data_9O66
# 
_entry.id   9O66 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9O66         pdb_00009o66 10.2210/pdb9o66/pdb 
WWPDB D_1000294965 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_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                        9O66 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-11 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 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 Tryptophanyl-tRNA synthetase from Klebsiella aerogenes' 
_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 'Seibold, S.'    1 0000-0001-8297-229X 
primary 'Lovell, S.'     2 0000-0002-3215-4472 
primary 'Battaile, K.P.' 3 0000-0003-0833-3259 
# 
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 'Tryptophan--tRNA ligase' 39766.152 2   6.1.1.2 ? ? ? 
2 non-polymer syn IMIDAZOLE                 69.085    2   ?       ? ? ? 
3 non-polymer syn 'CALCIUM ION'             40.078    1   ?       ? ? ? 
4 water       nat water                     18.015    169 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Tryptophanyl-tRNA synthetase,TrpRS' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAHHHHHHMGTLEAQTQGPGSMTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDPQNLRKA
TLDTLALYLACGIDPQKSTIFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLY
QTNQVPVGEDQKQHLELSRDVAQRFNAIYGDIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKK
IKRAVTDSDEPPVVRYDVQNKAGVSNLLDILSAVTGQSIPELEQHFEGKMYGHLKGEVAEAVSGMLTELQERYHRFRNDE
AFLNQVMKEGAEKASAHASKTLKAVYEAIGFVAKP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHMGTLEAQTQGPGSMTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDPQNLRKA
TLDTLALYLACGIDPQKSTIFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLY
QTNQVPVGEDQKQHLELSRDVAQRFNAIYGDIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKK
IKRAVTDSDEPPVVRYDVQNKAGVSNLLDILSAVTGQSIPELEQHFEGKMYGHLKGEVAEAVSGMLTELQERYHRFRNDE
AFLNQVMKEGAEKASAHASKTLKAVYEAIGFVAKP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 IMIDAZOLE     IMD 
3 'CALCIUM ION' CA  
4 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   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   MET n 
1 10  GLY n 
1 11  THR n 
1 12  LEU n 
1 13  GLU n 
1 14  ALA n 
1 15  GLN n 
1 16  THR n 
1 17  GLN n 
1 18  GLY n 
1 19  PRO n 
1 20  GLY n 
1 21  SER n 
1 22  MET n 
1 23  THR n 
1 24  LYS n 
1 25  PRO n 
1 26  ILE n 
1 27  VAL n 
1 28  PHE n 
1 29  SER n 
1 30  GLY n 
1 31  ALA n 
1 32  GLN n 
1 33  PRO n 
1 34  SER n 
1 35  GLY n 
1 36  GLU n 
1 37  LEU n 
1 38  THR n 
1 39  ILE n 
1 40  GLY n 
1 41  ASN n 
1 42  TYR n 
1 43  MET n 
1 44  GLY n 
1 45  ALA n 
1 46  LEU n 
1 47  ARG n 
1 48  GLN n 
1 49  TRP n 
1 50  VAL n 
1 51  ASN n 
1 52  MET n 
1 53  GLN n 
1 54  ASP n 
1 55  ASP n 
1 56  TYR n 
1 57  HIS n 
1 58  CYS n 
1 59  ILE n 
1 60  TYR n 
1 61  CYS n 
1 62  ILE n 
1 63  VAL n 
1 64  ASP n 
1 65  GLN n 
1 66  HIS n 
1 67  ALA n 
1 68  ILE n 
1 69  THR n 
1 70  VAL n 
1 71  ARG n 
1 72  GLN n 
1 73  ASP n 
1 74  PRO n 
1 75  GLN n 
1 76  ASN n 
1 77  LEU n 
1 78  ARG n 
1 79  LYS n 
1 80  ALA n 
1 81  THR n 
1 82  LEU n 
1 83  ASP n 
1 84  THR n 
1 85  LEU n 
1 86  ALA n 
1 87  LEU n 
1 88  TYR n 
1 89  LEU n 
1 90  ALA n 
1 91  CYS n 
1 92  GLY n 
1 93  ILE n 
1 94  ASP n 
1 95  PRO n 
1 96  GLN n 
1 97  LYS n 
1 98  SER n 
1 99  THR n 
1 100 ILE n 
1 101 PHE n 
1 102 VAL n 
1 103 GLN n 
1 104 SER n 
1 105 HIS n 
1 106 VAL n 
1 107 PRO n 
1 108 GLU n 
1 109 HIS n 
1 110 ALA n 
1 111 GLN n 
1 112 LEU n 
1 113 GLY n 
1 114 TRP n 
1 115 ALA n 
1 116 LEU n 
1 117 ASN n 
1 118 CYS n 
1 119 TYR n 
1 120 THR n 
1 121 TYR n 
1 122 PHE n 
1 123 GLY n 
1 124 GLU n 
1 125 LEU n 
1 126 SER n 
1 127 ARG n 
1 128 MET n 
1 129 THR n 
1 130 GLN n 
1 131 PHE n 
1 132 LYS n 
1 133 ASP n 
1 134 LYS n 
1 135 SER n 
1 136 ALA n 
1 137 ARG n 
1 138 TYR n 
1 139 ALA n 
1 140 GLU n 
1 141 ASN n 
1 142 ILE n 
1 143 ASN n 
1 144 ALA n 
1 145 GLY n 
1 146 LEU n 
1 147 PHE n 
1 148 ASP n 
1 149 TYR n 
1 150 PRO n 
1 151 VAL n 
1 152 LEU n 
1 153 MET n 
1 154 ALA n 
1 155 ALA n 
1 156 ASP n 
1 157 ILE n 
1 158 LEU n 
1 159 LEU n 
1 160 TYR n 
1 161 GLN n 
1 162 THR n 
1 163 ASN n 
1 164 GLN n 
1 165 VAL n 
1 166 PRO n 
1 167 VAL n 
1 168 GLY n 
1 169 GLU n 
1 170 ASP n 
1 171 GLN n 
1 172 LYS n 
1 173 GLN n 
1 174 HIS n 
1 175 LEU n 
1 176 GLU n 
1 177 LEU n 
1 178 SER n 
1 179 ARG n 
1 180 ASP n 
1 181 VAL n 
1 182 ALA n 
1 183 GLN n 
1 184 ARG n 
1 185 PHE n 
1 186 ASN n 
1 187 ALA n 
1 188 ILE n 
1 189 TYR n 
1 190 GLY n 
1 191 ASP n 
1 192 ILE n 
1 193 PHE n 
1 194 LYS n 
1 195 VAL n 
1 196 PRO n 
1 197 GLU n 
1 198 PRO n 
1 199 PHE n 
1 200 ILE n 
1 201 PRO n 
1 202 LYS n 
1 203 SER n 
1 204 GLY n 
1 205 ALA n 
1 206 ARG n 
1 207 VAL n 
1 208 MET n 
1 209 SER n 
1 210 LEU n 
1 211 LEU n 
1 212 GLU n 
1 213 PRO n 
1 214 THR n 
1 215 LYS n 
1 216 LYS n 
1 217 MET n 
1 218 SER n 
1 219 LYS n 
1 220 SER n 
1 221 ASP n 
1 222 ASP n 
1 223 ASN n 
1 224 ARG n 
1 225 ASN n 
1 226 ASN n 
1 227 VAL n 
1 228 ILE n 
1 229 GLY n 
1 230 LEU n 
1 231 LEU n 
1 232 GLU n 
1 233 ASP n 
1 234 PRO n 
1 235 LYS n 
1 236 SER n 
1 237 VAL n 
1 238 VAL n 
1 239 LYS n 
1 240 LYS n 
1 241 ILE n 
1 242 LYS n 
1 243 ARG n 
1 244 ALA n 
1 245 VAL n 
1 246 THR n 
1 247 ASP n 
1 248 SER n 
1 249 ASP n 
1 250 GLU n 
1 251 PRO n 
1 252 PRO n 
1 253 VAL n 
1 254 VAL n 
1 255 ARG n 
1 256 TYR n 
1 257 ASP n 
1 258 VAL n 
1 259 GLN n 
1 260 ASN n 
1 261 LYS n 
1 262 ALA n 
1 263 GLY n 
1 264 VAL n 
1 265 SER n 
1 266 ASN n 
1 267 LEU n 
1 268 LEU n 
1 269 ASP n 
1 270 ILE n 
1 271 LEU n 
1 272 SER n 
1 273 ALA n 
1 274 VAL n 
1 275 THR n 
1 276 GLY n 
1 277 GLN n 
1 278 SER n 
1 279 ILE n 
1 280 PRO n 
1 281 GLU n 
1 282 LEU n 
1 283 GLU n 
1 284 GLN n 
1 285 HIS n 
1 286 PHE n 
1 287 GLU n 
1 288 GLY n 
1 289 LYS n 
1 290 MET n 
1 291 TYR n 
1 292 GLY n 
1 293 HIS n 
1 294 LEU n 
1 295 LYS n 
1 296 GLY n 
1 297 GLU n 
1 298 VAL n 
1 299 ALA n 
1 300 GLU n 
1 301 ALA n 
1 302 VAL n 
1 303 SER n 
1 304 GLY n 
1 305 MET n 
1 306 LEU n 
1 307 THR n 
1 308 GLU n 
1 309 LEU n 
1 310 GLN n 
1 311 GLU n 
1 312 ARG n 
1 313 TYR n 
1 314 HIS n 
1 315 ARG n 
1 316 PHE n 
1 317 ARG n 
1 318 ASN n 
1 319 ASP n 
1 320 GLU n 
1 321 ALA n 
1 322 PHE n 
1 323 LEU n 
1 324 ASN n 
1 325 GLN n 
1 326 VAL n 
1 327 MET n 
1 328 LYS n 
1 329 GLU n 
1 330 GLY n 
1 331 ALA n 
1 332 GLU n 
1 333 LYS n 
1 334 ALA n 
1 335 SER n 
1 336 ALA n 
1 337 HIS n 
1 338 ALA n 
1 339 SER n 
1 340 LYS n 
1 341 THR n 
1 342 LEU n 
1 343 LYS n 
1 344 ALA n 
1 345 VAL n 
1 346 TYR n 
1 347 GLU n 
1 348 ALA n 
1 349 ILE n 
1 350 GLY n 
1 351 PHE n 
1 352 VAL n 
1 353 ALA n 
1 354 LYS n 
1 355 PRO n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   355 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'trpS, EAE_05135' 
_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      'Klebsiella aerogenes KCTC 2190' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1028307 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       KlaeA.00241.a.UX1 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
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 
IMD non-polymer         . IMIDAZOLE       ? 'C3 H5 N2 1'     69.085  
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -20 ?   ?   ?   A . n 
A 1 2   ALA 2   -19 ?   ?   ?   A . n 
A 1 3   HIS 3   -18 ?   ?   ?   A . n 
A 1 4   HIS 4   -17 ?   ?   ?   A . n 
A 1 5   HIS 5   -16 ?   ?   ?   A . n 
A 1 6   HIS 6   -15 ?   ?   ?   A . n 
A 1 7   HIS 7   -14 ?   ?   ?   A . n 
A 1 8   HIS 8   -13 ?   ?   ?   A . n 
A 1 9   MET 9   -12 ?   ?   ?   A . n 
A 1 10  GLY 10  -11 ?   ?   ?   A . n 
A 1 11  THR 11  -10 ?   ?   ?   A . n 
A 1 12  LEU 12  -9  ?   ?   ?   A . n 
A 1 13  GLU 13  -8  ?   ?   ?   A . n 
A 1 14  ALA 14  -7  ?   ?   ?   A . n 
A 1 15  GLN 15  -6  ?   ?   ?   A . n 
A 1 16  THR 16  -5  ?   ?   ?   A . n 
A 1 17  GLN 17  -4  ?   ?   ?   A . n 
A 1 18  GLY 18  -3  ?   ?   ?   A . n 
A 1 19  PRO 19  -2  ?   ?   ?   A . n 
A 1 20  GLY 20  -1  ?   ?   ?   A . n 
A 1 21  SER 21  0   ?   ?   ?   A . n 
A 1 22  MET 22  1   ?   ?   ?   A . n 
A 1 23  THR 23  2   ?   ?   ?   A . n 
A 1 24  LYS 24  3   3   LYS LYS A . n 
A 1 25  PRO 25  4   4   PRO PRO A . n 
A 1 26  ILE 26  5   5   ILE ILE A . n 
A 1 27  VAL 27  6   6   VAL VAL A . n 
A 1 28  PHE 28  7   7   PHE PHE A . n 
A 1 29  SER 29  8   8   SER SER A . n 
A 1 30  GLY 30  9   9   GLY GLY A . n 
A 1 31  ALA 31  10  10  ALA ALA A . n 
A 1 32  GLN 32  11  11  GLN GLN A . n 
A 1 33  PRO 33  12  12  PRO PRO A . n 
A 1 34  SER 34  13  13  SER SER A . n 
A 1 35  GLY 35  14  14  GLY GLY A . n 
A 1 36  GLU 36  15  15  GLU GLU A . n 
A 1 37  LEU 37  16  16  LEU LEU A . n 
A 1 38  THR 38  17  17  THR THR A . n 
A 1 39  ILE 39  18  18  ILE ILE A . n 
A 1 40  GLY 40  19  19  GLY GLY A . n 
A 1 41  ASN 41  20  20  ASN ASN A . n 
A 1 42  TYR 42  21  21  TYR TYR A . n 
A 1 43  MET 43  22  22  MET MET A . n 
A 1 44  GLY 44  23  23  GLY GLY A . n 
A 1 45  ALA 45  24  24  ALA ALA A . n 
A 1 46  LEU 46  25  25  LEU LEU A . n 
A 1 47  ARG 47  26  26  ARG ARG A . n 
A 1 48  GLN 48  27  27  GLN GLN A . n 
A 1 49  TRP 49  28  28  TRP TRP A . n 
A 1 50  VAL 50  29  29  VAL VAL A . n 
A 1 51  ASN 51  30  30  ASN ASN A . n 
A 1 52  MET 52  31  31  MET MET A . n 
A 1 53  GLN 53  32  32  GLN GLN A . n 
A 1 54  ASP 54  33  33  ASP ASP A . n 
A 1 55  ASP 55  34  34  ASP ASP A . n 
A 1 56  TYR 56  35  35  TYR TYR A . n 
A 1 57  HIS 57  36  36  HIS HIS A . n 
A 1 58  CYS 58  37  37  CYS CYS A . n 
A 1 59  ILE 59  38  38  ILE ILE A . n 
A 1 60  TYR 60  39  39  TYR TYR A . n 
A 1 61  CYS 61  40  40  CYS CYS A . n 
A 1 62  ILE 62  41  41  ILE ILE A . n 
A 1 63  VAL 63  42  42  VAL VAL A . n 
A 1 64  ASP 64  43  43  ASP ASP A . n 
A 1 65  GLN 65  44  44  GLN GLN A . n 
A 1 66  HIS 66  45  45  HIS HIS A . n 
A 1 67  ALA 67  46  46  ALA ALA A . n 
A 1 68  ILE 68  47  47  ILE ILE A . n 
A 1 69  THR 69  48  48  THR THR A . n 
A 1 70  VAL 70  49  49  VAL VAL A . n 
A 1 71  ARG 71  50  50  ARG ARG A . n 
A 1 72  GLN 72  51  51  GLN GLN A . n 
A 1 73  ASP 73  52  52  ASP ASP A . n 
A 1 74  PRO 74  53  53  PRO PRO A . n 
A 1 75  GLN 75  54  54  GLN GLN A . n 
A 1 76  ASN 76  55  55  ASN ASN A . n 
A 1 77  LEU 77  56  56  LEU LEU A . n 
A 1 78  ARG 78  57  57  ARG ARG A . n 
A 1 79  LYS 79  58  58  LYS LYS A . n 
A 1 80  ALA 80  59  59  ALA ALA A . n 
A 1 81  THR 81  60  60  THR THR A . n 
A 1 82  LEU 82  61  61  LEU LEU A . n 
A 1 83  ASP 83  62  62  ASP ASP A . n 
A 1 84  THR 84  63  63  THR THR A . n 
A 1 85  LEU 85  64  64  LEU LEU A . n 
A 1 86  ALA 86  65  65  ALA ALA A . n 
A 1 87  LEU 87  66  66  LEU LEU A . n 
A 1 88  TYR 88  67  67  TYR TYR A . n 
A 1 89  LEU 89  68  68  LEU LEU A . n 
A 1 90  ALA 90  69  69  ALA ALA A . n 
A 1 91  CYS 91  70  70  CYS CYS A . n 
A 1 92  GLY 92  71  71  GLY GLY A . n 
A 1 93  ILE 93  72  72  ILE ILE A . n 
A 1 94  ASP 94  73  73  ASP ASP A . n 
A 1 95  PRO 95  74  74  PRO PRO A . n 
A 1 96  GLN 96  75  75  GLN GLN A . n 
A 1 97  LYS 97  76  76  LYS LYS A . n 
A 1 98  SER 98  77  77  SER SER A . n 
A 1 99  THR 99  78  78  THR THR A . n 
A 1 100 ILE 100 79  79  ILE ILE A . n 
A 1 101 PHE 101 80  80  PHE PHE A . n 
A 1 102 VAL 102 81  81  VAL VAL A . n 
A 1 103 GLN 103 82  82  GLN GLN A . n 
A 1 104 SER 104 83  83  SER SER A . n 
A 1 105 HIS 105 84  84  HIS HIS A . n 
A 1 106 VAL 106 85  85  VAL VAL A . n 
A 1 107 PRO 107 86  86  PRO PRO A . n 
A 1 108 GLU 108 87  87  GLU GLU A . n 
A 1 109 HIS 109 88  88  HIS HIS A . n 
A 1 110 ALA 110 89  89  ALA ALA A . n 
A 1 111 GLN 111 90  90  GLN GLN A . n 
A 1 112 LEU 112 91  91  LEU LEU A . n 
A 1 113 GLY 113 92  92  GLY GLY A . n 
A 1 114 TRP 114 93  93  TRP TRP A . n 
A 1 115 ALA 115 94  94  ALA ALA A . n 
A 1 116 LEU 116 95  95  LEU LEU A . n 
A 1 117 ASN 117 96  96  ASN ASN A . n 
A 1 118 CYS 118 97  97  CYS CYS A . n 
A 1 119 TYR 119 98  98  TYR TYR A . n 
A 1 120 THR 120 99  99  THR THR A . n 
A 1 121 TYR 121 100 100 TYR TYR A . n 
A 1 122 PHE 122 101 101 PHE PHE A . n 
A 1 123 GLY 123 102 102 GLY GLY A . n 
A 1 124 GLU 124 103 103 GLU GLU A . n 
A 1 125 LEU 125 104 104 LEU LEU A . n 
A 1 126 SER 126 105 105 SER SER A . n 
A 1 127 ARG 127 106 106 ARG ARG A . n 
A 1 128 MET 128 107 107 MET MET A . n 
A 1 129 THR 129 108 108 THR THR A . n 
A 1 130 GLN 130 109 109 GLN GLN A . n 
A 1 131 PHE 131 110 ?   ?   ?   A . n 
A 1 132 LYS 132 111 ?   ?   ?   A . n 
A 1 133 ASP 133 112 ?   ?   ?   A . n 
A 1 134 LYS 134 113 ?   ?   ?   A . n 
A 1 135 SER 135 114 ?   ?   ?   A . n 
A 1 136 ALA 136 115 ?   ?   ?   A . n 
A 1 137 ARG 137 116 ?   ?   ?   A . n 
A 1 138 TYR 138 117 ?   ?   ?   A . n 
A 1 139 ALA 139 118 118 ALA ALA A . n 
A 1 140 GLU 140 119 119 GLU GLU A . n 
A 1 141 ASN 141 120 120 ASN ASN A . n 
A 1 142 ILE 142 121 121 ILE ILE A . n 
A 1 143 ASN 143 122 122 ASN ASN A . n 
A 1 144 ALA 144 123 123 ALA ALA A . n 
A 1 145 GLY 145 124 124 GLY GLY A . n 
A 1 146 LEU 146 125 125 LEU LEU A . n 
A 1 147 PHE 147 126 126 PHE PHE A . n 
A 1 148 ASP 148 127 127 ASP ASP A . n 
A 1 149 TYR 149 128 128 TYR TYR A . n 
A 1 150 PRO 150 129 129 PRO PRO A . n 
A 1 151 VAL 151 130 130 VAL VAL A . n 
A 1 152 LEU 152 131 131 LEU LEU A . n 
A 1 153 MET 153 132 132 MET MET A . n 
A 1 154 ALA 154 133 133 ALA ALA A . n 
A 1 155 ALA 155 134 134 ALA ALA A . n 
A 1 156 ASP 156 135 135 ASP ASP A . n 
A 1 157 ILE 157 136 136 ILE ILE A . n 
A 1 158 LEU 158 137 137 LEU LEU A . n 
A 1 159 LEU 159 138 138 LEU LEU A . n 
A 1 160 TYR 160 139 139 TYR TYR A . n 
A 1 161 GLN 161 140 140 GLN GLN A . n 
A 1 162 THR 162 141 141 THR THR A . n 
A 1 163 ASN 163 142 142 ASN ASN A . n 
A 1 164 GLN 164 143 143 GLN GLN A . n 
A 1 165 VAL 165 144 144 VAL VAL A . n 
A 1 166 PRO 166 145 145 PRO PRO A . n 
A 1 167 VAL 167 146 146 VAL VAL A . n 
A 1 168 GLY 168 147 147 GLY GLY A . n 
A 1 169 GLU 169 148 148 GLU GLU A . n 
A 1 170 ASP 170 149 149 ASP ASP A . n 
A 1 171 GLN 171 150 150 GLN GLN A . n 
A 1 172 LYS 172 151 151 LYS LYS A . n 
A 1 173 GLN 173 152 152 GLN GLN A . n 
A 1 174 HIS 174 153 153 HIS HIS A . n 
A 1 175 LEU 175 154 154 LEU LEU A . n 
A 1 176 GLU 176 155 155 GLU GLU A . n 
A 1 177 LEU 177 156 156 LEU LEU A . n 
A 1 178 SER 178 157 157 SER SER A . n 
A 1 179 ARG 179 158 158 ARG ARG A . n 
A 1 180 ASP 180 159 159 ASP ASP A . n 
A 1 181 VAL 181 160 160 VAL VAL A . n 
A 1 182 ALA 182 161 161 ALA ALA A . n 
A 1 183 GLN 183 162 162 GLN GLN A . n 
A 1 184 ARG 184 163 163 ARG ARG A . n 
A 1 185 PHE 185 164 164 PHE PHE A . n 
A 1 186 ASN 186 165 165 ASN ASN A . n 
A 1 187 ALA 187 166 166 ALA ALA A . n 
A 1 188 ILE 188 167 167 ILE ILE A . n 
A 1 189 TYR 189 168 168 TYR TYR A . n 
A 1 190 GLY 190 169 169 GLY GLY A . n 
A 1 191 ASP 191 170 170 ASP ASP A . n 
A 1 192 ILE 192 171 171 ILE ILE A . n 
A 1 193 PHE 193 172 172 PHE PHE A . n 
A 1 194 LYS 194 173 173 LYS LYS A . n 
A 1 195 VAL 195 174 174 VAL VAL A . n 
A 1 196 PRO 196 175 175 PRO PRO A . n 
A 1 197 GLU 197 176 176 GLU GLU A . n 
A 1 198 PRO 198 177 177 PRO PRO A . n 
A 1 199 PHE 199 178 ?   ?   ?   A . n 
A 1 200 ILE 200 179 ?   ?   ?   A . n 
A 1 201 PRO 201 180 ?   ?   ?   A . n 
A 1 202 LYS 202 181 ?   ?   ?   A . n 
A 1 203 SER 203 182 ?   ?   ?   A . n 
A 1 204 GLY 204 183 ?   ?   ?   A . n 
A 1 205 ALA 205 184 ?   ?   ?   A . n 
A 1 206 ARG 206 185 185 ARG ARG A . n 
A 1 207 VAL 207 186 186 VAL VAL A . n 
A 1 208 MET 208 187 187 MET MET A . n 
A 1 209 SER 209 188 188 SER SER A . n 
A 1 210 LEU 210 189 189 LEU LEU A . n 
A 1 211 LEU 211 190 190 LEU LEU A . n 
A 1 212 GLU 212 191 191 GLU GLU A . n 
A 1 213 PRO 213 192 192 PRO PRO A . n 
A 1 214 THR 214 193 193 THR THR A . n 
A 1 215 LYS 215 194 194 LYS LYS A . n 
A 1 216 LYS 216 195 195 LYS LYS A . n 
A 1 217 MET 217 196 196 MET MET A . n 
A 1 218 SER 218 197 197 SER SER A . n 
A 1 219 LYS 219 198 198 LYS LYS A . n 
A 1 220 SER 220 199 199 SER SER A . n 
A 1 221 ASP 221 200 200 ASP ASP A . n 
A 1 222 ASP 222 201 201 ASP ASP A . n 
A 1 223 ASN 223 202 202 ASN ASN A . n 
A 1 224 ARG 224 203 203 ARG ARG A . n 
A 1 225 ASN 225 204 204 ASN ASN A . n 
A 1 226 ASN 226 205 205 ASN ASN A . n 
A 1 227 VAL 227 206 206 VAL VAL A . n 
A 1 228 ILE 228 207 207 ILE ILE A . n 
A 1 229 GLY 229 208 208 GLY GLY A . n 
A 1 230 LEU 230 209 209 LEU LEU A . n 
A 1 231 LEU 231 210 210 LEU LEU A . n 
A 1 232 GLU 232 211 211 GLU GLU A . n 
A 1 233 ASP 233 212 212 ASP ASP A . n 
A 1 234 PRO 234 213 213 PRO PRO A . n 
A 1 235 LYS 235 214 214 LYS LYS A . n 
A 1 236 SER 236 215 215 SER SER A . n 
A 1 237 VAL 237 216 216 VAL VAL A . n 
A 1 238 VAL 238 217 217 VAL VAL A . n 
A 1 239 LYS 239 218 218 LYS LYS A . n 
A 1 240 LYS 240 219 219 LYS LYS A . n 
A 1 241 ILE 241 220 220 ILE ILE A . n 
A 1 242 LYS 242 221 221 LYS LYS A . n 
A 1 243 ARG 243 222 222 ARG ARG A . n 
A 1 244 ALA 244 223 223 ALA ALA A . n 
A 1 245 VAL 245 224 224 VAL VAL A . n 
A 1 246 THR 246 225 225 THR THR A . n 
A 1 247 ASP 247 226 226 ASP ASP A . n 
A 1 248 SER 248 227 227 SER SER A . n 
A 1 249 ASP 249 228 228 ASP ASP A . n 
A 1 250 GLU 250 229 229 GLU GLU A . n 
A 1 251 PRO 251 230 230 PRO PRO A . n 
A 1 252 PRO 252 231 231 PRO PRO A . n 
A 1 253 VAL 253 232 232 VAL VAL A . n 
A 1 254 VAL 254 233 233 VAL VAL A . n 
A 1 255 ARG 255 234 234 ARG ARG A . n 
A 1 256 TYR 256 235 235 TYR TYR A . n 
A 1 257 ASP 257 236 236 ASP ASP A . n 
A 1 258 VAL 258 237 237 VAL VAL A . n 
A 1 259 GLN 259 238 238 GLN GLN A . n 
A 1 260 ASN 260 239 239 ASN ASN A . n 
A 1 261 LYS 261 240 240 LYS LYS A . n 
A 1 262 ALA 262 241 241 ALA ALA A . n 
A 1 263 GLY 263 242 242 GLY GLY A . n 
A 1 264 VAL 264 243 243 VAL VAL A . n 
A 1 265 SER 265 244 244 SER SER A . n 
A 1 266 ASN 266 245 245 ASN ASN A . n 
A 1 267 LEU 267 246 246 LEU LEU A . n 
A 1 268 LEU 268 247 247 LEU LEU A . n 
A 1 269 ASP 269 248 248 ASP ASP A . n 
A 1 270 ILE 270 249 249 ILE ILE A . n 
A 1 271 LEU 271 250 250 LEU LEU A . n 
A 1 272 SER 272 251 251 SER SER A . n 
A 1 273 ALA 273 252 252 ALA ALA A . n 
A 1 274 VAL 274 253 253 VAL VAL A . n 
A 1 275 THR 275 254 254 THR THR A . n 
A 1 276 GLY 276 255 255 GLY GLY A . n 
A 1 277 GLN 277 256 256 GLN GLN A . n 
A 1 278 SER 278 257 257 SER SER A . n 
A 1 279 ILE 279 258 258 ILE ILE A . n 
A 1 280 PRO 280 259 259 PRO PRO A . n 
A 1 281 GLU 281 260 260 GLU GLU A . n 
A 1 282 LEU 282 261 261 LEU LEU A . n 
A 1 283 GLU 283 262 262 GLU GLU A . n 
A 1 284 GLN 284 263 263 GLN GLN A . n 
A 1 285 HIS 285 264 264 HIS HIS A . n 
A 1 286 PHE 286 265 265 PHE PHE A . n 
A 1 287 GLU 287 266 266 GLU GLU A . n 
A 1 288 GLY 288 267 267 GLY GLY A . n 
A 1 289 LYS 289 268 268 LYS LYS A . n 
A 1 290 MET 290 269 269 MET MET A . n 
A 1 291 TYR 291 270 270 TYR TYR A . n 
A 1 292 GLY 292 271 271 GLY GLY A . n 
A 1 293 HIS 293 272 272 HIS HIS A . n 
A 1 294 LEU 294 273 273 LEU LEU A . n 
A 1 295 LYS 295 274 274 LYS LYS A . n 
A 1 296 GLY 296 275 275 GLY GLY A . n 
A 1 297 GLU 297 276 276 GLU GLU A . n 
A 1 298 VAL 298 277 277 VAL VAL A . n 
A 1 299 ALA 299 278 278 ALA ALA A . n 
A 1 300 GLU 300 279 279 GLU GLU A . n 
A 1 301 ALA 301 280 280 ALA ALA A . n 
A 1 302 VAL 302 281 281 VAL VAL A . n 
A 1 303 SER 303 282 282 SER SER A . n 
A 1 304 GLY 304 283 283 GLY GLY A . n 
A 1 305 MET 305 284 284 MET MET A . n 
A 1 306 LEU 306 285 285 LEU LEU A . n 
A 1 307 THR 307 286 286 THR THR A . n 
A 1 308 GLU 308 287 287 GLU GLU A . n 
A 1 309 LEU 309 288 288 LEU LEU A . n 
A 1 310 GLN 310 289 289 GLN GLN A . n 
A 1 311 GLU 311 290 290 GLU GLU A . n 
A 1 312 ARG 312 291 291 ARG ARG A . n 
A 1 313 TYR 313 292 292 TYR TYR A . n 
A 1 314 HIS 314 293 293 HIS HIS A . n 
A 1 315 ARG 315 294 294 ARG ARG A . n 
A 1 316 PHE 316 295 295 PHE PHE A . n 
A 1 317 ARG 317 296 296 ARG ARG A . n 
A 1 318 ASN 318 297 297 ASN ASN A . n 
A 1 319 ASP 319 298 298 ASP ASP A . n 
A 1 320 GLU 320 299 299 GLU GLU A . n 
A 1 321 ALA 321 300 300 ALA ALA A . n 
A 1 322 PHE 322 301 301 PHE PHE A . n 
A 1 323 LEU 323 302 302 LEU LEU A . n 
A 1 324 ASN 324 303 303 ASN ASN A . n 
A 1 325 GLN 325 304 304 GLN GLN A . n 
A 1 326 VAL 326 305 305 VAL VAL A . n 
A 1 327 MET 327 306 306 MET MET A . n 
A 1 328 LYS 328 307 307 LYS LYS A . n 
A 1 329 GLU 329 308 308 GLU GLU A . n 
A 1 330 GLY 330 309 309 GLY GLY A . n 
A 1 331 ALA 331 310 310 ALA ALA A . n 
A 1 332 GLU 332 311 311 GLU GLU A . n 
A 1 333 LYS 333 312 312 LYS LYS A . n 
A 1 334 ALA 334 313 313 ALA ALA A . n 
A 1 335 SER 335 314 314 SER SER A . n 
A 1 336 ALA 336 315 315 ALA ALA A . n 
A 1 337 HIS 337 316 316 HIS HIS A . n 
A 1 338 ALA 338 317 317 ALA ALA A . n 
A 1 339 SER 339 318 318 SER SER A . n 
A 1 340 LYS 340 319 319 LYS LYS A . n 
A 1 341 THR 341 320 320 THR THR A . n 
A 1 342 LEU 342 321 321 LEU LEU A . n 
A 1 343 LYS 343 322 322 LYS LYS A . n 
A 1 344 ALA 344 323 323 ALA ALA A . n 
A 1 345 VAL 345 324 324 VAL VAL A . n 
A 1 346 TYR 346 325 325 TYR TYR A . n 
A 1 347 GLU 347 326 326 GLU GLU A . n 
A 1 348 ALA 348 327 327 ALA ALA A . n 
A 1 349 ILE 349 328 328 ILE ILE A . n 
A 1 350 GLY 350 329 329 GLY GLY A . n 
A 1 351 PHE 351 330 330 PHE PHE A . n 
A 1 352 VAL 352 331 331 VAL VAL A . n 
A 1 353 ALA 353 332 332 ALA ALA A . n 
A 1 354 LYS 354 333 333 LYS LYS A . n 
A 1 355 PRO 355 334 334 PRO PRO A . n 
B 1 1   MET 1   -20 ?   ?   ?   B . n 
B 1 2   ALA 2   -19 ?   ?   ?   B . n 
B 1 3   HIS 3   -18 ?   ?   ?   B . n 
B 1 4   HIS 4   -17 ?   ?   ?   B . n 
B 1 5   HIS 5   -16 ?   ?   ?   B . n 
B 1 6   HIS 6   -15 ?   ?   ?   B . n 
B 1 7   HIS 7   -14 ?   ?   ?   B . n 
B 1 8   HIS 8   -13 ?   ?   ?   B . n 
B 1 9   MET 9   -12 ?   ?   ?   B . n 
B 1 10  GLY 10  -11 ?   ?   ?   B . n 
B 1 11  THR 11  -10 ?   ?   ?   B . n 
B 1 12  LEU 12  -9  ?   ?   ?   B . n 
B 1 13  GLU 13  -8  ?   ?   ?   B . n 
B 1 14  ALA 14  -7  ?   ?   ?   B . n 
B 1 15  GLN 15  -6  ?   ?   ?   B . n 
B 1 16  THR 16  -5  ?   ?   ?   B . n 
B 1 17  GLN 17  -4  ?   ?   ?   B . n 
B 1 18  GLY 18  -3  ?   ?   ?   B . n 
B 1 19  PRO 19  -2  ?   ?   ?   B . n 
B 1 20  GLY 20  -1  ?   ?   ?   B . n 
B 1 21  SER 21  0   ?   ?   ?   B . n 
B 1 22  MET 22  1   ?   ?   ?   B . n 
B 1 23  THR 23  2   2   THR THR B . n 
B 1 24  LYS 24  3   3   LYS LYS B . n 
B 1 25  PRO 25  4   4   PRO PRO B . n 
B 1 26  ILE 26  5   5   ILE ILE B . n 
B 1 27  VAL 27  6   6   VAL VAL B . n 
B 1 28  PHE 28  7   7   PHE PHE B . n 
B 1 29  SER 29  8   8   SER SER B . n 
B 1 30  GLY 30  9   9   GLY GLY B . n 
B 1 31  ALA 31  10  10  ALA ALA B . n 
B 1 32  GLN 32  11  11  GLN GLN B . n 
B 1 33  PRO 33  12  12  PRO PRO B . n 
B 1 34  SER 34  13  13  SER SER B . n 
B 1 35  GLY 35  14  14  GLY GLY B . n 
B 1 36  GLU 36  15  15  GLU GLU B . n 
B 1 37  LEU 37  16  16  LEU LEU B . n 
B 1 38  THR 38  17  17  THR THR B . n 
B 1 39  ILE 39  18  18  ILE ILE B . n 
B 1 40  GLY 40  19  19  GLY GLY B . n 
B 1 41  ASN 41  20  20  ASN ASN B . n 
B 1 42  TYR 42  21  21  TYR TYR B . n 
B 1 43  MET 43  22  22  MET MET B . n 
B 1 44  GLY 44  23  23  GLY GLY B . n 
B 1 45  ALA 45  24  24  ALA ALA B . n 
B 1 46  LEU 46  25  25  LEU LEU B . n 
B 1 47  ARG 47  26  26  ARG ARG B . n 
B 1 48  GLN 48  27  27  GLN GLN B . n 
B 1 49  TRP 49  28  28  TRP TRP B . n 
B 1 50  VAL 50  29  29  VAL VAL B . n 
B 1 51  ASN 51  30  30  ASN ASN B . n 
B 1 52  MET 52  31  31  MET MET B . n 
B 1 53  GLN 53  32  32  GLN GLN B . n 
B 1 54  ASP 54  33  33  ASP ASP B . n 
B 1 55  ASP 55  34  34  ASP ASP B . n 
B 1 56  TYR 56  35  35  TYR TYR B . n 
B 1 57  HIS 57  36  36  HIS HIS B . n 
B 1 58  CYS 58  37  37  CYS CYS B . n 
B 1 59  ILE 59  38  38  ILE ILE B . n 
B 1 60  TYR 60  39  39  TYR TYR B . n 
B 1 61  CYS 61  40  40  CYS CYS B . n 
B 1 62  ILE 62  41  41  ILE ILE B . n 
B 1 63  VAL 63  42  42  VAL VAL B . n 
B 1 64  ASP 64  43  43  ASP ASP B . n 
B 1 65  GLN 65  44  44  GLN GLN B . n 
B 1 66  HIS 66  45  45  HIS HIS B . n 
B 1 67  ALA 67  46  46  ALA ALA B . n 
B 1 68  ILE 68  47  47  ILE ILE B . n 
B 1 69  THR 69  48  48  THR THR B . n 
B 1 70  VAL 70  49  49  VAL VAL B . n 
B 1 71  ARG 71  50  50  ARG ARG B . n 
B 1 72  GLN 72  51  51  GLN GLN B . n 
B 1 73  ASP 73  52  52  ASP ASP B . n 
B 1 74  PRO 74  53  53  PRO PRO B . n 
B 1 75  GLN 75  54  54  GLN GLN B . n 
B 1 76  ASN 76  55  55  ASN ASN B . n 
B 1 77  LEU 77  56  56  LEU LEU B . n 
B 1 78  ARG 78  57  57  ARG ARG B . n 
B 1 79  LYS 79  58  58  LYS LYS B . n 
B 1 80  ALA 80  59  59  ALA ALA B . n 
B 1 81  THR 81  60  60  THR THR B . n 
B 1 82  LEU 82  61  61  LEU LEU B . n 
B 1 83  ASP 83  62  62  ASP ASP B . n 
B 1 84  THR 84  63  63  THR THR B . n 
B 1 85  LEU 85  64  64  LEU LEU B . n 
B 1 86  ALA 86  65  65  ALA ALA B . n 
B 1 87  LEU 87  66  66  LEU LEU B . n 
B 1 88  TYR 88  67  67  TYR TYR B . n 
B 1 89  LEU 89  68  68  LEU LEU B . n 
B 1 90  ALA 90  69  69  ALA ALA B . n 
B 1 91  CYS 91  70  70  CYS CYS B . n 
B 1 92  GLY 92  71  71  GLY GLY B . n 
B 1 93  ILE 93  72  72  ILE ILE B . n 
B 1 94  ASP 94  73  73  ASP ASP B . n 
B 1 95  PRO 95  74  74  PRO PRO B . n 
B 1 96  GLN 96  75  75  GLN GLN B . n 
B 1 97  LYS 97  76  76  LYS LYS B . n 
B 1 98  SER 98  77  77  SER SER B . n 
B 1 99  THR 99  78  78  THR THR B . n 
B 1 100 ILE 100 79  79  ILE ILE B . n 
B 1 101 PHE 101 80  80  PHE PHE B . n 
B 1 102 VAL 102 81  81  VAL VAL B . n 
B 1 103 GLN 103 82  82  GLN GLN B . n 
B 1 104 SER 104 83  83  SER SER B . n 
B 1 105 HIS 105 84  84  HIS HIS B . n 
B 1 106 VAL 106 85  85  VAL VAL B . n 
B 1 107 PRO 107 86  86  PRO PRO B . n 
B 1 108 GLU 108 87  87  GLU GLU B . n 
B 1 109 HIS 109 88  88  HIS HIS B . n 
B 1 110 ALA 110 89  89  ALA ALA B . n 
B 1 111 GLN 111 90  90  GLN GLN B . n 
B 1 112 LEU 112 91  91  LEU LEU B . n 
B 1 113 GLY 113 92  92  GLY GLY B . n 
B 1 114 TRP 114 93  93  TRP TRP B . n 
B 1 115 ALA 115 94  94  ALA ALA B . n 
B 1 116 LEU 116 95  95  LEU LEU B . n 
B 1 117 ASN 117 96  96  ASN ASN B . n 
B 1 118 CYS 118 97  97  CYS CYS B . n 
B 1 119 TYR 119 98  98  TYR TYR B . n 
B 1 120 THR 120 99  99  THR THR B . n 
B 1 121 TYR 121 100 100 TYR TYR B . n 
B 1 122 PHE 122 101 101 PHE PHE B . n 
B 1 123 GLY 123 102 102 GLY GLY B . n 
B 1 124 GLU 124 103 103 GLU GLU B . n 
B 1 125 LEU 125 104 104 LEU LEU B . n 
B 1 126 SER 126 105 105 SER SER B . n 
B 1 127 ARG 127 106 106 ARG ARG B . n 
B 1 128 MET 128 107 107 MET MET B . n 
B 1 129 THR 129 108 108 THR THR B . n 
B 1 130 GLN 130 109 ?   ?   ?   B . n 
B 1 131 PHE 131 110 ?   ?   ?   B . n 
B 1 132 LYS 132 111 ?   ?   ?   B . n 
B 1 133 ASP 133 112 ?   ?   ?   B . n 
B 1 134 LYS 134 113 ?   ?   ?   B . n 
B 1 135 SER 135 114 ?   ?   ?   B . n 
B 1 136 ALA 136 115 ?   ?   ?   B . n 
B 1 137 ARG 137 116 ?   ?   ?   B . n 
B 1 138 TYR 138 117 ?   ?   ?   B . n 
B 1 139 ALA 139 118 ?   ?   ?   B . n 
B 1 140 GLU 140 119 119 GLU GLU B . n 
B 1 141 ASN 141 120 120 ASN ASN B . n 
B 1 142 ILE 142 121 121 ILE ILE B . n 
B 1 143 ASN 143 122 122 ASN ASN B . n 
B 1 144 ALA 144 123 123 ALA ALA B . n 
B 1 145 GLY 145 124 124 GLY GLY B . n 
B 1 146 LEU 146 125 125 LEU LEU B . n 
B 1 147 PHE 147 126 126 PHE PHE B . n 
B 1 148 ASP 148 127 127 ASP ASP B . n 
B 1 149 TYR 149 128 128 TYR TYR B . n 
B 1 150 PRO 150 129 129 PRO PRO B . n 
B 1 151 VAL 151 130 130 VAL VAL B . n 
B 1 152 LEU 152 131 131 LEU LEU B . n 
B 1 153 MET 153 132 132 MET MET B . n 
B 1 154 ALA 154 133 133 ALA ALA B . n 
B 1 155 ALA 155 134 134 ALA ALA B . n 
B 1 156 ASP 156 135 135 ASP ASP B . n 
B 1 157 ILE 157 136 136 ILE ILE B . n 
B 1 158 LEU 158 137 137 LEU LEU B . n 
B 1 159 LEU 159 138 138 LEU LEU B . n 
B 1 160 TYR 160 139 139 TYR TYR B . n 
B 1 161 GLN 161 140 140 GLN GLN B . n 
B 1 162 THR 162 141 141 THR THR B . n 
B 1 163 ASN 163 142 142 ASN ASN B . n 
B 1 164 GLN 164 143 143 GLN GLN B . n 
B 1 165 VAL 165 144 144 VAL VAL B . n 
B 1 166 PRO 166 145 145 PRO PRO B . n 
B 1 167 VAL 167 146 146 VAL VAL B . n 
B 1 168 GLY 168 147 147 GLY GLY B . n 
B 1 169 GLU 169 148 148 GLU GLU B . n 
B 1 170 ASP 170 149 149 ASP ASP B . n 
B 1 171 GLN 171 150 150 GLN GLN B . n 
B 1 172 LYS 172 151 151 LYS LYS B . n 
B 1 173 GLN 173 152 152 GLN GLN B . n 
B 1 174 HIS 174 153 153 HIS HIS B . n 
B 1 175 LEU 175 154 154 LEU LEU B . n 
B 1 176 GLU 176 155 155 GLU GLU B . n 
B 1 177 LEU 177 156 156 LEU LEU B . n 
B 1 178 SER 178 157 157 SER SER B . n 
B 1 179 ARG 179 158 158 ARG ARG B . n 
B 1 180 ASP 180 159 159 ASP ASP B . n 
B 1 181 VAL 181 160 160 VAL VAL B . n 
B 1 182 ALA 182 161 161 ALA ALA B . n 
B 1 183 GLN 183 162 162 GLN GLN B . n 
B 1 184 ARG 184 163 163 ARG ARG B . n 
B 1 185 PHE 185 164 164 PHE PHE B . n 
B 1 186 ASN 186 165 165 ASN ASN B . n 
B 1 187 ALA 187 166 166 ALA ALA B . n 
B 1 188 ILE 188 167 167 ILE ILE B . n 
B 1 189 TYR 189 168 168 TYR TYR B . n 
B 1 190 GLY 190 169 169 GLY GLY B . n 
B 1 191 ASP 191 170 170 ASP ASP B . n 
B 1 192 ILE 192 171 171 ILE ILE B . n 
B 1 193 PHE 193 172 172 PHE PHE B . n 
B 1 194 LYS 194 173 173 LYS LYS B . n 
B 1 195 VAL 195 174 174 VAL VAL B . n 
B 1 196 PRO 196 175 175 PRO PRO B . n 
B 1 197 GLU 197 176 176 GLU GLU B . n 
B 1 198 PRO 198 177 177 PRO PRO B . n 
B 1 199 PHE 199 178 178 PHE PHE B . n 
B 1 200 ILE 200 179 179 ILE ILE B . n 
B 1 201 PRO 201 180 180 PRO PRO B . n 
B 1 202 LYS 202 181 ?   ?   ?   B . n 
B 1 203 SER 203 182 ?   ?   ?   B . n 
B 1 204 GLY 204 183 183 GLY GLY B . n 
B 1 205 ALA 205 184 184 ALA ALA B . n 
B 1 206 ARG 206 185 185 ARG ARG B . n 
B 1 207 VAL 207 186 186 VAL VAL B . n 
B 1 208 MET 208 187 187 MET MET B . n 
B 1 209 SER 209 188 188 SER SER B . n 
B 1 210 LEU 210 189 189 LEU LEU B . n 
B 1 211 LEU 211 190 190 LEU LEU B . n 
B 1 212 GLU 212 191 191 GLU GLU B . n 
B 1 213 PRO 213 192 192 PRO PRO B . n 
B 1 214 THR 214 193 ?   ?   ?   B . n 
B 1 215 LYS 215 194 ?   ?   ?   B . n 
B 1 216 LYS 216 195 195 LYS LYS B . n 
B 1 217 MET 217 196 196 MET MET B . n 
B 1 218 SER 218 197 197 SER SER B . n 
B 1 219 LYS 219 198 198 LYS LYS B . n 
B 1 220 SER 220 199 199 SER SER B . n 
B 1 221 ASP 221 200 200 ASP ASP B . n 
B 1 222 ASP 222 201 201 ASP ASP B . n 
B 1 223 ASN 223 202 202 ASN ASN B . n 
B 1 224 ARG 224 203 203 ARG ARG B . n 
B 1 225 ASN 225 204 204 ASN ASN B . n 
B 1 226 ASN 226 205 205 ASN ASN B . n 
B 1 227 VAL 227 206 206 VAL VAL B . n 
B 1 228 ILE 228 207 207 ILE ILE B . n 
B 1 229 GLY 229 208 208 GLY GLY B . n 
B 1 230 LEU 230 209 209 LEU LEU B . n 
B 1 231 LEU 231 210 210 LEU LEU B . n 
B 1 232 GLU 232 211 211 GLU GLU B . n 
B 1 233 ASP 233 212 212 ASP ASP B . n 
B 1 234 PRO 234 213 213 PRO PRO B . n 
B 1 235 LYS 235 214 214 LYS LYS B . n 
B 1 236 SER 236 215 215 SER SER B . n 
B 1 237 VAL 237 216 216 VAL VAL B . n 
B 1 238 VAL 238 217 217 VAL VAL B . n 
B 1 239 LYS 239 218 218 LYS LYS B . n 
B 1 240 LYS 240 219 219 LYS LYS B . n 
B 1 241 ILE 241 220 220 ILE ILE B . n 
B 1 242 LYS 242 221 221 LYS LYS B . n 
B 1 243 ARG 243 222 222 ARG ARG B . n 
B 1 244 ALA 244 223 223 ALA ALA B . n 
B 1 245 VAL 245 224 224 VAL VAL B . n 
B 1 246 THR 246 225 225 THR THR B . n 
B 1 247 ASP 247 226 226 ASP ASP B . n 
B 1 248 SER 248 227 227 SER SER B . n 
B 1 249 ASP 249 228 228 ASP ASP B . n 
B 1 250 GLU 250 229 229 GLU GLU B . n 
B 1 251 PRO 251 230 230 PRO PRO B . n 
B 1 252 PRO 252 231 231 PRO PRO B . n 
B 1 253 VAL 253 232 232 VAL VAL B . n 
B 1 254 VAL 254 233 233 VAL VAL B . n 
B 1 255 ARG 255 234 234 ARG ARG B . n 
B 1 256 TYR 256 235 235 TYR TYR B . n 
B 1 257 ASP 257 236 236 ASP ASP B . n 
B 1 258 VAL 258 237 ?   ?   ?   B . n 
B 1 259 GLN 259 238 ?   ?   ?   B . n 
B 1 260 ASN 260 239 ?   ?   ?   B . n 
B 1 261 LYS 261 240 ?   ?   ?   B . n 
B 1 262 ALA 262 241 241 ALA ALA B . n 
B 1 263 GLY 263 242 242 GLY GLY B . n 
B 1 264 VAL 264 243 243 VAL VAL B . n 
B 1 265 SER 265 244 244 SER SER B . n 
B 1 266 ASN 266 245 245 ASN ASN B . n 
B 1 267 LEU 267 246 246 LEU LEU B . n 
B 1 268 LEU 268 247 247 LEU LEU B . n 
B 1 269 ASP 269 248 248 ASP ASP B . n 
B 1 270 ILE 270 249 249 ILE ILE B . n 
B 1 271 LEU 271 250 250 LEU LEU B . n 
B 1 272 SER 272 251 251 SER SER B . n 
B 1 273 ALA 273 252 252 ALA ALA B . n 
B 1 274 VAL 274 253 253 VAL VAL B . n 
B 1 275 THR 275 254 254 THR THR B . n 
B 1 276 GLY 276 255 255 GLY GLY B . n 
B 1 277 GLN 277 256 256 GLN GLN B . n 
B 1 278 SER 278 257 257 SER SER B . n 
B 1 279 ILE 279 258 258 ILE ILE B . n 
B 1 280 PRO 280 259 259 PRO PRO B . n 
B 1 281 GLU 281 260 260 GLU GLU B . n 
B 1 282 LEU 282 261 261 LEU LEU B . n 
B 1 283 GLU 283 262 262 GLU GLU B . n 
B 1 284 GLN 284 263 263 GLN GLN B . n 
B 1 285 HIS 285 264 264 HIS HIS B . n 
B 1 286 PHE 286 265 265 PHE PHE B . n 
B 1 287 GLU 287 266 ?   ?   ?   B . n 
B 1 288 GLY 288 267 267 GLY GLY B . n 
B 1 289 LYS 289 268 268 LYS LYS B . n 
B 1 290 MET 290 269 269 MET MET B . n 
B 1 291 TYR 291 270 270 TYR TYR B . n 
B 1 292 GLY 292 271 271 GLY GLY B . n 
B 1 293 HIS 293 272 272 HIS HIS B . n 
B 1 294 LEU 294 273 273 LEU LEU B . n 
B 1 295 LYS 295 274 274 LYS LYS B . n 
B 1 296 GLY 296 275 275 GLY GLY B . n 
B 1 297 GLU 297 276 276 GLU GLU B . n 
B 1 298 VAL 298 277 277 VAL VAL B . n 
B 1 299 ALA 299 278 278 ALA ALA B . n 
B 1 300 GLU 300 279 279 GLU GLU B . n 
B 1 301 ALA 301 280 280 ALA ALA B . n 
B 1 302 VAL 302 281 281 VAL VAL B . n 
B 1 303 SER 303 282 282 SER SER B . n 
B 1 304 GLY 304 283 283 GLY GLY B . n 
B 1 305 MET 305 284 284 MET MET B . n 
B 1 306 LEU 306 285 285 LEU LEU B . n 
B 1 307 THR 307 286 286 THR THR B . n 
B 1 308 GLU 308 287 287 GLU GLU B . n 
B 1 309 LEU 309 288 288 LEU LEU B . n 
B 1 310 GLN 310 289 289 GLN GLN B . n 
B 1 311 GLU 311 290 290 GLU GLU B . n 
B 1 312 ARG 312 291 291 ARG ARG B . n 
B 1 313 TYR 313 292 292 TYR TYR B . n 
B 1 314 HIS 314 293 293 HIS HIS B . n 
B 1 315 ARG 315 294 294 ARG ARG B . n 
B 1 316 PHE 316 295 295 PHE PHE B . n 
B 1 317 ARG 317 296 296 ARG ARG B . n 
B 1 318 ASN 318 297 297 ASN ASN B . n 
B 1 319 ASP 319 298 298 ASP ASP B . n 
B 1 320 GLU 320 299 299 GLU GLU B . n 
B 1 321 ALA 321 300 300 ALA ALA B . n 
B 1 322 PHE 322 301 301 PHE PHE B . n 
B 1 323 LEU 323 302 302 LEU LEU B . n 
B 1 324 ASN 324 303 303 ASN ASN B . n 
B 1 325 GLN 325 304 304 GLN GLN B . n 
B 1 326 VAL 326 305 305 VAL VAL B . n 
B 1 327 MET 327 306 306 MET MET B . n 
B 1 328 LYS 328 307 307 LYS LYS B . n 
B 1 329 GLU 329 308 308 GLU GLU B . n 
B 1 330 GLY 330 309 309 GLY GLY B . n 
B 1 331 ALA 331 310 310 ALA ALA B . n 
B 1 332 GLU 332 311 311 GLU GLU B . n 
B 1 333 LYS 333 312 312 LYS LYS B . n 
B 1 334 ALA 334 313 313 ALA ALA B . n 
B 1 335 SER 335 314 314 SER SER B . n 
B 1 336 ALA 336 315 315 ALA ALA B . n 
B 1 337 HIS 337 316 316 HIS HIS B . n 
B 1 338 ALA 338 317 317 ALA ALA B . n 
B 1 339 SER 339 318 318 SER SER B . n 
B 1 340 LYS 340 319 319 LYS LYS B . n 
B 1 341 THR 341 320 320 THR THR B . n 
B 1 342 LEU 342 321 321 LEU LEU B . n 
B 1 343 LYS 343 322 322 LYS LYS B . n 
B 1 344 ALA 344 323 323 ALA ALA B . n 
B 1 345 VAL 345 324 324 VAL VAL B . n 
B 1 346 TYR 346 325 325 TYR TYR B . n 
B 1 347 GLU 347 326 326 GLU GLU B . n 
B 1 348 ALA 348 327 327 ALA ALA B . n 
B 1 349 ILE 349 328 328 ILE ILE B . n 
B 1 350 GLY 350 329 329 GLY GLY B . n 
B 1 351 PHE 351 330 330 PHE PHE B . n 
B 1 352 VAL 352 331 331 VAL VAL B . n 
B 1 353 ALA 353 332 332 ALA ALA B . n 
B 1 354 LYS 354 333 333 LYS LYS B . n 
B 1 355 PRO 355 334 334 PRO PRO B . 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 
C 2 IMD 1  401 404 IMD IMD A . 
