1844  -0.0479 77  LYS B C   
3816 O O   . LYS B 77  ? 0.6241 0.562  0.5128 -0.0078 0.1808  -0.0524 77  LYS B O   
3817 C CB  . LYS B 77  ? 0.6102 0.5644 0.5464 -0.0027 0.2057  -0.0624 77  LYS B CB  
3818 C CG  . LYS B 77  ? 0.6389 0.6018 0.6049 0.0032  0.2122  -0.0687 77  LYS B CG  
3819 C CD  . LYS B 77  ? 0.6864 0.6489 0.6488 0.0061  0.228   -0.0789 77  LYS B CD  
3820 C CE  . LYS B 77  ? 0.7293 0.693  0.6737 0.0008  0.242   -0.0788 77  LYS B CE  
3821 N NZ  . LYS B 77  ? 0.7596 0.734  0.7168 -0.0041 0.2462  -0.0706 77  LYS B NZ  
3822 N N   . THR B 78  ? 0.6278 0.5732 0.5354 -0.0122 0.1824  -0.0383 78  THR B N   
3823 C CA  . THR B 78  ? 0.6391 0.5761 0.5168 -0.0148 0.1791  -0.0319 78  THR B CA  
3824 C C   . THR B 78  ? 0.6213 0.5546 0.495  -0.0136 0.1624  -0.0271 78  THR B C   
3825 O O   . THR B 78  ? 0.5637 0.5006 0.459  -0.0126 0.1541  -0.0257 78  THR B O   
3826 C CB  . THR B 78  ? 0.6239 0.5599 0.4973 -0.0195 0.1886  -0.024  78  THR B CB  
3827 O OG1 . THR B 78  ? 0.5781 0.518  0.4738 -0.0213 0.1831  -0.0182 78  THR B OG1 
3828 C CG2 . THR B 78  ? 0.677  0.6174 0.5531 -0.0216 0.2065  -0.0284 78  THR B CG2 
3829 N N   . LYS B 79  ? 0.6108 0.5377 0.4558 -0.0136 0.1579  -0.024  79  LYS B N   
3830 C CA  . LYS B 79  ? 0.6077 0.5314 0.4445 -0.0125 0.1442  -0.0175 79  LYS B CA  
3831 C C   . LYS B 79  ? 0.6013 0.5243 0.453  -0.0142 0.1422  -0.0087 79  LYS B C   
3832 O O   . LYS B 79  ? 0.5368 0.4602 0.3978 -0.0131 0.1305  -0.0059 79  LYS B O   
3833 C CB  . LYS B 79  ? 0.6485 0.5669 0.4517 -0.0116 0.1432  -0.014  79  LYS B CB  
3834 C CG  . LYS B 79  ? 0.6491 0.5663 0.4427 -0.0089 0.1286  -0.0087 79  LYS B CG  
3835 C CD  . LYS B 79  ? 0.6973 0.6106 0.4581 -0.0065 0.1271  -0.004  79  LYS B CD  
3836 C CE  . LYS B 79  ? 0.7222 0.6356 0.4774 -0.0029 0.1136  0.0021  79  LYS B CE  
3837 N NZ  . LYS B 79  ? 0.7831 0.6917 0.5084 0.0008  0.113   0.0095  79  LYS B NZ  
3838 N N   . ALA B 80  ? 0.5784 0.4996 0.4307 -0.0177 0.154   -0.0046 80  ALA B N   
3839 C CA  . ALA B 80  ? 0.5715 0.4912 0.4371 -0.0209 0.1536  0.0028  80  ALA B CA  
3840 C C   . ALA B 80  ? 0.5384 0.4676 0.4366 -0.0211 0.1479  -0.0006 80  ALA B C   
3841 O O   . ALA B 80  ? 0.5015 0.4294 0.4078 -0.0218 0.139   0.004   80  ALA B O   
3842 C CB  . ALA B 80  ? 0.5596 0.4764 0.4214 -0.026  0.1688  0.0064  80  ALA B CB  
3843 N N   . ALA B 81  ? 0.5538 0.4921 0.4699 -0.02   0.153   -0.0084 81  ALA B N   
3844 C CA  . ALA B 81  ? 0.5251 0.4728 0.4713 -0.0187 0.1472  -0.0113 81  ALA B CA  
3845 C C   . ALA B 81  ? 0.5046 0.4497 0.4504 -0.015  0.132   -0.0117 81  ALA B C   
3846 O O   . ALA B 81  ? 0.4391 0.3876 0.402  -0.0151 0.1237  -0.0094 81  ALA B O   
3847 C CB  . ALA B 81  ? 0.5156 0.4725 0.4788 -0.0163 0.1559  -0.0193 81  ALA B CB  
3848 N N   . ARG B 82  ? 0.511  0.4508 0.4378 -0.0123 0.1288  -0.0155 82  ARG B N   
3849 C CA  . ARG B 82  ? 0.4945 0.4319 0.4188 -0.01   0.1156  -0.0163 82  ARG B CA  
3850 C C   . ARG B 82  ? 0.5158 0.4496 0.4335 -0.0111 0.1064  -0.0082 82  ARG B C   
3851 O O   . ARG B 82  ? 0.4552 0.3902 0.3846 -0.0104 0.0967  -0.007  82  ARG B O   
3852 C CB  . ARG B 82  ? 0.5474 0.4812 0.4522 -0.0084 0.1152  -0.0226 82  ARG B CB  
3853 C CG  . ARG B 82  ? 0.5262 0.4617 0.4407 -0.0066 0.1228  -0.0316 82  ARG B CG  
3854 C CD  . ARG B 82  ? 0.5525 0.4834 0.4485 -0.0063 0.121   -0.0391 82  ARG B CD  
3855 N NE  . ARG B 82  ? 0.5531 0.482  0.4223 -0.0079 0.1259  -0.0394 82  ARG B NE  
3856 C CZ  . ARG B 82  ? 0.5791 0.5076 0.4405 -0.0084 0.1385  -0.0434 82  ARG B CZ  
3857 N NH1 . ARG B 82  ? 0.604  0.5303 0.4383 -0.0097 0.1409  -0.0432 82  ARG B NH1 
3858 N NH2 . ARG B 82  ? 0.5823 0.5132 0.4616 -0.0071 0.1487  -0.0478 82  ARG B NH2 
3859 N N   . SER B 83  ? 0.4935 0.4219 0.3928 -0.0126 0.1105  -0.0024 83  SER B N   
3860 C CA  . SER B 83  ? 0.4993 0.4224 0.3922 -0.013  0.1036  0.0056  83  SER B CA  
3861 C C   . SER B 83  ? 0.4687 0.3938 0.3839 -0.0162 0.103   0.0088  83  SER B C   
3862 O O   . SER B 83  ? 0.4674 0.3905 0.3858 -0.0159 0.0938  0.0122  83  SER B O   
3863 C CB  . SER B 83  ? 0.5092 0.424  0.3772 -0.013  0.1091  0.0116  83  SER B CB  
3864 O OG  . SER B 83  ? 0.5404 0.4552 0.3872 -0.0101 0.1093  0.0083  83  SER B OG  
3865 N N   . ALA B 84  ? 0.4987 0.4288 0.4286 -0.0196 0.1132  0.0073  84  ALA B N   
3866 C CA  . ALA B 84  ? 0.4982 0.4335 0.451  -0.0237 0.1136  0.0089  84  ALA B CA  
3867 C C   . ALA B 84  ? 0.4542 0.3971 0.4273 -0.0213 0.103   0.0057  84  ALA B C   
3868 O O   . ALA B 84  ? 0.4657 0.4099 0.4502 -0.0237 0.0971  0.0085  84  ALA B O   
3869 C CB  . ALA B 84  ? 0.52   0.4625 0.4852 -0.0274 0.1272  0.0064  84  ALA B CB  
3870 N N   . LEU B 85  ? 0.4374 0.3838 0.4136 -0.0168 0.1007  -0.0001 85  LEU B N   
3871 C CA  . LEU B 85  ? 0.4077 0.3582 0.399  -0.0139 0.0906  -0.0023 85  LEU B CA  
3872 C C   . LEU B 85  ? 0.3966 0.3406 0.3777 -0.0137 0.0789  0.0014  85  LEU B C   
3873 O O   . LEU B 85  ? 0.407  0.3536 0.4008 -0.0141 0.0713  0.003   85  LEU B O   
3874 C CB  . LEU B 85  ? 0.4115 0.3631 0.4045 -0.0093 0.0922  -0.0092 85  LEU B CB  
3875 C CG  . LEU B 85  ? 0.4058 0.3587 0.4117 -0.0057 0.0827  -0.0113 85  LEU B CG  
3876 C CD1 . LEU B 85  ? 0.3943 0.3563 0.4243 -0.0059 0.0793  -0.009  85  LEU B CD1 
3877 C CD2 . LEU B 85  ? 0.446  0.3979 0.4538 -0.0015 0.0876  -0.0183 85  LEU B CD2 
3878 N N   . GLU B 86  ? 0.4011 0.338  0.3594 -0.0126 0.0773  0.0026  86  GLU B N   
3879 C CA  . GLU B 86  ? 0.4088 0.3412 0.3577 -0.0119 0.0672  0.0061  86  GLU B CA  
3880 C C   . GLU B 86  ? 0.4163 0.3454 0.368  -0.0149 0.0665  0.0123  86  GLU B C   
3881 O O   . GLU B 86  ? 0.4189 0.3475 0.3759 -0.015  0.0582  0.014   86  GLU B O   
3882 C CB  . GLU B 86  ? 0.4457 0.3741 0.3707 -0.0096 0.066   0.0058  86  GLU B CB  
3883 C CG  . GLU B 86  ? 0.4367 0.3619 0.3506 -0.008  0.0571  0.0101  86  GLU B CG  
3884 C CD  . GLU B 86  ? 0.446  0.3737 0.3707 -0.0078 0.0472  0.0085  86  GLU B CD  
3885 O OE1 . GLU B 86  ? 0.4543 0.3853 0.3923 -0.0083 0.0465  0.0039  86  GLU B OE1 
3886 O OE2 . GLU B 86  ? 0.4501 0.376  0.3684 -0.0067 0.0405  0.0118  86  GLU B OE2 
3887 N N   . TYR B 87  ? 0.4453 0.371  0.392  -0.0177 0.0758  0.0155  87  TYR B N   
3888 C CA  . TYR B 87  ? 0.4525 0.3731 0.402  -0.0219 0.0768  0.0206  87  TYR B CA  
3889 C C   . TYR B 87  ? 0.3974 0.3264 0.3718 -0.0248 0.0723  0.0186  87  TYR B C   
3890 O O   . TYR B 87  ? 0.4298 0.3558 0.4066 -0.0262 0.0654  0.0209  87  TYR B O   
3891 C CB  . TYR B 87  ? 0.449  0.3648 0.3908 -0.0255 0.0896  0.0234  87  TYR B CB  
3892 C CG  . TYR B 87  ? 0.4478 0.3586 0.3961 -0.032  0.0935  0.0273  87  TYR B CG  
3893 C CD1 . TYR B 87  ? 0.4632 0.3598 0.3956 -0.0321 0.0917  0.0334  87  TYR B CD1 
3894 C CD2 . TYR B 87  ? 0.4655 0.3863 0.4366 -0.038  0.0987  0.0244  87  TYR B CD2 
3895 C CE1 . TYR B 87  ? 0.4882 0.3784 0.4264 -0.0389 0.0952  0.0361  87  TYR B CE1 
3896 C CE2 . TYR B 87  ? 0.4733 0.3905 0.4512 -0.0456 0.1022  0.0268  87  TYR B CE2 
3897 C CZ  . TYR B 87  ? 0.4803 0.3809 0.4409 -0.0465 0.1006  0.0325  87  TYR B CZ  
3898 O OH  . TYR B 87  ? 0.502  0.3967 0.4681 -0.0547 0.1045  0.0342  87  TYR B OH  
3899 N N   . ALA B 88  ? 0.3674 0.3071 0.3596 -0.0255 0.0765  0.0142  88  ALA B N   
3900 C CA  . ALA B 88  ? 0.4013 0.3516 0.4178 -0.0275 0.0724  0.0123  88  ALA B CA  
3901 C C   . ALA B 88  ? 0.3992 0.3498 0.4187 -0.0239 0.0597  0.0117  88  ALA B C   
3902 O O   . ALA B 88  ? 0.4091 0.3613 0.4368 -0.0263 0.0529  0.0131  88  ALA B O   
3903 C CB  . ALA B 88  ? 0.4086 0.3712 0.4426 -0.0267 0.0796  0.0077  88  ALA B CB  
3904 N N   . ASP B 89  ? 0.4008 0.3489 0.4115 -0.0188 0.0566  0.0095  89  ASP B N   
3905 C CA  . ASP B 89  ? 0.3799 0.3273 0.3921 -0.016  0.0457  0.009   89  ASP B CA  
3906 C C   . ASP B 89  ? 0.369  0.3088 0.3686 -0.0174 0.0392  0.0128  89  ASP B C   
3907 O O   . ASP B 89  ? 0.4    0.341  0.4067 -0.0182 0.0315  0.0137  89  ASP B O   
3908 C CB  . ASP B 89  ? 0.3856 0.331  0.391  -0.0117 0.0447  0.0051  89  ASP B CB  
3909 C CG  . ASP B 89  ? 0.3931 0.337  0.4011 -0.0097 0.0349  0.0045  89  ASP B CG  
3910 O OD1 . ASP B 89  ? 0.3925 0.341  0.416  -0.0077 0.0328  0.0032  89  ASP B OD1 
3911 O OD2 . ASP B 89  ? 0.4012 0.3401 0.3961 -0.0102 0.0296  0.0059  89  ASP B OD2 
3912 N N   . ALA B 90  ? 0.3835 0.316  0.3645 -0.0171 0.0422  0.0152  90  ALA B N   
3913 C CA  . ALA B 90  ? 0.3986 0.3237 0.3673 -0.017  0.037   0.019   90  ALA B CA  
3914 C C   . ALA B 90  ? 0.3995 0.3226 0.3767 -0.0214 0.036   0.0215  90  ALA B C   
3915 O O   . ALA B 90  ? 0.3983 0.3183 0.3736 -0.0214 0.029   0.0227  90  ALA B O   
3916 C CB  . ALA B 90  ? 0.4002 0.3184 0.3488 -0.015  0.0419  0.0218  90  ALA B CB  
3917 N N   . ASN B 91  ? 0.3871 0.3121 0.3731 -0.0258 0.0435  0.0219  91  ASN B N   
3918 C CA  . ASN B 91  ? 0.421  0.3442 0.4149 -0.0319 0.044   0.0233  91  ASN B CA  
3919 C C   . ASN B 91  ? 0.4651 0.4001 0.4802 -0.034  0.0377  0.0202  91  ASN B C   
3920 O O   . ASN B 91  ? 0.4501 0.3854 0.4724 -0.0395 0.0364  0.0204  91  ASN B O   
3921 C CB  . ASN B 91  ? 0.4251 0.346  0.4197 -0.0372 0.0554  0.0246  91  ASN B CB  
3922 C CG  . ASN B 91  ? 0.447  0.3521 0.4189 -0.0365 0.0611  0.0297  91  ASN B CG  
3923 O OD1 . ASN B 91  ? 0.4497 0.3436 0.4141 -0.0385 0.0597  0.0327  91  ASN B OD1 
3924 N ND2 . ASN B 91  ? 0.4416 0.3445 0.4005 -0.0326 0.0665  0.0307  91  ASN B ND2 
3925 N N   . MET B 92  ? 0.4269 0.371  0.4514 -0.0297 0.0342  0.0172  92  MET B N   
3926 C CA  . MET B 92  ? 0.4771 0.4332 0.5218 -0.03   0.0286  0.0149  92  MET B CA  
3927 C C   . MET B 92  ? 0.4831 0.45   0.5455 -0.0354 0.0347  0.0134  92  MET B C   
3928 O O   . MET B 92  ? 0.4321 0.4085 0.5097 -0.0386 0.0297  0.0122  92  MET B O   
3929 C CB  . MET B 92  ? 0.4347 0.3886 0.4783 -0.0305 0.018   0.0158  92  MET B CB  
3930 C CG  . MET B 92  ? 0.4818 0.428  0.5108 -0.0256 0.0127  0.0165  92  MET B CG  
3931 S SD  . MET B 92  ? 0.5091 0.4538 0.5373 -0.0257 0.001   0.0172  92  MET B SD  
3932 C CE  . MET B 92  ? 0.5355 0.4736 0.5485 -0.0206 -0.002  0.017   92  MET B CE  
3933 N N   . PHE B 93  ? 0.4427 0.4101 0.504  -0.0363 0.0456  0.0129  93  PHE B N   
3934 C CA  . PHE B 93  ? 0.4331 0.413  0.5124 -0.0411 0.0532  0.0107  93  PHE B CA  
3935 C C   . PHE B 93  ? 0.427  0.4209 0.523  -0.0349 0.0533  0.0072  93  PHE B C   
3936 O O   . PHE B 93  ? 0.4375 0.4324 0.5321 -0.0325 0.0622  0.0056  93  PHE B O   
3937 C CB  . PHE B 93  ? 0.4511 0.4225 0.5183 -0.0454 0.0659  0.0124  93  PHE B CB  
3938 C CG  . PHE B 93  ? 0.4729 0.4286 0.5239 -0.0512 0.0677  0.0164  93  PHE B CG  
3939 C CD1 . PHE B 93  ? 0.4775 0.4304 0.5308 -0.0553 0.0601  0.0169  93  PHE B CD1 
3940 C CD2 . PHE B 93  ? 0.466  0.4085 0.4979 -0.052  0.0774  0.0197  93  PHE B CD2 
3941 C CE1 . PHE B 93  ? 0.4865 0.4227 0.5241 -0.0598 0.0627  0.0204  93  PHE B CE1 
3942 C CE2 . PHE B 93  ? 0.5047 0.4303 0.5202 -0.0559 0.0794  0.0241  93  PHE B CE2 
3943 C CZ  . PHE B 93  ? 0.4928 0.4149 0.5117 -0.0598 0.0724  0.0242  93  PHE B CZ  
3944 N N   . PHE B 94  ? 0.394  0.3977 0.5046 -0.0321 0.0434  0.0061  94  PHE B N   
3945 C CA  . PHE B 94  ? 0.4498 0.4626 0.5729 -0.0237 0.0411  0.0038  94  PHE B CA  
3946 C C   . PHE B 94  ? 0.4295 0.4579 0.5717 -0.023  0.0506  0.0003  94  PHE B C   
3947 O O   . PHE B 94  ? 0.4391 0.4687 0.5839 -0.0158 0.0543  -0.0018 94  PHE B O   
3948 C CB  . PHE B 94  ? 0.4499 0.4695 0.5835 -0.0205 0.0284  0.0044  94  PHE B CB  
3949 C CG  . PHE B 94  ? 0.4506 0.4559 0.5663 -0.0204 0.0191  0.0073  94  PHE B CG  
3950 C CD1 . PHE B 94  ? 0.4641 0.4537 0.559  -0.0178 0.0202  0.0084  94  PHE B CD1 
3951 C CD2 . PHE B 94  ? 0.5094 0.5183 0.6292 -0.0234 0.0095  0.0085  94  PHE B CD2 
3952 C CE1 . PHE B 94  ? 0.4837 0.4628 0.5643 -0.0179 0.0123  0.0106  94  PHE B CE1 
3953 C CE2 . PHE B 94  ? 0.4815 0.478  0.5852 -0.0234 0.0019  0.0108  94  PHE B CE2 
3954 C CZ  . PHE B 94  ? 0.4895 0.4714 0.5741 -0.0207 0.0037  0.0119  94  PHE B CZ  
3955 N N   . GLU B 95  ? 0.4317 0.4716 0.5872 -0.0309 0.0555  -0.0007 95  GLU B N   
3956 C CA  . GLU B 95  ? 0.4824 0.5397 0.6581 -0.0309 0.0651  -0.0045 95  GLU B CA  
3957 C C   . GLU B 95  ? 0.4634 0.5112 0.6251 -0.0308 0.0785  -0.0051 95  GLU B C   
3958 O O   . GLU B 95  ? 0.459  0.5159 0.6314 -0.0256 0.0854  -0.0085 95  GLU B O   
3959 C CB  . GLU B 95  ? 0.5455 0.619  0.7397 -0.0409 0.0676  -0.0061 95  GLU B CB  
3960 C CG  . GLU B 95  ? 0.5807 0.667  0.79   -0.0411 0.0539  -0.0064 95  GLU B CG  
3961 C CD  . GLU B 95  ? 0.6731 0.78   0.9046 -0.0514 0.0557  -0.0097 95  GLU B CD  
3962 O OE1 . GLU B 95  ? 0.7117 0.8313 0.9568 -0.0564 0.0675  -0.0129 95  GLU B OE1 
3963 O OE2 . GLU B 95  ? 0.7134 0.8234 0.9475 -0.0554 0.0452  -0.0095 95  GLU B OE2 
3964 N N   . ILE B 96  ? 0.4615 0.4907 0.5985 -0.0354 0.0818  -0.0019 96  ILE B N   
3965 C CA  . ILE B 96  ? 0.4553 0.4746 0.5755 -0.0347 0.0933  -0.002  96  ILE B CA  
3966 C C   . ILE B 96  ? 0.4362 0.4493 0.5476 -0.0248 0.0901  -0.0037 96  ILE B C   
3967 O O   . ILE B 96  ? 0.4503 0.4661 0.5629 -0.021  0.0987  -0.0072 96  ILE B O   
3968 C CB  . ILE B 96  ? 0.4774 0.4784 0.5725 -0.0409 0.0968  0.0026  96  ILE B CB  
3969 C CG1 . ILE B 96  ? 0.4725 0.4761 0.575  -0.0518 0.1007  0.0042  96  ILE B CG1 
3970 C CG2 . ILE B 96  ? 0.4936 0.4858 0.5704 -0.0395 0.1084  0.0027  96  ILE B CG2 
3971 C CD1 . ILE B 96  ? 0.494  0.4765 0.5711 -0.0565 0.1025  0.0095  96  ILE B CD1 
3972 N N   . GLU B 97  ? 0.4117 0.4151 0.5126 -0.0216 0.0785  -0.0016 97  GLU B N   
3973 C CA  . GLU B 97  ? 0.4348 0.43   0.5251 -0.0141 0.0749  -0.0032 97  GLU B CA  
3974 C C   . GLU B 97  ? 0.3918 0.3971 0.5003 -0.0068 0.0765  -0.0075 97  GLU B C   
3975 O O   . GLU B 97  ? 0.4268 0.4273 0.5284 -0.0024 0.0826  -0.011  97  GLU B O   
3976 C CB  . GLU B 97  ? 0.4612 0.4482 0.543  -0.0135 0.0619  -0.0001 97  GLU B CB  
3977 C CG  . GLU B 97  ? 0.4441 0.4233 0.5173 -0.007  0.0575  -0.0021 97  GLU B CG  
3978 C CD  . GLU B 97  ? 0.4486 0.4182 0.5085 -0.0077 0.0471  0.0008  97  GLU B CD  
3979 O OE1 . GLU B 97  ? 0.4564 0.4269 0.5182 -0.0114 0.0411  0.0041  97  GLU B OE1 
3980 O OE2 . GLU B 97  ? 0.4452 0.4065 0.4933 -0.0045 0.0456  -0.001  97  GLU B OE2 
3981 N N   . ASP B 98  ? 0.3901 0.409  0.5212 -0.0049 0.0707  -0.0075 98  ASP B N   
3982 C CA  . ASP B 98  ? 0.4191 0.4471 0.5678 0.0041  0.0705  -0.0107 98  ASP B CA  
3983 C C   . ASP B 98  ? 0.4078 0.4458 0.5674 0.0056  0.0842  -0.0152 98  ASP B C   
3984 O O   . ASP B 98  ? 0.419  0.4556 0.5818 0.0138  0.0882  -0.0189 98  ASP B O   
3985 C CB  . ASP B 98  ? 0.4511 0.4923 0.62   0.0064  0.0598  -0.0088 98  ASP B CB  
3986 C CG  . ASP B 98  ? 0.464  0.4942 0.6212 0.0065  0.0466  -0.0049 98  ASP B CG  
3987 O OD1 . ASP B 98  ? 0.4585 0.4709 0.5941 0.0068  0.045   -0.004  98  ASP B OD1 
3988 O OD2 . ASP B 98  ? 0.4494 0.4898 0.6191 0.0056  0.038   -0.0029 98  ASP B OD2 
3989 N N   . ALA B 99  ? 0.4188 0.4655 0.5832 -0.0025 0.0924  -0.0152 99  ALA B N   
3990 C CA  . ALA B 99  ? 0.4372 0.4936 0.6105 -0.0023 0.1069  -0.0195 99  ALA B CA  
3991 C C   . ALA B 99  ? 0.4278 0.4674 0.5763 -0.0011 0.1155  -0.0215 99  ALA B C   
3992 O O   . ALA B 99  ? 0.4488 0.491  0.6014 0.0046  0.1242  -0.0264 99  ALA B O   
3993 C CB  . ALA B 99  ? 0.4341 0.502  0.6166 -0.0129 0.1135  -0.0187 99  ALA B CB  
3994 N N   . LEU B 100 ? 0.4433 0.4661 0.5656 -0.006  0.1127  -0.0179 100 LEU B N   
3995 C CA  . LEU B 100 ? 0.4506 0.4583 0.5476 -0.0048 0.1184  -0.0198 100 LEU B CA  
3996 C C   . LEU B 100 ? 0.4597 0.4607 0.5544 0.0039  0.1142  -0.0238 100 LEU B C   
3997 O O   . LEU B 100 ? 0.4307 0.4283 0.5197 0.0075  0.1229  -0.0291 100 LEU B O   
3998 C CB  . LEU B 100 ? 0.4658 0.4594 0.5374 -0.0104 0.1141  -0.0147 100 LEU B CB  
3999 C CG  . LEU B 100 ? 0.4816 0.4746 0.546  -0.0186 0.1225  -0.011  100 LEU B CG  
4000 C CD1 . LEU B 100 ? 0.5144 0.4928 0.5557 -0.0216 0.1154  -0.0053 100 LEU B CD1 
4001 C CD2 . LEU B 100 ? 0.5394 0.5317 0.5942 -0.0195 0.1376  -0.014  100 LEU B CD2 
4002 N N   . ILE B 101 ? 0.4362 0.4344 0.535  0.0069  0.1014  -0.0215 101 ILE B N   
4003 C CA  . ILE B 101 ? 0.4191 0.4085 0.5153 0.0143  0.0975  -0.0247 101 ILE B CA  
4004 C C   . ILE B 101 ? 0.444  0.4411 0.5579 0.0221  0.1058  -0.03   101 ILE B C   
4005 O O   . ILE B 101 ? 0.4774 0.4648 0.5817 0.0261  0.1119  -0.0353 101 ILE B O   
4006 C CB  . ILE B 101 ? 0.4073 0.3938 0.5073 0.0161  0.0832  -0.0206 101 ILE B CB  
4007 C CG1 . ILE B 101 ? 0.4115 0.3868 0.4899 0.0102  0.0762  -0.0171 101 ILE B CG1 
4008 C CG2 . ILE B 101 ? 0.4299 0.4093 0.5337 0.0247  0.0809  -0.0235 101 ILE B CG2 
4009 C CD1 . ILE B 101 ? 0.4002 0.3742 0.4819 0.0101  0.063   -0.0125 101 ILE B CD1 
4010 N N   . ASP B 102 ? 0.4782 0.4935 0.6185 0.0244  0.1059  -0.0291 102 ASP B N   
4011 C CA  . ASP B 102 ? 0.5035 0.5292 0.6648 0.0335  0.1122  -0.0335 102 ASP B CA  
4012 C C   . ASP B 102 ? 0.5243 0.5498 0.68   0.0332  0.1282  -0.0396 102 ASP B C   
4013 O O   . ASP B 102 ? 0.5045 0.5246 0.6613 0.0412  0.1342  -0.045  102 ASP B O   
4014 C CB  . ASP B 102 ? 0.5475 0.5963 0.7385 0.0351  0.1085  -0.0314 102 ASP B CB  
4015 C CG  . ASP B 102 ? 0.6365 0.6966 0.8516 0.0478  0.1095  -0.0343 102 ASP B CG  
4016 O OD1 . ASP B 102 ? 0.6425 0.6913 0.8548 0.0561  0.102   -0.0332 102 ASP B OD1 
4017 O OD2 . ASP B 102 ? 0.7601 0.8409 0.9973 0.0495  0.118   -0.0374 102 ASP B OD2 
4018 N N   . SER B 103 ? 0.464  0.4922 0.6105 0.024   0.1356  -0.0388 103 SER B N   
4019 C CA  . SER B 103 ? 0.506  0.5338 0.6452 0.0234  0.1513  -0.0444 103 SER B CA  
4020 C C   . SER B 103 ? 0.5011 0.5078 0.6089 0.0224  0.153   -0.0471 103 SER B C   
4021 O O   . SER B 103 ? 0.5211 0.5241 0.6223 0.025   0.1644  -0.0536 103 SER B O   
4022 C CB  . SER B 103 ? 0.5091 0.5495 0.6534 0.0148  0.1607  -0.0429 103 SER B CB  
4023 O OG  . SER B 103 ? 0.5585 0.5931 0.6894 0.0059  0.154   -0.0363 103 SER B OG  
4024 N N   . MET B 104 ? 0.4964 0.4901 0.5854 0.0188  0.142   -0.0431 104 MET B N   
4025 C CA  . MET B 104 ? 0.5073 0.4838 0.5681 0.0176  0.1422  -0.0463 104 MET B CA  
4026 C C   . MET B 104 ? 0.5046 0.4712 0.5662 0.0252  0.1412  -0.0523 104 MET B C   
4027 O O   . MET B 104 ? 0.4992 0.4561 0.545  0.0258  0.1488  -0.0591 104 MET B O   
4028 C CB  . MET B 104 ? 0.5379 0.5065 0.5807 0.0117  0.1311  -0.0403 104 MET B CB  
4029 C CG  . MET B 104 ? 0.544  0.516  0.5772 0.0045  0.1357  -0.0357 104 MET B CG  
4030 S SD  . MET B 104 ? 0.5675 0.5324 0.5841 -0.0011 0.1233  -0.0276 104 MET B SD  
4031 C CE  . MET B 104 ? 0.5862 0.5377 0.574  -0.0002 0.1217  -0.0324 104 MET B CE  
4032 N N   . ILE B 105 ? 0.5014 0.4698 0.5807 0.031   0.1326  -0.0501 105 ILE B N   
4033 C CA  . ILE B 105 ? 0.5792 0.5362 0.6603 0.0389  0.132   -0.0547 105 ILE B CA  
4034 C C   . ILE B 105 ? 0.6153 0.5741 0.7041 0.0454  0.1463  -0.0625 105 ILE B C   
4035 O O   . ILE B 105 ? 0.6985 0.6419 0.7756 0.0486  0.1504  -0.069  105 ILE B O   
4036 C CB  . ILE B 105 ? 0.5745 0.5339 0.6732 0.0446  0.1203  -0.0493 105 ILE B CB  
4037 C CG1 . ILE B 105 ? 0.5664 0.5172 0.6506 0.0385  0.1076  -0.0441 105 ILE B CG1 
4038 C CG2 . ILE B 105 ? 0.6105 0.5608 0.7178 0.0556  0.1224  -0.0533 105 ILE B CG2 
4039 C CD1 . ILE B 105 ? 0.5929 0.5487 0.6924 0.0418  0.0957  -0.0375 105 ILE B CD1 
4040 N N   . SER B 106 ? 0.6229 0.6    0.7302 0.0467  0.1545  -0.0625 106 SER B N   
4041 C CA  . SER B 106 ? 0.6427 0.6251 0.761  0.0535  0.1688  -0.0697 106 SER B CA  
4042 C C   . SER B 106 ? 0.6521 0.6293 0.7492 0.0478  0.182   -0.0758 106 SER B C   
4043 O O   . SER B 106 ? 0.6619 0.6403 0.7642 0.0533  0.1946  -0.0831 106 SER B O   
4044 C CB  . SER B 106 ? 0.6687 0.6762 0.8178 0.0565  0.1721  -0.0674 106 SER B CB  
4045 O OG  . SER B 106 ? 0.7174 0.7315 0.8872 0.0635  0.1604  -0.0627 106 SER B OG  
4046 N N   . CYS B 107 ? 0.6279 0.6007 0.7021 0.0375  0.18    -0.0729 107 CYS B N   
4047 C CA  . CYS B 107 ? 0.6604 0.6315 0.7156 0.0323  0.1928  -0.0773 107 CYS B CA  
4048 C C   . CYS B 107 ? 0.6489 0.6012 0.6794 0.0328  0.1953  -0.0853 107 CYS B C   
4049 O O   . CYS B 107 ? 0.675  0.6149 0.7011 0.035   0.1862  -0.0863 107 CYS B O   
4050 C CB  . CYS B 107 ? 0.6514 0.6261 0.6928 0.0223  0.1904  -0.0701 107 CYS B CB  
4051 S SG  . CYS B 107 ? 0.6633 0.6216 0.6729 0.0163  0.1773  -0.0668 107 CYS B SG  
4052 N N   . SER B 108 ? 0.6394 0.5893 0.6518 0.0294  0.2076  -0.091  108 SER B N   
4053 C CA  . SER B 108 ? 0.6773 0.6113 0.6664 0.0293  0.2126  -0.1006 108 SER B CA  
4054 C C   . SER B 108 ? 0.6801 0.6047 0.638  0.0208  0.2045  -0.0992 108 SER B C   
4055 O O   . SER B 108 ? 0.7595 0.6723 0.6959 0.0189  0.2074  -0.1075 108 SER B O   
4056 C CB  . SER B 108 ? 0.697  0.6344 0.6837 0.0308  0.2307  -0.1084 108 SER B CB  
4057 O OG  . SER B 108 ? 0.7072 0.6552 0.6868 0.0241  0.2361  -0.1032 108 SER B OG  
4058 N N   . ASN B 109 ? 0.6177 0.5479 0.5725 0.0157  0.1945  -0.0894 109 ASN B N   
4059 C CA  . ASN B 109 ? 0.6173 0.5408 0.5451 0.0093  0.1858  -0.0875 109 ASN B CA  
4060 C C   . ASN B 109 ? 0.5937 0.5099 0.5248 0.0101  0.1717  -0.0868 109 ASN B C   
4061 O O   . ASN B 109 ? 0.5543 0.4751 0.5049 0.0123  0.1634  -0.0798 109 ASN B O   
4062 C CB  . ASN B 109 ? 0.6154 0.5466 0.537  0.0045  0.1832  -0.0774 109 ASN B CB  
4063 C CG  . ASN B 109 ? 0.6387 0.5641 0.5318 -0.0004 0.1746  -0.0755 109 ASN B CG  
4064 O OD1 . ASN B 109 ? 0.6187 0.5419 0.5117 -0.0011 0.1614  -0.0723 109 ASN B OD1 
4065 N ND2 . ASN B 109 ? 0.6819 0.6058 0.5504 -0.0035 0.1817  -0.0776 109 ASN B ND2 
4066 N N   . MET B 110 ? 0.603  0.5081 0.5137 0.0073  0.1691  -0.0941 110 MET B N   
4067 C CA  . MET B 110 ? 0.6603 0.5565 0.5731 0.0072  0.1583  -0.0954 110 MET B CA  
4068 C C   . MET B 110 ? 0.6263 0.5276 0.538  0.0037  0.144   -0.0858 110 MET B C   
4069 O O   . MET B 110 ? 0.5828 0.4811 0.5068 0.0052  0.1353  -0.0827 110 MET B O   
4070 C CB  . MET B 110 ? 0.7344 0.6184 0.6252 0.0032  0.1599  -0.1066 110 MET B CB  
4071 C CG  . MET B 110 ? 0.8128 0.6873 0.7053 0.0072  0.1732  -0.1174 110 MET B CG  
4072 S SD  . MET B 110 ? 0.9345 0.8004 0.8558 0.0169  0.1744  -0.1175 110 MET B SD  
4073 C CE  . MET B 110 ? 0.9593 0.8399 0.905  0.0252  0.1853  -0.1134 110 MET B CE  
4074 N N   . LYS B 111 ? 0.6186 0.5263 0.5139 -0.0006 0.142   -0.0813 111 LYS B N   
4075 C CA  . LYS B 111 ? 0.6293 0.5421 0.523  -0.003  0.1299  -0.072  111 LYS B CA  
4076 C C   . LYS B 111 ? 0.5624 0.4816 0.4805 0       0.1274  -0.0631 111 LYS B C   
4077 O O   . LYS B 111 ? 0.5298 0.4492 0.4564 0.0001  0.1169  -0.0583 111 LYS B O   
4078 C CB  . LYS B 111 ? 0.7114 0.6287 0.5822 -0.0065 0.13    -0.0685 111 LYS B CB  
4079 C CG  . LYS B 111 ? 0.8459 0.7619 0.6945 -0.0103 0.1221  -0.0724 111 LYS B CG  
4080 C CD  . LYS B 111 ? 0.8962 0.8171 0.7219 -0.0118 0.1217  -0.0678 111 LYS B CD  
4081 C CE  . LYS B 111 ? 0.9863 0.9079 0.7895 -0.0153 0.1165  -0.075  111 LYS B CE  
4082 N NZ  . LYS B 111 ? 1.0666 0.994  0.8477 -0.0153 0.1133  -0.0692 111 LYS B NZ  
4083 N N   . SER B 112 ? 0.5524 0.4778 0.4804 0.0017  0.1372  -0.0611 112 SER B N   
4084 C CA  . SER B 112 ? 0.5347 0.4682 0.4864 0.0035  0.1356  -0.0539 112 SER B CA  
4085 C C   . SER B 112 ? 0.5312 0.4635 0.5047 0.0087  0.1312  -0.0557 112 SER B C   
4086 O O   . SER B 112 ? 0.5064 0.4425 0.494  0.0094  0.1224  -0.0496 112 SER B O   
4087 C CB  . SER B 112 ? 0.5507 0.4923 0.5096 0.0034  0.1483  -0.0532 112 SER B CB  
4088 O OG  . SER B 112 ? 0.5187 0.4599 0.4569 -0.0015 0.1515  -0.049  112 SER B OG  
4089 N N   . LYS B 113 ? 0.5381 0.4637 0.5129 0.0126  0.1371  -0.064  113 LYS B N   
4090 C CA  . LYS B 113 ? 0.5712 0.4923 0.5635 0.0185  0.1331  -0.0652 113 LYS B CA  
4091 C C   . LYS B 113 ? 0.5168 0.4304 0.5027 0.016   0.1197  -0.0621 113 LYS B C   
4092 O O   . LYS B 113 ? 0.4572 0.3727 0.4587 0.0189  0.112   -0.0569 113 LYS B O   
4093 C CB  . LYS B 113 ? 0.613  0.5251 0.6035 0.023   0.1436  -0.0752 113 LYS B CB  
4094 C CG  . LYS B 113 ? 0.7029 0.6093 0.7123 0.0315  0.1427  -0.0766 113 LYS B CG  
4095 C CD  . LYS B 113 ? 0.7592 0.6532 0.7645 0.0363  0.1538  -0.087  113 LYS B CD  
4096 C CE  . LYS B 113 ? 0.8315 0.7331 0.8401 0.0388  0.1686  -0.0923 113 LYS B CE  
4097 N NZ  . LYS B 113 ? 0.8824 0.7982 0.92   0.0472  0.1728  -0.0893 113 LYS B NZ  
4098 N N   . GLU B 114 ? 0.5155 0.4219 0.4784 0.0104  0.1169  -0.0657 114 GLU B N   
4099 C CA  . GLU B 114 ? 0.5088 0.4099 0.4648 0.0069  0.1052  -0.0636 114 GLU B CA  
4100 C C   . GLU B 114 ? 0.5176 0.4277 0.4813 0.0058  0.0957  -0.0535 114 GLU B C   
4101 O O   . GLU B 114 ? 0.4211 0.329  0.3935 0.0067  0.0872  -0.0496 114 GLU B O   
4102 C CB  . GLU B 114 ? 0.5043 0.401  0.4352 0.0006  0.1045  -0.0696 114 GLU B CB  
4103 C CG  . GLU B 114 ? 0.5031 0.3967 0.4275 -0.0037 0.0931  -0.0684 114 GLU B CG  
4104 C CD  . GLU B 114 ? 0.5563 0.4477 0.4584 -0.0101 0.0923  -0.076  114 GLU B CD  
4105 O OE1 . GLU B 114 ? 0.5272 0.4087 0.423  -0.0111 0.0992  -0.0857 114 GLU B OE1 
4106 O OE2 . GLU B 114 ? 0.5369 0.4361 0.4285 -0.0139 0.0847  -0.0728 114 GLU B OE2 
4107 N N   . TYR B 115 ? 0.503  0.4217 0.4618 0.0035  0.0977  -0.0492 115 TYR B N   
4108 C CA  . TYR B 115 ? 0.4657 0.3911 0.4307 0.0022  0.0899  -0.0401 115 TYR B CA  
4109 C C   . TYR B 115 ? 0.4403 0.3706 0.4304 0.0061  0.0883  -0.0364 115 TYR B C   
4110 O O   . TYR B 115 ? 0.4214 0.3522 0.4183 0.006   0.0789  -0.0315 115 TYR B O   
4111 C CB  . TYR B 115 ? 0.4697 0.4011 0.4267 -0.0004 0.0944  -0.0358 115 TYR B CB  
4112 C CG  . TYR B 115 ? 0.4707 0.4001 0.4028 -0.0038 0.0919  -0.0353 115 TYR B CG  
4113 C CD1 . TYR B 115 ? 0.4812 0.4063 0.3962 -0.0051 0.0923  -0.0423 115 TYR B CD1 
4114 C CD2 . TYR B 115 ? 0.4808 0.4129 0.4066 -0.0054 0.0891  -0.0275 115 TYR B CD2 
4115 C CE1 . TYR B 115 ? 0.4831 0.4094 0.3761 -0.0075 0.0892  -0.0417 115 TYR B CE1 
4116 C CE2 . TYR B 115 ? 0.4973 0.4282 0.4004 -0.0068 0.0866  -0.0261 115 TYR B CE2 
4117 C CZ  . TYR B 115 ? 0.4954 0.4249 0.3823 -0.0075 0.0865  -0.0331 115 TYR B CZ  
4118 O OH  . TYR B 115 ? 0.5165 0.4475 0.3817 -0.0082 0.0832  -0.0314 115 TYR B OH  
4119 N N   . GLY B 116 ? 0.4528 0.3877 0.4568 0.01    0.0974  -0.039  116 GLY B N   
4120 C CA  . GLY B 116 ? 0.4506 0.3934 0.4797 0.0144  0.0955  -0.0358 116 GLY B CA  
4121 C C   . GLY B 116 ? 0.4418 0.3775 0.4774 0.0185  0.0869  -0.0354 116 GLY B C   
4122 O O   . GLY B 116 ? 0.4124 0.3529 0.4599 0.0194  0.0787  -0.0299 116 GLY B O   
4123 N N   . LYS B 117 ? 0.4401 0.3632 0.4664 0.0205  0.0893  -0.0415 117 LYS B N   
4124 C CA  . LYS B 117 ? 0.4639 0.3767 0.4944 0.0245  0.0831  -0.0412 117 LYS B CA  
4125 C C   . LYS B 117 ? 0.4611 0.3704 0.4826 0.0194  0.0715  -0.0365 117 LYS B C   
4126 O O   . LYS B 117 ? 0.4269 0.335  0.4577 0.0222  0.0639  -0.0318 117 LYS B O   
4127 C CB  . LYS B 117 ? 0.5158 0.4134 0.5351 0.026   0.0899  -0.0497 117 LYS B CB  
4128 C CG  . LYS B 117 ? 0.6017 0.5002 0.6314 0.033   0.1018  -0.0551 117 LYS B CG  
4129 C CD  . LYS B 117 ? 0.6683 0.568  0.7202 0.0436  0.1018  -0.053  117 LYS B CD  
4130 C CE  . LYS B 117 ? 0.7547 0.6342 0.8021 0.0483  0.1012  -0.0559 117 LYS B CE  
4131 N NZ  . LYS B 117 ? 0.7723 0.6545 0.8404 0.0589  0.0974  -0.0507 117 LYS B NZ  
4132 N N   . VAL B 118 ? 0.4241 0.3329 0.4276 0.0125  0.07    -0.0374 118 VAL B N   
4133 C CA  . VAL B 118 ? 0.4278 0.3339 0.4223 0.0079  0.0602  -0.034  118 VAL B CA  
4134 C C   . VAL B 118 ? 0.4479 0.3638 0.4524 0.0075  0.0532  -0.026  118 VAL B C   
4135 O O   . VAL B 118 ? 0.3738 0.2871 0.3801 0.007   0.0448  -0.0223 118 VAL B O   
4136 C CB  . VAL B 118 ? 0.4253 0.3298 0.3987 0.0017  0.0605  -0.038  118 VAL B CB  
4137 C CG1 . VAL B 118 ? 0.414  0.319  0.3798 -0.0026 0.0508  -0.0346 118 VAL B CG1 
4138 C CG2 . VAL B 118 ? 0.4382 0.3317 0.4018 0.0008  0.0662  -0.047  118 VAL B CG2 
4139 N N   . TYR B 119 ? 0.4039 0.3299 0.4128 0.0068  0.057   -0.0235 119 TYR B N   
4140 C CA  . TYR B 119 ? 0.3987 0.3329 0.4177 0.0057  0.0514  -0.0169 119 TYR B CA  
4141 C C   . TYR B 119 ? 0.3787 0.3164 0.4177 0.0106  0.0478  -0.0148 119 TYR B C   
4142 O O   . TYR B 119 ? 0.39   0.3307 0.4347 0.0098  0.0395  -0.01   119 TYR B O   
4143 C CB  . TYR B 119 ? 0.3919 0.3341 0.4115 0.0032  0.0578  -0.0152 119 TYR B CB  