D 3 CA  1  401 1   CA  CA  B . 
E 2 IMD 1  402 403 IMD IMD B . 
F 4 HOH 1  501 122 HOH HOH A . 
F 4 HOH 2  502 140 HOH HOH A . 
F 4 HOH 3  503 25  HOH HOH A . 
F 4 HOH 4  504 41  HOH HOH A . 
F 4 HOH 5  505 47  HOH HOH A . 
F 4 HOH 6  506 124 HOH HOH A . 
F 4 HOH 7  507 94  HOH HOH A . 
F 4 HOH 8  508 51  HOH HOH A . 
F 4 HOH 9  509 81  HOH HOH A . 
F 4 HOH 10 510 141 HOH HOH A . 
F 4 HOH 11 511 63  HOH HOH A . 
F 4 HOH 12 512 165 HOH HOH A . 
F 4 HOH 13 513 131 HOH HOH A . 
F 4 HOH 14 514 61  HOH HOH A . 
F 4 HOH 15 515 40  HOH HOH A . 
F 4 HOH 16 516 89  HOH HOH A . 
F 4 HOH 17 517 66  HOH HOH A . 
F 4 HOH 18 518 45  HOH HOH A . 
F 4 HOH 19 519 50  HOH HOH A . 
F 4 HOH 20 520 146 HOH HOH A . 
F 4 HOH 21 521 19  HOH HOH A . 
F 4 HOH 22 522 27  HOH HOH A . 
F 4 HOH 23 523 36  HOH HOH A . 
F 4 HOH 24 524 125 HOH HOH A . 
F 4 HOH 25 525 13  HOH HOH A . 
F 4 HOH 26 526 9   HOH HOH A . 
F 4 HOH 27 527 21  HOH HOH A . 
F 4 HOH 28 528 75  HOH HOH A . 
F 4 HOH 29 529 167 HOH HOH A . 
F 4 HOH 30 530 97  HOH HOH A . 
F 4 HOH 31 531 20  HOH HOH A . 
F 4 HOH 32 532 56  HOH HOH A . 
F 4 HOH 33 533 53  HOH HOH A . 
F 4 HOH 34 534 83  HOH HOH A . 
F 4 HOH 35 535 4   HOH HOH A . 
F 4 HOH 36 536 17  HOH HOH A . 
F 4 HOH 37 537 52  HOH HOH A . 
F 4 HOH 38 538 22  HOH HOH A . 
F 4 HOH 39 539 18  HOH HOH A . 
F 4 HOH 40 540 14  HOH HOH A . 
F 4 HOH 41 541 76  HOH HOH A . 
F 4 HOH 42 542 82  HOH HOH A . 
F 4 HOH 43 543 69  HOH HOH A . 
F 4 HOH 44 544 78  HOH HOH A . 
F 4 HOH 45 545 153 HOH HOH A . 
F 4 HOH 46 546 84  HOH HOH A . 
F 4 HOH 47 547 112 HOH HOH A . 
F 4 HOH 48 548 35  HOH HOH A . 
F 4 HOH 49 549 77  HOH HOH A . 
F 4 HOH 50 550 80  HOH HOH A . 
F 4 HOH 51 551 145 HOH HOH A . 
F 4 HOH 52 552 121 HOH HOH A . 
F 4 HOH 53 553 102 HOH HOH A . 
F 4 HOH 54 554 96  HOH HOH A . 
F 4 HOH 55 555 113 HOH HOH A . 
F 4 HOH 56 556 29  HOH HOH A . 
F 4 HOH 57 557 134 HOH HOH A . 
F 4 HOH 58 558 92  HOH HOH A . 
F 4 HOH 59 559 85  HOH HOH A . 
F 4 HOH 60 560 104 HOH HOH A . 
F 4 HOH 61 561 130 HOH HOH A . 
F 4 HOH 62 562 127 HOH HOH A . 
F 4 HOH 63 563 117 HOH HOH A . 
F 4 HOH 64 564 86  HOH HOH A . 
F 4 HOH 65 565 90  HOH HOH A . 
F 4 HOH 66 566 95  HOH HOH A . 
F 4 HOH 67 567 144 HOH HOH A . 
F 4 HOH 68 568 101 HOH HOH A . 
F 4 HOH 69 569 133 HOH HOH A . 
F 4 HOH 70 570 65  HOH HOH A . 
F 4 HOH 71 571 160 HOH HOH A . 
F 4 HOH 72 572 6   HOH HOH A . 
F 4 HOH 73 573 7   HOH HOH A . 
F 4 HOH 74 574 59  HOH HOH A . 
F 4 HOH 75 575 169 HOH HOH A . 
F 4 HOH 76 576 159 HOH HOH A . 
F 4 HOH 77 577 106 HOH HOH A . 
F 4 HOH 78 578 161 HOH HOH A . 
F 4 HOH 79 579 30  HOH HOH A . 
F 4 HOH 80 580 116 HOH HOH A . 
G 4 HOH 1  501 164 HOH HOH B . 
G 4 HOH 2  502 62  HOH HOH B . 
G 4 HOH 3  503 71  HOH HOH B . 
G 4 HOH 4  504 148 HOH HOH B . 
G 4 HOH 5  505 137 HOH HOH B . 
G 4 HOH 6  506 126 HOH HOH B . 
G 4 HOH 7  507 37  HOH HOH B . 
G 4 HOH 8  508 1   HOH HOH B . 
G 4 HOH 9  509 109 HOH HOH B . 
G 4 HOH 10 510 111 HOH HOH B . 
G 4 HOH 11 511 55  HOH HOH B . 
G 4 HOH 12 512 151 HOH HOH B . 
G 4 HOH 13 513 107 HOH HOH B . 
G 4 HOH 14 514 48  HOH HOH B . 
G 4 HOH 15 515 110 HOH HOH B . 
G 4 HOH 16 516 24  HOH HOH B . 
G 4 HOH 17 517 67  HOH HOH B . 
G 4 HOH 18 518 11  HOH HOH B . 
G 4 HOH 19 519 57  HOH HOH B . 
G 4 HOH 20 520 44  HOH HOH B . 
G 4 HOH 21 521 73  HOH HOH B . 
G 4 HOH 22 522 157 HOH HOH B . 
G 4 HOH 23 523 118 HOH HOH B . 
G 4 HOH 24 524 16  HOH HOH B . 
G 4 HOH 25 525 31  HOH HOH B . 
G 4 HOH 26 526 105 HOH HOH B . 
G 4 HOH 27 527 12  HOH HOH B . 
G 4 HOH 28 528 132 HOH HOH B . 
G 4 HOH 29 529 119 HOH HOH B . 
G 4 HOH 30 530 154 HOH HOH B . 
G 4 HOH 31 531 2   HOH HOH B . 
G 4 HOH 32 532 58  HOH HOH B . 
G 4 HOH 33 533 26  HOH HOH B . 
G 4 HOH 34 534 46  HOH HOH B . 
G 4 HOH 35 535 70  HOH HOH B . 
G 4 HOH 36 536 34  HOH HOH B . 
G 4 HOH 37 537 49  HOH HOH B . 
G 4 HOH 38 538 15  HOH HOH B . 
G 4 HOH 39 539 72  HOH HOH B . 
G 4 HOH 40 540 128 HOH HOH B . 
G 4 HOH 41 541 10  HOH HOH B . 
G 4 HOH 42 542 163 HOH HOH B . 
G 4 HOH 43 543 142 HOH HOH B . 
G 4 HOH 44 544 79  HOH HOH B . 
G 4 HOH 45 545 38  HOH HOH B . 
G 4 HOH 46 546 87  HOH HOH B . 
G 4 HOH 47 547 120 HOH HOH B . 
G 4 HOH 48 548 68  HOH HOH B . 
G 4 HOH 49 549 64  HOH HOH B . 
G 4 HOH 50 550 5   HOH HOH B . 
G 4 HOH 51 551 155 HOH HOH B . 
G 4 HOH 52 552 43  HOH HOH B . 
G 4 HOH 53 553 74  HOH HOH B . 
G 4 HOH 54 554 42  HOH HOH B . 
G 4 HOH 55 555 39  HOH HOH B . 
G 4 HOH 56 556 103 HOH HOH B . 
G 4 HOH 57 557 93  HOH HOH B . 
G 4 HOH 58 558 98  HOH HOH B . 
G 4 HOH 59 559 54  HOH HOH B . 
G 4 HOH 60 560 123 HOH HOH B . 
G 4 HOH 61 561 88  HOH HOH B . 
G 4 HOH 62 562 28  HOH HOH B . 
G 4 HOH 63 563 166 HOH HOH B . 
G 4 HOH 64 564 3   HOH HOH B . 
G 4 HOH 65 565 139 HOH HOH B . 
G 4 HOH 66 566 162 HOH HOH B . 
G 4 HOH 67 567 33  HOH HOH B . 
G 4 HOH 68 568 149 HOH HOH B . 
G 4 HOH 69 569 115 HOH HOH B . 
G 4 HOH 70 570 23  HOH HOH B . 
G 4 HOH 71 571 158 HOH HOH B . 
G 4 HOH 72 572 152 HOH HOH B . 
G 4 HOH 73 573 143 HOH HOH B . 
G 4 HOH 74 574 114 HOH HOH B . 
G 4 HOH 75 575 60  HOH HOH B . 
G 4 HOH 76 576 100 HOH HOH B . 
G 4 HOH 77 577 32  HOH HOH B . 
G 4 HOH 78 578 129 HOH HOH B . 
G 4 HOH 79 579 147 HOH HOH B . 
G 4 HOH 80 580 8   HOH HOH B . 
G 4 HOH 81 581 108 HOH HOH B . 
G 4 HOH 82 582 99  HOH HOH B . 
G 4 HOH 83 583 156 HOH HOH B . 
G 4 HOH 84 584 136 HOH HOH B . 
G 4 HOH 85 585 150 HOH HOH B . 
G 4 HOH 86 586 168 HOH HOH B . 
G 4 HOH 87 587 91  HOH HOH B . 
G 4 HOH 88 588 138 HOH HOH B . 
G 4 HOH 89 589 135 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ASN 120 ? CG  ? A ASN 141 CG  
2   1 Y 1 A ASN 120 ? OD1 ? A ASN 141 OD1 
3   1 Y 1 A ASN 120 ? ND2 ? A ASN 141 ND2 
4   1 Y 1 A LYS 194 ? CG  ? A LYS 215 CG  
5   1 Y 1 A LYS 194 ? CD  ? A LYS 215 CD  
6   1 Y 1 A LYS 194 ? CE  ? A LYS 215 CE  
7   1 Y 1 A LYS 194 ? NZ  ? A LYS 215 NZ  
8   1 Y 1 A LYS 198 ? CG  ? A LYS 219 CG  
9   1 Y 1 A LYS 198 ? CD  ? A LYS 219 CD  
10  1 Y 1 A LYS 198 ? CE  ? A LYS 219 CE  
11  1 Y 1 A LYS 198 ? NZ  ? A LYS 219 NZ  
12  1 Y 1 A ASP 201 ? CG  ? A ASP 222 CG  
13  1 Y 1 A ASP 201 ? OD1 ? A ASP 222 OD1 
14  1 Y 1 A ASP 201 ? OD2 ? A ASP 222 OD2 
15  1 Y 1 A GLU 211 ? CG  ? A GLU 232 CG  
16  1 Y 1 A GLU 211 ? CD  ? A GLU 232 CD  
17  1 Y 1 A GLU 211 ? OE1 ? A GLU 232 OE1 
18  1 Y 1 A GLU 211 ? OE2 ? A GLU 232 OE2 
19  1 Y 1 A LYS 214 ? CG  ? A LYS 235 CG  
20  1 Y 1 A LYS 214 ? CD  ? A LYS 235 CD  
21  1 Y 1 A LYS 214 ? CE  ? A LYS 235 CE  
22  1 Y 1 A LYS 214 ? NZ  ? A LYS 235 NZ  
23  1 Y 1 A VAL 217 ? CG1 ? A VAL 238 CG1 
24  1 Y 1 A VAL 217 ? CG2 ? A VAL 238 CG2 
25  1 Y 1 A LYS 221 ? CG  ? A LYS 242 CG  
26  1 Y 1 A LYS 221 ? CD  ? A LYS 242 CD  
27  1 Y 1 A LYS 221 ? CE  ? A LYS 242 CE  
28  1 Y 1 A LYS 221 ? NZ  ? A LYS 242 NZ  
29  1 Y 1 A ARG 222 ? CG  ? A ARG 243 CG  
30  1 Y 1 A ARG 222 ? CD  ? A ARG 243 CD  
31  1 Y 1 A ARG 222 ? NE  ? A ARG 243 NE  
32  1 Y 1 A ARG 222 ? CZ  ? A ARG 243 CZ  
33  1 Y 1 A ARG 222 ? NH1 ? A ARG 243 NH1 
34  1 Y 1 A ARG 222 ? NH2 ? A ARG 243 NH2 
35  1 Y 1 A GLU 229 ? CG  ? A GLU 250 CG  
36  1 Y 1 A GLU 229 ? CD  ? A GLU 250 CD  
37  1 Y 1 A GLU 229 ? OE1 ? A GLU 250 OE1 
38  1 Y 1 A GLU 229 ? OE2 ? A GLU 250 OE2 
39  1 Y 1 A VAL 232 ? CG1 ? A VAL 253 CG1 
40  1 Y 1 A VAL 232 ? CG2 ? A VAL 253 CG2 
41  1 Y 1 A GLN 238 ? CG  ? A GLN 259 CG  
42  1 Y 1 A GLN 238 ? CD  ? A GLN 259 CD  
43  1 Y 1 A GLN 238 ? OE1 ? A GLN 259 OE1 
44  1 Y 1 A GLN 238 ? NE2 ? A GLN 259 NE2 
45  1 Y 1 A LYS 268 ? CG  ? A LYS 289 CG  
46  1 Y 1 A LYS 268 ? CD  ? A LYS 289 CD  
47  1 Y 1 A LYS 268 ? CE  ? A LYS 289 CE  
48  1 Y 1 A LYS 268 ? NZ  ? A LYS 289 NZ  
49  1 Y 1 A GLU 279 ? CG  ? A GLU 300 CG  
50  1 Y 1 A GLU 279 ? CD  ? A GLU 300 CD  
51  1 Y 1 A GLU 279 ? OE1 ? A GLU 300 OE1 
52  1 Y 1 A GLU 279 ? OE2 ? A GLU 300 OE2 
53  1 Y 1 B GLU 15  ? CG  ? B GLU 36  CG  
54  1 Y 1 B GLU 15  ? CD  ? B GLU 36  CD  
55  1 Y 1 B GLU 15  ? OE1 ? B GLU 36  OE1 
56  1 Y 1 B GLU 15  ? OE2 ? B GLU 36  OE2 
57  1 Y 1 B GLN 27  ? CG  ? B GLN 48  CG  
58  1 Y 1 B GLN 27  ? CD  ? B GLN 48  CD  
59  1 Y 1 B GLN 27  ? OE1 ? B GLN 48  OE1 
60  1 Y 1 B GLN 27  ? NE2 ? B GLN 48  NE2 
61  1 Y 1 B ARG 106 ? CG  ? B ARG 127 CG  
62  1 Y 1 B ARG 106 ? CD  ? B ARG 127 CD  
63  1 Y 1 B ARG 106 ? NE  ? B ARG 127 NE  
64  1 Y 1 B ARG 106 ? CZ  ? B ARG 127 CZ  
65  1 Y 1 B ARG 106 ? NH1 ? B ARG 127 NH1 
66  1 Y 1 B ARG 106 ? NH2 ? B ARG 127 NH2 
67  1 Y 1 B VAL 146 ? CG1 ? B VAL 167 CG1 
68  1 Y 1 B VAL 146 ? CG2 ? B VAL 167 CG2 
69  1 Y 1 B GLU 148 ? CG  ? B GLU 169 CG  
70  1 Y 1 B GLU 148 ? CD  ? B GLU 169 CD  
71  1 Y 1 B GLU 148 ? OE1 ? B GLU 169 OE1 
72  1 Y 1 B GLU 148 ? OE2 ? B GLU 169 OE2 
73  1 Y 1 B ARG 185 ? CG  ? B ARG 206 CG  
74  1 Y 1 B ARG 185 ? CD  ? B ARG 206 CD  
75  1 Y 1 B ARG 185 ? NE  ? B ARG 206 NE  
76  1 Y 1 B ARG 185 ? CZ  ? B ARG 206 CZ  
77  1 Y 1 B ARG 185 ? NH1 ? B ARG 206 NH1 
78  1 Y 1 B ARG 185 ? NH2 ? B ARG 206 NH2 
79  1 Y 1 B GLU 191 ? CG  ? B GLU 212 CG  
80  1 Y 1 B GLU 191 ? CD  ? B GLU 212 CD  
81  1 Y 1 B GLU 191 ? OE1 ? B GLU 212 OE1 
82  1 Y 1 B GLU 191 ? OE2 ? B GLU 212 OE2 
83  1 Y 1 B LYS 195 ? CG  ? B LYS 216 CG  
84  1 Y 1 B LYS 195 ? CD  ? B LYS 216 CD  
85  1 Y 1 B LYS 195 ? CE  ? B LYS 216 CE  
86  1 Y 1 B LYS 195 ? NZ  ? B LYS 216 NZ  
87  1 Y 1 B LYS 198 ? CG  ? B LYS 219 CG  
88  1 Y 1 B LYS 198 ? CD  ? B LYS 219 CD  
89  1 Y 1 B LYS 198 ? CE  ? B LYS 219 CE  
90  1 Y 1 B LYS 198 ? NZ  ? B LYS 219 NZ  
91  1 Y 1 B ASP 201 ? CG  ? B ASP 222 CG  
92  1 Y 1 B ASP 201 ? OD1 ? B ASP 222 OD1 
93  1 Y 1 B ASP 201 ? OD2 ? B ASP 222 OD2 
94  1 Y 1 B ARG 203 ? CG  ? B ARG 224 CG  
95  1 Y 1 B ARG 203 ? CD  ? B ARG 224 CD  
96  1 Y 1 B ARG 203 ? NE  ? B ARG 224 NE  
97  1 Y 1 B ARG 203 ? CZ  ? B ARG 224 CZ  
98  1 Y 1 B ARG 203 ? NH1 ? B ARG 224 NH1 
99  1 Y 1 B ARG 203 ? NH2 ? B ARG 224 NH2 
100 1 Y 1 B LYS 214 ? CG  ? B LYS 235 CG  
101 1 Y 1 B LYS 214 ? CD  ? B LYS 235 CD  
102 1 Y 1 B LYS 214 ? CE  ? B LYS 235 CE  
103 1 Y 1 B LYS 214 ? NZ  ? B LYS 235 NZ  
104 1 Y 1 B LYS 221 ? CG  ? B LYS 242 CG  
105 1 Y 1 B LYS 221 ? CD  ? B LYS 242 CD  
106 1 Y 1 B LYS 221 ? CE  ? B LYS 242 CE  
107 1 Y 1 B LYS 221 ? NZ  ? B LYS 242 NZ  
108 1 Y 1 B ARG 222 ? CG  ? B ARG 243 CG  
109 1 Y 1 B ARG 222 ? CD  ? B ARG 243 CD  
110 1 Y 1 B ARG 222 ? NE  ? B ARG 243 NE  
111 1 Y 1 B ARG 222 ? CZ  ? B ARG 243 CZ  
112 1 Y 1 B ARG 222 ? NH1 ? B ARG 243 NH1 
113 1 Y 1 B ARG 222 ? NH2 ? B ARG 243 NH2 
114 1 Y 1 B VAL 224 ? CG1 ? B VAL 245 CG1 
115 1 Y 1 B VAL 224 ? CG2 ? B VAL 245 CG2 
116 1 Y 1 B ASP 226 ? CG  ? B ASP 247 CG  
117 1 Y 1 B ASP 226 ? OD1 ? B ASP 247 OD1 
118 1 Y 1 B ASP 226 ? OD2 ? B ASP 247 OD2 
119 1 Y 1 B ASP 228 ? CG  ? B ASP 249 CG  
120 1 Y 1 B ASP 228 ? OD1 ? B ASP 249 OD1 
121 1 Y 1 B ASP 228 ? OD2 ? B ASP 249 OD2 
122 1 Y 1 B VAL 232 ? CG1 ? B VAL 253 CG1 
123 1 Y 1 B VAL 232 ? CG2 ? B VAL 253 CG2 
124 1 Y 1 B ARG 234 ? CG  ? B ARG 255 CG  
125 1 Y 1 B ARG 234 ? CD  ? B ARG 255 CD  
126 1 Y 1 B ARG 234 ? NE  ? B ARG 255 NE  
127 1 Y 1 B ARG 234 ? CZ  ? B ARG 255 CZ  
128 1 Y 1 B ARG 234 ? NH1 ? B ARG 255 NH1 
129 1 Y 1 B ARG 234 ? NH2 ? B ARG 255 NH2 
130 1 Y 1 B TYR 235 ? CG  ? B TYR 256 CG  
131 1 Y 1 B TYR 235 ? CD1 ? B TYR 256 CD1 
132 1 Y 1 B TYR 235 ? CD2 ? B TYR 256 CD2 
133 1 Y 1 B TYR 235 ? CE1 ? B TYR 256 CE1 
134 1 Y 1 B TYR 235 ? CE2 ? B TYR 256 CE2 
135 1 Y 1 B TYR 235 ? CZ  ? B TYR 256 CZ  
136 1 Y 1 B TYR 235 ? OH  ? B TYR 256 OH  
137 1 Y 1 B ASN 245 ? CG  ? B ASN 266 CG  
138 1 Y 1 B ASN 245 ? OD1 ? B ASN 266 OD1 
139 1 Y 1 B ASN 245 ? ND2 ? B ASN 266 ND2 
140 1 Y 1 B ILE 258 ? CG1 ? B ILE 279 CG1 
141 1 Y 1 B ILE 258 ? CG2 ? B ILE 279 CG2 
142 1 Y 1 B ILE 258 ? CD1 ? B ILE 279 CD1 
143 1 Y 1 B GLU 260 ? CG  ? B GLU 281 CG  
144 1 Y 1 B GLU 260 ? CD  ? B GLU 281 CD  
145 1 Y 1 B GLU 260 ? OE1 ? B GLU 281 OE1 
146 1 Y 1 B GLU 260 ? OE2 ? B GLU 281 OE2 
147 1 Y 1 B LYS 268 ? CG  ? B LYS 289 CG  
148 1 Y 1 B LYS 268 ? CD  ? B LYS 289 CD  
149 1 Y 1 B LYS 268 ? CE  ? B LYS 289 CE  
150 1 Y 1 B LYS 268 ? NZ  ? B LYS 289 NZ  
151 1 Y 1 B HIS 272 ? CG  ? B HIS 293 CG  
152 1 Y 1 B HIS 272 ? ND1 ? B HIS 293 ND1 
153 1 Y 1 B HIS 272 ? CD2 ? B HIS 293 CD2 
154 1 Y 1 B HIS 272 ? CE1 ? B HIS 293 CE1 
155 1 Y 1 B HIS 272 ? NE2 ? B HIS 293 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? dev_5660 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        ? 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        ? 4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.93 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9O66 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     153.156 
_cell.length_a_esd                 ? 
_cell.length_b                     75.510 
_cell.length_b_esd                 ? 
_cell.length_c                     56.754 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9O66 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9O66 
_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             2.05 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.06 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Morpheus A1: 20%(v/v) PEG 500 MME, 10%(w/v) PEG 20000, 100 mM Imidazole/MES, pH 6.5, 30 mM MgCl2 and 30 mM CaCl2. KlaeA.00241.a.UX1.PW39324 at 11.1 mg/mL. plate 19612 A1 drop 1. Puck: PSL-1906, Cryo: Direct
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-12-15 
_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                    'Double Crystal Si 111' 
_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   0.9786 
_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                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9O66 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               47.77 
_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                                     37570 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.06 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.188 
_reflns.pdbx_Rpim_I_all                                0.073 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       251613 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.978 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.173 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           20511 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3047 
_reflns_shell.percent_possible_obs                          100.0 
_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                               6.7 
_reflns_shell.pdbx_chi_squared                              0.99 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.3 
_reflns_shell.pdbx_Rrim_I_all                               1.191 
_reflns_shell.pdbx_Rpim_I_all                               0.456 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.618 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.098 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9O66 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             43.27 
_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                     37529 
_refine.ls_number_reflns_R_free                  1840 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.67 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2036 
_refine.ls_R_factor_R_free                       0.2470 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2014 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.17 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        43.27 
_refine_hist.number_atoms_solvent             169 
_refine_hist.number_atoms_total               4987 
_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        4807 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         11 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? 4937 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.544  ? 6705 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 17.073 ? 1782 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 757  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 880  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.10 2.16  . . 145 2715 100.00 . . . . 0.2691 . . . . . . . . . . . . . . . 0.3128 
'X-RAY DIFFRACTION' 2.16 2.22  . . 155 2705 100.00 . . . . 0.2554 . . . . . . . . . . . . . . . 0.2905 
'X-RAY DIFFRACTION' 2.22 2.29  . . 136 2712 98.00  . . . . 0.2835 . . . . . . . . . . . . . . . 0.3193 
'X-RAY DIFFRACTION' 2.29 2.37  . . 134 2746 100.00 . . . . 0.2289 . . . . . . . . . . . . . . . 0.2808 
'X-RAY DIFFRACTION' 2.37 2.47  . . 139 2747 100.00 . . . . 0.2168 . . . . . . . . . . . . . . . 0.2795 
'X-RAY DIFFRACTION' 2.47 2.58  . . 139 2752 100.00 . . . . 0.2119 . . . . . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 2.58 2.72  . . 141 2706 100.00 . . . . 0.2003 . . . . . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 2.72 2.89  . . 160 2731 100.00 . . . . 0.1948 . . . . . . . . . . . . . . . 0.2494 
'X-RAY DIFFRACTION' 2.89 3.11  . . 148 2748 100.00 . . . . 0.2030 . . . . . . . . . . . . . . . 0.2656 
'X-RAY DIFFRACTION' 3.11 3.42  . . 121 2785 100.00 . . . . 0.1968 . . . . . . . . . . . . . . . 0.2668 
'X-RAY DIFFRACTION' 3.42 3.92  . . 132 2757 99.00  . . . . 0.1839 . . . . . . . . . . . . . . . 0.2056 
'X-RAY DIFFRACTION' 3.92 4.93  . . 146 2754 99.00  . . . . 0.1620 . . . . . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 4.94 43.27 . . 144 2831 100.00 . . . . 0.1963 . . . . . . . . . . . . . . . 0.2382 
# 
_struct.entry_id                     9O66 
_struct.title                        'Crystal Structure of Tryptophanyl-tRNA synthetase from Klebsiella aerogenes' 
_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        9O66 
_struct_keywords.text            
;SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, Tryptophanyl-tRNA synthetase, Klebsiella aerogenes, LIGASE
;
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0H3FKK2_KLEAK 
_struct_ref.pdbx_db_accession          A0A0H3FKK2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDPQNLRKATLDTLALYLACGIDPQKSTIF
VQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNQVPVGEDQKQHLELSRDV
AQRFNAIYGDIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNK
AGVSNLLDILSAVTGQSIPELEQHFEGKMYGHLKGEVAEAVSGMLTELQERYHRFRNDEAFLNQVMKEGAEKASAHASKT
LKAVYEAIGFVAKP
;
_struct_ref.pdbx_align_begin           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 9O66 A 22 ? 355 ? A0A0H3FKK2 1 ? 334 ? 1 334 
2 1 9O66 B 22 ? 355 ? A0A0H3FKK2 1 ? 334 ? 1 334 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9O66 MET A 1  ? UNP A0A0H3FKK2 ? ? 'initiating methionine' -20 1  
1 9O66 ALA A 2  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -19 2  
1 9O66 HIS A 3  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -18 3  
1 9O66 HIS A 4  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -17 4  
1 9O66 HIS A 5  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -16 5  
1 9O66 HIS A 6  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -15 6  
1 9O66 HIS A 7  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -14 7  
1 9O66 HIS A 8  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -13 8  
1 9O66 MET A 9  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -12 9  
1 9O66 GLY A 10 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -11 10 
1 9O66 THR A 11 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -10 11 
1 9O66 LEU A 12 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -9  12 
1 9O66 GLU A 13 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -8  13 
1 9O66 ALA A 14 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -7  14 
1 9O66 GLN A 15 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -6  15 
1 9O66 THR A 16 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -5  16 
1 9O66 GLN A 17 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -4  17 
1 9O66 GLY A 18 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -3  18 
1 9O66 PRO A 19 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -2  19 
1 9O66 GLY A 20 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -1  20 
1 9O66 SER A 21 ? UNP A0A0H3FKK2 ? ? 'expression tag'        0   21 
2 9O66 MET B 1  ? UNP A0A0H3FKK2 ? ? 'initiating methionine' -20 22 
2 9O66 ALA B 2  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -19 23 
2 9O66 HIS B 3  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -18 24 
2 9O66 HIS B 4  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -17 25 
2 9O66 HIS B 5  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -16 26 
2 9O66 HIS B 6  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -15 27 
2 9O66 HIS B 7  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -14 28 
2 9O66 HIS B 8  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -13 29 
2 9O66 MET B 9  ? UNP A0A0H3FKK2 ? ? 'expression tag'        -12 30 
2 9O66 GLY B 10 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -11 31 
2 9O66 THR B 11 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -10 32 
2 9O66 LEU B 12 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -9  33 
2 9O66 GLU B 13 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -8  34 
2 9O66 ALA B 14 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -7  35 
2 9O66 GLN B 15 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -6  36 
2 9O66 THR B 16 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -5  37 
2 9O66 GLN B 17 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -4  38 
2 9O66 GLY B 18 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -3  39 
2 9O66 PRO B 19 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -2  40 
2 9O66 GLY B 20 ? UNP A0A0H3FKK2 ? ? 'expression tag'        -1  41 
2 9O66 SER B 21 ? UNP A0A0H3FKK2 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5180  ? 
1 MORE         -33   ? 
1 'SSA (A^2)'  26780 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 38  ? ALA A 45  ? THR A 17  ALA A 24  1 ? 8  
HELX_P HELX_P2  AA2 ALA A 45  ? ASN A 51  ? ALA A 24  ASN A 30  1 ? 7  
HELX_P HELX_P3  AA3 VAL A 63  ? ILE A 68  ? VAL A 42  ILE A 47  1 ? 6  
HELX_P HELX_P4  AA4 ASP A 73  ? GLY A 92  ? ASP A 52  GLY A 71  1 ? 20 
HELX_P HELX_P5  AA5 SER A 104 ? VAL A 106 ? SER A 83  VAL A 85  5 ? 3  
HELX_P HELX_P6  AA6 PRO A 107 ? CYS A 118 ? PRO A 86  CYS A 97  1 ? 12 
HELX_P HELX_P7  AA7 TYR A 121 ? ARG A 127 ? TYR A 100 ARG A 106 1 ? 7  
HELX_P HELX_P8  AA8 ASN A 143 ? LEU A 159 ? ASN A 122 LEU A 138 1 ? 17 
HELX_P HELX_P9  AA9 GLY A 168 ? ASP A 170 ? GLY A 147 ASP A 149 5 ? 3  
HELX_P HELX_P10 AB1 GLN A 171 ? GLY A 190 ? GLN A 150 GLY A 169 1 ? 20 
HELX_P HELX_P11 AB2 ASN A 223 ? VAL A 227 ? ASN A 202 VAL A 206 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 233 ? ARG A 243 ? ASP A 212 ARG A 222 1 ? 11 
HELX_P HELX_P13 AB4 LYS A 261 ? GLY A 276 ? LYS A 240 GLY A 255 1 ? 16 
HELX_P HELX_P14 AB5 SER A 278 ? PHE A 286 ? SER A 257 PHE A 265 1 ? 9  
HELX_P HELX_P15 AB6 MET A 290 ? ASN A 318 ? MET A 269 ASN A 297 1 ? 29 
HELX_P HELX_P16 AB7 ASP A 319 ? GLY A 350 ? ASP A 298 GLY A 329 1 ? 32 
HELX_P HELX_P17 AB8 THR B 38  ? ALA B 45  ? THR B 17  ALA B 24  1 ? 8  
HELX_P HELX_P18 AB9 ALA B 45  ? MET B 52  ? ALA B 24  MET B 31  1 ? 8  
HELX_P HELX_P19 AC1 VAL B 63  ? ILE B 68  ? VAL B 42  ILE B 47  1 ? 6  
HELX_P HELX_P20 AC2 ASP B 73  ? GLY B 92  ? ASP B 52  GLY B 71  1 ? 20 
HELX_P HELX_P21 AC3 SER B 104 ? VAL B 106 ? SER B 83  VAL B 85  5 ? 3  
HELX_P HELX_P22 AC4 PRO B 107 ? CYS B 118 ? PRO B 86  CYS B 97  1 ? 12 
HELX_P HELX_P23 AC5 TYR B 121 ? MET B 128 ? TYR B 100 MET B 107 1 ? 8  
HELX_P HELX_P24 AC6 ASN B 143 ? LEU B 159 ? ASN B 122 LEU B 138 1 ? 17 
HELX_P HELX_P25 AC7 GLY B 168 ? ASP B 170 ? GLY B 147 ASP B 149 5 ? 3  
HELX_P HELX_P26 AC8 GLN B 171 ? GLY B 190 ? GLN B 150 GLY B 169 1 ? 20 
HELX_P HELX_P27 AC9 ASN B 223 ? VAL B 227 ? ASN B 202 VAL B 206 5 ? 5  
HELX_P HELX_P28 AD1 ASP B 233 ? ARG B 243 ? ASP B 212 ARG B 222 1 ? 11 
HELX_P HELX_P29 AD2 GLY B 263 ? GLY B 276 ? GLY B 242 GLY B 255 1 ? 14 
HELX_P HELX_P30 AD3 SER B 278 ? PHE B 286 ? SER B 257 PHE B 265 1 ? 9  
HELX_P HELX_P31 AD4 MET B 290 ? ASN B 318 ? MET B 269 ASN B 297 1 ? 29 
HELX_P HELX_P32 AD5 ASP B 319 ? GLY B 350 ? ASP B 298 GLY B 329 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A ASP 180 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 159 B CA  401 4_555 ? ? ? ? ? ? ? 2.472 ? ? 
metalc2 metalc ? ? A GLN 183 OE1 ? ? ? 1_555 D CA  . CA ? ? A GLN 162 B CA  401 4_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc3 metalc ? ? F HOH .   O   ? ? ? 4_545 D CA  . CA ? ? A HOH 533 B CA  401 1_555 ? ? ? ? ? ? ? 2.245 ? ? 
metalc4 metalc ? ? B ASP 94  OD1 ? ? ? 1_555 D CA  . CA ? ? B ASP 73  B CA  401 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc5 metalc ? ? B ASP 94  OD2 ? ? ? 1_555 D CA  . CA ? ? B ASP 73  B CA  401 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc6 metalc ? ? B GLN 96  OE1 ? ? ? 1_555 D CA  . CA ? ? B GLN 75  B CA  401 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc7 metalc ? ? D CA  .   CA  ? ? ? 1_555 G HOH . O  ? ? B CA  401 B HOH 562 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 180 ? A ASP 159 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OE1 ? A GLN 183 ? A GLN 162 ? 1_555 91.0 ? 