4144 C CG  . TYR B 119 ? 0.3953 0.3346 0.3947 -0.0012 0.0576  -0.0137 119 TYR B CG  
4145 C CD1 . TYR B 119 ? 0.3842 0.3242 0.3798 -0.004  0.0511  -0.0082 119 TYR B CD1 
4146 C CD2 . TYR B 119 ? 0.4024 0.3384 0.3857 -0.0019 0.064   -0.0179 119 TYR B CD2 
4147 C CE1 . TYR B 119 ? 0.3978 0.3349 0.3749 -0.0062 0.0507  -0.0064 119 TYR B CE1 
4148 C CE2 . TYR B 119 ? 0.4006 0.3351 0.3651 -0.0046 0.063   -0.016  119 TYR B CE2 
4149 C CZ  . TYR B 119 ? 0.3972 0.3322 0.3587 -0.0062 0.0564  -0.01   119 TYR B CZ  
4150 O OH  . TYR B 119 ? 0.3985 0.3319 0.3412 -0.0071 0.0554  -0.0079 119 TYR B OH  
4151 N N   . LYS B 120 ? 0.3748 0.3125 0.4241 0.0164  0.0539  -0.0184 120 LYS B N   
4152 C CA  . LYS B 120 ? 0.4065 0.3477 0.4743 0.023   0.0502  -0.0164 120 LYS B CA  
4153 C C   . LYS B 120 ? 0.4086 0.3387 0.471  0.0244  0.0412  -0.014  120 LYS B C   
4154 O O   . LYS B 120 ? 0.4275 0.3623 0.5009 0.0271  0.0338  -0.0093 120 LYS B O   
4155 C CB  . LYS B 120 ? 0.4097 0.3527 0.4896 0.0305  0.0589  -0.0208 120 LYS B CB  
4156 C CG  . LYS B 120 ? 0.4367 0.3906 0.54   0.038   0.055   -0.0175 120 LYS B CG  
4157 C CD  . LYS B 120 ? 0.4765 0.4369 0.5957 0.0463  0.0642  -0.0217 120 LYS B CD  
4158 C CE  . LYS B 120 ? 0.5177 0.4949 0.6616 0.0526  0.059   -0.018  120 LYS B CE  
4159 N NZ  . LYS B 120 ? 0.5965 0.5819 0.7575 0.0617  0.068   -0.0221 120 LYS B NZ  
4160 N N   . ILE B 121 ? 0.4107 0.3266 0.456  0.0219  0.0421  -0.0173 121 ILE B N   
4161 C CA  . ILE B 121 ? 0.398  0.3021 0.4358 0.0214  0.0348  -0.0153 121 ILE B CA  
4162 C C   . ILE B 121 ? 0.3981 0.3083 0.434  0.0166  0.0257  -0.0097 121 ILE B C   
4163 O O   . ILE B 121 ? 0.3714 0.2802 0.4123 0.0188  0.0184  -0.0052 121 ILE B O   
4164 C CB  . ILE B 121 ? 0.4203 0.3096 0.44   0.0174  0.0383  -0.0211 121 ILE B CB  
4165 C CG1 . ILE B 121 ? 0.4406 0.3208 0.4614 0.0223  0.0473  -0.0271 121 ILE B CG1 
4166 C CG2 . ILE B 121 ? 0.4479 0.3264 0.459  0.0145  0.0311  -0.0187 121 ILE B CG2 
4167 C CD1 . ILE B 121 ? 0.4638 0.3335 0.4664 0.0165  0.053   -0.0351 121 ILE B CD1 
4168 N N   . HIS B 122 ? 0.3618 0.2786 0.3905 0.0109  0.0264  -0.0098 122 HIS B N   
4169 C CA  . HIS B 122 ? 0.3705 0.2924 0.3971 0.0068  0.019   -0.005  122 HIS B CA  
4170 C C   . HIS B 122 ? 0.3746 0.3062 0.4183 0.0095  0.0146  -0.0005 122 HIS B C   
4171 O O   . HIS B 122 ? 0.3606 0.2921 0.4045 0.0083  0.0065  0.0034  122 HIS B O   
4172 C CB  . HIS B 122 ? 0.3962 0.3221 0.4119 0.0018  0.0215  -0.0055 122 HIS B CB  
4173 C CG  . HIS B 122 ? 0.4121 0.3427 0.4274 -0.0014 0.0155  -0.0008 122 HIS B CG  
4174 N ND1 . HIS B 122 ? 0.4195 0.3465 0.4308 -0.0028 0.0076  0.0016  122 HIS B ND1 
4175 C CD2 . HIS B 122 ? 0.4143 0.3517 0.4331 -0.0035 0.0167  0.0019  122 HIS B CD2 
4176 C CE1 . HIS B 122 ? 0.4306 0.362  0.4418 -0.0055 0.004   0.0051  122 HIS B CE1 
4177 N NE2 . HIS B 122 ? 0.4255 0.3625 0.4415 -0.006  0.0094  0.0054  122 HIS B NE2 
4178 N N   . ARG B 123 ? 0.3914 0.3329 0.4489 0.0119  0.0201  -0.0014 123 ARG B N   
4179 C CA  . ARG B 123 ? 0.4009 0.3551 0.4766 0.0137  0.0162  0.0017  123 ARG B CA  
4180 C C   . ARG B 123 ? 0.3894 0.3419 0.4737 0.0203  0.0095  0.0041  123 ARG B C   
4181 O O   . ARG B 123 ? 0.3804 0.338  0.4695 0.0197  0.0009  0.008   123 ARG B O   
4182 C CB  . ARG B 123 ? 0.4081 0.3742 0.4977 0.015   0.0249  -0.0008 123 ARG B CB  
4183 C CG  . ARG B 123 ? 0.4114 0.3806 0.4941 0.0079  0.0304  -0.001  123 ARG B CG  
4184 C CD  . ARG B 123 ? 0.4354 0.4111 0.5216 0.0021  0.0249  0.0027  123 ARG B CD  
4185 N NE  . ARG B 123 ? 0.4447 0.4363 0.5537 0.0031  0.0241  0.0029  123 ARG B NE  
4186 C CZ  . ARG B 123 ? 0.4179 0.4177 0.5375 0.0021  0.0153  0.0052  123 ARG B CZ  
4187 N NH1 . ARG B 123 ? 0.41   0.4024 0.5189 -0.0002 0.0067  0.008   123 ARG B NH1 
4188 N NH2 . ARG B 123 ? 0.4075 0.4245 0.5489 0.0035  0.0154  0.0043  123 ARG B NH2 
4189 N N   . GLU B 124 ? 0.3998 0.3431 0.4832 0.0265  0.0133  0.0018  124 GLU B N   
4190 C CA  . GLU B 124 ? 0.4076 0.3457 0.4965 0.034   0.0077  0.0047  124 GLU B CA  
4191 C C   . GLU B 124 ? 0.4118 0.3389 0.4867 0.0307  -0.0007 0.0085  124 GLU B C   
4192 O O   . GLU B 124 ? 0.4082 0.3383 0.4887 0.0339  -0.009  0.0132  124 GLU B O   
4193 C CB  . GLU B 124 ? 0.427  0.3548 0.5166 0.0413  0.0153  0.001   124 GLU B CB  
4194 C CG  . GLU B 124 ? 0.4875 0.4301 0.5964 0.047   0.0221  -0.0017 124 GLU B CG  
4195 C CD  . GLU B 124 ? 0.5637 0.4971 0.6756 0.0558  0.0301  -0.0056 124 GLU B CD  
4196 O OE1 . GLU B 124 ? 0.5757 0.4887 0.6729 0.0567  0.0314  -0.0069 124 GLU B OE1 
4197 O OE2 . GLU B 124 ? 0.6783 0.6256 0.8082 0.0616  0.0353  -0.0075 124 GLU B OE2 
4198 N N   . LEU B 125 ? 0.4088 0.3247 0.4659 0.0243  0.0012  0.0062  125 LEU B N   
4199 C CA  . LEU B 125 ? 0.4277 0.3335 0.4712 0.0204  -0.0053 0.009   125 LEU B CA  
4200 C C   . LEU B 125 ? 0.4194 0.3357 0.4652 0.0165  -0.0129 0.0129  125 LEU B C   
4201 O O   . LEU B 125 ? 0.3974 0.3114 0.4419 0.0174  -0.0203 0.0171  125 LEU B O   
4202 C CB  . LEU B 125 ? 0.4002 0.2958 0.4265 0.014   -0.0013 0.0049  125 LEU B CB  
4203 C CG  . LEU B 125 ? 0.3945 0.2806 0.4071 0.0091  -0.0065 0.0067  125 LEU B CG  
4204 C CD1 . LEU B 125 ? 0.4273 0.2999 0.4382 0.0135  -0.0092 0.0099  125 LEU B CD1 
4205 C CD2 . LEU B 125 ? 0.4137 0.294  0.4128 0.0031  -0.0016 0.0011  125 LEU B CD2 
4206 N N   . SER B 126 ? 0.4189 0.3462 0.468  0.0123  -0.0107 0.0116  126 SER B N   
4207 C CA  . SER B 126 ? 0.4631 0.3981 0.5131 0.0078  -0.0168 0.0144  126 SER B CA  
4208 C C   . SER B 126 ? 0.4671 0.4127 0.5326 0.0115  -0.0231 0.0175  126 SER B C   
4209 O O   . SER B 126 ? 0.4346 0.3827 0.4982 0.0087  -0.0304 0.0202  126 SER B O   
4210 C CB  . SER B 126 ? 0.4397 0.3808 0.4881 0.0027  -0.0121 0.0126  126 SER B CB  
4211 O OG  . SER B 126 ? 0.4831 0.4343 0.5461 0.0048  -0.0069 0.0111  126 SER B OG  
4212 N N   . LYS B 127 ? 0.4368 0.3899 0.5179 0.0179  -0.0204 0.0168  127 LYS B N   
4213 C CA  . LYS B 127 ? 0.4584 0.4249 0.5559 0.0223  -0.0269 0.0194  127 LYS B CA  
4214 C C   . LYS B 127 ? 0.4951 0.453  0.5894 0.0294  -0.0338 0.0235  127 LYS B C   
4215 O O   . LYS B 127 ? 0.4642 0.4334 0.5704 0.0338  -0.0408 0.0263  127 LYS B O   
4216 C CB  . LYS B 127 ? 0.4452 0.4262 0.5627 0.0267  -0.0211 0.0168  127 LYS B CB  
4217 C CG  . LYS B 127 ? 0.5028 0.4951 0.6262 0.0192  -0.0152 0.0138  127 LYS B CG  
4218 C CD  . LYS B 127 ? 0.5342 0.5317 0.6671 0.0219  -0.0041 0.0098  127 LYS B CD  
4219 C CE  . LYS B 127 ? 0.5248 0.5413 0.6815 0.0269  -0.0034 0.0088  127 LYS B CE  
4220 N NZ  . LYS B 127 ? 0.5564 0.5723 0.7188 0.0329  0.007   0.0052  127 LYS B NZ  
4221 N N   . GLY B 128 ? 0.4337 0.3726 0.513  0.0309  -0.0314 0.0238  128 GLY B N   
4222 C CA  . GLY B 128 ? 0.4299 0.3575 0.5048 0.038   -0.0362 0.0282  128 GLY B CA  
4223 C C   . GLY B 128 ? 0.4332 0.3617 0.5213 0.0495  -0.0333 0.0284  128 GLY B C   
4224 O O   . GLY B 128 ? 0.4628 0.3856 0.5512 0.0576  -0.0384 0.0332  128 GLY B O   
4225 N N   . GLU B 129 ? 0.4527 0.3876 0.5512 0.051   -0.0245 0.0235  129 GLU B N   
4226 C CA  . GLU B 129 ? 0.459  0.3927 0.5688 0.0623  -0.0197 0.0226  129 GLU B CA  
4227 C C   . GLU B 129 ? 0.4456 0.3532 0.5394 0.0647  -0.0137 0.0214  129 GLU B C   
4228 O O   . GLU B 129 ? 0.4225 0.322  0.521  0.0753  -0.0114 0.0224  129 GLU B O   
4229 C CB  . GLU B 129 ? 0.5258 0.4759 0.6517 0.0622  -0.0115 0.0172  129 GLU B CB  
4230 C CG  . GLU B 129 ? 0.569  0.545  0.7126 0.0595  -0.0166 0.018   129 GLU B CG  
4231 C CD  . GLU B 129 ? 0.6548 0.6464 0.8126 0.0572  -0.0073 0.0127  129 GLU B CD  
4232 O OE1 . GLU B 129 ? 0.7182 0.7295 0.8891 0.0526  -0.0104 0.0127  129 GLU B OE1 
4233 O OE2 . GLU B 129 ? 0.7186 0.7029 0.8741 0.0592  0.0032  0.0084  129 GLU B OE2 
4234 N N   . ILE B 130 ? 0.4455 0.3406 0.5213 0.0547  -0.0103 0.0184  130 ILE B N   
4235 C CA  . ILE B 130 ? 0.4141 0.2847 0.4732 0.0542  -0.0055 0.0168  130 ILE B CA  
4236 C C   . ILE B 130 ? 0.4276 0.2895 0.4693 0.0449  -0.0106 0.019   130 ILE B C   
4237 O O   . ILE B 130 ? 0.4192 0.2942 0.4614 0.0384  -0.0153 0.0198  130 ILE B O   
4238 C CB  . ILE B 130 ? 0.4087 0.2742 0.4641 0.0512  0.0058  0.0087  130 ILE B CB  
4239 C CG1 . ILE B 130 ? 0.3977 0.2727 0.4464 0.0398  0.0073  0.0049  130 ILE B CG1 
4240 C CG2 . ILE B 130 ? 0.4228 0.2954 0.495  0.0612  0.0121  0.0062  130 ILE B CG2 
4241 C CD1 . ILE B 130 ? 0.4175 0.2908 0.4621 0.0368  0.0175  -0.0029 130 ILE B CD1 
4242 N N   . ASP B 131 ? 0.4528 0.2923 0.4795 0.0442  -0.0088 0.0197  131 ASP B N   
4243 C CA  . ASP B 131 ? 0.497  0.3275 0.5066 0.0343  -0.0112 0.0202  131 ASP B CA  
4244 C C   . ASP B 131 ? 0.4801 0.3058 0.48   0.0254  -0.0032 0.0121  131 ASP B C   
4245 O O   . ASP B 131 ? 0.4691 0.296  0.4736 0.0273  0.0039  0.0066  131 ASP B O   
4246 C CB  . ASP B 131 ? 0.5368 0.3479 0.5358 0.0375  -0.0145 0.0263  131 ASP B CB  
4247 C CG  . ASP B 131 ? 0.6544 0.4401 0.6446 0.0408  -0.0068 0.0246  131 ASP B CG  
4248 O OD1 . ASP B 131 ? 0.6632 0.4448 0.653  0.0384  0.0019  0.0169  131 ASP B OD1 
4249 O OD2 . ASP B 131 ? 0.7483 0.5172 0.7315 0.0462  -0.0093 0.031   131 ASP B OD2 
4250 N N   . VAL B 132 ? 0.4625 0.2832 0.4485 0.0159  -0.0046 0.0114  132 VAL B N   
4251 C CA  . VAL B 132 ? 0.4891 0.3097 0.466  0.0066  0.0007  0.004   132 VAL B CA  
4252 C C   . VAL B 132 ? 0.4723 0.2739 0.4417 0.006   0.0092  -0.0017 132 VAL B C   
4253 O O   . VAL B 132 ? 0.4587 0.2632 0.4256 0.0019  0.015   -0.0092 132 VAL B O   
4254 C CB  . VAL B 132 ? 0.5246 0.3474 0.4908 -0.0025 -0.0035 0.0049  132 VAL B CB  
4255 C CG1 . VAL B 132 ? 0.548  0.3515 0.5021 -0.0056 -0.0035 0.0073  132 VAL B CG1 
4256 C CG2 . VAL B 132 ? 0.5433 0.3751 0.5041 -0.0107 -0.0002 -0.0023 132 VAL B CG2 
4257 N N   . PHE B 133 ? 0.4904 0.2719 0.4556 0.0104  0.0103  0.0017  133 PHE B N   
4258 C CA  . PHE B 133 ? 0.5261 0.2868 0.4842 0.0104  0.0192  -0.0039 133 PHE B CA  
4259 C C   . PHE B 133 ? 0.487  0.2513 0.4562 0.0189  0.0249  -0.0079 133 PHE B C   
4260 O O   . PHE B 133 ? 0.4746 0.2322 0.4385 0.0151  0.033   -0.0164 133 PHE B O   
4261 C CB  . PHE B 133 ? 0.5968 0.332  0.5465 0.0142  0.0196  0.0016  133 PHE B CB  
4262 C CG  . PHE B 133 ? 0.6196 0.3486 0.5562 0.0047  0.016   0.0047  133 PHE B CG  
4263 C CD1 . PHE B 133 ? 0.661  0.382  0.5848 -0.0084 0.0213  -0.0024 133 PHE B CD1 
4264 C CD2 . PHE B 133 ? 0.7186 0.4514 0.6559 0.0084  0.0075  0.0142  133 PHE B CD2 
4265 C CE1 . PHE B 133 ? 0.6919 0.4094 0.6049 -0.0176 0.0188  0       133 PHE B CE1 
4266 C CE2 . PHE B 133 ? 0.7201 0.4469 0.6446 -0.0004 0.0053  0.0167  133 PHE B CE2 
4267 C CZ  . PHE B 133 ? 0.721  0.4398 0.6338 -0.0134 0.0114  0.0097  133 PHE B CZ  
4268 N N   . GLU B 134 ? 0.4973 0.2729 0.4818 0.0297  0.0211  -0.0024 134 GLU B N   
4269 C CA  . GLU B 134 ? 0.5272 0.311  0.5246 0.0374  0.0267  -0.0062 134 GLU B CA  
4270 C C   . GLU B 134 ? 0.4579 0.2596 0.4563 0.03    0.0295  -0.0126 134 GLU B C   
4271 O O   . GLU B 134 ? 0.4365 0.2363 0.435  0.0308  0.0379  -0.0197 134 GLU B O   
4272 C CB  . GLU B 134 ? 0.527  0.3247 0.5434 0.0496  0.0219  0.0003  134 GLU B CB  
4273 C CG  . GLU B 134 ? 0.6764 0.4592 0.6935 0.06    0.0181  0.0079  134 GLU B CG  
4274 C CD  . GLU B 134 ? 0.6914 0.4943 0.7268 0.0698  0.0097  0.015   134 GLU B CD  
4275 O OE1 . GLU B 134 ? 0.6668 0.4784 0.7177 0.0792  0.0138  0.013   134 GLU B OE1 
4276 O OE2 . GLU B 134 ? 0.556  0.3682 0.5908 0.067   -0.0001 0.0211  134 GLU B OE2 
4277 N N   . ALA B 135 ? 0.4799 0.2977 0.4782 0.0237  0.0227  -0.0098 135 ALA B N   
4278 C CA  . ALA B 135 ? 0.4478 0.2806 0.4445 0.0172  0.0249  -0.0147 135 ALA B CA  
4279 C C   . ALA B 135 ? 0.4717 0.2947 0.4534 0.0092  0.0313  -0.0233 135 ALA B C   
4280 O O   . ALA B 135 ? 0.4716 0.2987 0.4526 0.0088  0.0378  -0.0294 135 ALA B O   
4281 C CB  . ALA B 135 ? 0.4334 0.2803 0.4297 0.0121  0.0171  -0.0103 135 ALA B CB  
4282 N N   . SER B 136 ? 0.4714 0.2807 0.4407 0.0028  0.03    -0.0241 136 SER B N   
4283 C CA  . SER B 136 ? 0.4837 0.2848 0.4393 -0.0061 0.0356  -0.0331 136 SER B CA  
4284 C C   . SER B 136 ? 0.4869 0.2732 0.4412 -0.0023 0.045   -0.0396 136 SER B C   
4285 O O   . SER B 136 ? 0.4946 0.2829 0.4419 -0.0074 0.0506  -0.0483 136 SER B O   
4286 C CB  . SER B 136 ? 0.5198 0.309  0.4637 -0.0145 0.0335  -0.0332 136 SER B CB  
4287 O OG  . SER B 136 ? 0.6035 0.4092 0.5487 -0.0179 0.0257  -0.0286 136 SER B OG  
4288 N N   . ALA B 137 ? 0.4853 0.2558 0.4448 0.0065  0.047   -0.0359 137 ALA B N   
4289 C CA  . ALA B 137 ? 0.5042 0.2594 0.4636 0.0121  0.0566  -0.0418 137 ALA B CA  
4290 C C   . ALA B 137 ? 0.4998 0.2715 0.4682 0.0164  0.061   -0.0457 137 ALA B C   
4291 O O   . ALA B 137 ? 0.5207 0.2862 0.4831 0.0147  0.0696  -0.0546 137 ALA B O   
4292 C CB  . ALA B 137 ? 0.5175 0.257  0.484  0.0241  0.0567  -0.0352 137 ALA B CB  
4293 N N   . ASN B 138 ? 0.4917 0.2835 0.4741 0.0217  0.0557  -0.0391 138 ASN B N   
4294 C CA  . ASN B 138 ? 0.4808 0.2886 0.4722 0.0252  0.0605  -0.042  138 ASN B CA  
4295 C C   . ASN B 138 ? 0.4507 0.2675 0.4299 0.0152  0.0628  -0.0486 138 ASN B C   
4296 O O   . ASN B 138 ? 0.4939 0.3136 0.4722 0.0162  0.0706  -0.0547 138 ASN B O   
4297 C CB  . ASN B 138 ? 0.4665 0.2935 0.4755 0.0315  0.0542  -0.0336 138 ASN B CB  
4298 C CG  . ASN B 138 ? 0.4988 0.3205 0.5219 0.0437  0.0532  -0.0285 138 ASN B CG  
4299 O OD1 . ASN B 138 ? 0.5088 0.3107 0.5283 0.0488  0.0579  -0.0306 138 ASN B OD1 
4300 N ND2 . ASN B 138 ? 0.5    0.3392 0.5387 0.0484  0.0467  -0.0216 138 ASN B ND2 
4301 N N   . ILE B 139 ? 0.4451 0.2665 0.4147 0.0063  0.0562  -0.0474 139 ILE B N   
4302 C CA  . ILE B 139 ? 0.4527 0.2827 0.4096 -0.0025 0.0572  -0.0534 139 ILE B CA  
4303 C C   . ILE B 139 ? 0.4855 0.3006 0.4296 -0.0069 0.0653  -0.0642 139 ILE B C   
4304 O O   . ILE B 139 ? 0.4911 0.311  0.4295 -0.0082 0.0713  -0.0708 139 ILE B O   
4305 C CB  . ILE B 139 ? 0.4585 0.2965 0.4095 -0.0097 0.0482  -0.0497 139 ILE B CB  
4306 C CG1 . ILE B 139 ? 0.4561 0.3095 0.4181 -0.0059 0.0416  -0.0406 139 ILE B CG1 
4307 C CG2 . ILE B 139 ? 0.485  0.3306 0.4217 -0.0184 0.0488  -0.0568 139 ILE B CG2 
4308 C CD1 . ILE B 139 ? 0.4514 0.3097 0.4104 -0.0106 0.0328  -0.0357 139 ILE B CD1 
4309 N N   . GLY B 140 ? 0.4977 0.2933 0.4365 -0.0094 0.0662  -0.0663 140 GLY B N   
4310 C CA  . GLY B 140 ? 0.5125 0.2909 0.439  -0.0144 0.0745  -0.0771 140 GLY B CA  
4311 C C   . GLY B 140 ? 0.537  0.3083 0.4675 -0.0064 0.0844  -0.0819 140 GLY B C   
4312 O O   . GLY B 140 ? 0.5434 0.3118 0.4632 -0.011  0.0914  -0.092  140 GLY B O   
4313 N N   . LYS B 141 ? 0.5416 0.3109 0.4875 0.0059  0.0853  -0.0752 141 LYS B N   
4314 C CA  . LYS B 141 ? 0.5763 0.3407 0.5288 0.015   0.0952  -0.0794 141 LYS B CA  
4315 C C   . LYS B 141 ? 0.5414 0.325  0.4936 0.0136  0.099   -0.0833 141 LYS B C   
4316 O O   . LYS B 141 ? 0.5642 0.3425 0.5139 0.0163  0.109   -0.0911 141 LYS B O   
4317 C CB  . LYS B 141 ? 0.6149 0.3831 0.5878 0.0288  0.0933  -0.0702 141 LYS B CB  
4318 C CG  . LYS B 141 ? 0.712  0.4587 0.6879 0.0363  0.0928  -0.0661 141 LYS B CG  
4319 C CD  . LYS B 141 ? 0.7659 0.5249 0.7627 0.0489  0.0871  -0.0555 141 LYS B CD  
4320 C CE  . LYS B 141 ? 0.8317 0.5698 0.8325 0.0601  0.0876  -0.0509 141 LYS B CE  
4321 N NZ  . LYS B 141 ? 0.8709 0.5904 0.8704 0.0675  0.0997  -0.0585 141 LYS B NZ  
4322 N N   . GLN B 142 ? 0.5241 0.3284 0.4777 0.0097  0.0916  -0.0779 142 GLN B N   
4323 C CA  . GLN B 142 ? 0.559  0.3807 0.5118 0.0089  0.095   -0.0796 142 GLN B CA  
4324 C C   . GLN B 142 ? 0.562  0.3815 0.4948 0.0005  0.1002  -0.0904 142 GLN B C   
4325 O O   . GLN B 142 ? 0.538  0.3659 0.4678 0.0014  0.1067  -0.0938 142 GLN B O   
4326 C CB  . GLN B 142 ? 0.5471 0.3879 0.5057 0.0074  0.0856  -0.0702 142 GLN B CB  
4327 C CG  . GLN B 142 ? 0.5665 0.4241 0.5276 0.0085  0.0893  -0.069  142 GLN B CG  
4328 C CD  . GLN B 142 ? 0.5411 0.4003 0.5167 0.0172  0.0984  -0.0699 142 GLN B CD  
4329 O OE1 . GLN B 142 ? 0.559  0.4163 0.5515 0.025   0.0973  -0.0657 142 GLN B OE1 
4330 N NE2 . GLN B 142 ? 0.5451 0.4084 0.514  0.0165  0.1076  -0.0757 142 GLN B NE2 
4331 N N   . ARG B 143 ? 0.5594 0.3688 0.4782 -0.0083 0.0976  -0.0958 143 ARG B N   
4332 C CA  . ARG B 143 ? 0.6052 0.4145 0.5047 -0.0176 0.101   -0.1067 143 ARG B CA  
4333 C C   . ARG B 143 ? 0.5967 0.4282 0.4911 -0.0195 0.0975  -0.1038 143 ARG B C   
4334 O O   . ARG B 143 ? 0.5879 0.424  0.476  -0.0183 0.1044  -0.1082 143 ARG B O   
4335 C CB  . ARG B 143 ? 0.6829 0.4755 0.577  -0.0154 0.1135  -0.1174 143 ARG B CB  
4336 C CG  . ARG B 143 ? 0.8022 0.5696 0.6987 -0.0139 0.1166  -0.1197 143 ARG B CG  
4337 C CD  . ARG B 143 ? 0.9335 0.6794 0.8257 -0.0104 0.1293  -0.1298 143 ARG B CD  
4338 N NE  . ARG B 143 ? 1.0919 0.8391 0.9663 -0.0182 0.1358  -0.1425 143 ARG B NE  
4339 C CZ  . ARG B 143 ? 1.2628 1.0124 1.1196 -0.0314 0.1328  -0.1505 143 ARG B CZ  
4340 N NH1 . ARG B 143 ? 1.2304 0.985  1.0854 -0.0392 0.1227  -0.1468 143 ARG B NH1 
4341 N NH2 . ARG B 143 ? 1.3812 1.1299 1.2221 -0.037  0.1398  -0.1628 143 ARG B NH2 
4342 N N   . ILE B 144 ? 0.5472 0.3911 0.4443 -0.0215 0.0871  -0.0956 144 ILE B N   
4343 C CA  . ILE B 144 ? 0.5596 0.4224 0.4537 -0.0214 0.0832  -0.0901 144 ILE B CA  
4344 C C   . ILE B 144 ? 0.5972 0.4665 0.4707 -0.0283 0.0842  -0.0984 144 ILE B C   
4345 O O   . ILE B 144 ? 0.6384 0.5055 0.502  -0.0359 0.0809  -0.105  144 ILE B O   
4346 C CB  . ILE B 144 ? 0.5225 0.3939 0.423  -0.0221 0.0722  -0.0807 144 ILE B CB  
4347 C CG1 . ILE B 144 ? 0.4923 0.36   0.4124 -0.0148 0.071   -0.0722 144 ILE B CG1 
4348 C CG2 . ILE B 144 ? 0.5498 0.4383 0.4434 -0.023  0.0671  -0.0757 144 ILE B CG2 
4349 C CD1 . ILE B 144 ? 0.4667 0.3416 0.3928 -0.0154 0.0608  -0.0633 144 ILE B CD1 
4350 N N   . LYS B 145 ? 0.5827 0.4606 0.4498 -0.0258 0.0889  -0.098  145 LYS B N   
4351 C CA  . LYS B 145 ? 0.641  0.5259 0.4872 -0.0311 0.0898  -0.105  145 LYS B CA  
4352 C C   . LYS B 145 ? 0.6146 0.5163 0.4537 -0.0309 0.082   -0.0972 145 LYS B C   
4353 O O   . LYS B 145 ? 0.6363 0.546  0.4582 -0.0357 0.0787  -0.1022 145 LYS B O   
4354 C CB  . LYS B 145 ? 0.6918 0.572  0.5309 -0.0288 0.102   -0.1116 145 LYS B CB  
4355 C CG  . LYS B 145 ? 0.779  0.6414 0.6191 -0.0297 0.1107  -0.1223 145 LYS B CG  
4356 C CD  . LYS B 145 ? 0.9681 0.8252 0.8168 -0.022  0.1228  -0.1227 145 LYS B CD  
4357 C CE  . LYS B 145 ? 1.05   0.8897 0.896  -0.0215 0.1337  -0.1344 145 LYS B CE  
4358 N NZ  . LYS B 145 ? 1.1148 0.9556 0.9406 -0.0252 0.1417  -0.1444 145 LYS B NZ  
4359 N N   . THR B 146 ? 0.5213 0.4282 0.3721 -0.0253 0.0796  -0.0857 146 THR B N   
4360 C CA  . THR B 146 ? 0.5264 0.446  0.3686 -0.0242 0.0739  -0.078  146 THR B CA  
4361 C C   . THR B 146 ? 0.5557 0.482  0.4    -0.0264 0.0621  -0.0744 146 THR B C   
4362 O O   . THR B 146 ? 0.5123 0.4337 0.3708 -0.0267 0.0586  -0.0724 146 THR B O   
4363 C CB  . THR B 146 ? 0.5191 0.4402 0.3705 -0.0185 0.0779  -0.0684 146 THR B CB  
4364 O OG1 . THR B 146 ? 0.523  0.4416 0.3951 -0.0159 0.0745  -0.0619 146 THR B OG1 
4365 C CG2 . THR B 146 ? 0.5544 0.4708 0.4048 -0.0165 0.0905  -0.0725 146 THR B CG2 
4366 N N   . ALA B 147 ? 0.541  0.4792 0.3711 -0.0271 0.056   -0.0725 147 ALA B N   
4367 C CA  . ALA B 147 ? 0.5449 0.4918 0.3774 -0.028  0.0453  -0.0685 147 ALA B CA  
4368 C C   . ALA B 147 ? 0.5061 0.4506 0.3543 -0.0232 0.0431  -0.0575 147 ALA B C   
4369 O O   . ALA B 147 ? 0.5054 0.4506 0.363  -0.0244 0.0368  -0.0553 147 ALA B O   
4370 C CB  . ALA B 147 ? 0.5864 0.5473 0.4013 -0.0272 0.0399  -0.0676 147 ALA B CB  
4371 N N   . GLU B 148 ? 0.4781 0.4198 0.3285 -0.0186 0.0486  -0.0511 148 GLU B N   
4372 C CA  . GLU B 148 ? 0.4889 0.429  0.3529 -0.015  0.0467  -0.0413 148 GLU B CA  
4373 C C   . GLU B 148 ? 0.441  0.3737 0.3245 -0.0152 0.047   -0.0413 148 GLU B C   
4374 O O   . GLU B 148 ? 0.433  0.3666 0.3257 -0.0145 0.0409  -0.0359 148 GLU B O   
4375 C CB  . GLU B 148 ? 0.5319 0.4717 0.392  -0.0113 0.0523  -0.0344 148 GLU B CB  
4376 C CG  . GLU B 148 ? 0.5815 0.5168 0.4406 -0.0112 0.0634  -0.0383 148 GLU B CG  
4377 C CD  . GLU B 148 ? 0.6398 0.5774 0.4771 -0.0122 0.0676  -0.0435 148 GLU B CD  
4378 O OE1 . GLU B 148 ? 0.5628 0.5063 0.3863 -0.0139 0.0612  -0.0473 148 GLU B OE1 
4379 O OE2 . GLU B 148 ? 0.6723 0.6063 0.5082 -0.0114 0.0779  -0.0445 148 GLU B OE2 
4380 N N   . MET B 149 ? 0.4497 0.375  0.3392 -0.0155 0.054   -0.0471 149 MET B N   
4381 C CA  . MET B 149 ? 0.4714 0.3895 0.3783 -0.0144 0.0537  -0.0465 149 MET B CA  
4382 C C   . MET B 149 ? 0.4538 0.3678 0.3597 -0.0185 0.048   -0.0508 149 MET B C   
4383 O O   . MET B 149 ? 0.4371 0.3467 0.3547 -0.0176 0.0443  -0.0473 149 MET B O   
4384 C CB  . MET B 149 ? 0.4821 0.3937 0.3969 -0.0115 0.0635  -0.0503 149 MET B CB  
4385 C CG  . MET B 149 ? 0.4823 0.3989 0.4036 -0.008  0.0691  -0.045  149 MET B CG  
4386 S SD  . MET B 149 ? 0.4367 0.3585 0.3737 -0.006  0.0626  -0.0341 149 MET B SD  
4387 C CE  . MET B 149 ? 0.4513 0.3792 0.3718 -0.0078 0.0594  -0.0285 149 MET B CE  
4388 N N   . ASN B 150 ? 0.4975 0.4137 0.3888 -0.0234 0.0471  -0.0581 150 ASN B N   
4389 C CA  . ASN B 150 ? 0.4766 0.3915 0.3662 -0.029  0.0414  -0.062  150 ASN B CA  
4390 C C   . ASN B 150 ? 0.5035 0.4263 0.3978 -0.0283 0.0326  -0.0541 150 ASN B C   
4391 O O   . ASN B 150 ? 0.4451 0.363  0.3477 -0.0296 0.029   -0.0521 150 ASN B O   
4392 C CB  . ASN B 150 ? 0.5564 0.4754 0.43   -0.0352 0.0421  -0.072  150 ASN B CB  
4393 C CG  . ASN B 150 ? 0.5957 0.5157 0.4684 -0.0423 0.0366  -0.0763 150 ASN B CG  
4394 O OD1 . ASN B 150 ? 0.6465 0.5538 0.5266 -0.0443 0.038   -0.0774 150 ASN B OD1 
4395 N ND2 . ASN B 150 ? 0.6554 0.5907 0.5201 -0.0454 0.0299  -0.0775 150 ASN B ND2 
4396 N N   . ILE B 151 ? 0.4549 0.3885 0.3438 -0.0254 0.0297  -0.0489 151 ILE B N   
4397 C CA  . ILE B 151 ? 0.4158 0.3559 0.3084 -0.0236 0.0224  -0.0414 151 ILE B CA  
4398 C C   . ILE B 151 ? 0.3906 0.3241 0.2983 -0.0202 0.0224  -0.0342 151 ILE B C   
4399 O O   . ILE B 151 ? 0.3588 0.292  0.2726 -0.0211 0.0169  -0.0311 151 ILE B O   
4400 C CB  . ILE B 151 ? 0.4271 0.3779 0.3085 -0.0204 0.02    -0.0376 151 ILE B CB  
4401 C CG1 . ILE B 151 ? 0.4547 0.4158 0.3223 -0.0239 0.0171  -0.0449 151 ILE B CG1 
4402 C CG2 . ILE B 151 ? 0.4379 0.3922 0.3242 -0.0171 0.0142  -0.0292 151 ILE B CG2 
4403 C CD1 . ILE B 151 ? 0.4944 0.4648 0.3475 -0.0198 0.0162  -0.0423 151 ILE B CD1 
4404 N N   . PHE B 152 ? 0.3919 0.3214 0.3051 -0.0167 0.0284  -0.0318 152 PHE B N   
4405 C CA  . PHE B 152 ? 0.4015 0.3275 0.3299 -0.0138 0.0281  -0.0257 152 PHE B CA  
4406 C C   . PHE B 152 ? 0.4069 0.325  0.3447 -0.0147 0.0264  -0.0274 152 PHE B C   
4407 O O   . PHE B 152 ? 0.3846 0.3018 0.3319 -0.0135 0.0218  -0.0222 152 PHE B O   
4408 C CB  . PHE B 152 ? 0.4075 0.3331 0.3419 -0.0106 0.0356  -0.0238 152 PHE B CB  
4409 C CG  . PHE B 152 ? 0.4019 0.3285 0.3509 -0.0085 0.0336  -0.0169 152 PHE B CG  
4410 C CD1 . PHE B 152 ? 0.445  0.3751 0.3915 -0.0086 0.0299  -0.0109 152 PHE B CD1 
4411 C CD2 . PHE B 152 ? 0.3968 0.3208 0.3615 -0.0064 0.0349  -0.0166 152 PHE B CD2 
4412 C CE1 . PHE B 152 ? 0.447  0.3779 0.406  -0.008  0.0277  -0.0057 152 PHE B CE1 
4413 C CE2 . PHE B 152 ? 0.4309 0.3581 0.409  -0.0051 0.0322  -0.011  152 PHE B CE2 
4414 C CZ  . PHE B 152 ? 0.4301 0.3606 0.4052 -0.0067 0.0286  -0.006  152 PHE B CZ  
4415 N N   . SER B 153 ? 0.4065 0.3179 0.3405 -0.0168 0.0301  -0.0346 153 SER B N   
4416 C CA  . SER B 153 ? 0.4528 0.3535 0.3936 -0.0172 0.0292  -0.0357 153 SER B CA  
4417 C C   . SER B 153 ? 0.4624 0.3639 0.4008 -0.0212 0.0217  -0.0337 153 SER B C   
4418 O O   . SER B 153 ? 0.4636 0.3584 0.4093 -0.0202 0.0188  -0.03   153 SER B O   
4419 C CB  . SER B 153 ? 0.488  0.3785 0.4239 -0.0188 0.0359  -0.044  153 SER B CB  
4420 O OG  . SER B 153 ? 0.4623 0.3545 0.3846 -0.0258 0.0349  -0.0508 153 SER B OG  
4421 N N   . LYS B 154 ? 0.4153 0.3261 0.3437 -0.0251 0.0184  -0.0355 154 LYS B N   
4422 C CA  . LYS B 154 ? 0.404  0.3188 0.3309 -0.0286 0.0119  -0.0339 154 LYS B CA  
4423 C C   . LYS B 154 ? 0.4123 0.3315 0.346  -0.0247 0.0072  -0.0255 154 LYS B C   
4424 O O   . LYS B 154 ? 0.3948 0.3109 0.3326 -0.0257 0.0032  -0.0223 154 LYS B O   
4425 C CB  . LYS B 154 ? 0.4445 0.3705 0.3601 -0.0331 0.01    -0.0393 154 LYS B CB  
4426 C CG  . LYS B 154 ? 0.4874 0.4074 0.3962 -0.039  0.0148  -0.0492 154 LYS B CG  
4427 C CD  . LYS B 154 ? 0.5752 0.5089 0.4727 -0.0426 0.0134  -0.0553 154 LYS B CD  
4428 C CE  . LYS B 154 ? 0.6129 0.5407 0.5028 -0.0488 0.0188  -0.066  154 LYS B CE  
4429 N NZ  . LYS B 154 ? 0.5955 0.5078 0.4887 -0.0541 0.0214  -0.0694 154 LYS B NZ  
4430 N N   . MET B 155 ? 0.3724 0.2972 0.3063 -0.0207 0.0084  -0.022  155 MET B N   
4431 C CA  . MET B 155 ? 0.3836 0.3114 0.323  -0.0179 0.0047  -0.0148 155 MET B CA  
4432 C C   . MET B 155 ? 0.3855 0.3065 0.3373 -0.0162 0.004   -0.0112 155 MET B C   
4433 O O   . MET B 155 ? 0.3607 0.2822 0.3159 -0.0163 -0.001  -0.0069 155 MET B O   
4434 C CB  . MET B 155 ? 0.4018 0.3343 0.3379 -0.0147 0.0075  -0.0119 155 MET B CB  
4435 C CG  . MET B 155 ? 0.4206 0.3611 0.3435 -0.0147 0.0057  -0.0131 155 MET B CG  
4436 S SD  . MET B 155 ? 0.4998 0.4423 0.4157 -0.0104 0.0095  -0.0081 155 MET B SD  
4437 C CE  . MET B 155 ? 0.512  0.4501 0.4301 -0.0101 0.0184  -0.0105 155 MET B CE  
4438 N N   . LEU B 156 ? 0.3521 0.2679 0.3106 -0.0141 0.0088  -0.0128 156 LEU B N   
4439 C CA  . LEU B 156 ? 0.3948 0.307  0.3662 -0.0111 0.0073  -0.0089 156 LEU B CA  
4440 C C   . LEU B 156 ? 0.3905 0.2956 0.3613 -0.0128 0.0023  -0.008  156 LEU B C   
4441 O O   . LEU B 156 ? 0.3557 0.2606 0.3332 -0.0113 -0.0022 -0.0032 156 LEU B O   
4442 C CB  . LEU B 156 ? 0.3722 0.282  0.3526 -0.0071 0.0134  -0.0106 156 LEU B CB  
4443 C CG  . LEU B 156 ? 0.4089 0.3086 0.3862 -0.0068 0.0177  -0.0162 156 LEU B CG  
4444 C CD1 . LEU B 156 ? 0.4124 0.3027 0.3966 -0.004  0.0148  -0.0138 156 LEU B CD1 
4445 C CD2 . LEU B 156 ? 0.4575 0.358  0.4372 -0.004  0.0263  -0.0203 156 LEU B CD2 
4446 N N   . LEU B 157 ? 0.3745 0.2741 0.3362 -0.0167 0.0034  -0.0127 157 LEU B N   
4447 C CA  . LEU B 157 ? 0.3835 0.276  0.3419 -0.0199 -0.0002 -0.012  157 LEU B CA  
4448 C C   . LEU B 157 ? 0.3669 0.2665 0.3222 -0.0224 -0.006  -0.0089 157 LEU B C   
4449 O O   . LEU B 157 ? 0.3932 0.2885 0.35   -0.0227 -0.0099 -0.005  157 LEU B O   
4450 C CB  . LEU B 157 ? 0.3779 0.2626 0.3276 -0.0249 0.0038  -0.0189 157 LEU B CB  
4451 C CG  . LEU B 157 ? 0.4168 0.29   0.369  -0.0219 0.0101  -0.0221 157 LEU B CG  
4452 C CD1 . LEU B 157 ? 0.4563 0.3218 0.3982 -0.0282 0.0149  -0.0306 157 LEU B CD1 
4453 C CD2 . LEU B 157 ? 0.4122 0.274  0.3718 -0.0168 0.0086  -0.0168 157 LEU B CD2 
4454 N N   . MET B 158 ? 0.3862 0.2964 0.3369 -0.0234 -0.0064 -0.0101 158 MET B N   
4455 C CA  . MET B 158 ? 0.3424 0.2598 0.2905 -0.0242 -0.0112 -0.0071 158 MET B CA  
4456 C C   . MET B 158 ? 0.3615 0.2784 0.3171 -0.0209 -0.0143 -0.001  158 MET B C   
4457 O O   . MET B 158 ? 0.3538 0.2705 0.3084 -0.0222 -0.0185 0.0015  158 MET B O   
4458 C CB  . MET B 158 ? 0.3444 0.2724 0.286  -0.0238 -0.0108 -0.0089 158 MET B CB  
4459 C CG  . MET B 158 ? 0.3982 0.3305 0.3321 -0.0279 -0.0092 -0.0157 158 MET B CG  
4460 S SD  . MET B 158 ? 0.4342 0.3801 0.3595 -0.0258 -0.0091 -0.0178 158 MET B SD  
4461 C CE  . MET B 158 ? 0.4115 0.3657 0.3362 -0.0243 -0.0147 -0.0139 158 MET B CE  
4462 N N   . TYR B 159 ? 0.3504 0.2679 0.3132 -0.0174 -0.012  0.0008  159 TYR B N   
4463 C CA  . TYR B 159 ? 0.3822 0.3008 0.3531 -0.0154 -0.0147 0.0055  159 TYR B CA  
4464 C C   . TYR B 159 ? 0.3819 0.2949 0.3579 -0.0151 -0.0186 0.0078  159 TYR B C   
4465 O O   . TYR B 159 ? 0.3546 0.2687 0.3322 -0.0156 -0.0234 0.011   159 TYR B O   
4466 C CB  . TYR B 159 ? 0.358  0.2796 0.337  -0.0128 -0.0105 0.0062  159 TYR B CB  
4467 C CG  . TYR B 159 ? 0.3574 0.2833 0.3303 -0.0128 -0.0069 0.0059  159 TYR B CG  
4468 C CD1 . TYR B 159 ? 0.3812 0.3088 0.3479 -0.0134 -0.0094 0.0083  159 TYR B CD1 
4469 C CD2 . TYR B 159 ? 0.359  0.2859 0.3308 -0.0116 -0.0006 0.0035  159 TYR B CD2 
4470 C CE1 . TYR B 159 ? 0.3893 0.3186 0.3487 -0.0123 -0.0061 0.0091  159 TYR B CE1 
4471 C CE2 . TYR B 159 ? 0.3779 0.3074 0.342  -0.0112 0.0027  0.0042  159 TYR B CE2 
4472 C CZ  . TYR B 159 ? 0.3814 0.3118 0.339  -0.0112 -0.0002 0.0073  159 TYR B CZ  