2  OD1 ? A ASP 180 ? A ASP 159 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 O   ? F HOH .   ? A HOH 533 ? 4_545 65.8 ? 
3  OE1 ? A GLN 183 ? A GLN 162 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 O   ? F HOH .   ? A HOH 533 ? 4_545 48.1 ? 
4  OD1 ? A ASP 180 ? A ASP 159 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OD1 ? B ASP 94  ? B ASP 73  ? 1_555 63.9 ? 
5  OE1 ? A GLN 183 ? A GLN 162 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OD1 ? B ASP 94  ? B ASP 73  ? 1_555 49.3 ? 
6  O   ? F HOH .   ? A HOH 533 ? 4_545 CA ? D CA . ? B CA 401 ? 4_555 OD1 ? B ASP 94  ? B ASP 73  ? 1_555 2.0  ? 
7  OD1 ? A ASP 180 ? A ASP 159 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OD2 ? B ASP 94  ? B ASP 73  ? 1_555 64.5 ? 
8  OE1 ? A GLN 183 ? A GLN 162 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OD2 ? B ASP 94  ? B ASP 73  ? 1_555 50.3 ? 
9  O   ? F HOH .   ? A HOH 533 ? 4_545 CA ? D CA . ? B CA 401 ? 4_555 OD2 ? B ASP 94  ? B ASP 73  ? 1_555 2.2  ? 
10 OD1 ? B ASP 94  ? B ASP 73  ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OD2 ? B ASP 94  ? B ASP 73  ? 1_555 1.4  ? 
11 OD1 ? A ASP 180 ? A ASP 159 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OE1 ? B GLN 96  ? B GLN 75  ? 1_555 65.2 ? 
12 OE1 ? A GLN 183 ? A GLN 162 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OE1 ? B GLN 96  ? B GLN 75  ? 1_555 46.1 ? 
13 O   ? F HOH .   ? A HOH 533 ? 4_545 CA ? D CA . ? B CA 401 ? 4_555 OE1 ? B GLN 96  ? B GLN 75  ? 1_555 2.6  ? 
14 OD1 ? B ASP 94  ? B ASP 73  ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OE1 ? B GLN 96  ? B GLN 75  ? 1_555 3.2  ? 
15 OD2 ? B ASP 94  ? B ASP 73  ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 OE1 ? B GLN 96  ? B GLN 75  ? 1_555 4.3  ? 
16 OD1 ? A ASP 180 ? A ASP 159 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 O   ? G HOH .   ? B HOH 562 ? 1_555 67.3 ? 
17 OE1 ? A GLN 183 ? A GLN 162 ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 O   ? G HOH .   ? B HOH 562 ? 1_555 47.6 ? 
18 O   ? F HOH .   ? A HOH 533 ? 4_545 CA ? D CA . ? B CA 401 ? 4_555 O   ? G HOH .   ? B HOH 562 ? 1_555 1.4  ? 
19 OD1 ? B ASP 94  ? B ASP 73  ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 O   ? G HOH .   ? B HOH 562 ? 1_555 3.4  ? 
20 OD2 ? B ASP 94  ? B ASP 73  ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 O   ? G HOH .   ? B HOH 562 ? 1_555 3.2  ? 
21 OE1 ? B GLN 96  ? B GLN 75  ? 1_555 CA ? D CA . ? B CA 401 ? 4_555 O   ? G HOH .   ? B HOH 562 ? 1_555 3.3  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 250 A . ? GLU 229 A PRO 251 A ? PRO 230 A 1 -0.54 
2 GLU 250 B . ? GLU 229 B PRO 251 B ? PRO 230 B 1 -3.45 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA3 1 2 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 26  ? ALA A 31  ? ILE A 5   ALA A 10  
AA1 2 HIS A 57  ? ILE A 62  ? HIS A 36  ILE A 41  
AA1 3 THR A 99  ? VAL A 102 ? THR A 78  VAL A 81  
AA2 1 ILE B 26  ? ALA B 31  ? ILE B 5   ALA B 10  
AA2 2 HIS B 57  ? ILE B 62  ? HIS B 36  ILE B 41  
AA2 3 THR B 99  ? VAL B 102 ? THR B 78  VAL B 81  
AA3 1 GLN B 164 ? VAL B 165 ? GLN B 143 VAL B 144 
AA3 2 GLU B 197 ? PRO B 198 ? GLU B 176 PRO B 177 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ALA A 31  ? N ALA A 10  O CYS A 61  ? O CYS A 40  
AA1 2 3 N TYR A 60  ? N TYR A 39  O THR A 99  ? O THR A 78  
AA2 1 2 N ALA B 31  ? N ALA B 10  O CYS B 61  ? O CYS B 40  
AA2 2 3 N TYR B 60  ? N TYR B 39  O THR B 99  ? O THR B 78  
AA3 1 2 N VAL B 165 ? N VAL B 144 O GLU B 197 ? O GLU B 176 
# 
_pdbx_entry_details.entry_id                   9O66 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 24  ? ? -95.72  -62.17  
2 1 GLU A 119 ? ? 73.91   -158.92 
3 1 GLU B 191 ? ? -155.26 65.67   
4 1 LEU B 210 ? ? -98.87  33.44   
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 16.6710 -0.5707  25.4032  0.4597 ? -0.0391 ? 0.0534  ? 0.3749 ? -0.0342 ? 0.3839 ? 1.7379 ? 
-0.5163 ? -1.4200 ? 2.2525 ? -0.6671 ? 1.7242 ? -0.2602 ? -0.5943 ? 0.4906  ? 0.8907  ? -0.0846 ? 0.2393  ? -0.2739 ? 0.1238  ? 
0.3360  ? 
2  'X-RAY DIFFRACTION' ? refined 25.5075 2.1569   17.7948  0.2387 ? -0.0015 ? 0.0117  ? 0.1652 ? -0.0120 ? 0.1832 ? 0.9047 ? 
0.1256  ? -0.1855 ? 1.2301 ? -0.1181 ? 1.1547 ? 0.0138  ? -0.1059 ? 0.0170  ? 0.1793  ? -0.0225 ? 0.2133  ? -0.0377 ? -0.0929 ? 
0.0117  ? 
3  'X-RAY DIFFRACTION' ? refined 16.7784 9.5126   25.4100  0.5711 ? 0.0054  ? -0.0051 ? 0.3763 ? -0.0097 ? 0.4049 ? 0.6112 ? 
0.3377  ? -0.4600 ? 0.3151 ? 0.0662  ? 3.6636 ? 0.1600  ? -0.0906 ? 0.0758  ? 0.4533  ? -0.0097 ? 0.1502  ? 0.1800  ? -0.8152 ? 
-0.0948 ? 
4  'X-RAY DIFFRACTION' ? refined 17.4098 -1.2242  43.8968  0.6207 ? -0.0745 ? 0.0904  ? 0.6103 ? -0.0800 ? 0.6328 ? 1.9162 ? 
-0.7146 ? 1.1094  ? 2.4090 ? 2.1108  ? 3.6329 ? 0.2782  ? -0.1685 ? -0.1297 ? -0.1934 ? -0.3363 ? -0.1260 ? 0.3255  ? -0.3323 ? 
0.1193  ? 
5  'X-RAY DIFFRACTION' ? refined 4.3425  1.4842   42.6794  0.4940 ? -0.1229 ? 0.1239  ? 0.7079 ? -0.2727 ? 0.8739 ? 0.9212 ? 
-0.2230 ? 0.3486  ? 0.9893 ? 0.3758  ? 1.0871 ? 0.0430  ? -0.3838 ? 0.4328  ? 0.1390  ? -0.4652 ? 0.6709  ? -0.0628 ? -0.6044 ? 
0.3842  ? 
6  'X-RAY DIFFRACTION' ? refined 26.7789 -8.3496  6.9259   0.3472 ? -0.0705 ? -0.0056 ? 0.1943 ? -0.0151 ? 0.2575 ? 0.9766 ? 
0.7366  ? -1.2735 ? 0.9209 ? -1.0986 ? 2.3153 ? -0.0806 ? 0.0040  ? -0.1677 ? 0.0384  ? -0.0170 ? 0.0716  ? 0.4560  ? -0.1221 ? 
0.0603  ? 
7  'X-RAY DIFFRACTION' ? refined 57.9055 -3.0469  -2.1337  0.2827 ? -0.0027 ? 0.0135  ? 0.3201 ? 0.0438  ? 0.2921 ? 2.2418 ? 
-0.0032 ? -0.9357 ? 0.0710 ? 0.2943  ? 1.6096 ? 0.0640  ? -0.0768 ? 0.3438  ? -0.3218 ? -0.0715 ? -0.4464 ? -0.0463 ? 0.3110  ? 
-0.0044 ? 
8  'X-RAY DIFFRACTION' ? refined 48.0085 -1.4224  2.3103   0.2120 ? -0.0168 ? -0.0246 ? 0.1923 ? 0.0032  ? 0.1473 ? 0.4778 ? 
-0.1784 ? -0.5704 ? 0.9098 ? 0.7444  ? 1.3241 ? -0.0141 ? -0.0635 ? 0.0162  ? 0.0321  ? 0.0192  ? -0.0831 ? 0.0032  ? 0.1525  ? 
-0.0071 ? 
9  'X-RAY DIFFRACTION' ? refined 50.1313 -0.9171  10.6627  0.2442 ? -0.0392 ? -0.0184 ? 0.2439 ? -0.0205 ? 0.1450 ? 1.7310 ? 
-1.4739 ? -0.1075 ? 3.0280 ? 0.2978  ? 1.1556 ? 0.1199  ? -0.1617 ? 0.2105  ? -0.2686 ? 0.0231  ? -0.2501 ? -0.0465 ? 0.4062  ? 
-0.1689 ? 
10 'X-RAY DIFFRACTION' ? refined 53.8412 -0.4144  18.4901  0.2775 ? -0.0528 ? -0.0706 ? 0.3126 ? -0.0229 ? 0.2796 ? 3.3588 ? 
0.6265  ? -0.6330 ? 3.6957 ? -0.8907 ? 3.2066 ? -0.1708 ? 0.1279  ? 0.5615  ? -0.1022 ? 0.0611  ? -0.4935 ? -0.1949 ? 0.4844  ? 
0.0783  ? 
11 'X-RAY DIFFRACTION' ? refined 62.6452 -1.3762  6.2484   0.2450 ? -0.1241 ? -0.0993 ? 0.4445 ? -0.0158 ? 0.3461 ? 1.9179 ? 
0.9680  ? -2.2347 ? 1.5587 ? -1.8335 ? 3.0641 ? -0.2582 ? -0.2698 ? 0.0242  ? -0.1416 ? -0.0542 ? -0.3704 ? 0.0332  ? 0.6050  ? 
0.3231  ? 
12 'X-RAY DIFFRACTION' ? refined 61.9370 10.5163  -10.4648 0.3966 ? -0.0546 ? 0.0070  ? 0.5775 ? 0.0743  ? 0.8359 ? 2.0687 ? 
1.0868  ? 0.1749  ? 3.0647 ? 0.3345  ? 0.9254 ? -0.0749 ? -0.3355 ? 1.2050  ? 0.0018  ? -0.2078 ? 0.2866  ? -0.5001 ? 0.0177  ? 
0.2945  ? 
13 'X-RAY DIFFRACTION' ? refined 70.9375 4.1061   -17.7302 0.3972 ? -0.0291 ? 0.0471  ? 0.7118 ? 0.1896  ? 0.7206 ? 1.5617 ? 
0.3490  ? -0.8384 ? 1.2240 ? -0.0135 ? 0.6632 ? -0.0804 ? 0.1724  ? -0.0082 ? -0.3298 ? -0.1033 ? -0.8839 ? 0.0248  ? 0.5951  ? 
0.1362  ? 
14 'X-RAY DIFFRACTION' ? refined 40.4439 -12.8042 6.3909   0.2176 ? -0.0135 ? -0.0351 ? 0.1217 ? 0.0102  ? 0.1853 ? 0.5549 ? 
-0.2987 ? -0.5676 ? 0.9678 ? 0.3820  ? 2.7763 ? 0.0490  ? -0.0607 ? -0.0691 ? 0.1630  ? -0.0428 ? 0.0875  ? 0.0926  ? 0.1455  ? 
-0.0198 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 24 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 25 through 168 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 169 through 195 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 196 through 221 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 222 through 298 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 299 through 334 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 24 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 25 through 122 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 123 through 147 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 148 through 168 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 169 through 191 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 192 through 212 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 213 through 298 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 299 through 334 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -20 ? A MET 1   
2  1 Y 1 A ALA -19 ? A ALA 2   
3  1 Y 1 A HIS -18 ? A HIS 3   
4  1 Y 1 A HIS -17 ? A HIS 4   
5  1 Y 1 A HIS -16 ? A HIS 5   
6  1 Y 1 A HIS -15 ? A HIS 6   
7  1 Y 1 A HIS -14 ? A HIS 7   
8  1 Y 1 A HIS -13 ? A HIS 8   
9  1 Y 1 A MET -12 ? A MET 9   
10 1 Y 1 A GLY -11 ? A GLY 10  
11 1 Y 1 A THR -10 ? A THR 11  
12 1 Y 1 A LEU -9  ? A LEU 12  
13 1 Y 1 A GLU -8  ? A GLU 13  
14 1 Y 1 A ALA -7  ? A ALA 14  
15 1 Y 1 A GLN -6  ? A GLN 15  
16 1 Y 1 A THR -5  ? A THR 16  
17 1 Y 1 A GLN -4  ? A GLN 17  
18 1 Y 1 A GLY -3  ? A GLY 18  
19 1 Y 1 A PRO -2  ? A PRO 19  
20 1 Y 1 A GLY -1  ? A GLY 20  
21 1 Y 1 A SER 0   ? A SER 21  
22 1 Y 1 A MET 1   ? A MET 22  
23 1 Y 1 A THR 2   ? A THR 23  
24 1 Y 1 A PHE 110 ? A PHE 131 
25 1 Y 1 A LYS 111 ? A LYS 132 
26 1 Y 1 A ASP 112 ? A ASP 133 
27 1 Y 1 A LYS 113 ? A LYS 134 
28 1 Y 1 A SER 114 ? A SER 135 
29 1 Y 1 A ALA 115 ? A ALA 136 
30 1 Y 1 A ARG 116 ? A ARG 137 
31 1 Y 1 A TYR 117 ? A TYR 138 
32 1 Y 1 A PHE 178 ? A PHE 199 
33 1 Y 1 A ILE 179 ? A ILE 200 
34 1 Y 1 A PRO 180 ? A PRO 201 
35 1 Y 1 A LYS 181 ? A LYS 202 
36 1 Y 1 A SER 182 ? A SER 203 
37 1 Y 1 A GLY 183 ? A GLY 204 
38 1 Y 1 A ALA 184 ? A ALA 205 
39 1 Y 1 B MET -20 ? B MET 1   
40 1 Y 1 B ALA -19 ? B ALA 2   
41 1 Y 1 B HIS -18 ? B HIS 3   
42 1 Y 1 B HIS -17 ? B HIS 4   
43 1 Y 1 B HIS -16 ? B HIS 5   
44 1 Y 1 B HIS -15 ? B HIS 6   
45 1 Y 1 B HIS -14 ? B HIS 7   
46 1 Y 1 B HIS -13 ? B HIS 8   
47 1 Y 1 B MET -12 ? B MET 9   
48 1 Y 1 B GLY -11 ? B GLY 10  
49 1 Y 1 B THR -10 ? B THR 11  
50 1 Y 1 B LEU -9  ? B LEU 12  
51 1 Y 1 B GLU -8  ? B GLU 13  
52 1 Y 1 B ALA -7  ? B ALA 14  
53 1 Y 1 B GLN -6  ? B GLN 15  
54 1 Y 1 B THR -5  ? B THR 16  
55 1 Y 1 B GLN -4  ? B GLN 17  
56 1 Y 1 B GLY -3  ? B GLY 18  
57 1 Y 1 B PRO -2  ? B PRO 19  
58 1 Y 1 B GLY -1  ? B GLY 20  
59 1 Y 1 B SER 0   ? B SER 21  
60 1 Y 1 B MET 1   ? B MET 22  
61 1 Y 1 B GLN 109 ? B GLN 130 
62 1 Y 1 B PHE 110 ? B PHE 131 
63 1 Y 1 B LYS 111 ? B LYS 132 
64 1 Y 1 B ASP 112 ? B ASP 133 
65 1 Y 1 B LYS 113 ? B LYS 134 
66 1 Y 1 B SER 114 ? B SER 135 
67 1 Y 1 B ALA 115 ? B ALA 136 
68 1 Y 1 B ARG 116 ? B ARG 137 
69 1 Y 1 B TYR 117 ? B TYR 138 
70 1 Y 1 B ALA 118 ? B ALA 139 
71 1 Y 1 B LYS 181 ? B LYS 202 
72 1 Y 1 B SER 182 ? B SER 203 
73 1 Y 1 B THR 193 ? B THR 214 
74 1 Y 1 B LYS 194 ? B LYS 215 
75 1 Y 1 B VAL 237 ? B VAL 258 
76 1 Y 1 B GLN 238 ? B GLN 259 
77 1 Y 1 B ASN 239 ? B ASN 260 
78 1 Y 1 B LYS 240 ? B LYS 261 
79 1 Y 1 B GLU 266 ? B GLU 287 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
IMD N1   N  Y N 184 
IMD C2   C  Y N 185 
IMD N3   N  Y N 186 
IMD C4   C  Y N 187 
IMD C5   C  Y N 188 
IMD HN1  H  N N 189 
IMD H2   H  N N 190 
IMD HN3  H  N N 191 
IMD H4   H  N N 192 
IMD H5   H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
IMD N1  C2   sing Y N 173 
IMD N1  C5   sing Y N 174 
IMD N1  HN1  sing N N 175 
IMD C2  N3   doub Y N 176 
IMD C2  H2   sing N N 177 
IMD N3  C4   sing Y N 178 
IMD N3  HN3  sing N N 179 
IMD C4  C5   doub Y N 180 
IMD C4  H4   sing N N 181 
IMD C5  H5   sing N N 182 
LEU N   CA   sing N N 183 
LEU N   H    sing N N 184 
LEU N   H2   sing N N 185 
LEU CA  C    sing N N 186 
LEU CA  CB   sing N N 187 
LEU CA  HA   sing N N 188 
LEU C   O    doub N N 189 
LEU C   OXT  sing N N 190 
LEU CB  CG   sing N N 191 
LEU CB  HB2  sing N N 192 
LEU CB  HB3  sing N N 193 
LEU CG  CD1  sing N N 194 
LEU CG  CD2  sing N N 195 
LEU CG  HG   sing N N 196 
LEU CD1 HD11 sing N N 197 
LEU CD1 HD12 sing N N 198 
LEU CD1 HD13 sing N N 199 
LEU CD2 HD21 sing N N 200 
LEU CD2 HD22 sing N N 201 
LEU CD2 HD23 sing N N 202 
LEU OXT HXT  sing N N 203 
LYS N   CA   sing N N 204 
LYS N   H    sing N N 205 
LYS N   H2   sing N N 206 
LYS CA  C    sing N N 207 
LYS CA  CB   sing N N 208 
LYS CA  HA   sing N N 209 
LYS C   O    doub N N 210 
LYS C   OXT  sing N N 211 
LYS CB  CG   sing N N 212 
LYS CB  HB2  sing N N 213 
LYS CB  HB3  sing N N 214 
LYS CG  CD   sing N N 215 
LYS CG  HG2  sing N N 216 
LYS CG  HG3  sing N N 217 
LYS CD  CE   sing N N 218 
LYS CD  HD2  sing N N 219 
LYS CD  HD3  sing N N 220 
LYS CE  NZ   sing N N 221 
LYS CE  HE2  sing N N 222 
LYS CE  HE3  sing N N 223 
LYS NZ  HZ1  sing N N 224 
LYS NZ  HZ2  sing N N 225 
LYS NZ  HZ3  sing N N 226 
LYS OXT HXT  sing N N 227 
MET N   CA   sing N N 228 
MET N   H    sing N N 229 
MET N   H2   sing N N 230 
MET CA  C    sing N N 231 
MET CA  CB   sing N N 232 
MET CA  HA   sing N N 233 
MET C   O    doub N N 234 
MET C   OXT  sing N N 235 
MET CB  CG   sing N N 236 
MET CB  HB2  sing N N 237 
MET CB  HB3  sing N N 238 
MET CG  SD   sing N N 239 
MET CG  HG2  sing N N 240 
MET CG  HG3  sing N N 241 
MET SD  CE   sing N N 242 
MET CE  HE1  sing N N 243 
MET CE  HE2  sing N N 244 
MET CE  HE3  sing N N 245 
MET OXT HXT  sing N N 246 
PHE N   CA   sing N N 247 
PHE N   H    sing N N 248 
PHE N   H2   sing N N 249 
PHE CA  C    sing N N 250 
PHE CA  CB   sing N N 251 
PHE CA  HA   sing N N 252 
PHE C   O    doub N N 253 
PHE C   OXT  sing N N 254 
PHE CB  CG   sing N N 255 
PHE CB  HB2  sing N N 256 
PHE CB  HB3  sing N N 257 
PHE CG  CD1  doub Y N 258 
PHE CG  CD2  sing Y N 259 
PHE CD1 CE1  sing Y N 260 
PHE CD1 HD1  sing N N 261 
PHE CD2 CE2  doub Y N 262 
PHE CD2 HD2  sing N N 263 
PHE CE1 CZ   doub Y N 264 
PHE CE1 HE1  sing N N 265 
PHE CE2 CZ   sing Y N 266 
PHE CE2 HE2  sing N N 267 
PHE CZ  HZ   sing N N 268 
PHE OXT HXT  sing N N 269 
PRO N   CA   sing N N 270 
PRO N   CD   sing N N 271 
PRO N   H    sing N N 272 
PRO CA  C    sing N N 273 
PRO CA  CB   sing N N 274 
PRO CA  HA   sing N N 275 
PRO C   O    doub N N 276 
PRO C   OXT  sing N N 277 
PRO CB  CG   sing N N 278 
PRO CB  HB2  sing N N 279 
PRO CB  HB3  sing N N 280 
PRO CG  CD   sing N N 281 
PRO CG  HG2  sing N N 282 
PRO CG  HG3  sing N N 283 
PRO CD  HD2  sing N N 284 
PRO CD  HD3  sing N N 285 
PRO OXT HXT  sing N N 286 
SER N   CA   sing N N 287 
SER N   H    sing N N 288 
SER N   H2   sing N N 289 
SER CA  C    sing N N 290 
SER CA  CB   sing N N 291 
SER CA  HA   sing N N 292 
SER C   O    doub N N 293 
SER C   OXT  sing N N 294 
SER CB  OG   sing N N 295 
SER CB  HB2  sing N N 296 
SER CB  HB3  sing N N 297 
SER OG  HG   sing N N 298 
SER OXT HXT  sing N N 299 
THR N   CA   sing N N 300 
THR N   H    sing N N 301 
THR N   H2   sing N N 302 
THR CA  C    sing N N 303 
THR CA  CB   sing N N 304 
THR CA  HA   sing N N 305 
THR C   O    doub N N 306 
THR C   OXT  sing N N 307 
THR CB  OG1  sing N N 308 
THR CB  CG2  sing N N 309 
THR CB  HB   sing N N 310 
THR OG1 HG1  sing N N 311 
THR CG2 HG21 sing N N 312 
THR CG2 HG22 sing N N 313 
THR CG2 HG23 sing N N 314 
THR OXT HXT  sing N N 315 
TRP N   CA   sing N N 316 
TRP N   H    sing N N 317 
TRP N   H2   sing N N 318 
TRP CA  C    sing N N 319 
TRP CA  CB   sing N N 320 
TRP CA  HA   sing N N 321 
TRP C   O    doub N N 322 
TRP C   OXT  sing N N 323 
TRP CB  CG   sing N N 324 
TRP CB  HB2  sing N N 325 
TRP CB  HB3  sing N N 326 
TRP CG  CD1  doub Y N 327 
TRP CG  CD2  sing Y N 328 
TRP CD1 NE1  sing Y N 329 
TRP CD1 HD1  sing N N 330 
TRP CD2 CE2  doub Y N 331 
TRP CD2 CE3  sing Y N 332 
TRP NE1 CE2  sing Y N 333 
TRP NE1 HE1  sing N N 334 
TRP CE2 CZ2  sing Y N 335 
TRP CE3 CZ3  doub Y N 336 
TRP CE3 HE3  sing N N 337 
TRP CZ2 CH2  doub Y N 338 
TRP CZ2 HZ2  sing N N 339 
TRP CZ3 CH2  sing Y N 340 
TRP CZ3 HZ3  sing N N 341 
TRP CH2 HH2  sing N N 342 
TRP OXT HXT  sing N N 343 
TYR N   CA   sing N N 344 
TYR N   H    sing N N 345 
TYR N   H2   sing N N 346 
TYR CA  C    sing N N 347 
TYR CA  CB   sing N N 348 
TYR CA  HA   sing N N 349 
TYR C   O    doub N N 350 
TYR C   OXT  sing N N 351 
TYR CB  CG   sing N N 352 
TYR CB  HB2  sing N N 353 
TYR CB  HB3  sing N N 354 
TYR CG  CD1  doub Y N 355 
TYR CG  CD2  sing Y N 356 
TYR CD1 CE1  sing Y N 357 
TYR CD1 HD1  sing N N 358 
TYR CD2 CE2  doub Y N 359 
TYR CD2 HD2  sing N N 360 
TYR CE1 CZ   doub Y N 361 
TYR CE1 HE1  sing N N 362 
TYR CE2 CZ   sing Y N 363 
TYR CE2 HE2  sing N N 364 
TYR CZ  OH   sing N N 365 
TYR OH  HH   sing N N 366 
TYR OXT HXT  sing N N 367 
VAL N   CA   sing N N 368 
VAL N   H    sing N N 369 
VAL N   H2   sing N N 370 
VAL CA  C    sing N N 371 
VAL CA  CB   sing N N 372 
VAL CA  HA   sing N N 373 
VAL C   O    doub N N 374 
VAL C   OXT  sing N N 375 
VAL CB  CG1  sing N N 376 
VAL CB  CG2  sing N N 377 
VAL CB  HB   sing N N 378 
VAL CG1 HG11 sing N N 379 
VAL CG1 HG12 sing N N 380 
VAL CG1 HG13 sing N N 381 
VAL CG2 HG21 sing N N 382 
VAL CG2 HG22 sing N N 383 
VAL CG2 HG23 sing N N 384 
VAL OXT HXT  sing N N 385 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00036 1 
'National Institutes of Health/Office of the Director'                                            'United States' S10OD030394    2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-A0A0H3FKK2-F1-v4 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9O66 
_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]   0.006529 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000678 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013243 
_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]   0.017715 
_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  
CA 
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   . LYS A 1 24  ? 8.136   -0.507  6.071   1.00 51.12  ? 3   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 24  ? 8.208   -0.284  7.511   1.00 47.82  ? 3   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 24  ? 9.445   0.534   7.871   1.00 43.48  ? 3   LYS A C   1 
ATOM   4    O  O   . LYS A 1 24  ? 10.530  0.257   7.367   1.00 40.88  ? 3   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 24  ? 8.233   -1.616  8.263   1.00 41.83  ? 3   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 24  ? 6.874   -2.273  8.404   1.00 52.82  ? 3   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 24  ? 6.858   -3.320  9.516   1.00 50.97  ? 3   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 24  ? 6.969   -4.736  8.975   1.00 63.83  ? 3   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 24  ? 6.596   -5.743  10.009  1.00 60.91  ? 3   LYS A NZ  1 
ATOM   10   N  N   . PRO A 1 25  ? 9.294   1.538   8.740   1.00 41.94  ? 4   PRO A N   1 
ATOM   11   C  CA  . PRO A 1 25  ? 10.464  2.326   9.143   1.00 41.97  ? 4   PRO A CA  1 
ATOM   12   C  C   . PRO A 1 25  ? 11.462  1.465   9.899   1.00 39.19  ? 4   PRO A C   1 
ATOM   13   O  O   . PRO A 1 25  ? 11.090  0.550   10.636  1.00 34.88  ? 4   PRO A O   1 
ATOM   14   C  CB  . PRO A 1 25  ? 9.877   3.419   10.046  1.00 43.42  ? 4   PRO A CB  1 
ATOM   15   C  CG  . PRO A 1 25  ? 8.408   3.378   9.836   1.00 45.43  ? 4   PRO A CG  1 
ATOM   16   C  CD  . PRO A 1 25  ? 8.076   1.978   9.443   1.00 47.32  ? 4   PRO A CD  1 
ATOM   17   N  N   . ILE A 1 26  ? 12.743  1.775   9.719   1.00 39.25  ? 5   ILE A N   1 
ATOM   18   C  CA  . ILE A 1 26  ? 13.830  1.072   10.389  1.00 35.22  ? 5   ILE A CA  1 
ATOM   19   C  C   . ILE A 1 26  ? 14.229  1.868   11.623  1.00 31.27  ? 5   ILE A C   1 
ATOM   20   O  O   . ILE A 1 26  ? 14.477  3.078   11.540  1.00 27.47  ? 5   ILE A O   1 
ATOM   21   C  CB  . ILE A 1 26  ? 15.030  0.870   9.448   1.00 35.83  ? 5   ILE A CB  1 
ATOM   22   C  CG1 . ILE A 1 26  ? 14.620  0.013   8.247   1.00 40.48  ? 5   ILE A CG1 1 
ATOM   23   C  CG2 . ILE A 1 26  ? 16.190  0.223   10.197  1.00 33.82  ? 5   ILE A CG2 1 
ATOM   24   C  CD1 . ILE A 1 26  ? 15.681  -0.095  7.171   1.00 32.69  ? 5   ILE A CD1 1 
ATOM   25   N  N   . VAL A 1 27  ? 14.280  1.192   12.768  1.00 31.56  ? 6   VAL A N   1 
ATOM   26   C  CA  . VAL A 1 27  ? 14.655  1.789   14.044  1.00 30.96  ? 6   VAL A CA  1 
ATOM   27   C  C   . VAL A 1 27  ? 15.878  1.048   14.558  1.00 29.51  ? 6   VAL A C   1 
ATOM   28   O  O   . VAL A 1 27  ? 15.878  -0.186  14.617  1.00 28.78  ? 6   VAL A O   1 
ATOM   29   C  CB  . VAL A 1 27  ? 13.509  1.713   15.071  1.00 37.28  ? 6   VAL A CB  1 
ATOM   30   C  CG1 . VAL A 1 27  ? 13.901  2.423   16.359  1.00 37.81  ? 6   VAL A CG1 1 
ATOM   31   C  CG2 . VAL A 1 27  ? 12.229  2.299   14.496  1.00 38.01  ? 6   VAL A CG2 1 
ATOM   32   N  N   . PHE A 1 28  ? 16.913  1.793   14.932  1.00 27.02  ? 7   PHE A N   1 
ATOM   33   C  CA  . PHE A 1 28  ? 18.153  1.223   15.439  1.00 29.11  ? 7   PHE A CA  1 
ATOM   34   C  C   . PHE A 1 28  ? 18.341  1.655   16.884  1.00 32.30  ? 7   PHE A C   1 
ATOM   35   O  O   . PHE A 1 28  ? 18.196  2.840   17.205  1.00 30.89  ? 7   PHE A O   1 
ATOM   36   C  CB  . PHE A 1 28  ? 19.352  1.665   14.593  1.00 28.15  ? 7   PHE A CB  1 
ATOM   37   C  CG  . PHE A 1 28  ? 20.651  1.002   14.975  1.00 28.72  ? 7   PHE A CG  1 
ATOM   38   C  CD1 . PHE A 1 28  ? 21.486  1.568   15.926  1.00 27.97  ? 7   PHE A CD1 1 
ATOM   39   C  CD2 . PHE A 1 28  ? 21.040  -0.182  14.373  1.00 25.45  ? 7   PHE A CD2 1 
ATOM   40   C  CE1 . PHE A 1 28  ? 22.680  0.958   16.274  1.00 28.15  ? 7   PHE A CE1 1 
ATOM   41   C  CE2 . PHE A 1 28  ? 22.229  -0.792  14.715  1.00 25.01  ? 7   PHE A CE2 1 
ATOM   42   C  CZ  . PHE A 1 28  ? 23.051  -0.221  15.668  1.00 26.89  ? 7   PHE A CZ  1 
ATOM   43   N  N   . SER A 1 29  ? 18.664  0.696   17.747  1.00 23.92  ? 8   SER A N   1 
ATOM   44   C  CA  . SER A 1 29  ? 18.946  0.977   19.147  1.00 25.51  ? 8   SER A CA  1 
ATOM   45   C  C   . SER A 1 29  ? 20.168  0.179   19.569  1.00 26.09  ? 8   SER A C   1 
ATOM   46   O  O   . SER A 1 29  ? 20.243  -1.025  19.309  1.00 27.52  ? 8   SER A O   1 
ATOM   47   C  CB  . SER A 1 29  ? 17.748  0.628   20.035  1.00 31.50  ? 8   SER A CB  1 
ATOM   48   O  OG  . SER A 1 29  ? 17.938  1.121   21.344  1.00 50.49  ? 8   SER A OG  1 
ATOM   49   N  N   . GLY A 1 30  ? 21.119  0.848   20.211  1.00 26.51  ? 9   GLY A N   1 
ATOM   50   C  CA  . GLY A 1 30  ? 22.295  0.192   20.758  1.00 30.64  ? 9   GLY A CA  1 
ATOM   51   C  C   . GLY A 1 30  ? 22.110  -0.107  22.236  1.00 35.03  ? 9   GLY A C   1 
ATOM   52   O  O   . GLY A 1 30  ? 21.623  0.731   22.995  1.00 38.54  ? 9   GLY A O   1 
ATOM   53   N  N   . ALA A 1 31  ? 22.509  -1.313  22.634  1.00 28.11  ? 10  ALA A N   1 
ATOM   54   C  CA  . ALA A 1 31  ? 22.415  -1.764  24.017  1.00 31.16  ? 10  ALA A CA  1 
ATOM   55   C  C   . ALA A 1 31  ? 23.811  -2.099  24.515  1.00 30.52  ? 10  ALA A C   1 
ATOM   56   O  O   . ALA A 1 31  ? 24.499  -2.937  23.923  1.00 29.36  ? 10  ALA A O   1 
ATOM   57   C  CB  . ALA A 1 31  ? 21.498  -2.983  24.139  1.00 34.38  ? 10  ALA A CB  1 
ATOM   58   N  N   . GLN A 1 32  ? 24.224  -1.451  25.593  1.00 37.97  ? 11  GLN A N   1 
ATOM   59   C  CA  . GLN A 1 32  ? 25.518  -1.755  26.179  1.00 33.97  ? 11  GLN A CA  1 
ATOM   60   C  C   . GLN A 1 32  ? 25.503  -3.183  26.723  1.00 39.33  ? 11  GLN A C   1 
ATOM   61   O  O   . GLN A 1 32  ? 24.485  -3.629  27.260  1.00 40.63  ? 11  GLN A O   1 
ATOM   62   C  CB  . GLN A 1 32  ? 25.836  -0.765  27.300  1.00 40.57  ? 11  GLN A CB  1 
ATOM   63   C  CG  . GLN A 1 32  ? 27.321  -0.529  27.534  1.00 48.54  ? 11  GLN A CG  1 
ATOM   64   C  CD  . GLN A 1 32  ? 27.950  0.357   26.469  1.00 43.68  ? 11  GLN A CD  1 
ATOM   65   O  OE1 . GLN A 1 32  ? 27.253  1.068   25.745  1.00 45.08  ? 11  GLN A OE1 1 
ATOM   66   N  NE2 . GLN A 1 32  ? 29.275  0.322   26.378  1.00 41.58  ? 11  GLN A NE2 1 
ATOM   67   N  N   . PRO A 1 33  ? 26.603  -3.936  26.580  1.00 34.68  ? 12  PRO A N   1 
ATOM   68   C  CA  . PRO A 1 33  ? 26.646  -5.276  27.209  1.00 37.01  ? 12  PRO A CA  1 
ATOM   69   C  C   . PRO A 1 33  ? 26.934  -5.198  28.703  1.00 46.45  ? 12  PRO A C   1 
ATOM   70   O  O   . PRO A 1 33  ? 28.002  -5.576  29.201  1.00 49.01  ? 12  PRO A O   1 
ATOM   71   C  CB  . PRO A 1 33  ? 27.765  -5.972  26.425  1.00 35.76  ? 12  PRO A CB  1 
ATOM   72   C  CG  . PRO A 1 33  ? 28.667  -4.876  26.020  1.00 38.65  ? 12  PRO A CG  1 
ATOM   73   C  CD  . PRO A 1 33  ? 27.774  -3.699  25.718  1.00 37.55  ? 12  PRO A CD  1 
ATOM   74   N  N   . SER A 1 34  ? 25.955  -4.691  29.446  1.00 46.64  ? 13  SER A N   1 
ATOM   75   C  CA  . SER A 1 34  ? 26.054  -4.530  30.891  1.00 66.13  ? 13  SER A CA  1 
ATOM   76   C  C   . SER A 1 34  ? 25.148  -5.476  31.662  1.00 79.13  ? 13  SER A C   1 
ATOM   77   O  O   . SER A 1 34  ? 25.539  -5.969  32.722  1.00 71.22  ? 13  SER A O   1 
ATOM   78   C  CB  . SER A 1 34  ? 25.719  -3.086  31.280  1.00 70.62  ? 13  SER A CB  1 
ATOM   79   O  OG  . SER A 1 34  ? 24.375  -2.773  30.958  1.00 78.69  ? 13  SER A OG  1 
ATOM   80   N  N   . GLY A 1 35  ? 23.946  -5.746  31.156  1.00 83.91  ? 14  GLY A N   1 
ATOM   81   C  CA  . GLY A 1 35  ? 23.038  -6.643  31.841  1.00 83.01  ? 14  GLY A CA  1 
ATOM   82   C  C   . GLY A 1 35  ? 22.407  -6.075  33.089  1.00 94.07  ? 14  GLY A C   1 
ATOM   83   O  O   . GLY A 1 35  ? 21.965  -6.841  33.949  1.00 95.82  ? 14  GLY A O   1 
ATOM   84   N  N   . GLU A 1 36  ? 22.342  -4.751  33.213  1.00 104.61 ? 15  GLU A N   1 
ATOM   85   C  CA  . GLU A 1 36  ? 21.817  -4.089  34.403  1.00 105.77 ? 15  GLU A CA  1 
ATOM   86   C  C   . GLU A 1 36  ? 20.748  -3.072  34.025  1.00 100.10 ? 15  GLU A C   1 
ATOM   87   O  O   . GLU A 1 36  ? 20.758  -1.924  34.475  1.00 107.14 ? 15  GLU A O   1 
ATOM   88   C  CB  . GLU A 1 36  ? 22.933  -3.408  35.195  1.00 113.33 ? 15  GLU A CB  1 
ATOM   89   C  CG  . GLU A 1 36  ? 23.697  -2.341  34.414  1.00 117.11 ? 15  GLU A CG  1 
ATOM   90   C  CD  . GLU A 1 36  ? 24.296  -1.265  35.307  1.00 131.66 ? 15  GLU A CD  1 
ATOM   91   O  OE1 . GLU A 1 36  ? 23.927  -1.196  36.500  1.00 130.96 ? 15  GLU A OE1 1 
ATOM   92   O  OE2 . GLU A 1 36  ? 25.135  -0.483  34.813  1.00 129.90 ? 15  GLU A OE2 1 
ATOM   93   N  N   . LEU A 1 37  ? 19.807  -3.482  33.180  1.00 82.51  ? 16  LEU A N   1 
ATOM   94   C  CA  . LEU A 1 37  ? 18.668  -2.625  32.882  1.00 72.50  ? 16  LEU A CA  1 
ATOM   95   C  C   . LEU A 1 37  ? 17.948  -2.258  34.173  1.00 69.52  ? 16  LEU A C   1 
ATOM   96   O  O   . LEU A 1 37  ? 17.759  -3.098  35.057  1.00 66.94  ? 16  LEU A O   1 
ATOM   97   C  CB  . LEU A 1 37  ? 17.703  -3.330  31.929  1.00 63.37  ? 16  LEU A CB  1 
ATOM   98   C  CG  . LEU A 1 37  ? 17.723  -2.919  30.456  1.00 74.90  ? 16  LEU A CG  1 
ATOM   99   C  CD1 . LEU A 1 37  ? 16.826  -3.838  29.644  1.00 73.85  ? 16  LEU A CD1 1 
ATOM   100  C  CD2 . LEU A 1 37  ? 17.279  -1.479  30.293  1.00 71.13  ? 16  LEU A CD2 1 
ATOM   101  N  N   . THR A 1 38  ? 17.562  -0.994  34.291  1.00 65.40  ? 17  THR A N   1 
ATOM   102  C  CA  . THR A 1 38  ? 16.773  -0.530  35.421  1.00 65.52  ? 17  THR A CA  1 
ATOM   103  C  C   . THR A 1 38  ? 15.301  -0.476  35.029  1.00 59.07  ? 17  THR A C   1 
ATOM   104  O  O   . THR A 1 38  ? 14.951  -0.360  33.853  1.00 56.02  ? 17  THR A O   1 
ATOM   105  C  CB  . THR A 1 38  ? 17.239  0.849   35.896  1.00 74.23  ? 17  THR A CB  1 
ATOM   106  O  OG1 . THR A 1 38  ? 16.779  1.856   34.985  1.00 70.65  ? 17  THR A OG1 1 
ATOM   107  C  CG2 . THR A 1 38  ? 18.760  0.899   35.983  1.00 74.22  ? 17  THR A CG2 1 
ATOM   108  N  N   . ILE A 1 39  ? 14.433  -0.568  36.040  1.00 59.20  ? 18  ILE A N   1 
ATOM   109  C  CA  . ILE A 1 39  ? 12.999  -0.544  35.770  1.00 59.52  ? 18  ILE A CA  1 
ATOM   110  C  C   . ILE A 1 39  ? 12.607  0.753   35.078  1.00 58.52  ? 18  ILE A C   1 
ATOM   111  O  O   . ILE A 1 39  ? 11.620  0.795   34.335  1.00 61.45  ? 18  ILE A O   1 
ATOM   112  C  CB  . ILE A 1 39  ? 12.195  -0.768  37.067  1.00 56.35  ? 18  ILE A CB  1 
ATOM   113  C  CG1 . ILE A 1 39  ? 12.583  0.237   38.156  1.00 61.00  ? 18  ILE A CG1 1 
ATOM   114  C  CG2 . ILE A 1 39  ? 12.415  -2.179  37.579  1.00 63.03  ? 18  ILE A CG2 1 
ATOM   115  C  CD1 . ILE A 1 39  ? 11.834  1.538   38.095  1.00 64.32  ? 18  ILE A CD1 1 
ATOM   116  N  N   . GLY A 1 40  ? 13.362  1.829   35.303  1.00 60.65  ? 19  GLY A N   1 
ATOM   117  C  CA  . GLY A 1 40  ? 13.092  3.064   34.586  1.00 59.75  ? 19  GLY A CA  1 
ATOM   118  C  C   . GLY A 1 40  ? 13.352  2.929   33.098  1.00 65.89  ? 19  GLY A C   1 
ATOM   119  O  O   . GLY A 1 40  ? 12.578  3.425   32.275  1.00 64.63  ? 19  GLY A O   1 
ATOM   120  N  N   . ASN A 1 41  ? 14.447  2.258   32.734  1.00 62.20  ? 20  ASN A N   1 
ATOM   121  C  CA  . ASN A 1 41  ? 14.735  2.023   31.324  1.00 63.74  ? 20  ASN A CA  1 
ATOM   122  C  C   . ASN A 1 41  ? 13.664  1.153   30.681  1.00 63.27  ? 20  ASN A C   1 
ATOM   123  O  O   . ASN A 1 41  ? 13.226  1.422   29.557  1.00 62.07  ? 20  ASN A O   1 
ATOM   124  C  CB  . ASN A 1 41  ? 16.107  1.366   31.173  1.00 67.89  ? 20  ASN A CB  1 
ATOM   125  C  CG  . ASN A 1 41  ? 17.245  2.326   31.430  1.00 69.14  ? 20  ASN A CG  1 
ATOM   126  O  OD1 . ASN A 1 41  ? 17.190  3.491   31.035  1.00 76.10  ? 20  ASN A OD1 1 
ATOM   127  N  ND2 . ASN A 1 41  ? 18.287  1.843   32.097  1.00 70.18  ? 20  ASN A ND2 1 
ATOM   128  N  N   . TYR A 1 42  ? 13.241  0.094   31.374  1.00 63.06  ? 21  TYR A N   1 
ATOM   129  C  CA  . TYR A 1 42  ? 12.256  -0.820  30.810  1.00 62.42  ? 21  TYR A CA  1 
ATOM   130  C  C   . TYR A 1 42  ? 10.920  -0.122  30.589  1.00 63.46  ? 21  TYR A C   1 
ATOM   131  O  O   . TYR A 1 42  ? 10.466  0.035   29.451  1.00 62.98  ? 21  TYR A O   1 
ATOM   132  C  CB  . TYR A 1 42  ? 12.085  -2.032  31.729  1.00 61.61  ? 21  TYR A CB  1 
ATOM   133  C  CG  . TYR A 1 42  ? 11.019  -3.003  31.268  1.00 61.27  ? 21  TYR A CG  1 
ATOM   134  C  CD1 . TYR A 1 42  ? 11.154  -3.695  30.071  1.00 63.84  ? 21  TYR A CD1 1 
ATOM   135  C  CD2 . TYR A 1 42  ? 9.882   -3.234  32.032  1.00 64.25  ? 21  TYR A CD2 1 
ATOM   136  C  CE1 . TYR A 1 42  ? 10.183  -4.588  29.645  1.00 62.38  ? 21  TYR A CE1 1 
ATOM   137  C  CE2 . TYR A 1 42  ? 8.905   -4.124  31.615  1.00 61.69  ? 21  TYR A CE2 1 
ATOM   138  C  CZ  . TYR A 1 42  ? 9.060   -4.798  30.422  1.00 61.89  ? 21  TYR A CZ  1 
ATOM   139  O  OH  . TYR A 1 42  ? 8.091   -5.684  30.006  1.00 66.71  ? 21  TYR A OH  1 
ATOM   140  N  N   . MET A 1 43  ? 10.284  0.327   31.672  1.00 66.67  ? 22  MET A N   1 
ATOM   141  C  CA  . MET A 1 43  ? 8.917   0.826   31.570  1.00 66.24  ? 22  MET A CA  1 
ATOM   142  C  C   . MET A 1 43  ? 8.828   2.018   30.629  1.00 61.38  ? 22  MET A C   1 
ATOM   143  O  O   . MET A 1 43  ? 7.826   2.188   29.923  1.00 68.48  ? 22  MET A O   1 
ATOM   144  C  CB  . MET A 1 43  ? 8.396   1.203   32.955  1.00 63.28  ? 22  MET A CB  1 
ATOM   145  C  CG  . MET A 1 43  ? 8.537   0.094   33.975  1.00 61.18  ? 22  MET A CG  1 
ATOM   146  S  SD  . MET A 1 43  ? 7.083   -0.046  35.019  1.00 65.87  ? 22  MET A SD  1 
ATOM   147  C  CE  . MET A 1 43  ? 7.580   0.941   36.428  1.00 65.94  ? 22  MET A CE  1 
ATOM   148  N  N   . GLY A 1 44  ? 9.856   2.857   30.608  1.00 63.82  ? 23  GLY A N   1 
ATOM   149  C  CA  . GLY A 1 44  ? 9.856   4.003   29.725  1.00 67.40  ? 23  GLY A CA  1 
ATOM   150  C  C   . GLY A 1 44  ? 10.134  3.643   28.280  1.00 81.13  ? 23  GLY A C   1 
ATOM   151  O  O   . GLY A 1 44  ? 9.292   3.863   27.405  1.00 88.88  ? 23  GLY A O   1 
ATOM   152  N  N   . ALA A 1 45  ? 11.315  3.077   28.022  1.00 88.33  ? 24  ALA A N   1 
ATOM   153  C  CA  . ALA A 1 45  ? 11.806  2.869   26.664  1.00 84.58  ? 24  ALA A CA  1 
ATOM   154  C  C   . ALA A 1 45  ? 11.522  1.473   26.119  1.00 78.25  ? 24  ALA A C   1 
ATOM   155  O  O   . ALA A 1 45  ? 10.797  1.325   25.130  1.00 79.30  ? 24  ALA A O   1 
ATOM   156  C  CB  . ALA A 1 45  ? 13.317  3.147   26.628  1.00 84.81  ? 24  ALA A CB  1 
ATOM   157  N  N   . LEU A 1 46  ? 12.073  0.437   26.754  1.00 68.63  ? 25  LEU A N   1 
ATOM   158  C  CA  . LEU A 1 46  ? 12.144  -0.869  26.102  1.00 63.82  ? 25  LEU A CA  1 
ATOM   159  C  C   . LEU A 1 46  ? 10.771  -1.521  25.985  1.00 66.38  ? 25  LEU A C   1 
ATOM   160  O  O   . LEU A 1 46  ? 10.437  -2.085  24.937  1.00 69.57  ? 25  LEU A O   1 
ATOM   161  C  CB  . LEU A 1 46  ? 13.109  -1.777  26.863  1.00 59.63  ? 25  LEU A CB  1 
ATOM   162  C  CG  . LEU A 1 46  ? 13.325  -3.179  26.289  1.00 58.67  ? 25  LEU A CG  1 
ATOM   163  C  CD1 . LEU A 1 46  ? 13.771  -3.128  24.835  1.00 51.67  ? 25  LEU A CD1 1 
ATOM   164  C  CD2 . LEU A 1 46  ? 14.345  -3.934  27.130  1.00 57.93  ? 25  LEU A CD2 1 
ATOM   165  N  N   . ARG A 1 47  ? 9.966   -1.460  27.048  1.00 58.54  ? 26  ARG A N   1 
ATOM   166  C  CA  . ARG A 1 47  ? 8.644   -2.079  27.012  1.00 65.97  ? 26  ARG A CA  1 
ATOM   167  C  C   . ARG A 1 47  ? 7.776   -1.463  25.924  1.00 65.57  ? 26  ARG A C   1 
ATOM   168  O  O   . ARG A 1 47  ? 6.973   -2.157  25.290  1.00 63.22  ? 26  ARG A O   1 
ATOM   169  C  CB  . ARG A 1 47  ? 7.965   -1.942  28.375  1.00 67.51  ? 26  ARG A CB  1 
ATOM   170  C  CG  . ARG A 1 47  ? 6.589   -2.583  28.447  1.00 70.29  ? 26  ARG A CG  1 
ATOM   171  C  CD  . ARG A 1 47  ? 5.989   -2.457  29.837  1.00 81.64  ? 26  ARG A CD  1 
ATOM   172  N  NE  . ARG A 1 47  ? 5.671   -1.076  30.177  1.00 82.23  ? 26  ARG A NE  1 
ATOM   173  C  CZ  . ARG A 1 47  ? 5.141   -0.692  31.330  1.00 78.35  ? 26  ARG A CZ  1 
ATOM   174  N  NH1 . ARG A 1 47  ? 4.861   -1.563  32.286  1.00 71.14  ? 26  ARG A NH1 1 
ATOM   175  N  NH2 . ARG A 1 47  ? 4.886   0.598   31.529  1.00 83.63  ? 26  ARG A NH2 1 
ATOM   176  N  N   . GLN A 1 48  ? 7.914   -0.154  25.702  1.00 78.55  ? 27  GLN A N   1 
ATOM   177  C  CA  . GLN A 1 48  ? 7.135   0.505   24.661  1.00 72.87  ? 27  GLN A CA  1 
ATOM   178  C  C   . GLN A 1 48  ? 7.475   -0.053  23.285  1.00 68.82  ? 27  GLN A C   1 
ATOM   179  O  O   . GLN A 1 48  ? 6.581   -0.303  22.467  1.00 66.57  ? 27  GLN A O   1 
ATOM   180  C  CB  . GLN A 1 48  ? 7.389   2.013   24.704  1.00 73.24  ? 27  GLN A CB  1 
ATOM   181  C  CG  . GLN A 1 48  ? 6.461   2.828   23.823  1.00 77.37  ? 27  GLN A CG  1 
ATOM   182  C  CD  . GLN A 1 48  ? 5.024   2.765   24.290  1.00 82.51  ? 27  GLN A CD  1 
ATOM   183  O  OE1 . GLN A 1 48  ? 4.752   2.701   25.489  1.00 83.90  ? 27  GLN A OE1 1 
ATOM   184  N  NE2 . GLN A 1 48  ? 4.094   2.771   23.344  1.00 85.41  ? 27  GLN A NE2 1 
ATOM   185  N  N   . TRP A 1 49  ? 8.765   -0.270  23.017  1.00 68.41  ? 28  TRP A N   1 
ATOM   186  C  CA  A TRP A 1 49  ? 9.197   -0.724  21.700  0.50 67.75  ? 28  TRP A CA  1 
ATOM   187  C  CA  B TRP A 1 49  ? 9.164   -0.713  21.687  0.50 67.75  ? 28  TRP A CA  1 
ATOM   188  C  C   . TRP A 1 49  ? 8.792   -2.169  21.437  1.00 65.17  ? 28  TRP A C   1 
ATOM   189  O  O   . TRP A 1 49  ? 8.583   -2.557  20.282  1.00 62.00  ? 28  TRP A O   1 
ATOM   190  C  CB  A TRP A 1 49  ? 10.716  -0.583  21.571  0.50 66.71  ? 28  TRP A CB  1 
ATOM   191  C  CB  B TRP A 1 49  ? 10.663  -0.494  21.492  0.50 66.72  ? 28  TRP A CB  1 
ATOM   192  C  CG  A TRP A 1 49  ? 11.272  0.725   22.064  0.50 65.18  ? 28  TRP A CG  1 
ATOM   193  C  CG  B TRP A 1 49  ? 11.001  0.938   21.203  0.50 65.16  ? 28  TRP A CG  1 
ATOM   194  C  CD1 A TRP A 1 49  ? 10.598  1.903   22.217  0.50 64.43  ? 28  TRP A CD1 1 
ATOM   195  C  CD1 B TRP A 1 49  ? 11.572  1.837   22.056  0.50 64.60  ? 28  TRP A CD1 1 
ATOM   196  C  CD2 A TRP A 1 49  ? 12.622  0.981   22.471  0.50 65.34  ? 28  TRP A CD2 1 
ATOM   197  C  CD2 B TRP A 1 49  ? 10.771  1.640   19.975  0.50 61.32  ? 28  TRP A CD2 1 
ATOM   198  N  NE1 A TRP A 1 49  ? 11.445  2.874   22.693  0.50 63.71  ? 28  TRP A NE1 1 
ATOM   199  N  NE1 B TRP A 1 49  ? 11.718  3.054   21.432  0.50 63.63  ? 28  TRP A NE1 1 
ATOM   200  C  CE2 A TRP A 1 49  ? 12.693  2.334   22.856  0.50 64.26  ? 28  TRP A CE2 1 
ATOM   201  C  CE2 B TRP A 1 49  ? 11.233  2.958   20.154  0.50 61.48  ? 28  TRP A CE2 1 
ATOM   202  C  CE3 A TRP A 1 49  ? 13.777  0.197   22.544  0.50 65.21  ? 28  TRP A CE3 1 
ATOM   203  C  CE3 B TRP A 1 49  ? 10.220  1.279   18.742  0.50 59.96  ? 28  TRP A CE3 1 
ATOM   204  C  CZ2 A TRP A 1 49  ? 13.874  2.920   23.305  0.50 64.15  ? 28  TRP A CZ2 1 
ATOM   205  C  CZ2 B TRP A 1 49  ? 11.161  3.916   19.146  0.50 63.28  ? 28  TRP A CZ2 1 
ATOM   206  C  CZ3 A TRP A 1 49  ? 14.947  0.780   22.993  0.50 67.24  ? 28  TRP A CZ3 1 
ATOM   207  C  CZ3 B TRP A 1 49  ? 10.151  2.231   17.743  0.50 59.99  ? 28  TRP A CZ3 1 
ATOM   208  C  CH2 A TRP A 1 49  ? 14.987  2.127   23.369  0.50 72.20  ? 28  TRP A CH2 1 
ATOM   209  C  CH2 B TRP A 1 49  ? 10.619  3.534   17.951  0.50 62.60  ? 28  TRP A CH2 1 
ATOM   210  N  N   . VAL A 1 50  ? 8.686   -2.981  22.491  1.00 61.58  ? 29  VAL A N   1 
ATOM   211  C  CA  . VAL A 1 50  ? 8.346   -4.389  22.309  1.00 57.72  ? 29  VAL A CA  1 
ATOM   212  C  C   . VAL A 1 50  ? 7.003   -4.535  21.608  1.00 60.84  ? 29  VAL A C   1 
ATOM   213  O  O   . VAL A 1 50  ? 6.801   -5.471  20.825  1.00 56.53  ? 29  VAL A O   1 
ATOM   214  C  CB  . VAL A 1 50  ? 8.352   -5.117  23.668  1.00 54.89  ? 29  VAL A CB  1 
ATOM   215  C  CG1 . VAL A 1 50  ? 7.600   -6.436  23.575  1.00 53.26  ? 29  VAL A CG1 1 
ATOM   216  C  CG2 . VAL A 1 50  ? 9.781   -5.351  24.136  1.00 54.22  ? 29  VAL A CG2 1 
ATOM   217  N  N   . ASN A 1 51  ? 6.067   -3.624  21.874  1.00 59.95  ? 30  ASN A N   1 
ATOM   218  C  CA  . ASN A 1 51  ? 4.733   -3.712  21.296  1.00 61.19  ? 30  ASN A CA  1 
ATOM   219  C  C   . ASN A 1 51  ? 4.661   -3.174  19.873  1.00 52.47  ? 30  ASN A C   1 
ATOM   220  O  O   . ASN A 1 51  ? 3.624   -3.337  19.221  1.00 58.73  ? 30  ASN A O   1 
ATOM   221  C  CB  . ASN A 1 51  ? 3.736   -2.955  22.177  1.00 64.52  ? 30  ASN A CB  1 
ATOM   222  C  CG  . ASN A 1 51  ? 3.911   -3.261  23.653  1.00 66.04  ? 30  ASN A CG  1 
ATOM   223  O  OD1 . ASN A 1 51  ? 4.018   -2.354  24.478  1.00 76.14  ? 30  ASN A OD1 1 
ATOM   224  N  ND2 . ASN A 1 51  ? 3.947   -4.545  23.992  1.00 60.30  ? 30  ASN A ND2 1 
ATOM   225  N  N   . MET A 1 52  ? 5.725   -2.544  19.375  1.00 53.87  ? 31  MET A N   1 
ATOM   226  C  CA  . MET A 1 52  ? 5.743   -1.964  18.038  1.00 52.35  ? 31  MET A CA  1 
ATOM   227  C  C   . MET A 1 52  ? 6.626   -2.754  17.077  1.00 53.77  ? 31  MET A C   1 
ATOM   228  O  O   . MET A 1 52  ? 7.036   -2.224  16.039  1.00 57.34  ? 31  MET A O   1 
ATOM   229  C  CB  . MET A 1 52  ? 6.203   -0.507  18.112  1.00 57.53  ? 31  MET A CB  1 
ATOM   230  C  CG  . MET A 1 52  ? 5.239   0.395   18.872  1.00 58.99  ? 31  MET A CG  1 
ATOM   231  S  SD  . MET A 1 52  ? 6.061   1.702   19.803  1.00 71.35  ? 31  MET A SD  1 
ATOM   232  C  CE  . MET A 1 52  ? 5.670   3.135   18.803  1.00 71.94  ? 31  MET A CE  1 
ATOM   233  N  N   . GLN A 1 53  ? 6.923   -4.015  17.399  1.00 49.35  ? 32  GLN A N   1 
ATOM   234  C  CA  . GLN A 1 53  ? 7.766   -4.826  16.530  1.00 47.84  ? 32  GLN A CA  1 
ATOM   235  C  C   . GLN A 1 53  ? 7.072   -5.209  15.230  1.00 44.50  ? 32  GLN A C   1 
ATOM   236  O  O   . GLN A 1 53  ? 7.752   -5.577  14.267  1.00 46.14  ? 32  GLN A O   1 
ATOM   237  C  CB  . GLN A 1 53  ? 8.213   -6.088  17.262  1.00 45.31  ? 32  GLN A CB  1 
ATOM   238  C  CG  . GLN A 1 53  ? 9.307   -5.845  18.278  1.00 49.45  ? 32  GLN A CG  1 
ATOM   239  C  CD  . GLN A 1 53  ? 9.750   -7.121  18.955  1.00 49.94  ? 32  GLN A CD  1 
ATOM   240  O  OE1 . GLN A 1 53  ? 10.709  -7.760  18.528  1.00 36.86  ? 32  GLN A OE1 1 
ATOM   241  N  NE2 . GLN A 1 53  ? 9.048   -7.503  20.014  1.00 46.01  ? 32  GLN A NE2 1 
ATOM   242  N  N   . ASP A 1 54  ? 5.745   -5.138  15.179  1.00 50.72  ? 33  ASP A N   1 
ATOM   243  C  CA  . ASP A 1 54  ? 5.014   -5.454  13.960  1.00 49.51  ? 33  ASP A CA  1 
ATOM   244  C  C   . ASP A 1 54  ? 4.905   -4.271  13.007  1.00 51.73  ? 33  ASP A C   1 
ATOM   245  O  O   . ASP A 1 54  ? 4.675   -4.478  11.810  1.00 50.37  ? 33  ASP A O   1 
ATOM   246  C  CB  . ASP A 1 54  ? 3.611   -5.956  14.313  1.00 53.09  ? 33  ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 54  ? 3.639   -7.285  15.045  1.00 60.29  ? 33  ASP A CG  1 
ATOM   248  O  OD1 . ASP A 1 54  ? 4.101   -8.280  14.449  1.00 60.36  ? 33  ASP A OD1 1 
ATOM   249  O  OD2 . ASP A 1 54  ? 3.215   -7.331  16.221  1.00 65.43  ? 33  ASP A OD2 1 
ATOM   250  N  N   . ASP A 1 55  ? 5.073   -3.046  13.504  1.00 48.13  ? 34  ASP A N   1 
ATOM   251  C  CA  . ASP A 1 55  ? 4.953   -1.847  12.687  1.00 53.79  ? 34  ASP A CA  1 
ATOM   252  C  C   . ASP A 1 55  ? 6.299   -1.252  12.296  1.00 52.55  ? 34  ASP A C   1 
ATOM   253  O  O   . ASP A 1 55  ? 6.338   -0.354  11.448  1.00 54.36  ? 34  ASP A O   1 
ATOM   254  C  CB  . ASP A 1 55  ? 4.129   -0.787  13.431  1.00 58.83  ? 34  ASP A CB  1 
ATOM   255  C  CG  . ASP A 1 55  ? 2.706   -1.238  13.700  1.00 64.93  ? 34  ASP A CG  1 
ATOM   256  O  OD1 . ASP A 1 55  ? 2.146   -1.974  12.860  1.00 58.77  ? 34  ASP A OD1 1 
ATOM   257  O  OD2 . ASP A 1 55  ? 2.150   -0.856  14.751  1.00 68.83  ? 34  ASP A OD2 1 
ATOM   258  N  N   . TYR A 1 56  ? 7.393   -1.725  12.887  1.00 48.63  ? 35  TYR A N   1 
ATOM   259  C  CA  . TYR A 1 56  ? 8.721   -1.219  12.585  1.00 45.98  ? 35  TYR A CA  1 
ATOM   260  C  C   . TYR A 1 56  ? 9.676   -2.389  12.417  1.00 43.87  ? 35  TYR A C   1 
ATOM   261  O  O   . TYR A 1 56  ? 9.472   -3.465  12.986  1.00 46.77  ? 35  TYR A O   1 
ATOM   262  C  CB  . TYR A 1 56  ? 9.248   -0.292  13.693  1.00 47.55  ? 35  TYR A CB  1 
ATOM   263  C  CG  . TYR A 1 56  ? 8.425   0.956   13.905  1.00 51.68  ? 35  TYR A CG  1 
ATOM   264  C  CD1 . TYR A 1 56  ? 7.317   0.944   14.739  1.00 51.55  ? 35  TYR A CD1 1 
ATOM   265  C  CD2 . TYR A 1 56  ? 8.759   2.146   13.275  1.00 51.43  ? 35  TYR A CD2 1 
ATOM   266  C  CE1 . TYR A 1 56  ? 6.560   2.080   14.937  1.00 56.54  ? 35  TYR A CE1 1 
ATOM   267  C  CE2 . TYR A 1 56  ? 8.007   3.289   13.465  1.00 59.95  ? 35  TYR A CE2 1 
ATOM   268  C  CZ  . TYR A 1 56  ? 6.908   3.249   14.297  1.00 62.56  ? 35  TYR A CZ  1 
ATOM   269  O  OH  . TYR A 1 56  ? 6.151   4.380   14.497  1.00 73.53  ? 35  TYR A OH  1 
ATOM   270  N  N   . HIS A 1 57  ? 10.719  -2.167  11.621  1.00 40.74  ? 36  HIS A N   1 
ATOM   271  C  CA  . HIS A 1 57  ? 11.874  -3.061  11.578  1.00 36.88  ? 36  HIS A CA  1 
ATOM   272  C  C   . HIS A 1 57  ? 12.824  -2.596  12.669  1.00 33.08  ? 36  HIS A C   1 
ATOM   273  O  O   . HIS A 1 57  ? 13.621  -1.681  12.473  1.00 32.34  ? 36  HIS A O   1 
ATOM   274  C  CB  . HIS A 1 57  ? 12.544  -3.035  10.211  1.00 40.32  ? 36  HIS A CB  1 
ATOM   275  C  CG  . HIS A 1 57  ? 11.862  -3.890  9.190   1.00 49.22  ? 36  HIS A CG  1 
ATOM   276  N  ND1 . HIS A 1 57  ? 11.192  -3.365  8.106   1.00 52.90  ? 36  HIS A ND1 1 
ATOM   277  C  CD2 . HIS A 1 57  ? 11.741  -5.235  9.093   1.00 53.80  ? 36  HIS A CD2 1 
ATOM   278  C  CE1 . HIS A 1 57  ? 10.690  -4.350  7.384   1.00 48.48  ? 36  HIS A CE1 1 
ATOM   279  N  NE2 . HIS A 1 57  ? 11.008  -5.495  7.961   1.00 57.59  ? 36  HIS A NE2 1 
ATOM   280  N  N   . CYS A 1 58  ? 12.724  -3.221  13.840  1.00 30.17  ? 37  CYS A N   1 
ATOM   281  C  CA  . CYS A 1 58  ? 13.570  -2.884  14.974  1.00 25.05  ? 37  CYS A CA  1 
ATOM   282  C  C   . CYS A 1 58  ? 14.878  -3.658  14.908  1.00 32.12  ? 37  CYS A C   1 
ATOM   283  O  O   . CYS A 1 58  ? 14.891  -4.864  14.644  1.00 30.05  ? 37  CYS A O   1 
ATOM   284  C  CB  . CYS A 1 58  ? 12.853  -3.191  16.287  1.00 35.99  ? 37  CYS A CB  1 
ATOM   285  S  SG  . CYS A 1 58  ? 11.344  -2.237  16.547  1.00 40.79  ? 37  CYS A SG  1 
ATOM   286  N  N   . ILE A 1 59  ? 15.976  -2.950  15.163  1.00 27.05  ? 38  ILE A N   1 
ATOM   287  C  CA  . ILE A 1 59  ? 17.321  -3.510  15.154  1.00 27.08  ? 38  ILE A CA  1 
ATOM   288  C  C   . ILE A 1 59  ? 17.949  -3.205  16.502  1.00 26.12  ? 38  ILE A C   1 
ATOM   289  O  O   . ILE A 1 59  ? 18.134  -2.034  16.853  1.00 30.45  ? 38  ILE A O   1 
ATOM   290  C  CB  . ILE A 1 59  ? 18.178  -2.928  14.020  1.00 25.09  ? 38  ILE A CB  1 
ATOM   291  C  CG1 . ILE A 1 59  ? 17.572  -3.267  12.658  1.00 29.04  ? 38  ILE A CG1 1 
ATOM   292  C  CG2 . ILE A 1 59  ? 19.602  -3.447  14.122  1.00 28.02  ? 38  ILE A CG2 1 
ATOM   293  C  CD1 . ILE A 1 59  ? 18.081  -2.386  11.534  1.00 30.61  ? 38  ILE A CD1 1 
ATOM   294  N  N   . TYR A 1 60  ? 18.279  -4.249  17.252  1.00 26.28  ? 39  TYR A N   1 
ATOM   295  C  CA  . TYR A 1 60  ? 18.924  -4.123  18.551  1.00 27.52  ? 39  TYR A CA  1 
ATOM   296  C  C   . TYR A 1 60  ? 20.339  -4.671  18.437  1.00 26.60  ? 39  TYR A C   1 
ATOM   297  O  O   . TYR A 1 60  ? 20.529  -5.857  18.149  1.00 31.04  ? 39  TYR A O   1 
ATOM   298  C  CB  . TYR A 1 60  ? 18.127  -4.862  19.624  1.00 26.65  ? 39  TYR A CB  1 
ATOM   299  C  CG  . TYR A 1 60  ? 16.751  -4.270  19.861  1.00 28.99  ? 39  TYR A CG  1 
ATOM   300  C  CD1 . TYR A 1 60  ? 16.555  -3.272  20.804  1.00 31.43  ? 39  TYR A CD1 1 
ATOM   301  C  CD2 . TYR A 1 60  ? 15.653  -4.705  19.132  1.00 32.25  ? 39  TYR A CD2 1 
ATOM   302  C  CE1 . TYR A 1 60  ? 15.300  -2.725  21.020  1.00 34.33  ? 39  TYR A CE1 1 
ATOM   303  C  CE2 . TYR A 1 60  ? 14.397  -4.166  19.339  1.00 32.43  ? 39  TYR A CE2 1 
ATOM   304  C  CZ  . TYR A 1 60  ? 14.226  -3.176  20.284  1.00 37.18  ? 39  TYR A CZ  1 
ATOM   305  O  OH  . TYR A 1 60  ? 12.975  -2.640  20.490  1.00 51.84  ? 39  TYR A OH  1 
ATOM   306  N  N   . CYS A 1 61  ? 21.325  -3.807  18.656  1.00 30.16  ? 40  CYS A N   1 
ATOM   307  C  CA  . CYS A 1 61  ? 22.731  -4.147  18.490  1.00 24.61  ? 40  CYS A CA  1 
ATOM   308  C  C   . CYS A 1 61  ? 23.426  -4.058  19.840  1.00 25.65  ? 40  CYS A C   1 
ATOM   309  O  O   . CYS A 1 61  ? 23.498  -2.978  20.434  1.00 24.48  ? 40  CYS A O   1 
ATOM   310  C  CB  . CYS A 1 61  ? 23.393  -3.212  17.476  1.00 24.46  ? 40  CYS A CB  1 
ATOM   311  S  SG  . CYS A 1 61  ? 25.173  -3.400  17.338  1.00 27.57  ? 40  CYS A SG  1 
ATOM   312  N  N   . ILE A 1 62  ? 23.939  -5.189  20.318  1.00 22.28  ? 41  ILE A N   1 
ATOM   313  C  CA  . ILE A 1 62  ? 24.686  -5.227  21.572  1.00 24.36  ? 41  ILE A CA  1 
ATOM   314  C  C   . ILE A 1 62  ? 26.105  -4.761  21.263  1.00 26.40  ? 41  ILE A C   1 
ATOM   315  O  O   . ILE A 1 62  ? 26.876  -5.472  20.614  1.00 22.03  ? 41  ILE A O   1 
ATOM   316  C  CB  . ILE A 1 62  ? 24.670  -6.626  22.196  1.00 27.00  ? 41  ILE A CB  1 
ATOM   317  C  CG1 . ILE A 1 62  ? 23.222  -7.105  22.353  1.00 25.50  ? 41  ILE A CG1 1 
ATOM   318  C  CG2 . ILE A 1 62  ? 25.385  -6.618  23.541  1.00 29.58  ? 41  ILE A CG2 1 
ATOM   319  C  CD1 . ILE A 1 62  ? 23.082  -8.476  22.980  1.00 29.68  ? 41  ILE A CD1 1 
ATOM   320  N  N   . VAL A 1 63  ? 26.445  -3.554  21.708  1.00 22.08  ? 42  VAL A N   1 
ATOM   321  C  CA  . VAL A 1 63  ? 27.625  -2.846  21.182  1.00 26.30  ? 42  VAL A CA  1 
ATOM   322  C  C   . VAL A 1 63  ? 28.802  -3.225  22.072  1.00 25.32  ? 42  VAL A C   1 
ATOM   323  O  O   . VAL A 1 63  ? 29.271  -2.455  22.914  1.00 27.93  ? 42  VAL A O   1 
ATOM   324  C  CB  . VAL A 1 63  ? 27.402  -1.329  21.117  1.00 28.20  ? 42  VAL A CB  1 
ATOM   325  C  CG1 . VAL A 1 63  ? 26.460  -0.979  19.976  1.00 26.82  ? 42  VAL A CG1 1 
ATOM   326  C  CG2 . VAL A 1 63  ? 26.848  -0.801  22.440  1.00 23.30  ? 42  VAL A CG2 1 
ATOM   327  N  N   . ASP A 1 64  ? 29.355  -4.414  21.822  1.00 21.45  ? 43  ASP A N   1 
ATOM   328  C  CA  . ASP A 1 64  ? 30.531  -4.825  22.580  1.00 28.35  ? 43  ASP A CA  1 
ATOM   329  C  C   . ASP A 1 64  ? 31.805  -4.132  22.100  1.00 24.33  ? 43  ASP A C   1 
ATOM   330  O  O   . ASP A 1 64  ? 32.762  -4.023  22.874  1.00 21.34  ? 43  ASP A O   1 
ATOM   331  C  CB  . ASP A 1 64  ? 30.700  -6.351  22.543  1.00 25.42  ? 43  ASP A CB  1 
ATOM   332  C  CG  . ASP A 1 64  ? 30.802  -6.914  21.137  1.00 26.06  ? 43  ASP A CG  1 
ATOM   333  O  OD1 . ASP A 1 64  ? 30.547  -6.180  20.163  1.00 21.96  ? 43  ASP A OD1 1 
ATOM   334  O  OD2 . ASP A 1 64  ? 31.144  -8.111  21.008  1.00 24.93  ? 43  ASP A OD2 1 
ATOM   335  N  N   . GLN A 1 65  ? 31.835  -3.637  20.859  1.00 19.81  ? 44  GLN A N   1 
ATOM   336  C  CA  . GLN A 1 65  ? 33.003  -2.890  20.399  1.00 21.20  ? 44  GLN A CA  1 
ATOM   337  C  C   . GLN A 1 65  ? 33.062  -1.500  21.024  1.00 20.10  ? 44  GLN A C   1 
ATOM   338  O  O   . GLN A 1 65  ? 34.155  -0.959  21.232  1.00 17.00  ? 44  GLN A O   1 
ATOM   339  C  CB  . GLN A 1 65  ? 32.996  -2.796  18.874  1.00 22.53  ? 44  GLN A CB  1 
ATOM   340  C  CG  . GLN A 1 65  ? 33.186  -4.142  18.195  1.00 18.89  ? 44  GLN A CG  1 
ATOM   341  C  CD  . GLN A 1 65  ? 33.151  -4.050  16.684  1.00 22.22  ? 44  GLN A CD  1 
ATOM   342  O  OE1 . GLN A 1 65  ? 32.083  -4.024  16.073  1.00 24.01  ? 44  GLN A OE1 1 
ATOM   343  N  NE2 . GLN A 1 65  ? 34.323  -4.006  16.073  1.00 23.31  ? 44  GLN A NE2 1 
ATOM   344  N  N   . HIS A 1 66  ? 31.906  -0.908  21.327  1.00 19.68  ? 45  HIS A N   1 
ATOM   345  C  CA  . HIS A 1 66  ? 31.886  0.344   22.076  1.00 22.75  ? 45  HIS A CA  1 
ATOM   346  C  C   . HIS A 1 66  ? 32.296  0.133   23.527  1.00 18.88  ? 45  HIS A C   1 
ATOM   347  O  O   . HIS A 1 66  ? 32.952  0.993   24.124  1.00 24.42  ? 45  HIS A O   1 
ATOM   348  C  CB  . HIS A 1 66  ? 30.495  0.971   22.008  1.00 23.44  ? 45  HIS A CB  1 
ATOM   349  C  CG  . HIS A 1 66  ? 30.209  1.645   20.706  1.00 25.25  ? 45  HIS A CG  1 
ATOM   350  N  ND1 . HIS A 1 66  ? 30.913  2.748   20.277  1.00 23.25  ? 45  HIS A ND1 1 
ATOM   351  C  CD2 . HIS A 1 66  ? 29.308  1.370   19.735  1.00 24.95  ? 45  HIS A CD2 1 
ATOM   352  C  CE1 . HIS A 1 66  ? 30.456  3.126   19.098  1.00 27.25  ? 45  HIS A CE1 1 
ATOM   353  N  NE2 . HIS A 1 66  ? 29.482  2.306   18.745  1.00 25.45  ? 45  HIS A NE2 1 
ATOM   354  N  N   . ALA A 1 67  ? 31.914  -1.000  24.115  1.00 21.97  ? 46  ALA A N   1 
ATOM   355  C  CA  . ALA A 1 67  ? 32.178  -1.211  25.533  1.00 22.20  ? 46  ALA A CA  1 
ATOM   356  C  C   . ALA A 1 67  ? 33.669  -1.206  25.833  1.00 26.24  ? 46  ALA A C   1 
ATOM   357  O  O   . ALA A 1 67  ? 34.081  -0.794  26.923  1.00 23.59  ? 46  ALA A O   1 
ATOM   358  C  CB  . ALA A 1 67  ? 31.553  -2.528  25.994  1.00 25.05  ? 46  ALA A CB  1 
ATOM   359  N  N   . ILE A 1 68  ? 34.500  -1.651  24.884  1.00 24.63  ? 47  ILE A N   1 
ATOM   360  C  CA  . ILE A 1 68  ? 35.926  -1.799  25.164  1.00 20.79  ? 47  ILE A CA  1 
ATOM   361  C  C   . ILE A 1 68  ? 36.685  -0.488  25.065  1.00 20.27  ? 47  ILE A C   1 
ATOM   362  O  O   . ILE A 1 68  ? 37.902  -0.475  25.289  1.00 22.54  ? 47  ILE A O   1 
ATOM   363  C  CB  . ILE A 1 68  ? 36.565  -2.855  24.238  1.00 20.59  ? 47  ILE A CB  1 
ATOM   364  C  CG1 . ILE A 1 68  ? 36.181  -2.617  22.779  1.00 23.52  ? 47  ILE A CG1 1 
ATOM   365  C  CG2 . ILE A 1 68  ? 36.125  -4.246  24.670  1.00 24.06  ? 47  ILE A CG2 1 
ATOM   366  C  CD1 . ILE A 1 68  ? 37.087  -3.337  21.780  1.00 22.60  ? 47  ILE A CD1 1 
ATOM   367  N  N   . THR A 1 69  ? 36.005  0.622   24.764  1.00 18.49  ? 48  THR A N   1 
ATOM   368  C  CA  . THR A 1 69  ? 36.625  1.929   24.942  1.00 23.38  ? 48  THR A CA  1 
ATOM   369  C  C   . THR A 1 69  ? 36.960  2.194   26.405  1.00 23.68  ? 48  THR A C   1 
ATOM   370  O  O   . THR A 1 69  ? 37.746  3.102   26.693  1.00 22.72  ? 48  THR A O   1 
ATOM   371  C  CB  . THR A 1 69  ? 35.717  3.050   24.427  1.00 25.69  ? 48  THR A CB  1 
ATOM   372  O  OG1 . THR A 1 69  ? 34.546  3.149   25.250  1.00 22.44  ? 48  THR A OG1 1 
ATOM   373  C  CG2 . THR A 1 69  ? 35.314  2.795   22.990  1.00 18.30  ? 48  THR A CG2 1 
ATOM   374  N  N   . VAL A 1 70  ? 36.359  1.444   27.327  1.00 25.98  ? 49  VAL A N   1 
ATOM   375  C  CA  . VAL A 1 70  ? 36.783  1.382   28.721  1.00 25.56  ? 49  VAL A CA  1 
ATOM   376  C  C   . VAL A 1 70  ? 37.285  -0.033  28.978  1.00 27.93  ? 49  VAL A C   1 
ATOM   377  O  O   . VAL A 1 70  ? 36.640  -1.007  28.571  1.00 27.90  ? 49  VAL A O   1 
ATOM   378  C  CB  . VAL A 1 70  ? 35.646  1.753   29.691  1.00 30.72  ? 49  VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 70  ? 35.327  3.235   29.601  1.00 28.18  ? 49  VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 70  ? 34.401  0.924   29.417  1.00 34.46  ? 49  VAL A CG2 1 
ATOM   381  N  N   . ARG A 1 71  ? 38.442  -0.149  29.624  1.00 27.16  ? 50  ARG A N   1 
ATOM   382  C  CA  . ARG A 1 71  ? 39.046  -1.458  29.833  1.00 31.23  ? 50  ARG A CA  1 
ATOM   383  C  C   . ARG A 1 71  ? 38.096  -2.361  30.615  1.00 34.96  ? 50  ARG A C   1 
ATOM   384  O  O   . ARG A 1 71  ? 37.519  -1.952  31.627  1.00 34.83  ? 50  ARG A O   1 
ATOM   385  C  CB  . ARG A 1 71  ? 40.378  -1.311  30.570  1.00 33.90  ? 50  ARG A CB  1 
ATOM   386  C  CG  . ARG A 1 71  ? 41.267  -2.549  30.513  1.00 40.37  ? 50  ARG A CG  1 
ATOM   387  C  CD  . ARG A 1 71  ? 41.919  -2.730  29.140  1.00 44.00  ? 50  ARG A CD  1 
ATOM   388  N  NE  . ARG A 1 71  ? 43.254  -2.138  29.077  1.00 43.53  ? 50  ARG A NE  1 
ATOM   389  C  CZ  . ARG A 1 71  ? 43.578  -1.041  28.402  1.00 38.59  ? 50  ARG A CZ  1 
ATOM   390  N  NH1 . ARG A 1 71  ? 42.690  -0.381  27.673  1.00 45.53  ? 50  ARG A NH1 1 
ATOM   391  N  NH2 . ARG A 1 71  ? 44.831  -0.600  28.450  1.00 50.71  ? 50  ARG A NH2 1 
ATOM   392  N  N   . GLN A 1 72  ? 37.939  -3.593  30.136  1.00 33.45  ? 51  GLN A N   1 
ATOM   393  C  CA  . GLN A 1 72  ? 37.007  -4.558  30.695  1.00 31.79  ? 51  GLN A CA  1 
ATOM   394  C  C   . GLN A 1 72  ? 37.759  -5.790  31.177  1.00 35.33  ? 51  GLN A C   1 
ATOM   395  O  O   . GLN A 1 72  ? 38.838  -6.117  30.672  1.00 37.16  ? 51  GLN A O   1 
ATOM   396  C  CB  . GLN A 1 72  ? 35.964  -5.006  29.655  1.00 35.21  ? 51  GLN A CB  1 
ATOM   397  C  CG  . GLN A 1 72  ? 35.135  -3.895  29.044  1.00 37.11  ? 51  GLN A CG  1 
ATOM   398  C  CD  . GLN A 1 72  ? 34.043  -3.415  29.966  1.00 29.83  ? 51  GLN A CD  1 
ATOM   399  O  OE1 . GLN A 1 72  ? 33.705  -4.080  30.942  1.00 43.53  ? 51  GLN A OE1 1 
ATOM   400  N  NE2 . GLN A 1 72  ? 33.483  -2.252  29.663  1.00 34.54  ? 51  GLN A NE2 1 
ATOM   401  N  N   . ASP A 1 73  ? 37.180  -6.474  32.151  1.00 25.84  ? 52  ASP A N   1 
ATOM   402  C  CA  . ASP A 1 73  ? 37.640  -7.812  32.481  1.00 32.06  ? 52  ASP A CA  1 
ATOM   403  C  C   . ASP A 1 73  ? 37.142  -8.763  31.399  1.00 26.15  ? 52  ASP A C   1 
ATOM   404  O  O   . ASP A 1 73  ? 35.934  -8.797  31.130  1.00 23.91  ? 52  ASP A O   1 
ATOM   405  C  CB  . ASP A 1 73  ? 37.134  -8.244  33.846  1.00 30.52  ? 52  ASP A CB  1 
ATOM   406  C  CG  . ASP A 1 73  ? 37.439  -9.691  34.131  1.00 30.25  ? 52  ASP A CG  1 
ATOM   407  O  OD1 . ASP A 1 73  ? 38.636  -10.040 34.214  1.00 33.11  ? 52  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A 1 73  ? 36.483  -10.482 34.258  1.00 36.26  ? 52  ASP A OD2 1 
ATOM   409  N  N   . PRO A 1 74  ? 38.015  -9.532  30.743  1.00 30.30  ? 53  PRO A N   1 
ATOM   410  C  CA  . PRO A 1 74  ? 37.549  -10.329 29.591  1.00 34.12  ? 53  PRO A CA  1 
ATOM   411  C  C   . PRO A 1 74  ? 36.352  -11.222 29.893  1.00 25.86  ? 53  PRO A C   1 
ATOM   412  O  O   . PRO A 1 74  ? 35.340  -11.160 29.184  1.00 26.76  ? 53  PRO A O   1 
ATOM   413  C  CB  . PRO A 1 74  ? 38.798  -11.141 29.215  1.00 30.28  ? 53  PRO A CB  1 
ATOM   414  C  CG  . PRO A 1 74  ? 39.945  -10.304 29.674  1.00 29.63  ? 53  PRO A CG  1 
ATOM   415  C  CD  . PRO A 1 74  ? 39.478  -9.613  30.924  1.00 26.63  ? 53  PRO A CD  1 
ATOM   416  N  N   . GLN A 1 75  ? 36.436  -12.048 30.936  1.00 25.36  ? 54  GLN A N   1 
ATOM   417  C  CA  . GLN A 1 75  ? 35.360  -12.994 31.217  1.00 30.13  ? 54  GLN A CA  1 
ATOM   418  C  C   . GLN A 1 75  ? 34.049  -12.278 31.518  1.00 29.53  ? 54  GLN A C   1 
ATOM   419  O  O   . GLN A 1 75  ? 32.981  -12.717 31.075  1.00 24.70  ? 54  GLN A O   1 
ATOM   420  C  CB  . GLN A 1 75  ? 35.759  -13.897 32.381  1.00 30.37  ? 54  GLN A CB  1 
ATOM   421  C  CG  . GLN A 1 75  ? 36.661  -15.047 31.979  1.00 51.63  ? 54  GLN A CG  1 
ATOM   422  C  CD  . GLN A 1 75  ? 35.878  -16.234 31.455  1.00 63.12  ? 54  GLN A CD  1 
ATOM   423  O  OE1 . GLN A 1 75  ? 35.449  -17.094 32.225  1.00 57.53  ? 54  GLN A OE1 1 
ATOM   424  N  NE2 . GLN A 1 75  ? 35.676  -16.280 30.143  1.00 56.01  ? 54  GLN A NE2 1 
ATOM   425  N  N   . ASN A 1 76  ? 34.107  -11.178 32.273  1.00 29.11  ? 55  ASN A N   1 
ATOM   426  C  CA  . ASN A 1 76  ? 32.886  -10.456 32.611  1.00 28.56  ? 55  ASN A CA  1 