4473 O OH  . TYR B 159 ? 0.3788 0.3097 0.3272 -0.0097 0.0032  0.0088  159 TYR B OH  
4474 N N   . ASP B 160 ? 0.3564 0.2628 0.3342 -0.0138 -0.0163 0.0061  160 ASP B N   
4475 C CA  . ASP B 160 ? 0.3818 0.281  0.3626 -0.0122 -0.0199 0.009   160 ASP B CA  
4476 C C   . ASP B 160 ? 0.389  0.2839 0.36   -0.0164 -0.0236 0.01    160 ASP B C   
4477 O O   . ASP B 160 ? 0.3753 0.2683 0.3471 -0.0157 -0.0286 0.0141  160 ASP B O   
4478 C CB  . ASP B 160 ? 0.3906 0.2812 0.3736 -0.0092 -0.0155 0.007   160 ASP B CB  
4479 C CG  . ASP B 160 ? 0.4768 0.3578 0.4619 -0.0058 -0.0187 0.0109  160 ASP B CG  
4480 O OD1 . ASP B 160 ? 0.4869 0.373  0.4811 -0.0017 -0.0233 0.0151  160 ASP B OD1 
4481 O OD2 . ASP B 160 ? 0.4915 0.36   0.4686 -0.0074 -0.0167 0.0096  160 ASP B OD2 
4482 N N   . CYS B 161 ? 0.3791 0.2729 0.3408 -0.0209 -0.0211 0.006   161 CYS B N   
4483 C CA  . CYS B 161 ? 0.4179 0.3103 0.3712 -0.0257 -0.0235 0.0061  161 CYS B CA  
4484 C C   . CYS B 161 ? 0.4105 0.3099 0.3639 -0.0255 -0.0281 0.0092  161 CYS B C   
4485 O O   . CYS B 161 ? 0.3786 0.2744 0.3286 -0.027  -0.0315 0.0119  161 CYS B O   
4486 C CB  . CYS B 161 ? 0.4056 0.3025 0.3516 -0.0306 -0.0204 0.0004  161 CYS B CB  
4487 S SG  . CYS B 161 ? 0.4694 0.3556 0.4112 -0.0342 -0.0147 -0.005  161 CYS B SG  
4488 N N   . LEU B 162 ? 0.3889 0.297  0.3452 -0.0238 -0.0277 0.0089  162 LEU B N   
4489 C CA  . LEU B 162 ? 0.3965 0.3091 0.3521 -0.0237 -0.0312 0.0112  162 LEU B CA  
4490 C C   . LEU B 162 ? 0.4215 0.3312 0.3828 -0.0222 -0.0355 0.0153  162 LEU B C   
4491 O O   . LEU B 162 ? 0.3902 0.299  0.3478 -0.0238 -0.0393 0.0171  162 LEU B O   
4492 C CB  . LEU B 162 ? 0.4157 0.335  0.3719 -0.0217 -0.0289 0.0105  162 LEU B CB  
4493 C CG  . LEU B 162 ? 0.4286 0.3504 0.3822 -0.0214 -0.0311 0.0122  162 LEU B CG  
4494 C CD1 . LEU B 162 ? 0.3914 0.3157 0.3371 -0.0231 -0.0322 0.0105  162 LEU B CD1 
4495 C CD2 . LEU B 162 ? 0.4383 0.3629 0.3921 -0.0188 -0.0281 0.0127  162 LEU B CD2 
4496 N N   . ASN B 163 ? 0.4033 0.3131 0.3741 -0.0191 -0.0348 0.0164  163 ASN B N   
4497 C CA  . ASN B 163 ? 0.4118 0.3223 0.3902 -0.0172 -0.0394 0.0197  163 ASN B CA  
4498 C C   . ASN B 163 ? 0.4229 0.3259 0.3966 -0.017  -0.0433 0.0224  163 ASN B C   
4499 O O   . ASN B 163 ? 0.4144 0.3187 0.39   -0.0164 -0.0488 0.0253  163 ASN B O   
4500 C CB  . ASN B 163 ? 0.453  0.3669 0.444  -0.0133 -0.0375 0.02    163 ASN B CB  
4501 C CG  . ASN B 163 ? 0.578  0.4986 0.5737 -0.0136 -0.033  0.0182  163 ASN B CG  
4502 O OD1 . ASN B 163 ? 0.6493 0.5714 0.6395 -0.0162 -0.0326 0.0178  163 ASN B OD1 
4503 N ND2 . ASN B 163 ? 0.6213 0.5445 0.6259 -0.0107 -0.0287 0.0171  163 ASN B ND2 
4504 N N   . LYS B 164 ? 0.3996 0.2942 0.3672 -0.0176 -0.0405 0.0214  164 LYS B N   
4505 C CA  . LYS B 164 ? 0.4623 0.3466 0.4243 -0.017  -0.0432 0.0247  164 LYS B CA  
4506 C C   . LYS B 164 ? 0.4367 0.3168 0.3856 -0.0226 -0.0437 0.0245  164 LYS B C   
4507 O O   . LYS B 164 ? 0.414  0.2832 0.3552 -0.0237 -0.0436 0.0266  164 LYS B O   
4508 C CB  . LYS B 164 ? 0.513  0.3876 0.4756 -0.0145 -0.0386 0.0238  164 LYS B CB  
4509 C CG  . LYS B 164 ? 0.5919 0.4697 0.5677 -0.0079 -0.0375 0.0241  164 LYS B CG  
4510 C CD  . LYS B 164 ? 0.7076 0.586  0.6908 -0.0015 -0.0433 0.0294  164 LYS B CD  
4511 C CE  . LYS B 164 ? 0.7079 0.5936 0.7068 0.0051  -0.0417 0.0289  164 LYS B CE  
4512 N NZ  . LYS B 164 ? 0.6597 0.5366 0.6585 0.0074  -0.0342 0.0256  164 LYS B NZ  
4513 N N   . GLY B 165 ? 0.4231 0.311  0.3692 -0.0261 -0.0429 0.0217  165 GLY B N   
4514 C CA  . GLY B 165 ? 0.4652 0.3518 0.4006 -0.0311 -0.0426 0.0207  165 GLY B CA  
4515 C C   . GLY B 165 ? 0.4765 0.3573 0.4056 -0.0354 -0.0376 0.0178  165 GLY B C   
4516 O O   . GLY B 165 ? 0.489  0.3643 0.4091 -0.0396 -0.0371 0.0185  165 GLY B O   
4517 N N   . ASN B 166 ? 0.4088 0.2895 0.3418 -0.0349 -0.0335 0.0145  166 ASN B N   
4518 C CA  . ASN B 166 ? 0.3991 0.2744 0.3263 -0.0401 -0.0284 0.0105  166 ASN B CA  
4519 C C   . ASN B 166 ? 0.4009 0.2894 0.3293 -0.0424 -0.0259 0.0046  166 ASN B C   
4520 O O   . ASN B 166 ? 0.415  0.3056 0.347  -0.0411 -0.0232 0.0014  166 ASN B O   
4521 C CB  . ASN B 166 ? 0.4222 0.2848 0.3511 -0.0377 -0.0257 0.011   166 ASN B CB  
4522 C CG  . ASN B 166 ? 0.4538 0.3079 0.3756 -0.0443 -0.0198 0.0062  166 ASN B CG  
4523 O OD1 . ASN B 166 ? 0.4883 0.344  0.4033 -0.0513 -0.0184 0.004   166 ASN B OD1 
4524 N ND2 . ASN B 166 ? 0.5054 0.3528 0.4294 -0.043  -0.0157 0.0032  166 ASN B ND2 
4525 N N   . PHE B 167 ? 0.3971 0.2952 0.3223 -0.0453 -0.0267 0.003   167 PHE B N   
4526 C CA  . PHE B 167 ? 0.3631 0.276  0.2902 -0.0449 -0.0259 -0.0012 167 PHE B CA  
4527 C C   . PHE B 167 ? 0.393  0.3112 0.3175 -0.0506 -0.022  -0.0078 167 PHE B C   
4528 O O   . PHE B 167 ? 0.4143 0.3437 0.3407 -0.0489 -0.0216 -0.0113 167 PHE B O   
4529 C CB  . PHE B 167 ? 0.3711 0.2926 0.2968 -0.0437 -0.0284 0       167 PHE B CB  
4530 C CG  . PHE B 167 ? 0.3826 0.2996 0.3103 -0.0393 -0.0322 0.0053  167 PHE B CG  
4531 C CD1 . PHE B 167 ? 0.4058 0.3189 0.3395 -0.0349 -0.0335 0.008   167 PHE B CD1 
4532 C CD2 . PHE B 167 ? 0.3792 0.2958 0.3025 -0.0403 -0.0343 0.007   167 PHE B CD2 
4533 C CE1 . PHE B 167 ? 0.4017 0.3123 0.338  -0.0322 -0.0371 0.0119  167 PHE B CE1 
4534 C CE2 . PHE B 167 ? 0.3781 0.291  0.3026 -0.0373 -0.038  0.0108  167 PHE B CE2 
4535 C CZ  . PHE B 167 ? 0.3969 0.3072 0.3282 -0.0337 -0.0397 0.0132  167 PHE B CZ  
4536 N N   . ALA B 168 ? 0.4231 0.333  0.3428 -0.0576 -0.0191 -0.0097 168 ALA B N   
4537 C CA  . ALA B 168 ? 0.432  0.3492 0.3496 -0.065  -0.0154 -0.0171 168 ALA B CA  
4538 C C   . ALA B 168 ? 0.4202 0.3402 0.3399 -0.0641 -0.0136 -0.0218 168 ALA B C   
4539 O O   . ALA B 168 ? 0.4406 0.3758 0.3606 -0.0666 -0.0132 -0.0276 168 ALA B O   
4540 C CB  . ALA B 168 ? 0.4357 0.3397 0.3471 -0.0735 -0.0115 -0.018  168 ALA B CB  
4541 N N   . PRO B 169 ? 0.3974 0.3039 0.3182 -0.0605 -0.0122 -0.0199 169 PRO B N   
4542 C CA  . PRO B 169 ? 0.3983 0.3067 0.3195 -0.0603 -0.0096 -0.0251 169 PRO B CA  
4543 C C   . PRO B 169 ? 0.3865 0.3104 0.3106 -0.0544 -0.012  -0.0253 169 PRO B C   
4544 O O   . PRO B 169 ? 0.3687 0.2977 0.291  -0.0555 -0.0099 -0.0307 169 PRO B O   
4545 C CB  . PRO B 169 ? 0.4328 0.3226 0.3554 -0.0566 -0.0071 -0.0223 169 PRO B CB  
4546 C CG  . PRO B 169 ? 0.4238 0.3006 0.3446 -0.0569 -0.0084 -0.0163 169 PRO B CG  
4547 C CD  . PRO B 169 ? 0.4187 0.3081 0.3401 -0.0566 -0.0129 -0.0134 169 PRO B CD  
4548 N N   . MET B 170 ? 0.3921 0.3217 0.3193 -0.0485 -0.0158 -0.0196 170 MET B N   
4549 C CA  . MET B 170 ? 0.3993 0.3385 0.328  -0.0421 -0.0172 -0.0184 170 MET B CA  
4550 C C   . MET B 170 ? 0.3664 0.3221 0.2913 -0.0436 -0.0176 -0.0239 170 MET B C   
4551 O O   . MET B 170 ? 0.3916 0.3513 0.3145 -0.041  -0.0165 -0.0257 170 MET B O   
4552 C CB  . MET B 170 ? 0.3897 0.3297 0.3213 -0.0367 -0.0206 -0.0119 170 MET B CB  
4553 C CG  . MET B 170 ? 0.3929 0.3198 0.3291 -0.0345 -0.0211 -0.0067 170 MET B CG  
4554 S SD  . MET B 170 ? 0.3919 0.3206 0.331  -0.0298 -0.0251 -0.0006 170 MET B SD  
4555 C CE  . MET B 170 ? 0.3795 0.3147 0.3191 -0.0245 -0.0235 0       170 MET B CE  
4556 N N   . MET B 171 ? 0.4337 0.4001 0.3575 -0.0477 -0.0191 -0.0267 171 MET B N   
4557 C CA  . MET B 171 ? 0.437  0.4226 0.3586 -0.0485 -0.0205 -0.0322 171 MET B CA  
4558 C C   . MET B 171 ? 0.4178 0.4047 0.3361 -0.0552 -0.0176 -0.0402 171 MET B C   
4559 O O   . MET B 171 ? 0.4254 0.4253 0.3405 -0.0537 -0.0187 -0.044  171 MET B O   
4560 C CB  . MET B 171 ? 0.4606 0.4593 0.3839 -0.0511 -0.0224 -0.0338 171 MET B CB  
4561 C CG  . MET B 171 ? 0.5909 0.6133 0.5137 -0.0502 -0.0248 -0.0391 171 MET B CG  
4562 S SD  . MET B 171 ? 0.6218 0.6535 0.5411 -0.0379 -0.0283 -0.035  171 MET B SD  
4563 C CE  . MET B 171 ? 0.6517 0.6979 0.5741 -0.0312 -0.0317 -0.0321 171 MET B CE  
4564 N N   . LEU B 172 ? 0.4075 0.3792 0.3255 -0.0621 -0.0137 -0.0425 172 LEU B N   
4565 C CA  . LEU B 172 ? 0.397  0.365  0.3111 -0.0691 -0.0098 -0.0505 172 LEU B CA  
4566 C C   . LEU B 172 ? 0.3772 0.34   0.2891 -0.0634 -0.0083 -0.0501 172 LEU B C   
4567 O O   . LEU B 172 ? 0.3781 0.3506 0.2853 -0.0654 -0.0078 -0.0566 172 LEU B O   
4568 C CB  . LEU B 172 ? 0.4525 0.4012 0.3654 -0.0769 -0.0052 -0.052  172 LEU B CB  
4569 C CG  . LEU B 172 ? 0.5132 0.4646 0.4268 -0.084  -0.0052 -0.0524 172 LEU B CG  
4570 C CD1 . LEU B 172 ? 0.5392 0.4701 0.4487 -0.093  0.0005  -0.0547 172 LEU B CD1 
4571 C CD2 . LEU B 172 ? 0.5282 0.5047 0.443  -0.0892 -0.0072 -0.0592 172 LEU B CD2 
4572 N N   . LEU B 173 ? 0.38   0.3297 0.2952 -0.0565 -0.0076 -0.0428 173 LEU B N   
4573 C CA  . LEU B 173 ? 0.4012 0.3464 0.3156 -0.0509 -0.0053 -0.0419 173 LEU B CA  
4574 C C   . LEU B 173 ? 0.3912 0.3527 0.302  -0.0458 -0.008  -0.0413 173 LEU B C   
4575 O O   . LEU B 173 ? 0.407  0.371  0.3124 -0.0453 -0.0057 -0.0452 173 LEU B O   
4576 C CB  . LEU B 173 ? 0.3797 0.3114 0.3006 -0.0448 -0.0045 -0.0343 173 LEU B CB  
4577 C CG  . LEU B 173 ? 0.3988 0.3122 0.3217 -0.0474 -0.0012 -0.0346 173 LEU B CG  
4578 C CD1 . LEU B 173 ? 0.4273 0.3336 0.3574 -0.0418 -0.0036 -0.0261 173 LEU B CD1 
4579 C CD2 . LEU B 173 ? 0.453  0.3571 0.3742 -0.0472 0.0047  -0.0395 173 LEU B CD2 
4580 N N   . PHE B 174 ? 0.4061 0.3775 0.3186 -0.0419 -0.0126 -0.0364 174 PHE B N   
4581 C CA  . PHE B 174 ? 0.377  0.3626 0.2848 -0.036  -0.0155 -0.0348 174 PHE B CA  
4582 C C   . PHE B 174 ? 0.3851 0.3855 0.2861 -0.0399 -0.0163 -0.0431 174 PHE B C   
4583 O O   . PHE B 174 ? 0.3579 0.3639 0.2518 -0.036  -0.0162 -0.0435 174 PHE B O   
4584 C CB  . PHE B 174 ? 0.4116 0.4047 0.3223 -0.0319 -0.0198 -0.0296 174 PHE B CB  
4585 C CG  . PHE B 174 ? 0.4047 0.4125 0.3093 -0.025  -0.0229 -0.0281 174 PHE B CG  
4586 C CD1 . PHE B 174 ? 0.4659 0.4684 0.3662 -0.0176 -0.0218 -0.0223 174 PHE B CD1 
4587 C CD2 . PHE B 174 ? 0.4816 0.5086 0.3846 -0.0258 -0.0267 -0.0326 174 PHE B CD2 
4588 C CE1 . PHE B 174 ? 0.4838 0.4977 0.3762 -0.0109 -0.0243 -0.0205 174 PHE B CE1 
4589 C CE2 . PHE B 174 ? 0.4873 0.5282 0.3839 -0.0184 -0.03   -0.0312 174 PHE B CE2 
4590 C CZ  . PHE B 174 ? 0.4721 0.505  0.3624 -0.0105 -0.0288 -0.0246 174 PHE B CZ  
4591 N N   . GLN B 175 ? 0.3889 0.3962 0.2911 -0.0483 -0.017  -0.05   175 GLN B N   
4592 C CA  . GLN B 175 ? 0.3924 0.416  0.2892 -0.0537 -0.0182 -0.0592 175 GLN B CA  
4593 C C   . GLN B 175 ? 0.3997 0.4155 0.2896 -0.0568 -0.0139 -0.0649 175 GLN B C   
4594 O O   . GLN B 175 ? 0.4198 0.4499 0.3025 -0.0585 -0.0156 -0.0712 175 GLN B O   
4595 C CB  . GLN B 175 ? 0.4126 0.4436 0.3132 -0.0644 -0.0184 -0.0665 175 GLN B CB  
4596 C CG  . GLN B 175 ? 0.4248 0.4656 0.332  -0.0624 -0.0219 -0.0624 175 GLN B CG  
4597 C CD  . GLN B 175 ? 0.4191 0.4822 0.3257 -0.0538 -0.0277 -0.0601 175 GLN B CD  
4598 O OE1 . GLN B 175 ? 0.4448 0.5241 0.3465 -0.0534 -0.0304 -0.0651 175 GLN B OE1 
4599 N NE2 . GLN B 175 ? 0.5313 0.5958 0.4422 -0.0471 -0.0299 -0.0532 175 GLN B NE2 
4600 N N   . GLN B 176 ? 0.418  0.4122 0.3096 -0.0568 -0.0085 -0.0629 176 GLN B N   
4601 C CA  . GLN B 176 ? 0.4308 0.4162 0.3161 -0.0585 -0.0032 -0.0683 176 GLN B CA  
4602 C C   . GLN B 176 ? 0.4706 0.4583 0.3503 -0.0499 -0.0027 -0.0639 176 GLN B C   
4603 O O   . GLN B 176 ? 0.4925 0.4753 0.3654 -0.0511 0.0018  -0.0689 176 GLN B O   
4604 C CB  . GLN B 176 ? 0.4692 0.4311 0.359  -0.061  0.0029  -0.0683 176 GLN B CB  
4605 C CG  . GLN B 176 ? 0.482  0.4373 0.3748 -0.0699 0.0037  -0.072  176 GLN B CG  
4606 C CD  . GLN B 176 ? 0.5275 0.4588 0.4249 -0.0693 0.0083  -0.0685 176 GLN B CD  
4607 O OE1 . GLN B 176 ? 0.58   0.4995 0.4781 -0.0641 0.0124  -0.0669 176 GLN B OE1 
4608 N NE2 . GLN B 176 ? 0.5434 0.4676 0.4434 -0.0746 0.0083  -0.0678 176 GLN B NE2 
4609 N N   . ILE B 177 ? 0.4353 0.4281 0.3169 -0.0416 -0.0062 -0.0548 177 ILE B N   
4610 C CA  . ILE B 177 ? 0.4449 0.4373 0.3203 -0.034  -0.0047 -0.0498 177 ILE B CA  
4611 C C   . ILE B 177 ? 0.507  0.5179 0.371  -0.0312 -0.0093 -0.0514 177 ILE B C   
4612 O O   . ILE B 177 ? 0.4713 0.4961 0.3364 -0.0292 -0.0153 -0.0498 177 ILE B O   
4613 C CB  . ILE B 177 ? 0.4438 0.4291 0.3265 -0.0271 -0.0053 -0.0391 177 ILE B CB  
4614 C CG1 . ILE B 177 ? 0.4224 0.3911 0.3154 -0.0288 -0.0011 -0.0376 177 ILE B CG1 
4615 C CG2 . ILE B 177 ? 0.4525 0.4382 0.3276 -0.0196 -0.0037 -0.0331 177 ILE B CG2 
4616 C CD1 . ILE B 177 ? 0.4399 0.4031 0.3419 -0.0247 -0.003  -0.029  177 ILE B CD1 
4617 N N   . ASP B 178 ? 0.5411 0.5517 0.394  -0.0293 -0.0061 -0.0531 178 ASP B N   
4618 C CA  . ASP B 178 ? 0.5049 0.5306 0.3444 -0.0244 -0.0101 -0.0524 178 ASP B CA  
4619 C C   . ASP B 178 ? 0.4778 0.4938 0.3089 -0.0175 -0.0052 -0.0454 178 ASP B C   
4620 O O   . ASP B 178 ? 0.5356 0.5458 0.3593 -0.0197 0.0006  -0.0498 178 ASP B O   
4621 C CB  . ASP B 178 ? 0.5369 0.5756 0.3682 -0.0316 -0.012  -0.0641 178 ASP B CB  
4622 C CG  . ASP B 178 ? 0.6171 0.6747 0.4335 -0.0269 -0.0175 -0.0645 178 ASP B CG  
4623 O OD1 . ASP B 178 ? 0.6762 0.7362 0.4873 -0.0168 -0.02   -0.0548 178 ASP B OD1 
4624 O OD2 . ASP B 178 ? 0.7044 0.773  0.5134 -0.0332 -0.019  -0.0746 178 ASP B OD2 
4625 N N   . LEU B 179 ? 0.535  0.549  0.3664 -0.0094 -0.0067 -0.0349 179 LEU B N   
4626 C CA  . LEU B 179 ? 0.5345 0.538  0.3585 -0.0035 -0.0013 -0.0274 179 LEU B CA  
4627 C C   . LEU B 179 ? 0.5699 0.58   0.3743 -0.0011 -0.0006 -0.0291 179 LEU B C   
4628 O O   . LEU B 179 ? 0.5595 0.5596 0.3565 0.0003  0.0066  -0.0266 179 LEU B O   
4629 C CB  . LEU B 179 ? 0.5385 0.5374 0.3654 0.0037  -0.0031 -0.0165 179 LEU B CB  
4630 C CG  . LEU B 179 ? 0.5489 0.539  0.3933 0.0016  -0.0029 -0.0139 179 LEU B CG  
4631 C CD1 . LEU B 179 ? 0.5741 0.5582 0.4178 0.0085  -0.0035 -0.0038 179 LEU B CD1 
4632 C CD2 . LEU B 179 ? 0.5679 0.5452 0.4221 -0.0032 0.0041  -0.0159 179 LEU B CD2 
4633 N N   . SER B 180 ? 0.5503 0.5782 0.3464 -0.0012 -0.0077 -0.0341 180 SER B N   
4634 C CA  . SER B 180 ? 0.5957 0.632  0.3719 0.0011  -0.0083 -0.0363 180 SER B CA  
4635 C C   . SER B 180 ? 0.6291 0.6586 0.4001 -0.0063 -0.0009 -0.0452 180 SER B C   
4636 O O   . SER B 180 ? 0.5939 0.6261 0.347  -0.0046 0.0008  -0.0465 180 SER B O   
4637 C CB  . SER B 180 ? 0.5935 0.6534 0.3639 0.0023  -0.0185 -0.0407 180 SER B CB  
4638 O OG  . SER B 180 ? 0.5862 0.6554 0.361  -0.0083 -0.0199 -0.0538 180 SER B OG  
4639 N N   . GLU B 181 ? 0.647  0.6671 0.4322 -0.0139 0.0036  -0.0515 181 GLU B N   
4640 C CA  . GLU B 181 ? 0.6468 0.6576 0.4281 -0.0197 0.0118  -0.0597 181 GLU B CA  
4641 C C   . GLU B 181 ? 0.6189 0.6143 0.399  -0.0157 0.0214  -0.0534 181 GLU B C   
4642 O O   . GLU B 181 ? 0.6209 0.6101 0.3946 -0.0189 0.0289  -0.0597 181 GLU B O   
4643 C CB  . GLU B 181 ? 0.7237 0.7272 0.5198 -0.0279 0.0141  -0.0678 181 GLU B CB  
4644 C CG  . GLU B 181 ? 0.8182 0.8366 0.6153 -0.0343 0.0064  -0.076  181 GLU B CG  
4645 C CD  . GLU B 181 ? 0.9221 0.9322 0.7231 -0.0444 0.011   -0.0878 181 GLU B CD  
4646 O OE1 . GLU B 181 ? 0.9058 0.9094 0.721  -0.0486 0.0108  -0.0887 181 GLU B OE1 
4647 O OE2 . GLU B 181 ? 0.913  0.9223 0.7006 -0.0474 0.0153  -0.0955 181 GLU B OE2 
4648 N N   . ILE B 182 ? 0.6287 0.6179 0.4154 -0.0097 0.0219  -0.042  182 ILE B N   
4649 C CA  . ILE B 182 ? 0.6341 0.6105 0.4202 -0.0068 0.0313  -0.0359 182 ILE B CA  
4650 C C   . ILE B 182 ? 0.6881 0.6675 0.4512 -0.002  0.0328  -0.0316 182 ILE B C   
4651 O O   . ILE B 182 ? 0.6612 0.6447 0.4166 0.0041  0.0272  -0.0234 182 ILE B O   
4652 C CB  . ILE B 182 ? 0.571  0.5396 0.3731 -0.0038 0.0314  -0.0264 182 ILE B CB  
4653 C CG1 . ILE B 182 ? 0.5228 0.4894 0.3451 -0.0078 0.0288  -0.03   182 ILE B CG1 
4654 C CG2 . ILE B 182 ? 0.5886 0.5459 0.3921 -0.0022 0.0415  -0.0209 182 ILE B CG2 
4655 C CD1 . ILE B 182 ? 0.5289 0.4895 0.3659 -0.0054 0.0275  -0.0215 182 ILE B CD1 
4656 N N   . LYS B 183 ? 0.7019 0.6777 0.4532 -0.0042 0.0407  -0.0366 183 LYS B N   
4657 C CA  . LYS B 183 ? 0.8026 0.7819 0.5286 -0.0004 0.0417  -0.0338 183 LYS B CA  
4658 C C   . LYS B 183 ? 0.8252 0.7915 0.5453 0.0025  0.0526  -0.0257 183 LYS B C   
4659 O O   . LYS B 183 ? 0.93   0.895  0.6328 0.0082  0.0521  -0.0168 183 LYS B O   
4660 C CB  . LYS B 183 ? 0.8599 0.8476 0.5724 -0.0054 0.0412  -0.0463 183 LYS B CB  
4661 C CG  . LYS B 183 ? 0.8672 0.8713 0.5812 -0.0076 0.0288  -0.0524 183 LYS B CG  
4662 C CD  . LYS B 183 ? 0.9965 1.0128 0.6939 -0.0127 0.0258  -0.0644 183 LYS B CD  
4663 C CE  . LYS B 183 ? 0.993  1.0304 0.6851 -0.0109 0.0124  -0.0653 183 LYS B CE  
4664 N NZ  . LYS B 183 ? 0.9751 1.0169 0.689  -0.0124 0.0061  -0.0647 183 LYS B NZ  
4665 N N   . GLU B 184 ? 0.8384 0.7952 0.5719 -0.0013 0.0628  -0.0286 184 GLU B N   
4666 C CA  . GLU B 184 ? 0.9912 0.9386 0.7162 -0.0004 0.0748  -0.0241 184 GLU B CA  
4667 C C   . GLU B 184 ? 0.8542 0.7932 0.5896 0.0024  0.0774  -0.0123 184 GLU B C   
4668 O O   . GLU B 184 ? 0.8702 0.8019 0.5932 0.0038  0.0855  -0.0058 184 GLU B O   
4669 C CB  . GLU B 184 ? 1.1588 1.1029 0.8883 -0.0052 0.0852  -0.0344 184 GLU B CB  
4670 C CG  . GLU B 184 ? 1.2757 1.2264 0.9869 -0.008  0.0836  -0.0455 184 GLU B CG  
4671 C CD  . GLU B 184 ? 1.4226 1.3766 1.1024 -0.0056 0.084   -0.0432 184 GLU B CD  
4672 O OE1 . GLU B 184 ? 1.4611 1.4085 1.1293 -0.006  0.0957  -0.0432 184 GLU B OE1 
4673 O OE2 . GLU B 184 ? 1.4783 1.4423 1.145  -0.0028 0.0728  -0.0414 184 GLU B OE2 
4674 N N   . ASN B 185 ? 0.7184 0.6577 0.4737 0.0027  0.0709  -0.0093 185 ASN B N   
4675 C CA  . ASN B 185 ? 0.6563 0.587  0.4255 0.0031  0.075   -0.001  185 ASN B CA  
4676 C C   . ASN B 185 ? 0.6527 0.5831 0.4214 0.0074  0.0656  0.0072  185 ASN B C   
4677 O O   . ASN B 185 ? 0.5781 0.5118 0.3635 0.0067  0.0586  0.0059  185 ASN B O   
4678 C CB  . ASN B 185 ? 0.5892 0.519  0.3844 -0.0012 0.0794  -0.0063 185 ASN B CB  
4679 C CG  . ASN B 185 ? 0.6102 0.5334 0.4199 -0.0022 0.0854  0.0006  185 ASN B CG  
4680 O OD1 . ASN B 185 ? 0.5807 0.4988 0.3854 -0.0002 0.0835  0.0095  185 ASN B OD1 
4681 N ND2 . ASN B 185 ? 0.6348 0.5584 0.4634 -0.0052 0.0926  -0.0037 185 ASN B ND2 
4682 N N   . ARG B 186 ? 0.6793 0.6043 0.4284 0.0122  0.0663  0.0162  186 ARG B N   
4683 C CA  . ARG B 186 ? 0.7209 0.6442 0.4673 0.0178  0.0581  0.0241  186 ARG B CA  
4684 C C   . ARG B 186 ? 0.651  0.5663 0.4182 0.0156  0.0593  0.0283  186 ARG B C   
4685 O O   . ARG B 186 ? 0.5872 0.5047 0.3618 0.0182  0.0508  0.0302  186 ARG B O   
4686 C CB  . ARG B 186 ? 0.7771 0.6936 0.4963 0.0245  0.0596  0.0335  186 ARG B CB  
4687 C CG  . ARG B 186 ? 0.9231 0.8379 0.6381 0.0322  0.0509  0.0414  186 ARG B CG  
4688 C CD  . ARG B 186 ? 1.1078 1.0235 0.7945 0.0418  0.0465  0.0483  186 ARG B CD  
4689 N NE  . ARG B 186 ? 1.1643 1.0734 0.8278 0.042   0.0551  0.051   186 ARG B NE  
4690 C CZ  . ARG B 186 ? 1.1068 0.999  0.7645 0.0387  0.0681  0.0566  186 ARG B CZ  
4691 N NH1 . ARG B 186 ? 1.1461 1.0361 0.7843 0.0376  0.0757  0.0562  186 ARG B NH1 
4692 N NH2 . ARG B 186 ? 1.095  0.9735 0.7668 0.0355  0.0741  0.0615  186 ARG B NH2 
4693 N N   . TYR B 187 ? 0.6128 0.52   0.3891 0.0106  0.07    0.0293  187 TYR B N   
4694 C CA  . TYR B 187 ? 0.5859 0.487  0.3822 0.0072  0.0718  0.0322  187 TYR B CA  
4695 C C   . TYR B 187 ? 0.5697 0.4799 0.3876 0.0053  0.0635  0.0258  187 TYR B C   
4696 O O   . TYR B 187 ? 0.5316 0.4402 0.3585 0.0061  0.0573  0.0286  187 TYR B O   
4697 C CB  . TYR B 187 ? 0.58   0.4759 0.3861 0.0013  0.0842  0.0322  187 TYR B CB  
4698 C CG  . TYR B 187 ? 0.5431 0.4366 0.3721 -0.0029 0.084   0.0335  187 TYR B CG  
4699 C CD1 . TYR B 187 ? 0.5698 0.4519 0.3951 -0.0027 0.0843  0.0414  187 TYR B CD1 
4700 C CD2 . TYR B 187 ? 0.5331 0.4353 0.3863 -0.0065 0.0828  0.0268  187 TYR B CD2 
4701 C CE1 . TYR B 187 ? 0.5198 0.4005 0.3651 -0.0072 0.0835  0.0416  187 TYR B CE1 
4702 C CE2 . TYR B 187 ? 0.5266 0.4286 0.3999 -0.0099 0.0809  0.0278  187 TYR B CE2 
4703 C CZ  . TYR B 187 ? 0.543  0.4348 0.4122 -0.0108 0.0813  0.0348  187 TYR B CZ  
4704 O OH  . TYR B 187 ? 0.5827 0.475  0.4709 -0.0149 0.0789  0.0347  187 TYR B OH  
4705 N N   . LEU B 188 ? 0.5345 0.4526 0.359  0.0029  0.064   0.0172  188 LEU B N   
4706 C CA  . LEU B 188 ? 0.5404 0.4648 0.3833 0.0009  0.0574  0.0113  188 LEU B CA  
4707 C C   . LEU B 188 ? 0.51   0.4406 0.347  0.0039  0.0461  0.0105  188 LEU B C   
4708 O O   . LEU B 188 ? 0.4733 0.4055 0.3234 0.0033  0.0397  0.0104  188 LEU B O   
4709 C CB  . LEU B 188 ? 0.5529 0.4811 0.4022 -0.002  0.0625  0.0026  188 LEU B CB  
4710 C CG  . LEU B 188 ? 0.5594 0.4915 0.4269 -0.0039 0.0573  -0.0035 188 LEU B CG  
4711 C CD1 . LEU B 188 ? 0.5843 0.5159 0.4646 -0.0059 0.0651  -0.009  188 LEU B CD1 
4712 C CD2 . LEU B 188 ? 0.5878 0.5256 0.446  -0.0038 0.0498  -0.0091 188 LEU B CD2 
4713 N N   . LYS B 189 ? 0.5076 0.4433 0.3255 0.0071  0.0435  0.0096  189 LYS B N   
4714 C CA  . LYS B 189 ? 0.5383 0.4832 0.3522 0.0098  0.0328  0.0082  189 LYS B CA  
4715 C C   . LYS B 189 ? 0.5094 0.4502 0.3261 0.0139  0.0282  0.0161  189 LYS B C   
4716 O O   . LYS B 189 ? 0.4789 0.425  0.3047 0.014   0.0209  0.0147  189 LYS B O   
4717 C CB  . LYS B 189 ? 0.5955 0.5476 0.387  0.0136  0.0306  0.0073  189 LYS B CB  
4718 C CG  . LYS B 189 ? 0.633  0.5995 0.4207 0.0157  0.0198  0.0036  189 LYS B CG  
4719 C CD  . LYS B 189 ? 0.7312 0.7048 0.4952 0.0208  0.0178  0.0049  189 LYS B CD  
4720 C CE  . LYS B 189 ? 0.8155 0.8068 0.5743 0.0195  0.01    -0.0036 189 LYS B CE  
4721 N NZ  . LYS B 189 ? 0.8478 0.8503 0.6079 0.0251  0.0001  -0.0006 189 LYS B NZ  
4722 N N   . ASN B 190 ? 0.5427 0.4727 0.3507 0.0168  0.0335  0.0243  190 ASN B N   
4723 C CA  . ASN B 190 ? 0.5589 0.4812 0.3677 0.0206  0.031   0.0319  190 ASN B CA  
4724 C C   . ASN B 190 ? 0.4743 0.3933 0.3047 0.0158  0.0303  0.0308  190 ASN B C   
4725 O O   . ASN B 190 ? 0.4858 0.4051 0.3209 0.018   0.0241  0.0325  190 ASN B O   
4726 C CB  . ASN B 190 ? 0.6378 0.5457 0.432  0.0235  0.0386  0.0408  190 ASN B CB  
4727 C CG  . ASN B 190 ? 0.8345 0.7417 0.6107 0.0329  0.033   0.047   190 ASN B CG  
4728 O OD1 . ASN B 190 ? 0.8904 0.8067 0.6514 0.0374  0.0298  0.046   190 ASN B OD1 
4729 N ND2 . ASN B 190 ? 0.7965 0.6949 0.576  0.0359  0.0312  0.0525  190 ASN B ND2 
4730 N N   . SER B 191 ? 0.4633 0.3794 0.3062 0.0098  0.0368  0.0282  191 SER B N   
4731 C CA  . SER B 191 ? 0.4518 0.3673 0.3157 0.0052  0.0353  0.0263  191 SER B CA  
4732 C C   . SER B 191 ? 0.4327 0.3577 0.3052 0.0048  0.0266  0.0208  191 SER B C   
4733 O O   . SER B 191 ? 0.417  0.3411 0.299  0.0041  0.0217  0.0217  191 SER B O   
4734 C CB  . SER B 191 ? 0.4368 0.3513 0.3126 0.0002  0.0432  0.0239  191 SER B CB  
4735 O OG  . SER B 191 ? 0.4113 0.3252 0.3062 -0.0035 0.0416  0.0236  191 SER B OG  
4736 N N   . PHE B 192 ? 0.4309 0.3638 0.2997 0.0043  0.0253  0.0146  192 PHE B N   
4737 C CA  . PHE B 192 ? 0.4252 0.3661 0.3003 0.0028  0.0182  0.0088  192 PHE B CA  
4738 C C   . PHE B 192 ? 0.44   0.3861 0.3091 0.0066  0.0105  0.0111  192 PHE B C   
4739 O O   . PHE B 192 ? 0.4213 0.3709 0.2994 0.0049  0.0052  0.0089  192 PHE B O   
4740 C CB  . PHE B 192 ? 0.4277 0.3746 0.2978 0.0006  0.0196  0.0012  192 PHE B CB  
4741 C CG  . PHE B 192 ? 0.4021 0.345  0.2834 -0.0033 0.0256  -0.0033 192 PHE B CG  
4742 C CD1 . PHE B 192 ? 0.3865 0.3232 0.2794 -0.004  0.0311  0       192 PHE B CD1 
4743 C CD2 . PHE B 192 ? 0.4107 0.3568 0.2908 -0.0061 0.026   -0.0116 192 PHE B CD2 
4744 C CE1 . PHE B 192 ? 0.3847 0.3199 0.2892 -0.0061 0.0363  -0.0043 192 PHE B CE1 
4745 C CE2 . PHE B 192 ? 0.4265 0.3677 0.3161 -0.0083 0.0321  -0.0158 192 PHE B CE2 
4746 C CZ  . PHE B 192 ? 0.4069 0.3434 0.309  -0.0075 0.0371  -0.0119 192 PHE B CZ  
4747 N N   . GLU B 193 ? 0.4504 0.3971 0.3041 0.0123  0.0101  0.0156  193 GLU B N   
4748 C CA  . GLU B 193 ? 0.4531 0.4052 0.3019 0.0176  0.0032  0.0181  193 GLU B CA  
4749 C C   . GLU B 193 ? 0.4369 0.3807 0.2957 0.0177  0.0022  0.0222  193 GLU B C   
4750 O O   . GLU B 193 ? 0.4209 0.3706 0.285  0.0184  -0.0036 0.0207  193 GLU B O   
4751 C CB  . GLU B 193 ? 0.4851 0.4376 0.3149 0.0256  0.0031  0.0236  193 GLU B CB  
4752 C CG  . GLU B 193 ? 0.5405 0.5057 0.3587 0.0263  0.0012  0.0187  193 GLU B CG  
4753 C CD  . GLU B 193 ? 0.6413 0.6047 0.4382 0.0342  0.0024  0.0249  193 GLU B CD  
4754 O OE1 . GLU B 193 ? 0.7341 0.6912 0.5245 0.0415  0.0012  0.0327  193 GLU B OE1 
4755 O OE2 . GLU B 193 ? 0.7312 0.6982 0.517  0.0332  0.0048  0.0223  193 GLU B OE2 
4756 N N   . THR B 194 ? 0.4207 0.3513 0.2819 0.0163  0.0083  0.0269  194 THR B N   
4757 C CA  . THR B 194 ? 0.4183 0.3408 0.2885 0.015   0.0076  0.0298  194 THR B CA  
4758 C C   . THR B 194 ? 0.4206 0.3479 0.3071 0.0092  0.0041  0.0245  194 THR B C   
4759 O O   . THR B 194 ? 0.3786 0.3062 0.27   0.0093  -0.0003 0.0245  194 THR B O   
4760 C CB  . THR B 194 ? 0.4503 0.3591 0.3209 0.0127  0.0152  0.0345  194 THR B CB  
4761 O OG1 . THR B 194 ? 0.4492 0.3513 0.3022 0.0182  0.019   0.0401  194 THR B OG1 
4762 C CG2 . THR B 194 ? 0.4781 0.3782 0.3556 0.0112  0.0142  0.037   194 THR B CG2 
4763 N N   . ARG B 195 ? 0.3923 0.3223 0.2865 0.0046  0.0067  0.0203  195 ARG B N   
4764 C CA  . ARG B 195 ? 0.3879 0.3212 0.2956 0.0002  0.0034  0.0159  195 ARG B CA  
4765 C C   . ARG B 195 ? 0.3812 0.3223 0.2873 0.0008  -0.0032 0.0128  195 ARG B C   
4766 O O   . ARG B 195 ? 0.3783 0.3188 0.2923 -0.0014 -0.0068 0.0122  195 ARG B O   
4767 C CB  . ARG B 195 ? 0.3803 0.3153 0.2943 -0.0031 0.007   0.0111  195 ARG B CB  
4768 C CG  . ARG B 195 ? 0.3897 0.3195 0.3105 -0.0046 0.0137  0.013   195 ARG B CG  
4769 C CD  . ARG B 195 ? 0.4087 0.3408 0.3349 -0.0063 0.0176  0.0078  195 ARG B CD  
4770 N NE  . ARG B 195 ? 0.3918 0.3217 0.3262 -0.0074 0.0247  0.0089  195 ARG B NE  
4771 C CZ  . ARG B 195 ? 0.413  0.3433 0.3638 -0.0091 0.0247  0.0087  195 ARG B CZ  
4772 N NH1 . ARG B 195 ? 0.4213 0.3528 0.3807 -0.0099 0.0317  0.0082  195 ARG B NH1 
4773 N NH2 . ARG B 195 ? 0.3895 0.3201 0.3482 -0.0098 0.0178  0.0088  195 ARG B NH2 
4774 N N   . ILE B 196 ? 0.3914 0.3407 0.2873 0.0031  -0.0045 0.0104  196 ILE B N   
4775 C CA  . ILE B 196 ? 0.4222 0.3822 0.3174 0.0026  -0.0101 0.0061  196 ILE B CA  
4776 C C   . ILE B 196 ? 0.401  0.3626 0.2949 0.0068  -0.0141 0.0097  196 ILE B C   
4777 O O   . ILE B 196 ? 0.3641 0.3306 0.2635 0.0045  -0.0178 0.0071  196 ILE B O   
4778 C CB  . ILE B 196 ? 0.4502 0.4207 0.3354 0.0034  -0.0106 0.0018  196 ILE B CB  
4779 C CG1 . ILE B 196 ? 0.4903 0.4587 0.3788 -0.0024 -0.0068 -0.004  196 ILE B CG1 
4780 C CG2 . ILE B 196 ? 0.4887 0.4738 0.3716 0.0042  -0.0166 -0.0017 196 ILE B CG2 
4781 C CD1 . ILE B 196 ? 0.5439 0.5119 0.4424 -0.0085 -0.0085 -0.009  196 ILE B CD1 
4782 N N   . ASN B 197 ? 0.406  0.3619 0.2922 0.0128  -0.0126 0.0156  197 ASN B N   
4783 C CA  . ASN B 197 ? 0.3978 0.3524 0.2825 0.0176  -0.0153 0.019   197 ASN B CA  
4784 C C   . ASN B 197 ? 0.3654 0.3127 0.2609 0.013   -0.0159 0.019   197 ASN B C   
4785 O O   . ASN B 197 ? 0.3814 0.3329 0.2791 0.0138  -0.0194 0.0178  197 ASN B O   
4786 C CB  . ASN B 197 ? 0.4084 0.3541 0.2816 0.025   -0.0125 0.0259  197 ASN B CB  
4787 C CG  . ASN B 197 ? 0.448  0.4038 0.3086 0.0319  -0.0144 0.0266  197 ASN B CG  
4788 O OD1 . ASN B 197 ? 0.4768 0.4487 0.3381 0.033   -0.0195 0.0221  197 ASN B OD1 
4789 N ND2 . ASN B 197 ? 0.4474 0.395  0.2958 0.0363  -0.0104 0.0319  197 ASN B ND2 
4790 N N   . VAL B 198 ? 0.3591 0.2968 0.2609 0.0085  -0.0125 0.0201  198 VAL B N   
4791 C CA  . VAL B 198 ? 0.3557 0.2874 0.2668 0.0043  -0.0138 0.0201  198 VAL B CA  
4792 C C   . VAL B 198 ? 0.3714 0.3101 0.2898 -0.0004 -0.0173 0.0153  198 VAL B C   
4793 O O   . VAL B 198 ? 0.3979 0.3362 0.3195 -0.002  -0.0204 0.0147  198 VAL B O   
4794 C CB  . VAL B 198 ? 0.3809 0.3031 0.298  0.0008  -0.0097 0.0223  198 VAL B CB  
4795 C CG1 . VAL B 198 ? 0.4074 0.3251 0.333  -0.0032 -0.0121 0.0223  198 VAL B CG1 
4796 C CG2 . VAL B 198 ? 0.3792 0.2928 0.2878 0.0042  -0.0048 0.0271  198 VAL B CG2 
4797 N N   . LEU B 199 ? 0.3705 0.3141 0.2902 -0.0027 -0.0164 0.0118  199 LEU B N   
4798 C CA  . LEU B 199 ? 0.3784 0.3264 0.3027 -0.0072 -0.0189 0.0073  199 LEU B CA  
4799 C C   . LEU B 199 ? 0.3753 0.3327 0.2956 -0.0065 -0.0224 0.005   199 LEU B C   
4800 O O   . LEU B 199 ? 0.3571 0.3143 0.2812 -0.0098 -0.0246 0.0037  199 LEU B O   