ATOM   427  C  C   . ASN A 1 76  ? 32.233  -9.856  31.372  1.00 31.90  ? 55  ASN A C   1 
ATOM   428  O  O   . ASN A 1 76  ? 31.003  -9.835  31.263  1.00 27.48  ? 55  ASN A O   1 
ATOM   429  C  CB  . ASN A 1 76  ? 33.182  -9.364  33.636  1.00 31.75  ? 55  ASN A CB  1 
ATOM   430  C  CG  . ASN A 1 76  ? 31.943  -8.574  34.012  1.00 34.39  ? 55  ASN A CG  1 
ATOM   431  O  OD1 . ASN A 1 76  ? 31.127  -9.025  34.814  1.00 39.21  ? 55  ASN A OD1 1 
ATOM   432  N  ND2 . ASN A 1 76  ? 31.791  -7.395  33.425  1.00 39.09  ? 55  ASN A ND2 1 
ATOM   433  N  N   . LEU A 1 77  ? 33.033  -9.343  30.436  1.00 29.44  ? 56  LEU A N   1 
ATOM   434  C  CA  . LEU A 1 77  ? 32.458  -8.810  29.206  1.00 25.89  ? 56  LEU A CA  1 
ATOM   435  C  C   . LEU A 1 77  ? 31.701  -9.890  28.442  1.00 25.03  ? 56  LEU A C   1 
ATOM   436  O  O   . LEU A 1 77  ? 30.587  -9.658  27.962  1.00 23.06  ? 56  LEU A O   1 
ATOM   437  C  CB  . LEU A 1 77  ? 33.557  -8.209  28.333  1.00 26.11  ? 56  LEU A CB  1 
ATOM   438  C  CG  . LEU A 1 77  ? 33.116  -7.787  26.935  1.00 28.37  ? 56  LEU A CG  1 
ATOM   439  C  CD1 . LEU A 1 77  ? 32.040  -6.727  27.028  1.00 24.21  ? 56  LEU A CD1 1 
ATOM   440  C  CD2 . LEU A 1 77  ? 34.306  -7.299  26.119  1.00 26.84  ? 56  LEU A CD2 1 
ATOM   441  N  N   . ARG A 1 78  ? 32.287  -11.081 28.323  1.00 25.67  ? 57  ARG A N   1 
ATOM   442  C  CA  . ARG A 1 78  ? 31.603  -12.170 27.634  1.00 30.50  ? 57  ARG A CA  1 
ATOM   443  C  C   . ARG A 1 78  ? 30.300  -12.527 28.340  1.00 31.19  ? 57  ARG A C   1 
ATOM   444  O  O   . ARG A 1 78  ? 29.260  -12.703 27.693  1.00 25.35  ? 57  ARG A O   1 
ATOM   445  C  CB  . ARG A 1 78  ? 32.530  -13.385 27.546  1.00 27.36  ? 57  ARG A CB  1 
ATOM   446  C  CG  . ARG A 1 78  ? 32.011  -14.527 26.689  1.00 31.29  ? 57  ARG A CG  1 
ATOM   447  C  CD  . ARG A 1 78  ? 33.152  -15.240 25.931  1.00 40.93  ? 57  ARG A CD  1 
ATOM   448  N  NE  . ARG A 1 78  ? 34.381  -15.329 26.715  1.00 43.53  ? 57  ARG A NE  1 
ATOM   449  C  CZ  . ARG A 1 78  ? 35.556  -14.815 26.365  1.00 38.27  ? 57  ARG A CZ  1 
ATOM   450  N  NH1 . ARG A 1 78  ? 35.742  -14.231 25.191  1.00 34.91  ? 57  ARG A NH1 1 
ATOM   451  N  NH2 . ARG A 1 78  ? 36.575  -14.895 27.215  1.00 44.25  ? 57  ARG A NH2 1 
ATOM   452  N  N   . LYS A 1 79  ? 30.332  -12.616 29.671  1.00 27.64  ? 58  LYS A N   1 
ATOM   453  C  CA  . LYS A 1 79  ? 29.123  -12.949 30.414  1.00 24.77  ? 58  LYS A CA  1 
ATOM   454  C  C   . LYS A 1 79  ? 28.071  -11.859 30.268  1.00 25.36  ? 58  LYS A C   1 
ATOM   455  O  O   . LYS A 1 79  ? 26.877  -12.150 30.146  1.00 24.11  ? 58  LYS A O   1 
ATOM   456  C  CB  . LYS A 1 79  ? 29.459  -13.170 31.888  1.00 33.54  ? 58  LYS A CB  1 
ATOM   457  C  CG  . LYS A 1 79  ? 28.329  -13.803 32.686  1.00 38.70  ? 58  LYS A CG  1 
ATOM   458  C  CD  . LYS A 1 79  ? 28.760  -14.148 34.110  1.00 49.17  ? 58  LYS A CD  1 
ATOM   459  C  CE  . LYS A 1 79  ? 28.758  -12.928 35.018  1.00 53.38  ? 58  LYS A CE  1 
ATOM   460  N  NZ  . LYS A 1 79  ? 27.378  -12.433 35.294  1.00 54.79  ? 58  LYS A NZ  1 
ATOM   461  N  N   . ALA A 1 80  ? 28.496  -10.597 30.280  1.00 24.89  ? 59  ALA A N   1 
ATOM   462  C  CA  . ALA A 1 80  ? 27.541  -9.498  30.238  1.00 30.05  ? 59  ALA A CA  1 
ATOM   463  C  C   . ALA A 1 80  ? 26.904  -9.361  28.863  1.00 25.23  ? 59  ALA A C   1 
ATOM   464  O  O   . ALA A 1 80  ? 25.773  -8.878  28.754  1.00 28.17  ? 59  ALA A O   1 
ATOM   465  C  CB  . ALA A 1 80  ? 28.228  -8.194  30.639  1.00 33.48  ? 59  ALA A CB  1 
ATOM   466  N  N   . THR A 1 81  ? 27.614  -9.757  27.806  1.00 24.55  ? 60  THR A N   1 
ATOM   467  C  CA  . THR A 1 81  ? 27.017  -9.748  26.475  1.00 25.48  ? 60  THR A CA  1 
ATOM   468  C  C   . THR A 1 81  ? 25.868  -10.746 26.395  1.00 22.08  ? 60  THR A C   1 
ATOM   469  O  O   . THR A 1 81  ? 24.778  -10.418 25.914  1.00 23.28  ? 60  THR A O   1 
ATOM   470  C  CB  . THR A 1 81  ? 28.086  -10.053 25.427  1.00 22.12  ? 60  THR A CB  1 
ATOM   471  O  OG1 . THR A 1 81  ? 29.108  -9.053  25.494  1.00 28.55  ? 60  THR A OG1 1 
ATOM   472  C  CG2 . THR A 1 81  ? 27.496  -10.063 24.025  1.00 23.60  ? 60  THR A CG2 1 
ATOM   473  N  N   . LEU A 1 82  ? 26.085  -11.966 26.894  1.00 26.18  ? 61  LEU A N   1 
ATOM   474  C  CA  . LEU A 1 82  ? 25.010  -12.953 26.915  1.00 27.05  ? 61  LEU A CA  1 
ATOM   475  C  C   . LEU A 1 82  ? 23.913  -12.554 27.898  1.00 25.54  ? 61  LEU A C   1 
ATOM   476  O  O   . LEU A 1 82  ? 22.728  -12.794 27.640  1.00 25.35  ? 61  LEU A O   1 
ATOM   477  C  CB  . LEU A 1 82  ? 25.575  -14.334 27.255  1.00 30.74  ? 61  LEU A CB  1 
ATOM   478  C  CG  . LEU A 1 82  ? 26.605  -14.887 26.262  1.00 35.08  ? 61  LEU A CG  1 
ATOM   479  C  CD1 . LEU A 1 82  ? 27.175  -16.202 26.760  1.00 44.87  ? 61  LEU A CD1 1 
ATOM   480  C  CD2 . LEU A 1 82  ? 26.001  -15.062 24.879  1.00 35.40  ? 61  LEU A CD2 1 
ATOM   481  N  N   . ASP A 1 83  ? 24.284  -11.936 29.026  1.00 28.32  ? 62  ASP A N   1 
ATOM   482  C  CA  . ASP A 1 83  ? 23.277  -11.433 29.957  1.00 30.22  ? 62  ASP A CA  1 
ATOM   483  C  C   . ASP A 1 83  ? 22.356  -10.440 29.264  1.00 31.49  ? 62  ASP A C   1 
ATOM   484  O  O   . ASP A 1 83  ? 21.131  -10.495 29.414  1.00 32.41  ? 62  ASP A O   1 
ATOM   485  C  CB  . ASP A 1 83  ? 23.940  -10.755 31.160  1.00 30.78  ? 62  ASP A CB  1 
ATOM   486  C  CG  . ASP A 1 83  ? 24.523  -11.738 32.152  1.00 36.53  ? 62  ASP A CG  1 
ATOM   487  O  OD1 . ASP A 1 83  ? 24.069  -12.899 32.182  1.00 38.91  ? 62  ASP A OD1 1 
ATOM   488  O  OD2 . ASP A 1 83  ? 25.425  -11.334 32.922  1.00 36.51  ? 62  ASP A OD2 1 
ATOM   489  N  N   . THR A 1 84  ? 22.941  -9.509  28.509  1.00 31.26  ? 63  THR A N   1 
ATOM   490  C  CA  . THR A 1 84  ? 22.145  -8.495  27.831  1.00 30.59  ? 63  THR A CA  1 
ATOM   491  C  C   . THR A 1 84  ? 21.211  -9.124  26.810  1.00 26.74  ? 63  THR A C   1 
ATOM   492  O  O   . THR A 1 84  ? 20.034  -8.759  26.730  1.00 26.86  ? 63  THR A O   1 
ATOM   493  C  CB  . THR A 1 84  ? 23.068  -7.476  27.161  1.00 34.02  ? 63  THR A CB  1 
ATOM   494  O  OG1 . THR A 1 84  ? 23.758  -6.725  28.167  1.00 35.00  ? 63  THR A OG1 1 
ATOM   495  C  CG2 . THR A 1 84  ? 22.281  -6.528  26.262  1.00 31.23  ? 63  THR A CG2 1 
ATOM   496  N  N   . LEU A 1 85  ? 21.717  -10.072 26.020  1.00 27.04  ? 64  LEU A N   1 
ATOM   497  C  CA  . LEU A 1 85  ? 20.880  -10.726 25.021  1.00 26.37  ? 64  LEU A CA  1 
ATOM   498  C  C   . LEU A 1 85  ? 19.714  -11.457 25.674  1.00 27.25  ? 64  LEU A C   1 
ATOM   499  O  O   . LEU A 1 85  ? 18.558  -11.289 25.275  1.00 28.33  ? 64  LEU A O   1 
ATOM   500  C  CB  . LEU A 1 85  ? 21.722  -11.699 24.197  1.00 25.62  ? 64  LEU A CB  1 
ATOM   501  C  CG  . LEU A 1 85  ? 20.921  -12.568 23.228  1.00 36.14  ? 64  LEU A CG  1 
ATOM   502  C  CD1 . LEU A 1 85  ? 20.195  -11.684 22.218  1.00 23.23  ? 64  LEU A CD1 1 
ATOM   503  C  CD2 . LEU A 1 85  ? 21.824  -13.578 22.541  1.00 32.46  ? 64  LEU A CD2 1 
ATOM   504  N  N   . ALA A 1 86  ? 20.004  -12.287 26.677  1.00 30.81  ? 65  ALA A N   1 
ATOM   505  C  CA  . ALA A 1 86  ? 18.938  -13.005 27.364  1.00 29.35  ? 65  ALA A CA  1 
ATOM   506  C  C   . ALA A 1 86  ? 17.928  -12.043 27.967  1.00 29.21  ? 65  ALA A C   1 
ATOM   507  O  O   . ALA A 1 86  ? 16.730  -12.342 28.000  1.00 25.79  ? 65  ALA A O   1 
ATOM   508  C  CB  . ALA A 1 86  ? 19.525  -13.903 28.454  1.00 29.56  ? 65  ALA A CB  1 
ATOM   509  N  N   . LEU A 1 87  ? 18.391  -10.883 28.440  1.00 28.83  ? 66  LEU A N   1 
ATOM   510  C  CA  . LEU A 1 87  ? 17.491  -9.934  29.085  1.00 26.00  ? 66  LEU A CA  1 
ATOM   511  C  C   . LEU A 1 87  ? 16.560  -9.280  28.072  1.00 28.24  ? 66  LEU A C   1 
ATOM   512  O  O   . LEU A 1 87  ? 15.354  -9.172  28.313  1.00 30.95  ? 66  LEU A O   1 
ATOM   513  C  CB  . LEU A 1 87  ? 18.306  -8.883  29.838  1.00 32.18  ? 66  LEU A CB  1 
ATOM   514  C  CG  . LEU A 1 87  ? 17.549  -7.849  30.674  1.00 37.91  ? 66  LEU A CG  1 
ATOM   515  C  CD1 . LEU A 1 87  ? 16.509  -8.515  31.558  1.00 44.58  ? 66  LEU A CD1 1 
ATOM   516  C  CD2 . LEU A 1 87  ? 18.531  -7.050  31.519  1.00 47.61  ? 66  LEU A CD2 1 
ATOM   517  N  N   . TYR A 1 88  ? 17.093  -8.850  26.927  1.00 30.42  ? 67  TYR A N   1 
ATOM   518  C  CA  . TYR A 1 88  ? 16.233  -8.293  25.888  1.00 31.90  ? 67  TYR A CA  1 
ATOM   519  C  C   . TYR A 1 88  ? 15.274  -9.340  25.336  1.00 30.52  ? 67  TYR A C   1 
ATOM   520  O  O   . TYR A 1 88  ? 14.139  -9.010  24.975  1.00 33.50  ? 67  TYR A O   1 
ATOM   521  C  CB  . TYR A 1 88  ? 17.085  -7.697  24.767  1.00 34.10  ? 67  TYR A CB  1 
ATOM   522  C  CG  . TYR A 1 88  ? 17.543  -6.283  25.051  1.00 30.97  ? 67  TYR A CG  1 
ATOM   523  C  CD1 . TYR A 1 88  ? 18.472  -6.021  26.048  1.00 34.58  ? 67  TYR A CD1 1 
ATOM   524  C  CD2 . TYR A 1 88  ? 17.045  -5.210  24.322  1.00 38.67  ? 67  TYR A CD2 1 
ATOM   525  C  CE1 . TYR A 1 88  ? 18.893  -4.731  26.313  1.00 38.04  ? 67  TYR A CE1 1 
ATOM   526  C  CE2 . TYR A 1 88  ? 17.460  -3.913  24.581  1.00 38.93  ? 67  TYR A CE2 1 
ATOM   527  C  CZ  . TYR A 1 88  ? 18.384  -3.682  25.576  1.00 37.12  ? 67  TYR A CZ  1 
ATOM   528  O  OH  . TYR A 1 88  ? 18.801  -2.400  25.840  1.00 34.80  ? 67  TYR A OH  1 
ATOM   529  N  N   . LEU A 1 89  ? 15.709  -10.599 25.253  1.00 34.00  ? 68  LEU A N   1 
ATOM   530  C  CA  . LEU A 1 89  ? 14.803  -11.669 24.846  1.00 30.86  ? 68  LEU A CA  1 
ATOM   531  C  C   . LEU A 1 89  ? 13.662  -11.838 25.844  1.00 33.07  ? 68  LEU A C   1 
ATOM   532  O  O   . LEU A 1 89  ? 12.498  -11.981 25.450  1.00 33.26  ? 68  LEU A O   1 
ATOM   533  C  CB  . LEU A 1 89  ? 15.574  -12.981 24.704  1.00 34.04  ? 68  LEU A CB  1 
ATOM   534  C  CG  . LEU A 1 89  ? 16.575  -13.065 23.552  1.00 33.91  ? 68  LEU A CG  1 
ATOM   535  C  CD1 . LEU A 1 89  ? 17.440  -14.317 23.682  1.00 31.80  ? 68  LEU A CD1 1 
ATOM   536  C  CD2 . LEU A 1 89  ? 15.845  -13.055 22.225  1.00 38.33  ? 68  LEU A CD2 1 
ATOM   537  N  N   . ALA A 1 90  ? 13.978  -11.828 27.144  1.00 30.41  ? 69  ALA A N   1 
ATOM   538  C  CA  . ALA A 1 90  ? 12.950  -12.005 28.164  1.00 35.56  ? 69  ALA A CA  1 
ATOM   539  C  C   . ALA A 1 90  ? 11.977  -10.833 28.192  1.00 37.66  ? 69  ALA A C   1 
ATOM   540  O  O   . ALA A 1 90  ? 10.793  -11.020 28.495  1.00 33.34  ? 69  ALA A O   1 
ATOM   541  C  CB  . ALA A 1 90  ? 13.597  -12.187 29.538  1.00 31.57  ? 69  ALA A CB  1 
ATOM   542  N  N   . CYS A 1 91  ? 12.453  -9.624  27.888  1.00 33.54  ? 70  CYS A N   1 
ATOM   543  C  CA  . CYS A 1 91  ? 11.565  -8.472  27.820  1.00 39.64  ? 70  CYS A CA  1 
ATOM   544  C  C   . CYS A 1 91  ? 10.575  -8.575  26.668  1.00 41.51  ? 70  CYS A C   1 
ATOM   545  O  O   . CYS A 1 91  ? 9.525   -7.924  26.713  1.00 44.13  ? 70  CYS A O   1 
ATOM   546  C  CB  . CYS A 1 91  ? 12.383  -7.187  27.699  1.00 40.55  ? 70  CYS A CB  1 
ATOM   547  S  SG  . CYS A 1 91  ? 13.249  -6.734  29.221  1.00 43.95  ? 70  CYS A SG  1 
ATOM   548  N  N   . GLY A 1 92  ? 10.880  -9.371  25.643  1.00 42.78  ? 71  GLY A N   1 
ATOM   549  C  CA  . GLY A 1 92  ? 9.919   -9.635  24.589  1.00 38.19  ? 71  GLY A CA  1 
ATOM   550  C  C   . GLY A 1 92  ? 10.414  -9.395  23.178  1.00 40.63  ? 71  GLY A C   1 
ATOM   551  O  O   . GLY A 1 92  ? 9.657   -9.579  22.221  1.00 39.13  ? 71  GLY A O   1 
ATOM   552  N  N   . ILE A 1 93  ? 11.673  -8.986  23.016  1.00 34.42  ? 72  ILE A N   1 
ATOM   553  C  CA  . ILE A 1 93  ? 12.205  -8.820  21.670  1.00 34.99  ? 72  ILE A CA  1 
ATOM   554  C  C   . ILE A 1 93  ? 12.220  -10.175 20.976  1.00 37.40  ? 72  ILE A C   1 
ATOM   555  O  O   . ILE A 1 93  ? 12.767  -11.157 21.494  1.00 37.75  ? 72  ILE A O   1 
ATOM   556  C  CB  . ILE A 1 93  ? 13.601  -8.187  21.709  1.00 32.90  ? 72  ILE A CB  1 
ATOM   557  C  CG1 . ILE A 1 93  ? 13.539  -6.786  22.327  1.00 38.20  ? 72  ILE A CG1 1 
ATOM   558  C  CG2 . ILE A 1 93  ? 14.179  -8.118  20.303  1.00 36.25  ? 72  ILE A CG2 1 
ATOM   559  C  CD1 . ILE A 1 93  ? 12.587  -5.829  21.621  1.00 43.29  ? 72  ILE A CD1 1 
ATOM   560  N  N   . ASP A 1 94  ? 11.613  -10.229 19.793  1.00 31.56  ? 73  ASP A N   1 
ATOM   561  C  CA  . ASP A 1 94  ? 11.413  -11.478 19.076  1.00 38.36  ? 73  ASP A CA  1 
ATOM   562  C  C   . ASP A 1 94  ? 12.430  -11.575 17.952  1.00 40.11  ? 73  ASP A C   1 
ATOM   563  O  O   . ASP A 1 94  ? 12.367  -10.771 17.013  1.00 35.76  ? 73  ASP A O   1 
ATOM   564  C  CB  . ASP A 1 94  ? 9.993   -11.539 18.517  1.00 44.40  ? 73  ASP A CB  1 
ATOM   565  C  CG  . ASP A 1 94  ? 9.639   -12.902 17.963  1.00 49.07  ? 73  ASP A CG  1 
ATOM   566  O  OD1 . ASP A 1 94  ? 10.562  -13.673 17.621  1.00 47.02  ? 73  ASP A OD1 1 
ATOM   567  O  OD2 . ASP A 1 94  ? 8.430   -13.198 17.868  1.00 53.89  ? 73  ASP A OD2 1 
ATOM   568  N  N   . PRO A 1 95  ? 13.365  -12.530 17.982  1.00 41.08  ? 74  PRO A N   1 
ATOM   569  C  CA  . PRO A 1 95  ? 14.385  -12.585 16.921  1.00 42.34  ? 74  PRO A CA  1 
ATOM   570  C  C   . PRO A 1 95  ? 13.822  -12.878 15.542  1.00 41.05  ? 74  PRO A C   1 
ATOM   571  O  O   . PRO A 1 95  ? 14.565  -12.767 14.558  1.00 44.43  ? 74  PRO A O   1 
ATOM   572  C  CB  . PRO A 1 95  ? 15.328  -13.704 17.391  1.00 48.94  ? 74  PRO A CB  1 
ATOM   573  C  CG  . PRO A 1 95  ? 14.514  -14.533 18.316  1.00 39.57  ? 74  PRO A CG  1 
ATOM   574  C  CD  . PRO A 1 95  ? 13.558  -13.589 18.988  1.00 42.22  ? 74  PRO A CD  1 
ATOM   575  N  N   . GLN A 1 96  ? 12.548  -13.249 15.435  1.00 46.86  ? 75  GLN A N   1 
ATOM   576  C  CA  . GLN A 1 96  ? 11.926  -13.473 14.137  1.00 44.59  ? 75  GLN A CA  1 
ATOM   577  C  C   . GLN A 1 96  ? 11.276  -12.219 13.569  1.00 46.03  ? 75  GLN A C   1 
ATOM   578  O  O   . GLN A 1 96  ? 11.198  -12.074 12.343  1.00 46.39  ? 75  GLN A O   1 
ATOM   579  C  CB  . GLN A 1 96  ? 10.881  -14.588 14.238  1.00 49.73  ? 75  GLN A CB  1 
ATOM   580  C  CG  . GLN A 1 96  ? 11.470  -15.994 14.264  1.00 56.81  ? 75  GLN A CG  1 
ATOM   581  C  CD  . GLN A 1 96  ? 12.328  -16.288 13.050  1.00 60.77  ? 75  GLN A CD  1 
ATOM   582  O  OE1 . GLN A 1 96  ? 13.447  -16.785 13.174  1.00 65.50  ? 75  GLN A OE1 1 
ATOM   583  N  NE2 . GLN A 1 96  ? 11.811  -15.973 11.868  1.00 64.55  ? 75  GLN A NE2 1 
ATOM   584  N  N   . LYS A 1 97  ? 10.802  -11.311 14.424  1.00 44.44  ? 76  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 97  ? 10.264  -10.039 13.956  1.00 45.03  ? 76  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 97  ? 11.345  -8.974  13.834  1.00 41.78  ? 76  LYS A C   1 
ATOM   587  O  O   . LYS A 1 97  ? 11.315  -8.160  12.905  1.00 40.59  ? 76  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 97  ? 9.174   -9.537  14.906  1.00 43.63  ? 76  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 97  ? 7.950   -10.426 14.990  1.00 48.92  ? 76  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 97  ? 6.896   -9.805  15.884  1.00 46.17  ? 76  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 97  ? 5.667   -10.691 15.998  1.00 53.20  ? 76  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 97  ? 4.662   -10.114 16.927  1.00 47.02  ? 76  LYS A NZ  1 
ATOM   593  N  N   . SER A 1 98  ? 12.293  -8.969  14.764  1.00 42.28  ? 77  SER A N   1 
ATOM   594  C  CA  . SER A 1 98  ? 13.349  -7.975  14.838  1.00 37.55  ? 77  SER A CA  1 
ATOM   595  C  C   . SER A 1 98  ? 14.702  -8.633  14.601  1.00 36.58  ? 77  SER A C   1 
ATOM   596  O  O   . SER A 1 98  ? 14.828  -9.859  14.527  1.00 40.27  ? 77  SER A O   1 
ATOM   597  C  CB  . SER A 1 98  ? 13.336  -7.273  16.203  1.00 35.82  ? 77  SER A CB  1 
ATOM   598  O  OG  . SER A 1 98  ? 12.065  -6.704  16.474  1.00 41.62  ? 77  SER A OG  1 
ATOM   599  N  N   . THR A 1 99  ? 15.721  -7.791  14.486  1.00 29.49  ? 78  THR A N   1 
ATOM   600  C  CA  . THR A 1 99  ? 17.099  -8.222  14.286  1.00 32.23  ? 78  THR A CA  1 
ATOM   601  C  C   . THR A 1 99  ? 17.885  -7.835  15.530  1.00 27.19  ? 78  THR A C   1 
ATOM   602  O  O   . THR A 1 99  ? 18.083  -6.648  15.797  1.00 27.52  ? 78  THR A O   1 
ATOM   603  C  CB  . THR A 1 99  ? 17.695  -7.580  13.035  1.00 32.18  ? 78  THR A CB  1 
ATOM   604  O  OG1 . THR A 1 99  ? 16.910  -7.945  11.893  1.00 37.26  ? 78  THR A OG1 1 
ATOM   605  C  CG2 . THR A 1 99  ? 19.135  -8.027  12.828  1.00 32.47  ? 78  THR A CG2 1 
ATOM   606  N  N   . ILE A 1 100 ? 18.316  -8.833  16.295  1.00 28.85  ? 79  ILE A N   1 
ATOM   607  C  CA  . ILE A 1 100 ? 19.145  -8.626  17.475  1.00 26.72  ? 79  ILE A CA  1 
ATOM   608  C  C   . ILE A 1 100 ? 20.439  -9.401  17.278  1.00 26.25  ? 79  ILE A C   1 
ATOM   609  O  O   . ILE A 1 100 ? 20.413  -10.576 16.895  1.00 24.91  ? 79  ILE A O   1 
ATOM   610  C  CB  . ILE A 1 100 ? 18.424  -9.060  18.764  1.00 28.27  ? 79  ILE A CB  1 
ATOM   611  C  CG1 . ILE A 1 100 ? 19.303  -8.754  19.975  1.00 25.50  ? 79  ILE A CG1 1 
ATOM   612  C  CG2 . ILE A 1 100 ? 18.073  -10.545 18.716  1.00 33.90  ? 79  ILE A CG2 1 
ATOM   613  C  CD1 . ILE A 1 100 ? 18.527  -8.487  21.241  1.00 28.11  ? 79  ILE A CD1 1 
ATOM   614  N  N   . PHE A 1 101 ? 21.566  -8.740  17.525  1.00 25.18  ? 80  PHE A N   1 
ATOM   615  C  CA  . PHE A 1 101 ? 22.861  -9.328  17.222  1.00 20.51  ? 80  PHE A CA  1 
ATOM   616  C  C   . PHE A 1 101 ? 23.928  -8.634  18.051  1.00 21.29  ? 80  PHE A C   1 
ATOM   617  O  O   . PHE A 1 101 ? 23.695  -7.583  18.651  1.00 23.01  ? 80  PHE A O   1 
ATOM   618  C  CB  . PHE A 1 101 ? 23.185  -9.214  15.727  1.00 24.83  ? 80  PHE A CB  1 
ATOM   619  C  CG  . PHE A 1 101 ? 23.363  -7.799  15.250  1.00 21.52  ? 80  PHE A CG  1 
ATOM   620  C  CD1 . PHE A 1 101 ? 22.267  -7.005  14.974  1.00 21.67  ? 80  PHE A CD1 1 
ATOM   621  C  CD2 . PHE A 1 101 ? 24.630  -7.267  15.068  1.00 19.31  ? 80  PHE A CD2 1 
ATOM   622  C  CE1 . PHE A 1 101 ? 22.425  -5.706  14.534  1.00 24.86  ? 80  PHE A CE1 1 
ATOM   623  C  CE2 . PHE A 1 101 ? 24.796  -5.967  14.623  1.00 23.60  ? 80  PHE A CE2 1 
ATOM   624  C  CZ  . PHE A 1 101 ? 23.690  -5.186  14.358  1.00 25.47  ? 80  PHE A CZ  1 
ATOM   625  N  N   . VAL A 1 102 ? 25.107  -9.243  18.067  1.00 20.79  ? 81  VAL A N   1 
ATOM   626  C  CA  . VAL A 1 102 ? 26.286  -8.680  18.714  1.00 18.19  ? 81  VAL A CA  1 
ATOM   627  C  C   . VAL A 1 102 ? 27.073  -7.890  17.677  1.00 20.44  ? 81  VAL A C   1 
ATOM   628  O  O   . VAL A 1 102 ? 27.315  -8.373  16.565  1.00 18.35  ? 81  VAL A O   1 
ATOM   629  C  CB  . VAL A 1 102 ? 27.149  -9.792  19.331  1.00 20.17  ? 81  VAL A CB  1 
ATOM   630  C  CG1 . VAL A 1 102 ? 28.431  -9.216  19.890  1.00 19.09  ? 81  VAL A CG1 1 
ATOM   631  C  CG2 . VAL A 1 102 ? 26.369  -10.538 20.414  1.00 22.20  ? 81  VAL A CG2 1 
ATOM   632  N  N   . GLN A 1 103 ? 27.489  -6.679  18.051  1.00 18.71  ? 82  GLN A N   1 
ATOM   633  C  CA  . GLN A 1 103 ? 28.139  -5.779  17.102  1.00 23.44  ? 82  GLN A CA  1 
ATOM   634  C  C   . GLN A 1 103 ? 29.391  -6.406  16.496  1.00 19.99  ? 82  GLN A C   1 
ATOM   635  O  O   . GLN A 1 103 ? 29.596  -6.345  15.277  1.00 17.79  ? 82  GLN A O   1 
ATOM   636  C  CB  . GLN A 1 103 ? 28.475  -4.468  17.817  1.00 21.98  ? 82  GLN A CB  1 
ATOM   637  C  CG  . GLN A 1 103 ? 28.935  -3.318  16.941  1.00 21.52  ? 82  GLN A CG  1 
ATOM   638  C  CD  . GLN A 1 103 ? 29.443  -2.161  17.778  1.00 23.27  ? 82  GLN A CD  1 
ATOM   639  O  OE1 . GLN A 1 103 ? 29.740  -2.327  18.959  1.00 25.82  ? 82  GLN A OE1 1 
ATOM   640  N  NE2 . GLN A 1 103 ? 29.540  -0.985  17.176  1.00 27.10  ? 82  GLN A NE2 1 
ATOM   641  N  N   . SER A 1 104 ? 30.229  -7.035  17.322  1.00 21.86  ? 83  SER A N   1 
ATOM   642  C  CA  . SER A 1 104 ? 31.485  -7.597  16.835  1.00 20.95  ? 83  SER A CA  1 
ATOM   643  C  C   . SER A 1 104 ? 31.287  -8.753  15.861  1.00 24.50  ? 83  SER A C   1 
ATOM   644  O  O   . SER A 1 104 ? 32.246  -9.132  15.180  1.00 22.46  ? 83  SER A O   1 
ATOM   645  C  CB  . SER A 1 104 ? 32.348  -8.067  18.009  1.00 21.89  ? 83  SER A CB  1 
ATOM   646  O  OG  . SER A 1 104 ? 31.767  -9.177  18.675  1.00 21.17  ? 83  SER A OG  1 
ATOM   647  N  N   . HIS A 1 105 ? 30.083  -9.322  15.783  1.00 21.05  ? 84  HIS A N   1 
ATOM   648  C  CA  . HIS A 1 105 ? 29.803  -10.404 14.847  1.00 23.06  ? 84  HIS A CA  1 
ATOM   649  C  C   . HIS A 1 105 ? 29.554  -9.914  13.427  1.00 23.00  ? 84  HIS A C   1 
ATOM   650  O  O   . HIS A 1 105 ? 29.446  -10.741 12.516  1.00 23.05  ? 84  HIS A O   1 
ATOM   651  C  CB  . HIS A 1 105 ? 28.580  -11.199 15.309  1.00 24.02  ? 84  HIS A CB  1 
ATOM   652  C  CG  . HIS A 1 105 ? 28.773  -11.910 16.611  1.00 22.65  ? 84  HIS A CG  1 
ATOM   653  N  ND1 . HIS A 1 105 ? 27.743  -12.551 17.266  1.00 26.33  ? 84  HIS A ND1 1 
ATOM   654  C  CD2 . HIS A 1 105 ? 29.874  -12.086 17.378  1.00 25.37  ? 84  HIS A CD2 1 
ATOM   655  C  CE1 . HIS A 1 105 ? 28.201  -13.089 18.381  1.00 29.32  ? 84  HIS A CE1 1 
ATOM   656  N  NE2 . HIS A 1 105 ? 29.492  -12.823 18.473  1.00 28.62  ? 84  HIS A NE2 1 
ATOM   657  N  N   . VAL A 1 106 ? 29.440  -8.609  13.225  1.00 20.42  ? 85  VAL A N   1 
ATOM   658  C  CA  . VAL A 1 106 ? 29.154  -8.019  11.926  1.00 24.09  ? 85  VAL A CA  1 
ATOM   659  C  C   . VAL A 1 106 ? 30.323  -7.118  11.552  1.00 18.22  ? 85  VAL A C   1 
ATOM   660  O  O   . VAL A 1 106 ? 30.391  -5.964  11.977  1.00 19.28  ? 85  VAL A O   1 
ATOM   661  C  CB  . VAL A 1 106 ? 27.828  -7.236  11.948  1.00 22.92  ? 85  VAL A CB  1 
ATOM   662  C  CG1 . VAL A 1 106 ? 27.573  -6.545  10.615  1.00 22.33  ? 85  VAL A CG1 1 
ATOM   663  C  CG2 . VAL A 1 106 ? 26.685  -8.172  12.290  1.00 22.72  ? 85  VAL A CG2 1 
ATOM   664  N  N   . PRO A 1 107 ? 31.271  -7.616  10.755  1.00 20.08  ? 86  PRO A N   1 
ATOM   665  C  CA  . PRO A 1 107 ? 32.471  -6.820  10.451  1.00 22.07  ? 86  PRO A CA  1 
ATOM   666  C  C   . PRO A 1 107 ? 32.167  -5.492  9.786   1.00 22.84  ? 86  PRO A C   1 
ATOM   667  O  O   . PRO A 1 107 ? 32.990  -4.572  9.869   1.00 18.56  ? 86  PRO A O   1 
ATOM   668  C  CB  . PRO A 1 107 ? 33.274  -7.735  9.514   1.00 24.50  ? 86  PRO A CB  1 
ATOM   669  C  CG  . PRO A 1 107 ? 32.787  -9.104  9.792   1.00 27.43  ? 86  PRO A CG  1 
ATOM   670  C  CD  . PRO A 1 107 ? 31.343  -8.969  10.172  1.00 23.62  ? 86  PRO A CD  1 
ATOM   671  N  N   . GLU A 1 108 ? 31.011  -5.360  9.136   1.00 21.11  ? 87  GLU A N   1 
ATOM   672  C  CA  . GLU A 1 108 ? 30.698  -4.137  8.413   1.00 20.02  ? 87  GLU A CA  1 
ATOM   673  C  C   . GLU A 1 108 ? 30.656  -2.920  9.325   1.00 21.29  ? 87  GLU A C   1 
ATOM   674  O  O   . GLU A 1 108 ? 30.846  -1.798  8.846   1.00 20.46  ? 87  GLU A O   1 
ATOM   675  C  CB  . GLU A 1 108 ? 29.363  -4.289  7.683   1.00 20.90  ? 87  GLU A CB  1 
ATOM   676  C  CG  . GLU A 1 108 ? 29.412  -5.217  6.476   1.00 21.14  ? 87  GLU A CG  1 
ATOM   677  C  CD  . GLU A 1 108 ? 29.233  -6.686  6.825   1.00 26.65  ? 87  GLU A CD  1 
ATOM   678  O  OE1 . GLU A 1 108 ? 28.920  -7.005  7.993   1.00 31.35  ? 87  GLU A OE1 1 
ATOM   679  O  OE2 . GLU A 1 108 ? 29.402  -7.527  5.919   1.00 31.63  ? 87  GLU A OE2 1 
ATOM   680  N  N   . HIS A 1 109 ? 30.405  -3.102  10.623  1.00 19.38  ? 88  HIS A N   1 
ATOM   681  C  CA  . HIS A 1 109 ? 30.408  -1.955  11.527  1.00 19.50  ? 88  HIS A CA  1 
ATOM   682  C  C   . HIS A 1 109 ? 31.792  -1.314  11.599  1.00 16.70  ? 88  HIS A C   1 
ATOM   683  O  O   . HIS A 1 109 ? 31.931  -0.095  11.447  1.00 19.07  ? 88  HIS A O   1 
ATOM   684  C  CB  . HIS A 1 109 ? 29.915  -2.384  12.908  1.00 20.14  ? 88  HIS A CB  1 
ATOM   685  C  CG  . HIS A 1 109 ? 28.449  -2.683  12.944  1.00 18.16  ? 88  HIS A CG  1 
ATOM   686  N  ND1 . HIS A 1 109 ? 27.543  -1.900  13.624  1.00 21.48  ? 88  HIS A ND1 1 
ATOM   687  C  CD2 . HIS A 1 109 ? 27.729  -3.662  12.349  1.00 20.09  ? 88  HIS A CD2 1 
ATOM   688  C  CE1 . HIS A 1 109 ? 26.329  -2.396  13.464  1.00 18.70  ? 88  HIS A CE1 1 
ATOM   689  N  NE2 . HIS A 1 109 ? 26.415  -3.463  12.692  1.00 18.91  ? 88  HIS A NE2 1 
ATOM   690  N  N   . ALA A 1 110 ? 32.834  -2.120  11.810  1.00 17.34  ? 89  ALA A N   1 
ATOM   691  C  CA  . ALA A 1 110 ? 34.186  -1.569  11.840  1.00 15.58  ? 89  ALA A CA  1 
ATOM   692  C  C   . ALA A 1 110 ? 34.606  -1.046  10.470  1.00 21.82  ? 89  ALA A C   1 
ATOM   693  O  O   . ALA A 1 110 ? 35.260  -0.001  10.373  1.00 19.25  ? 89  ALA A O   1 
ATOM   694  C  CB  . ALA A 1 110 ? 35.176  -2.625  12.328  1.00 21.31  ? 89  ALA A CB  1 
ATOM   695  N  N   . GLN A 1 111 ? 34.248  -1.760  9.400   1.00 17.07  ? 90  GLN A N   1 
ATOM   696  C  CA  . GLN A 1 111 ? 34.626  -1.316  8.063   1.00 17.46  ? 90  GLN A CA  1 
ATOM   697  C  C   . GLN A 1 111 ? 34.078  0.076   7.772   1.00 20.61  ? 90  GLN A C   1 
ATOM   698  O  O   . GLN A 1 111 ? 34.822  0.974   7.357   1.00 20.51  ? 90  GLN A O   1 
ATOM   699  C  CB  . GLN A 1 111 ? 34.133  -2.314  7.017   1.00 16.28  ? 90  GLN A CB  1 
ATOM   700  C  CG  . GLN A 1 111 ? 34.723  -3.709  7.164   1.00 19.06  ? 90  GLN A CG  1 
ATOM   701  C  CD  . GLN A 1 111 ? 34.105  -4.708  6.210   1.00 20.04  ? 90  GLN A CD  1 
ATOM   702  O  OE1 . GLN A 1 111 ? 33.178  -5.430  6.569   1.00 23.82  ? 90  GLN A OE1 1 
ATOM   703  N  NE2 . GLN A 1 111 ? 34.618  -4.756  4.985   1.00 21.75  ? 90  GLN A NE2 1 
ATOM   704  N  N   . LEU A 1 112 ? 32.770  0.272   7.969   1.00 17.79  ? 91  LEU A N   1 
ATOM   705  C  CA  . LEU A 1 112 ? 32.193  1.592   7.735   1.00 21.12  ? 91  LEU A CA  1 
ATOM   706  C  C   . LEU A 1 112 ? 32.685  2.595   8.764   1.00 19.39  ? 91  LEU A C   1 
ATOM   707  O  O   . LEU A 1 112 ? 32.753  3.794   8.477   1.00 19.52  ? 91  LEU A O   1 
ATOM   708  C  CB  . LEU A 1 112 ? 30.664  1.533   7.758   1.00 19.30  ? 91  LEU A CB  1 
ATOM   709  C  CG  . LEU A 1 112 ? 29.967  2.864   7.437   1.00 21.48  ? 91  LEU A CG  1 
ATOM   710  C  CD1 . LEU A 1 112 ? 30.328  3.346   6.033   1.00 24.46  ? 91  LEU A CD1 1 
ATOM   711  C  CD2 . LEU A 1 112 ? 28.457  2.756   7.585   1.00 25.11  ? 91  LEU A CD2 1 
ATOM   712  N  N   . GLY A 1 113 ? 33.024  2.129   9.966   1.00 21.52  ? 92  GLY A N   1 
ATOM   713  C  CA  . GLY A 1 113 ? 33.555  3.034   10.966  1.00 21.15  ? 92  GLY A CA  1 
ATOM   714  C  C   . GLY A 1 113 ? 34.841  3.693   10.512  1.00 26.19  ? 92  GLY A C   1 
ATOM   715  O  O   . GLY A 1 113 ? 35.038  4.896   10.707  1.00 23.74  ? 92  GLY A O   1 
ATOM   716  N  N   . TRP A 1 114 ? 35.736  2.920   9.897   1.00 21.57  ? 93  TRP A N   1 
ATOM   717  C  CA  . TRP A 1 114 ? 36.965  3.524   9.403   1.00 24.03  ? 93  TRP A CA  1 
ATOM   718  C  C   . TRP A 1 114 ? 36.690  4.489   8.254   1.00 24.22  ? 93  TRP A C   1 
ATOM   719  O  O   . TRP A 1 114 ? 37.252  5.590   8.210   1.00 20.47  ? 93  TRP A O   1 
ATOM   720  C  CB  . TRP A 1 114 ? 37.961  2.470   8.937   1.00 22.87  ? 93  TRP A CB  1 
ATOM   721  C  CG  . TRP A 1 114 ? 39.023  3.153   8.173   1.00 21.59  ? 93  TRP A CG  1 
ATOM   722  C  CD1 . TRP A 1 114 ? 39.166  3.192   6.819   1.00 23.15  ? 93  TRP A CD1 1 
ATOM   723  C  CD2 . TRP A 1 114 ? 40.059  3.977   8.714   1.00 22.47  ? 93  TRP A CD2 1 
ATOM   724  N  NE1 . TRP A 1 114 ? 40.243  3.972   6.483   1.00 27.21  ? 93  TRP A NE1 1 
ATOM   725  C  CE2 . TRP A 1 114 ? 40.809  4.466   7.629   1.00 24.12  ? 93  TRP A CE2 1 
ATOM   726  C  CE3 . TRP A 1 114 ? 40.431  4.341   10.013  1.00 24.57  ? 93  TRP A CE3 1 
ATOM   727  C  CZ2 . TRP A 1 114 ? 41.917  5.295   7.801   1.00 26.55  ? 93  TRP A CZ2 1 
ATOM   728  C  CZ3 . TRP A 1 114 ? 41.533  5.163   10.183  1.00 24.01  ? 93  TRP A CZ3 1 
ATOM   729  C  CH2 . TRP A 1 114 ? 42.260  5.632   9.083   1.00 26.38  ? 93  TRP A CH2 1 
ATOM   730  N  N   . ALA A 1 115 ? 35.845  4.088   7.303   1.00 21.22  ? 94  ALA A N   1 
ATOM   731  C  CA  . ALA A 1 115 ? 35.594  4.942   6.147   1.00 21.89  ? 94  ALA A CA  1 
ATOM   732  C  C   . ALA A 1 115 ? 35.002  6.279   6.574   1.00 19.91  ? 94  ALA A C   1 
ATOM   733  O  O   . ALA A 1 115 ? 35.349  7.328   6.018   1.00 19.27  ? 94  ALA A O   1 
ATOM   734  C  CB  . ALA A 1 115 ? 34.670  4.232   5.158   1.00 17.91  ? 94  ALA A CB  1 
ATOM   735  N  N   . LEU A 1 116 ? 34.110  6.265   7.568   1.00 26.25  ? 95  LEU A N   1 
ATOM   736  C  CA  . LEU A 1 116 ? 33.470  7.501   7.997   1.00 21.63  ? 95  LEU A CA  1 
ATOM   737  C  C   . LEU A 1 116 ? 34.402  8.389   8.810   1.00 17.19  ? 95  LEU A C   1 
ATOM   738  O  O   . LEU A 1 116 ? 34.141  9.590   8.924   1.00 20.47  ? 95  LEU A O   1 
ATOM   739  C  CB  . LEU A 1 116 ? 32.210  7.190   8.798   1.00 23.41  ? 95  LEU A CB  1 
ATOM   740  C  CG  . LEU A 1 116 ? 31.043  6.601   8.001   1.00 23.21  ? 95  LEU A CG  1 
ATOM   741  C  CD1 . LEU A 1 116 ? 29.842  6.423   8.914   1.00 23.87  ? 95  LEU A CD1 1 
ATOM   742  C  CD2 . LEU A 1 116 ? 30.673  7.460   6.801   1.00 25.90  ? 95  LEU A CD2 1 
ATOM   743  N  N   . ASN A 1 117 ? 35.487  7.839   9.363   1.00 16.40  ? 96  ASN A N   1 
ATOM   744  C  CA  . ASN A 1 117 ? 36.508  8.692   9.962   1.00 17.12  ? 96  ASN A CA  1 
ATOM   745  C  C   . ASN A 1 117 ? 36.988  9.741   8.969   1.00 20.70  ? 96  ASN A C   1 
ATOM   746  O  O   . ASN A 1 117 ? 37.178  10.909  9.326   1.00 18.40  ? 96  ASN A O   1 
ATOM   747  C  CB  . ASN A 1 117 ? 37.698  7.858   10.434  1.00 21.65  ? 96  ASN A CB  1 
ATOM   748  C  CG  . ASN A 1 117 ? 37.531  7.343   11.844  1.00 25.96  ? 96  ASN A CG  1 
ATOM   749  O  OD1 . ASN A 1 117 ? 36.810  7.924   12.650  1.00 27.03  ? 96  ASN A OD1 1 
ATOM   750  N  ND2 . ASN A 1 117 ? 38.219  6.254   12.154  1.00 24.66  ? 96  ASN A ND2 1 
ATOM   751  N  N   . CYS A 1 118 ? 37.186  9.335   7.713   1.00 17.57  ? 97  CYS A N   1 
ATOM   752  C  CA  . CYS A 1 118 ? 37.704  10.213  6.672   1.00 20.42  ? 97  CYS A CA  1 
ATOM   753  C  C   . CYS A 1 118 ? 36.707  11.277  6.239   1.00 19.35  ? 97  CYS A C   1 
ATOM   754  O  O   . CYS A 1 118 ? 37.079  12.166  5.467   1.00 24.02  ? 97  CYS A O   1 
ATOM   755  C  CB  . CYS A 1 118 ? 38.113  9.379   5.459   1.00 18.95  ? 97  CYS A CB  1 
ATOM   756  S  SG  . CYS A 1 118 ? 39.301  8.086   5.841   1.00 24.24  ? 97  CYS A SG  1 
ATOM   757  N  N   . TYR A 1 119 ? 35.457  11.195  6.691   1.00 20.15  ? 98  TYR A N   1 
ATOM   758  C  CA  . TYR A 1 119 ? 34.439  12.197  6.397   1.00 17.62  ? 98  TYR A CA  1 
ATOM   759  C  C   . TYR A 1 119 ? 33.937  12.881  7.664   1.00 20.60  ? 98  TYR A C   1 
ATOM   760  O  O   . TYR A 1 119 ? 32.850  13.466  7.667   1.00 22.20  ? 98  TYR A O   1 
ATOM   761  C  CB  . TYR A 1 119 ? 33.288  11.550  5.629   1.00 20.50  ? 98  TYR A CB  1 
ATOM   762  C  CG  . TYR A 1 119 ? 33.747  10.962  4.317   1.00 25.96  ? 98  TYR A CG  1 
ATOM   763  C  CD1 . TYR A 1 119 ? 34.226  9.662   4.248   1.00 19.05  ? 98  TYR A CD1 1 
ATOM   764  C  CD2 . TYR A 1 119 ? 33.735  11.721  3.151   1.00 26.18  ? 98  TYR A CD2 1 
ATOM   765  C  CE1 . TYR A 1 119 ? 34.661  9.126   3.052   1.00 22.71  ? 98  TYR A CE1 1 
ATOM   766  C  CE2 . TYR A 1 119 ? 34.168  11.190  1.949   1.00 23.45  ? 98  TYR A CE2 1 
ATOM   767  C  CZ  . TYR A 1 119 ? 34.629  9.894   1.908   1.00 21.31  ? 98  TYR A CZ  1 
ATOM   768  O  OH  . TYR A 1 119 ? 35.064  9.358   0.725   1.00 24.91  ? 98  TYR A OH  1 
ATOM   769  N  N   . THR A 1 120 ? 34.714  12.806  8.741   1.00 24.25  ? 99  THR A N   1 
ATOM   770  C  CA  . THR A 1 120 ? 34.404  13.423  10.022  1.00 17.60  ? 99  THR A CA  1 
ATOM   771  C  C   . THR A 1 120 ? 35.555  14.344  10.392  1.00 17.41  ? 99  THR A C   1 
ATOM   772  O  O   . THR A 1 120 ? 36.722  13.972  10.249  1.00 21.23  ? 99  THR A O   1 
ATOM   773  C  CB  . THR A 1 120 ? 34.215  12.368  11.119  1.00 18.73  ? 99  THR A CB  1 
ATOM   774  O  OG1 . THR A 1 120 ? 33.273  11.381  10.685  1.00 23.78  ? 99  THR A OG1 1 
ATOM   775  C  CG2 . THR A 1 120 ? 33.708  13.006  12.404  1.00 19.57  ? 99  THR A CG2 1 
ATOM   776  N  N   . TYR A 1 121 ? 35.236  15.547  10.853  1.00 20.03  ? 100 TYR A N   1 
ATOM   777  C  CA  . TYR A 1 121 ? 36.274  16.486  11.253  1.00 23.03  ? 100 TYR A CA  1 
ATOM   778  C  C   . TYR A 1 121 ? 36.776  16.172  12.656  1.00 18.89  ? 100 TYR A C   1 
ATOM   779  O  O   . TYR A 1 121 ? 35.997  15.848  13.554  1.00 21.68  ? 100 TYR A O   1 
ATOM   780  C  CB  . TYR A 1 121 ? 35.751  17.919  11.207  1.00 22.16  ? 100 TYR A CB  1 
ATOM   781  C  CG  . TYR A 1 121 ? 35.617  18.486  9.819   1.00 24.19  ? 100 TYR A CG  1 
ATOM   782  C  CD1 . TYR A 1 121 ? 36.735  18.906  9.111   1.00 27.52  ? 100 TYR A CD1 1 
ATOM   783  C  CD2 . TYR A 1 121 ? 34.372  18.615  9.221   1.00 22.65  ? 100 TYR A CD2 1 
ATOM   784  C  CE1 . TYR A 1 121 ? 36.615  19.431  7.839   1.00 31.16  ? 100 TYR A CE1 1 
ATOM   785  C  CE2 . TYR A 1 121 ? 34.241  19.139  7.954   1.00 25.48  ? 100 TYR A CE2 1 
ATOM   786  C  CZ  . TYR A 1 121 ? 35.364  19.544  7.268   1.00 28.48  ? 100 TYR A CZ  1 
ATOM   787  O  OH  . TYR A 1 121 ? 35.229  20.066  6.008   1.00 34.11  ? 100 TYR A OH  1 
ATOM   788  N  N   . PHE A 1 122 ? 38.095  16.285  12.834  1.00 23.30  ? 101 PHE A N   1 
ATOM   789  C  CA  . PHE A 1 122 ? 38.695  16.139  14.154  1.00 24.82  ? 101 PHE A CA  1 
ATOM   790  C  C   . PHE A 1 122 ? 37.994  17.028  15.169  1.00 26.41  ? 101 PHE A C   1 
ATOM   791  O  O   . PHE A 1 122 ? 37.726  16.604  16.297  1.00 25.21  ? 101 PHE A O   1 
ATOM   792  C  CB  . PHE A 1 122 ? 40.186  16.484  14.080  1.00 26.20  ? 101 PHE A CB  1 
ATOM   793  C  CG  . PHE A 1 122 ? 40.891  16.440  15.408  1.00 33.95  ? 101 PHE A CG  1 
ATOM   794  C  CD1 . PHE A 1 122 ? 40.876  17.537  16.257  1.00 36.19  ? 101 PHE A CD1 1 
ATOM   795  C  CD2 . PHE A 1 122 ? 41.580  15.305  15.803  1.00 33.09  ? 101 PHE A CD2 1 
ATOM   796  C  CE1 . PHE A 1 122 ? 41.525  17.496  17.479  1.00 35.64  ? 101 PHE A CE1 1 
ATOM   797  C  CE2 . PHE A 1 122 ? 42.232  15.261  17.023  1.00 29.90  ? 101 PHE A CE2 1 
ATOM   798  C  CZ  . PHE A 1 122 ? 42.204  16.354  17.861  1.00 31.58  ? 101 PHE A CZ  1 
ATOM   799  N  N   . GLY A 1 123 ? 37.686  18.266  14.782  1.00 24.04  ? 102 GLY A N   1 
ATOM   800  C  CA  . GLY A 1 123 ? 37.046  19.184  15.706  1.00 28.39  ? 102 GLY A CA  1 
ATOM   801  C  C   . GLY A 1 123 ? 35.646  18.761  16.095  1.00 26.62  ? 102 GLY A C   1 
ATOM   802  O  O   . GLY A 1 123 ? 35.169  19.112  17.177  1.00 23.09  ? 102 GLY A O   1 
ATOM   803  N  N   . GLU A 1 124 ? 34.962  18.012  15.225  1.00 23.56  ? 103 GLU A N   1 
ATOM   804  C  CA  . GLU A 1 124 ? 33.635  17.517  15.579  1.00 25.47  ? 103 GLU A CA  1 
ATOM   805  C  C   . GLU A 1 124 ? 33.721  16.501  16.710  1.00 30.18  ? 103 GLU A C   1 
ATOM   806  O  O   . GLU A 1 124 ? 32.847  16.463  17.584  1.00 26.18  ? 103 GLU A O   1 
ATOM   807  C  CB  . GLU A 1 124 ? 32.947  16.915  14.351  1.00 25.47  ? 103 GLU A CB  1 
ATOM   808  C  CG  . GLU A 1 124 ? 32.568  17.965  13.303  1.00 31.34  ? 103 GLU A CG  1 
ATOM   809  C  CD  . GLU A 1 124 ? 31.940  17.375  12.044  1.00 28.54  ? 103 GLU A CD  1 
ATOM   810  O  OE1 . GLU A 1 124 ? 32.463  16.371  11.515  1.00 24.77  ? 103 GLU A OE1 1 
ATOM   811  O  OE2 . GLU A 1 124 ? 30.915  17.921  11.582  1.00 26.25  ? 103 GLU A OE2 1 
ATOM   812  N  N   . LEU A 1 125 ? 34.773  15.678  16.716  1.00 21.83  ? 104 LEU A N   1 
ATOM   813  C  CA  . LEU A 1 125 ? 34.997  14.749  17.815  1.00 21.14  ? 104 LEU A CA  1 
ATOM   814  C  C   . LEU A 1 125 ? 35.554  15.447  19.048  1.00 28.90  ? 104 LEU A C   1 
ATOM   815  O  O   . LEU A 1 125 ? 35.247  15.042  20.175  1.00 27.80  ? 104 LEU A O   1 
ATOM   816  C  CB  . LEU A 1 125 ? 35.949  13.638  17.377  1.00 21.44  ? 104 LEU A CB  1 
ATOM   817  C  CG  . LEU A 1 125 ? 35.452  12.775  16.217  1.00 21.74  ? 104 LEU A CG  1 
ATOM   818  C  CD1 . LEU A 1 125 ? 36.518  11.780  15.780  1.00 20.07  ? 104 LEU A CD1 1 
ATOM   819  C  CD2 . LEU A 1 125 ? 34.169  12.054  16.607  1.00 22.79  ? 104 LEU A CD2 1 
ATOM   820  N  N   . SER A 1 126 ? 36.373  16.484  18.858  1.00 27.46  ? 105 SER A N   1 
ATOM   821  C  CA  . SER A 1 126 ? 36.915  17.215  19.998  1.00 30.69  ? 105 SER A CA  1 
ATOM   822  C  C   . SER A 1 126 ? 35.807  17.899  20.788  1.00 35.98  ? 105 SER A C   1 
ATOM   823  O  O   . SER A 1 126 ? 35.842  17.934  22.024  1.00 30.89  ? 105 SER A O   1 
ATOM   824  C  CB  . SER A 1 126 ? 37.944  18.237  19.519  1.00 33.27  ? 105 SER A CB  1 
ATOM   825  O  OG  . SER A 1 126 ? 38.471  18.969  20.608  1.00 43.95  ? 105 SER A OG  1 
ATOM   826  N  N   . ARG A 1 127 ? 34.813  18.451  20.093  1.00 34.21  ? 106 ARG A N   1 
ATOM   827  C  CA  . ARG A 1 127 ? 33.697  19.094  20.770  1.00 35.19  ? 106 ARG A CA  1 
ATOM   828  C  C   . ARG A 1 127 ? 32.749  18.095  21.416  1.00 32.35  ? 106 ARG A C   1 
ATOM   829  O  O   . ARG A 1 127 ? 31.850  18.510  22.153  1.00 38.21  ? 106 ARG A O   1 
ATOM   830  C  CB  . ARG A 1 127 ? 32.935  19.983  19.789  1.00 36.16  ? 106 ARG A CB  1 
ATOM   831  C  CG  . ARG A 1 127 ? 33.710  21.221  19.369  1.00 34.01  ? 106 ARG A CG  1 
ATOM   832  C  CD  . ARG A 1 127 ? 32.836  22.188  18.593  1.00 41.52  ? 106 ARG A CD  1 
ATOM   833  N  NE  . ARG A 1 127 ? 32.367  21.618  17.336  1.00 36.49  ? 106 ARG A NE  1 
ATOM   834  C  CZ  . ARG A 1 127 ? 33.040  21.657  16.193  1.00 34.53  ? 106 ARG A CZ  1 
ATOM   835  N  NH1 . ARG A 1 127 ? 34.233  22.225  16.110  1.00 30.96  ? 106 ARG A NH1 1 
ATOM   836  N  NH2 . ARG A 1 127 ? 32.501  21.111  15.107  1.00 26.30  ? 106 ARG A NH2 1 
ATOM   837  N  N   . MET A 1 128 ? 32.917  16.801  21.163  1.00 36.22  ? 107 MET A N   1 
ATOM   838  C  CA  . MET A 1 128 ? 32.150  15.785  21.879  1.00 42.39  ? 107 MET A CA  1 
ATOM   839  C  C   . MET A 1 128 ? 32.637  15.757  23.322  1.00 45.11  ? 107 MET A C   1 
ATOM   840  O  O   . MET A 1 128 ? 33.703  15.212  23.620  1.00 49.87  ? 107 MET A O   1 
ATOM   841  C  CB  . MET A 1 128 ? 32.311  14.422  21.220  1.00 45.99  ? 107 MET A CB  1 
ATOM   842  C  CG  . MET A 1 128 ? 31.821  14.355  19.786  1.00 36.99  ? 107 MET A CG  1 
ATOM   843  S  SD  . MET A 1 128 ? 30.073  14.767  19.595  1.00 56.31  ? 107 MET A SD  1 
ATOM   844  C  CE  . MET A 1 128 ? 29.316  13.617  20.734  1.00 39.60  ? 107 MET A CE  1 
ATOM   845  N  N   . THR A 1 129 ? 31.857  16.355  24.227  1.00 56.27  ? 108 THR A N   1 
ATOM   846  C  CA  . THR A 1 129 ? 32.257  16.416  25.630  1.00 54.77  ? 108 THR A CA  1 
ATOM   847  C  C   . THR A 1 129 ? 32.395  15.019  26.224  1.00 62.33  ? 108 THR A C   1 
ATOM   848  O  O   . THR A 1 129 ? 33.414  14.694  26.843  1.00 68.89  ? 108 THR A O   1 
ATOM   849  C  CB  . THR A 1 129 ? 31.244  17.236  26.432  1.00 57.53  ? 108 THR A CB  1 
ATOM   850  O  OG1 . THR A 1 129 ? 29.933  16.680  26.264  1.00 52.26  ? 108 THR A OG1 1 
ATOM   851  C  CG2 . THR A 1 129 ? 31.249  18.689  25.973  1.00 53.52  ? 108 THR A CG2 1 
ATOM   852  N  N   . GLN A 1 130 ? 31.377  14.180  26.045  1.00 72.22  ? 109 GLN A N   1 
ATOM   853  C  CA  . GLN A 1 130 ? 31.419  12.804  26.529  1.00 72.13  ? 109 GLN A CA  1 
ATOM   854  C  C   . GLN A 1 130 ? 31.354  11.824  25.363  1.00 69.02  ? 109 GLN A C   1 
ATOM   855  O  O   . GLN A 1 130 ? 32.378  11.469  24.782  1.00 68.91  ? 109 GLN A O   1 
ATOM   856  C  CB  . GLN A 1 130 ? 30.272  12.534  27.504  1.00 73.88  ? 109 GLN A CB  1 
ATOM   857  C  CG  . GLN A 1 130 ? 30.333  11.157  28.150  1.00 80.93  ? 109 GLN A CG  1 
ATOM   858  C  CD  . GLN A 1 130 ? 29.464  11.048  29.390  1.00 90.65  ? 109 GLN A CD  1 
ATOM   859  O  OE1 . GLN A 1 130 ? 29.955  10.758  30.482  1.00 88.32  ? 109 GLN A OE1 1 
ATOM   860  N  NE2 . GLN A 1 130 ? 28.166  11.275  29.225  1.00 91.90  ? 109 GLN A NE2 1 
ATOM   861  N  N   . ALA A 1 139 ? 39.474  12.679  33.036  1.00 59.50  ? 118 ALA A N   1 
ATOM   862  C  CA  . ALA A 1 139 ? 39.486  11.788  31.882  1.00 75.18  ? 118 ALA A CA  1 
ATOM   863  C  C   . ALA A 1 139 ? 40.759  10.943  31.854  1.00 64.48  ? 118 ALA A C   1 
ATOM   864  O  O   . ALA A 1 139 ? 40.719  9.765   31.503  1.00 82.42  ? 118 ALA A O   1 
ATOM   865  C  CB  . ALA A 1 139 ? 39.355  12.589  30.595  1.00 66.22  ? 118 ALA A CB  1 
ATOM   866  N  N   . GLU A 1 140 ? 41.884  11.561  32.224  1.00 69.56  ? 119 GLU A N   1 
ATOM   867  C  CA  . GLU A 1 140 ? 43.188  10.903  32.265  1.00 66.96  ? 119 GLU A CA  1 
ATOM   868  C  C   . GLU A 1 140 ? 43.731  10.690  30.853  1.00 60.23  ? 119 GLU A C   1 
ATOM   869  O  O   . GLU A 1 140 ? 43.319  11.379  29.914  1.00 62.37  ? 119 GLU A O   1 
ATOM   870  C  CB  . GLU A 1 140 ? 43.109  9.569   33.020  1.00 67.71  ? 119 GLU A CB  1 
ATOM   871  C  CG  . GLU A 1 140 ? 42.558  9.682   34.439  1.00 73.92  ? 119 GLU A CG  1 
ATOM   872  C  CD  . GLU A 1 140 ? 41.087  9.321   34.528  1.00 72.27  ? 119 GLU A CD  1 
ATOM   873  O  OE1 . GLU A 1 140 ? 40.736  8.166   34.206  1.00 68.02  ? 119 GLU A OE1 1 
ATOM   874  O  OE2 . GLU A 1 140 ? 40.281  10.194  34.913  1.00 76.57  ? 119 GLU A OE2 1 
ATOM   875  N  N   . ASN A 1 141 ? 44.663  9.749   30.697  1.00 62.00  ? 120 ASN A N   1 
ATOM   876  C  CA  . ASN A 1 141 ? 45.275  9.439   29.403  1.00 56.70  ? 120 ASN A CA  1 
ATOM   877  C  C   . ASN A 1 141 ? 44.254  8.661   28.578  1.00 54.52  ? 120 ASN A C   1 
ATOM   878  O  O   . ASN A 1 141 ? 44.235  7.427   28.550  1.00 57.71  ? 120 ASN A O   1 
ATOM   879  C  CB  . ASN A 1 141 ? 46.567  8.656   29.586  1.00 57.37  ? 120 ASN A CB  1 
ATOM   880  N  N   . ILE A 1 142 ? 43.383  9.416   27.907  1.00 40.88  ? 121 ILE A N   1 
ATOM   881  C  CA  . ILE A 1 142 ? 42.332  8.832   27.084  1.00 38.57  ? 121 ILE A CA  1 
ATOM   882  C  C   . ILE A 1 142 ? 42.941  7.963   25.985  1.00 38.20  ? 121 ILE A C   1 
ATOM   883  O  O   . ILE A 1 142 ? 44.055  8.212   25.507  1.00 35.21  ? 121 ILE A O   1 
ATOM   884  C  CB  . ILE A 1 142 ? 41.452  9.950   26.490  1.00 33.30  ? 121 ILE A CB  1 
ATOM   885  C  CG1 . ILE A 1 142 ? 40.499  9.394   25.427  1.00 44.34  ? 121 ILE A CG1 1 
ATOM   886  C  CG2 . ILE A 1 142 ? 42.309  11.065  25.886  1.00 46.63  ? 121 ILE A CG2 1 
ATOM   887  C  CD1 . ILE A 1 142 ? 39.534  10.422  24.820  1.00 32.22  ? 121 ILE A CD1 1 
ATOM   888  N  N   . ASN A 1 143 ? 42.205  6.925   25.587  1.00 30.61  ? 122 ASN A N   1 
ATOM   889  C  CA  . ASN A 1 143 ? 42.570  6.104   24.440  1.00 29.70  ? 122 ASN A CA  1 
ATOM   890  C  C   . ASN A 1 143 ? 41.778  6.532   23.209  1.00 26.19  ? 122 ASN A C   1 
ATOM   891  O  O   . ASN A 1 143 ? 40.723  7.164   23.304  1.00 30.91  ? 122 ASN A O   1 
ATOM   892  C  CB  . ASN A 1 143 ? 42.345  4.612   24.720  1.00 26.25  ? 122 ASN A CB  1 
ATOM   893  C  CG  . ASN A 1 143 ? 40.881  4.254   24.902  1.00 25.71  ? 122 ASN A CG  1 
ATOM   894  O  OD1 . ASN A 1 143 ? 40.097  4.269   23.953  1.00 22.45  ? 122 ASN A OD1 1 
ATOM   895  N  ND2 . ASN A 1 143 ? 40.514  3.899   26.124  1.00 31.35  ? 122 ASN A ND2 1 
ATOM   896  N  N   . ALA A 1 144 ? 42.301  6.162   22.038  1.00 26.96  ? 123 ALA A N   1 
ATOM   897  C  CA  . ALA A 1 144 ? 41.759  6.678   20.785  1.00 27.22  ? 123 ALA A CA  1 
ATOM   898  C  C   . ALA A 1 144 ? 40.331  6.217   20.543  1.00 27.50  ? 123 ALA A C   1 
ATOM   899  O  O   . ALA A 1 144 ? 39.572  6.905   19.852  1.00 22.42  ? 123 ALA A O   1 
ATOM   900  C  CB  . ALA A 1 144 ? 42.646  6.255   19.616  1.00 23.82  ? 123 ALA A CB  1 
ATOM   901  N  N   . GLY A 1 145 ? 39.953  5.052   21.072  1.00 19.77  ? 124 GLY A N   1 
ATOM   902  C  CA  . GLY A 1 145 ? 38.588  4.586   20.894  1.00 20.38  ? 124 GLY A CA  1 
ATOM   903  C  C   . GLY A 1 145 ? 37.583  5.467   21.609  1.00 25.20  ? 124 GLY A C   1 
ATOM   904  O  O   . GLY A 1 145 ? 36.498  5.740   21.088  1.00 21.29  ? 124 GLY A O   1 
ATOM   905  N  N   . LEU A 1 146 ? 37.928  5.918   22.818  1.00 24.64  ? 125 LEU A N   1 
ATOM   906  C  CA  . LEU A 1 146 ? 37.054  6.826   23.550  1.00 30.26  ? 125 LEU A CA  1 
ATOM   907  C  C   . LEU A 1 146 ? 36.837  8.116   22.775  1.00 28.33  ? 125 LEU A C   1 
ATOM   908  O  O   . LEU A 1 146 ? 35.750  8.702   22.825  1.00 27.37  ? 125 LEU A O   1 
ATOM   909  C  CB  . LEU A 1 146 ? 37.661  7.116   24.922  1.00 28.26  ? 125 LEU A CB  1 
ATOM   910  C  CG  . LEU A 1 146 ? 36.749  7.609   26.041  1.00 36.85  ? 125 LEU A CG  1 
ATOM   911  C  CD1 . LEU A 1 146 ? 35.612  6.638   26.287  1.00 31.22  ? 125 LEU A CD1 1 
ATOM   912  C  CD2 . LEU A 1 146 ? 37.562  7.812   27.316  1.00 33.51  ? 125 LEU A CD2 1 
ATOM   913  N  N   . PHE A 1 147 ? 37.862  8.568   22.053  1.00 25.29  ? 126 PHE A N   1 
ATOM   914  C  CA  . PHE A 1 147 ? 37.738  9.766   21.228  1.00 24.60  ? 126 PHE A CA  1 
ATOM   915  C  C   . PHE A 1 147 ? 36.925  9.493   19.969  1.00 24.60  ? 126 PHE A C   1 
ATOM   916  O  O   . PHE A 1 147 ? 36.105  10.324  19.561  1.00 25.77  ? 126 PHE A O   1 
ATOM   917  C  CB  . PHE A 1 147 ? 39.139  10.277  20.876  1.00 25.08  ? 126 PHE A CB  1 
ATOM   918  C  CG  . PHE A 1 147 ? 39.151  11.537  20.053  1.00 26.99  ? 126 PHE A CG  1 
ATOM   919  C  CD1 . PHE A 1 147 ? 38.751  12.747  20.599  1.00 26.24  ? 126 PHE A CD1 1 
ATOM   920  C  CD2 . PHE A 1 147 ? 39.595  11.517  18.742  1.00 26.24  ? 126 PHE A CD2 1 
ATOM   921  C  CE1 . PHE A 1 147 ? 38.774  13.906  19.843  1.00 29.14  ? 126 PHE A CE1 1 
ATOM   922  C  CE2 . PHE A 1 147 ? 39.623  12.674  17.982  1.00 27.08  ? 126 PHE A CE2 1 
ATOM   923  C  CZ  . PHE A 1 147 ? 39.213  13.868  18.534  1.00 30.00  ? 126 PHE A CZ  1 
ATOM   924  N  N   . ASP A 1 148 ? 37.112  8.326   19.356  1.00 23.67  ? 127 ASP A N   1 
ATOM   925  C  CA  . ASP A 1 148 ? 36.608  8.060   18.017  1.00 25.06  ? 127 ASP A CA  1 
ATOM   926  C  C   . ASP A 1 148 ? 35.277  7.321   17.994  1.00 28.47  ? 127 ASP A C   1 
ATOM   927  O  O   . ASP A 1 148 ? 34.721  7.126   16.910  1.00 21.25  ? 127 ASP A O   1 
ATOM   928  C  CB  . ASP A 1 148 ? 37.651  7.258   17.230  1.00 27.69  ? 127 ASP A CB  1 
ATOM   929  C  CG  . ASP A 1 148 ? 37.400  7.276   15.732  1.00 30.82  ? 127 ASP A CG  1 
ATOM   930  O  OD1 . ASP A 1 148 ? 37.176  8.376   15.179  1.00 25.33  ? 127 ASP A OD1 1 
ATOM   931  O  OD2 . ASP A 1 148 ? 37.443  6.193   15.108  1.00 26.91  ? 127 ASP A OD2 1 
ATOM   932  N  N   . TYR A 1 149 ? 34.734  6.927   19.151  1.00 25.04  ? 128 TYR A N   1 
ATOM   933  C  CA  . TYR A 1 149 ? 33.569  6.046   19.143  1.00 18.97  ? 128 TYR A CA  1 
ATOM   934  C  C   . TYR A 1 149 ? 32.326  6.712   18.552  1.00 15.59  ? 128 TYR A C   1 
ATOM   935  O  O   . TYR A 1 149 ? 31.443  6.001   18.061  1.00 18.07  ? 128 TYR A O   1 
ATOM   936  C  CB  . TYR A 1 149 ? 33.272  5.513   20.558  1.00 23.27  ? 128 TYR A CB  1 
ATOM   937  C  CG  . TYR A 1 149 ? 32.543  6.469   21.484  1.00 19.88  ? 128 TYR A CG  1 
ATOM   938  C  CD1 . TYR A 1 149 ? 31.164  6.623   21.415  1.00 24.23  ? 128 TYR A CD1 1 
ATOM   939  C  CD2 . TYR A 1 149 ? 33.235  7.205   22.438  1.00 25.93  ? 128 TYR A CD2 1 
ATOM   940  C  CE1 . TYR A 1 149 ? 30.497  7.499   22.260  1.00 26.39  ? 128 TYR A CE1 1 
ATOM   941  C  CE2 . TYR A 1 149 ? 32.576  8.084   23.284  1.00 26.58  ? 128 TYR A CE2 1 
ATOM   942  C  CZ  . TYR A 1 149 ? 31.209  8.223   23.193  1.00 30.09  ? 128 TYR A CZ  1 
ATOM   943  O  OH  . TYR A 1 149 ? 30.553  9.091   24.037  1.00 35.97  ? 128 TYR A OH  1 
ATOM   944  N  N   . PRO A 1 150 ? 32.185  8.043   18.582  1.00 19.44  ? 129 PRO A N   1 
ATOM   945  C  CA  . PRO A 1 150 ? 31.037  8.643   17.878  1.00 20.19  ? 129 PRO A CA  1 
ATOM   946  C  C   . PRO A 1 150 ? 31.014  8.340   16.388  1.00 22.34  ? 129 PRO A C   1 
ATOM   947  O  O   . PRO A 1 150 ? 29.930  8.321   15.790  1.00 18.76  ? 129 PRO A O   1 
ATOM   948  C  CB  . PRO A 1 150 ? 31.205  10.145  18.149  1.00 23.15  ? 129 PRO A CB  1 
ATOM   949  C  CG  . PRO A 1 150 ? 31.941  10.204  19.435  1.00 23.12  ? 129 PRO A CG  1 
ATOM   950  C  CD  . PRO A 1 150 ? 32.904  9.050   19.385  1.00 20.00  ? 129 PRO A CD  1 
ATOM   951  N  N   . VAL A 1 151 ? 32.178  8.127   15.763  1.00 15.06  ? 130 VAL A N   1 
ATOM   952  C  CA  . VAL A 1 151 ? 32.198  7.732   14.356  1.00 19.17  ? 130 VAL A CA  1 
ATOM   953  C  C   . VAL A 1 151 ? 31.657  6.318   14.199  1.00 15.46  ? 130 VAL A C   1 
ATOM   954  O  O   . VAL A 1 151 ? 30.848  6.046   13.308  1.00 19.94  ? 130 VAL A O   1 
ATOM   955  C  CB  . VAL A 1 151 ? 33.618  7.856   13.776  1.00 18.26  ? 130 VAL A CB  1 
ATOM   956  C  CG1 . VAL A 1 151 ? 33.662  7.369   12.318  1.00 20.10  ? 130 VAL A CG1 1 
ATOM   957  C  CG2 . VAL A 1 151 ? 34.101  9.292   13.850  1.00 25.07  ? 130 VAL A CG2 1 
ATOM   958  N  N   . LEU A 1 152 ? 32.083  5.399   15.065  1.00 20.96  ? 131 LEU A N   1 
ATOM   959  C  CA  . LEU A 1 152 ? 31.566  4.037   14.998  1.00 19.19  ? 131 LEU A CA  1 
ATOM   960  C  C   . LEU A 1 152 ? 30.063  4.009   15.252  1.00 19.36  ? 131 LEU A C   1 
ATOM   961  O  O   . LEU A 1 152 ? 29.342  3.218   14.636  1.00 24.08  ? 131 LEU A O   1 
ATOM   962  C  CB  . LEU A 1 152 ? 32.311  3.149   15.992  1.00 22.10  ? 131 LEU A CB  1 
ATOM   963  C  CG  . LEU A 1 152 ? 31.959  1.658   15.977  1.00 23.67  ? 131 LEU A CG  1 
ATOM   964  C  CD1 . LEU A 1 152 ? 32.326  1.015   14.647  1.00 24.72  ? 131 LEU A CD1 1 
ATOM   965  C  CD2 . LEU A 1 152 ? 32.654  0.950   17.121  1.00 19.10  ? 131 LEU A CD2 1 
ATOM   966  N  N   . MET A 1 153 ? 29.566  4.875   16.143  1.00 21.97  ? 132 MET A N   1 
ATOM   967  C  CA  . MET A 1 153 ? 28.122  4.971   16.353  1.00 26.44  ? 132 MET A CA  1 
ATOM   968  C  C   . MET A 1 153 ? 27.407  5.389   15.076  1.00 21.16  ? 132 MET A C   1 
ATOM   969  O  O   . MET A 1 153 ? 26.334  4.865   14.753  1.00 21.43  ? 132 MET A O   1 
ATOM   970  C  CB  . MET A 1 153 ? 27.800  5.980   17.457  1.00 25.33  ? 132 MET A CB  1 
ATOM   971  C  CG  . MET A 1 153 ? 28.115  5.539   18.871  1.00 33.17  ? 132 MET A CG  1 
ATOM   972  S  SD  . MET A 1 153 ? 27.561  6.758   20.097  1.00 39.79  ? 132 MET A SD  1 
ATOM   973  C  CE  . MET A 1 153 ? 25.794  6.831   19.777  1.00 28.19  ? 132 MET A CE  1 
ATOM   974  N  N   . ALA A 1 154 ? 27.962  6.365   14.359  1.00 23.36  ? 133 ALA A N   1 
ATOM   975  C  CA  . ALA A 1 154 ? 27.367  6.762   13.090  1.00 23.74  ? 133 ALA A CA  1 
ATOM   976  C  C   . ALA A 1 154 ? 27.360  5.594   12.115  1.00 21.49  ? 133 ALA A C   1 
ATOM   977  O  O   . ALA A 1 154 ? 26.369  5.361   11.415  1.00 20.68  ? 133 ALA A O   1 
ATOM   978  C  CB  . ALA A 1 154 ? 28.122  7.953   12.505  1.00 22.01  ? 133 ALA A CB  1 
ATOM   979  N  N   . ALA A 1 155 ? 28.451  4.829   12.079  1.00 19.07  ? 134 ALA A N   1 
ATOM   980  C  CA  . ALA A 1 155 ? 28.500  3.655   11.216  1.00 22.68  ? 134 ALA A CA  1 
ATOM   981  C  C   . ALA A 1 155 ? 27.419  2.649   11.590  1.00 25.55  ? 134 ALA A C   1 
ATOM   982  O  O   . ALA A 1 155 ? 26.741  2.107   10.710  1.00 23.49  ? 134 ALA A O   1 
ATOM   983  C  CB  . ALA A 1 155 ? 29.882  3.009   11.294  1.00 21.82  ? 134 ALA A CB  1 
ATOM   984  N  N   . ASP A 1 156 ? 27.233  2.393   12.893  1.00 23.93  ? 135 ASP A N   1 
ATOM   985  C  CA  . ASP A 1 156 ? 26.227  1.419   13.313  1.00 26.26  ? 135 ASP A CA  1 
ATOM   986  C  C   . ASP A 1 156 ? 24.850  1.809   12.796  1.00 23.43  ? 135 ASP A C   1 
ATOM   987  O  O   . ASP A 1 156 ? 24.080  0.959   12.338  1.00 23.84  ? 135 ASP A O   1 
ATOM   988  C  CB  . ASP A 1 156 ? 26.166  1.304   14.841  1.00 23.62  ? 135 ASP A CB  1 
ATOM   989  C  CG  . ASP A 1 156 ? 27.522  1.083   15.488  1.00 29.23  ? 135 ASP A CG  1 
ATOM   990  O  OD1 . ASP A 1 156 ? 28.433  0.512   14.859  1.00 31.63  ? 135 ASP A OD1 1 
ATOM   991  O  OD2 . ASP A 1 156 ? 27.670  1.481   16.660  1.00 28.82  ? 135 ASP A OD2 1 
ATOM   992  N  N   . ILE A 1 157 ? 24.519  3.096   12.890  1.00 24.88  ? 136 ILE A N   1 
ATOM   993  C  CA  . ILE A 1 157 ? 23.201  3.568   12.486  1.00 24.12  ? 136 ILE A CA  1 
ATOM   994  C  C   . ILE A 1 157 ? 23.046  3.511   10.969  1.00 21.43  ? 136 ILE A C   1 
ATOM   995  O  O   . ILE A 1 157 ? 22.037  3.018   10.451  1.00 23.66  ? 136 ILE A O   1 
ATOM   996  C  CB  . ILE A 1 157 ? 22.974  4.992   13.026  1.00 23.66  ? 136 ILE A CB  1 
ATOM   997  C  CG1 . ILE A 1 157 ? 22.946  4.965   14.560  1.00 26.10  ? 136 ILE A CG1 1 
ATOM   998  C  CG2 . ILE A 1 157 ? 21.695  5.579   12.453  1.00 22.96  ? 136 ILE A CG2 1 
ATOM   999  C  CD1 . ILE A 1 157 ? 23.066  6.333   15.209  1.00 30.72  ? 136 ILE A CD1 1 
ATOM   1000 N  N   . LEU A 1 158 ? 24.045  4.004   10.235  1.00 21.95  ? 137 LEU A N   1 
ATOM   1001 C  CA  . LEU A 1 158 ? 23.886  4.225   8.801   1.00 26.51  ? 137 LEU A CA  1 
ATOM   1002 C  C   . LEU A 1 158 ? 23.945  2.943   7.981   1.00 22.92  ? 137 LEU A C   1 
ATOM   1003 O  O   . LEU A 1 158 ? 23.410  2.915   6.868   1.00 25.79  ? 137 LEU A O   1 
ATOM   1004 C  CB  . LEU A 1 158 ? 24.957  5.202   8.303   1.00 23.57  ? 137 LEU A CB  1 
ATOM   1005 C  CG  . LEU A 1 158 ? 24.915  6.598   8.928   1.00 24.62  ? 137 LEU A CG  1 
ATOM   1006 C  CD1 . LEU A 1 158 ? 26.017  7.474   8.353   1.00 24.62  ? 137 LEU A CD1 1 
ATOM   1007 C  CD2 . LEU A 1 158 ? 23.554  7.247   8.726   1.00 26.50  ? 137 LEU A CD2 1 
ATOM   1008 N  N   . LEU A 1 159 ? 24.569  1.884   8.501   1.00 20.84  ? 138 LEU A N   1 
ATOM   1009 C  CA  . LEU A 1 159 ? 24.644  0.632   7.757   1.00 25.65  ? 138 LEU A CA  1 
ATOM   1010 C  C   . LEU A 1 159 ? 23.265  0.118   7.365   1.00 22.63  ? 138 LEU A C   1 
ATOM   1011 O  O   . LEU A 1 159 ? 23.118  -0.517  6.316   1.00 25.38  ? 138 LEU A O   1 
ATOM   1012 C  CB  . LEU A 1 159 ? 25.357  -0.438  8.585   1.00 25.70  ? 138 LEU A CB  1 
ATOM   1013 C  CG  . LEU A 1 159 ? 26.880  -0.426  8.679   1.00 21.21  ? 138 LEU A CG  1 
ATOM   1014 C  CD1 . LEU A 1 159 ? 27.318  -1.473  9.693   1.00 24.34  ? 138 LEU A CD1 1 
ATOM   1015 C  CD2 . LEU A 1 159 ? 27.519  -0.688  7.325   1.00 25.93  ? 138 LEU A CD2 1 
ATOM   1016 N  N   . TYR A 1 160 ? 22.249  0.364   8.192   1.00 22.68  ? 139 TYR A N   1 
ATOM   1017 C  CA  . TYR A 1 160 ? 20.954  -0.286  8.034   1.00 28.19  ? 139 TYR A CA  1 
ATOM   1018 C  C   . TYR A 1 160 ? 19.896  0.647   7.470   1.00 27.90  ? 139 TYR A C   1 
ATOM   1019 O  O   . TYR A 1 160 ? 18.699  0.384   7.622   1.00 29.85  ? 139 TYR A O   1 
ATOM   1020 C  CB  . TYR A 1 160 ? 20.508  -0.873  9.374   1.00 27.49  ? 139 TYR A CB  1 
ATOM   1021 C  CG  . TYR A 1 160 ? 21.528  -1.853  9.888   1.00 24.53  ? 139 TYR A CG  1 
ATOM   1022 C  CD1 . TYR A 1 160 ? 21.626  -3.123  9.340   1.00 26.39  ? 139 TYR A CD1 1 
ATOM   1023 C  CD2 . TYR A 1 160 ? 22.426  -1.494  10.880  1.00 21.72  ? 139 TYR A CD2 1 
ATOM   1024 C  CE1 . TYR A 1 160 ? 22.572  -4.019  9.784   1.00 21.53  ? 139 TYR A CE1 1 
ATOM   1025 C  CE2 . TYR A 1 160 ? 23.378  -2.385  11.330  1.00 26.64  ? 139 TYR A CE2 1 
ATOM   1026 C  CZ  . TYR A 1 160 ? 23.443  -3.647  10.778  1.00 22.51  ? 139 TYR A CZ  1 
ATOM   1027 O  OH  . TYR A 1 160 ? 24.386  -4.543  11.213  1.00 28.19  ? 139 TYR A OH  1 
ATOM   1028 N  N   . GLN A 1 161 ? 20.311  1.719   6.798   1.00 27.05  ? 140 GLN A N   1 
ATOM   1029 C  CA  . GLN A 1 161 ? 19.368  2.654   6.196   1.00 28.65  ? 140 GLN A CA  1 
ATOM   1030 C  C   . GLN A 1 161 ? 18.370  3.130   7.243   1.00 28.56  ? 140 GLN A C   1 
ATOM   1031 O  O   . GLN A 1 161 ? 17.171  3.254   6.987   1.00 27.86  ? 140 GLN A O   1 
ATOM   1032 C  CB  . GLN A 1 161 ? 18.663  2.010   5.004   1.00 33.37  ? 140 GLN A CB  1 
ATOM   1033 C  CG  . GLN A 1 161 ? 19.613  1.626   3.880   1.00 27.53  ? 140 GLN A CG  1 
ATOM   1034 C  CD  . GLN A 1 161 ? 20.244  2.840   3.218   1.00 36.44  ? 140 GLN A CD  1 
ATOM   1035 O  OE1 . GLN A 1 161 ? 19.545  3.776   2.829   1.00 33.45  ? 140 GLN A OE1 1 
ATOM   1036 N  NE2 . GLN A 1 161 ? 21.571  2.835   3.097   1.00 33.71  ? 140 GLN A NE2 1 
ATOM   1037 N  N   . THR A 1 162 ? 18.884  3.398   8.440   1.00 27.33  ? 141 THR A N   1 
ATOM   1038 C  CA  . THR A 1 162 ? 18.035  3.637   9.597   1.00 24.75  ? 141 THR A CA  1 
ATOM   1039 C  C   . THR A 1 162 ? 17.258  4.939   9.459   1.00 27.42  ? 141 THR A C   1 
ATOM   1040 O  O   . THR A 1 162 ? 17.799  5.969   9.045   1.00 26.54  ? 141 THR A O   1 
ATOM   1041 C  CB  . THR A 1 162 ? 18.883  3.670   10.866  1.00 24.16  ? 141 THR A CB  1 
ATOM   1042 O  OG1 . THR A 1 162 ? 19.552  2.412   11.027  1.00 26.67  ? 141 THR A OG1 1 
ATOM   1043 C  CG2 . THR A 1 162 ? 18.019  3.943   12.086  1.00 29.63  ? 141 THR A CG2 1 
ATOM   1044 N  N   . ASN A 1 163 ? 15.978  4.884   9.829   1.00 29.13  ? 142 ASN A N   1 
ATOM   1045 C  CA  . ASN A 1 163 ? 15.100  6.047   9.803   1.00 32.29  ? 142 ASN A CA  1 
ATOM   1046 C  C   . ASN A 1 163 ? 15.057  6.783   11.138  1.00 33.59  ? 142 ASN A C   1 
ATOM   1047 O  O   . ASN A 1 163 ? 14.970  8.015   11.158  1.00 31.26  ? 142 ASN A O   1 
ATOM   1048 C  CB  . ASN A 1 163 ? 13.681  5.623   9.413   1.00 32.47  ? 142 ASN A CB  1 
ATOM   1049 C  CG  . ASN A 1 163 ? 13.588  5.153   7.976   1.00 36.50  ? 142 ASN A CG  1 
ATOM   1050 O  OD1 . ASN A 1 163 ? 13.351  3.976   7.706   1.00 34.57  ? 142 ASN A OD1 1 