4801 C CB  . LEU B 199 ? 0.378  0.3276 0.3027 -0.0098 -0.0163 0.0033  199 LEU B CB  
4802 C CG  . LEU B 199 ? 0.3822 0.3237 0.3148 -0.0114 -0.0132 0.0043  199 LEU B CG  
4803 C CD1 . LEU B 199 ? 0.3851 0.3275 0.3156 -0.0119 -0.0088 0.0006  199 LEU B CD1 
4804 C CD2 . LEU B 199 ? 0.3878 0.3249 0.3283 -0.0146 -0.0156 0.004   199 LEU B CD2 
4805 N N   . LEU B 200 ? 0.3659 0.332  0.2788 -0.0018 -0.0229 0.0047  200 LEU B N   
4806 C CA  . LEU B 200 ? 0.361  0.3396 0.2719 -0.0002 -0.0263 0.0022  200 LEU B CA  
4807 C C   . LEU B 200 ? 0.359  0.3339 0.2715 0.0022  -0.0276 0.0051  200 LEU B C   
4808 O O   . LEU B 200 ? 0.3505 0.3325 0.2656 0       -0.0296 0.0021  200 LEU B O   
4809 C CB  . LEU B 200 ? 0.3752 0.3659 0.2782 0.0057  -0.0275 0.0016  200 LEU B CB  
4810 C CG  . LEU B 200 ? 0.4146 0.4159 0.3159 0.0016  -0.0278 -0.0045 200 LEU B CG  
4811 C CD1 . LEU B 200 ? 0.433  0.4454 0.3244 0.0092  -0.0296 -0.0034 200 LEU B CD1 
4812 C CD2 . LEU B 200 ? 0.4479 0.4597 0.3548 -0.0053 -0.0298 -0.011  200 LEU B CD2 
4813 N N   . SER B 201 ? 0.3568 0.3199 0.2671 0.0061  -0.0259 0.0103  201 SER B N   
4814 C CA  . SER B 201 ? 0.3707 0.3276 0.2816 0.0077  -0.0266 0.0124  201 SER B CA  
4815 C C   . SER B 201 ? 0.3796 0.3345 0.297  0.0006  -0.0281 0.01    201 SER B C   
4816 O O   . SER B 201 ? 0.3512 0.309  0.2686 0.0007  -0.0295 0.0087  201 SER B O   
4817 C CB  . SER B 201 ? 0.3966 0.3388 0.3044 0.0105  -0.0236 0.0176  201 SER B CB  
4818 O OG  . SER B 201 ? 0.3857 0.3213 0.2928 0.0118  -0.024  0.0186  201 SER B OG  
4819 N N   . ASN B 202 ? 0.3619 0.3112 0.2843 -0.0047 -0.0274 0.0098  202 ASN B N   
4820 C CA  . ASN B 202 ? 0.378  0.324  0.3052 -0.0106 -0.0291 0.0085  202 ASN B CA  
4821 C C   . ASN B 202 ? 0.367  0.322  0.2938 -0.0141 -0.03   0.0041  202 ASN B C   
4822 O O   . ASN B 202 ? 0.3634 0.3174 0.2905 -0.0174 -0.0313 0.0034  202 ASN B O   
4823 C CB  . ASN B 202 ? 0.3593 0.298  0.2922 -0.0137 -0.0283 0.0096  202 ASN B CB  
4824 C CG  . ASN B 202 ? 0.3729 0.3034 0.3085 -0.0131 -0.0282 0.013   202 ASN B CG  
4825 O OD1 . ASN B 202 ? 0.3596 0.2858 0.2975 -0.0157 -0.0306 0.0138  202 ASN B OD1 
4826 N ND2 . ASN B 202 ? 0.3995 0.3277 0.3343 -0.0104 -0.0251 0.015   202 ASN B ND2 
4827 N N   . ILE B 203 ? 0.3433 0.3069 0.269  -0.0144 -0.0291 0.001   203 ILE B N   
4828 C CA  . ILE B 203 ? 0.3286 0.3014 0.2545 -0.0194 -0.0294 -0.0042 203 ILE B CA  
4829 C C   . ILE B 203 ? 0.379  0.362  0.3037 -0.0177 -0.0307 -0.0054 203 ILE B C   
4830 O O   . ILE B 203 ? 0.3615 0.3468 0.2872 -0.023  -0.0306 -0.0079 203 ILE B O   
4831 C CB  . ILE B 203 ? 0.3348 0.3159 0.2589 -0.0201 -0.0284 -0.0082 203 ILE B CB  
4832 C CG1 . ILE B 203 ? 0.3749 0.3453 0.3008 -0.0234 -0.0261 -0.0084 203 ILE B CG1 
4833 C CG2 . ILE B 203 ? 0.3638 0.3589 0.2879 -0.025  -0.0289 -0.0144 203 ILE B CG2 
4834 C CD1 . ILE B 203 ? 0.3635 0.3388 0.2864 -0.0235 -0.0242 -0.012  203 ILE B CD1 
4835 N N   . TYR B 204 ? 0.3291 0.3174 0.2512 -0.0099 -0.0314 -0.0035 204 TYR B N   
4836 C CA  . TYR B 204 ? 0.3457 0.3442 0.2674 -0.0062 -0.0323 -0.0047 204 TYR B CA  
4837 C C   . TYR B 204 ? 0.353  0.3414 0.2746 -0.007  -0.0319 -0.0026 204 TYR B C   
4838 O O   . TYR B 204 ? 0.3562 0.3522 0.2785 -0.0084 -0.0316 -0.0053 204 TYR B O   
4839 C CB  . TYR B 204 ? 0.3293 0.3356 0.2474 0.0038  -0.0332 -0.0028 204 TYR B CB  
4840 C CG  . TYR B 204 ? 0.3922 0.4157 0.31   0.0043  -0.0347 -0.0067 204 TYR B CG  
4841 C CD1 . TYR B 204 ? 0.4052 0.4455 0.3275 -0.0017 -0.0354 -0.0133 204 TYR B CD1 
4842 C CD2 . TYR B 204 ? 0.4442 0.4671 0.3567 0.0095  -0.035  -0.0043 204 TYR B CD2 
4843 C CE1 . TYR B 204 ? 0.4535 0.5111 0.3756 -0.002  -0.0373 -0.0178 204 TYR B CE1 
4844 C CE2 . TYR B 204 ? 0.4544 0.4932 0.3653 0.0095  -0.0368 -0.0083 204 TYR B CE2 
4845 C CZ  . TYR B 204 ? 0.488  0.5447 0.4039 0.0036  -0.0383 -0.0153 204 TYR B CZ  
4846 O OH  . TYR B 204 ? 0.5222 0.5962 0.4361 0.0039  -0.0407 -0.0197 204 TYR B OH  
4847 N N   . LEU B 205 ? 0.3443 0.3168 0.2648 -0.0066 -0.0317 0.0016  205 LEU B N   
4848 C CA  . LEU B 205 ? 0.3559 0.3185 0.2756 -0.009  -0.0319 0.0029  205 LEU B CA  
4849 C C   . LEU B 205 ? 0.3939 0.3576 0.3148 -0.0169 -0.0322 0.0003  205 LEU B C   
4850 O O   . LEU B 205 ? 0.3535 0.3191 0.2723 -0.0183 -0.0317 -0.0011 205 LEU B O   
4851 C CB  . LEU B 205 ? 0.3733 0.3214 0.2935 -0.0093 -0.0321 0.0067  205 LEU B CB  
4852 C CG  . LEU B 205 ? 0.401  0.339  0.3201 -0.0126 -0.0333 0.0077  205 LEU B CG  
4853 C CD1 . LEU B 205 ? 0.3955 0.3307 0.3098 -0.0081 -0.0322 0.0076  205 LEU B CD1 
4854 C CD2 . LEU B 205 ? 0.4512 0.3795 0.3737 -0.015  -0.0342 0.0104  205 LEU B CD2 
4855 N N   . ASN B 206 ? 0.3607 0.3227 0.2838 -0.0218 -0.0322 -0.0003 206 ASN B N   
4856 C CA  . ASN B 206 ? 0.3826 0.3412 0.3051 -0.0293 -0.0319 -0.0016 206 ASN B CA  
4857 C C   . ASN B 206 ? 0.4171 0.3885 0.3392 -0.0331 -0.03   -0.0064 206 ASN B C   
4858 O O   . ASN B 206 ? 0.43   0.3985 0.3497 -0.0393 -0.0287 -0.0073 206 ASN B O   
4859 C CB  . ASN B 206 ? 0.3702 0.3201 0.2949 -0.0322 -0.0319 -0.0003 206 ASN B CB  
4860 C CG  . ASN B 206 ? 0.3838 0.3231 0.3107 -0.0295 -0.0338 0.0041  206 ASN B CG  
4861 O OD1 . ASN B 206 ? 0.4169 0.3523 0.3476 -0.0287 -0.0334 0.0052  206 ASN B OD1 
4862 N ND2 . ASN B 206 ? 0.3963 0.332  0.3213 -0.028  -0.0354 0.0061  206 ASN B ND2 
4863 N N   . GLU B 207 ? 0.3667 0.3531 0.291  -0.0296 -0.0297 -0.0095 207 GLU B N   
4864 C CA  . GLU B 207 ? 0.3792 0.3827 0.3053 -0.0322 -0.0283 -0.0148 207 GLU B CA  
4865 C C   . GLU B 207 ? 0.3777 0.3883 0.3034 -0.0271 -0.028  -0.0149 207 GLU B C   
4866 O O   . GLU B 207 ? 0.3855 0.4125 0.314  -0.0284 -0.0266 -0.0194 207 GLU B O   
4867 C CB  . GLU B 207 ? 0.3968 0.4156 0.3256 -0.0303 -0.029  -0.0185 207 GLU B CB  
4868 C CG  . GLU B 207 ? 0.4323 0.4476 0.3613 -0.0382 -0.0278 -0.0214 207 GLU B CG  
4869 C CD  . GLU B 207 ? 0.5151 0.5348 0.4449 -0.0485 -0.0249 -0.0263 207 GLU B CD  
4870 O OE1 . GLU B 207 ? 0.6115 0.6511 0.5448 -0.051  -0.0244 -0.0321 207 GLU B OE1 
4871 O OE2 . GLU B 207 ? 0.5873 0.5909 0.514  -0.0536 -0.0232 -0.0238 207 GLU B OE2 
4872 N N   . ASN B 208 ? 0.3711 0.3698 0.2935 -0.0219 -0.0288 -0.0107 208 ASN B N   
4873 C CA  . ASN B 208 ? 0.4027 0.4058 0.3238 -0.0163 -0.0278 -0.0112 208 ASN B CA  
4874 C C   . ASN B 208 ? 0.4396 0.4595 0.3638 -0.0071 -0.0282 -0.0128 208 ASN B C   
4875 O O   . ASN B 208 ? 0.4351 0.4666 0.3609 -0.0031 -0.0267 -0.0154 208 ASN B O   
4876 C CB  . ASN B 208 ? 0.4315 0.4376 0.3513 -0.0229 -0.0251 -0.0142 208 ASN B CB  
4877 C CG  . ASN B 208 ? 0.4588 0.4632 0.3754 -0.0176 -0.0235 -0.0142 208 ASN B CG  
4878 O OD1 . ASN B 208 ? 0.6002 0.6141 0.5171 -0.0195 -0.0205 -0.0178 208 ASN B OD1 
4879 N ND2 . ASN B 208 ? 0.4676 0.4585 0.3805 -0.0119 -0.0249 -0.0106 208 ASN B ND2 
4880 N N   . ASN B 209 ? 0.4071 0.4286 0.3317 -0.003  -0.0301 -0.0111 209 ASN B N   
4881 C CA  . ASN B 209 ? 0.3699 0.4039 0.2949 0.0077  -0.0314 -0.0108 209 ASN B CA  
4882 C C   . ASN B 209 ? 0.4055 0.4221 0.3246 0.0157  -0.0313 -0.0048 209 ASN B C   
4883 O O   . ASN B 209 ? 0.3905 0.4    0.307  0.0172  -0.0321 -0.0016 209 ASN B O   
4884 C CB  . ASN B 209 ? 0.3984 0.447  0.3257 0.007   -0.0335 -0.0132 209 ASN B CB  
4885 C CG  . ASN B 209 ? 0.5416 0.6067 0.469  0.019   -0.0355 -0.013  209 ASN B CG  
4886 O OD1 . ASN B 209 ? 0.4858 0.5454 0.4097 0.0295  -0.0351 -0.0091 209 ASN B OD1 
4887 N ND2 . ASN B 209 ? 0.6149 0.7012 0.5461 0.0175  -0.0377 -0.0176 209 ASN B ND2 
4888 N N   . LEU B 210 ? 0.3663 0.375  0.2827 0.02    -0.0296 -0.0037 210 LEU B N   
4889 C CA  . LEU B 210 ? 0.4292 0.4169 0.3396 0.0239  -0.0285 0.0012  210 LEU B CA  
4890 C C   . LEU B 210 ? 0.4433 0.4305 0.3493 0.0355  -0.0285 0.0051  210 LEU B C   
4891 O O   . LEU B 210 ? 0.4153 0.3866 0.3166 0.0365  -0.0276 0.0095  210 LEU B O   
4892 C CB  . LEU B 210 ? 0.4242 0.4024 0.3319 0.0236  -0.0263 0.0002  210 LEU B CB  
4893 C CG  . LEU B 210 ? 0.4494 0.4266 0.3588 0.0124  -0.0264 -0.0027 210 LEU B CG  
4894 C CD1 . LEU B 210 ? 0.4789 0.4458 0.3834 0.0122  -0.0242 -0.0038 210 LEU B CD1 
4895 C CD2 . LEU B 210 ? 0.4818 0.4497 0.3922 0.0041  -0.0283 -0.0007 210 LEU B CD2 
4896 N N   . GLU B 211 ? 0.4067 0.412  0.3143 0.0438  -0.0295 0.0035  211 GLU B N   
4897 C CA  . GLU B 211 ? 0.465  0.4707 0.367  0.0564  -0.0301 0.0079  211 GLU B CA  
4898 C C   . GLU B 211 ? 0.4556 0.462  0.3554 0.0542  -0.032  0.0101  211 GLU B C   
4899 O O   . GLU B 211 ? 0.4724 0.4645 0.3643 0.0597  -0.0307 0.0158  211 GLU B O   
4900 C CB  . GLU B 211 ? 0.5425 0.5696 0.4474 0.0672  -0.0315 0.0058  211 GLU B CB  
4901 C CG  . GLU B 211 ? 0.6492 0.6752 0.5558 0.071   -0.0285 0.0033  211 GLU B CG  
4902 C CD  . GLU B 211 ? 0.8116 0.8501 0.7266 0.0602  -0.0277 -0.0035 211 GLU B CD  
4903 O OE1 . GLU B 211 ? 0.7529 0.7944 0.6716 0.0473  -0.0288 -0.006  211 GLU B OE1 
4904 O OE2 . GLU B 211 ? 0.9089 0.9542 0.8263 0.0654  -0.0254 -0.0063 211 GLU B OE2 
4905 N N   . LEU B 212 ? 0.4153 0.4367 0.321  0.0457  -0.0343 0.0056  212 LEU B N   
4906 C CA  . LEU B 212 ? 0.4222 0.4439 0.3257 0.0425  -0.0354 0.0065  212 LEU B CA  
4907 C C   . LEU B 212 ? 0.3902 0.3899 0.2917 0.0358  -0.0328 0.0096  212 LEU B C   
4908 O O   . LEU B 212 ? 0.3944 0.3871 0.2905 0.0378  -0.032  0.0132  212 LEU B O   
4909 C CB  . LEU B 212 ? 0.518  0.559  0.4276 0.0343  -0.0377 0       212 LEU B CB  
4910 C CG  . LEU B 212 ? 0.6551 0.7229 0.5668 0.0401  -0.0413 -0.0036 212 LEU B CG  
4911 C CD1 . LEU B 212 ? 0.6457 0.7293 0.5632 0.0287  -0.0426 -0.011  212 LEU B CD1 
4912 C CD2 . LEU B 212 ? 0.627  0.696  0.5296 0.0518  -0.0433 0.0015  212 LEU B CD2 
4913 N N   . CYS B 213 ? 0.3677 0.3575 0.2732 0.0282  -0.0315 0.0084  213 CYS B N   
4914 C CA  . CYS B 213 ? 0.3644 0.3351 0.2694 0.0229  -0.0296 0.0113  213 CYS B CA  
4915 C C   . CYS B 213 ? 0.3791 0.3349 0.2768 0.03    -0.0271 0.0169  213 CYS B C   
4916 O O   . CYS B 213 ? 0.4129 0.3602 0.3086 0.0285  -0.0253 0.0198  213 CYS B O   
4917 C CB  . CYS B 213 ? 0.3694 0.333  0.278  0.0161  -0.0294 0.0095  213 CYS B CB  
4918 S SG  . CYS B 213 ? 0.4104 0.3525 0.3186 0.0117  -0.0278 0.013   213 CYS B SG  
4919 N N   . ARG B 214 ? 0.3623 0.3139 0.2558 0.0374  -0.0261 0.0183  214 ARG B N   
4920 C CA  . ARG B 214 ? 0.4058 0.3396 0.2909 0.0438  -0.0227 0.0237  214 ARG B CA  
4921 C C   . ARG B 214 ? 0.4172 0.3535 0.2948 0.0518  -0.0224 0.028   214 ARG B C   
4922 O O   . ARG B 214 ? 0.402  0.3227 0.2732 0.0524  -0.019  0.0327  214 ARG B O   
4923 C CB  . ARG B 214 ? 0.4395 0.3673 0.3211 0.0505  -0.0212 0.0236  214 ARG B CB  
4924 C CG  . ARG B 214 ? 0.4677 0.3878 0.3537 0.0411  -0.0208 0.0201  214 ARG B CG  
4925 C CD  . ARG B 214 ? 0.5286 0.4383 0.4096 0.0465  -0.0181 0.0197  214 ARG B CD  
4926 N NE  . ARG B 214 ? 0.5426 0.4707 0.4269 0.0517  -0.0198 0.0161  214 ARG B NE  
4927 C CZ  . ARG B 214 ? 0.5184 0.4525 0.4065 0.0475  -0.02   0.0113  214 ARG B CZ  
4928 N NH1 . ARG B 214 ? 0.5068 0.4519 0.3954 0.0556  -0.0193 0.0091  214 ARG B NH1 
4929 N NH2 . ARG B 214 ? 0.4956 0.4226 0.3854 0.0369  -0.0204 0.0092  214 ARG B NH2 
4930 N N   . GLU B 215 ? 0.4161 0.3726 0.2942 0.0575  -0.0259 0.0262  215 GLU B N   
4931 C CA  . GLU B 215 ? 0.448  0.4091 0.3176 0.0654  -0.0267 0.0301  215 GLU B CA  
4932 C C   . GLU B 215 ? 0.432  0.3878 0.3004 0.0579  -0.0251 0.031   215 GLU B C   
4933 O O   . GLU B 215 ? 0.4149 0.3614 0.2732 0.0626  -0.0227 0.0363  215 GLU B O   
4934 C CB  . GLU B 215 ? 0.4786 0.4666 0.3511 0.0708  -0.0318 0.0264  215 GLU B CB  
4935 C CG  . GLU B 215 ? 0.6757 0.6723 0.5391 0.0783  -0.034  0.0295  215 GLU B CG  
4936 C CD  . GLU B 215 ? 0.7613 0.7883 0.6288 0.0812  -0.04   0.0244  215 GLU B CD  
4937 O OE1 . GLU B 215 ? 0.7185 0.7593 0.5932 0.0849  -0.0421 0.0211  215 GLU B OE1 
4938 O OE2 . GLU B 215 ? 0.8488 0.8863 0.7126 0.0795  -0.0424 0.0231  215 GLU B OE2 
4939 N N   . TYR B 216 ? 0.3856 0.3487 0.2632 0.0471  -0.0263 0.0257  216 TYR B N   
4940 C CA  . TYR B 216 ? 0.4145 0.3738 0.2922 0.0405  -0.0243 0.0256  216 TYR B CA  
4941 C C   . TYR B 216 ? 0.4131 0.3515 0.2906 0.0364  -0.0194 0.0294  216 TYR B C   
4942 O O   . TYR B 216 ? 0.4337 0.3655 0.3064 0.0358  -0.016  0.0322  216 TYR B O   
4943 C CB  . TYR B 216 ? 0.4175 0.3894 0.3044 0.0313  -0.0266 0.0189  216 TYR B CB  
4944 C CG  . TYR B 216 ? 0.4504 0.4426 0.3352 0.0336  -0.0302 0.015   216 TYR B CG  
4945 C CD1 . TYR B 216 ? 0.4718 0.467  0.349  0.0353  -0.0297 0.0157  216 TYR B CD1 
4946 C CD2 . TYR B 216 ? 0.5345 0.5439 0.4246 0.0336  -0.0339 0.0102  216 TYR B CD2 
4947 C CE1 . TYR B 216 ? 0.523  0.538  0.3978 0.0367  -0.0335 0.0114  216 TYR B CE1 
4948 C CE2 . TYR B 216 ? 0.5119 0.5422 0.4014 0.0344  -0.0374 0.0056  216 TYR B CE2 
4949 C CZ  . TYR B 216 ? 0.5663 0.5993 0.4478 0.036   -0.0376 0.0062  216 TYR B CZ  
4950 O OH  . TYR B 216 ? 0.6223 0.6762 0.5019 0.0368  -0.0415 0.0014  216 TYR B OH  
4951 N N   . ALA B 217 ? 0.404  0.3327 0.286  0.0335  -0.0187 0.0293  217 ALA B N   
4952 C CA  . ALA B 217 ? 0.4187 0.3289 0.3006 0.0294  -0.0142 0.0324  217 ALA B CA  
4953 C C   . ALA B 217 ? 0.4289 0.3254 0.2984 0.037   -0.0099 0.0386  217 ALA B C   
4954 O O   . ALA B 217 ? 0.4271 0.3128 0.2937 0.0341  -0.0052 0.0417  217 ALA B O   
4955 C CB  . ALA B 217 ? 0.4144 0.3187 0.3027 0.0244  -0.0151 0.0302  217 ALA B CB  
4956 N N   . GLN B 218 ? 0.4535 0.3501 0.3153 0.0469  -0.0111 0.0407  218 GLN B N   
4957 C CA  . GLN B 218 ? 0.4907 0.3727 0.3385 0.0559  -0.007  0.0475  218 GLN B CA  
4958 C C   . GLN B 218 ? 0.4872 0.3727 0.3264 0.0589  -0.0058 0.0511  218 GLN B C   
4959 O O   . GLN B 218 ? 0.5081 0.3768 0.3367 0.0608  -0.0002 0.0569  218 GLN B O   
4960 C CB  . GLN B 218 ? 0.4953 0.3794 0.3369 0.0681  -0.0091 0.049   218 GLN B CB  
4961 C CG  . GLN B 218 ? 0.582  0.4502 0.4242 0.0676  -0.0064 0.0483  218 GLN B CG  
4962 C CD  . GLN B 218 ? 0.6581 0.4991 0.4907 0.0664  0.0008  0.0536  218 GLN B CD  
4963 O OE1 . GLN B 218 ? 0.7805 0.6102 0.5996 0.075   0.0042  0.0603  218 GLN B OE1 
4964 N NE2 . GLN B 218 ? 0.6529 0.4831 0.492  0.0554  0.0033  0.0507  218 GLN B NE2 
4965 N N   . LYS B 219 ? 0.444  0.3504 0.2868 0.0588  -0.0106 0.0473  219 LYS B N   
4966 C CA  . LYS B 219 ? 0.5243 0.4357 0.3589 0.0604  -0.0098 0.0492  219 LYS B CA  
4967 C C   . LYS B 219 ? 0.5086 0.4087 0.3455 0.0508  -0.0039 0.0497  219 LYS B C   
4968 O O   . LYS B 219 ? 0.4911 0.382  0.3166 0.053   0.0009  0.0546  219 LYS B O   
4969 C CB  . LYS B 219 ? 0.5572 0.4939 0.3969 0.0598  -0.0162 0.043   219 LYS B CB  
4970 C CG  . LYS B 219 ? 0.6962 0.6433 0.5247 0.0648  -0.0178 0.0442  219 LYS B CG  
4971 C CD  . LYS B 219 ? 0.8049 0.7787 0.6378 0.0659  -0.0251 0.0376  219 LYS B CD  
4972 C CE  . LYS B 219 ? 0.9106 0.8959 0.7502 0.0712  -0.0298 0.0356  219 LYS B CE  
4973 N NZ  . LYS B 219 ? 0.9717 0.9844 0.8142 0.0743  -0.0366 0.0303  219 LYS B NZ  
4974 N N   . ALA B 220 ? 0.4406 0.3424 0.2921 0.0407  -0.004  0.0446  220 ALA B N   
4975 C CA  . ALA B 220 ? 0.4663 0.3601 0.3232 0.032   0.0013  0.0444  220 ALA B CA  
4976 C C   . ALA B 220 ? 0.4566 0.3293 0.3074 0.0317  0.0081  0.0501  220 ALA B C   
4977 O O   . ALA B 220 ? 0.463  0.3276 0.3079 0.0299  0.0143  0.0534  220 ALA B O   
4978 C CB  . ALA B 220 ? 0.4292 0.3296 0.3028 0.0232  -0.0014 0.0385  220 ALA B CB  
4979 N N   . ILE B 221 ? 0.455  0.318  0.3052 0.0337  0.0075  0.0513  221 ILE B N   
4980 C CA  . ILE B 221 ? 0.4677 0.3087 0.3116 0.0324  0.0143  0.0558  221 ILE B CA  
4981 C C   . ILE B 221 ? 0.5162 0.3451 0.3414 0.0405  0.0194  0.0634  221 ILE B C   
4982 O O   . ILE B 221 ? 0.5554 0.369  0.3755 0.0361  0.0272  0.067   221 ILE B O   
4983 C CB  . ILE B 221 ? 0.5195 0.3523 0.3649 0.0337  0.0125  0.0547  221 ILE B CB  
4984 C CG1 . ILE B 221 ? 0.4715 0.3113 0.3336 0.0235  0.0092  0.0482  221 ILE B CG1 
4985 C CG2 . ILE B 221 ? 0.5374 0.3443 0.3706 0.0354  0.02    0.0601  221 ILE B CG2 
4986 C CD1 . ILE B 221 ? 0.4898 0.3285 0.3542 0.0249  0.0055  0.0452  221 ILE B CD1 
4987 N N   . SER B 222 ? 0.5228 0.3597 0.3377 0.0521  0.015   0.0658  222 SER B N   
4988 C CA  . SER B 222 ? 0.5592 0.3857 0.3542 0.0619  0.0185  0.0737  222 SER B CA  
4989 C C   . SER B 222 ? 0.5862 0.4155 0.375  0.0588  0.0222  0.0754  222 SER B C   
4990 O O   . SER B 222 ? 0.5788 0.3963 0.3497 0.0653  0.0265  0.0826  222 SER B O   
4991 C CB  . SER B 222 ? 0.5955 0.4341 0.3832 0.0752  0.0116  0.0751  222 SER B CB  
4992 O OG  . SER B 222 ? 0.6846 0.5182 0.4772 0.0781  0.0098  0.0738  222 SER B OG  
4993 N N   . SER B 223 ? 0.5809 0.4259 0.3825 0.0504  0.0206  0.069   223 SER B N   
4994 C CA  . SER B 223 ? 0.6028 0.4524 0.3976 0.0486  0.024   0.0697  223 SER B CA  
4995 C C   . SER B 223 ? 0.5992 0.4469 0.4066 0.0363  0.0301  0.0661  223 SER B C   
4996 O O   . SER B 223 ? 0.6024 0.4587 0.4091 0.0337  0.0319  0.0638  223 SER B O   
4997 C CB  . SER B 223 ? 0.6272 0.5    0.4231 0.0522  0.0161  0.0647  223 SER B CB  
4998 O OG  . SER B 223 ? 0.6184 0.5037 0.4333 0.0461  0.0109  0.0571  223 SER B OG  
4999 N N   . THR B 224 ? 0.5481 0.3875 0.3685 0.0286  0.0327  0.0645  224 THR B N   
5000 C CA  . THR B 224 ? 0.5396 0.3802 0.3742 0.0175  0.0378  0.0608  224 THR B CA  
5001 C C   . THR B 224 ? 0.5715 0.3927 0.4056 0.0117  0.0459  0.0644  224 THR B C   
5002 O O   . THR B 224 ? 0.5672 0.375  0.3951 0.0147  0.0456  0.0674  224 THR B O   
5003 C CB  . THR B 224 ? 0.5464 0.4021 0.4017 0.0121  0.0312  0.0532  224 THR B CB  
5004 O OG1 . THR B 224 ? 0.4985 0.3589 0.3661 0.004   0.0359  0.05    224 THR B OG1 
5005 C CG2 . THR B 224 ? 0.5284 0.3781 0.3922 0.0093  0.0282  0.0521  224 THR B CG2 
5006 N N   . ASP B 225 ? 0.5668 0.3876 0.4089 0.0028  0.0533  0.063   225 ASP B N   
5007 C CA  . ASP B 225 ? 0.6344 0.4423 0.483  -0.0064 0.0604  0.0636  225 ASP B CA  
5008 C C   . ASP B 225 ? 0.5807 0.4037 0.4535 -0.0161 0.0598  0.0566  225 ASP B C   
5009 O O   . ASP B 225 ? 0.587  0.4057 0.4681 -0.0252 0.067   0.0559  225 ASP B O   
5010 C CB  . ASP B 225 ? 0.7756 0.567  0.6098 -0.0087 0.0725  0.0696  225 ASP B CB  
5011 C CG  . ASP B 225 ? 0.9741 0.7517 0.7814 0.002   0.0748  0.0779  225 ASP B CG  
5012 O OD1 . ASP B 225 ? 1.1024 0.8664 0.8983 0.0089  0.0723  0.082   225 ASP B OD1 
5013 O OD2 . ASP B 225 ? 1.048  0.828  0.8454 0.0035  0.0795  0.0802  225 ASP B OD2 
5014 N N   . THR B 226 ? 0.5248 0.3659 0.4093 -0.0142 0.0514  0.0514  226 THR B N   
5015 C CA  . THR B 226 ? 0.4937 0.3491 0.4003 -0.0211 0.0497  0.0454  226 THR B CA  
5016 C C   . THR B 226 ? 0.4484 0.3048 0.3657 -0.024  0.0425  0.0426  226 THR B C   
5017 O O   . THR B 226 ? 0.4362 0.2949 0.3498 -0.0185 0.0347  0.042   226 THR B O   
5018 C CB  . THR B 226 ? 0.4689 0.3396 0.3791 -0.0169 0.0452  0.0418  226 THR B CB  
5019 O OG1 . THR B 226 ? 0.5065 0.3742 0.4046 -0.0151 0.0529  0.0444  226 THR B OG1 
5020 C CG2 . THR B 226 ? 0.4653 0.3503 0.397  -0.0215 0.0431  0.0361  226 THR B CG2 
5021 N N   . GLN B 227 ? 0.4523 0.3093 0.3836 -0.0328 0.0451  0.0403  227 GLN B N   
5022 C CA  . GLN B 227 ? 0.4729 0.3309 0.4136 -0.0368 0.0386  0.0372  227 GLN B CA  
5023 C C   . GLN B 227 ? 0.4344 0.3055 0.3817 -0.0323 0.0281  0.034   227 GLN B C   
5024 O O   . GLN B 227 ? 0.4505 0.3184 0.3941 -0.0304 0.022   0.0335  227 GLN B O   
5025 C CB  . GLN B 227 ? 0.4742 0.3381 0.4326 -0.0472 0.0419  0.0339  227 GLN B CB  
5026 C CG  . GLN B 227 ? 0.4741 0.3403 0.442  -0.0524 0.0349  0.0301  227 GLN B CG  
5027 C CD  . GLN B 227 ? 0.5222 0.3999 0.5103 -0.0625 0.0365  0.0259  227 GLN B CD  
5028 O OE1 . GLN B 227 ? 0.5249 0.415  0.525  -0.0639 0.0404  0.0248  227 GLN B OE1 
5029 N NE2 . GLN B 227 ? 0.4767 0.3525 0.4697 -0.0693 0.033   0.0228  227 GLN B NE2 
5030 N N   . ARG B 228 ? 0.4016 0.2869 0.3596 -0.0315 0.0268  0.0315  228 ARG B N   
5031 C CA  . ARG B 228 ? 0.413  0.3086 0.3769 -0.0282 0.018   0.0287  228 ARG B CA  
5032 C C   . ARG B 228 ? 0.4097 0.3011 0.359  -0.0215 0.0133  0.03    228 ARG B C   
5033 O O   . ARG B 228 ? 0.3738 0.268  0.3254 -0.0209 0.0062  0.0283  228 ARG B O   
5034 C CB  . ARG B 228 ? 0.4057 0.3129 0.3792 -0.0271 0.0196  0.0264  228 ARG B CB  
5035 C CG  . ARG B 228 ? 0.3842 0.2995 0.3622 -0.0236 0.0121  0.0237  228 ARG B CG  
5036 C CD  . ARG B 228 ? 0.3862 0.3002 0.3505 -0.0181 0.0112  0.0239  228 ARG B CD  
5037 N NE  . ARG B 228 ? 0.4169 0.3372 0.3844 -0.016  0.006   0.0208  228 ARG B NE  
5038 C CZ  . ARG B 228 ? 0.4229 0.3489 0.3988 -0.0156 0.0075  0.0181  228 ARG B CZ  
5039 N NH1 . ARG B 228 ? 0.4003 0.3287 0.3823 -0.0165 0.0144  0.0176  228 ARG B NH1 
5040 N NH2 . ARG B 228 ? 0.4306 0.3588 0.4071 -0.0141 0.003   0.0157  228 ARG B NH2 
5041 N N   . PHE B 229 ? 0.4012 0.2877 0.3358 -0.0163 0.017   0.0329  229 PHE B N   
5042 C CA  . PHE B 229 ? 0.4234 0.3098 0.3461 -0.0095 0.0124  0.0337  229 PHE B CA  
5043 C C   . PHE B 229 ? 0.4325 0.3083 0.3478 -0.0079 0.0109  0.0359  229 PHE B C   
5044 O O   . PHE B 229 ? 0.404  0.2831 0.3169 -0.0045 0.0051  0.0346  229 PHE B O   
5045 C CB  . PHE B 229 ? 0.4345 0.3214 0.344  -0.0039 0.0156  0.0358  229 PHE B CB  
5046 C CG  . PHE B 229 ? 0.4246 0.3217 0.3401 -0.0052 0.017   0.0325  229 PHE B CG  
5047 C CD1 . PHE B 229 ? 0.4587 0.3658 0.3836 -0.0062 0.0115  0.0279  229 PHE B CD1 
5048 C CD2 . PHE B 229 ? 0.448  0.3433 0.359  -0.0057 0.0244  0.0338  229 PHE B CD2 
5049 C CE1 . PHE B 229 ? 0.4666 0.3806 0.3965 -0.0071 0.0134  0.0244  229 PHE B CE1 
5050 C CE2 . PHE B 229 ? 0.4549 0.3589 0.3707 -0.0064 0.0263  0.0299  229 PHE B CE2 
5051 C CZ  . PHE B 229 ? 0.4736 0.3863 0.3993 -0.0071 0.0209  0.0251  229 PHE B CZ  
5052 N N   . LEU B 230 ? 0.4257 0.2883 0.3375 -0.011  0.0169  0.0387  230 LEU B N   
5053 C CA  . LEU B 230 ? 0.4189 0.2684 0.3235 -0.0102 0.0167  0.0401  230 LEU B CA  
5054 C C   . LEU B 230 ? 0.4327 0.2872 0.3484 -0.015  0.0104  0.0356  230 LEU B C   
5055 O O   . LEU B 230 ? 0.439  0.2911 0.3495 -0.0113 0.0064  0.0349  230 LEU B O   
5056 C CB  . LEU B 230 ? 0.4513 0.284  0.3502 -0.0142 0.0255  0.0434  230 LEU B CB  
5057 C CG  . LEU B 230 ? 0.4835 0.3071 0.3665 -0.0085 0.0322  0.0493  230 LEU B CG  
5058 C CD1 . LEU B 230 ? 0.4908 0.2979 0.3702 -0.0153 0.0425  0.0522  230 LEU B CD1 
5059 C CD2 . LEU B 230 ? 0.5086 0.3248 0.3751 0.0027  0.0298  0.0531  230 LEU B CD2 
5060 N N   . VAL B 231 ? 0.3971 0.2595 0.3278 -0.0225 0.0096  0.0325  231 VAL B N   
5061 C CA  . VAL B 231 ? 0.4054 0.2734 0.3462 -0.0271 0.0031  0.0286  231 VAL B CA  
5062 C C   . VAL B 231 ? 0.4035 0.2797 0.3426 -0.0221 -0.004  0.0272  231 VAL B C   
5063 O O   . VAL B 231 ? 0.4109 0.2846 0.3471 -0.0221 -0.0081 0.0257  231 VAL B O   
5064 C CB  . VAL B 231 ? 0.4184 0.2968 0.3762 -0.0341 0.0029  0.0262  231 VAL B CB  
5065 C CG1 . VAL B 231 ? 0.4383 0.3282 0.4069 -0.0358 -0.0057 0.0229  231 VAL B CG1 
5066 C CG2 . VAL B 231 ? 0.4636 0.3343 0.4246 -0.0418 0.0088  0.0259  231 VAL B CG2 
5067 N N   . PHE B 232 ? 0.3731 0.2592 0.3146 -0.019  -0.0051 0.0271  232 PHE B N   
5068 C CA  . PHE B 232 ? 0.4068 0.3006 0.3474 -0.0159 -0.011  0.0253  232 PHE B CA  
5069 C C   . PHE B 232 ? 0.3913 0.2823 0.3195 -0.0097 -0.0117 0.0262  232 PHE B C   
5070 O O   . PHE B 232 ? 0.3791 0.2747 0.3067 -0.0089 -0.0163 0.0242  232 PHE B O   
5071 C CB  . PHE B 232 ? 0.3523 0.256  0.299  -0.0153 -0.0113 0.024   232 PHE B CB  
5072 C CG  . PHE B 232 ? 0.3803 0.289  0.3412 -0.02   -0.013  0.0224  232 PHE B CG  
5073 C CD1 . PHE B 232 ? 0.3849 0.2946 0.3513 -0.0232 -0.0185 0.0213  232 PHE B CD1 
5074 C CD2 . PHE B 232 ? 0.4043 0.3173 0.3728 -0.0206 -0.0091 0.0222  232 PHE B CD2 
5075 C CE1 . PHE B 232 ? 0.4609 0.3769 0.4404 -0.0261 -0.0209 0.0203  232 PHE B CE1 
5076 C CE2 . PHE B 232 ? 0.4465 0.3659 0.4292 -0.0233 -0.0109 0.0208  232 PHE B CE2 
5077 C CZ  . PHE B 232 ? 0.4729 0.3942 0.4614 -0.0258 -0.0172 0.0201  232 PHE B CZ  
5078 N N   . SER B 233 ? 0.3771 0.2608 0.2952 -0.0051 -0.0071 0.0294  233 SER B N   
5079 C CA  . SER B 233 ? 0.3829 0.2647 0.2898 0.0023  -0.0079 0.0307  233 SER B CA  
5080 C C   . SER B 233 ? 0.3858 0.2587 0.2905 0.0016  -0.0088 0.0299  233 SER B C   
5081 O O   . SER B 233 ? 0.3891 0.2671 0.2919 0.0047  -0.0124 0.028   233 SER B O   
5082 C CB  . SER B 233 ? 0.4065 0.2822 0.302  0.0086  -0.0031 0.0352  233 SER B CB  
5083 O OG  . SER B 233 ? 0.4175 0.3026 0.3137 0.0091  -0.0024 0.035   233 SER B OG  
5084 N N   . TYR B 234 ? 0.3851 0.2454 0.2904 -0.0033 -0.0054 0.0306  234 TYR B N   
5085 C CA  . TYR B 234 ? 0.4149 0.2653 0.3169 -0.0047 -0.0059 0.0289  234 TYR B CA  
5086 C C   . TYR B 234 ? 0.4025 0.2624 0.3125 -0.0095 -0.0122 0.0245  234 TYR B C   
5087 O O   . TYR B 234 ? 0.3822 0.2396 0.2878 -0.0081 -0.0141 0.0224  234 TYR B O   
5088 C CB  . TYR B 234 ? 0.4071 0.2412 0.3074 -0.0103 -0.0002 0.0298  234 TYR B CB  
5089 C CG  . TYR B 234 ? 0.4144 0.2334 0.3014 -0.0038 0.0065  0.0347  234 TYR B CG  
5090 C CD1 . TYR B 234 ? 0.4156 0.2256 0.2907 0.0051  0.0073  0.0362  234 TYR B CD1 
5091 C CD2 . TYR B 234 ? 0.4176 0.2315 0.303  -0.0055 0.0124  0.0384  234 TYR B CD2 
5092 C CE1 . TYR B 234 ? 0.4372 0.2315 0.2989 0.0121  0.0133  0.0416  234 TYR B CE1 
5093 C CE2 . TYR B 234 ? 0.4491 0.2479 0.3201 0.001   0.0187  0.0439  234 TYR B CE2 
5094 C CZ  . TYR B 234 ? 0.4678 0.2562 0.3267 0.0101  0.0189  0.0458  234 TYR B CZ  
5095 O OH  . TYR B 234 ? 0.4813 0.2533 0.3248 0.0176  0.025   0.0522  234 TYR B OH  
5096 N N   . LEU B 235 ? 0.3623 0.2321 0.2834 -0.015  -0.0151 0.0232  235 LEU B N   
5097 C CA  . LEU B 235 ? 0.3636 0.2416 0.2908 -0.0188 -0.0212 0.0202  235 LEU B CA  
5098 C C   . LEU B 235 ? 0.3598 0.2448 0.2822 -0.0139 -0.0239 0.0193  235 LEU B C   
5099 O O   . LEU B 235 ? 0.3678 0.2527 0.2875 -0.0149 -0.0267 0.017   235 LEU B O   
5100 C CB  . LEU B 235 ? 0.359  0.2464 0.2981 -0.0228 -0.0235 0.0199  235 LEU B CB  
5101 C CG  . LEU B 235 ? 0.3529 0.2465 0.2976 -0.0266 -0.0299 0.0179  235 LEU B CG  
5102 C CD1 . LEU B 235 ? 0.3612 0.2507 0.3084 -0.0327 -0.0319 0.016   235 LEU B CD1 
5103 C CD2 . LEU B 235 ? 0.3529 0.2557 0.3073 -0.0268 -0.0315 0.0184  235 LEU B CD2 
5104 N N   . THR B 236 ? 0.3396 0.2315 0.2609 -0.0092 -0.0228 0.0205  236 THR B N   
5105 C CA  . THR B 236 ? 0.3363 0.2378 0.2551 -0.0059 -0.0252 0.0189  236 THR B CA  
5106 C C   . THR B 236 ? 0.3573 0.2558 0.2677 -0.0002 -0.0241 0.0186  236 THR B C   
5107 O O   . THR B 236 ? 0.3769 0.281  0.2863 -0.0001 -0.0263 0.016   236 THR B O   
5108 C CB  . THR B 236 ? 0.3647 0.2748 0.2844 -0.0033 -0.0243 0.0194  236 THR B CB  
5109 O OG1 . THR B 236 ? 0.3695 0.2803 0.2969 -0.0077 -0.0241 0.0196  236 THR B OG1 
5110 C CG2 . THR B 236 ? 0.373  0.2946 0.2927 -0.0029 -0.027  0.0165  236 THR B CG2 
5111 N N   . ILE B 237 ? 0.375  0.2634 0.2789 0.0046  -0.0202 0.0212  237 ILE B N   
5112 C CA  . ILE B 237 ? 0.4052 0.2886 0.3011 0.0112  -0.0188 0.0211  237 ILE B CA  
5113 C C   . ILE B 237 ? 0.4067 0.2837 0.3024 0.0064  -0.0198 0.0178  237 ILE B C   
5114 O O   . ILE B 237 ? 0.4345 0.3151 0.3271 0.0095  -0.0205 0.0154  237 ILE B O   
5115 C CB  . ILE B 237 ? 0.4234 0.2935 0.3109 0.0176  -0.0139 0.0253  237 ILE B CB  
5116 C CG1 . ILE B 237 ? 0.4391 0.317  0.324  0.0237  -0.0132 0.0287  237 ILE B CG1 
5117 C CG2 . ILE B 237 ? 0.4225 0.2838 0.3015 0.025   -0.0117 0.0251  237 ILE B CG2 
5118 C CD1 . ILE B 237 ? 0.4491 0.3111 0.324  0.029   -0.0078 0.034   237 ILE B CD1 
5119 N N   . GLY B 238 ? 0.4048 0.2729 0.3033 -0.0012 -0.0198 0.0174  238 GLY B N   
5120 C CA  . GLY B 238 ? 0.3922 0.2549 0.2897 -0.0069 -0.0215 0.0138  238 GLY B CA  
5121 C C   . GLY B 238 ? 0.382  0.2567 0.2818 -0.0091 -0.0261 0.0112  238 GLY B C   
5122 O O   . GLY B 238 ? 0.422  0.2954 0.3167 -0.0087 -0.0263 0.0083  238 GLY B O   
5123 N N   . THR B 239 ? 0.3794 0.2649 0.2864 -0.0115 -0.029  0.0121  239 THR B N   
5124 C CA  . THR B 239 ? 0.3997 0.2946 0.3078 -0.0141 -0.0325 0.0103  239 THR B CA  
5125 C C   . THR B 239 ? 0.4351 0.3378 0.3392 -0.0088 -0.0309 0.0087  239 THR B C   
5126 O O   . THR B 239 ? 0.4245 0.3308 0.3261 -0.0112 -0.032  0.0063  239 THR B O   
5127 C CB  . THR B 239 ? 0.3724 0.2744 0.2881 -0.017  -0.0348 0.0118  239 THR B CB  
5128 O OG1 . THR B 239 ? 0.3936 0.2903 0.3143 -0.0211 -0.0361 0.0128  239 THR B OG1 
5129 C CG2 . THR B 239 ? 0.3823 0.2898 0.2982 -0.0207 -0.0379 0.0107  239 THR B CG2 
5130 N N   . SER B 240 ? 0.3906 0.2965 0.2937 -0.0016 -0.0283 0.01    240 SER B N   
5131 C CA  . SER B 240 ? 0.3809 0.2971 0.2819 0.0043  -0.0272 0.0082  240 SER B CA  
5132 C C   . SER B 240 ? 0.4082 0.3192 0.3033 0.0068  -0.0252 0.0058  240 SER B C   
5133 O O   . SER B 240 ? 0.4089 0.3304 0.3038 0.0099  -0.0245 0.0032  240 SER B O   
5134 C CB  . SER B 240 ? 0.3964 0.3177 0.2968 0.0125  -0.0257 0.0105  240 SER B CB  
5135 O OG  . SER B 240 ? 0.3817 0.2916 0.2756 0.0196  -0.0226 0.0125  240 SER B OG  
5136 N N   . TYR B 241 ? 0.4049 0.3002 0.2955 0.0053  -0.024  0.0059  241 TYR B N   
5137 C CA  . TYR B 241 ? 0.4471 0.3349 0.3307 0.0075  -0.0214 0.0029  241 TYR B CA  
5138 C C   . TYR B 241 ? 0.4474 0.3311 0.3286 -0.0015 -0.0235 -0.0002 241 TYR B C   
5139 O O   . TYR B 241 ? 0.4624 0.3388 0.3366 -0.0009 -0.0212 -0.0036 241 TYR B O   
5140 C CB  . TYR B 241 ? 0.4357 0.3058 0.3137 0.0115  -0.0178 0.0045  241 TYR B CB  
5141 C CG  . TYR B 241 ? 0.4348 0.3052 0.3105 0.023   -0.0147 0.0076  241 TYR B CG  
5142 C CD1 . TYR B 241 ? 0.5114 0.3895 0.385  0.0323  -0.0129 0.006   241 TYR B CD1 
5143 C CD2 . TYR B 241 ? 0.4773 0.3413 0.3527 0.0251  -0.0136 0.0123  241 TYR B CD2 
5144 C CE1 . TYR B 241 ? 0.5233 0.4034 0.3947 0.0443  -0.011  0.0093  241 TYR B CE1 
5145 C CE2 . TYR B 241 ? 0.4922 0.3555 0.3632 0.0365  -0.0112 0.016   241 TYR B CE2 
5146 C CZ  . TYR B 241 ? 0.5146 0.3861 0.3836 0.0466  -0.0103 0.0146  241 TYR B CZ  
5147 O OH  . TYR B 241 ? 0.4933 0.365  0.3576 0.0593  -0.0087 0.0186  241 TYR B OH  
5148 N N   . ILE B 242 ? 0.4415 0.3288 0.3273 -0.0091 -0.0278 0.0009  242 ILE B N   
5149 C CA  . ILE B 242 ? 0.5138 0.3961 0.3969 -0.0172 -0.031  -0.0008 242 ILE B CA  
5150 C C   . ILE B 242 ? 0.5287 0.4141 0.4048 -0.0184 -0.0302 -0.0043 242 ILE B C   
5151 O O   . ILE B 242 ? 0.5475 0.4247 0.4165 -0.0227 -0.0309 -0.007  242 ILE B O   
5152 C CB  . ILE B 242 ? 0.5249 0.4122 0.4154 -0.0226 -0.0358 0.0021  242 ILE B CB  
5153 C CG1 . ILE B 242 ? 0.6061 0.4864 0.496  -0.0293 -0.0396 0.0016  242 ILE B CG1 
5154 C CG2 . ILE B 242 ? 0.5381 0.4359 0.4297 -0.0243 -0.0373 0.0025  242 ILE B CG2 
5155 C CD1 . ILE B 242 ? 0.6464 0.5315 0.5451 -0.0327 -0.044  0.0047  242 ILE B CD1 
5156 N N   . PHE B 243 ? 0.5154 0.4127 0.393  -0.0148 -0.0281 -0.005  243 PHE B N   
5157 C CA  . PHE B 243 ? 0.5741 0.4762 0.4459 -0.0164 -0.0261 -0.0084 243 PHE B CA  
5158 C C   . PHE B 243 ? 0.643  0.5453 0.5115 -0.0086 -0.0207 -0.0117 243 PHE B C   
5159 O O   . PHE B 243 ? 0.6917 0.5964 0.5546 -0.0098 -0.0181 -0.0154 243 PHE B O   
5160 C CB  . PHE B 243 ? 0.5308 0.4466 0.4063 -0.0195 -0.0265 -0.0079 243 PHE B CB  
5161 C CG  . PHE B 243 ? 0.5296 0.4421 0.4063 -0.0266 -0.0314 -0.0046 243 PHE B CG  
5162 C CD1 . PHE B 243 ? 0.5205 0.4238 0.3901 -0.0322 -0.0346 -0.0043 243 PHE B CD1 
5163 C CD2 . PHE B 243 ? 0.5955 0.5134 0.4802 -0.0269 -0.0331 -0.0018 243 PHE B CD2 
5164 C CE1 . PHE B 243 ? 0.5172 0.418  0.3883 -0.0368 -0.0396 -0.0008 243 PHE B CE1 
5165 C CE2 . PHE B 243 ? 0.5824 0.496  0.4686 -0.0318 -0.0373 0.0014  243 PHE B CE2 
5166 C CZ  . PHE B 243 ? 0.6254 0.5309 0.5052 -0.0363 -0.0407 0.0022  243 PHE B CZ  
5167 N N   . SER B 244 ? 0.5839 0.483  0.4548 -0.0004 -0.0187 -0.0104 244 SER B N   
5168 C CA  . SER B 244 ? 0.576  0.4778 0.4452 0.0095  -0.0137 -0.0128 244 SER B CA  
5169 C C   . SER B 244 ? 0.6459 0.5285 0.508  0.0146  -0.0105 -0.0132 244 SER B C   
5170 O O   . SER B 244 ? 0.6286 0.509  0.4865 0.0218  -0.0058 -0.0163 244 SER B O   
5171 C CB  . SER B 244 ? 0.589  0.5069 0.4663 0.0171  -0.0137 -0.0108 244 SER B CB  
5172 O OG  . SER B 244 ? 0.6397 0.5533 0.5201 0.0184  -0.0161 -0.0061 244 SER B OG  
5173 N N   . ASP B 245 ? 0.5416 0.4103 0.4029 0.0116  -0.0121 -0.0104 245 ASP B N   
5174 C CA  . ASP B 245 ? 0.5252 0.3742 0.3795 0.0161  -0.008  -0.0106 245 ASP B CA  
5175 C C   . ASP B 245 ? 0.5046 0.3395 0.3575 0.0065  -0.0102 -0.01   245 ASP B C   
5176 O O   . ASP B 245 ? 0.4924 0.3265 0.3505 0.0055  -0.0117 -0.0056 245 ASP B O   
5177 C CB  . ASP B 245 ? 0.5485 0.3975 0.4041 0.0283  -0.0052 -0.0066 245 ASP B CB  
5178 C CG  . ASP B 245 ? 0.6127 0.4392 0.4591 0.0353  0.0006  -0.0063 245 ASP B CG  
5179 O OD1 . ASP B 245 ? 0.6081 0.4158 0.4486 0.0281  0.002   -0.0082 245 ASP B OD1 
5180 O OD2 . ASP B 245 ? 0.6762 0.5042 0.5215 0.0481  0.0035  -0.0039 245 ASP B OD2 
5181 N N   . PHE B 246 ? 0.4821 0.3072 0.3281 -0.0006 -0.0101 -0.0148 246 PHE B N   
5182 C CA  . PHE B 246 ? 0.4858 0.3013 0.3314 -0.0111 -0.0131 -0.0156 246 PHE B CA  
5183 C C   . PHE B 246 ? 0.491  0.2914 0.3365 -0.0093 -0.0095 -0.013  246 PHE B C   
5184 O O   . PHE B 246 ? 0.494  0.2956 0.3461 -0.0151 -0.0122 -0.0104 246 PHE B O   
5185 C CB  . PHE B 246 ? 0.5096 0.3159 0.3455 -0.0181 -0.0131 -0.0221 246 PHE B CB  
5186 C CG  . PHE B 246 ? 0.524  0.3216 0.3599 -0.0292 -0.0164 -0.0239 246 PHE B CG  
5187 C CD1 . PHE B 246 ? 0.5158 0.3254 0.3576 -0.0374 -0.024  -0.0228 246 PHE B CD1 
5188 C CD2 . PHE B 246 ? 0.5748 0.3526 0.4051 -0.0313 -0.0117 -0.0267 246 PHE B CD2 
5189 C CE1 . PHE B 246 ? 0.5261 0.3312 0.3699 -0.0471 -0.0276 -0.0248 246 PHE B CE1 
5190 C CE2 . PHE B 246 ? 0.5865 0.3589 0.4187 -0.0426 -0.0146 -0.0291 246 PHE B CE2 
5191 C CZ  . PHE B 246 ? 0.5884 0.3761 0.4281 -0.0504 -0.023  -0.0283 246 PHE B CZ  
5192 N N   . ASN B 247 ? 0.5188 0.3042 0.3563 -0.0013 -0.0028 -0.0139 247 ASN B N   
5193 C CA  . ASN B 247 ? 0.5483 0.3144 0.3823 -0.0001 0.0021  -0.0116 247 ASN B CA  
5194 C C   . ASN B 247 ? 0.5026 0.2761 0.3441 0.004   0.0012  -0.0042 247 ASN B C   
5195 O O   . ASN B 247 ? 0.501  0.266  0.3445 -0.002  0.0021  -0.0022 247 ASN B O   
5196 C CB  . ASN B 247 ? 0.611  0.3578 0.4335 0.0094  0.0099  -0.0133 247 ASN B CB  
5197 C CG  . ASN B 247 ? 0.7379 0.4674 0.5507 0.0021  0.0127  -0.021  247 ASN B CG  
5198 O OD1 . ASN B 247 ? 0.7413 0.4719 0.5553 -0.011  0.0087  -0.0251 247 ASN B OD1 
5199 N ND2 . ASN B 247 ? 0.8214 0.5339 0.6237 0.011   0.0199  -0.0233 247 ASN B ND2 
5200 N N   . LEU B 248 ? 0.4946 0.2847 0.3404 0.0132  -0.0004 -0.0009 248 LEU B N   
5201 C CA  . LEU B 248 ? 0.4932 0.2899 0.344  0.0175  -0.001  0.0055  248 LEU B CA  
5202 C C   . LEU B 248 ? 0.487  0.2971 0.3483 0.0076  -0.0066 0.0063  248 LEU B C   
5203 O O   . LEU B 248 ? 0.4603 0.2698 0.3252 0.0064  -0.0062 0.0103  248 LEU B O   
5204 C CB  . LEU B 248 ? 0.4883 0.2989 0.3398 0.0304  -0.0011 0.008   248 LEU B CB  
5205 C CG  . LEU B 248 ? 0.541  0.3388 0.383  0.0437  0.0046  0.009   248 LEU B CG  
5206 C CD1 . LEU B 248 ? 0.5098 0.327  0.3551 0.0561  0.003   0.0115  248 LEU B CD1 
5207 C CD2 . LEU B 248 ? 0.6026 0.3755 0.4358 0.046   0.0102  0.0133  248 LEU B CD2 
5208 N N   . SER B 249 ? 0.4672 0.2894 0.3329 0.0012  -0.0116 0.0027  249 SER B N   
5209 C CA  . SER B 249 ? 0.4205 0.2532 0.2954 -0.0076 -0.0169 0.0034  249 SER B CA  
5210 C C   . SER B 249 ? 0.4225 0.2437 0.299  -0.016  -0.0163 0.0031  249 SER B C   
5211 O O   . SER B 249 ? 0.4123 0.2366 0.296  -0.0184 -0.0166 0.0062  249 SER B O   
5212 C CB  . SER B 249 ? 0.4069 0.2504 0.2829 -0.0126 -0.0218 0.0001  249 SER B CB  
5213 O OG  . SER B 249 ? 0.4068 0.2603 0.2916 -0.0187 -0.0269 0.0018  249 SER B OG  
5214 N N   . LYS B 250 ? 0.429  0.2373 0.299  -0.0208 -0.0148 -0.0014 250 LYS B N   
5215 C CA  . LYS B 250 ? 0.4656 0.2642 0.3374 -0.0306 -0.0143 -0.0034 250 LYS B CA  
5216 C C   . LYS B 250 ? 0.4717 0.258  0.3427 -0.0282 -0.0079 0.0005  250 LYS B C   
5217 O O   . LYS B 250 ? 0.4872 0.2745 0.3656 -0.0353 -0.0079 0.0014  250 LYS B O   
5218 C CB  . LYS B 250 ? 0.4681 0.2531 0.3301 -0.0354 -0.0128 -0.0099 250 LYS B CB  
5219 C CG  . LYS B 250 ? 0.5339 0.3064 0.3959 -0.046  -0.011  -0.0134 250 LYS B CG  
5220 C CD  . LYS B 250 ? 0.5887 0.3464 0.4394 -0.0512 -0.0092 -0.0209 250 LYS B CD  
5221 C CE  . LYS B 250 ? 0.6912 0.4235 0.5335 -0.0523 -0.0002 -0.0224 250 LYS B CE  
5222 N NZ  . LYS B 250 ? 0.8258 0.5443 0.6626 -0.0644 0.0013  -0.0303 250 LYS B NZ  
5223 N N   . GLN B 251 ? 0.4974 0.2716 0.3588 -0.0183 -0.002  0.0028  251 GLN B N   
5224 C CA  . GLN B 251 ? 0.5075 0.2667 0.3647 -0.0151 0.0048  0.0074  251 GLN B CA  
5225 C C   . GLN B 251 ? 0.4685 0.2409 0.3349 -0.015  0.0032  0.0125  251 GLN B C   
5226 O O   . GLN B 251 ? 0.4802 0.2449 0.3486 -0.0206 0.007   0.0143  251 GLN B O   
5227 C CB  . GLN B 251 ? 0.5526 0.2993 0.3979 -0.0017 0.0101  0.0101  251 GLN B CB  
5228 C CG  . GLN B 251 ? 0.7087 0.4347 0.5458 0.0018  0.0179  0.0154  251 GLN B CG  
5229 C CD  . GLN B 251 ? 0.7141 0.4289 0.5392 0.0177  0.0225  0.0199  251 GLN B CD  
5230 O OE1 . GLN B 251 ? 0.6948 0.4167 0.518  0.0265  0.0206  0.0181  251 GLN B OE1 
5231 N NE2 . GLN B 251 ? 0.6456 0.3439 0.4627 0.0219  0.0287  0.0262  251 GLN B NE2 
5232 N N   . ASN B 252 ? 0.4604 0.2512 0.3312 -0.0085 -0.0013 0.0146  252 ASN B N   
5233 C CA  . ASN B 252 ? 0.449  0.2525 0.3274 -0.0078 -0.0027 0.0186  252 ASN B CA  
5234 C C   . ASN B 252 ? 0.446  0.2585 0.3368 -0.0189 -0.0061 0.0168  252 ASN B C   
5235 O O   . ASN B 252 ? 0.4083 0.2228 0.3041 -0.021  -0.0039 0.0196  252 ASN B O   
5236 C CB  . ASN B 252 ? 0.4254 0.2462 0.3055 0.0004  -0.0066 0.0199  252 ASN B CB  
5237 C CG  . ASN B 252 ? 0.47   0.2841 0.3398 0.0126  -0.0027 0.0236  252 ASN B CG  
5238 O OD1 . ASN B 252 ? 0.4557 0.2669 0.3225 0.0166  0.0002  0.0285  252 ASN B OD1 
5239 N ND2 . ASN B 252 ? 0.4629 0.2751 0.327  0.019   -0.0024 0.0216  252 ASN B ND2 
5240 N N   . TYR B 253 ? 0.4133 0.2319 0.3085 -0.0255 -0.0114 0.0121  253 TYR B N   
5241 C CA  . TYR B 253 ? 0.427  0.2545 0.334  -0.035  -0.0152 0.0104  253 TYR B CA  
5242 C C   . TYR B 253 ? 0.4281 0.2439 0.3366 -0.0431 -0.0105 0.0092  253 TYR B C   
5243 O O   . TYR B 253 ? 0.4254 0.2489 0.3447 -0.0482 -0.0105 0.0099  253 TYR B O   
5244 C CB  . TYR B 253 ? 0.4168 0.2529 0.3262 -0.0395 -0.0224 0.0063  253 TYR B CB  
5245 C CG  . TYR B 253 ? 0.3906 0.2404 0.3015 -0.0349 -0.0274 0.0074  253 TYR B CG  
5246 C CD1 . TYR B 253 ? 0.3912 0.2513 0.3079 -0.0306 -0.0277 0.0109  253 TYR B CD1 
5247 C CD2 . TYR B 253 ? 0.4072 0.2587 0.3125 -0.0354 -0.031  0.0045  253 TYR B CD2 
5248 C CE1 . TYR B 253 ? 0.4017 0.2722 0.3188 -0.0275 -0.0313 0.0113  253 TYR B CE1 
5249 C CE2 . TYR B 253 ? 0.425  0.2874 0.3307 -0.0323 -0.0344 0.0054  253 TYR B CE2 
5250 C CZ  . TYR B 253 ? 0.3986 0.2703 0.3105 -0.0288 -0.0346 0.0087  253 TYR B CZ  
5251 O OH  . TYR B 253 ? 0.4041 0.2853 0.3165 -0.0272 -0.0374 0.0091  253 TYR B OH  
5252 N N   . LEU B 254 ? 0.4429 0.2399 0.3408 -0.0445 -0.0056 0.007   254 LEU B N   
5253 C CA  . LEU B 254 ? 0.4628 0.2467 0.3611 -0.0537 -0.0002 0.0051  254 LEU B CA  
5254 C C   . LEU B 254 ? 0.4939 0.2705 0.3912 -0.051  0.0074  0.0108  254 LEU B C   
5255 O O   . LEU B 254 ? 0.4916 0.2673 0.3961 -0.0601 0.0109  0.0101  254 LEU B O   
5256 C CB  . LEU B 254 ? 0.5126 0.2757 0.3986 -0.0564 0.0037  0.0007  254 LEU B CB  
5257 C CG  . LEU B 254 ? 0.565  0.334  0.4512 -0.0622 -0.003  -0.0061 254 LEU B CG  
5258 C CD1 . LEU B 254 ? 0.6087 0.3547 0.4806 -0.0639 0.0022  -0.0109 254 LEU B CD1 
5259 C CD2 . LEU B 254 ? 0.5892 0.3742 0.4896 -0.074  -0.0093 -0.0098 254 LEU B CD2 
5260 N N   . ILE B 255 ? 0.479  0.2505 0.3667 -0.0389 0.0102  0.016   255 ILE B N   
5261 C CA  . ILE B 255 ? 0.4891 0.2557 0.3738 -0.0348 0.0164  0.0222  255 ILE B CA  
5262 C C   . ILE B 255 ? 0.4401 0.227  0.3398 -0.039  0.0133  0.0228  255 ILE B C   
5263 O O   . ILE B 255 ? 0.4656 0.2505 0.3698 -0.0449 0.0185  0.0241  255 ILE B O   
5264 C CB  . ILE B 255 ? 0.5135 0.2768 0.3864 -0.0202 0.0174  0.0275  255 ILE B CB  
5265 C CG1 . ILE B 255 ? 0.5234 0.2641 0.3809 -0.0143 0.0222  0.0279  255 ILE B CG1 
5266 C CG2 . ILE B 255 ? 0.4846 0.248  0.3547 -0.0158 0.0219  0.0339  255 ILE B CG2 
5267 C CD1 . ILE B 255 ? 0.5277 0.2718 0.3768 0.0011  0.0204  0.0312  255 ILE B CD1 
5268 N N   . GLY B 256 ? 0.4436 0.2493 0.3502 -0.0353 0.0058  0.022   256 GLY B N   
5269 C CA  . GLY B 256 ? 0.4454 0.2688 0.365  -0.0373 0.0032  0.0226  256 GLY B CA  
5270 C C   . GLY B 256 ? 0.4648 0.2941 0.3982 -0.0488 0.0028  0.0191  256 GLY B C   
5271 O O   . GLY B 256 ? 0.4493 0.2859 0.3918 -0.0515 0.0058  0.0204  256 GLY B O   
5272 N N   . LEU B 257 ? 0.4456 0.2739 0.3812 -0.0554 -0.0012 0.0142  257 LEU B N   
5273 C CA  . LEU B 257 ? 0.4669 0.3023 0.4156 -0.0667 -0.0024 0.0101  257 LEU B CA  
5274 C C   . LEU B 257 ? 0.4826 0.3066 0.4314 -0.0736 0.0073  0.0106  257 LEU B C   
5275 O O   . LEU B 257 ? 0.4899 0.3255 0.4529 -0.0801 0.0086  0.0095  257 LEU B O   
5276 C CB  . LEU B 257 ? 0.4849 0.3186 0.4311 -0.0718 -0.0082 0.0046  257 LEU B CB  
5277 C CG  . LEU B 257 ? 0.5495 0.3935 0.5089 -0.0837 -0.0119 -0.0008 257 LEU B CG  
5278 C CD1 . LEU B 257 ? 0.4959 0.3635 0.4729 -0.0833 -0.0177 0       257 LEU B CD1 
5279 C CD2 . LEU B 257 ? 0.576  0.4172 0.5286 -0.087  -0.0182 -0.006  257 LEU B CD2 
5280 N N   . LYS B 258 ? 0.476  0.2773 0.409  -0.0712 0.0149  0.0129  258 LYS B N   
5281 C CA  . LYS B 258 ? 0.4902 0.2772 0.4202 -0.0772 0.0254  0.0146  258 LYS B CA  
5282 C C   . LYS B 258 ? 0.481  0.2756 0.4147 -0.073  0.0297  0.0199  258 LYS B C   
5283 O O   . LYS B 258 ? 0.5141 0.3107 0.4561 -0.0814 0.0358  0.0193  258 LYS B O   
5284 C CB  . LYS B 258 ? 0.5312 0.2889 0.4411 -0.0742 0.0332  0.0169  258 LYS B CB  
5285 C CG  . LYS B 258 ? 0.5906 0.3346 0.4939 -0.0794 0.0323  0.0112  258 LYS B CG  
5286 C CD  . LYS B 258 ? 0.628  0.3751 0.543  -0.0961 0.0335  0.0044  258 LYS B CD  
5287 C CE  . LYS B 258 ? 0.7289 0.4624 0.6364 -0.1023 0.0326  -0.0023 258 LYS B CE  
5288 N NZ  . LYS B 258 ? 0.7531 0.4977 0.6749 -0.1184 0.0307  -0.0099 258 LYS B NZ  
5289 N N   . PHE B 259 ? 0.4944 0.2945 0.4227 -0.0611 0.0269  0.0243  259 PHE B N   
5290 C CA  . PHE B 259 ? 0.4878 0.2978 0.4202 -0.0576 0.0299  0.028   259 PHE B CA  
5291 C C   . PHE B 259 ? 0.4919 0.3251 0.4454 -0.0632 0.0257  0.0243  259 PHE B C   
5292 O O   . PHE B 259 ? 0.4611 0.3012 0.4216 -0.065  0.0309  0.0256  259 PHE B O   
5293 C CB  . PHE B 259 ? 0.4674 0.2807 0.3902 -0.0446 0.0267  0.0321  259 PHE B CB  
5294 C CG  . PHE B 259 ? 0.4846 0.2774 0.3872 -0.0372 0.033   0.0377  259 PHE B CG  
5295 C CD1 . PHE B 259 ? 0.4835 0.2619 0.3744 -0.0327 0.0319  0.0378  259 PHE B CD1 
5296 C CD2 . PHE B 259 ? 0.5239 0.3103 0.4187 -0.0349 0.0407  0.0429  259 PHE B CD2 
5297 C CE1 . PHE B 259 ? 0.532  0.2909 0.4043 -0.0245 0.0377  0.0435  259 PHE B CE1 
5298 C CE2 . PHE B 259 ? 0.5266 0.2929 0.4013 -0.0273 0.0464  0.049   259 PHE B CE2 
5299 C CZ  . PHE B 259 ? 0.5317 0.2842 0.3956 -0.0216 0.0446  0.0495  259 PHE B CZ  
5300 N N   . ALA B 260 ? 0.445  0.2907 0.4082 -0.065  0.0163  0.02    260 ALA B N   
5301 C CA  . ALA B 260 ? 0.4386 0.3062 0.4215 -0.0685 0.0114  0.017   260 ALA B CA  
5302 C C   . ALA B 260 ? 0.491  0.3643 0.4881 -0.0805 0.0147  0.0131  260 ALA B C   
5303 O O   . ALA B 260 ? 0.5045 0.3973 0.5194 -0.0827 0.0118  0.011   260 ALA B O   
5304 C CB  . ALA B 260 ? 0.4283 0.3059 0.4145 -0.0657 0.0003  0.0147  260 ALA B CB  
5305 N N   . LYS B 261 ? 0.5329 0.3905 0.5233 -0.0885 0.0202  0.0114  261 LYS B N   
5306 C CA  . LYS B 261 ? 0.6171 0.4804 0.6206 -0.1019 0.022   0.006   261 LYS B CA  
5307 C C   . LYS B 261 ? 0.5921 0.4738 0.6144 -0.106  0.0261  0.0054  261 LYS B C   
5308 O O   . LYS B 261 ? 0.5554 0.4314 0.5732 -0.1032 0.0348  0.0095  261 LYS B O   
5309 C CB  . LYS B 261 ? 0.6895 0.5277 0.6797 -0.1095 0.0321  0.0058  261 LYS B CB  
5310 C CG  . LYS B 261 ? 0.7861 0.6272 0.7879 -0.1256 0.0352  -0.0009 261 LYS B CG  
5311 C CD  . LYS B 261 ? 0.8645 0.7141 0.8716 -0.1308 0.0247  -0.0077 261 LYS B CD  
5312 C CE  . LYS B 261 ? 0.9514 0.8065 0.9708 -0.1476 0.0274  -0.0151 261 LYS B CE  
5313 N NZ  . LYS B 261 ? 1.0063 0.8632 1.0242 -0.1525 0.0181  -0.0217 261 LYS B NZ  
5314 N N   . GLY B 262 ? 0.6361 0.5402 0.6789 -0.1122 0.0197  0.0001  262 GLY B N   
5315 C CA  . GLY B 262 ? 0.6454 0.5708 0.7095 -0.1158 0.0227  -0.0016 262 GLY B CA  
5316 C C   . GLY B 262 ? 0.621  0.5629 0.6937 -0.1044 0.0182  0.0012  262 GLY B C   
5317 O O   . GLY B 262 ? 0.6573 0.6141 0.7454 -0.1055 0.0228  0.0005  262 GLY B O   
5318 N N   . ASN B 263 ? 0.595  0.5324 0.6568 -0.0938 0.0109  0.0042  263 ASN B N   
5319 C CA  . ASN B 263 ? 0.5626 0.514  0.632  -0.0839 0.0056  0.0059  263 ASN B CA  
5320 C C   . ASN B 263 ? 0.5768 0.5335 0.6459 -0.0807 -0.0073 0.0047  263 ASN B C   
5321 O O   . ASN B 263 ? 0.4846 0.4276 0.5368 -0.0763 -0.0104 0.0067  263 ASN B O   
5322 C CB  . ASN B 263 ? 0.5385 0.4781 0.5929 -0.0747 0.0104  0.0107  263 ASN B CB  
5323 C CG  . ASN B 263 ? 0.5715 0.5236 0.6332 -0.0657 0.0061  0.0116  263 ASN B CG  
5324 O OD1 . ASN B 263 ? 0.5906 0.5495 0.6557 -0.0617 -0.0036 0.0111  263 ASN B OD1 
5325 N ND2 . ASN B 263 ? 0.5856 0.5386 0.6476 -0.0622 0.0139  0.0132  263 ASN B ND2 
5326 N N   . PRO B 264 ? 0.5747 0.5516 0.6619 -0.0831 -0.0149 0.0014  264 PRO B N   
5327 C CA  . PRO B 264 ? 0.5482 0.5296 0.6335 -0.0807 -0.0271 0.0006  264 PRO B CA  
5328 C C   . PRO B 264 ? 0.4753 0.4508 0.5495 -0.0697 -0.0318 0.0048  264 PRO B C   
5329 O O   . PRO B 264 ? 0.4546 0.4235 0.5176 -0.0687 -0.0385 0.0049  264 PRO B O   
5330 C CB  . PRO B 264 ? 0.5668 0.5739 0.6757 -0.0829 -0.0331 -0.0025 264 PRO B CB  
5331 C CG  . PRO B 264 ? 0.6009 0.6131 0.7213 -0.093  -0.0237 -0.0059 264 PRO B CG  
5332 C CD  . PRO B 264 ? 0.601  0.5984 0.7113 -0.0887 -0.0122 -0.0019 264 PRO B CD  
5333 N N   . GLY B 265 ? 0.4513 0.4296 0.529  -0.0622 -0.0281 0.0075  265 GLY B N   
5334 C CA  . GLY B 265 ? 0.4554 0.427  0.5223 -0.0531 -0.0309 0.0108  265 GLY B CA  
5335 C C   . GLY B 265 ? 0.4516 0.4044 0.4972 -0.0524 -0.0287 0.0124  265 GLY B C   
5336 O O   . GLY B 265 ? 0.4186 0.3664 0.4541 -0.0491 -0.0346 0.0133  265 GLY B O   
5337 N N   . PHE B 266 ? 0.4442 0.3869 0.4829 -0.0551 -0.0199 0.0128  266 PHE B N   
5338 C CA  . PHE B 266 ? 0.454  0.3797 0.4734 -0.0533 -0.0173 0.0145  266 PHE B CA  
5339 C C   . PHE B 266 ? 0.4215 0.3409 0.4344 -0.0579 -0.0221 0.0124  266 PHE B C   
5340 O O   . PHE B 266 ? 0.4555 0.3673 0.4558 -0.0541 -0.0253 0.0132  266 PHE B O   
5341 C CB  . PHE B 266 ? 0.4132 0.3288 0.426  -0.0544 -0.0068 0.0163  266 PHE B CB  
5342 C CG  . PHE B 266 ? 0.4269 0.346  0.4409 -0.0493 -0.0011 0.0183  266 PHE B CG  
5343 C CD1 . PHE B 266 ? 0.439  0.3654 0.4553 -0.0428 -0.0049 0.0187  266 PHE B CD1 
5344 C CD2 . PHE B 266 ? 0.4596 0.3734 0.4717 -0.0518 0.0087  0.0197  266 PHE B CD2 
5345 C CE1 . PHE B 266 ? 0.4527 0.3813 0.4689 -0.0388 0.0008  0.0196  266 PHE B CE1 
5346 C CE2 . PHE B 266 ? 0.4592 0.3761 0.471  -0.0476 0.0143  0.0211  266 PHE B CE2 
5347 C CZ  . PHE B 266 ? 0.4428 0.3673 0.4568 -0.0411 0.0102  0.0207  266 PHE B CZ  
5348 N N   . GLU B 267 ? 0.4078 0.3312 0.4293 -0.0664 -0.0226 0.0091  267 GLU B N   
5349 C CA  . GLU B 267 ? 0.439  0.3551 0.4532 -0.0718 -0.0263 0.006   267 GLU B CA  
5350 C C   . GLU B 267 ? 0.4193 0.341  0.4307 -0.0684 -0.0365 0.0057  267 GLU B C   
5351 O O   . GLU B 267 ? 0.4027 0.3141 0.4007 -0.0684 -0.0385 0.0047  267 GLU B O   
5352 C CB  . GLU B 267 ? 0.4613 0.3834 0.4869 -0.0829 -0.0255 0.0014  267 GLU B CB  
5353 C CG  . GLU B 267 ? 0.4732 0.3848 0.4976 -0.0883 -0.014  0.0015  267 GLU B CG  
5354 C CD  . GLU B 267 ? 0.568  0.4887 0.6068 -0.1009 -0.0127 -0.0038 267 GLU B CD  
5355 O OE1 . GLU B 267 ? 0.6497 0.556  0.6822 -0.1089 -0.0053 -0.0057 267 GLU B OE1 
5356 O OE2 . GLU B 267 ? 0.6951 0.6375 0.7517 -0.103  -0.019  -0.0063 267 GLU B OE2 
5357 N N   . GLU B 268 ? 0.4161 0.3532 0.4393 -0.0651 -0.0422 0.0066  268 GLU B N   
5358 C CA  . GLU B 268 ? 0.4511 0.3929 0.4713 -0.0617 -0.0517 0.0072  268 GLU B CA  
5359 C C   . GLU B 268 ? 0.4259 0.3563 0.4298 -0.0555 -0.0516 0.0098  268 GLU B C   
5360 O O   . GLU B 268 ? 0.3998 0.3284 0.3954 -0.0554 -0.0575 0.0093  268 GLU B O   
5361 C CB  . GLU B 268 ? 0.4385 0.3968 0.4748 -0.0577 -0.0559 0.0088  268 GLU B CB  
5362 C CG  . GLU B 268 ? 0.4432 0.4055 0.4762 -0.0532 -0.0654 0.0107  268 GLU B CG  
5363 C CD  . GLU B 268 ? 0.52   0.4972 0.5688 -0.0481 -0.0693 0.0125  268 GLU B CD  
5364 O OE1 . GLU B 268 ? 0.4915 0.4801 0.547  -0.0486 -0.0779 0.0121  268 GLU B OE1 
5365 O OE2 . GLU B 268 ? 0.4963 0.4739 0.5507 -0.0434 -0.0635 0.0142  268 GLU B OE2 
5366 N N   . PHE B 269 ? 0.3982 0.3229 0.3977 -0.0503 -0.0452 0.0123  269 PHE B N   
5367 C CA  . PHE B 269 ? 0.4025 0.3188 0.388  -0.0453 -0.0447 0.0138  269 PHE B CA  
5368 C C   . PHE B 269 ? 0.407  0.3126 0.3798 -0.0481 -0.0444 0.0117  269 PHE B C   
5369 O O   . PHE B 269 ? 0.3826 0.2856 0.3462 -0.0463 -0.0477 0.0115  269 PHE B O   
5370 C CB  . PHE B 269 ? 0.4046 0.3173 0.3869 -0.0404 -0.0378 0.0159  269 PHE B CB  
5371 C CG  . PHE B 269 ? 0.3871 0.3083 0.3781 -0.0366 -0.038  0.0174  269 PHE B CG  
5372 C CD1 . PHE B 269 ? 0.4307 0.3585 0.4343 -0.0375 -0.0346 0.0174  269 PHE B CD1 
5373 C CD2 . PHE B 269 ? 0.4043 0.3259 0.3907 -0.0324 -0.0406 0.0184  269 PHE B CD2 
5374 C CE1 . PHE B 269 ? 0.3896 0.3242 0.401  -0.0334 -0.0341 0.0182  269 PHE B CE1 
5375 C CE2 . PHE B 269 ? 0.3867 0.3133 0.38   -0.0291 -0.0398 0.0192  269 PHE B CE2 
5376 C CZ  . PHE B 269 ? 0.3586 0.2916 0.3645 -0.0291 -0.0368 0.0191  269 PHE B CZ  
5377 N N   . PHE B 270 ? 0.3658 0.264  0.3375 -0.0523 -0.0395 0.0101  270 PHE B N   
5378 C CA  . PHE B 270 ? 0.3969 0.2821 0.3559 -0.0542 -0.0378 0.0078  270 PHE B CA  
5379 C C   . PHE B 270 ? 0.4218 0.3094 0.3797 -0.06   -0.0446 0.004   270 PHE B C   
5380 O O   . PHE B 270 ? 0.4457 0.3264 0.3917 -0.0591 -0.046  0.0024  270 PHE B O   
5381 C CB  . PHE B 270 ? 0.394  0.2675 0.3507 -0.0574 -0.0297 0.0073  270 PHE B CB  
5382 C CG  . PHE B 270 ? 0.4101 0.2801 0.3639 -0.0506 -0.0234 0.0116  270 PHE B CG  
5383 C CD1 . PHE B 270 ? 0.4056 0.2684 0.347  -0.0429 -0.0215 0.0135  270 PHE B CD1 
5384 C CD2 . PHE B 270 ? 0.4458 0.3221 0.4096 -0.0515 -0.0198 0.0134  270 PHE B CD2 
5385 C CE1 . PHE B 270 ? 0.3995 0.2612 0.3375 -0.0365 -0.0168 0.0173  270 PHE B CE1 
5386 C CE2 . PHE B 270 ? 0.4277 0.3012 0.3869 -0.0453 -0.0144 0.0172  270 PHE B CE2 
5387 C CZ  . PHE B 270 ? 0.4283 0.2949 0.3744 -0.0378 -0.0134 0.0192  270 PHE B CZ  
5388 N N   . LYS B 271 ? 0.4326 0.331  0.4028 -0.0659 -0.0489 0.0021  271 LYS B N   
5389 C CA  . LYS B 271 ? 0.4339 0.3368 0.403  -0.0714 -0.0565 -0.0016 271 LYS B CA  
5390 C C   . LYS B 271 ? 0.3991 0.3055 0.3611 -0.0664 -0.0631 0.0005  271 LYS B C   
5391 O O   . LYS B 271 ? 0.4207 0.3226 0.3717 -0.0687 -0.0665 -0.0021 271 LYS B O   
5392 C CB  . LYS B 271 ? 0.4782 0.3962 0.4641 -0.0775 -0.0607 -0.0036 271 LYS B CB  
5393 C CG  . LYS B 271 ? 0.5384 0.4522 0.53   -0.0856 -0.054  -0.0071 271 LYS B CG  
5394 C CD  . LYS B 271 ? 0.6409 0.5705 0.6464 -0.0944 -0.06   -0.0117 271 LYS B CD  
5395 C CE  . LYS B 271 ? 0.7964 0.7234 0.8095 -0.1039 -0.0526 -0.0155 271 LYS B CE  
5396 N NZ  . LYS B 271 ? 0.8847 0.8175 0.9099 -0.1008 -0.0462 -0.0118 271 LYS B NZ  
5397 N N   . ARG B 272 ? 0.4061 0.3189 0.3731 -0.0599 -0.0639 0.0049  272 ARG B N   
5398 C CA  . ARG B 272 ? 0.4074 0.3216 0.3675 -0.0555 -0.0687 0.0075  272 ARG B CA  
5399 C C   . ARG B 272 ? 0.4152 0.3183 0.3597 -0.0532 -0.0648 0.007   272 ARG B C   
5400 O O   . ARG B 272 ? 0.3869 0.288  0.3213 -0.054  -0.0685 0.0062  272 ARG B O   
5401 C CB  . ARG B 272 ? 0.4266 0.3475 0.3956 -0.0496 -0.0684 0.0118  272 ARG B CB  
5402 C CG  . ARG B 272 ? 0.4421 0.3758 0.4251 -0.0501 -0.0745 0.0126  272 ARG B CG  
5403 C CD  . ARG B 272 ? 0.4206 0.3599 0.4133 -0.044  -0.0736 0.0162  272 ARG B CD  
5404 N NE  . ARG B 272 ? 0.4096 0.3617 0.4146 -0.0429 -0.0807 0.0173  272 ARG B NE  
5405 C CZ  . ARG B 272 ? 0.4015 0.3596 0.4169 -0.037  -0.0808 0.0201  272 ARG B CZ  
5406 N NH1 . ARG B 272 ? 0.4194 0.3732 0.4365 -0.0336 -0.0734 0.021   272 ARG B NH1 
5407 N NH2 . ARG B 272 ? 0.4153 0.3842 0.4397 -0.0342 -0.0882 0.0218  272 ARG B NH2 
5408 N N   . ASN B 273 ? 0.3802 0.2769 0.3227 -0.05   -0.0574 0.0075  273 ASN B N   
5409 C CA  . ASN B 273 ? 0.3945 0.2837 0.3245 -0.0466 -0.0539 0.0069  273 ASN B CA  
5410 C C   . ASN B 273 ? 0.3749 0.2544 0.295  -0.0501 -0.0527 0.0027  273 ASN B C   
5411 O O   . ASN B 273 ? 0.3812 0.2572 0.2906 -0.0485 -0.0524 0.0013  273 ASN B O   
5412 C CB  . ASN B 273 ? 0.3727 0.2602 0.3029 -0.0408 -0.0476 0.009   273 ASN B CB  
5413 C CG  . ASN B 273 ? 0.397  0.2926 0.3322 -0.0373 -0.0488 0.0119  273 ASN B CG  
5414 O OD1 . ASN B 273 ? 0.3896 0.2897 0.3259 -0.0384 -0.0537 0.0128  273 ASN B OD1 
5415 N ND2 . ASN B 273 ? 0.3875 0.284  0.3247 -0.0331 -0.0441 0.0134  273 ASN B ND2 
5416 N N   . LEU B 274 ? 0.3882 0.2632 0.3116 -0.0552 -0.0512 0.0002  274 LEU B N   
5417 C CA  . LEU B 274 ? 0.4123 0.2771 0.3262 -0.0601 -0.0504 -0.0049 274 LEU B CA  
5418 C C   . LEU B 274 ? 0.4442 0.3141 0.3531 -0.0644 -0.0581 -0.0074 274 LEU B C   
5419 O O   . LEU B 274 ? 0.4241 0.2859 0.3204 -0.0656 -0.0572 -0.0111 274 LEU B O   
5420 C CB  . LEU B 274 ? 0.4413 0.3    0.3603 -0.0661 -0.0468 -0.0073 274 LEU B CB  
5421 C CG  . LEU B 274 ? 0.4354 0.2822 0.3517 -0.0614 -0.0376 -0.0051 274 LEU B CG  
5422 C CD1 . LEU B 274 ? 0.4859 0.3302 0.4108 -0.068  -0.0341 -0.0059 274 LEU B CD1 
5423 C CD2 . LEU B 274 ? 0.4256 0.2557 0.3268 -0.0591 -0.0327 -0.008  274 LEU B CD2 
5424 N N   . SER B 275 ? 0.4134 0.2962 0.3315 -0.0663 -0.0654 -0.0055 275 SER B N   
5425 C CA  . SER B 275 ? 0.4353 0.3235 0.3474 -0.0691 -0.0735 -0.0065 275 SER B CA  
5426 C C   . SER B 275 ? 0.4366 0.3207 0.3358 -0.0645 -0.0724 -0.0048 275 SER B C   
5427 O O   . SER B 275 ? 0.436  0.3157 0.3223 -0.0672 -0.074  -0.008  275 SER B O   
5428 C CB  . SER B 275 ? 0.4161 0.3188 0.3402 -0.0687 -0.0811 -0.0029 275 SER B CB  
5429 O OG  . SER B 275 ? 0.4495 0.3591 0.3867 -0.0739 -0.0826 -0.0054 275 SER B OG  
5430 N N   . PHE B 276 ? 0.421  0.3076 0.324  -0.0582 -0.0695 -0.0002 276 PHE B N   
5431 C CA  . PHE B 276 ? 0.4311 0.3159 0.3242 -0.0547 -0.0677 0.0013  276 PHE B CA  
5432 C C   . PHE B 276 ? 0.4478 0.3237 0.3304 -0.0538 -0.0615 -0.0028 276 PHE B C   
5433 O O   . PHE B 276 ? 0.4094 0.2827 0.2803 -0.0547 -0.0615 -0.0046 276 PHE B O   
5434 C CB  . PHE B 276 ? 0.4537 0.3431 0.3539 -0.0494 -0.0653 0.0057  276 PHE B CB  
5435 C CG  . PHE B 276 ? 0.4667 0.3552 0.3572 -0.0474 -0.0631 0.0065  276 PHE B CG  
5436 C CD1 . PHE B 276 ? 0.4911 0.3808 0.3755 -0.049  -0.0675 0.009   276 PHE B CD1 
5437 C CD2 . PHE B 276 ? 0.4563 0.3428 0.343  -0.0442 -0.0565 0.0045  276 PHE B CD2 
5438 C CE1 . PHE B 276 ? 0.5008 0.3892 0.3759 -0.0486 -0.0643 0.0092  276 PHE B CE1 
5439 C CE2 . PHE B 276 ? 0.4987 0.3866 0.3778 -0.0435 -0.0541 0.0042  276 PHE B CE2 
5440 C CZ  . PHE B 276 ? 0.4952 0.3838 0.3686 -0.0464 -0.0576 0.0064  276 PHE B CZ  
5441 N N   . LEU B 277 ? 0.4229 0.2934 0.309  -0.0515 -0.0556 -0.004  277 LEU B N   
5442 C CA  . LEU B 277 ? 0.4333 0.2947 0.31   -0.0486 -0.0493 -0.0073 277 LEU B CA  
5443 C C   . LEU B 277 ? 0.4262 0.2801 0.2915 -0.0539 -0.0505 -0.0128 277 LEU B C   
5444 O O   . LEU B 277 ? 0.466  0.3168 0.3207 -0.0523 -0.0479 -0.0153 277 LEU B O   
5445 C CB  . LEU B 277 ? 0.4339 0.2886 0.3155 -0.0454 -0.0436 -0.0068 277 LEU B CB  
5446 C CG  . LEU B 277 ? 0.4779 0.3211 0.3501 -0.0407 -0.0366 -0.0096 277 LEU B CG  
5447 C CD1 . LEU B 277 ? 0.4759 0.3255 0.3462 -0.0327 -0.0337 -0.008  277 LEU B CD1 
5448 C CD2 . LEU B 277 ? 0.5097 0.3418 0.3839 -0.0392 -0.0315 -0.009  277 LEU B CD2 
5449 N N   . ASN B 278 ? 0.4399 0.2913 0.3074 -0.0607 -0.054  -0.0154 278 ASN B N   
5450 C CA  . ASN B 278 ? 0.4784 0.3228 0.3347 -0.0671 -0.0556 -0.0216 278 ASN B CA  
5451 C C   . ASN B 278 ? 0.4831 0.3336 0.33   -0.069  -0.0613 -0.0216 278 ASN B C   
5452 O O   . ASN B 278 ? 0.4728 0.3166 0.3056 -0.0704 -0.0593 -0.0262 278 ASN B O   
5453 C CB  . ASN B 278 ? 0.493  0.3357 0.3553 -0.075  -0.0582 -0.0249 278 ASN B CB  
5454 C CG  . ASN B 278 ? 0.5321 0.3609 0.3952 -0.0743 -0.0497 -0.027  278 ASN B CG  
5455 O OD1 . ASN B 278 ? 0.5167 0.3314 0.3679 -0.0742 -0.0444 -0.0318 278 ASN B OD1 
5456 N ND2 . ASN B 278 ? 0.4816 0.3126 0.357  -0.073  -0.0476 -0.0231 278 ASN B ND2 
5457 N N   . ASN B 279 ? 0.4833 0.3452 0.3366 -0.0683 -0.0675 -0.0162 279 ASN B N   