ATOM   1051 N  ND2 . ASN A 1 163 ? 13.778  6.075   7.042   1.00 41.55  ? 142 ASN A ND2 1 
ATOM   1052 N  N   . GLN A 1 164 ? 15.104  6.062   12.257  1.00 29.16  ? 143 GLN A N   1 
ATOM   1053 C  CA  . GLN A 1 164 ? 14.909  6.669   13.566  1.00 30.96  ? 143 GLN A CA  1 
ATOM   1054 C  C   . GLN A 1 164 ? 15.794  5.993   14.598  1.00 27.90  ? 143 GLN A C   1 
ATOM   1055 O  O   . GLN A 1 164 ? 15.938  4.768   14.598  1.00 27.97  ? 143 GLN A O   1 
ATOM   1056 C  CB  . GLN A 1 164 ? 13.438  6.580   13.989  1.00 37.04  ? 143 GLN A CB  1 
ATOM   1057 C  CG  . GLN A 1 164 ? 12.500  7.155   12.945  1.00 39.94  ? 143 GLN A CG  1 
ATOM   1058 C  CD  . GLN A 1 164 ? 11.047  7.094   13.340  1.00 54.17  ? 143 GLN A CD  1 
ATOM   1059 O  OE1 . GLN A 1 164 ? 10.711  6.844   14.496  1.00 58.06  ? 143 GLN A OE1 1 
ATOM   1060 N  NE2 . GLN A 1 164 ? 10.168  7.323   12.372  1.00 64.61  ? 143 GLN A NE2 1 
ATOM   1061 N  N   . VAL A 1 165 ? 16.382  6.801   15.475  1.00 25.48  ? 144 VAL A N   1 
ATOM   1062 C  CA  . VAL A 1 165 ? 17.252  6.308   16.538  1.00 32.10  ? 144 VAL A CA  1 
ATOM   1063 C  C   . VAL A 1 165 ? 16.729  6.838   17.869  1.00 35.23  ? 144 VAL A C   1 
ATOM   1064 O  O   . VAL A 1 165 ? 16.847  8.041   18.139  1.00 34.81  ? 144 VAL A O   1 
ATOM   1065 C  CB  . VAL A 1 165 ? 18.711  6.736   16.310  1.00 35.28  ? 144 VAL A CB  1 
ATOM   1066 C  CG1 . VAL A 1 165 ? 19.625  6.083   17.338  1.00 37.35  ? 144 VAL A CG1 1 
ATOM   1067 C  CG2 . VAL A 1 165 ? 19.160  6.387   14.896  1.00 37.89  ? 144 VAL A CG2 1 
ATOM   1068 N  N   . PRO A 1 166 ? 16.146  5.994   18.729  1.00 38.72  ? 145 PRO A N   1 
ATOM   1069 C  CA  . PRO A 1 166 ? 15.637  6.484   20.032  1.00 42.13  ? 145 PRO A CA  1 
ATOM   1070 C  C   . PRO A 1 166 ? 16.733  6.688   21.077  1.00 44.39  ? 145 PRO A C   1 
ATOM   1071 O  O   . PRO A 1 166 ? 16.987  5.862   21.954  1.00 54.16  ? 145 PRO A O   1 
ATOM   1072 C  CB  . PRO A 1 166 ? 14.660  5.380   20.453  1.00 43.74  ? 145 PRO A CB  1 
ATOM   1073 C  CG  . PRO A 1 166 ? 14.523  4.458   19.284  1.00 43.64  ? 145 PRO A CG  1 
ATOM   1074 C  CD  . PRO A 1 166 ? 15.771  4.592   18.493  1.00 39.67  ? 145 PRO A CD  1 
ATOM   1075 N  N   . VAL A 1 167 ? 17.406  7.831   20.995  1.00 44.42  ? 146 VAL A N   1 
ATOM   1076 C  CA  . VAL A 1 167 ? 18.473  8.155   21.930  1.00 52.83  ? 146 VAL A CA  1 
ATOM   1077 C  C   . VAL A 1 167 ? 17.896  8.907   23.123  1.00 45.83  ? 146 VAL A C   1 
ATOM   1078 O  O   . VAL A 1 167 ? 16.812  9.493   23.062  1.00 48.01  ? 146 VAL A O   1 
ATOM   1079 C  CB  . VAL A 1 167 ? 19.596  8.983   21.267  1.00 51.27  ? 146 VAL A CB  1 
ATOM   1080 C  CG1 . VAL A 1 167 ? 20.360  8.141   20.262  1.00 49.91  ? 146 VAL A CG1 1 
ATOM   1081 C  CG2 . VAL A 1 167 ? 19.026  10.242  20.611  1.00 42.57  ? 146 VAL A CG2 1 
ATOM   1082 N  N   . GLY A 1 168 ? 18.637  8.886   24.227  1.00 60.58  ? 147 GLY A N   1 
ATOM   1083 C  CA  . GLY A 1 168 ? 18.346  9.749   25.347  1.00 66.37  ? 147 GLY A CA  1 
ATOM   1084 C  C   . GLY A 1 168 ? 18.899  11.142  25.124  1.00 63.65  ? 147 GLY A C   1 
ATOM   1085 O  O   . GLY A 1 168 ? 19.562  11.435  24.128  1.00 58.69  ? 147 GLY A O   1 
ATOM   1086 N  N   . GLU A 1 169 ? 18.617  12.022  26.087  1.00 61.01  ? 148 GLU A N   1 
ATOM   1087 C  CA  . GLU A 1 169 ? 19.071  13.403  25.967  1.00 57.06  ? 148 GLU A CA  1 
ATOM   1088 C  C   . GLU A 1 169 ? 20.591  13.490  25.933  1.00 54.40  ? 148 GLU A C   1 
ATOM   1089 O  O   . GLU A 1 169 ? 21.147  14.383  25.283  1.00 53.99  ? 148 GLU A O   1 
ATOM   1090 C  CB  . GLU A 1 169 ? 18.528  14.240  27.125  1.00 63.05  ? 148 GLU A CB  1 
ATOM   1091 C  CG  . GLU A 1 169 ? 18.138  15.658  26.736  1.00 70.79  ? 148 GLU A CG  1 
ATOM   1092 C  CD  . GLU A 1 169 ? 16.760  15.731  26.103  1.00 76.36  ? 148 GLU A CD  1 
ATOM   1093 O  OE1 . GLU A 1 169 ? 16.484  16.719  25.391  1.00 84.19  ? 148 GLU A OE1 1 
ATOM   1094 O  OE2 . GLU A 1 169 ? 15.954  14.802  26.319  1.00 79.12  ? 148 GLU A OE2 1 
ATOM   1095 N  N   . ASP A 1 170 ? 21.277  12.577  26.621  1.00 47.90  ? 149 ASP A N   1 
ATOM   1096 C  CA  . ASP A 1 170 ? 22.730  12.621  26.724  1.00 52.82  ? 149 ASP A CA  1 
ATOM   1097 C  C   . ASP A 1 170 ? 23.437  12.003  25.525  1.00 45.15  ? 149 ASP A C   1 
ATOM   1098 O  O   . ASP A 1 170 ? 24.672  12.017  25.487  1.00 45.74  ? 149 ASP A O   1 
ATOM   1099 C  CB  . ASP A 1 170 ? 23.198  11.930  28.011  1.00 53.35  ? 149 ASP A CB  1 
ATOM   1100 C  CG  . ASP A 1 170 ? 22.666  10.512  28.154  1.00 61.79  ? 149 ASP A CG  1 
ATOM   1101 O  OD1 . ASP A 1 170 ? 21.896  10.055  27.283  1.00 63.23  ? 149 ASP A OD1 1 
ATOM   1102 O  OD2 . ASP A 1 170 ? 23.023  9.851   29.154  1.00 78.70  ? 149 ASP A OD2 1 
ATOM   1103 N  N   . GLN A 1 171 ? 22.699  11.460  24.557  1.00 39.85  ? 150 GLN A N   1 
ATOM   1104 C  CA  . GLN A 1 171 ? 23.271  11.038  23.282  1.00 49.04  ? 150 GLN A CA  1 
ATOM   1105 C  C   . GLN A 1 171 ? 22.704  11.845  22.120  1.00 39.89  ? 150 GLN A C   1 
ATOM   1106 O  O   . GLN A 1 171 ? 22.834  11.439  20.960  1.00 29.99  ? 150 GLN A O   1 
ATOM   1107 C  CB  . GLN A 1 171 ? 23.048  9.541   23.056  1.00 42.37  ? 150 GLN A CB  1 
ATOM   1108 C  CG  . GLN A 1 171 ? 24.167  8.678   23.619  1.00 46.93  ? 150 GLN A CG  1 
ATOM   1109 C  CD  . GLN A 1 171 ? 23.873  7.197   23.520  1.00 51.48  ? 150 GLN A CD  1 
ATOM   1110 O  OE1 . GLN A 1 171 ? 22.750  6.794   23.217  1.00 59.67  ? 150 GLN A OE1 1 
ATOM   1111 N  NE2 . GLN A 1 171 ? 24.883  6.375   23.779  1.00 50.71  ? 150 GLN A NE2 1 
ATOM   1112 N  N   . LYS A 1 172 ? 22.077  12.987  22.419  1.00 41.22  ? 151 LYS A N   1 
ATOM   1113 C  CA  . LYS A 1 172 ? 21.552  13.855  21.371  1.00 37.03  ? 151 LYS A CA  1 
ATOM   1114 C  C   . LYS A 1 172 ? 22.665  14.342  20.452  1.00 37.84  ? 151 LYS A C   1 
ATOM   1115 O  O   . LYS A 1 172 ? 22.515  14.331  19.224  1.00 31.92  ? 151 LYS A O   1 
ATOM   1116 C  CB  . LYS A 1 172 ? 20.816  15.032  22.013  1.00 39.52  ? 151 LYS A CB  1 
ATOM   1117 C  CG  . LYS A 1 172 ? 20.453  16.169  21.076  1.00 43.23  ? 151 LYS A CG  1 
ATOM   1118 C  CD  . LYS A 1 172 ? 19.633  17.222  21.811  1.00 52.66  ? 151 LYS A CD  1 
ATOM   1119 C  CE  . LYS A 1 172 ? 19.800  18.607  21.200  1.00 67.53  ? 151 LYS A CE  1 
ATOM   1120 N  NZ  . LYS A 1 172 ? 19.126  19.658  22.021  1.00 62.16  ? 151 LYS A NZ  1 
ATOM   1121 N  N   . GLN A 1 173 ? 23.798  14.753  21.029  1.00 36.45  ? 152 GLN A N   1 
ATOM   1122 C  CA  . GLN A 1 173 ? 24.917  15.210  20.214  1.00 35.13  ? 152 GLN A CA  1 
ATOM   1123 C  C   . GLN A 1 173 ? 25.404  14.107  19.286  1.00 33.77  ? 152 GLN A C   1 
ATOM   1124 O  O   . GLN A 1 173 ? 25.714  14.360  18.115  1.00 25.16  ? 152 GLN A O   1 
ATOM   1125 C  CB  . GLN A 1 173 ? 26.066  15.687  21.103  1.00 37.70  ? 152 GLN A CB  1 
ATOM   1126 C  CG  . GLN A 1 173 ? 25.819  17.007  21.816  1.00 52.51  ? 152 GLN A CG  1 
ATOM   1127 C  CD  . GLN A 1 173 ? 27.066  17.533  22.511  1.00 56.09  ? 152 GLN A CD  1 
ATOM   1128 O  OE1 . GLN A 1 173 ? 27.868  16.766  23.047  1.00 55.59  ? 152 GLN A OE1 1 
ATOM   1129 N  NE2 . GLN A 1 173 ? 27.240  18.849  22.490  1.00 60.62  ? 152 GLN A NE2 1 
ATOM   1130 N  N   . HIS A 1 174 ? 25.489  12.876  19.796  1.00 28.90  ? 153 HIS A N   1 
ATOM   1131 C  CA  . HIS A 1 174 ? 25.986  11.773  18.983  1.00 25.36  ? 153 HIS A CA  1 
ATOM   1132 C  C   . HIS A 1 174 ? 25.085  11.529  17.779  1.00 26.53  ? 153 HIS A C   1 
ATOM   1133 O  O   . HIS A 1 174 ? 25.573  11.321  16.661  1.00 20.41  ? 153 HIS A O   1 
ATOM   1134 C  CB  . HIS A 1 174 ? 26.105  10.508  19.836  1.00 28.77  ? 153 HIS A CB  1 
ATOM   1135 C  CG  . HIS A 1 174 ? 27.045  10.645  20.995  1.00 31.41  ? 153 HIS A CG  1 
ATOM   1136 N  ND1 . HIS A 1 174 ? 26.695  11.278  22.168  1.00 34.62  ? 153 HIS A ND1 1 
ATOM   1137 C  CD2 . HIS A 1 174 ? 28.326  10.236  21.156  1.00 35.60  ? 153 HIS A CD2 1 
ATOM   1138 C  CE1 . HIS A 1 174 ? 27.719  11.250  23.004  1.00 34.49  ? 153 HIS A CE1 1 
ATOM   1139 N  NE2 . HIS A 1 174 ? 28.720  10.623  22.415  1.00 31.50  ? 153 HIS A NE2 1 
ATOM   1140 N  N   . LEU A 1 175 ? 23.766  11.552  17.983  1.00 26.65  ? 154 LEU A N   1 
ATOM   1141 C  CA  . LEU A 1 175 ? 22.851  11.382  16.861  1.00 20.31  ? 154 LEU A CA  1 
ATOM   1142 C  C   . LEU A 1 175 ? 23.004  12.520  15.863  1.00 24.13  ? 154 LEU A C   1 
ATOM   1143 O  O   . LEU A 1 175 ? 22.963  12.303  14.647  1.00 23.54  ? 154 LEU A O   1 
ATOM   1144 C  CB  . LEU A 1 175 ? 21.408  11.298  17.361  1.00 24.44  ? 154 LEU A CB  1 
ATOM   1145 C  CG  . LEU A 1 175 ? 20.337  11.250  16.266  1.00 31.51  ? 154 LEU A CG  1 
ATOM   1146 C  CD1 . LEU A 1 175 ? 20.597  10.073  15.329  1.00 31.25  ? 154 LEU A CD1 1 
ATOM   1147 C  CD2 . LEU A 1 175 ? 18.928  11.175  16.852  1.00 34.52  ? 154 LEU A CD2 1 
ATOM   1148 N  N   . GLU A 1 176 ? 23.186  13.743  16.358  1.00 25.69  ? 155 GLU A N   1 
ATOM   1149 C  CA  . GLU A 1 176 ? 23.290  14.884  15.457  1.00 29.67  ? 155 GLU A CA  1 
ATOM   1150 C  C   . GLU A 1 176 ? 24.553  14.798  14.611  1.00 29.83  ? 155 GLU A C   1 
ATOM   1151 O  O   . GLU A 1 176 ? 24.547  15.193  13.439  1.00 27.41  ? 155 GLU A O   1 
ATOM   1152 C  CB  . GLU A 1 176 ? 23.248  16.182  16.263  1.00 31.50  ? 155 GLU A CB  1 
ATOM   1153 C  CG  . GLU A 1 176 ? 22.956  17.441  15.449  1.00 50.72  ? 155 GLU A CG  1 
ATOM   1154 C  CD  . GLU A 1 176 ? 22.111  17.170  14.216  1.00 51.99  ? 155 GLU A CD  1 
ATOM   1155 O  OE1 . GLU A 1 176 ? 22.643  17.314  13.091  1.00 37.44  ? 155 GLU A OE1 1 
ATOM   1156 O  OE2 . GLU A 1 176 ? 20.928  16.786  14.377  1.00 43.97  ? 155 GLU A OE2 1 
ATOM   1157 N  N   . LEU A 1 177 ? 25.645  14.283  15.182  1.00 25.04  ? 156 LEU A N   1 
ATOM   1158 C  CA  . LEU A 1 177 ? 26.854  14.062  14.396  1.00 27.78  ? 156 LEU A CA  1 
ATOM   1159 C  C   . LEU A 1 177 ? 26.623  13.006  13.322  1.00 30.29  ? 156 LEU A C   1 
ATOM   1160 O  O   . LEU A 1 177 ? 27.090  13.153  12.187  1.00 25.34  ? 156 LEU A O   1 
ATOM   1161 C  CB  . LEU A 1 177 ? 28.014  13.654  15.305  1.00 31.58  ? 156 LEU A CB  1 
ATOM   1162 C  CG  . LEU A 1 177 ? 29.311  13.251  14.593  1.00 35.73  ? 156 LEU A CG  1 
ATOM   1163 C  CD1 . LEU A 1 177 ? 29.876  14.412  13.786  1.00 30.34  ? 156 LEU A CD1 1 
ATOM   1164 C  CD2 . LEU A 1 177 ? 30.351  12.741  15.578  1.00 29.86  ? 156 LEU A CD2 1 
ATOM   1165 N  N   . SER A 1 178 ? 25.908  11.932  13.661  1.00 22.96  ? 157 SER A N   1 
ATOM   1166 C  CA  A SER A 1 178 ? 25.610  10.911  12.663  0.38 22.09  ? 157 SER A CA  1 
ATOM   1167 C  CA  B SER A 1 178 ? 25.605  10.910  12.666  0.62 21.86  ? 157 SER A CA  1 
ATOM   1168 C  C   . SER A 1 178 ? 24.802  11.496  11.512  1.00 23.75  ? 157 SER A C   1 
ATOM   1169 O  O   . SER A 1 178 ? 25.041  11.165  10.345  1.00 25.74  ? 157 SER A O   1 
ATOM   1170 C  CB  A SER A 1 178 ? 24.861  9.744   13.306  0.38 25.85  ? 157 SER A CB  1 
ATOM   1171 C  CB  B SER A 1 178 ? 24.844  9.755   13.319  0.62 29.73  ? 157 SER A CB  1 
ATOM   1172 O  OG  A SER A 1 178 ? 23.510  10.078  13.562  0.38 24.72  ? 157 SER A OG  1 
ATOM   1173 O  OG  B SER A 1 178 ? 25.613  9.153   14.345  0.62 25.40  ? 157 SER A OG  1 
ATOM   1174 N  N   . ARG A 1 179 ? 23.838  12.368  11.820  1.00 21.34  ? 158 ARG A N   1 
ATOM   1175 C  CA  . ARG A 1 179 ? 23.062  13.009  10.764  1.00 26.77  ? 158 ARG A CA  1 
ATOM   1176 C  C   . ARG A 1 179 ? 23.941  13.913  9.906   1.00 22.46  ? 158 ARG A C   1 
ATOM   1177 O  O   . ARG A 1 179 ? 23.806  13.933  8.678   1.00 24.04  ? 158 ARG A O   1 
ATOM   1178 C  CB  . ARG A 1 179 ? 21.900  13.799  11.371  1.00 27.35  ? 158 ARG A CB  1 
ATOM   1179 C  CG  . ARG A 1 179 ? 20.854  12.924  12.055  1.00 30.40  ? 158 ARG A CG  1 
ATOM   1180 C  CD  . ARG A 1 179 ? 19.699  13.732  12.638  1.00 33.90  ? 158 ARG A CD  1 
ATOM   1181 N  NE  . ARG A 1 179 ? 18.829  14.297  11.611  1.00 37.52  ? 158 ARG A NE  1 
ATOM   1182 C  CZ  . ARG A 1 179 ? 18.781  15.581  11.280  1.00 38.98  ? 158 ARG A CZ  1 
ATOM   1183 N  NH1 . ARG A 1 179 ? 19.522  16.485  11.900  1.00 37.12  ? 158 ARG A NH1 1 
ATOM   1184 N  NH2 . ARG A 1 179 ? 17.962  15.970  10.309  1.00 38.54  ? 158 ARG A NH2 1 
ATOM   1185 N  N   . ASP A 1 180 ? 24.850  14.664  10.534  1.00 24.54  ? 159 ASP A N   1 
ATOM   1186 C  CA  . ASP A 1 180 ? 25.728  15.553  9.781   1.00 29.61  ? 159 ASP A CA  1 
ATOM   1187 C  C   . ASP A 1 180 ? 26.640  14.770  8.843   1.00 31.45  ? 159 ASP A C   1 
ATOM   1188 O  O   . ASP A 1 180 ? 26.900  15.201  7.713   1.00 23.31  ? 159 ASP A O   1 
ATOM   1189 C  CB  . ASP A 1 180 ? 26.565  16.404  10.738  1.00 28.37  ? 159 ASP A CB  1 
ATOM   1190 C  CG  . ASP A 1 180 ? 25.790  17.570  11.327  1.00 32.57  ? 159 ASP A CG  1 
ATOM   1191 O  OD1 . ASP A 1 180 ? 24.621  17.792  10.935  1.00 26.99  ? 159 ASP A OD1 1 
ATOM   1192 O  OD2 . ASP A 1 180 ? 26.362  18.273  12.187  1.00 32.11  ? 159 ASP A OD2 1 
ATOM   1193 N  N   . VAL A 1 181 ? 27.158  13.630  9.302   1.00 26.52  ? 160 VAL A N   1 
ATOM   1194 C  CA  . VAL A 1 181 ? 28.074  12.855  8.472   1.00 27.00  ? 160 VAL A CA  1 
ATOM   1195 C  C   . VAL A 1 181 ? 27.328  12.227  7.304   1.00 26.25  ? 160 VAL A C   1 
ATOM   1196 O  O   . VAL A 1 181 ? 27.845  12.164  6.183   1.00 25.29  ? 160 VAL A O   1 
ATOM   1197 C  CB  . VAL A 1 181 ? 28.801  11.797  9.320   1.00 27.43  ? 160 VAL A CB  1 
ATOM   1198 C  CG1 . VAL A 1 181 ? 29.545  10.825  8.426   1.00 27.41  ? 160 VAL A CG1 1 
ATOM   1199 C  CG2 . VAL A 1 181 ? 29.760  12.465  10.285  1.00 25.56  ? 160 VAL A CG2 1 
ATOM   1200 N  N   . ALA A 1 182 ? 26.105  11.752  7.542   1.00 24.37  ? 161 ALA A N   1 
ATOM   1201 C  CA  . ALA A 1 182 ? 25.312  11.208  6.448   1.00 27.20  ? 161 ALA A CA  1 
ATOM   1202 C  C   . ALA A 1 182 ? 25.016  12.279  5.407   1.00 21.46  ? 161 ALA A C   1 
ATOM   1203 O  O   . ALA A 1 182 ? 25.126  12.030  4.201   1.00 20.00  ? 161 ALA A O   1 
ATOM   1204 C  CB  . ALA A 1 182 ? 24.014  10.611  6.987   1.00 23.49  ? 161 ALA A CB  1 
ATOM   1205 N  N   . GLN A 1 183 ? 24.645  13.480  5.856   1.00 20.30  ? 162 GLN A N   1 
ATOM   1206 C  CA  . GLN A 1 183 ? 24.381  14.574  4.929   1.00 23.79  ? 162 GLN A CA  1 
ATOM   1207 C  C   . GLN A 1 183 ? 25.633  14.943  4.144   1.00 22.70  ? 162 GLN A C   1 
ATOM   1208 O  O   . GLN A 1 183 ? 25.570  15.174  2.932   1.00 23.75  ? 162 GLN A O   1 
ATOM   1209 C  CB  . GLN A 1 183 ? 23.856  15.787  5.699   1.00 24.29  ? 162 GLN A CB  1 
ATOM   1210 C  CG  . GLN A 1 183 ? 22.510  15.569  6.378   1.00 30.55  ? 162 GLN A CG  1 
ATOM   1211 C  CD  . GLN A 1 183 ? 22.198  16.615  7.439   1.00 31.40  ? 162 GLN A CD  1 
ATOM   1212 O  OE1 . GLN A 1 183 ? 23.080  17.343  7.899   1.00 24.46  ? 162 GLN A OE1 1 
ATOM   1213 N  NE2 . GLN A 1 183 ? 20.933  16.690  7.833   1.00 33.24  ? 162 GLN A NE2 1 
ATOM   1214 N  N   . ARG A 1 184 ? 26.781  15.003  4.825   1.00 23.19  ? 163 ARG A N   1 
ATOM   1215 C  CA  . ARG A 1 184 ? 28.034  15.359  4.164   1.00 21.37  ? 163 ARG A CA  1 
ATOM   1216 C  C   . ARG A 1 184 ? 28.417  14.328  3.111   1.00 23.93  ? 163 ARG A C   1 
ATOM   1217 O  O   . ARG A 1 184 ? 28.823  14.685  1.998   1.00 20.55  ? 163 ARG A O   1 
ATOM   1218 C  CB  . ARG A 1 184 ? 29.142  15.495  5.212   1.00 19.24  ? 163 ARG A CB  1 
ATOM   1219 C  CG  . ARG A 1 184 ? 30.526  15.775  4.658   1.00 26.66  ? 163 ARG A CG  1 
ATOM   1220 C  CD  . ARG A 1 184 ? 31.563  15.896  5.772   1.00 20.85  ? 163 ARG A CD  1 
ATOM   1221 N  NE  . ARG A 1 184 ? 31.317  17.045  6.639   1.00 18.69  ? 163 ARG A NE  1 
ATOM   1222 C  CZ  . ARG A 1 184 ? 31.233  17.002  7.964   1.00 22.76  ? 163 ARG A CZ  1 
ATOM   1223 N  NH1 . ARG A 1 184 ? 31.387  15.873  8.637   1.00 20.82  ? 163 ARG A NH1 1 
ATOM   1224 N  NH2 . ARG A 1 184 ? 31.010  18.128  8.634   1.00 20.96  ? 163 ARG A NH2 1 
ATOM   1225 N  N   . PHE A 1 185 ? 28.304  13.043  3.448   1.00 21.22  ? 164 PHE A N   1 
ATOM   1226 C  CA  . PHE A 1 185 ? 28.627  11.995  2.487   1.00 21.40  ? 164 PHE A CA  1 
ATOM   1227 C  C   . PHE A 1 185 ? 27.689  12.053  1.291   1.00 21.68  ? 164 PHE A C   1 
ATOM   1228 O  O   . PHE A 1 185 ? 28.132  11.985  0.138   1.00 24.61  ? 164 PHE A O   1 
ATOM   1229 C  CB  . PHE A 1 185 ? 28.552  10.628  3.170   1.00 21.44  ? 164 PHE A CB  1 
ATOM   1230 C  CG  . PHE A 1 185 ? 29.139  9.504   2.361   1.00 21.62  ? 164 PHE A CG  1 
ATOM   1231 C  CD1 . PHE A 1 185 ? 28.364  8.805   1.455   1.00 22.18  ? 164 PHE A CD1 1 
ATOM   1232 C  CD2 . PHE A 1 185 ? 30.465  9.139   2.523   1.00 21.84  ? 164 PHE A CD2 1 
ATOM   1233 C  CE1 . PHE A 1 185 ? 28.905  7.764   0.713   1.00 25.90  ? 164 PHE A CE1 1 
ATOM   1234 C  CE2 . PHE A 1 185 ? 31.010  8.106   1.791   1.00 20.77  ? 164 PHE A CE2 1 
ATOM   1235 C  CZ  . PHE A 1 185 ? 30.230  7.414   0.883   1.00 20.64  ? 164 PHE A CZ  1 
ATOM   1236 N  N   . ASN A 1 186 ? 26.391  12.211  1.547   1.00 22.97  ? 165 ASN A N   1 
ATOM   1237 C  CA  . ASN A 1 186 ? 25.428  12.262  0.456   1.00 22.10  ? 165 ASN A CA  1 
ATOM   1238 C  C   . ASN A 1 186 ? 25.649  13.476  -0.431  1.00 27.32  ? 165 ASN A C   1 
ATOM   1239 O  O   . ASN A 1 186 ? 25.407  13.410  -1.641  1.00 25.36  ? 165 ASN A O   1 
ATOM   1240 C  CB  . ASN A 1 186 ? 24.009  12.273  1.013   1.00 19.23  ? 165 ASN A CB  1 
ATOM   1241 C  CG  . ASN A 1 186 ? 23.583  10.927  1.523   1.00 23.87  ? 165 ASN A CG  1 
ATOM   1242 O  OD1 . ASN A 1 186 ? 24.354  9.969   1.503   1.00 21.16  ? 165 ASN A OD1 1 
ATOM   1243 N  ND2 . ASN A 1 186 ? 22.349  10.841  1.991   1.00 26.95  ? 165 ASN A ND2 1 
ATOM   1244 N  N   . ALA A 1 187 ? 26.094  14.592  0.147   1.00 19.80  ? 166 ALA A N   1 
ATOM   1245 C  CA  . ALA A 1 187 ? 26.342  15.781  -0.657  1.00 21.23  ? 166 ALA A CA  1 
ATOM   1246 C  C   . ALA A 1 187 ? 27.511  15.592  -1.615  1.00 25.79  ? 166 ALA A C   1 
ATOM   1247 O  O   . ALA A 1 187 ? 27.601  16.316  -2.611  1.00 26.58  ? 166 ALA A O   1 
ATOM   1248 C  CB  . ALA A 1 187 ? 26.602  16.983  0.250   1.00 20.73  ? 166 ALA A CB  1 
ATOM   1249 N  N   . ILE A 1 188 ? 28.405  14.648  -1.332  1.00 22.27  ? 167 ILE A N   1 
ATOM   1250 C  CA  . ILE A 1 188 ? 29.539  14.370  -2.206  1.00 29.67  ? 167 ILE A CA  1 
ATOM   1251 C  C   . ILE A 1 188 ? 29.183  13.329  -3.258  1.00 30.81  ? 167 ILE A C   1 
ATOM   1252 O  O   . ILE A 1 188 ? 29.478  13.499  -4.443  1.00 32.12  ? 167 ILE A O   1 
ATOM   1253 C  CB  . ILE A 1 188 ? 30.748  13.906  -1.363  1.00 28.27  ? 167 ILE A CB  1 
ATOM   1254 C  CG1 . ILE A 1 188 ? 31.171  14.988  -0.368  1.00 28.75  ? 167 ILE A CG1 1 
ATOM   1255 C  CG2 . ILE A 1 188 ? 31.910  13.518  -2.269  1.00 29.13  ? 167 ILE A CG2 1 
ATOM   1256 C  CD1 . ILE A 1 188 ? 32.121  14.484  0.707   1.00 28.00  ? 167 ILE A CD1 1 
ATOM   1257 N  N   . TYR A 1 189 ? 28.540  12.240  -2.836  1.00 23.36  ? 168 TYR A N   1 
ATOM   1258 C  CA  . TYR A 1 189 ? 28.407  11.042  -3.650  1.00 23.66  ? 168 TYR A CA  1 
ATOM   1259 C  C   . TYR A 1 189 ? 26.986  10.758  -4.107  1.00 26.49  ? 168 TYR A C   1 
ATOM   1260 O  O   . TYR A 1 189 ? 26.786  9.831   -4.901  1.00 28.80  ? 168 TYR A O   1 
ATOM   1261 C  CB  . TYR A 1 189 ? 28.931  9.827   -2.869  1.00 24.23  ? 168 TYR A CB  1 
ATOM   1262 C  CG  . TYR A 1 189 ? 30.397  9.926   -2.507  1.00 20.57  ? 168 TYR A CG  1 
ATOM   1263 C  CD1 . TYR A 1 189 ? 31.384  9.779   -3.474  1.00 18.24  ? 168 TYR A CD1 1 
ATOM   1264 C  CD2 . TYR A 1 189 ? 30.792  10.175  -1.204  1.00 21.30  ? 168 TYR A CD2 1 
ATOM   1265 C  CE1 . TYR A 1 189 ? 32.723  9.876   -3.147  1.00 21.75  ? 168 TYR A CE1 1 
ATOM   1266 C  CE2 . TYR A 1 189 ? 32.128  10.277  -0.868  1.00 22.14  ? 168 TYR A CE2 1 
ATOM   1267 C  CZ  . TYR A 1 189 ? 33.089  10.126  -1.844  1.00 20.62  ? 168 TYR A CZ  1 
ATOM   1268 O  OH  . TYR A 1 189 ? 34.422  10.221  -1.511  1.00 22.07  ? 168 TYR A OH  1 
ATOM   1269 N  N   . GLY A 1 190 ? 26.006  11.533  -3.660  1.00 25.16  ? 169 GLY A N   1 
ATOM   1270 C  CA  . GLY A 1 190 ? 24.610  11.203  -3.855  1.00 28.48  ? 169 GLY A CA  1 
ATOM   1271 C  C   . GLY A 1 190 ? 24.033  10.485  -2.648  1.00 28.16  ? 169 GLY A C   1 
ATOM   1272 O  O   . GLY A 1 190 ? 24.734  10.111  -1.706  1.00 31.79  ? 169 GLY A O   1 
ATOM   1273 N  N   . ASP A 1 191 ? 22.718  10.265  -2.698  1.00 30.22  ? 170 ASP A N   1 
ATOM   1274 C  CA  . ASP A 1 191 ? 21.973  9.747   -1.550  1.00 30.64  ? 170 ASP A CA  1 
ATOM   1275 C  C   . ASP A 1 191 ? 22.283  8.264   -1.354  1.00 31.59  ? 170 ASP A C   1 
ATOM   1276 O  O   . ASP A 1 191 ? 21.540  7.371   -1.767  1.00 38.11  ? 170 ASP A O   1 
ATOM   1277 C  CB  . ASP A 1 191 ? 20.478  9.981   -1.742  1.00 30.79  ? 170 ASP A CB  1 
ATOM   1278 C  CG  . ASP A 1 191 ? 20.102  11.448  -1.661  1.00 39.27  ? 170 ASP A CG  1 
ATOM   1279 O  OD1 . ASP A 1 191 ? 21.017  12.297  -1.579  1.00 41.05  ? 170 ASP A OD1 1 
ATOM   1280 O  OD2 . ASP A 1 191 ? 18.891  11.749  -1.673  1.00 49.47  ? 170 ASP A OD2 1 
ATOM   1281 N  N   . ILE A 1 192 ? 23.403  8.006   -0.686  1.00 29.46  ? 171 ILE A N   1 
ATOM   1282 C  CA  . ILE A 1 192 ? 23.798  6.646   -0.336  1.00 31.62  ? 171 ILE A CA  1 
ATOM   1283 C  C   . ILE A 1 192 ? 23.207  6.232   1.004   1.00 28.39  ? 171 ILE A C   1 
ATOM   1284 O  O   . ILE A 1 192 ? 22.776  5.090   1.176   1.00 29.28  ? 171 ILE A O   1 
ATOM   1285 C  CB  . ILE A 1 192 ? 25.337  6.543   -0.321  1.00 29.60  ? 171 ILE A CB  1 
ATOM   1286 C  CG1 . ILE A 1 192 ? 25.921  6.879   -1.697  1.00 32.12  ? 171 ILE A CG1 1 
ATOM   1287 C  CG2 . ILE A 1 192 ? 25.765  5.164   0.140   1.00 29.27  ? 171 ILE A CG2 1 
ATOM   1288 C  CD1 . ILE A 1 192 ? 25.476  5.953   -2.804  1.00 35.63  ? 171 ILE A CD1 1 
ATOM   1289 N  N   . PHE A 1 193 ? 23.190  7.148   1.963   1.00 25.24  ? 172 PHE A N   1 
ATOM   1290 C  CA  . PHE A 1 193 ? 22.668  6.890   3.293   1.00 25.37  ? 172 PHE A CA  1 
ATOM   1291 C  C   . PHE A 1 193 ? 21.265  7.462   3.441   1.00 26.20  ? 172 PHE A C   1 
ATOM   1292 O  O   . PHE A 1 193 ? 20.907  8.452   2.799   1.00 25.59  ? 172 PHE A O   1 
ATOM   1293 C  CB  . PHE A 1 193 ? 23.552  7.526   4.365   1.00 23.12  ? 172 PHE A CB  1 
ATOM   1294 C  CG  . PHE A 1 193 ? 24.946  6.988   4.419   1.00 23.56  ? 172 PHE A CG  1 
ATOM   1295 C  CD1 . PHE A 1 193 ? 25.180  5.644   4.632   1.00 22.90  ? 172 PHE A CD1 1 
ATOM   1296 C  CD2 . PHE A 1 193 ? 26.028  7.843   4.306   1.00 21.74  ? 172 PHE A CD2 1 
ATOM   1297 C  CE1 . PHE A 1 193 ? 26.466  5.158   4.705   1.00 22.55  ? 172 PHE A CE1 1 
ATOM   1298 C  CE2 . PHE A 1 193 ? 27.317  7.364   4.381   1.00 21.65  ? 172 PHE A CE2 1 
ATOM   1299 C  CZ  . PHE A 1 193 ? 27.538  6.019   4.583   1.00 21.83  ? 172 PHE A CZ  1 
ATOM   1300 N  N   . LYS A 1 194 ? 20.476  6.834   4.305   1.00 33.89  ? 173 LYS A N   1 
ATOM   1301 C  CA  . LYS A 1 194 ? 19.318  7.502   4.879   1.00 32.17  ? 173 LYS A CA  1 
ATOM   1302 C  C   . LYS A 1 194 ? 19.800  8.406   6.006   1.00 30.56  ? 173 LYS A C   1 
ATOM   1303 O  O   . LYS A 1 194 ? 20.622  7.995   6.829   1.00 30.16  ? 173 LYS A O   1 
ATOM   1304 C  CB  . LYS A 1 194 ? 18.306  6.490   5.410   1.00 32.16  ? 173 LYS A CB  1 
ATOM   1305 C  CG  . LYS A 1 194 ? 17.545  5.754   4.331   1.00 34.06  ? 173 LYS A CG  1 
ATOM   1306 C  CD  . LYS A 1 194 ? 16.044  5.968   4.457   1.00 41.80  ? 173 LYS A CD  1 
ATOM   1307 C  CE  . LYS A 1 194 ? 15.654  7.407   4.154   1.00 46.26  ? 173 LYS A CE  1 
ATOM   1308 N  NZ  . LYS A 1 194 ? 14.171  7.580   4.067   1.00 54.99  ? 173 LYS A NZ  1 
ATOM   1309 N  N   . VAL A 1 195 ? 19.314  9.640   6.030   1.00 26.28  ? 174 VAL A N   1 
ATOM   1310 C  CA  . VAL A 1 195 ? 19.627  10.541  7.135   1.00 26.23  ? 174 VAL A CA  1 
ATOM   1311 C  C   . VAL A 1 195 ? 18.679  10.188  8.274   1.00 27.65  ? 174 VAL A C   1 
ATOM   1312 O  O   . VAL A 1 195 ? 17.456  10.298  8.104   1.00 29.58  ? 174 VAL A O   1 
ATOM   1313 C  CB  . VAL A 1 195 ? 19.485  12.015  6.731   1.00 26.81  ? 174 VAL A CB  1 
ATOM   1314 C  CG1 . VAL A 1 195 ? 19.897  12.916  7.888   1.00 34.21  ? 174 VAL A CG1 1 
ATOM   1315 C  CG2 . VAL A 1 195 ? 20.310  12.319  5.490   1.00 27.22  ? 174 VAL A CG2 1 
ATOM   1316 N  N   . PRO A 1 196 ? 19.175  9.764   9.438   1.00 27.26  ? 175 PRO A N   1 
ATOM   1317 C  CA  . PRO A 1 196 ? 18.264  9.466   10.548  1.00 31.49  ? 175 PRO A CA  1 
ATOM   1318 C  C   . PRO A 1 196 ? 17.517  10.719  10.973  1.00 34.18  ? 175 PRO A C   1 
ATOM   1319 O  O   . PRO A 1 196 ? 17.974  11.844  10.762  1.00 35.74  ? 175 PRO A O   1 
ATOM   1320 C  CB  . PRO A 1 196 ? 19.193  8.961   11.659  1.00 32.79  ? 175 PRO A CB  1 
ATOM   1321 C  CG  . PRO A 1 196 ? 20.471  8.624   10.986  1.00 27.83  ? 175 PRO A CG  1 
ATOM   1322 C  CD  . PRO A 1 196 ? 20.580  9.543   9.815   1.00 29.80  ? 175 PRO A CD  1 
ATOM   1323 N  N   . GLU A 1 197 ? 16.347  10.516  11.560  1.00 40.37  ? 176 GLU A N   1 
ATOM   1324 C  CA  . GLU A 1 197 ? 15.517  11.647  11.933  1.00 42.59  ? 176 GLU A CA  1 
ATOM   1325 C  C   . GLU A 1 197 ? 16.117  12.378  13.134  1.00 49.95  ? 176 GLU A C   1 
ATOM   1326 O  O   . GLU A 1 197 ? 16.819  11.777  13.952  1.00 49.84  ? 176 GLU A O   1 
ATOM   1327 C  CB  . GLU A 1 197 ? 14.100  11.187  12.251  1.00 43.87  ? 176 GLU A CB  1 
ATOM   1328 C  CG  . GLU A 1 197 ? 13.138  11.369  11.088  1.00 47.43  ? 176 GLU A CG  1 
ATOM   1329 C  CD  . GLU A 1 197 ? 11.951  10.430  11.151  1.00 55.36  ? 176 GLU A CD  1 
ATOM   1330 O  OE1 . GLU A 1 197 ? 11.503  10.104  12.270  1.00 57.26  ? 176 GLU A OE1 1 
ATOM   1331 O  OE2 . GLU A 1 197 ? 11.472  10.009  10.076  1.00 60.76  ? 176 GLU A OE2 1 
ATOM   1332 N  N   . PRO A 1 198 ? 15.862  13.692  13.255  1.00 43.43  ? 177 PRO A N   1 
ATOM   1333 C  CA  . PRO A 1 198 ? 16.344  14.478  14.398  1.00 43.81  ? 177 PRO A CA  1 
ATOM   1334 C  C   . PRO A 1 198 ? 15.558  14.196  15.677  1.00 35.17  ? 177 PRO A C   1 
ATOM   1335 O  O   . PRO A 1 198 ? 15.842  13.203  16.347  1.00 46.66  ? 177 PRO A O   1 
ATOM   1336 C  CB  . PRO A 1 198 ? 16.141  15.925  13.937  1.00 42.85  ? 177 PRO A CB  1 
ATOM   1337 C  CG  . PRO A 1 198 ? 15.000  15.856  12.979  1.00 42.51  ? 177 PRO A CG  1 
ATOM   1338 C  CD  . PRO A 1 198 ? 15.125  14.523  12.283  1.00 39.52  ? 177 PRO A CD  1 
ATOM   1339 N  N   . ARG A 1 206 ? 8.238   7.476   33.894  1.00 81.08  ? 185 ARG A N   1 
ATOM   1340 C  CA  . ARG A 1 206 ? 9.362   8.259   34.393  1.00 85.76  ? 185 ARG A CA  1 
ATOM   1341 C  C   . ARG A 1 206 ? 9.641   7.931   35.854  1.00 77.70  ? 185 ARG A C   1 
ATOM   1342 O  O   . ARG A 1 206 ? 9.069   8.542   36.757  1.00 75.35  ? 185 ARG A O   1 
ATOM   1343 C  CB  . ARG A 1 206 ? 9.084   9.754   34.243  1.00 89.96  ? 185 ARG A CB  1 
ATOM   1344 C  CG  . ARG A 1 206 ? 10.288  10.638  34.537  1.00 90.35  ? 185 ARG A CG  1 
ATOM   1345 C  CD  . ARG A 1 206 ? 9.876   12.014  35.045  1.00 81.57  ? 185 ARG A CD  1 
ATOM   1346 N  NE  . ARG A 1 206 ? 9.284   11.957  36.378  1.00 89.50  ? 185 ARG A NE  1 
ATOM   1347 C  CZ  . ARG A 1 206 ? 7.981   11.953  36.635  1.00 93.30  ? 185 ARG A CZ  1 
ATOM   1348 N  NH1 . ARG A 1 206 ? 7.080   12.001  35.665  1.00 96.73  ? 185 ARG A NH1 1 
ATOM   1349 N  NH2 . ARG A 1 206 ? 7.571   11.903  37.899  1.00 84.07  ? 185 ARG A NH2 1 
ATOM   1350 N  N   . VAL A 1 207 ? 10.528  6.977   36.083  1.00 75.08  ? 186 VAL A N   1 
ATOM   1351 C  CA  . VAL A 1 207 ? 10.850  6.528   37.430  1.00 72.28  ? 186 VAL A CA  1 
ATOM   1352 C  C   . VAL A 1 207 ? 12.066  7.285   37.942  1.00 63.07  ? 186 VAL A C   1 
ATOM   1353 O  O   . VAL A 1 207 ? 13.021  7.541   37.200  1.00 72.94  ? 186 VAL A O   1 
ATOM   1354 C  CB  . VAL A 1 207 ? 11.090  5.009   37.462  1.00 67.71  ? 186 VAL A CB  1 
ATOM   1355 C  CG1 . VAL A 1 207 ? 11.800  4.630   38.753  1.00 66.14  ? 186 VAL A CG1 1 
ATOM   1356 C  CG2 . VAL A 1 207 ? 9.774   4.259   37.311  1.00 86.64  ? 186 VAL A CG2 1 
ATOM   1357 N  N   . MET A 1 208 ? 12.034  7.622   39.230  1.00 61.62  ? 187 MET A N   1 
ATOM   1358 C  CA  . MET A 1 208 ? 13.071  8.391   39.894  1.00 63.86  ? 187 MET A CA  1 
ATOM   1359 C  C   . MET A 1 208 ? 13.725  7.559   40.991  1.00 60.35  ? 187 MET A C   1 
ATOM   1360 O  O   . MET A 1 208 ? 13.203  6.525   41.418  1.00 58.04  ? 187 MET A O   1 
ATOM   1361 C  CB  . MET A 1 208 ? 12.493  9.676   40.503  1.00 60.19  ? 187 MET A CB  1 
ATOM   1362 C  CG  . MET A 1 208 ? 11.417  10.344  39.646  1.00 67.76  ? 187 MET A CG  1 