5458 C CA  . ASN B 279 ? 0.4817 0.3473 0.3243 -0.0695 -0.0723 -0.0148 279 ASN B CA  
5459 C C   . ASN B 279 ? 0.4794 0.3417 0.3127 -0.0652 -0.0657 -0.0146 279 ASN B C   
5460 O O   . ASN B 279 ? 0.4866 0.3452 0.3052 -0.0675 -0.0652 -0.0177 279 ASN B O   
5461 C CB  . ASN B 279 ? 0.4568 0.3328 0.3075 -0.0686 -0.0797 -0.0085 279 ASN B CB  
5462 C CG  . ASN B 279 ? 0.4506 0.3334 0.3077 -0.0734 -0.0882 -0.0093 279 ASN B CG  
5463 O OD1 . ASN B 279 ? 0.4772 0.3576 0.328  -0.0795 -0.0906 -0.0151 279 ASN B OD1 
5464 N ND2 . ASN B 279 ? 0.4483 0.3406 0.3181 -0.0708 -0.0931 -0.004  279 ASN B ND2 
5465 N N   . PHE B 280 ? 0.4434 0.3081 0.285  -0.0592 -0.0604 -0.0116 280 PHE B N   
5466 C CA  . PHE B 280 ? 0.4713 0.3369 0.3073 -0.0552 -0.0545 -0.0115 280 PHE B CA  
5467 C C   . PHE B 280 ? 0.5034 0.3612 0.3297 -0.0542 -0.0481 -0.0177 280 PHE B C   
5468 O O   . PHE B 280 ? 0.5258 0.3841 0.3423 -0.054  -0.0449 -0.0195 280 PHE B O   
5469 C CB  . PHE B 280 ? 0.5003 0.3723 0.3481 -0.0496 -0.0511 -0.0076 280 PHE B CB  
5470 C CG  . PHE B 280 ? 0.5013 0.3777 0.3449 -0.0467 -0.0456 -0.0081 280 PHE B CG  
5471 C CD1 . PHE B 280 ? 0.5056 0.3863 0.3454 -0.0493 -0.0471 -0.0051 280 PHE B CD1 
5472 C CD2 . PHE B 280 ? 0.5176 0.3939 0.3606 -0.0415 -0.0387 -0.0115 280 PHE B CD2 
5473 C CE1 . PHE B 280 ? 0.5455 0.4311 0.3815 -0.0485 -0.0415 -0.0063 280 PHE B CE1 
5474 C CE2 . PHE B 280 ? 0.5684 0.4522 0.4095 -0.0394 -0.0339 -0.0125 280 PHE B CE2 
5475 C CZ  . PHE B 280 ? 0.5206 0.4093 0.3583 -0.0437 -0.035  -0.0103 280 PHE B CZ  
5476 N N   . TRP B 281 ? 0.4946 0.3439 0.3224 -0.054  -0.0459 -0.0213 281 TRP B N   
5477 C CA  . TRP B 281 ? 0.5026 0.3418 0.3208 -0.052  -0.0392 -0.0274 281 TRP B CA  
5478 C C   . TRP B 281 ? 0.5236 0.3546 0.3288 -0.0596 -0.0418 -0.0333 281 TRP B C   
5479 O O   . TRP B 281 ? 0.5305 0.3501 0.3273 -0.0591 -0.0364 -0.0393 281 TRP B O   
5480 C CB  . TRP B 281 ? 0.5219 0.3533 0.3468 -0.0468 -0.034  -0.0276 281 TRP B CB  
5481 C CG  . TRP B 281 ? 0.5084 0.3478 0.3421 -0.0381 -0.0304 -0.0232 281 TRP B CG  
5482 C CD1 . TRP B 281 ? 0.5496 0.3989 0.395  -0.0364 -0.0332 -0.0174 281 TRP B CD1 
5483 C CD2 . TRP B 281 ? 0.514  0.3534 0.3453 -0.0294 -0.0232 -0.0248 281 TRP B CD2 
5484 N NE1 . TRP B 281 ? 0.5031 0.3589 0.3527 -0.0284 -0.0288 -0.0157 281 TRP B NE1 
5485 C CE2 . TRP B 281 ? 0.4981 0.3489 0.3399 -0.0236 -0.023  -0.0199 281 TRP B CE2 
5486 C CE3 . TRP B 281 ? 0.5582 0.3893 0.3798 -0.0257 -0.017  -0.0302 281 TRP B CE3 
5487 C CZ2 . TRP B 281 ? 0.5404 0.3971 0.3839 -0.0143 -0.0177 -0.0201 281 TRP B CZ2 
5488 C CZ3 . TRP B 281 ? 0.6019 0.4381 0.4259 -0.0154 -0.0111 -0.0301 281 TRP B CZ3 
5489 C CH2 . TRP B 281 ? 0.5564 0.4063 0.3916 -0.0099 -0.0119 -0.0251 281 TRP B CH2 
5490 N N   . ASN B 282 ? 0.5497 0.3861 0.353  -0.0664 -0.0503 -0.0318 282 ASN B N   
5491 C CA  . ASN B 282 ? 0.5761 0.4076 0.3658 -0.074  -0.0544 -0.0374 282 ASN B CA  
5492 C C   . ASN B 282 ? 0.6083 0.4287 0.3979 -0.0784 -0.0528 -0.0439 282 ASN B C   
5493 O O   . ASN B 282 ? 0.6024 0.4121 0.3788 -0.0813 -0.0493 -0.0512 282 ASN B O   
5494 C CB  . ASN B 282 ? 0.5985 0.4274 0.3717 -0.0736 -0.0501 -0.0406 282 ASN B CB  
5495 C CG  . ASN B 282 ? 0.6842 0.5105 0.4414 -0.0817 -0.0558 -0.0451 282 ASN B CG  
5496 O OD1 . ASN B 282 ? 0.6446 0.4767 0.4037 -0.0868 -0.0654 -0.043  282 ASN B OD1 
5497 N ND2 . ASN B 282 ? 0.6922 0.5095 0.4339 -0.0829 -0.05   -0.0522 282 ASN B ND2 
5498 N N   . LYS B 283 ? 0.5686 0.3908 0.3722 -0.0796 -0.0551 -0.0417 283 LYS B N   
5499 C CA  . LYS B 283 ? 0.6038 0.4157 0.4078 -0.0858 -0.0537 -0.0477 283 LYS B CA  
5500 C C   . LYS B 283 ? 0.5775 0.4004 0.3889 -0.0941 -0.0639 -0.0476 283 LYS B C   
5501 O O   . LYS B 283 ? 0.566  0.4031 0.3865 -0.092  -0.0702 -0.0409 283 LYS B O   
5502 C CB  . LYS B 283 ? 0.6203 0.4247 0.435  -0.0814 -0.0469 -0.0456 283 LYS B CB  
5503 C CG  . LYS B 283 ? 0.6353 0.436  0.4503 -0.0704 -0.0391 -0.0421 283 LYS B CG  
5504 C CD  . LYS B 283 ? 0.7078 0.4935 0.509  -0.0667 -0.0308 -0.048  283 LYS B CD  
5505 C CE  . LYS B 283 ? 0.723  0.5062 0.5297 -0.055  -0.0236 -0.0435 283 LYS B CE  
5506 N NZ  . LYS B 283 ? 0.8016 0.5671 0.5974 -0.0504 -0.0148 -0.0489 283 LYS B NZ  
5507 N N   . GLU B 284 ? 0.6004 0.4166 0.4091 -0.1031 -0.0647 -0.055  284 GLU B N   
5508 C CA  . GLU B 284 ? 0.6443 0.473  0.4625 -0.1117 -0.074  -0.0561 284 GLU B CA  
5509 C C   . GLU B 284 ? 0.6246 0.4606 0.4633 -0.109  -0.0733 -0.0501 284 GLU B C   
5510 O O   . GLU B 284 ? 0.5637 0.3883 0.4062 -0.1062 -0.0645 -0.0497 284 GLU B O   
5511 C CB  . GLU B 284 ? 0.6698 0.4913 0.4803 -0.1236 -0.0752 -0.0667 284 GLU B CB  
5512 C CG  . GLU B 284 ? 0.6869 0.5275 0.5068 -0.1323 -0.0873 -0.0681 284 GLU B CG  
5513 C CD  . GLU B 284 ? 0.726  0.5818 0.5382 -0.1321 -0.0991 -0.0658 284 GLU B CD  
5514 O OE1 . GLU B 284 ? 0.668  0.5162 0.4626 -0.1284 -0.0969 -0.0658 284 GLU B OE1 
5515 O OE2 . GLU B 284 ? 0.6621 0.5371 0.485  -0.1352 -0.1099 -0.064  284 GLU B OE2 
5516 N N   . ASN B 285 ? 0.5559 0.4106 0.4063 -0.1085 -0.0823 -0.0449 285 ASN B N   
5517 C CA  . ASN B 285 ? 0.5191 0.3824 0.388  -0.1041 -0.0815 -0.0383 285 ASN B CA  
5518 C C   . ASN B 285 ? 0.5381 0.4088 0.4208 -0.113  -0.0842 -0.0421 285 ASN B C   
5519 O O   . ASN B 285 ? 0.6142 0.4934 0.496  -0.1211 -0.092  -0.0472 285 ASN B O   
5520 C CB  . ASN B 285 ? 0.5325 0.4106 0.4066 -0.0978 -0.0886 -0.0306 285 ASN B CB  
5521 C CG  . ASN B 285 ? 0.4934 0.3726 0.3784 -0.0895 -0.0835 -0.0236 285 ASN B CG  
5522 O OD1 . ASN B 285 ? 0.4658 0.344  0.3623 -0.0899 -0.0788 -0.0234 285 ASN B OD1 
5523 N ND2 . ASN B 285 ? 0.5241 0.4048 0.4042 -0.0824 -0.0838 -0.0183 285 ASN B ND2 
5524 N N   . GLU B 286 ? 0.5155 0.3825 0.41   -0.1123 -0.0772 -0.0403 286 GLU B N   
5525 C CA  . GLU B 286 ? 0.516  0.3924 0.4263 -0.1208 -0.0788 -0.0432 286 GLU B CA  
5526 C C   . GLU B 286 ? 0.4949 0.3859 0.4239 -0.1151 -0.0797 -0.036  286 GLU B C   
5527 O O   . GLU B 286 ? 0.4899 0.3884 0.4335 -0.1211 -0.0786 -0.0377 286 GLU B O   
5528 C CB  . GLU B 286 ? 0.5977 0.4538 0.5027 -0.1275 -0.0685 -0.0491 286 GLU B CB  
5529 C CG  . GLU B 286 ? 0.7014 0.5433 0.6074 -0.1201 -0.0573 -0.0438 286 GLU B CG  
5530 C CD  . GLU B 286 ? 0.8179 0.6369 0.716  -0.1272 -0.0472 -0.0498 286 GLU B CD  
5531 O OE1 . GLU B 286 ? 0.8643 0.6791 0.7713 -0.1289 -0.0406 -0.0476 286 GLU B OE1 
5532 O OE2 . GLU B 286 ? 0.8372 0.6423 0.7206 -0.132  -0.0458 -0.0569 286 GLU B OE2 
5533 N N   . TRP B 287 ? 0.4498 0.3446 0.3784 -0.1045 -0.081  -0.0286 287 TRP B N   
5534 C CA  . TRP B 287 ? 0.4285 0.3313 0.372  -0.0981 -0.0786 -0.0221 287 TRP B CA  
5535 C C   . TRP B 287 ? 0.4323 0.3541 0.3858 -0.0936 -0.0879 -0.0174 287 TRP B C   
5536 O O   . TRP B 287 ? 0.449  0.3779 0.415  -0.0882 -0.0862 -0.0126 287 TRP B O   
5537 C CB  . TRP B 287 ? 0.4334 0.3232 0.3689 -0.0891 -0.0706 -0.0175 287 TRP B CB  
5538 C CG  . TRP B 287 ? 0.486  0.3566 0.4122 -0.0909 -0.061  -0.0206 287 TRP B CG  
5539 C CD1 . TRP B 287 ? 0.5206 0.3762 0.4302 -0.0895 -0.0575 -0.0234 287 TRP B CD1 
5540 C CD2 . TRP B 287 ? 0.4987 0.3623 0.4316 -0.0941 -0.0532 -0.0211 287 TRP B CD2 
5541 N NE1 . TRP B 287 ? 0.5654 0.4041 0.4708 -0.0908 -0.0483 -0.0253 287 TRP B NE1 
5542 C CE2 . TRP B 287 ? 0.5175 0.3599 0.4361 -0.094  -0.0454 -0.0237 287 TRP B CE2 
5543 C CE3 . TRP B 287 ? 0.504  0.3767 0.453  -0.097  -0.0515 -0.0195 287 TRP B CE3 
5544 C CZ2 . TRP B 287 ? 0.5476 0.3757 0.4661 -0.0964 -0.0361 -0.024  287 TRP B CZ2 
5545 C CZ3 . TRP B 287 ? 0.5474 0.4072 0.4967 -0.1004 -0.0419 -0.0202 287 TRP B CZ3 
5546 C CH2 . TRP B 287 ? 0.552  0.3888 0.4854 -0.0999 -0.0343 -0.0219 287 TRP B CH2 
5547 N N   . ILE B 288 ? 0.4379 0.3653 0.3834 -0.0942 -0.0969 -0.0181 288 ILE B N   
5548 C CA  . ILE B 288 ? 0.4387 0.379  0.3883 -0.0875 -0.1052 -0.0122 288 ILE B CA  
5549 C C   . ILE B 288 ? 0.4157 0.3759 0.3862 -0.089  -0.1109 -0.012  288 ILE B C   
5550 O O   . ILE B 288 ? 0.4248 0.3924 0.4024 -0.0978 -0.1128 -0.0181 288 ILE B O   
5551 C CB  . ILE B 288 ? 0.4454 0.3844 0.3778 -0.0885 -0.1128 -0.0131 288 ILE B CB  
5552 C CG1 . ILE B 288 ? 0.4648 0.3867 0.379  -0.085  -0.1064 -0.0119 288 ILE B CG1 
5553 C CG2 . ILE B 288 ? 0.4627 0.4158 0.3988 -0.0832 -0.1234 -0.0075 288 ILE B CG2 
5554 C CD1 . ILE B 288 ? 0.4776 0.3943 0.372  -0.0885 -0.1106 -0.0152 288 ILE B CD1 
5555 N N   . ASN B 289 ? 0.4206 0.3897 0.401  -0.0805 -0.1133 -0.0055 289 ASN B N   
5556 C CA  . ASN B 289 ? 0.4419 0.432  0.4424 -0.0794 -0.1197 -0.0047 289 ASN B CA  
5557 C C   . ASN B 289 ? 0.446  0.4462 0.4418 -0.0749 -0.1321 -0.0013 289 ASN B C   
5558 O O   . ASN B 289 ? 0.4251 0.4216 0.416  -0.0657 -0.1336 0.0056  289 ASN B O   
5559 C CB  . ASN B 289 ? 0.4424 0.4349 0.4571 -0.0725 -0.1133 -0.0002 289 ASN B CB  
5560 C CG  . ASN B 289 ? 0.4559 0.4711 0.4939 -0.0718 -0.1179 -0.0005 289 ASN B CG  
5561 O OD1 . ASN B 289 ? 0.4443 0.4755 0.4881 -0.0746 -0.1278 -0.0029 289 ASN B OD1 
5562 N ND2 . ASN B 289 ? 0.4955 0.5136 0.5472 -0.0678 -0.111  0.0015  289 ASN B ND2 
5563 N N   . TYR B 290 ? 0.4591 0.4713 0.4552 -0.0819 -0.1409 -0.0064 290 TYR B N   
5564 C CA  . TYR B 290 ? 0.4849 0.5074 0.4743 -0.0784 -0.1538 -0.0036 290 TYR B CA  
5565 C C   . TYR B 290 ? 0.491  0.5348 0.5005 -0.0703 -0.1612 0.001   290 TYR B C   
5566 O O   . TYR B 290 ? 0.5    0.5509 0.5042 -0.0641 -0.1715 0.0056  290 TYR B O   
5567 C CB  . TYR B 290 ? 0.5051 0.5347 0.4879 -0.0892 -0.161  -0.0117 290 TYR B CB  
5568 C CG  . TYR B 290 ? 0.5175 0.525  0.479  -0.0963 -0.1537 -0.0167 290 TYR B CG  
5569 C CD1 . TYR B 290 ? 0.521  0.5156 0.4587 -0.0937 -0.1558 -0.0142 290 TYR B CD1 
5570 C CD2 . TYR B 290 ? 0.5309 0.5295 0.4959 -0.1052 -0.144  -0.0237 290 TYR B CD2 
5571 C CE1 . TYR B 290 ? 0.5442 0.5197 0.4638 -0.099  -0.1484 -0.0189 290 TYR B CE1 
5572 C CE2 . TYR B 290 ? 0.5288 0.5063 0.4749 -0.1098 -0.1368 -0.0279 290 TYR B CE2 
5573 C CZ  . TYR B 290 ? 0.5468 0.5137 0.4707 -0.1066 -0.1392 -0.0259 290 TYR B CZ  
5574 O OH  . TYR B 290 ? 0.4985 0.4456 0.4048 -0.1103 -0.1314 -0.0304 290 TYR B OH  
5575 N N   . ASP B 291 ? 0.4859 0.5408 0.5185 -0.0704 -0.1562 -0.0004 291 ASP B N   
5576 C CA  . ASP B 291 ? 0.5368 0.6138 0.5912 -0.0626 -0.1621 0.003   291 ASP B CA  
5577 C C   . ASP B 291 ? 0.4936 0.562  0.5502 -0.0498 -0.1571 0.0112  291 ASP B C   
5578 O O   . ASP B 291 ? 0.6164 0.6984 0.6853 -0.0404 -0.1629 0.0157  291 ASP B O   
5579 C CB  . ASP B 291 ? 0.6253 0.7209 0.7047 -0.07   -0.1587 -0.0037 291 ASP B CB  
5580 C CG  . ASP B 291 ? 0.7235 0.8281 0.8031 -0.0846 -0.1625 -0.0132 291 ASP B CG  
5581 O OD1 . ASP B 291 ? 0.7223 0.8408 0.7987 -0.0854 -0.1752 -0.0145 291 ASP B OD1 
5582 O OD2 . ASP B 291 ? 0.8332 0.9285 0.9137 -0.095  -0.1524 -0.0192 291 ASP B OD2 
5583 N N   . SER B 292 ? 0.4643 0.5101 0.5086 -0.0491 -0.1466 0.0131  292 SER B N   
5584 C CA  . SER B 292 ? 0.4721 0.5098 0.52   -0.0394 -0.1399 0.0189  292 SER B CA  
5585 C C   . SER B 292 ? 0.5069 0.5363 0.5412 -0.0295 -0.1458 0.0267  292 SER B C   
5586 O O   . SER B 292 ? 0.4816 0.5007 0.4957 -0.0317 -0.1496 0.0277  292 SER B O   
5587 C CB  . SER B 292 ? 0.4543 0.473  0.4934 -0.0432 -0.1276 0.0173  292 SER B CB  
5588 O OG  . SER B 292 ? 0.4331 0.4413 0.4709 -0.035  -0.1213 0.0223  292 SER B OG  
5589 N N   . ASP B 293 ? 0.5369 0.5681 0.5805 -0.0187 -0.1452 0.0321  293 ASP B N   
5590 C CA  . ASP B 293 ? 0.6324 0.649  0.6604 -0.0098 -0.1475 0.0399  293 ASP B CA  
5591 C C   . ASP B 293 ? 0.5641 0.5611 0.5859 -0.0075 -0.1358 0.0418  293 ASP B C   
5592 O O   . ASP B 293 ? 0.5864 0.572  0.601  0.0005  -0.1353 0.0477  293 ASP B O   
5593 C CB  . ASP B 293 ? 0.6965 0.7253 0.733  0.0015  -0.1574 0.0457  293 ASP B CB  
5594 C CG  . ASP B 293 ? 0.7892 0.8326 0.8515 0.0086  -0.1546 0.0455  293 ASP B CG  
5595 O OD1 . ASP B 293 ? 0.7718 0.8098 0.8414 0.0062  -0.1433 0.0424  293 ASP B OD1 
5596 O OD2 . ASP B 293 ? 1.0103 1.0728 1.0857 0.0159  -0.1641 0.0477  293 ASP B OD2 
5597 N N   . ALA B 294 ? 0.4718 0.4635 0.494  -0.0148 -0.1265 0.0367  294 ALA B N   
5598 C CA  . ALA B 294 ? 0.4915 0.4648 0.503  -0.0146 -0.1168 0.0376  294 ALA B CA  
5599 C C   . ALA B 294 ? 0.4373 0.3957 0.4252 -0.0178 -0.1179 0.0391  294 ALA B C   
5600 O O   . ALA B 294 ? 0.4757 0.4362 0.4557 -0.0242 -0.1218 0.0362  294 ALA B O   
5601 C CB  . ALA B 294 ? 0.4667 0.4405 0.4857 -0.0202 -0.1074 0.0323  294 ALA B CB  
5602 N N   . VAL B 295 ? 0.4542 0.3977 0.4306 -0.0137 -0.1144 0.0435  295 VAL B N   
5603 C CA  . VAL B 295 ? 0.4529 0.3826 0.4073 -0.0168 -0.1142 0.0451  295 VAL B CA  
5604 C C   . VAL B 295 ? 0.449  0.3763 0.3968 -0.0252 -0.1092 0.0392  295 VAL B C   
5605 O O   . VAL B 295 ? 0.4729 0.3971 0.4069 -0.0295 -0.1123 0.0383  295 VAL B O   
5606 C CB  . VAL B 295 ? 0.4857 0.3997 0.4316 -0.0129 -0.1082 0.0492  295 VAL B CB  
5607 C CG1 . VAL B 295 ? 0.4762 0.3768 0.4015 -0.0183 -0.1044 0.049   295 VAL B CG1 
5608 C CG2 . VAL B 295 ? 0.5068 0.4185 0.4539 -0.0038 -0.1137 0.0561  295 VAL B CG2 
5609 N N   . THR B 296 ? 0.4156 0.3438 0.3721 -0.0272 -0.1014 0.0353  296 THR B N   
5610 C CA  . THR B 296 ? 0.4348 0.3589 0.3837 -0.0334 -0.0965 0.0305  296 THR B CA  
5611 C C   . THR B 296 ? 0.4154 0.3463 0.3646 -0.0389 -0.1014 0.0265  296 THR B C   
5612 O O   . THR B 296 ? 0.4447 0.3695 0.3814 -0.0435 -0.1    0.0235  296 THR B O   
5613 C CB  . THR B 296 ? 0.4711 0.3945 0.4279 -0.0333 -0.0877 0.0279  296 THR B CB  
5614 O OG1 . THR B 296 ? 0.4786 0.3965 0.426  -0.0375 -0.0832 0.0243  296 THR B OG1 
5615 C CG2 . THR B 296 ? 0.5129 0.4467 0.487  -0.0337 -0.0872 0.0258  296 THR B CG2 
5616 N N   . ASP B 297 ? 0.4089 0.3526 0.3725 -0.0388 -0.1066 0.0258  297 ASP B N   
5617 C CA  . ASP B 297 ? 0.3993 0.3506 0.364  -0.0453 -0.1118 0.0212  297 ASP B CA  
5618 C C   . ASP B 297 ? 0.43   0.3806 0.3799 -0.0462 -0.1205 0.0227  297 ASP B C   
5619 O O   . ASP B 297 ? 0.4007 0.3492 0.3406 -0.0527 -0.1221 0.0181  297 ASP B O   
5620 C CB  . ASP B 297 ? 0.4126 0.3801 0.3982 -0.0459 -0.1144 0.0194  297 ASP B CB  
5621 C CG  . ASP B 297 ? 0.447  0.4143 0.4451 -0.0464 -0.1048 0.0175  297 ASP B CG  
5622 O OD1 . ASP B 297 ? 0.4635 0.4193 0.4536 -0.0492 -0.0971 0.0154  297 ASP B OD1 
5623 O OD2 . ASP B 297 ? 0.4292 0.4082 0.4446 -0.0435 -0.1052 0.0182  297 ASP B OD2 
5624 N N   . MET B 298 ? 0.392  0.3435 0.3399 -0.0394 -0.126  0.029   298 MET B N   
5625 C CA  . MET B 298 ? 0.4347 0.385  0.367  -0.0391 -0.1346 0.0318  298 MET B CA  
5626 C C   . MET B 298 ? 0.4196 0.354  0.3298 -0.0426 -0.1297 0.0313  298 MET B C   
5627 O O   . MET B 298 ? 0.4164 0.3496 0.3122 -0.0465 -0.1346 0.0298  298 MET B O   
5628 C CB  . MET B 298 ? 0.4869 0.4396 0.4218 -0.0296 -0.1407 0.0397  298 MET B CB  
5629 C CG  . MET B 298 ? 0.5291 0.5014 0.4865 -0.0255 -0.1471 0.0397  298 MET B CG  
5630 S SD  . MET B 298 ? 0.631  0.6023 0.5958 -0.0118 -0.1492 0.0488  298 MET B SD  
5631 C CE  . MET B 298 ? 0.6537 0.6255 0.6    -0.0086 -0.1624 0.0545  298 MET B CE  
5632 N N   . GLN B 299 ? 0.4246 0.3483 0.333  -0.0414 -0.12   0.032   299 GLN B N   
5633 C CA  . GLN B 299 ? 0.4441 0.3557 0.3356 -0.0449 -0.1136 0.0303  299 GLN B CA  
5634 C C   . GLN B 299 ? 0.4384 0.3501 0.3252 -0.0517 -0.1118 0.0231  299 GLN B C   
5635 O O   . GLN B 299 ? 0.4303 0.3356 0.3002 -0.0549 -0.1116 0.0216  299 GLN B O   
5636 C CB  . GLN B 299 ? 0.4454 0.3501 0.3399 -0.0429 -0.1038 0.0309  299 GLN B CB  
5637 C CG  . GLN B 299 ? 0.4716 0.3701 0.3636 -0.0377 -0.1036 0.0375  299 GLN B CG  
5638 C CD  . GLN B 299 ? 0.4651 0.3581 0.3603 -0.0368 -0.0943 0.0369  299 GLN B CD  
5639 O OE1 . GLN B 299 ? 0.451  0.3471 0.3534 -0.0383 -0.0887 0.0324  299 GLN B OE1 
5640 N NE2 . GLN B 299 ? 0.4525 0.3366 0.3407 -0.0345 -0.0925 0.0416  299 GLN B NE2 
5641 N N   . GLU B 300 ? 0.4508 0.3687 0.3517 -0.054  -0.1101 0.0185  300 GLU B N   
5642 C CA  . GLU B 300 ? 0.4432 0.3584 0.339  -0.0605 -0.1077 0.0115  300 GLU B CA  
5643 C C   . GLU B 300 ? 0.4634 0.3837 0.3522 -0.0657 -0.1164 0.0083  300 GLU B C   
5644 O O   . GLU B 300 ? 0.4231 0.3366 0.2987 -0.0708 -0.1146 0.0031  300 GLU B O   
5645 C CB  . GLU B 300 ? 0.4866 0.4035 0.3971 -0.0616 -0.1016 0.0082  300 GLU B CB  
5646 C CG  . GLU B 300 ? 0.4819 0.3924 0.3943 -0.0571 -0.0925 0.0101  300 GLU B CG  
5647 C CD  . GLU B 300 ? 0.5201 0.4214 0.4174 -0.0556 -0.0879 0.0107  300 GLU B CD  
5648 O OE1 . GLU B 300 ? 0.549  0.4445 0.4337 -0.0588 -0.0865 0.0068  300 GLU B OE1 
5649 O OE2 . GLU B 300 ? 0.5253 0.4256 0.4231 -0.0515 -0.0854 0.0147  300 GLU B OE2 
5650 N N   . VAL B 301 ? 0.4561 0.3888 0.3531 -0.0641 -0.126  0.0111  301 VAL B N   
5651 C CA  . VAL B 301 ? 0.4715 0.4114 0.3606 -0.0683 -0.1361 0.0088  301 VAL B CA  
5652 C C   . VAL B 301 ? 0.4704 0.3995 0.335  -0.0682 -0.1369 0.0109  301 VAL B C   
5653 O O   . VAL B 301 ? 0.4713 0.398  0.3217 -0.0743 -0.1393 0.0057  301 VAL B O   
5654 C CB  . VAL B 301 ? 0.467  0.424  0.3699 -0.0643 -0.1468 0.0128  301 VAL B CB  
5655 C CG1 . VAL B 301 ? 0.4864 0.4525 0.3793 -0.0673 -0.1588 0.0115  301 VAL B CG1 
5656 C CG2 . VAL B 301 ? 0.4702 0.4402 0.3981 -0.0657 -0.1454 0.0096  301 VAL B CG2 
5657 N N   . ILE B 302 ? 0.4491 0.3711 0.3084 -0.0617 -0.1344 0.0183  302 ILE B N   
5658 C CA  . ILE B 302 ? 0.4861 0.3977 0.3225 -0.0616 -0.1343 0.0215  302 ILE B CA  
5659 C C   . ILE B 302 ? 0.4665 0.3675 0.291  -0.0666 -0.1249 0.0155  302 ILE B C   
5660 O O   . ILE B 302 ? 0.4912 0.3876 0.2971 -0.0706 -0.1262 0.0129  302 ILE B O   
5661 C CB  . ILE B 302 ? 0.4812 0.3866 0.3164 -0.0544 -0.1325 0.0305  302 ILE B CB  
5662 C CG1 . ILE B 302 ? 0.497  0.411  0.3384 -0.0481 -0.1431 0.0372  302 ILE B CG1 
5663 C CG2 . ILE B 302 ? 0.4948 0.3866 0.3067 -0.0558 -0.128  0.033   302 ILE B CG2 
5664 C CD1 . ILE B 302 ? 0.478  0.3857 0.3249 -0.0404 -0.1398 0.0448  302 ILE B CD1 
5665 N N   . PHE B 303 ? 0.4546 0.3524 0.2897 -0.0658 -0.1154 0.0131  303 PHE B N   
5666 C CA  . PHE B 303 ? 0.4569 0.346  0.2827 -0.0687 -0.1063 0.0078  303 PHE B CA  
5667 C C   . PHE B 303 ? 0.4667 0.3549 0.2859 -0.0751 -0.1078 -0.0004 303 PHE B C   
5668 O O   . PHE B 303 ? 0.4702 0.351  0.2728 -0.078  -0.1043 -0.0043 303 PHE B O   
5669 C CB  . PHE B 303 ? 0.4492 0.337  0.2888 -0.0655 -0.0975 0.0072  303 PHE B CB  
5670 C CG  . PHE B 303 ? 0.4536 0.3342 0.2854 -0.0648 -0.0877 0.0049  303 PHE B CG  
5671 C CD1 . PHE B 303 ? 0.4827 0.3574 0.297  -0.0679 -0.0851 0.0012  303 PHE B CD1 
5672 C CD2 . PHE B 303 ? 0.4892 0.3703 0.3322 -0.0609 -0.0808 0.0056  303 PHE B CD2 
5673 C CE1 . PHE B 303 ? 0.487  0.3578 0.297  -0.0665 -0.0757 -0.0013 303 PHE B CE1 
5674 C CE2 . PHE B 303 ? 0.4844 0.3622 0.3225 -0.0596 -0.0724 0.0031  303 PHE B CE2 
5675 C CZ  . PHE B 303 ? 0.4909 0.3641 0.3134 -0.0622 -0.0698 -0.0003 303 PHE B CZ  
5676 N N   . GLU B 304 ? 0.4544 0.3503 0.2865 -0.0778 -0.1127 -0.0034 304 GLU B N   
5677 C CA  . GLU B 304 ? 0.483  0.3783 0.3086 -0.0853 -0.1152 -0.0116 304 GLU B CA  
5678 C C   . GLU B 304 ? 0.5015 0.3973 0.3074 -0.0885 -0.1227 -0.0121 304 GLU B C   
5679 O O   . GLU B 304 ? 0.5171 0.4058 0.3077 -0.0939 -0.1206 -0.019  304 GLU B O   
5680 C CB  . GLU B 304 ? 0.4825 0.3879 0.3263 -0.0889 -0.1195 -0.0147 304 GLU B CB  
5681 C CG  . GLU B 304 ? 0.4991 0.4045 0.3362 -0.0984 -0.1227 -0.0239 304 GLU B CG  
5682 C CD  . GLU B 304 ? 0.5827 0.4976 0.4391 -0.1034 -0.1248 -0.0278 304 GLU B CD  
5683 O OE1 . GLU B 304 ? 0.5788 0.4841 0.4363 -0.1089 -0.1173 -0.0347 304 GLU B OE1 
5684 O OE2 . GLU B 304 ? 0.5183 0.4498 0.3871 -0.1022 -0.134  -0.0243 304 GLU B OE2 
5685 N N   . LEU B 305 ? 0.4847 0.3887 0.29   -0.085  -0.1319 -0.005  305 LEU B N   
5686 C CA  . LEU B 305 ? 0.5009 0.4053 0.2856 -0.0874 -0.1397 -0.0046 305 LEU B CA  
5687 C C   . LEU B 305 ? 0.5194 0.4097 0.2823 -0.0878 -0.1317 -0.0047 305 LEU B C   
5688 O O   . LEU B 305 ? 0.586  0.4725 0.3296 -0.093  -0.1334 -0.0096 305 LEU B O   
5689 C CB  . LEU B 305 ? 0.517  0.4312 0.3044 -0.0816 -0.1506 0.0045  305 LEU B CB  
5690 C CG  . LEU B 305 ? 0.5494 0.4816 0.3552 -0.0823 -0.161  0.0032  305 LEU B CG  
5691 C CD1 . LEU B 305 ? 0.5873 0.5286 0.4013 -0.0733 -0.1692 0.0132  305 LEU B CD1 
5692 C CD2 . LEU B 305 ? 0.591  0.5304 0.3857 -0.0902 -0.1698 -0.0041 305 LEU B CD2 
5693 N N   . ILE B 306 ? 0.5391 0.4228 0.305  -0.0827 -0.1231 0.0002  306 ILE B N   
5694 C CA  . ILE B 306 ? 0.5752 0.448  0.3242 -0.0833 -0.114  -0.0005 306 ILE B CA  
5695 C C   . ILE B 306 ? 0.5834 0.4504 0.3266 -0.0881 -0.107  -0.0108 306 ILE B C   
5696 O O   . ILE B 306 ? 0.5829 0.444  0.3063 -0.0916 -0.1051 -0.0145 306 ILE B O   
5697 C CB  . ILE B 306 ? 0.5841 0.4536 0.3409 -0.0781 -0.1057 0.005   306 ILE B CB  
5698 C CG1 . ILE B 306 ? 0.5575 0.4287 0.3163 -0.0734 -0.1115 0.0151  306 ILE B CG1 
5699 C CG2 . ILE B 306 ? 0.6082 0.4693 0.3502 -0.0796 -0.0953 0.0025  306 ILE B CG2 
5700 C CD1 . ILE B 306 ? 0.5692 0.4389 0.3412 -0.069  -0.1043 0.0191  306 ILE B CD1 
5701 N N   . ASN B 307 ? 0.5621 0.4296 0.3214 -0.088  -0.1028 -0.0155 307 ASN B N   
5702 C CA  . ASN B 307 ? 0.584  0.4437 0.3375 -0.092  -0.0964 -0.0252 307 ASN B CA  
5703 C C   . ASN B 307 ? 0.5941 0.4536 0.3345 -0.0997 -0.1032 -0.0321 307 ASN B C   
5704 O O   . ASN B 307 ? 0.6465 0.4967 0.3731 -0.1032 -0.0976 -0.0398 307 ASN B O   
5705 C CB  . ASN B 307 ? 0.5595 0.4179 0.3315 -0.0904 -0.091  -0.0281 307 ASN B CB  
5706 C CG  . ASN B 307 ? 0.57   0.4279 0.3522 -0.0832 -0.0832 -0.0232 307 ASN B CG  
5707 O OD1 . ASN B 307 ? 0.5225 0.3794 0.2969 -0.0804 -0.0792 -0.0201 307 ASN B OD1 
5708 N ND2 . ASN B 307 ? 0.5223 0.3812 0.3215 -0.0806 -0.0802 -0.0229 307 ASN B ND2 
5709 N N   . HIS B 308 ? 0.6142 0.4844 0.359  -0.1022 -0.1152 -0.0301 308 HIS B N   
5710 C CA  . HIS B 308 ? 0.628  0.501  0.3601 -0.1101 -0.1233 -0.0368 308 HIS B CA  
5711 C C   . HIS B 308 ? 0.6615 0.5346 0.3703 -0.1104 -0.1291 -0.0333 308 HIS B C   
5712 O O   . HIS B 308 ? 0.6551 0.5335 0.3529 -0.1161 -0.1384 -0.0372 308 HIS B O   
5713 C CB  . HIS B 308 ? 0.6347 0.522  0.3843 -0.1133 -0.1336 -0.0376 308 HIS B CB  
5714 C CG  . HIS B 308 ? 0.7192 0.6048 0.4875 -0.116  -0.1278 -0.043  308 HIS B CG  
5715 N ND1 . HIS B 308 ? 0.6918 0.5907 0.4816 -0.1172 -0.1337 -0.042  308 HIS B ND1 
5716 C CD2 . HIS B 308 ? 0.774  0.6457 0.5419 -0.1178 -0.1166 -0.0495 308 HIS B CD2 
5717 C CE1 . HIS B 308 ? 0.7059 0.5981 0.5068 -0.1203 -0.1256 -0.0473 308 HIS B CE1 
5718 N NE2 . HIS B 308 ? 0.711  0.5859 0.4984 -0.1202 -0.1155 -0.0516 308 HIS B NE2 
5719 N N   . LYS B 309 ? 0.687  0.5545 0.3874 -0.1049 -0.1238 -0.026  309 LYS B N   
5720 C CA  . LYS B 309 ? 0.7379 0.6015 0.4129 -0.1056 -0.1261 -0.0227 309 LYS B CA  
5721 C C   . LYS B 309 ? 0.714  0.5876 0.386  -0.1036 -0.1404 -0.0146 309 LYS B C   
5722 O O   . LYS B 309 ? 0.757  0.6285 0.4058 -0.1054 -0.1452 -0.0129 309 LYS B O   
5723 C CB  . LYS B 309 ? 0.8104 0.667  0.4616 -0.1129 -0.1243 -0.0325 309 LYS B CB  
5724 C CG  . LYS B 309 ? 0.926  0.7721 0.5768 -0.1151 -0.1114 -0.0423 309 LYS B CG  
5725 C CD  . LYS B 309 ? 0.9275 0.767  0.5787 -0.1096 -0.0987 -0.0387 309 LYS B CD  
5726 C CE  . LYS B 309 ? 0.9695 0.8012 0.6269 -0.1092 -0.0871 -0.0474 309 LYS B CE  
5727 N NZ  . LYS B 309 ? 0.982  0.8125 0.6474 -0.1027 -0.0767 -0.0431 309 LYS B NZ  
5728 N N   . GLU B 310 ? 0.6245 0.5091 0.319  -0.0995 -0.1471 -0.0099 310 GLU B N   
5729 C CA  . GLU B 310 ? 0.6662 0.562  0.3612 -0.0959 -0.1609 -0.0023 310 GLU B CA  
5730 C C   . GLU B 310 ? 0.6536 0.5441 0.3498 -0.0872 -0.1584 0.01    310 GLU B C   
5731 O O   . GLU B 310 ? 0.62   0.5176 0.3365 -0.0813 -0.1613 0.0155  310 GLU B O   
5732 C CB  . GLU B 310 ? 0.696  0.608  0.4146 -0.0974 -0.169  -0.0062 310 GLU B CB  
5733 C CG  . GLU B 310 ? 0.7916 0.7084 0.5038 -0.1076 -0.1734 -0.0183 310 GLU B CG  
5734 C CD  . GLU B 310 ? 0.8523 0.7872 0.5886 -0.11   -0.1817 -0.0219 310 GLU B CD  
5735 O OE1 . GLU B 310 ? 0.9008 0.8509 0.6428 -0.1056 -0.1941 -0.0158 310 GLU B OE1 
5736 O OE2 . GLU B 310 ? 0.9702 0.9037 0.7199 -0.1157 -0.1755 -0.0302 310 GLU B OE2 
5737 N N   . LEU B 311 ? 0.6622 0.5397 0.3362 -0.0872 -0.1521 0.0136  311 LEU B N   
5738 C CA  . LEU B 311 ? 0.6815 0.5503 0.3553 -0.0812 -0.1461 0.0235  311 LEU B CA  
5739 C C   . LEU B 311 ? 0.6774 0.5496 0.3496 -0.074  -0.1574 0.0348  311 LEU B C   
5740 O O   . LEU B 311 ? 0.663  0.5329 0.348  -0.0676 -0.1553 0.0421  311 LEU B O   
5741 C CB  . LEU B 311 ? 0.7293 0.5841 0.3792 -0.0847 -0.1357 0.0233  311 LEU B CB  
5742 C CG  . LEU B 311 ? 0.765  0.6158 0.4177 -0.0893 -0.1227 0.0133  311 LEU B CG  
5743 C CD1 . LEU B 311 ? 0.7803 0.6197 0.4149 -0.0912 -0.1109 0.0147  311 LEU B CD1 
5744 C CD2 . LEU B 311 ? 0.7406 0.5958 0.4213 -0.0863 -0.1175 0.0113  311 LEU B CD2 
5745 N N   . SER B 312 ? 0.6897 0.5671 0.3455 -0.0748 -0.1692 0.0359  312 SER B N   
5746 C CA  . SER B 312 ? 0.7201 0.6012 0.3715 -0.0669 -0.1811 0.0468  312 SER B CA  
5747 C C   . SER B 312 ? 0.7222 0.6188 0.4043 -0.0608 -0.1881 0.0482  312 SER B C   
5748 O O   . SER B 312 ? 0.7117 0.6049 0.4006 -0.0521 -0.1889 0.058   312 SER B O   
5749 C CB  . SER B 312 ? 0.7885 0.6741 0.4152 -0.0694 -0.1928 0.0465  312 SER B CB  
5750 O OG  . SER B 312 ? 0.8223 0.7182 0.4525 -0.0606 -0.2071 0.0554  312 SER B OG  
5751 N N   . LYS B 313 ? 0.664  0.5756 0.3645 -0.0658 -0.1911 0.0381  313 LYS B N   
5752 C CA  . LYS B 313 ? 0.6685 0.5955 0.3994 -0.0612 -0.1958 0.0384  313 LYS B CA  
5753 C C   . LYS B 313 ? 0.6185 0.5373 0.3674 -0.0578 -0.1834 0.0404  313 LYS B C   
5754 O O   . LYS B 313 ? 0.6447 0.57   0.4122 -0.0502 -0.1862 0.0458  313 LYS B O   
5755 C CB  . LYS B 313 ? 0.7405 0.6853 0.4873 -0.0684 -0.2012 0.0273  313 LYS B CB  
5756 C CG  . LYS B 313 ? 0.8001 0.7628 0.5782 -0.0633 -0.2064 0.0284  313 LYS B CG  
5757 C CD  . LYS B 313 ? 0.9207 0.9062 0.713  -0.0693 -0.2167 0.0199  313 LYS B CD  
5758 C CE  . LYS B 313 ? 1.0244 1.0093 0.8291 -0.0797 -0.2077 0.008   313 LYS B CE  
5759 N NZ  . LYS B 313 ? 1.085  1.0871 0.8956 -0.0892 -0.2159 -0.0023 313 LYS B NZ  
5760 N N   . ALA B 314 ? 0.5642 0.4711 0.3097 -0.0631 -0.1703 0.0352  314 ALA B N   
5761 C CA  . ALA B 314 ? 0.5308 0.4307 0.2912 -0.0603 -0.159  0.0367  314 ALA B CA  
5762 C C   . ALA B 314 ? 0.5528 0.4427 0.3074 -0.0525 -0.1579 0.0481  314 ALA B C   
5763 O O   . ALA B 314 ? 0.5381 0.4293 0.3105 -0.0468 -0.1558 0.0517  314 ALA B O   
5764 C CB  . ALA B 314 ? 0.5242 0.4136 0.2773 -0.0664 -0.1464 0.0301  314 ALA B CB  
5765 N N   . LEU B 315 ? 0.5966 0.4754 0.3253 -0.0525 -0.1591 0.0535  315 LEU B N   
5766 C CA  . LEU B 315 ? 0.6722 0.5377 0.3915 -0.046  -0.1572 0.0646  315 LEU B CA  
5767 C C   . LEU B 315 ? 0.739  0.6123 0.4694 -0.036  -0.1682 0.0724  315 LEU B C   
5768 O O   . LEU B 315 ? 0.7333 0.6    0.4733 -0.0296 -0.1645 0.0783  315 LEU B O   
5769 C CB  . LEU B 315 ? 0.734  0.5849 0.4213 -0.0488 -0.1555 0.0691  315 LEU B CB  
5770 C CG  . LEU B 315 ? 0.8257 0.658  0.5004 -0.0443 -0.15   0.08    315 LEU B CG  
5771 C CD1 . LEU B 315 ? 0.7828 0.6068 0.4701 -0.0456 -0.1365 0.0789  315 LEU B CD1 
5772 C CD2 . LEU B 315 ? 0.8774 0.6966 0.5187 -0.049  -0.148  0.083   315 LEU B CD2 
5773 N N   . GLN B 316 ? 0.7557 0.6441 0.4865 -0.0345 -0.1816 0.0716  316 GLN B N   
5774 C CA  . GLN B 316 ? 0.7944 0.6944 0.5387 -0.0242 -0.1928 0.0782  316 GLN B CA  
5775 C C   . GLN B 316 ? 0.7306 0.6402 0.5072 -0.0212 -0.1889 0.0751  316 GLN B C   
5776 O O   . GLN B 316 ? 0.7524 0.66   0.5385 -0.0114 -0.19   0.0825  316 GLN B O   
5777 C CB  . GLN B 316 ? 0.7943 0.7125 0.5341 -0.0238 -0.2086 0.0768  316 GLN B CB  
5778 C CG  . GLN B 316 ? 0.8899 0.7971 0.595  -0.0246 -0.2134 0.0823  316 GLN B CG  
5779 C CD  . GLN B 316 ? 0.9548 0.8809 0.6529 -0.0254 -0.2294 0.0798  316 GLN B CD  
5780 O OE1 . GLN B 316 ? 1.0069 0.9537 0.7237 -0.0304 -0.2347 0.0702  316 GLN B OE1 
5781 N NE2 . GLN B 316 ? 0.9338 0.8524 0.6036 -0.0213 -0.2368 0.0883  316 GLN B NE2 
5782 N N   . LEU B 317 ? 0.6655 0.5839 0.4577 -0.029  -0.1837 0.0645  317 LEU B N   
5783 C CA  . LEU B 317 ? 0.6541 0.5805 0.4748 -0.0269 -0.1788 0.0616  317 LEU B CA  
5784 C C   . LEU B 317 ? 0.616  0.5251 0.4376 -0.0241 -0.1664 0.0654  317 LEU B C   
5785 O O   . LEU B 317 ? 0.6085 0.5207 0.4489 -0.018  -0.1644 0.0674  317 LEU B O   
5786 C CB  . LEU B 317 ? 0.6575 0.5953 0.4927 -0.0358 -0.1759 0.0502  317 LEU B CB  
5787 C CG  . LEU B 317 ? 0.7643 0.7225 0.6052 -0.0393 -0.1882 0.045   317 LEU B CG  
5788 C CD1 . LEU B 317 ? 0.7051 0.6677 0.5534 -0.0503 -0.183  0.0333  317 LEU B CD1 
5789 C CD2 . LEU B 317 ? 0.7795 0.7573 0.6432 -0.0313 -0.1973 0.0483  317 LEU B CD2 
5790 N N   . LEU B 318 ? 0.5701 0.4626 0.3724 -0.0291 -0.1579 0.0654  318 LEU B N   
5791 C CA  . LEU B 318 ? 0.5722 0.4498 0.3744 -0.0283 -0.1462 0.0677  318 LEU B CA  
5792 C C   . LEU B 318 ? 0.6184 0.4851 0.4155 -0.0191 -0.1484 0.0784  318 LEU B C   
5793 O O   . LEU B 318 ? 0.5928 0.4543 0.4016 -0.0151 -0.1425 0.0803  318 LEU B O   
5794 C CB  . LEU B 318 ? 0.5774 0.4431 0.3615 -0.0364 -0.1369 0.0644  318 LEU B CB  
5795 C CG  . LEU B 318 ? 0.6163 0.471  0.4033 -0.0378 -0.1241 0.0641  318 LEU B CG  
5796 C CD1 . LEU B 318 ? 0.5444 0.4082 0.3539 -0.039  -0.1186 0.057   318 LEU B CD1 
5797 C CD2 . LEU B 318 ? 0.6755 0.5195 0.442  -0.0449 -0.1163 0.0623  318 LEU B CD2 
5798 N N   . ASN B 319 ? 0.6467 0.5094 0.4256 -0.0153 -0.1569 0.0855  319 ASN B N   
5799 C CA  . ASN B 319 ? 0.7329 0.5853 0.5063 -0.0047 -0.1608 0.0966  319 ASN B CA  
5800 C C   . ASN B 319 ? 0.7421 0.6072 0.5413 0.0052  -0.166  0.0981  319 ASN B C   
5801 O O   . ASN B 319 ? 0.7966 0.6494 0.5985 0.0124  -0.1618 0.1041  319 ASN B O   
5802 C CB  . ASN B 319 ? 0.8243 0.6751 0.5756 -0.0009 -0.172  0.1038  319 ASN B CB  
5803 C CG  . ASN B 319 ? 0.8777 0.7097 0.5984 -0.0078 -0.1661 0.1062  319 ASN B CG  
5804 O OD1 . ASN B 319 ? 0.8031 0.6222 0.5201 -0.0145 -0.1531 0.1035  319 ASN B OD1 
5805 N ND2 . ASN B 319 ? 0.9504 0.7813 0.6493 -0.0054 -0.1759 0.1119  319 ASN B ND2 
5806 N N   . LYS B 320 ? 0.7796 0.6685 0.5978 0.0049  -0.1737 0.0922  320 LYS B N   
5807 C CA  . LYS B 320 ? 0.8626 0.7662 0.7082 0.0127  -0.1766 0.0918  320 LYS B CA  
5808 C C   . LYS B 320 ? 0.7968 0.6934 0.6573 0.0115  -0.1637 0.0883  320 LYS B C   
5809 O O   . LYS B 320 ? 0.7411 0.6391 0.6167 0.0203  -0.1631 0.0914  320 LYS B O   
5810 C CB  . LYS B 320 ? 1.0026 0.934  0.8665 0.0097  -0.1855 0.0844  320 LYS B CB  
5811 C CG  . LYS B 320 ? 1.1174 1.0618 0.9719 0.0128  -0.2009 0.0876  320 LYS B CG  
5812 C CD  . LYS B 320 ? 1.2154 1.1851 1.0828 0.005   -0.2083 0.0778  320 LYS B CD  
5813 C CE  . LYS B 320 ? 1.2794 1.2692 1.1794 0.0049  -0.2071 0.0715  320 LYS B CE  
5814 N NZ  . LYS B 320 ? 1.3842 1.3852 1.3005 0.0187  -0.2137 0.0782  320 LYS B NZ  
5815 N N   . LEU B 321 ? 0.7078 0.598  0.5643 0.0012  -0.1538 0.0817  321 LEU B N   
5816 C CA  . LEU B 321 ? 0.6635 0.5479 0.5317 -0.0005 -0.1421 0.0781  321 LEU B CA  
5817 C C   . LEU B 321 ? 0.6349 0.4973 0.4921 0.0033  -0.1349 0.0845  321 LEU B C   
5818 O O   . LEU B 321 ? 0.6717 0.5309 0.5414 0.0052  -0.1276 0.0828  321 LEU B O   
5819 C CB  . LEU B 321 ? 0.6225 0.5082 0.4903 -0.0114 -0.1344 0.0694  321 LEU B CB  
5820 C CG  . LEU B 321 ? 0.5949 0.5    0.4795 -0.0153 -0.1377 0.0618  321 LEU B CG  
5821 C CD1 . LEU B 321 ? 0.5553 0.4583 0.4366 -0.0245 -0.1298 0.0543  321 LEU B CD1 
5822 C CD2 . LEU B 321 ? 0.6288 0.5449 0.538  -0.0099 -0.1371 0.0609  321 LEU B CD2 
5823 N N   . GLU B 322 ? 0.6669 0.5133 0.5003 0.0037  -0.1361 0.0912  322 GLU B N   
5824 C CA  . GLU B 322 ? 0.7575 0.5807 0.5793 0.0071  -0.1291 0.0978  322 GLU B CA  
5825 C C   . GLU B 322 ? 0.7954 0.6163 0.6291 0.0198  -0.1321 0.1037  322 GLU B C   
5826 O O   . GLU B 322 ? 0.8664 0.6705 0.699  0.0219  -0.1238 0.1058  322 GLU B O   
5827 C CB  . GLU B 322 ? 0.8278 0.6339 0.6202 0.0044  -0.1296 0.1043  322 GLU B CB  
5828 C CG  . GLU B 322 ? 0.846  0.6532 0.6283 -0.0082 -0.1236 0.0973  322 GLU B CG  
5829 C CD  . GLU B 322 ? 0.9115 0.6987 0.6679 -0.0149 -0.1161 0.1005  322 GLU B CD  
5830 O OE1 . GLU B 322 ? 0.8711 0.6604 0.6247 -0.0248 -0.1084 0.0934  322 GLU B OE1 
5831 O OE2 . GLU B 322 ? 0.9587 0.7285 0.6976 -0.01   -0.1176 0.1102  322 GLU B OE2 
5832 N N   . GLU B 323 ? 0.8315 0.6704 0.678  0.0279  -0.1433 0.1054  323 GLU B N   
5833 C CA  . GLU B 323 ? 0.9395 0.7811 0.8011 0.0411  -0.1467 0.11    323 GLU B CA  
5834 C C   . GLU B 323 ? 0.8922 0.7427 0.7789 0.0406  -0.1391 0.1026  323 GLU B C   
5835 O O   . GLU B 323 ? 0.8879 0.7378 0.7872 0.051   -0.1387 0.1054  323 GLU B O   
5836 C CB  . GLU B 323 ? 0.9919 0.8553 0.8607 0.0487  -0.1618 0.1128  323 GLU B CB  
5837 C CG  . GLU B 323 ? 1.1756 1.0398 1.0526 0.0654  -0.1683 0.1211  323 GLU B CG  
5838 C CD  . GLU B 323 ? 1.2547 1.0921 1.1068 0.0743  -0.1693 0.1333  323 GLU B CD  
5839 O OE1 . GLU B 323 ? 1.46   1.2827 1.2859 0.0674  -0.1687 0.1364  323 GLU B OE1 
5840 O OE2 . GLU B 323 ? 1.047  0.8764 0.9047 0.0881  -0.1697 0.1398  323 GLU B OE2 
5841 N N   . ARG B 324 ? 0.6776 0.5365 0.5712 0.0294  -0.1332 0.0934  324 ARG B N   
5842 C CA  . ARG B 324 ? 0.6461 0.5177 0.5634 0.0288  -0.1279 0.0863  324 ARG B CA  
5843 C C   . ARG B 324 ? 0.6195 0.4742 0.5335 0.0247  -0.115  0.0836  324 ARG B C   
5844 O O   . ARG B 324 ? 0.5956 0.4351 0.4918 0.0178  -0.1096 0.0838  324 ARG B O   
5845 C CB  . ARG B 324 ? 0.6251 0.5167 0.5524 0.02    -0.1298 0.0782  324 ARG B CB  
5846 C CG  . ARG B 324 ? 0.6462 0.5581 0.5805 0.0225  -0.1424 0.0787  324 ARG B CG  
5847 C CD  . ARG B 324 ? 0.6289 0.5571 0.5864 0.0324  -0.1469 0.0797  324 ARG B CD  
5848 N NE  . ARG B 324 ? 0.5994 0.5363 0.5763 0.0285  -0.1386 0.0723  324 ARG B NE  
5849 C CZ  . ARG B 324 ? 0.5827 0.535  0.57   0.0201  -0.1383 0.065   324 ARG B CZ  
5850 N NH1 . ARG B 324 ? 0.5424 0.5064 0.5265 0.0148  -0.1466 0.063   324 ARG B NH1 
5851 N NH2 . ARG B 324 ? 0.5509 0.5054 0.5505 0.0165  -0.1292 0.0595  324 ARG B NH2 
5852 N N   . ASP B 325 ? 0.6064 0.4661 0.5386 0.0285  -0.11   0.0802  325 ASP B N   
5853 C CA  . ASP B 325 ? 0.6109 0.4587 0.543  0.0245  -0.0984 0.0761  325 ASP B CA  
5854 C C   . ASP B 325 ? 0.5197 0.3765 0.4525 0.0133  -0.0945 0.0686  325 ASP B C   
5855 O O   . ASP B 325 ? 0.5329 0.4082 0.4785 0.0117  -0.0983 0.0648  325 ASP B O   
5856 C CB  . ASP B 325 ? 0.6591 0.5119 0.6104 0.032   -0.0948 0.0741  325 ASP B CB  
5857 C CG  . ASP B 325 ? 0.7641 0.6049 0.7145 0.0446  -0.0967 0.0813  325 ASP B CG  
5858 O OD1 . ASP B 325 ? 0.7857 0.6047 0.7166 0.0453  -0.0957 0.0871  325 ASP B OD1 
5859 O OD2 . ASP B 325 ? 0.9837 0.8358 0.9527 0.0538  -0.0982 0.0812  325 ASP B OD2 
5860 N N   . GLN B 326 ? 0.5034 0.3471 0.4223 0.0057  -0.0874 0.0667  326 GLN B N   
5861 C CA  . GLN B 326 ? 0.5078 0.359  0.4264 -0.0036 -0.0832 0.0599  326 GLN B CA  
5862 C C   . GLN B 326 ? 0.5205 0.3622 0.4362 -0.008  -0.0731 0.056   326 GLN B C   
5863 O O   . GLN B 326 ? 0.4808 0.3057 0.3855 -0.0079 -0.0695 0.059   326 GLN B O   
5864 C CB  . GLN B 326 ? 0.5176 0.3655 0.4192 -0.0096 -0.0859 0.0612  326 GLN B CB  
5865 C CG  . GLN B 326 ? 0.5309 0.3894 0.4333 -0.007  -0.0963 0.0637  326 GLN B CG  
5866 C CD  . GLN B 326 ? 0.5402 0.3963 0.4255 -0.0136 -0.0982 0.0636  326 GLN B CD  
5867 O OE1 . GLN B 326 ? 0.5215 0.3813 0.4048 -0.0206 -0.094  0.058   326 GLN B OE1 
5868 N NE2 . GLN B 326 ? 0.5584 0.408  0.4303 -0.0107 -0.1046 0.07    326 GLN B NE2 
5869 N N   . ASN B 327 ? 0.5057 0.3577 0.4289 -0.0127 -0.0689 0.0494  327 ASN B N   
5870 C CA  . ASN B 327 ? 0.5362 0.3827 0.4555 -0.0181 -0.0603 0.0448  327 ASN B CA  
5871 C C   . ASN B 327 ? 0.5189 0.3616 0.4235 -0.0259 -0.0583 0.0438  327 ASN B C   
5872 O O   . ASN B 327 ? 0.4787 0.3231 0.3759 -0.0273 -0.0629 0.0461  327 ASN B O   
5873 C CB  . ASN B 327 ? 0.4664 0.3248 0.399  -0.0181 -0.0569 0.0391  327 ASN B CB  
5874 C CG  . ASN B 327 ? 0.4542 0.3257 0.3893 -0.0215 -0.0587 0.0361  327 ASN B CG  
5875 O OD1 . ASN B 327 ? 0.4646 0.3355 0.3899 -0.0267 -0.0578 0.0347  327 ASN B OD1 
5876 N ND2 . ASN B 327 ? 0.4547 0.3372 0.4026 -0.0189 -0.0599 0.0345  327 ASN B ND2 
5877 N N   . GLU B 328 ? 0.4771 0.3151 0.3773 -0.0314 -0.0509 0.0398  328 GLU B N   
5878 C CA  . GLU B 328 ? 0.4928 0.3282 0.3807 -0.0391 -0.0475 0.0382  328 GLU B CA  
5879 C C   . GLU B 328 ? 0.4499 0.2995 0.339  -0.0415 -0.0495 0.035   328 GLU B C   
5880 O O   . GLU B 328 ? 0.4265 0.2742 0.3047 -0.0455 -0.0496 0.0358  328 GLU B O   
5881 C CB  . GLU B 328 ? 0.5123 0.343  0.3981 -0.045  -0.0393 0.0334  328 GLU B CB  
5882 C CG  . GLU B 328 ? 0.608  0.4184 0.4861 -0.0445 -0.0363 0.0373  328 GLU B CG  
5883 C CD  . GLU B 328 ? 0.727  0.5317 0.602  -0.0523 -0.0277 0.0316  328 GLU B CD  
5884 O OE1 . GLU B 328 ? 0.6402 0.4584 0.5229 -0.0554 -0.025  0.0245  328 GLU B OE1 
5885 O OE2 . GLU B 328 ? 0.7928 0.5792 0.6561 -0.0557 -0.0239 0.0344  328 GLU B OE2 
5886 N N   . ASN B 329 ? 0.4125 0.2747 0.3135 -0.0391 -0.0501 0.0314  329 ASN B N   
5887 C CA  . ASN B 329 ? 0.4325 0.3055 0.334  -0.0405 -0.0514 0.0286  329 ASN B CA  
5888 C C   . ASN B 329 ? 0.4343 0.307  0.3327 -0.0387 -0.0583 0.0321  329 ASN B C   
5889 O O   . ASN B 329 ? 0.4132 0.2874 0.3034 -0.0417 -0.0593 0.0313  329 ASN B O   
5890 C CB  . ASN B 329 ? 0.4053 0.2888 0.3185 -0.038  -0.05   0.0249  329 ASN B CB  
5891 C CG  . ASN B 329 ? 0.4059 0.2979 0.3176 -0.0395 -0.049  0.0214  329 ASN B CG  
5892 O OD1 . ASN B 329 ? 0.4164 0.3122 0.3311 -0.0377 -0.0519 0.0215  329 ASN B OD1 
5893 N ND2 . ASN B 329 ? 0.3952 0.2902 0.302  -0.043  -0.0446 0.0181  329 ASN B ND2 
5894 N N   . GLU B 330 ? 0.4265 0.298  0.3314 -0.0338 -0.0632 0.0358  330 GLU B N   
5895 C CA  . GLU B 330 ? 0.4441 0.3173 0.3468 -0.0322 -0.0708 0.039   330 GLU B CA  
5896 C C   . GLU B 330 ? 0.4311 0.2945 0.3167 -0.0347 -0.0725 0.0427  330 GLU B C   
5897 O O   . GLU B 330 ? 0.4299 0.2955 0.3083 -0.0366 -0.0765 0.0428  330 GLU B O   
5898 C CB  . GLU B 330 ? 0.4563 0.332  0.3703 -0.0259 -0.0758 0.0423  330 GLU B CB  
5899 C CG  . GLU B 330 ? 0.5057 0.393  0.4363 -0.0242 -0.075  0.0387  330 GLU B CG  
5900 C CD  . GLU B 330 ? 0.5554 0.4475 0.4998 -0.0179 -0.0784 0.0411  330 GLU B CD  
5901 O OE1 . GLU B 330 ? 0.5038 0.3881 0.4463 -0.0133 -0.0794 0.0454  330 GLU B OE1 
5902 O OE2 . GLU B 330 ? 0.5199 0.4234 0.4773 -0.0176 -0.0795 0.0387  330 GLU B OE2 
5903 N N   . LEU B 331 ? 0.456  0.3074 0.3341 -0.0352 -0.0688 0.0456  331 LEU B N   
5904 C CA  . LEU B 331 ? 0.4884 0.3282 0.3484 -0.0383 -0.0687 0.0495  331 LEU B CA  
5905 C C   . LEU B 331 ? 0.485  0.3279 0.3361 -0.0456 -0.0639 0.045   331 LEU B C   
5906 O O   . LEU B 331 ? 0.4854 0.3238 0.3222 -0.0482 -0.0655 0.0472  331 LEU B O   
5907 C CB  . LEU B 331 ? 0.516  0.3403 0.3707 -0.0377 -0.0642 0.0532  331 LEU B CB  
5908 C CG  . LEU B 331 ? 0.528  0.3457 0.3863 -0.0291 -0.0697 0.0597  331 LEU B CG  
5909 C CD1 . LEU B 331 ? 0.5468 0.3478 0.4014 -0.0283 -0.0636 0.0619  331 LEU B CD1 
5910 C CD2 . LEU B 331 ? 0.5639 0.3785 0.4104 -0.0258 -0.0784 0.0664  331 LEU B CD2 
5911 N N   . GLY B 332 ? 0.4401 0.2912 0.2989 -0.0483 -0.0581 0.0389  332 GLY B N   
5912 C CA  . GLY B 332 ? 0.4473 0.3052 0.3011 -0.0532 -0.0544 0.034   332 GLY B CA  
5913 C C   . GLY B 332 ? 0.443  0.3056 0.2932 -0.0523 -0.0597 0.0334  332 GLY B C   
5914 O O   . GLY B 332 ? 0.4851 0.3459 0.3228 -0.0561 -0.0585 0.0327  332 GLY B O   
5915 N N   . PHE B 333 ? 0.4249 0.2935 0.2863 -0.0481 -0.0648 0.0331  333 PHE B N   
5916 C CA  . PHE B 333 ? 0.446  0.3188 0.3055 -0.048  -0.0701 0.0318  333 PHE B CA  
5917 C C   . PHE B 333 ? 0.4459 0.312  0.2925 -0.0483 -0.0764 0.0368  333 PHE B C   
5918 O O   . PHE B 333 ? 0.4338 0.2995 0.269  -0.0513 -0.0778 0.0351  333 PHE B O   
5919 C CB  . PHE B 333 ? 0.4285 0.3092 0.3036 -0.0446 -0.0732 0.0301  333 PHE B CB  
5920 C CG  . PHE B 333 ? 0.4789 0.3653 0.3617 -0.0446 -0.0672 0.025   333 PHE B CG  
5921 C CD1 . PHE B 333 ? 0.5314 0.4198 0.4097 -0.0464 -0.0651 0.0207  333 PHE B CD1 
5922 C CD2 . PHE B 333 ? 0.5152 0.4039 0.4079 -0.0423 -0.0632 0.0247  333 PHE B CD2 
5923 C CE1 . PHE B 333 ? 0.494  0.387  0.3786 -0.0447 -0.0598 0.0169  333 PHE B CE1 
5924 C CE2 . PHE B 333 ? 0.5147 0.409  0.4126 -0.0416 -0.0583 0.0207  333 PHE B CE2 
5925 C CZ  . PHE B 333 ? 0.5099 0.4063 0.4037 -0.0423 -0.0568 0.0173  333 PHE B CZ  
5926 N N   . HIS B 334 ? 0.4411 0.3017 0.2887 -0.0445 -0.08   0.0428  334 HIS B N   
5927 C CA  . HIS B 334 ? 0.4653 0.3194 0.3001 -0.0431 -0.0869 0.0488  334 HIS B CA  
5928 C C   . HIS B 334 ? 0.507  0.3522 0.3207 -0.0485 -0.0834 0.0496  334 HIS B C   
5929 O O   . HIS B 334 ? 0.4918 0.3368 0.293  -0.05   -0.0883 0.0503  334 HIS B O   
5930 C CB  . HIS B 334 ? 0.477  0.323  0.3142 -0.0375 -0.0885 0.0555  334 HIS B CB  
5931 C CG  . HIS B 334 ? 0.5134 0.352  0.3369 -0.0342 -0.0959 0.0629  334 HIS B CG  
5932 N ND1 . HIS B 334 ? 0.5156 0.3632 0.346  -0.0287 -0.1062 0.0652  334 HIS B ND1 
5933 C CD2 . HIS B 334 ? 0.5483 0.3724 0.352  -0.0353 -0.0949 0.0687  334 HIS B CD2 
5934 C CE1 . HIS B 334 ? 0.5417 0.3808 0.3565 -0.0256 -0.1119 0.0725  334 HIS B CE1 
5935 N NE2 . HIS B 334 ? 0.5314 0.3547 0.3284 -0.0296 -0.105  0.0751  334 HIS B NE2 
5936 N N   . TYR B 335 ? 0.4991 0.337  0.3084 -0.0518 -0.0746 0.0495  335 TYR B N   
5937 C CA  . TYR B 335 ? 0.516  0.3453 0.3061 -0.0578 -0.0695 0.0503  335 TYR B CA  
5938 C C   . TYR B 335 ? 0.4979 0.3358 0.2845 -0.0623 -0.0663 0.0433  335 TYR B C   
5939 O O   . TYR B 335 ? 0.492  0.325  0.2611 -0.0662 -0.0652 0.0439  335 TYR B O   
5940 C CB  . TYR B 335 ? 0.5089 0.3282 0.2969 -0.0606 -0.0612 0.0522  335 TYR B CB  
5941 C CG  . TYR B 335 ? 0.5189 0.3228 0.2994 -0.0564 -0.0646 0.061   335 TYR B CG  
5942 C CD1 . TYR B 335 ? 0.5825 0.3733 0.3418 -0.057  -0.0669 0.0679  335 TYR B CD1 
5943 C CD2 . TYR B 335 ? 0.544  0.3461 0.3381 -0.0509 -0.0657 0.0627  335 TYR B CD2 
5944 C CE1 . TYR B 335 ? 0.5997 0.3749 0.3511 -0.0516 -0.0701 0.0769  335 TYR B CE1 
5945 C CE2 . TYR B 335 ? 0.5901 0.3771 0.3777 -0.0458 -0.0681 0.0707  335 TYR B CE2 
5946 C CZ  . TYR B 335 ? 0.6278 0.4012 0.3941 -0.0456 -0.0707 0.0782  335 TYR B CZ  
5947 O OH  . TYR B 335 ? 0.6802 0.4379 0.4409 -0.039  -0.073  0.0865  335 TYR B OH  
5948 N N   . TYR B 336 ? 0.4842 0.3336 0.2859 -0.0614 -0.0645 0.0369  336 TYR B N   
5949 C CA  . TYR B 336 ? 0.4721 0.3282 0.271  -0.0638 -0.062  0.0305  336 TYR B CA  
5950 C C   . TYR B 336 ? 0.5068 0.3621 0.2965 -0.0637 -0.0697 0.0307  336 TYR B C   
5951 O O   . TYR B 336 ? 0.5042 0.3574 0.2791 -0.0674 -0.0677 0.0283  336 TYR B O   
5952 C CB  . TYR B 336 ? 0.4581 0.3246 0.2746 -0.0611 -0.0598 0.0249  336 TYR B CB  
5953 C CG  . TYR B 336 ? 0.4659 0.3375 0.2799 -0.0622 -0.0566 0.0183  336 TYR B CG  
5954 C CD1 . TYR B 336 ? 0.5046 0.3781 0.3117 -0.0653 -0.0487 0.0148  336 TYR B CD1 
5955 C CD2 . TYR B 336 ? 0.476  0.3499 0.2938 -0.0604 -0.0609 0.0154  336 TYR B CD2 
5956 C CE1 . TYR B 336 ? 0.4733 0.3503 0.2771 -0.0652 -0.0455 0.0089  336 TYR B CE1 
5957 C CE2 . TYR B 336 ? 0.4868 0.3622 0.3004 -0.0611 -0.0573 0.0094  336 TYR B CE2 
5958 C CZ  . TYR B 336 ? 0.4923 0.3692 0.2991 -0.0628 -0.0497 0.0062  336 TYR B CZ  
5959 O OH  . TYR B 336 ? 0.4972 0.3753 0.3004 -0.0622 -0.0455 0.0002  336 TYR B OH  
5960 N N   . LEU B 337 ? 0.5049 0.363  0.3033 -0.0597 -0.0782 0.0331  337 LEU B N   
5961 C CA  . LEU B 337 ? 0.5291 0.3883 0.3195 -0.0602 -0.0868 0.0331  337 LEU B CA  
5962 C C   . LEU B 337 ? 0.5702 0.4202 0.3389 -0.0619 -0.0894 0.0387  337 LEU B C   
5963 O O   . LEU B 337 ? 0.5862 0.4353 0.3402 -0.0653 -0.0914 0.0363  337 LEU B O   
5964 C CB  . LEU B 337 ? 0.5536 0.4195 0.3585 -0.0559 -0.0956 0.0352  337 LEU B CB  
5965 C CG  . LEU B 337 ? 0.5174 0.3918 0.3426 -0.0546 -0.0935 0.0302  337 LEU B CG  
5966 C CD1 . LEU B 337 ? 0.5044 0.386  0.3444 -0.0506 -0.101  0.0328  337 LEU B CD1 
5967 C CD2 . LEU B 337 ? 0.5191 0.3959 0.3416 -0.0585 -0.0916 0.0227  337 LEU B CD2 
5968 N N   . LYS B 338 ? 0.5638 0.4056 0.3292 -0.0597 -0.0887 0.0459  338 LYS B N   
5969 C CA  . LYS B 338 ? 0.5862 0.4163 0.3293 -0.0607 -0.0906 0.0528  338 LYS B CA  
5970 C C   . LYS B 338 ? 0.58   0.4054 0.3052 -0.0676 -0.0827 0.0494  338 LYS B C   
5971 O O   . LYS B 338 ? 0.5994 0.4199 0.3045 -0.0698 -0.0857 0.0513  338 LYS B O   
5972 C CB  . LYS B 338 ? 0.6125 0.4311 0.3545 -0.0576 -0.0884 0.0607  338 LYS B CB  
5973 C CG  . LYS B 338 ? 0.6387 0.4428 0.3569 -0.0569 -0.0917 0.0697  338 LYS B CG  
5974 C CD  . LYS B 338 ? 0.6673 0.4597 0.3876 -0.0509 -0.0925 0.0783  338 LYS B CD  
5975 C CE  . LYS B 338 ? 0.7579 0.5383 0.4571 -0.0465 -0.1    0.0884  338 LYS B CE  
5976 N NZ  . LYS B 338 ? 0.796  0.563  0.4976 -0.0399 -0.0995 0.0964  338 LYS B NZ  
5977 N N   . GLY B 339 ? 0.5764 0.4042 0.3088 -0.0709 -0.0723 0.0444  339 GLY B N   
5978 C CA  . GLY B 339 ? 0.5614 0.389  0.2825 -0.077  -0.0632 0.0394  339 GLY B CA  
5979 C C   . GLY B 339 ? 0.56   0.3931 0.2749 -0.0784 -0.0654 0.0329  339 GLY B C   
5980 O O   . GLY B 339 ? 0.6167 0.4451 0.3122 -0.0827 -0.0624 0.0321  339 GLY B O   
5981 N N   . LEU B 340 ? 0.5387 0.3809 0.2694 -0.0753 -0.0696 0.028   340 LEU B N   
5982 C CA  . LEU B 340 ? 0.5543 0.3998 0.2796 -0.077  -0.0714 0.0211  340 LEU B CA  
5983 C C   . LEU B 340 ? 0.5843 0.4251 0.2909 -0.0785 -0.0805 0.0244  340 LEU B C   
5984 O O   . LEU B 340 ? 0.5731 0.412  0.264  -0.0824 -0.0788 0.0197  340 LEU B O   
5985 C CB  . LEU B 340 ? 0.541  0.3945 0.2857 -0.0741 -0.074  0.0159  340 LEU B CB  
5986 C CG  . LEU B 340 ? 0.5254 0.3841 0.2863 -0.072  -0.0656 0.0117  340 LEU B CG  
5987 C CD1 . LEU B 340 ? 0.5405 0.4043 0.3178 -0.0691 -0.0691 0.0083  340 LEU B CD1 
5988 C CD2 . LEU B 340 ? 0.5527 0.412  0.3062 -0.0741 -0.056  0.0056  340 LEU B CD2 
5989 N N   . ILE B 341 ? 0.6042 0.4436 0.312  -0.075  -0.0897 0.0322  341 ILE B N   
5990 C CA  . ILE B 341 ? 0.658  0.4955 0.3492 -0.0751 -0.1    0.0359  341 ILE B CA  
5991 C C   . ILE B 341 ? 0.7178 0.5432 0.382  -0.0782 -0.0963 0.041   341 ILE B C   
5992 O O   . ILE B 341 ? 0.7394 0.563  0.384  -0.0815 -0.0996 0.0392  341 ILE B O   
5993 C CB  . ILE B 341 ? 0.6386 0.4802 0.3416 -0.0688 -0.111  0.0427  341 ILE B CB  
5994 C CG1 . ILE B 341 ? 0.6266 0.4808 0.3541 -0.0672 -0.1146 0.037   341 ILE B CG1 
5995 C CG2 . ILE B 341 ? 0.6818 0.5218 0.3661 -0.0675 -0.1224 0.0485  341 ILE B CG2 
5996 C CD1 . ILE B 341 ? 0.6416 0.5009 0.3872 -0.0604 -0.1208 0.0429  341 ILE B CD1 
5997 N N   . THR B 342 ? 0.6782 0.4947 0.3406 -0.0776 -0.0898 0.0474  342 THR B N   
5998 C CA  . THR B 342 ? 0.7043 0.5068 0.3411 -0.0802 -0.0866 0.0547  342 THR B CA  
5999 C C   . THR B 342 ? 0.7155 0.5146 0.3418 -0.0874 -0.0729 0.0497  342 THR B C   
6000 O O   . THR B 342 ? 0.7076 0.4957 0.3096 -0.0913 -0.0693 0.0539  342 THR B O   
6001 C CB  . THR B 342 ? 0.7213 0.5139 0.3607 -0.0758 -0.0871 0.0647  342 THR B CB  
6002 O OG1 . THR B 342 ? 0.683  0.4772 0.3403 -0.0774 -0.0769 0.0615  342 THR B OG1 
6003 C CG2 . THR B 342 ? 0.6878 0.4846 0.3374 -0.0675 -0.1005 0.0701  342 THR B CG2 
6004 N N   . ASN B 343 ? 0.692  0.5004 0.3359 -0.089  -0.0649 0.0412  343 ASN B N   
6005 C CA  . ASN B 343 ? 0.7662 0.5748 0.4049 -0.0949 -0.0514 0.036   343 ASN B CA  
6006 C C   . ASN B 343 ? 0.7852 0.5842 0.4179 -0.0985 -0.0429 0.0422  343 ASN B C   
6007 O O   . ASN B 343 ? 0.7638 0.5611 0.3857 -0.1049 -0.032  0.0396  343 ASN B O   
6008 C CB  . ASN B 343 ? 0.8528 0.6596 0.4695 -0.0992 -0.0494 0.0316  343 ASN B CB  
6009 C CG  . ASN B 343 ? 0.9431 0.7573 0.5645 -0.1028 -0.0368 0.0222  343 ASN B CG  
6010 O OD1 . ASN B 343 ? 1.1351 0.9459 0.7447 -0.1082 -0.0264 0.0223  343 ASN B OD1 
6011 N ND2 . ASN B 343 ? 0.9696 0.7942 0.6087 -0.0995 -0.0372 0.0141  343 ASN B ND2 
6012 N N   . GLU B 344 ? 0.7477 0.5408 0.3887 -0.0949 -0.0467 0.0494  344 GLU B N   
6013 C CA  . GLU B 344 ? 0.7703 0.5517 0.4062 -0.0986 -0.0388 0.0552  344 GLU B CA  
6014 C C   . GLU B 344 ? 0.7322 0.5244 0.3915 -0.1004 -0.0306 0.0487  344 GLU B C   
6015 O O   . GLU B 344 ? 0.6921 0.4925 0.3725 -0.095  -0.0355 0.0468  344 GLU B O   
6016 C CB  . GLU B 344 ? 0.765  0.533  0.3973 -0.093  -0.0467 0.066   344 GLU B CB  
6017 C CG  . GLU B 344 ? 0.8605 0.6167 0.4663 -0.0911 -0.0546 0.074   344 GLU B CG  
6018 C CD  . GLU B 344 ? 0.95   0.691  0.5273 -0.0987 -0.0454 0.0782  344 GLU B CD  
6019 O OE1 . GLU B 344 ? 0.9784 0.7152 0.5573 -0.1056 -0.0328 0.0765  344 GLU B OE1 
6020 O OE2 . GLU B 344 ? 1.025  0.759  0.578  -0.0985 -0.0504 0.0826  344 GLU B OE2 
6021 N N   . LYS B 345 ? 0.6725 0.4653 0.3279 -0.1083 -0.0181 0.0454  345 LYS B N   
6022 C CA  . LYS B 345 ? 0.6752 0.4785 0.3513 -0.1107 -0.0105 0.0398  345 LYS B CA  
6023 C C   . LYS B 345 ? 0.6699 0.4648 0.3554 -0.1081 -0.0135 0.0453  345 LYS B C   
6024 O O   . LYS B 345 ? 0.6097 0.4163 0.3171 -0.1057 -0.0135 0.0404  345 LYS B O   
6025 C CB  . LYS B 345 ? 0.6759 0.4799 0.3446 -0.1208 0.0032  0.0367  345 LYS B CB  
6026 C CG  . LYS B 345 ? 0.6844 0.5022 0.3516 -0.123  0.0088  0.0284  345 LYS B CG  
6027 C CD  . LYS B 345 ? 0.7013 0.5195 0.36   -0.1336 0.0228  0.0261  345 LYS B CD  
6028 C CE  . LYS B 345 ? 0.6879 0.5239 0.3516 -0.1343 0.0292  0.0165  345 LYS B CE  
6029 N NZ  . LYS B 345 ? 0.7038 0.5411 0.3597 -0.1452 0.043   0.0144  345 LYS B NZ  
6030 N N   . GLU B 346 ? 0.6348 0.4093 0.3034 -0.1078 -0.0161 0.0552  346 GLU B N   
6031 C CA  . GLU B 346 ? 0.6804 0.4441 0.3562 -0.1045 -0.0184 0.0607  346 GLU B CA  
6032 C C   . GLU B 346 ? 0.6239 0.4002 0.323  -0.0954 -0.0275 0.058   346 GLU B C   
6033 O O   . GLU B 346 ? 0.5724 0.3516 0.2881 -0.0947 -0.0253 0.0557  346 GLU B O   
6034 C CB  . GLU B 346 ? 0.6949 0.4343 0.3478 -0.1026 -0.0216 0.0725  346 GLU B CB  
6035 C CG  . GLU B 346 ? 0.7238 0.4499 0.3834 -0.0973 -0.0242 0.0786  346 GLU B CG  
6036 C CD  . GLU B 346 ? 0.7338 0.4559 0.403  -0.1043 -0.0133 0.0748  346 GLU B CD  
6037 O OE1 . GLU B 346 ? 0.7327 0.456  0.3964 -0.1151 -0.0023 0.0705  346 GLU B OE1 
6038 O OE2 . GLU B 346 ? 0.7068 0.4268 0.3905 -0.0997 -0.0154 0.0751  346 GLU B OE2 
6039 N N   . ALA B 347 ? 0.584  0.3671 0.2835 -0.0892 -0.0375 0.0582  347 ALA B N   
6040 C CA  . ALA B 347 ? 0.5834 0.3772 0.3036 -0.0814 -0.0456 0.0562  347 ALA B CA  
6041 C C   . ALA B 347 ? 0.5602 0.371  0.3008 -0.0828 -0.0404 0.0467  347 ALA B C   
6042 O O   . ALA B 347 ? 0.5527 0.369  0.3112 -0.0788 -0.0423 0.0453  347 ALA B O   
6043 C CB  . ALA B 347 ? 0.6173 0.4155 0.3332 -0.0764 -0.0565 0.0574  347 ALA B CB  
6044 N N   . PHE B 348 ? 0.5086 0.3285 0.2466 -0.0877 -0.0341 0.0402  348 PHE B N   
6045 C CA  . PHE B 348 ? 0.4966 0.3328 0.2529 -0.0879 -0.0292 0.0318  348 PHE B CA  
6046 C C   . PHE B 348 ? 0.5087 0.3457 0.2736 -0.092  -0.0219 0.0305  348 PHE B C   
6047 O O   . PHE B 348 ? 0.5049 0.3523 0.2877 -0.0891 -0.0222 0.0265  348 PHE B O   
6048 C CB  . PHE B 348 ? 0.517  0.3625 0.2682 -0.0911 -0.0238 0.0253  348 PHE B CB  
6049 C CG  . PHE B 348 ? 0.5089 0.3562 0.2556 -0.0869 -0.0307 0.0238  348 PHE B CG  
6050 C CD1 . PHE B 348 ? 0.5118 0.3651 0.2727 -0.0805 -0.0378 0.0222  348 PHE B CD1 
6051 C CD2 . PHE B 348 ? 0.5509 0.3926 0.2776 -0.0904 -0.0297 0.024   348 PHE B CD2 
6052 C CE1 . PHE B 348 ? 0.5287 0.3827 0.2849 -0.0783 -0.0435 0.0201  348 PHE B CE1 
6053 C CE2 . PHE B 348 ? 0.5678 0.4105 0.2892 -0.0877 -0.0358 0.0217  348 PHE B CE2 
6054 C CZ  . PHE B 348 ? 0.5647 0.4136 0.3013 -0.082  -0.0425 0.0194  348 PHE B CZ  
6055 N N   . PHE B 349 ? 0.513  0.3375 0.2645 -0.099  -0.0156 0.0339  349 PHE B N   
6056 C CA  . PHE B 349 ? 0.5096 0.3324 0.2677 -0.1044 -0.0086 0.0324  349 PHE B CA  
6057 C C   . PHE B 349 ? 0.5347 0.3511 0.303  -0.0984 -0.0142 0.0358  349 PHE B C   
6058 O O   . PHE B 349 ? 0.5141 0.3391 0.2973 -0.0992 -0.0115 0.031   349 PHE B O   
6059 C CB  . PHE B 349 ? 0.5639 0.3702 0.3032 -0.1136 -0.0004 0.0364  349 PHE B CB  
6060 C CG  . PHE B 349 ? 0.5922 0.4054 0.3218 -0.1216 0.0081  0.0322  349 PHE B CG  
6061 C CD1 . PHE B 349 ? 0.5929 0.4288 0.3368 -0.1242 0.0135  0.0226  349 PHE B CD1 
6062 C CD2 . PHE B 349 ? 0.6253 0.4216 0.3311 -0.1271 0.0121  0.0381  349 PHE B CD2 
6063 C CE1 . PHE B 349 ? 0.6032 0.446  0.339  -0.1313 0.0222  0.0185  349 PHE B CE1 
6064 C CE2 . PHE B 349 ? 0.6414 0.4437 0.3378 -0.1351 0.0212  0.0341  349 PHE B CE2 
6065 C CZ  . PHE B 349 ? 0.6278 0.4541 0.3401 -0.137  0.0262  0.024   349 PHE B CZ  
6066 N N   . LYS B 350 ? 0.5364 0.3387 0.2967 -0.0923 -0.022  0.0439  350 LYS B N   
6067 C CA  . LYS B 350 ? 0.5614 0.359  0.3325 -0.0852 -0.0275 0.047   350 LYS B CA  
6068 C C   . LYS B 350 ? 0.4961 0.3123 0.288  -0.0797 -0.0317 0.0412  350 LYS B C   
6069 O O   . LYS B 350 ? 0.4761 0.2942 0.2807 -0.0777 -0.031  0.0394  350 LYS B O   
6070 C CB  . LYS B 350 ? 0.6277 0.4122 0.3893 -0.0778 -0.0364 0.0562  350 LYS B CB  
6071 C CG  . LYS B 350 ? 0.7449 0.5065 0.4849 -0.0803 -0.034  0.0646  350 LYS B CG  
6072 C CD  . LYS B 350 ? 0.8693 0.6131 0.609  -0.0751 -0.035  0.0712  350 LYS B CD  
6073 C CE  . LYS B 350 ? 0.9453 0.6694 0.6651 -0.0699 -0.0401 0.0824  350 LYS B CE  
6074 N NZ  . LYS B 350 ? 0.9653 0.6841 0.6629 -0.0747 -0.0394 0.0857  350 LYS B NZ  
6075 N N   . SER B 351 ? 0.4707 0.2983 0.2642 -0.0773 -0.0357 0.0386  351 SER B N   
6076 C CA  . SER B 351 ? 0.4896 0.3327 0.3003 -0.0725 -0.0388 0.0334  351 SER B CA  
6077 C C   . SER B 351 ? 0.4738 0.3284 0.2965 -0.0753 -0.0319 0.0267  351 SER B C   
6078 O O   . SER B 351 ? 0.4423 0.3025 0.2788 -0.0715 -0.0333 0.0249  351 SER B O   
6079 C CB  . SER B 351 ? 0.4659 0.3163 0.2732 -0.0712 -0.0421 0.031   351 SER B CB  
6080 O OG  . SER B 351 ? 0.4453 0.3078 0.2678 -0.0665 -0.0444 0.0266  351 SER B OG  
6081 N N   . VAL B 352 ? 0.4661 0.3243 0.283  -0.0824 -0.0244 0.0231  352 VAL B N   
6082 C CA  . VAL B 352 ? 0.443  0.3139 0.2699 -0.0864 -0.0177 0.0164  352 VAL B CA  
6083 C C   . VAL B 352 ? 0.4481 0.3119 0.2801 -0.0879 -0.0163 0.0172  352 VAL B C   
6084 O O   . VAL B 352 ? 0.4314 0.3062 0.2766 -0.086  -0.0161 0.0129  352 VAL B O   
6085 C CB  . VAL B 352 ? 0.4628 0.3398 0.283  -0.0945 -0.0095 0.0123  352 VAL B CB  
6086 C CG1 . VAL B 352 ? 0.4721 0.3645 0.3044 -0.0988 -0.0036 0.0051  352 VAL B CG1 
6087 C CG2 . VAL B 352 ? 0.4541 0.3402 0.2713 -0.0919 -0.0101 0.0097  352 VAL B CG2 
6088 N N   . GLU B 353 ? 0.4581 0.3027 0.2784 -0.091  -0.0151 0.023   353 GLU B N   
6089 C CA  . GLU B 353 ? 0.46   0.2943 0.2826 -0.0935 -0.012  0.0233  353 GLU B CA  
6090 C C   . GLU B 353 ? 0.4921 0.3276 0.327  -0.0846 -0.0182 0.0244  353 GLU B C   
6091 O O   . GLU B 353 ? 0.4364 0.2751 0.2804 -0.0856 -0.0156 0.0203  353 GLU B O   
6092 C CB  . GLU B 353 ? 0.4721 0.2823 0.2774 -0.0974 -0.0092 0.0303  353 GLU B CB  
6093 C CG  . GLU B 353 ? 0.4872 0.2958 0.2813 -0.1087 -0.0003 0.0281  353 GLU B CG  
6094 C CD  . GLU B 353 ? 0.5703 0.3534 0.3433 -0.1124 0.0027  0.0362  353 GLU B CD  
6095 O OE1 . GLU B 353 ? 0.5869 0.3592 0.3504 -0.1051 -0.0044 0.0441  353 GLU B OE1 
6096 O OE2 . GLU B 353 ? 0.5777 0.3548 0.3431 -0.1234 0.0122  0.034   353 GLU B OE2 
6097 N N   . TYR B 354 ? 0.4847 0.3184 0.3196 -0.0766 -0.0261 0.0293  354 TYR B N   
6098 C CA  . TYR B 354 ? 0.4543 0.2907 0.3017 -0.0685 -0.0315 0.0302  354 TYR B CA  
6099 C C   . TYR B 354 ? 0.4323 0.2873 0.2935 -0.067  -0.031  0.0235  354 TYR B C   
6100 O O   . TYR B 354 ? 0.4518 0.3089 0.3229 -0.064  -0.0311 0.0219  354 TYR B O   
6101 C CB  . TYR B 354 ? 0.4734 0.3057 0.3186 -0.0614 -0.0399 0.0364  354 TYR B CB  
6102 C CG  . TYR B 354 ? 0.518  0.3311 0.3531 -0.0591 -0.0417 0.0441  354 TYR B CG  
6103 C CD1 . TYR B 354 ? 0.5334 0.3375 0.3741 -0.0555 -0.0406 0.0458  354 TYR B CD1 
6104 C CD2 . TYR B 354 ? 0.5706 0.3742 0.3896 -0.06   -0.0442 0.0498  354 TYR B CD2 
6105 C CE1 . TYR B 354 ? 0.5848 0.3699 0.416  -0.0519 -0.042  0.0532  354 TYR B CE1 
6106 C CE2 . TYR B 354 ? 0.5835 0.3688 0.392  -0.0565 -0.0462 0.0578  354 TYR B CE2 
6107 C CZ  . TYR B 354 ? 0.6109 0.3867 0.4258 -0.052  -0.0451 0.0597  354 TYR B CZ  
6108 O OH  . TYR B 354 ? 0.6642 0.4206 0.4687 -0.0473 -0.0466 0.0679  354 TYR B OH  
6109 N N   . PHE B 355 ? 0.4228 0.2903 0.2841 -0.0684 -0.0304 0.0199  355 PHE B N   
6110 C CA  . PHE B 355 ? 0.4062 0.2904 0.2792 -0.066  -0.0299 0.0143  355 PHE B CA  
6111 C C   . PHE B 355 ? 0.4158 0.307  0.2933 -0.0708 -0.0241 0.0088  355 PHE B C   
6112 O O   . PHE B 355 ? 0.4088 0.3087 0.296  -0.0676 -0.0246 0.0058  355 PHE B O   
6113 C CB  . PHE B 355 ? 0.4148 0.3095 0.2869 -0.0646 -0.0305 0.0119  355 PHE B CB  
6114 C CG  . PHE B 355 ? 0.419  0.3097 0.2898 -0.0594 -0.0369 0.0155  355 PHE B CG  
6115 C CD1 . PHE B 355 ? 0.4003 0.2905 0.2799 -0.0539 -0.0414 0.0174  355 PHE B CD1 
6116 C CD2 . PHE B 355 ? 0.4237 0.3118 0.2845 -0.0608 -0.038  0.0164  355 PHE B CD2 
6117 C CE1 . PHE B 355 ? 0.4136 0.3021 0.2931 -0.0505 -0.047  0.0197  355 PHE B CE1 
6118 C CE2 . PHE B 355 ? 0.4004 0.2858 0.26   -0.0572 -0.044  0.0185  355 PHE B CE2 
6119 C CZ  . PHE B 355 ? 0.4158 0.3021 0.2853 -0.0524 -0.0485 0.0199  355 PHE B CZ  
6120 N N   . LYS B 356 ? 0.4305 0.3175 0.3007 -0.0791 -0.0185 0.0074  356 LYS B N   
6121 C CA  . LYS B 356 ? 0.4414 0.3335 0.3154 -0.0855 -0.0131 0.0017  356 LYS B CA  
6122 C C   . LYS B 356 ? 0.4727 0.3537 0.3496 -0.0839 -0.0135 0.0029  356 LYS B C   
6123 O O   . LYS B 356 ? 0.4304 0.3207 0.3153 -0.0843 -0.0122 -0.0024 356 LYS B O   
6124 C CB  . LYS B 356 ? 0.5008 0.3868 0.3647 -0.096  -0.0063 0.0008  356 LYS B CB  
6125 C CG  . LYS B 356 ? 0.5029 0.4064 0.3678 -0.0992 -0.0034 -0.0038 356 LYS B CG  
6126 C CD  . LYS B 356 ? 0.5432 0.4672 0.419  -0.1034 0.0001  -0.0124 356 LYS B CD  
6127 C CE  . LYS B 356 ? 0.5064 0.4511 0.3865 -0.1025 0.0014  -0.0166 356 LYS B CE  
6128 N NZ  . LYS B 356 ? 0.4505 0.4156 0.3399 -0.1084 0.0054  -0.025  356 LYS B NZ  
6129 N N   . ALA B 357 ? 0.4547 0.3163 0.3248 -0.0815 -0.0154 0.0096  357 ALA B N   
6130 C CA  . ALA B 357 ? 0.4987 0.3482 0.3714 -0.079  -0.0151 0.0107  357 ALA B CA  
6131 C C   . ALA B 357 ? 0.4707 0.3304 0.3557 -0.0708 -0.0194 0.0096  357 ALA B C   
6132 O O   . ALA B 357 ? 0.4607 0.3208 0.351  -0.0708 -0.0172 0.0058  357 ALA B O   
6133 C CB  . ALA B 357 ? 0.5171 0.3447 0.3802 -0.0763 -0.0167 0.0188  357 ALA B CB  
6134 N N   . SER B 358 ? 0.4227 0.2902 0.3114 -0.0644 -0.025  0.0123  358 SER B N   
6135 C CA  . SER B 358 ? 0.4014 0.2786 0.301  -0.0577 -0.0281 0.0112  358 SER B CA  
6136 C C   . SER B 358 ? 0.4166 0.3114 0.3217 -0.0587 -0.0262 0.0049  358 SER B C   
6137 O O   . SER B 358 ? 0.3866 0.2881 0.2989 -0.0537 -0.0277 0.004   358 SER B O   
6138 C CB  . SER B 358 ? 0.4545 0.3324 0.356  -0.0517 -0.0341 0.0159  358 SER B CB  
6139 O OG  . SER B 358 ? 0.5074 0.3909 0.4039 -0.0534 -0.0352 0.0157  358 SER B OG  
6140 N N   . GLN B 359 ? 0.4114 0.3144 0.3132 -0.0649 -0.0228 0.0007  359 GLN B N   
6141 C CA  . GLN B 359 ? 0.4176 0.3397 0.3244 -0.0651 -0.0217 -0.0051 359 GLN B CA  
6142 C C   . GLN B 359 ? 0.4684 0.3985 0.3787 -0.0574 -0.0257 -0.0031 359 GLN B C   
6143 O O   . GLN B 359 ? 0.3757 0.3159 0.2915 -0.0526 -0.0266 -0.005  359 GLN B O   
6144 C CB  . GLN B 359 ? 0.4251 0.3528 0.3361 -0.0671 -0.0193 -0.0104 359 GLN B CB  
6145 C CG  . GLN B 359 ? 0.4351 0.3831 0.349  -0.0706 -0.0175 -0.0172 359 GLN B CG  
6146 C CD  . GLN B 359 ? 0.4646 0.4196 0.3819 -0.0722 -0.0162 -0.0227 359 GLN B CD  
6147 O OE1 . GLN B 359 ? 0.5037 0.4523 0.4187 -0.0798 -0.0125 -0.0265 359 GLN B OE1 
6148 N NE2 . GLN B 359 ? 0.4879 0.4534 0.4093 -0.0648 -0.0192 -0.0229 359 GLN B NE2 
6149 N N   . ASP B 360 ? 0.4192 0.3434 0.3248 -0.0565 -0.0276 0.0006  360 ASP B N   
6150 C CA  . ASP B 360 ? 0.418  0.3471 0.325  -0.0507 -0.0305 0.0018  360 ASP B CA  
6151 C C   . ASP B 360 ? 0.4362 0.3753 0.34   -0.0526 -0.028  -0.0015 360 ASP B C   
6152 O O   . ASP B 360 ? 0.4457 0.3793 0.3425 -0.0557 -0.0275 -0.0001 360 ASP B O   
6153 C CB  . ASP B 360 ? 0.4082 0.3254 0.3129 -0.0483 -0.0346 0.0071  360 ASP B CB  
6154 C CG  . ASP B 360 ? 0.3965 0.3161 0.3023 -0.0434 -0.0373 0.0079  360 ASP B CG  
6155 O OD1 . ASP B 360 ? 0.4104 0.3394 0.3173 -0.041  -0.0355 0.0049  360 ASP B OD1 
6156 O OD2 . ASP B 360 ? 0.4349 0.347  0.3406 -0.0418 -0.0412 0.0114  360 ASP B OD2 
6157 N N   . LYS B 361 ? 0.3699 0.3241 0.2788 -0.0495 -0.0268 -0.0054 361 LYS B N   
6158 C CA  . LYS B 361 ? 0.3802 0.3467 0.2884 -0.0495 -0.0244 -0.0089 361 LYS B CA  
6159 C C   . LYS B 361 ? 0.3823 0.3475 0.2887 -0.0427 -0.0259 -0.0074 361 LYS B C   
6160 O O   . LYS B 361 ? 0.4247 0.3988 0.3302 -0.0416 -0.0235 -0.0103 361 LYS B O   
6161 C CB  . LYS B 361 ? 0.4072 0.3928 0.3223 -0.0483 -0.0228 -0.0141 361 LYS B CB  
6162 C CG  . LYS B 361 ? 0.481  0.4698 0.3977 -0.0565 -0.0205 -0.0175 361 LYS B CG  
6163 C CD  . LYS B 361 ? 0.5505 0.5628 0.4739 -0.0563 -0.0193 -0.0239 361 LYS B CD  
6164 C CE  . LYS B 361 ? 0.6464 0.6661 0.5712 -0.067  -0.0155 -0.0295 361 LYS B CE  
6165 N NZ  . LYS B 361 ? 0.7261 0.7348 0.6497 -0.0709 -0.0157 -0.0294 361 LYS B NZ  
6166 N N   . LEU B 362 ? 0.3751 0.3298 0.2814 -0.0384 -0.0293 -0.0035 362 LEU B N   
6167 C CA  . LEU B 362 ? 0.4142 0.3646 0.3177 -0.0334 -0.0303 -0.0025 362 LEU B CA  
6168 C C   . LEU B 362 ? 0.4145 0.3538 0.31   -0.0379 -0.0314 -0.0009 362 LEU B C   
6169 O O   . LEU B 362 ? 0.4394 0.3798 0.3294 -0.038  -0.0294 -0.0029 362 LEU B O   
6170 C CB  . LEU B 362 ? 0.4047 0.3493 0.3119 -0.0285 -0.0328 0.0004  362 LEU B CB  
6171 C CG  . LEU B 362 ? 0.4639 0.4009 0.3682 -0.0243 -0.0335 0.0014  362 LEU B CG  
6172 C CD1 . LEU B 362 ? 0.5114 0.4561 0.4146 -0.018  -0.0305 -0.0013 362 LEU B CD1 
6173 C CD2 . LEU B 362 ? 0.5062 0.4359 0.414  -0.0222 -0.0354 0.0044  362 LEU B CD2 
6174 N N   . SER B 363 ? 0.4266 0.3558 0.321  -0.0411 -0.0345 0.0027  363 SER B N   
6175 C CA  . SER B 363 ? 0.4212 0.3398 0.3075 -0.0441 -0.0372 0.0052  363 SER B CA  
6176 C C   . SER B 363 ? 0.4058 0.324  0.2833 -0.0499 -0.0342 0.0043  363 SER B C   
6177 O O   . SER B 363 ? 0.4073 0.3194 0.2757 -0.0517 -0.0353 0.005   363 SER B O   
6178 C CB  . SER B 363 ? 0.434  0.344  0.3224 -0.0446 -0.0418 0.0096  363 SER B CB  
6179 O OG  . SER B 363 ? 0.4076 0.3185 0.3048 -0.0403 -0.0437 0.0103  363 SER B OG  
6180 N N   . ILE B 364 ? 0.4035 0.3287 0.2831 -0.0532 -0.03   0.0021  364 ILE B N   
6181 C CA  . ILE B 364 ? 0.4059 0.3306 0.2775 -0.0601 -0.0258 0.0011  364 ILE B CA  
6182 C C   . ILE B 364 ? 0.4232 0.3531 0.2891 -0.0601 -0.0227 -0.0021 364 ILE B C   
6183 O O   . ILE B 364 ? 0.4121 0.3376 0.2678 -0.0656 -0.02   -0.0018 364 ILE B O   
6184 C CB  . ILE B 364 ? 0.4264 0.3595 0.3033 -0.0646 -0.0214 -0.0019 364 ILE B CB  
6185 C CG1 . ILE B 364 ? 0.4054 0.332  0.2724 -0.074  -0.0167 -0.0014 364 ILE B CG1 
6186 C CG2 . ILE B 364 ? 0.4106 0.3631 0.2964 -0.0616 -0.0185 -0.0077 364 ILE B CG2 
6187 C CD1 . ILE B 364 ? 0.4082 0.3399 0.2801 -0.0801 -0.0123 -0.0046 364 ILE B CD1 
6188 N N   . LYS B 365 ? 0.4177 0.3559 0.2891 -0.0535 -0.0226 -0.0051 365 LYS B N   
6189 C CA  . LYS B 365 ? 0.4797 0.422  0.3462 -0.0519 -0.0192 -0.0086 365 LYS B CA  
6190 C C   . LYS B 365 ? 0.4609 0.3892 0.3144 -0.0545 -0.0214 -0.0065 365 LYS B C   
6191 O O   . LYS B 365 ? 0.475  0.4043 0.3203 -0.0569 -0.0174 -0.0091 365 LYS B O   
6192 C CB  . LYS B 365 ? 0.5803 0.5284 0.4532 -0.0428 -0.0195 -0.011  365 LYS B CB  
6193 C CG  . LYS B 365 ? 0.8616 0.8249 0.7463 -0.0378 -0.0182 -0.0131 365 LYS B CG  
6194 C CD  . LYS B 365 ? 0.953  0.9171 0.8416 -0.0277 -0.0193 -0.0132 365 LYS B CD  
6195 C CE  . LYS B 365 ? 0.9655 0.9369 0.8632 -0.0235 -0.0214 -0.012  365 LYS B CE  
6196 N NZ  . LYS B 365 ? 0.8025 0.7764 0.7031 -0.0131 -0.0214 -0.0118 365 LYS B NZ  
6197 N N   . MET B 366 ? 0.4168 0.3336 0.2685 -0.0541 -0.0277 -0.0021 366 MET B N   
6198 C CA  . MET B 366 ? 0.4716 0.3775 0.3113 -0.0562 -0.0309 -0.0006 366 MET B CA  
6199 C C   . MET B 366 ? 0.485  0.3862 0.3115 -0.0631 -0.0286 0.0009  366 MET B C   
6200 O O   . MET B 366 ? 0.46   0.3602 0.276  -0.0649 -0.0256 -0.0018 366 MET B O   
6201 C CB  . MET B 366 ? 0.482  0.3798 0.324  -0.0549 -0.0385 0.0035  366 MET B CB  
6202 C CG  . MET B 366 ? 0.5088 0.4089 0.3619 -0.0493 -0.0403 0.0023  366 MET B CG  
6203 S SD  . MET B 366 ? 0.5677 0.4603 0.4235 -0.0496 -0.0487 0.0066  366 MET B SD  
6204 C CE  . MET B 366 ? 0.6373 0.5283 0.4953 -0.0514 -0.0509 0.0121  366 MET B CE  
6205 N N   . PRO B 367 ? 0.4199 0.3164 0.2449 -0.067  -0.0292 0.0054  367 PRO B N   
6206 C CA  . PRO B 367 ? 0.4379 0.3274 0.2483 -0.0737 -0.026  0.0076  367 PRO B CA  
6207 C C   . PRO B 367 ? 0.4515 0.3508 0.2608 -0.0778 -0.0168 0.0024  367 PRO B C   
6208 O O   . PRO B 367 ? 0.4724 0.3669 0.2674 -0.0829 -0.0132 0.0027  367 PRO B O   
6209 C CB  . PRO B 367 ? 0.4347 0.3155 0.2458 -0.0755 -0.0283 0.0134  367 PRO B CB  
6210 C CG  . PRO B 367 ? 0.4202 0.3096 0.2491 -0.0713 -0.0291 0.0115  367 PRO B CG  
6211 C CD  . PRO B 367 ? 0.3906 0.285  0.2253 -0.0653 -0.0328 0.009   367 PRO B CD  
6212 N N   . LEU B 368 ? 0.4458 0.3596 0.2695 -0.0756 -0.0132 -0.0022 368 LEU B N   
6213 C CA  . LEU B 368 ? 0.4564 0.3839 0.2822 -0.0789 -0.0047 -0.0079 368 LEU B CA  
6214 C C   . LEU B 368 ? 0.4562 0.3869 0.2754 -0.0766 -0.0016 -0.012  368 LEU B C   
6215 O O   . LEU B 368 ? 0.4542 0.3881 0.2655 -0.082  0.0053  -0.0145 368 LEU B O   
6216 C CB  . LEU B 368 ? 0.4338 0.3788 0.277  -0.076  -0.0028 -0.0121 368 LEU B CB  
6217 C CG  . LEU B 368 ? 0.4377 0.381  0.286  -0.0808 -0.0032 -0.0101 368 LEU B CG  
6218 C CD1 . LEU B 368 ? 0.4181 0.3796 0.2827 -0.0768 -0.0029 -0.0146 368 LEU B CD1 
6219 C CD2 . LEU B 368 ? 0.4282 0.3674 0.2682 -0.0915 0.0032  -0.0099 368 LEU B CD2 
6220 N N   . ILE B 369 ? 0.465  0.3942 0.2869 -0.0689 -0.0059 -0.013  369 ILE B N   
6221 C CA  . ILE B 369 ? 0.5213 0.4494 0.3353 -0.0663 -0.0034 -0.017  369 ILE B CA  
6222 C C   . ILE B 369 ? 0.515  0.4306 0.3095 -0.0729 -0.003  -0.015  369 ILE B C   
6223 O O   . ILE B 369 ? 0.5225 0.4412 0.3087 -0.0751 0.0036  -0.0192 369 ILE B O   
6224 C CB  . ILE B 369 ? 0.5839 0.5075 0.4023 -0.0583 -0.0085 -0.0176 369 ILE B CB  
6225 C CG1 . ILE B 369 ? 0.6653 0.6022 0.5001 -0.0505 -0.0069 -0.0203 369 ILE B CG1 
6226 C CG2 . ILE B 369 ? 0.5826 0.4985 0.3888 -0.0572 -0.0071 -0.0213 369 ILE B CG2 
6227 C CD1 . ILE B 369 ? 0.7027 0.6324 0.5423 -0.0435 -0.0121 -0.0191 369 ILE B CD1 
6228 N N   . GLN B 370 ? 0.5068 0.4091 0.2936 -0.0758 -0.0099 -0.0086 370 GLN B N   
6229 C CA  . GLN B 370 ? 0.5334 0.4234 0.3    -0.0811 -0.011  -0.0058 370 GLN B CA  
6230 C C   . GLN B 370 ? 0.5519 0.4425 0.3096 -0.0889 -0.0028 -0.0051 370 GLN B C   
6231 O O   . GLN B 370 ? 0.5464 0.4333 0.2881 -0.0929 0.0017  -0.0066 370 GLN B O   
6232 C CB  . GLN B 370 ? 0.5392 0.4166 0.3006 -0.0809 -0.021  0.0013  370 GLN B CB  
6233 C CG  . GLN B 370 ? 0.5445 0.4211 0.3132 -0.0752 -0.0286 0.0001  370 GLN B CG  
6234 C CD  . GLN B 370 ? 0.5496 0.4251 0.3101 -0.0742 -0.0274 -0.006  370 GLN B CD  
6235 O OE1 . GLN B 370 ? 0.5815 0.4612 0.3515 -0.0694 -0.0262 -0.0108 370 GLN B OE1 
6236 N NE2 . GLN B 370 ? 0.508  0.3773 0.2497 -0.0789 -0.0261 -0.0062 370 GLN B NE2 
6237 N N   . LEU B 371 ? 0.5007 0.3959 0.2681 -0.0916 -0.0001 -0.0034 371 LEU B N   
6238 C CA  . LEU B 371 ? 0.52   0.4162 0.2804 -0.1003 0.0089  -0.0035 371 LEU B CA  
6239 C C   . LEU B 371 ? 0.4938 0.4056 0.2569 -0.1016 0.0185  -0.0115 371 LEU B C   
6240 O O   . LEU B 371 ? 0.5683 0.4775 0.3176 -0.1089 0.026   -0.0121 371 LEU B O   
6241 C CB  . LEU B 371 ? 0.5134 0.4112 0.2845 -0.1036 0.0099  -0.0014 371 LEU B CB  
6242 C CG  . LEU B 371 ? 0.5163 0.3959 0.2811 -0.1036 0.0027  0.0072  371 LEU B CG  
6243 C CD1 . LEU B 371 ? 0.4963 0.3791 0.275  -0.105  0.0037  0.0073  371 LEU B CD1 
6244 C CD2 . LEU B 371 ? 0.5365 0.3984 0.2779 -0.11   0.0048  0.0133  371 LEU B CD2 
6245 N N   . GLU B 372 ? 0.4905 0.4178 0.2701 -0.0943 0.0187  -0.0175 372 GLU B N   
6246 C CA  . GLU B 372 ? 0.5214 0.4651 0.3055 -0.093  0.0274  -0.0253 372 GLU B CA  
6247 C C   . GLU B 372 ? 0.5551 0.49   0.3211 -0.0932 0.0299  -0.0272 372 GLU B C   
6248 O O   . GLU B 372 ? 0.5433 0.4845 0.3026 -0.0978 0.0393  -0.0313 372 GLU B O   
6249 C CB  . GLU B 372 ? 0.5162 0.4754 0.3197 -0.0826 0.0257  -0.03   372 GLU B CB  
6250 C CG  . GLU B 372 ? 0.642  0.62   0.4522 -0.0793 0.0346  -0.0381 372 GLU B CG  
6251 C CD  . GLU B 372 ? 0.7152 0.7164 0.5473 -0.0723 0.0359  -0.0427 372 GLU B CD  
6252 O OE1 . GLU B 372 ? 0.8082 0.8153 0.6513 -0.0736 0.0323  -0.0406 372 GLU B OE1 
6253 O OE2 . GLU B 372 ? 0.8389 0.8531 0.6769 -0.0652 0.0407  -0.0485 372 GLU B OE2 
6254 N N   . LYS B 373 ? 0.5936 0.5148 0.3519 -0.0887 0.0216  -0.0247 373 LYS B N   
6255 C CA  . LYS B 373 ? 0.6374 0.5486 0.3768 -0.0896 0.0226  -0.0267 373 LYS B CA  
6256 C C   . LYS B 373 ? 0.6022 0.5023 0.32   -0.0993 0.0255  -0.0224 373 LYS B C   
6257 O O   . LYS B 373 ? 0.6586 0.5552 0.3603 -0.102  0.0306  -0.0256 373 LYS B O   
6258 C CB  . LYS B 373 ? 0.7067 0.6053 0.4421 -0.0848 0.0121  -0.0247 373 LYS B CB  
6259 C CG  . LYS B 373 ? 0.8031 0.7071 0.5549 -0.0756 0.0093  -0.0282 373 LYS B CG  
6260 C CD  . LYS B 373 ? 0.8762 0.7675 0.6217 -0.0728 0.0012  -0.0282 373 LYS B CD  
6261 C CE  . LYS B 373 ? 0.8601 0.7553 0.6213 -0.0641 0.0002  -0.0313 373 LYS B CE  
6262 N NZ  . LYS B 373 ? 0.9808 0.8642 0.7393 -0.0633 -0.0084 -0.03   373 LYS B NZ  
6263 N N   . MET B 374 ? 0.6152 0.5077 0.3308 -0.1041 0.0221  -0.0148 374 MET B N   
6264 C CA  . MET B 374 ? 0.6636 0.5426 0.3574 -0.1126 0.0246  -0.0091 374 MET B CA  
6265 C C   . MET B 374 ? 0.6657 0.5524 0.3594 -0.1211 0.0373  -0.0112 374 MET B C   
6266 O O   . MET B 374 ? 0.6843 0.5581 0.3611 -0.129  0.0402  -0.0053 374 MET B O   
6267 C CB  . MET B 374 ? 0.6968 0.5612 0.3872 -0.1124 0.0147  0.0005  374 MET B CB  
6268 C CG  . MET B 374 ? 0.6972 0.5544 0.3849 -0.1059 0.0025  0.0026  374 MET B CG  
6269 S SD  . MET B 374 ? 0.6983 0.5473 0.3952 -0.1025 -0.0084 0.0115  374 MET B SD  
6270 C CE  . MET B 374 ? 0.6961 0.525  0.3646 -0.1061 -0.0134 0.0213  374 MET B CE  
6271 N N   . GLY B 375 ? 0.6105 0.5181 0.3223 -0.1197 0.045   -0.0193 375 GLY B N   
6272 C CA  . GLY B 375 ? 0.5967 0.5157 0.3097 -0.1283 0.0579  -0.0231 375 GLY B CA  
6273 C C   . GLY B 375 ? 0.594  0.5204 0.3222 -0.1336 0.0601  -0.022  375 GLY B C   
6274 O O   . GLY B 375 ? 0.578  0.5137 0.3073 -0.1426 0.071   -0.0252 375 GLY B O   
6275 N N   . GLU B 376 ? 0.5797 0.5033 0.32   -0.1291 0.051   -0.0183 376 GLU B N   
6276 C CA  . GLU B 376 ? 0.5571 0.4885 0.3116 -0.1346 0.0538  -0.0188 376 GLU B CA  
6277 C C   . GLU B 376 ? 0.5224 0.4835 0.3001 -0.1324 0.0591  -0.0284 376 GLU B C   
6278 O O   . GLU B 376 ? 0.4952 0.4684 0.2822 -0.1224 0.0567  -0.0329 376 GLU B O   
6279 C CB  . GLU B 376 ? 0.5621 0.4807 0.3209 -0.1305 0.0433  -0.0123 376 GLU B CB  
6280 C CG  . GLU B 376 ? 0.5773 0.4684 0.3144 -0.1343 0.0397  -0.0024 376 GLU B CG  
6281 C CD  . GLU B 376 ? 0.689  0.5678 0.4105 -0.1467 0.049   0.001   376 GLU B CD  
6282 O OE1 . GLU B 376 ? 0.7014 0.563  0.3994 -0.1495 0.0499  0.0066  376 GLU B OE1 
6283 O OE2 . GLU B 376 ? 0.6812 0.5676 0.413  -0.1542 0.0558  -0.0022 376 GLU B OE2 
6284 N N   . ASN B 377 ? 0.5162 0.4887 0.3031 -0.1419 0.0663  -0.0315 377 ASN B N   
6285 C CA  . ASN B 377 ? 0.5131 0.5169 0.3214 -0.1418 0.0723  -0.041  377 ASN B CA  
6286 C C   . ASN B 377 ? 0.5007 0.5175 0.328  -0.1286 0.063   -0.043  377 ASN B C   
6287 O O   . ASN B 377 ? 0.5088 0.5198 0.3418 -0.1279 0.0564  -0.0398 377 ASN B O   
6288 C CB  . ASN B 377 ? 0.5276 0.5396 0.3424 -0.1554 0.0798  -0.0437 377 ASN B CB  
6289 C CG  . ASN B 377 ? 0.5437 0.5917 0.3809 -0.1565 0.0863  -0.0543 377 ASN B CG  
6290 O OD1 . ASN B 377 ? 0.5747 0.6425 0.4267 -0.1443 0.0826  -0.0588 377 ASN B OD1 
6291 N ND2 . ASN B 377 ? 0.5831 0.6404 0.423  -0.1711 0.0964  -0.0584 377 ASN B ND2 
6292 N N   . PRO B 378 ? 0.5116 0.5456 0.3489 -0.1178 0.0629  -0.0484 378 PRO B N   
6293 C CA  . PRO B 378 ? 0.5008 0.5443 0.3536 -0.1048 0.0543  -0.0493 378 PRO B CA  
6294 C C   . PRO B 378 ? 0.4422 0.5052 0.314  -0.1065 0.053   -0.0524 378 PRO B C   
6295 O O   . PRO B 378 ? 0.4143 0.4761 0.2937 -0.0991 0.0446  -0.0502 378 PRO B O   
6296 C CB  . PRO B 378 ? 0.5407 0.5995 0.399  -0.0945 0.0579  -0.0552 378 PRO B CB  
6297 C CG  . PRO B 378 ? 0.5478 0.5945 0.387  -0.1007 0.0652  -0.0553 378 PRO B CG  
6298 C CD  . PRO B 378 ? 0.5702 0.613  0.4026 -0.1168 0.0713  -0.0535 378 PRO B CD  
6299 N N   . ARG B 379 ? 0.4106 0.4929 0.29   -0.1168 0.0616  -0.0584 379 ARG B N   
6300 C CA  . ARG B 379 ? 0.3955 0.4995 0.2931 -0.1196 0.0606  -0.0629 379 ARG B CA  
6301 C C   . ARG B 379 ? 0.393  0.4764 0.285  -0.1257 0.0552  -0.0573 379 ARG B C   
6302 O O   . ARG B 379 ? 0.3658 0.4571 0.2692 -0.121  0.0487  -0.0581 379 ARG B O   
6303 C CB  . ARG B 379 ? 0.4124 0.5416 0.3189 -0.1307 0.0717  -0.0711 379 ARG B CB  
6304 C CG  . ARG B 379 ? 0.3926 0.5492 0.319  -0.1355 0.0714  -0.0779 379 ARG B CG  
6305 C CD  . ARG B 379 ? 0.3833 0.5622 0.327  -0.1192 0.063   -0.0805 379 ARG B CD  
6306 N NE  . ARG B 379 ? 0.3551 0.5688 0.3196 -0.1219 0.063   -0.0886 379 ARG B NE  
6307 C CZ  . ARG B 379 ? 0.35   0.5948 0.3278 -0.1281 0.0709  -0.0974 379 ARG B CZ  
6308 N NH1 . ARG B 379 ? 0.3994 0.647  0.3729 -0.1316 0.0807  -0.0996 379 ARG B NH1 
6309 N NH2 . ARG B 379 ? 0.3396 0.6155 0.3359 -0.1312 0.0694  -0.1047 379 ARG B NH2 
6310 N N   . LEU B 380 ? 0.3946 0.4514 0.2683 -0.1354 0.0581  -0.0517 380 LEU B N   
6311 C CA  . LEU B 380 ? 0.4154 0.4494 0.2819 -0.1403 0.0538  -0.0457 380 LEU B CA  
6312 C C   . LEU B 380 ? 0.4149 0.4348 0.2801 -0.1275 0.0425  -0.0396 380 LEU B C   
6313 O O   . LEU B 380 ? 0.3902 0.4072 0.2616 -0.1261 0.0372  -0.0384 380 LEU B O   
6314 C CB  . LEU B 380 ? 0.4659 0.4744 0.3119 -0.1524 0.06    -0.0404 380 LEU B CB  
6315 C CG  . LEU B 380 ? 0.4975 0.5163 0.3442 -0.1683 0.0724  -0.0461 380 LEU B CG  
6316 C CD1 . LEU B 380 ? 0.5532 0.5398 0.3764 -0.1789 0.0773  -0.0386 380 LEU B CD1 
6317 C CD2 . LEU B 380 ? 0.4986 0.5372 0.363  -0.1752 0.0739  -0.0534 380 LEU B CD2 
6318 N N   . LEU B 381 ? 0.4016 0.4148 0.2599 -0.1183 0.0392  -0.0368 381 LEU B N   
6319 C CA  . LEU B 381 ? 0.4206 0.4229 0.2791 -0.1067 0.0293  -0.032  381 LEU B CA  
6320 C C   . LEU B 381 ? 0.3889 0.411  0.2658 -0.0977 0.0248  -0.036  381 LEU B C   
6321 O O   . LEU B 381 ? 0.4097 0.4241 0.2897 -0.0931 0.0179  -0.0325 381 LEU B O   
6322 C CB  . LEU B 381 ? 0.4193 0.4112 0.2662 -0.1006 0.0279  -0.0297 381 LEU B CB  
6323 C CG  . LEU B 381 ? 0.452  0.4238 0.2782 -0.1086 0.0312  -0.0251 381 LEU B CG  
6324 C CD1 . LEU B 381 ? 0.4831 0.449  0.2993 -0.102  0.0297  -0.0249 381 LEU B CD1 
6325 C CD2 . LEU B 381 ? 0.4892 0.4382 0.3059 -0.1117 0.026   -0.0173 381 LEU B CD2 
6326 N N   . LYS B 382 ? 0.3819 0.4301 0.2707 -0.0957 0.0291  -0.0431 382 LYS B N   
6327 C CA  . LYS B 382 ? 0.3768 0.4453 0.282  -0.0866 0.0248  -0.0465 382 LYS B CA  
6328 C C   . LYS B 382 ? 0.3533 0.4265 0.2655 -0.0937 0.0232  -0.0478 382 LYS B C   
6329 O O   . LYS B 382 ? 0.3584 0.4306 0.2756 -0.0873 0.0166  -0.046  382 LYS B O   
6330 C CB  . LYS B 382 ? 0.3944 0.4915 0.3109 -0.0826 0.0299  -0.0538 382 LYS B CB  
6331 C CG  . LYS B 382 ? 0.4675 0.5866 0.3995 -0.071  0.0251  -0.0568 382 LYS B CG  
6332 C CD  . LYS B 382 ? 0.5126 0.6636 0.4579 -0.0673 0.0303  -0.0645 382 LYS B CD  
6333 C CE  . LYS B 382 ? 0.6074 0.7789 0.5666 -0.0555 0.024   -0.0662 382 LYS B CE  
6334 N NZ  . LYS B 382 ? 0.6837 0.8908 0.6585 -0.0527 0.0281  -0.0741 382 LYS B NZ  
6335 N N   . ILE B 383 ? 0.3427 0.4181 0.2534 -0.1077 0.0298  -0.0508 383 ILE B N   
6336 C CA  . ILE B 383 ? 0.3614 0.4398 0.2774 -0.1164 0.0298  -0.0533 383 ILE B CA  
6337 C C   . ILE B 383 ? 0.3781 0.4295 0.2857 -0.1151 0.0238  -0.0462 383 ILE B C   
6338 O O   . ILE B 383 ? 0.3647 0.4209 0.2797 -0.114  0.0199  -0.0479 383 ILE B O   
6339 C CB  . ILE B 383 ? 0.3679 0.4521 0.2827 -0.1329 0.0396  -0.0583 383 ILE B CB  
6340 C CG1 . ILE B 383 ? 0.3554 0.4745 0.2847 -0.1334 0.0444  -0.0671 383 ILE B CG1 
6341 C CG2 . ILE B 383 ? 0.3834 0.4618 0.2995 -0.1435 0.04    -0.0601 383 ILE B CG2 
6342 C CD1 . ILE B 383 ? 0.4005 0.5279 0.3291 -0.1495 0.0558  -0.0725 383 ILE B CD1 
6343 N N   . ILE B 384 ? 0.3574 0.3828 0.2505 -0.1135 0.0226  -0.0387 384 ILE B N   
6344 C CA  . ILE B 384 ? 0.3921 0.3933 0.2783 -0.1106 0.0166  -0.0317 384 ILE B CA  
6345 C C   . ILE B 384 ? 0.4064 0.4126 0.3012 -0.098  0.0086  -0.0306 384 ILE B C   
6346 O O   . ILE B 384 ? 0.4078 0.4024 0.3024 -0.097  0.0047  -0.0276 384 ILE B O   
6347 C CB  . ILE B 384 ? 0.4222 0.3983 0.2914 -0.1112 0.0164  -0.0243 384 ILE B CB  
6348 C CG1 . ILE B 384 ? 0.4492 0.415  0.3076 -0.1249 0.0247  -0.024  384 ILE B CG1 
6349 C CG2 . ILE B 384 ? 0.4371 0.3927 0.3018 -0.1047 0.0087  -0.017  384 ILE B CG2 
6350 C CD1 . ILE B 384 ? 0.4854 0.4297 0.3252 -0.126  0.0254  -0.0171 384 ILE B CD1 
6351 N N   . THR B 385 ? 0.3961 0.4192 0.2981 -0.0888 0.007   -0.0331 385 THR B N   
6352 C CA  . THR B 385 ? 0.4054 0.4322 0.3142 -0.0772 0.0003  -0.0317 385 THR B CA  
6353 C C   . THR B 385 ? 0.4338 0.4804 0.3544 -0.077  -0.0007 -0.0368 385 THR B C   
6354 O O   . THR B 385 ? 0.4792 0.5262 0.4034 -0.0685 -0.006  -0.035  385 THR B O   
6355 C CB  . THR B 385 ? 0.3971 0.4303 0.3071 -0.0665 -0.0007 -0.0317 385 THR B CB  
6356 O OG1 . THR B 385 ? 0.4136 0.4726 0.3327 -0.0657 0.0032  -0.0383 385 THR B OG1 
6357 C CG2 . THR B 385 ? 0.442  0.4582 0.3398 -0.0672 0.0005  -0.0282 385 THR B CG2 
6358 N N   . MET B 386 ? 0.4781 0.541  0.4041 -0.0866 0.004   -0.0433 386 MET B N   
6359 C CA  . MET B 386 ? 0.509  0.5947 0.4465 -0.0863 0.0022  -0.0493 386 MET B CA  
6360 C C   . MET B 386 ? 0.5741 0.6471 0.5097 -0.0894 -0.0008 -0.048  386 MET B C   
6361 O O   . MET B 386 ? 0.5427 0.5923 0.4693 -0.0967 0.0014  -0.0446 386 MET B O   
6362 C CB  . MET B 386 ? 0.4617 0.5695 0.4063 -0.0974 0.0084  -0.0576 386 MET B CB  
6363 C CG  . MET B 386 ? 0.4429 0.5685 0.3921 -0.0936 0.0119  -0.0603 386 MET B CG  
6364 S SD  . MET B 386 ? 0.4011 0.5536 0.3598 -0.1086 0.0201  -0.0705 386 MET B SD  
6365 C CE  . MET B 386 ? 0.4064 0.597  0.383  -0.1056 0.0155  -0.0791 386 MET B CE  
6366 N N   . GLY C 1   ? 0.4005 0.2872 0.3242 -0.0023 0.0552  -0.0328 1   GLY C N   
6367 C CA  . GLY C 1   ? 0.4195 0.289  0.3261 -0.0115 0.0482  -0.0315 1   GLY C CA  
6368 C C   . GLY C 1   ? 0.3883 0.2796 0.3101 -0.013  0.0369  -0.0329 1   GLY C C   
6369 O O   . GLY C 1   ? 0.419  0.3329 0.3618 -0.0109 0.0365  -0.0377 1   GLY C O   
6370 N N   . VAL C 2   ? 0.3888 0.2774 0.303  -0.0189 0.0301  -0.0333 2   VAL C N   
6371 C CA  . VAL C 2   ? 0.3586 0.2638 0.2844 -0.0199 0.0209  -0.0332 2   VAL C CA  
6372 C C   . VAL C 2   ? 0.3396 0.2522 0.2727 -0.0144 0.0219  -0.0314 2   VAL C C   
6373 O O   . VAL C 2   ? 0.3499 0.2453 0.2718 -0.0117 0.0324  -0.029  2   VAL C O   
6374 C CB  . VAL C 2   ? 0.4004 0.3114 0.3176 -0.0258 0.0135  -0.0369 2   VAL C CB  
6375 C CG1 . VAL C 2   ? 0.4128 0.3409 0.3432 -0.0258 0.0062  -0.036  2   VAL C CG1 
6376 C CG2 . VAL C 2   ? 0.4382 0.3486 0.339  -0.0185 0.0127  -0.0338 2   VAL C CG2 
6377 N N   . VAL C 3   ? 0.2924 0.2256 0.2397 -0.011  0.0161  -0.0327 3   VAL C N   
6378 C CA  . VAL C 3   ? 0.3143 0.2575 0.2614 -0.0004 0.0164  -0.0297 3   VAL C CA  
6379 C C   . VAL C 3   ? 0.3146 0.259  0.2675 -0.0073 0.0113  -0.0299 3   VAL C C   
6380 O O   . VAL C 3   ? 0.33   0.2771 0.2904 -0.0156 0.0065  -0.0321 3   VAL C O   
6381 C CB  . VAL C 3   ? 0.3152 0.2962 0.2728 0.0133  0.0132  -0.0362 3   VAL C CB  
6382 C CG1 . VAL C 3   ? 0.3731 0.3604 0.3251 0.0269  0.0196  -0.0341 3   VAL C CG1 
6383 C CG2 . VAL C 3   ? 0.3124 0.3151 0.2936 -0.0005 0.0099  -0.052  3   VAL C CG2 
6384 N N   . ARG C 4   ? 0.3456 0.2856 0.2921 0.0009  0.0167  -0.025  4   ARG C N   
6385 C CA  . ARG C 4   ? 0.3578 0.296  0.3109 -0.0059 0.0158  -0.0251 4   ARG C CA  
6386 C C   . ARG C 4   ? 0.3447 0.29   0.2899 0.0115  0.0196  -0.0201 4   ARG C C   
6387 O O   . ARG C 4   ? 0.3418 0.2867 0.2696 0.0321  0.0274  -0.0135 4   ARG C O   
6388 C CB  . ARG C 4   ? 0.3736 0.2915 0.3263 -0.0189 0.0274  -0.0285 4   ARG C CB  
6389 C CG  . ARG C 4   ? 0.3607 0.2844 0.3171 -0.0335 0.022   -0.0385 4   ARG C CG  
6390 C CD  . ARG C 4   ? 0.4159 0.3349 0.3771 -0.0526 0.0343  -0.0552 4   ARG C CD  
6391 N NE  . ARG C 4   ? 0.4697 0.3801 0.4197 -0.0585 0.0379  -0.0623 4   ARG C NE  
6392 C CZ  . ARG C 4   ? 0.5318 0.4568 0.479  -0.0693 0.033   -0.0771 4   ARG C CZ  
6393 N NH1 . ARG C 4   ? 0.5997 0.5687 0.558  -0.0812 0.0214  -0.0983 4   ARG C NH1 
6394 N NH2 . ARG C 4   ? 0.5136 0.4107 0.4441 -0.065  0.0427  -0.0715 4   ARG C NH2 
6395 N N   . GLY C 5   ? 0.334  0.2861 0.2875 0.0077  0.016   -0.0217 5   GLY C N   
6396 C CA  . GLY C 5   ? 0.3568 0.3099 0.2968 0.0252  0.0227  -0.016  5   GLY C CA  
6397 C C   . GLY C 5   ? 0.3238 0.2731 0.2757 0.0147  0.023   -0.0172 5   GLY C C   
6398 O O   . GLY C 5   ? 0.3296 0.2834 0.3001 -0.0015 0.0162  -0.0217 5   GLY C O   
6399 N N   . ALA C 6   ? 0.366  0.3077 0.3028 0.0299  0.0332  -0.0107 6   ALA C N   
6400 C CA  . ALA C 6   ? 0.3987 0.3347 0.3445 0.0234  0.0371  -0.0106 6   ALA C CA  
6401 C C   . ALA C 6   ? 0.4136 0.3611 0.3368 0.0465  0.039   -0.0083 6   ALA C C   
6402 O O   . ALA C 6   ? 0.4599 0.4155 0.3544 0.0743  0.0425  -0.0023 6   ALA C O   
6403 C CB  . ALA C 6   ? 0.4037 0.3078 0.3565 0.0125  0.0584  -0.0075 6   ALA C CB  
6404 O OXT . ALA C 6   ? 0.4322 0.3833 0.3635 0.0405  0.038   -0.012  6   ALA C OXT 
6405 N N   . GLY D 1   ? 0.4914 0.378  0.4526 -0.0237 -0.0093 0.0315  1   GLY D N   
6406 C CA  . GLY D 1   ? 0.4372 0.3307 0.4005 -0.0222 0.0012  0.0218  1   GLY D CA  
6407 C C   . GLY D 1   ? 0.4095 0.3167 0.3835 -0.0203 -0.0005 0.0182  1   GLY D C   
6408 O O   . GLY D 1   ? 0.4383 0.3457 0.4139 -0.0214 -0.0092 0.0228  1   GLY D O   
6409 N N   . VAL D 2   ? 0.42   0.3406 0.4015 -0.0197 0.0069  0.0118  2   VAL D N   
6410 C CA  . VAL D 2   ? 0.3594 0.2928 0.3498 -0.0178 0.006   0.0081  2   VAL D CA  
6411 C C   . VAL D 2   ? 0.3651 0.3019 0.3688 -0.0198 0.0068  0.0084  2   VAL D C   
6412 O O   . VAL D 2   ? 0.3611 0.2918 0.3646 -0.0227 0.0123  0.0081  2   VAL D O   
6413 C CB  . VAL D 2   ? 0.3727 0.3237 0.3657 -0.017  0.0129  0.0043  2   VAL D CB  
6414 C CG1 . VAL D 2   ? 0.3844 0.3504 0.3864 -0.0155 0.0118  0.0009  2   VAL D CG1 
6415 C CG2 . VAL D 2   ? 0.4225 0.3705 0.3995 -0.0082 0.0158  0.0061  2   VAL D CG2 
6416 N N   . VAL D 3   ? 0.32   0.2627 0.3301 -0.0178 0.0029  0.0091  3   VAL D N   
6417 C CA  . VAL D 3   ? 0.3209 0.2669 0.3403 -0.0163 0.0066  0.0096  3   VAL D CA  
6418 C C   . VAL D 3   ? 0.3273 0.2815 0.3482 -0.0177 0.0077  0.0027  3   VAL D C   
6419 O O   . VAL D 3   ? 0.3287 0.2889 0.3465 -0.017  0.0038  0.0003  3   VAL D O   
6420 C CB  . VAL D 3   ? 0.3267 0.2792 0.3551 -0.0125 0.0024  0.0201  3   VAL D CB  
6421 C CG1 . VAL D 3   ? 0.3603 0.3094 0.389  -0.0105 0.0006  0.0297  3   VAL D CG1 
6422 C CG2 . VAL D 3   ? 0.3324 0.291  0.3592 -0.0171 -0.0079 0.0231  3   VAL D CG2 
6423 N N   . ARG D 4   ? 0.3787 0.3284 0.3991 -0.0182 0.0134  0.0002  4   ARG D N   
6424 C CA  . ARG D 4   ? 0.372  0.326  0.3901 -0.0219 0.0141  -0.0059 4   ARG D CA  
6425 C C   . ARG D 4   ? 0.3872 0.3325 0.4028 -0.0168 0.0191  -0.0046 4   ARG D C   
6426 O O   . ARG D 4   ? 0.38   0.3143 0.3932 -0.0095 0.0252  0.0008  4   ARG D O   
6427 C CB  . ARG D 4   ? 0.3783 0.3274 0.3864 -0.0329 0.0167  -0.0104 4   ARG D CB  
6428 C CG  . ARG D 4   ? 0.4004 0.367  0.4132 -0.0376 0.0144  -0.0095 4   ARG D CG  
6429 C CD  . ARG D 4   ? 0.4279 0.3881 0.4304 -0.052  0.017   -0.0097 4   ARG D CD  
6430 N NE  . ARG D 4   ? 0.4139 0.4009 0.4249 -0.0554 0.0163  -0.0061 4   ARG D NE  
6431 C CZ  . ARG D 4   ? 0.4707 0.4585 0.4799 -0.0579 0.0193  -0.0026 4   ARG D CZ  
6432 N NH1 . ARG D 4   ? 0.463  0.4254 0.464  -0.0536 0.0215  -0.0021 4   ARG D NH1 
6433 N NH2 . ARG D 4   ? 0.4558 0.4755 0.4731 -0.063  0.0204  0.0025  4   ARG D NH2 
6434 N N   . GLY D 5   ? 0.3234 0.2742 0.3385 -0.0179 0.0175  -0.0081 5   GLY D N   
6435 C CA  . GLY D 5   ? 0.3454 0.2852 0.3528 -0.0129 0.0244  -0.0076 5   GLY D CA  
6436 C C   . GLY D 5   ? 0.3734 0.3143 0.3731 -0.0195 0.0213  -0.0143 5   GLY D C   
6437 O O   . GLY D 5   ? 0.3342 0.2913 0.3402 -0.0243 0.0133  -0.0167 5   GLY D O   
6438 N N   . ALA D 6   ? 0.4255 0.347  0.4083 -0.0171 0.0286  -0.016  6   ALA D N   
6439 C CA  . ALA D 6   ? 0.4352 0.3523 0.4054 -0.0232 0.0262  -0.0214 6   ALA D CA  
6440 C C   . ALA D 6   ? 0.4712 0.3755 0.4318 -0.012  0.0365  -0.0183 6   ALA D C   
6441 O O   . ALA D 6   ? 0.5031 0.3988 0.4624 0.0015  0.0479  -0.0115 6   ALA D O   
6442 C CB  . ALA D 6   ? 0.437  0.3354 0.3836 -0.0388 0.0236  -0.0276 6   ALA D CB  
6443 O OXT . ALA D 6   ? 0.4494 0.3566 0.4055 -0.0146 0.0336  -0.0208 6   ALA D OXT 
# 