ATOM   1363 S  SD  . MET A 1 208 ? 12.002  10.962  38.052  1.00 67.49  ? 187 MET A SD  1 
ATOM   1364 C  CE  . MET A 1 208 ? 13.326  12.051  38.559  1.00 69.41  ? 187 MET A CE  1 
ATOM   1365 N  N   . SER A 1 209 ? 14.880  8.033   41.449  1.00 59.50  ? 188 SER A N   1 
ATOM   1366 C  CA  . SER A 1 209 ? 15.596  7.355   42.521  1.00 59.69  ? 188 SER A CA  1 
ATOM   1367 C  C   . SER A 1 209 ? 14.729  7.274   43.772  1.00 57.57  ? 188 SER A C   1 
ATOM   1368 O  O   . SER A 1 209 ? 14.044  8.233   44.140  1.00 51.11  ? 188 SER A O   1 
ATOM   1369 C  CB  . SER A 1 209 ? 16.901  8.092   42.828  1.00 56.33  ? 188 SER A CB  1 
ATOM   1370 O  OG  . SER A 1 209 ? 17.742  8.135   41.687  1.00 64.35  ? 188 SER A OG  1 
ATOM   1371 N  N   . LEU A 1 210 ? 14.769  6.114   44.432  1.00 51.25  ? 189 LEU A N   1 
ATOM   1372 C  CA  . LEU A 1 210 ? 13.900  5.892   45.583  1.00 55.54  ? 189 LEU A CA  1 
ATOM   1373 C  C   . LEU A 1 210 ? 14.228  6.848   46.725  1.00 55.29  ? 189 LEU A C   1 
ATOM   1374 O  O   . LEU A 1 210 ? 13.321  7.387   47.368  1.00 53.40  ? 189 LEU A O   1 
ATOM   1375 C  CB  . LEU A 1 210 ? 14.007  4.438   46.045  1.00 56.60  ? 189 LEU A CB  1 
ATOM   1376 C  CG  . LEU A 1 210 ? 13.692  3.375   44.985  1.00 64.47  ? 189 LEU A CG  1 
ATOM   1377 C  CD1 . LEU A 1 210 ? 13.641  1.988   45.619  1.00 63.16  ? 189 LEU A CD1 1 
ATOM   1378 C  CD2 . LEU A 1 210 ? 12.389  3.672   44.246  1.00 56.28  ? 189 LEU A CD2 1 
ATOM   1379 N  N   . LEU A 1 211 ? 15.513  7.070   46.998  1.00 55.14  ? 190 LEU A N   1 
ATOM   1380 C  CA  . LEU A 1 211 ? 15.929  7.966   48.069  1.00 54.26  ? 190 LEU A CA  1 
ATOM   1381 C  C   . LEU A 1 211 ? 16.229  9.380   47.584  1.00 58.68  ? 190 LEU A C   1 
ATOM   1382 O  O   . LEU A 1 211 ? 16.543  10.247  48.406  1.00 57.22  ? 190 LEU A O   1 
ATOM   1383 C  CB  . LEU A 1 211 ? 17.161  7.398   48.785  1.00 53.99  ? 190 LEU A CB  1 
ATOM   1384 C  CG  . LEU A 1 211 ? 17.002  6.006   49.403  1.00 54.20  ? 190 LEU A CG  1 
ATOM   1385 C  CD1 . LEU A 1 211 ? 18.345  5.462   49.873  1.00 52.32  ? 190 LEU A CD1 1 
ATOM   1386 C  CD2 . LEU A 1 211 ? 16.013  6.035   50.556  1.00 58.26  ? 190 LEU A CD2 1 
ATOM   1387 N  N   . GLU A 1 212 ? 16.137  9.637   46.280  1.00 52.29  ? 191 GLU A N   1 
ATOM   1388 C  CA  . GLU A 1 212 ? 16.378  10.965  45.710  1.00 58.05  ? 191 GLU A CA  1 
ATOM   1389 C  C   . GLU A 1 212 ? 15.425  11.163  44.539  1.00 61.16  ? 191 GLU A C   1 
ATOM   1390 O  O   . GLU A 1 212 ? 15.831  11.151  43.371  1.00 56.20  ? 191 GLU A O   1 
ATOM   1391 C  CB  . GLU A 1 212 ? 17.838  11.115  45.277  1.00 62.76  ? 191 GLU A CB  1 
ATOM   1392 C  CG  . GLU A 1 212 ? 18.777  11.557  46.391  1.00 68.34  ? 191 GLU A CG  1 
ATOM   1393 C  CD  . GLU A 1 212 ? 20.222  11.155  46.140  1.00 69.95  ? 191 GLU A CD  1 
ATOM   1394 O  OE1 . GLU A 1 212 ? 20.798  10.442  46.991  1.00 77.67  ? 191 GLU A OE1 1 
ATOM   1395 O  OE2 . GLU A 1 212 ? 20.779  11.542  45.091  1.00 74.13  ? 191 GLU A OE2 1 
ATOM   1396 N  N   . PRO A 1 213 ? 14.134  11.358  44.823  1.00 57.64  ? 192 PRO A N   1 
ATOM   1397 C  CA  . PRO A 1 213 ? 13.122  11.344  43.754  1.00 57.92  ? 192 PRO A CA  1 
ATOM   1398 C  C   . PRO A 1 213 ? 13.160  12.543  42.822  1.00 58.04  ? 192 PRO A C   1 
ATOM   1399 O  O   . PRO A 1 213 ? 12.295  12.640  41.944  1.00 63.17  ? 192 PRO A O   1 
ATOM   1400 C  CB  . PRO A 1 213 ? 11.797  11.298  44.533  1.00 62.72  ? 192 PRO A CB  1 
ATOM   1401 C  CG  . PRO A 1 213 ? 12.118  11.879  45.867  1.00 58.92  ? 192 PRO A CG  1 
ATOM   1402 C  CD  . PRO A 1 213 ? 13.531  11.478  46.161  1.00 52.91  ? 192 PRO A CD  1 
ATOM   1403 N  N   . THR A 1 214 ? 14.110  13.463  42.975  1.00 60.20  ? 193 THR A N   1 
ATOM   1404 C  CA  . THR A 1 214 ? 14.277  14.559  42.031  1.00 62.11  ? 193 THR A CA  1 
ATOM   1405 C  C   . THR A 1 214 ? 15.321  14.262  40.962  1.00 65.70  ? 193 THR A C   1 
ATOM   1406 O  O   . THR A 1 214 ? 15.537  15.097  40.078  1.00 68.23  ? 193 THR A O   1 
ATOM   1407 C  CB  . THR A 1 214 ? 14.648  15.851  42.770  1.00 52.58  ? 193 THR A CB  1 
ATOM   1408 O  OG1 . THR A 1 214 ? 15.872  15.668  43.489  1.00 62.83  ? 193 THR A OG1 1 
ATOM   1409 C  CG2 . THR A 1 214 ? 13.545  16.243  43.740  1.00 52.86  ? 193 THR A CG2 1 
ATOM   1410 N  N   . LYS A 1 215 ? 15.965  13.098  41.017  1.00 70.03  ? 194 LYS A N   1 
ATOM   1411 C  CA  . LYS A 1 215 ? 16.907  12.651  39.999  1.00 72.47  ? 194 LYS A CA  1 
ATOM   1412 C  C   . LYS A 1 215 ? 16.451  11.297  39.474  1.00 64.40  ? 194 LYS A C   1 
ATOM   1413 O  O   . LYS A 1 215 ? 16.036  10.434  40.252  1.00 57.65  ? 194 LYS A O   1 
ATOM   1414 C  CB  . LYS A 1 215 ? 18.326  12.548  40.566  1.00 60.98  ? 194 LYS A CB  1 
ATOM   1415 N  N   . LYS A 1 216 ? 16.512  11.113  38.156  1.00 64.27  ? 195 LYS A N   1 
ATOM   1416 C  CA  . LYS A 1 216 ? 15.996  9.884   37.564  1.00 68.00  ? 195 LYS A CA  1 
ATOM   1417 C  C   . LYS A 1 216 ? 16.807  8.684   38.042  1.00 64.39  ? 195 LYS A C   1 
ATOM   1418 O  O   . LYS A 1 216 ? 17.984  8.799   38.394  1.00 61.85  ? 195 LYS A O   1 
ATOM   1419 C  CB  . LYS A 1 216 ? 16.013  9.974   36.033  1.00 69.26  ? 195 LYS A CB  1 
ATOM   1420 C  CG  . LYS A 1 216 ? 17.386  9.852   35.373  1.00 72.55  ? 195 LYS A CG  1 
ATOM   1421 C  CD  . LYS A 1 216 ? 17.796  8.400   35.164  1.00 71.68  ? 195 LYS A CD  1 
ATOM   1422 C  CE  . LYS A 1 216 ? 19.064  8.279   34.342  1.00 74.03  ? 195 LYS A CE  1 
ATOM   1423 N  NZ  . LYS A 1 216 ? 19.865  7.131   34.821  1.00 74.01  ? 195 LYS A NZ  1 
ATOM   1424 N  N   . MET A 1 217 ? 16.164  7.516   38.049  1.00 67.89  ? 196 MET A N   1 
ATOM   1425 C  CA  . MET A 1 217 ? 16.809  6.300   38.535  1.00 67.59  ? 196 MET A CA  1 
ATOM   1426 C  C   . MET A 1 217 ? 18.005  5.946   37.660  1.00 67.64  ? 196 MET A C   1 
ATOM   1427 O  O   . MET A 1 217 ? 17.856  5.710   36.457  1.00 69.56  ? 196 MET A O   1 
ATOM   1428 C  CB  . MET A 1 217 ? 15.802  5.152   38.550  1.00 66.18  ? 196 MET A CB  1 
ATOM   1429 C  CG  . MET A 1 217 ? 16.188  4.012   39.470  1.00 55.44  ? 196 MET A CG  1 
ATOM   1430 S  SD  . MET A 1 217 ? 14.972  2.682   39.455  1.00 52.73  ? 196 MET A SD  1 
ATOM   1431 C  CE  . MET A 1 217 ? 13.948  3.139   40.858  1.00 51.60  ? 196 MET A CE  1 
ATOM   1432 N  N   . SER A 1 218 ? 19.191  5.889   38.266  1.00 90.44  ? 197 SER A N   1 
ATOM   1433 C  CA  . SER A 1 218 ? 20.442  5.758   37.531  1.00 86.28  ? 197 SER A CA  1 
ATOM   1434 C  C   . SER A 1 218 ? 21.200  4.513   37.958  1.00 90.22  ? 197 SER A C   1 
ATOM   1435 O  O   . SER A 1 218 ? 21.380  4.266   39.155  1.00 83.65  ? 197 SER A O   1 
ATOM   1436 C  CB  . SER A 1 218 ? 21.328  6.992   37.738  1.00 77.98  ? 197 SER A CB  1 
ATOM   1437 O  OG  . SER A 1 218 ? 22.553  6.865   37.038  1.00 84.77  ? 197 SER A OG  1 
ATOM   1438 N  N   . LYS A 1 219 ? 21.667  3.748   36.970  1.00 93.63  ? 198 LYS A N   1 
ATOM   1439 C  CA  . LYS A 1 219 ? 22.543  2.618   37.247  1.00 95.40  ? 198 LYS A CA  1 
ATOM   1440 C  C   . LYS A 1 219 ? 23.875  3.066   37.832  1.00 95.03  ? 198 LYS A C   1 
ATOM   1441 O  O   . LYS A 1 219 ? 24.559  2.263   38.476  1.00 97.50  ? 198 LYS A O   1 
ATOM   1442 C  CB  . LYS A 1 219 ? 22.781  1.816   35.966  1.00 94.50  ? 198 LYS A CB  1 
ATOM   1443 N  N   . SER A 1 220 ? 24.255  4.327   37.627  1.00 82.11  ? 199 SER A N   1 
ATOM   1444 C  CA  . SER A 1 220 ? 25.513  4.850   38.137  1.00 86.16  ? 199 SER A CA  1 
ATOM   1445 C  C   . SER A 1 220 ? 25.416  5.363   39.568  1.00 86.82  ? 199 SER A C   1 
ATOM   1446 O  O   . SER A 1 220 ? 26.449  5.707   40.153  1.00 87.99  ? 199 SER A O   1 
ATOM   1447 C  CB  . SER A 1 220 ? 26.016  5.983   37.235  1.00 88.37  ? 199 SER A CB  1 
ATOM   1448 O  OG  . SER A 1 220 ? 25.146  7.100   37.289  1.00 88.97  ? 199 SER A OG  1 
ATOM   1449 N  N   . ASP A 1 221 ? 24.216  5.421   40.143  1.00 80.87  ? 200 ASP A N   1 
ATOM   1450 C  CA  . ASP A 1 221 ? 24.056  5.978   41.481  1.00 79.72  ? 200 ASP A CA  1 
ATOM   1451 C  C   . ASP A 1 221 ? 24.970  5.256   42.465  1.00 75.46  ? 200 ASP A C   1 
ATOM   1452 O  O   . ASP A 1 221 ? 24.983  4.023   42.528  1.00 76.75  ? 200 ASP A O   1 
ATOM   1453 C  CB  . ASP A 1 221 ? 22.596  5.865   41.921  1.00 73.94  ? 200 ASP A CB  1 
ATOM   1454 C  CG  . ASP A 1 221 ? 22.287  6.705   43.145  1.00 70.14  ? 200 ASP A CG  1 
ATOM   1455 O  OD1 . ASP A 1 221 ? 23.169  6.841   44.017  1.00 63.88  ? 200 ASP A OD1 1 
ATOM   1456 O  OD2 . ASP A 1 221 ? 21.159  7.234   43.233  1.00 70.53  ? 200 ASP A OD2 1 
ATOM   1457 N  N   . ASP A 1 222 ? 25.743  6.030   43.231  1.00 81.02  ? 201 ASP A N   1 
ATOM   1458 C  CA  . ASP A 1 222 ? 26.657  5.426   44.197  1.00 83.00  ? 201 ASP A CA  1 
ATOM   1459 C  C   . ASP A 1 222 ? 25.894  4.617   45.239  1.00 86.37  ? 201 ASP A C   1 
ATOM   1460 O  O   . ASP A 1 222 ? 26.288  3.495   45.578  1.00 83.53  ? 201 ASP A O   1 
ATOM   1461 C  CB  . ASP A 1 222 ? 27.502  6.508   44.869  1.00 75.24  ? 201 ASP A CB  1 
ATOM   1462 N  N   . ASN A 1 223 ? 24.797  5.169   45.755  1.00 65.83  ? 202 ASN A N   1 
ATOM   1463 C  CA  . ASN A 1 223 ? 23.925  4.453   46.683  1.00 64.97  ? 202 ASN A CA  1 
ATOM   1464 C  C   . ASN A 1 223 ? 22.987  3.578   45.860  1.00 54.50  ? 202 ASN A C   1 
ATOM   1465 O  O   . ASN A 1 223 ? 22.007  4.061   45.287  1.00 49.25  ? 202 ASN A O   1 
ATOM   1466 C  CB  . ASN A 1 223 ? 23.152  5.434   47.559  1.00 51.58  ? 202 ASN A CB  1 
ATOM   1467 C  CG  . ASN A 1 223 ? 22.343  4.743   48.647  1.00 48.02  ? 202 ASN A CG  1 
ATOM   1468 O  OD1 . ASN A 1 223 ? 22.103  3.537   48.589  1.00 48.01  ? 202 ASN A OD1 1 
ATOM   1469 N  ND2 . ASN A 1 223 ? 21.912  5.512   49.645  1.00 47.97  ? 202 ASN A ND2 1 
ATOM   1470 N  N   . ARG A 1 224 ? 23.283  2.277   45.802  1.00 56.28  ? 203 ARG A N   1 
ATOM   1471 C  CA  . ARG A 1 224 ? 22.490  1.363   44.988  1.00 58.57  ? 203 ARG A CA  1 
ATOM   1472 C  C   . ARG A 1 224 ? 21.071  1.176   45.514  1.00 55.53  ? 203 ARG A C   1 
ATOM   1473 O  O   . ARG A 1 224 ? 20.241  0.601   44.802  1.00 54.96  ? 203 ARG A O   1 
ATOM   1474 C  CB  . ARG A 1 224 ? 23.182  0.000   44.892  1.00 60.89  ? 203 ARG A CB  1 
ATOM   1475 C  CG  . ARG A 1 224 ? 24.188  -0.128  43.748  1.00 60.76  ? 203 ARG A CG  1 
ATOM   1476 C  CD  . ARG A 1 224 ? 25.504  0.585   44.038  1.00 69.75  ? 203 ARG A CD  1 
ATOM   1477 N  NE  . ARG A 1 224 ? 26.108  0.147   45.292  1.00 68.89  ? 203 ARG A NE  1 
ATOM   1478 C  CZ  . ARG A 1 224 ? 27.054  -0.778  45.401  1.00 64.81  ? 203 ARG A CZ  1 
ATOM   1479 N  NH1 . ARG A 1 224 ? 27.540  -1.404  44.340  1.00 66.46  ? 203 ARG A NH1 1 
ATOM   1480 N  NH2 . ARG A 1 224 ? 27.525  -1.084  46.606  1.00 58.58  ? 203 ARG A NH2 1 
ATOM   1481 N  N   . ASN A 1 225 ? 20.770  1.634   46.731  1.00 48.01  ? 204 ASN A N   1 
ATOM   1482 C  CA  . ASN A 1 225 ? 19.399  1.593   47.230  1.00 47.98  ? 204 ASN A CA  1 
ATOM   1483 C  C   . ASN A 1 225 ? 18.497  2.623   46.560  1.00 47.79  ? 204 ASN A C   1 
ATOM   1484 O  O   . ASN A 1 225 ? 17.319  2.716   46.923  1.00 47.96  ? 204 ASN A O   1 
ATOM   1485 C  CB  . ASN A 1 225 ? 19.382  1.798   48.746  1.00 48.11  ? 204 ASN A CB  1 
ATOM   1486 C  CG  . ASN A 1 225 ? 19.904  0.590   49.504  1.00 48.69  ? 204 ASN A CG  1 
ATOM   1487 O  OD1 . ASN A 1 225 ? 19.659  -0.554  49.118  1.00 49.12  ? 204 ASN A OD1 1 
ATOM   1488 N  ND2 . ASN A 1 225 ? 20.632  0.840   50.584  1.00 48.89  ? 204 ASN A ND2 1 
ATOM   1489 N  N   . ASN A 1 226 ? 19.020  3.397   45.609  1.00 47.96  ? 205 ASN A N   1 
ATOM   1490 C  CA  . ASN A 1 226 ? 18.215  4.272   44.771  1.00 49.27  ? 205 ASN A CA  1 
ATOM   1491 C  C   . ASN A 1 226 ? 17.690  3.581   43.521  1.00 51.24  ? 205 ASN A C   1 
ATOM   1492 O  O   . ASN A 1 226 ? 16.869  4.168   42.807  1.00 53.35  ? 205 ASN A O   1 
ATOM   1493 C  CB  . ASN A 1 226 ? 19.033  5.491   44.329  1.00 52.32  ? 205 ASN A CB  1 
ATOM   1494 C  CG  . ASN A 1 226 ? 19.167  6.532   45.414  1.00 58.83  ? 205 ASN A CG  1 
ATOM   1495 O  OD1 . ASN A 1 226 ? 18.181  7.139   45.830  1.00 52.85  ? 205 ASN A OD1 1 
ATOM   1496 N  ND2 . ASN A 1 226 ? 20.395  6.767   45.862  1.00 54.58  ? 205 ASN A ND2 1 
ATOM   1497 N  N   . VAL A 1 227 ? 18.137  2.358   43.242  1.00 49.87  ? 206 VAL A N   1 
ATOM   1498 C  CA  . VAL A 1 227 ? 17.961  1.736   41.936  1.00 52.87  ? 206 VAL A CA  1 
ATOM   1499 C  C   . VAL A 1 227 ? 17.307  0.373   42.103  1.00 52.82  ? 206 VAL A C   1 
ATOM   1500 O  O   . VAL A 1 227 ? 17.662  -0.392  43.007  1.00 52.77  ? 206 VAL A O   1 
ATOM   1501 C  CB  . VAL A 1 227 ? 19.312  1.597   41.199  1.00 57.50  ? 206 VAL A CB  1 
ATOM   1502 C  CG1 . VAL A 1 227 ? 19.088  1.420   39.707  1.00 53.56  ? 206 VAL A CG1 1 
ATOM   1503 C  CG2 . VAL A 1 227 ? 20.202  2.799   41.484  1.00 61.96  ? 206 VAL A CG2 1 
ATOM   1504 N  N   . ILE A 1 228 ? 16.347  0.077   41.231  1.00 49.20  ? 207 ILE A N   1 
ATOM   1505 C  CA  . ILE A 1 228 ? 15.761  -1.253  41.105  1.00 51.38  ? 207 ILE A CA  1 
ATOM   1506 C  C   . ILE A 1 228 ? 16.114  -1.774  39.719  1.00 50.82  ? 207 ILE A C   1 
ATOM   1507 O  O   . ILE A 1 228 ? 15.762  -1.152  38.707  1.00 50.38  ? 207 ILE A O   1 
ATOM   1508 C  CB  . ILE A 1 228 ? 14.237  -1.234  41.316  1.00 50.29  ? 207 ILE A CB  1 
ATOM   1509 C  CG1 . ILE A 1 228 ? 13.878  -1.025  42.796  1.00 54.81  ? 207 ILE A CG1 1 
ATOM   1510 C  CG2 . ILE A 1 228 ? 13.593  -2.511  40.777  1.00 53.87  ? 207 ILE A CG2 1 
ATOM   1511 C  CD1 . ILE A 1 228 ? 14.867  -1.608  43.793  1.00 57.20  ? 207 ILE A CD1 1 
ATOM   1512 N  N   . GLY A 1 229 ? 16.804  -2.903  39.666  1.00 53.05  ? 208 GLY A N   1 
ATOM   1513 C  CA  . GLY A 1 229 ? 17.154  -3.526  38.408  1.00 55.22  ? 208 GLY A CA  1 
ATOM   1514 C  C   . GLY A 1 229 ? 16.153  -4.594  38.012  1.00 54.48  ? 208 GLY A C   1 
ATOM   1515 O  O   . GLY A 1 229 ? 15.487  -5.188  38.857  1.00 52.68  ? 208 GLY A O   1 
ATOM   1516 N  N   . LEU A 1 230 ? 16.055  -4.835  36.705  1.00 54.47  ? 209 LEU A N   1 
ATOM   1517 C  CA  . LEU A 1 230 ? 15.160  -5.880  36.226  1.00 54.80  ? 209 LEU A CA  1 
ATOM   1518 C  C   . LEU A 1 230 ? 15.497  -7.225  36.853  1.00 54.05  ? 209 LEU A C   1 
ATOM   1519 O  O   . LEU A 1 230 ? 14.605  -8.055  37.057  1.00 54.97  ? 209 LEU A O   1 
ATOM   1520 C  CB  . LEU A 1 230 ? 15.224  -5.978  34.702  1.00 54.11  ? 209 LEU A CB  1 
ATOM   1521 C  CG  . LEU A 1 230 ? 14.484  -4.922  33.876  1.00 58.20  ? 209 LEU A CG  1 
ATOM   1522 C  CD1 . LEU A 1 230 ? 14.506  -5.325  32.406  1.00 56.56  ? 209 LEU A CD1 1 
ATOM   1523 C  CD2 . LEU A 1 230 ? 13.047  -4.711  34.345  1.00 62.37  ? 209 LEU A CD2 1 
ATOM   1524 N  N   . LEU A 1 231 ? 16.771  -7.456  37.171  1.00 55.02  ? 210 LEU A N   1 
ATOM   1525 C  CA  . LEU A 1 231 ? 17.226  -8.707  37.763  1.00 56.43  ? 210 LEU A CA  1 
ATOM   1526 C  C   . LEU A 1 231 ? 17.563  -8.545  39.243  1.00 66.07  ? 210 LEU A C   1 
ATOM   1527 O  O   . LEU A 1 231 ? 18.490  -9.181  39.751  1.00 63.05  ? 210 LEU A O   1 
ATOM   1528 C  CB  . LEU A 1 231 ? 18.428  -9.243  36.991  1.00 56.65  ? 210 LEU A CB  1 
ATOM   1529 C  CG  . LEU A 1 231 ? 18.171  -9.451  35.497  1.00 55.73  ? 210 LEU A CG  1 
ATOM   1530 C  CD1 . LEU A 1 231 ? 19.427  -9.963  34.806  1.00 56.43  ? 210 LEU A CD1 1 
ATOM   1531 C  CD2 . LEU A 1 231 ? 17.004  -10.403 35.264  1.00 56.80  ? 210 LEU A CD2 1 
ATOM   1532 N  N   . GLU A 1 232 ? 16.815  -7.697  39.943  1.00 76.20  ? 211 GLU A N   1 
ATOM   1533 C  CA  . GLU A 1 232 ? 16.959  -7.533  41.382  1.00 77.45  ? 211 GLU A CA  1 
ATOM   1534 C  C   . GLU A 1 232 ? 16.051  -8.530  42.090  1.00 82.65  ? 211 GLU A C   1 
ATOM   1535 O  O   . GLU A 1 232 ? 14.875  -8.664  41.737  1.00 76.08  ? 211 GLU A O   1 
ATOM   1536 C  CB  . GLU A 1 232 ? 16.612  -6.104  41.800  1.00 68.99  ? 211 GLU A CB  1 
ATOM   1537 N  N   . ASP A 1 233 ? 16.595  -9.220  43.087  1.00 85.26  ? 212 ASP A N   1 
ATOM   1538 C  CA  . ASP A 1 233 ? 15.831  -10.249 43.780  1.00 84.57  ? 212 ASP A CA  1 
ATOM   1539 C  C   . ASP A 1 233 ? 14.548  -9.647  44.350  1.00 83.20  ? 212 ASP A C   1 
ATOM   1540 O  O   . ASP A 1 233 ? 14.581  -8.557  44.931  1.00 83.11  ? 212 ASP A O   1 
ATOM   1541 C  CB  . ASP A 1 233 ? 16.670  -10.867 44.901  1.00 90.44  ? 212 ASP A CB  1 
ATOM   1542 C  CG  . ASP A 1 233 ? 15.875  -11.830 45.767  1.00 90.80  ? 212 ASP A CG  1 
ATOM   1543 O  OD1 . ASP A 1 233 ? 15.577  -12.951 45.302  1.00 90.09  ? 212 ASP A OD1 1 
ATOM   1544 O  OD2 . ASP A 1 233 ? 15.552  -11.466 46.918  1.00 91.73  ? 212 ASP A OD2 1 
ATOM   1545 N  N   . PRO A 1 234 ? 13.402  -10.325 44.206  1.00 80.32  ? 213 PRO A N   1 
ATOM   1546 C  CA  . PRO A 1 234 ? 12.134  -9.705  44.634  1.00 80.71  ? 213 PRO A CA  1 
ATOM   1547 C  C   . PRO A 1 234 ? 12.135  -9.207  46.069  1.00 79.45  ? 213 PRO A C   1 
ATOM   1548 O  O   . PRO A 1 234 ? 11.623  -8.113  46.336  1.00 74.58  ? 213 PRO A O   1 
ATOM   1549 C  CB  . PRO A 1 234 ? 11.116  -10.838 44.438  1.00 73.13  ? 213 PRO A CB  1 
ATOM   1550 C  CG  . PRO A 1 234 ? 11.696  -11.686 43.366  1.00 79.14  ? 213 PRO A CG  1 
ATOM   1551 C  CD  . PRO A 1 234 ? 13.187  -11.628 43.548  1.00 83.04  ? 213 PRO A CD  1 
ATOM   1552 N  N   . LYS A 1 235 ? 12.701  -9.973  47.004  1.00 78.51  ? 214 LYS A N   1 
ATOM   1553 C  CA  . LYS A 1 235 ? 12.741  -9.523  48.392  1.00 77.29  ? 214 LYS A CA  1 
ATOM   1554 C  C   . LYS A 1 235 ? 13.550  -8.238  48.524  1.00 78.16  ? 214 LYS A C   1 
ATOM   1555 O  O   . LYS A 1 235 ? 13.173  -7.331  49.275  1.00 69.93  ? 214 LYS A O   1 
ATOM   1556 C  CB  . LYS A 1 235 ? 13.324  -10.620 49.282  1.00 73.66  ? 214 LYS A CB  1 
ATOM   1557 N  N   . SER A 1 236 ? 14.671  -8.147  47.804  1.00 73.41  ? 215 SER A N   1 
ATOM   1558 C  CA  . SER A 1 236 ? 15.480  -6.933  47.841  1.00 69.52  ? 215 SER A CA  1 
ATOM   1559 C  C   . SER A 1 236 ? 14.711  -5.742  47.284  1.00 73.64  ? 215 SER A C   1 
ATOM   1560 O  O   . SER A 1 236 ? 14.797  -4.631  47.820  1.00 69.88  ? 215 SER A O   1 
ATOM   1561 C  CB  . SER A 1 236 ? 16.777  -7.146  47.059  1.00 69.87  ? 215 SER A CB  1 
ATOM   1562 O  OG  . SER A 1 236 ? 17.693  -6.091  47.291  1.00 84.45  ? 215 SER A OG  1 
ATOM   1563 N  N   . VAL A 1 237 ? 13.957  -5.952  46.202  1.00 77.67  ? 216 VAL A N   1 
ATOM   1564 C  CA  . VAL A 1 237 ? 13.206  -4.855  45.599  1.00 73.98  ? 216 VAL A CA  1 
ATOM   1565 C  C   . VAL A 1 237 ? 12.143  -4.351  46.566  1.00 68.14  ? 216 VAL A C   1 
ATOM   1566 O  O   . VAL A 1 237 ? 11.907  -3.141  46.678  1.00 58.29  ? 216 VAL A O   1 
ATOM   1567 C  CB  . VAL A 1 237 ? 12.585  -5.299  44.260  1.00 74.80  ? 216 VAL A CB  1 
ATOM   1568 C  CG1 . VAL A 1 237 ? 12.009  -4.102  43.518  1.00 71.43  ? 216 VAL A CG1 1 
ATOM   1569 C  CG2 . VAL A 1 237 ? 13.617  -6.016  43.400  1.00 73.15  ? 216 VAL A CG2 1 
ATOM   1570 N  N   . VAL A 1 238 ? 11.486  -5.268  47.277  1.00 71.01  ? 217 VAL A N   1 
ATOM   1571 C  CA  . VAL A 1 238 ? 10.453  -4.870  48.226  1.00 65.93  ? 217 VAL A CA  1 
ATOM   1572 C  C   . VAL A 1 238 ? 11.063  -4.087  49.382  1.00 63.64  ? 217 VAL A C   1 
ATOM   1573 O  O   . VAL A 1 238 ? 10.453  -3.146  49.901  1.00 66.84  ? 217 VAL A O   1 
ATOM   1574 C  CB  . VAL A 1 238 ? 9.684   -6.107  48.725  1.00 64.16  ? 217 VAL A CB  1 
ATOM   1575 N  N   . LYS A 1 239 ? 12.268  -4.469  49.813  1.00 62.47  ? 218 LYS A N   1 
ATOM   1576 C  CA  . LYS A 1 239 ? 12.922  -3.765  50.912  1.00 63.07  ? 218 LYS A CA  1 
ATOM   1577 C  C   . LYS A 1 239 ? 13.221  -2.318  50.538  1.00 59.95  ? 218 LYS A C   1 
ATOM   1578 O  O   . LYS A 1 239 ? 12.941  -1.393  51.311  1.00 53.82  ? 218 LYS A O   1 
ATOM   1579 C  CB  . LYS A 1 239 ? 14.207  -4.494  51.304  1.00 66.49  ? 218 LYS A CB  1 
ATOM   1580 C  CG  . LYS A 1 239 ? 14.001  -5.627  52.295  1.00 64.16  ? 218 LYS A CG  1 
ATOM   1581 C  CD  . LYS A 1 239 ? 15.052  -6.714  52.122  1.00 70.25  ? 218 LYS A CD  1 
ATOM   1582 C  CE  . LYS A 1 239 ? 14.970  -7.754  53.233  1.00 69.22  ? 218 LYS A CE  1 
ATOM   1583 N  NZ  . LYS A 1 239 ? 14.509  -9.086  52.741  1.00 74.08  ? 218 LYS A NZ  1 
ATOM   1584 N  N   . LYS A 1 240 ? 13.795  -2.104  49.353  1.00 58.22  ? 219 LYS A N   1 
ATOM   1585 C  CA  . LYS A 1 240 ? 14.118  -0.748  48.922  1.00 63.52  ? 219 LYS A CA  1 
ATOM   1586 C  C   . LYS A 1 240 ? 12.857  0.090   48.760  1.00 58.16  ? 219 LYS A C   1 
ATOM   1587 O  O   . LYS A 1 240 ? 12.828  1.265   49.145  1.00 56.82  ? 219 LYS A O   1 
ATOM   1588 C  CB  . LYS A 1 240 ? 14.907  -0.792  47.614  1.00 54.01  ? 219 LYS A CB  1 
ATOM   1589 C  CG  . LYS A 1 240 ? 16.206  -1.579  47.701  1.00 61.71  ? 219 LYS A CG  1 
ATOM   1590 C  CD  . LYS A 1 240 ? 16.916  -1.626  46.358  1.00 55.25  ? 219 LYS A CD  1 
ATOM   1591 C  CE  . LYS A 1 240 ? 18.343  -2.122  46.502  1.00 49.53  ? 219 LYS A CE  1 
ATOM   1592 N  NZ  . LYS A 1 240 ? 19.042  -2.171  45.193  1.00 49.32  ? 219 LYS A NZ  1 
ATOM   1593 N  N   . ILE A 1 241 ? 11.804  -0.496  48.191  1.00 59.58  ? 220 ILE A N   1 
ATOM   1594 C  CA  . ILE A 1 241 ? 10.537  0.217   48.065  1.00 58.67  ? 220 ILE A CA  1 
ATOM   1595 C  C   . ILE A 1 241 ? 10.002  0.585   49.442  1.00 53.87  ? 220 ILE A C   1 
ATOM   1596 O  O   . ILE A 1 241 ? 9.447   1.672   49.638  1.00 54.47  ? 220 ILE A O   1 
ATOM   1597 C  CB  . ILE A 1 241 ? 9.529   -0.633  47.267  1.00 56.93  ? 220 ILE A CB  1 
ATOM   1598 C  CG1 . ILE A 1 241 ? 9.900   -0.660  45.775  1.00 59.28  ? 220 ILE A CG1 1 
ATOM   1599 C  CG2 . ILE A 1 241 ? 8.106   -0.128  47.462  1.00 58.56  ? 220 ILE A CG2 1 
ATOM   1600 C  CD1 . ILE A 1 241 ? 10.103  0.715   45.134  1.00 64.43  ? 220 ILE A CD1 1 
ATOM   1601 N  N   . LYS A 1 242 ? 10.164  -0.315  50.417  1.00 54.71  ? 221 LYS A N   1 
ATOM   1602 C  CA  . LYS A 1 242 ? 9.681   -0.048  51.768  1.00 55.61  ? 221 LYS A CA  1 
ATOM   1603 C  C   . LYS A 1 242 ? 10.420  1.118   52.409  1.00 59.25  ? 221 LYS A C   1 
ATOM   1604 O  O   . LYS A 1 242 ? 9.854   1.823   53.254  1.00 61.02  ? 221 LYS A O   1 
ATOM   1605 C  CB  . LYS A 1 242 ? 9.827   -1.303  52.629  1.00 56.96  ? 221 LYS A CB  1 
ATOM   1606 N  N   . ARG A 1 243 ? 11.680  1.332   52.032  1.00 58.00  ? 222 ARG A N   1 
ATOM   1607 C  CA  . ARG A 1 243 ? 12.491  2.419   52.559  1.00 58.59  ? 222 ARG A CA  1 
ATOM   1608 C  C   . ARG A 1 243 ? 12.519  3.634   51.637  1.00 57.02  ? 222 ARG A C   1 
ATOM   1609 O  O   . ARG A 1 243 ? 13.279  4.573   51.892  1.00 52.24  ? 222 ARG A O   1 
ATOM   1610 C  CB  . ARG A 1 243 ? 13.918  1.927   52.817  1.00 53.47  ? 222 ARG A CB  1 
ATOM   1611 N  N   . ALA A 1 244 ? 11.718  3.638   50.573  1.00 58.76  ? 223 ALA A N   1 
ATOM   1612 C  CA  . ALA A 1 244 ? 11.697  4.775   49.663  1.00 54.55  ? 223 ALA A CA  1 
ATOM   1613 C  C   . ALA A 1 244 ? 11.251  6.032   50.399  1.00 60.72  ? 223 ALA A C   1 
ATOM   1614 O  O   . ALA A 1 244 ? 10.395  5.982   51.287  1.00 58.02  ? 223 ALA A O   1 
ATOM   1615 C  CB  . ALA A 1 244 ? 10.768  4.497   48.482  1.00 60.67  ? 223 ALA A CB  1 
ATOM   1616 N  N   . VAL A 1 245 ? 11.838  7.169   50.024  1.00 62.31  ? 224 VAL A N   1 
ATOM   1617 C  CA  . VAL A 1 245 ? 11.566  8.408   50.739  1.00 61.26  ? 224 VAL A CA  1 
ATOM   1618 C  C   . VAL A 1 245 ? 10.130  8.852   50.486  1.00 60.13  ? 224 VAL A C   1 
ATOM   1619 O  O   . VAL A 1 245 ? 9.537   8.573   49.434  1.00 59.45  ? 224 VAL A O   1 
ATOM   1620 C  CB  . VAL A 1 245 ? 12.565  9.508   50.332  1.00 65.10  ? 224 VAL A CB  1 
ATOM   1621 C  CG1 . VAL A 1 245 ? 12.269  10.022  48.928  1.00 65.85  ? 224 VAL A CG1 1 
ATOM   1622 C  CG2 . VAL A 1 245 ? 12.541  10.649  51.337  1.00 68.09  ? 224 VAL A CG2 1 
ATOM   1623 N  N   . THR A 1 246 ? 9.569   9.557   51.464  1.00 61.28  ? 225 THR A N   1 
ATOM   1624 C  CA  . THR A 1 246 ? 8.245   10.152  51.360  1.00 68.53  ? 225 THR A CA  1 
ATOM   1625 C  C   . THR A 1 246 ? 8.321   11.543  51.987  1.00 71.68  ? 225 THR A C   1 
ATOM   1626 O  O   . THR A 1 246 ? 9.410   12.079  52.217  1.00 75.30  ? 225 THR A O   1 
ATOM   1627 C  CB  . THR A 1 246 ? 7.189   9.257   52.025  1.00 69.24  ? 225 THR A CB  1 
ATOM   1628 O  OG1 . THR A 1 246 ? 7.528   9.044   53.401  1.00 66.95  ? 225 THR A OG1 1 
ATOM   1629 C  CG2 . THR A 1 246 ? 7.103   7.912   51.314  1.00 62.12  ? 225 THR A CG2 1 
ATOM   1630 N  N   . ASP A 1 247 ? 7.165   12.141  52.250  1.00 77.57  ? 226 ASP A N   1 
ATOM   1631 C  CA  . ASP A 1 247 ? 7.087   13.457  52.868  1.00 75.60  ? 226 ASP A CA  1 
ATOM   1632 C  C   . ASP A 1 247 ? 6.561   13.327  54.297  1.00 83.84  ? 226 ASP A C   1 
ATOM   1633 O  O   . ASP A 1 247 ? 6.344   12.227  54.812  1.00 84.95  ? 226 ASP A O   1 
ATOM   1634 C  CB  . ASP A 1 247 ? 6.215   14.394  52.030  1.00 79.72  ? 226 ASP A CB  1 
ATOM   1635 C  CG  . ASP A 1 247 ? 4.819   13.856  51.819  1.00 87.68  ? 226 ASP A CG  1 
ATOM   1636 O  OD1 . ASP A 1 247 ? 4.043   13.832  52.795  1.00 81.35  ? 226 ASP A OD1 1 
ATOM   1637 O  OD2 . ASP A 1 247 ? 4.500   13.461  50.678  1.00 78.06  ? 226 ASP A OD2 1 
ATOM   1638 N  N   . SER A 1 248 ? 6.359   14.478  54.940  1.00 85.44  ? 227 SER A N   1 
ATOM   1639 C  CA  . SER A 1 248 ? 6.015   14.549  56.355  1.00 84.91  ? 227 SER A CA  1 
ATOM   1640 C  C   . SER A 1 248 ? 4.659   15.209  56.579  1.00 88.01  ? 227 SER A C   1 
ATOM   1641 O  O   . SER A 1 248 ? 4.439   15.860  57.603  1.00 88.29  ? 227 SER A O   1 
ATOM   1642 C  CB  . SER A 1 248 ? 7.100   15.303  57.120  1.00 84.85  ? 227 SER A CB  1 
ATOM   1643 O  OG  . SER A 1 248 ? 7.406   16.517  56.457  1.00 81.75  ? 227 SER A OG  1 
ATOM   1644 N  N   . ASP A 1 249 ? 3.740   15.054  55.630  1.00 92.49  ? 228 ASP A N   1 
ATOM   1645 C  CA  . ASP A 1 249 ? 2.404   15.609  55.795  1.00 91.69  ? 228 ASP A CA  1 
ATOM   1646 C  C   . ASP A 1 249 ? 1.730   14.990  57.012  1.00 93.36  ? 228 ASP A C   1 
ATOM   1647 O  O   . ASP A 1 249 ? 1.759   13.770  57.201  1.00 94.67  ? 228 ASP A O   1 
ATOM   1648 C  CB  . ASP A 1 249 ? 1.566   15.360  54.541  1.00 88.30  ? 228 ASP A CB  1 
ATOM   1649 C  CG  . ASP A 1 249 ? 2.083   16.116  53.330  1.00 88.92  ? 228 ASP A CG  1 
ATOM   1650 O  OD1 . ASP A 1 249 ? 3.094   16.840  53.459  1.00 89.38  ? 228 ASP A OD1 1 
ATOM   1651 O  OD2 . ASP A 1 249 ? 1.475   15.987  52.246  1.00 80.52  ? 228 ASP A OD2 1 
ATOM   1652 N  N   . GLU A 1 250 ? 1.129   15.835  57.839  1.00 100.35 ? 229 GLU A N   1 
ATOM   1653 C  CA  . GLU A 1 250 ? 0.405   15.396  59.031  1.00 90.65  ? 229 GLU A CA  1 
ATOM   1654 C  C   . GLU A 1 250 ? -1.070  15.737  58.874  1.00 90.29  ? 229 GLU A C   1 
ATOM   1655 O  O   . GLU A 1 250 ? -1.440  16.921  58.985  1.00 97.63  ? 229 GLU A O   1 
ATOM   1656 C  CB  . GLU A 1 250 ? 0.977   16.062  60.283  1.00 99.42  ? 229 GLU A CB  1 
ATOM   1657 N  N   . PRO A 1 251 ? -1.959  14.763  58.612  1.00 93.14  ? 230 PRO A N   1 
ATOM   1658 C  CA  . PRO A 1 251 ? -1.719  13.323  58.430  1.00 99.78  ? 230 PRO A CA  1 
ATOM   1659 C  C   . PRO A 1 251 ? -1.225  12.997  57.026  1.00 102.21 ? 230 PRO A C   1 
ATOM   1660 O  O   . PRO A 1 251 ? -1.318  13.830  56.129  1.00 97.48  ? 230 PRO A O   1 
ATOM   1661 C  CB  . PRO A 1 251 ? -3.100  12.717  58.709  1.00 94.72  ? 230 PRO A CB  1 
ATOM   1662 C  CG  . PRO A 1 251 ? -4.050  13.753  58.182  1.00 95.14  ? 230 PRO A CG  1 
ATOM   1663 C  CD  . PRO A 1 251 ? -3.392  15.090  58.472  1.00 99.45  ? 230 PRO A CD  1 
ATOM   1664 N  N   . PRO A 1 252 ? -0.692  11.797  56.803  1.00 101.14 ? 231 PRO A N   1 
ATOM   1665 C  CA  . PRO A 1 252 ? -0.236  11.444  55.453  1.00 101.77 ? 231 PRO A CA  1 
ATOM   1666 C  C   . PRO A 1 252 ? -1.369  11.530  54.441  1.00 98.50  ? 231 PRO A C   1 
ATOM   1667 O  O   . PRO A 1 252 ? -2.511  11.160  54.721  1.00 100.30 ? 231 PRO A O   1 
ATOM   1668 C  CB  . PRO A 1 252 ? 0.269   10.004  55.613  1.00 95.84  ? 231 PRO A CB  1 
ATOM   1669 C  CG  . PRO A 1 252 ? 0.608   9.875   57.059  1.00 99.13  ? 231 PRO A CG  1 
ATOM   1670 C  CD  . PRO A 1 252 ? -0.370  10.752  57.791  1.00 101.59 ? 231 PRO A CD  1 
ATOM   1671 N  N   . VAL A 1 253 ? -1.038  12.031  53.254  1.00 90.58  ? 232 VAL A N   1 
ATOM   1672 C  CA  . VAL A 1 253 ? -1.963  12.105  52.132  1.00 89.36  ? 232 VAL A CA  1 
ATOM   1673 C  C   . VAL A 1 253 ? -1.275  11.505  50.915  1.00 99.46  ? 232 VAL A C   1 
ATOM   1674 O  O   . VAL A 1 253 ? -0.096  11.774  50.664  1.00 96.46  ? 232 VAL A O   1 
ATOM   1675 C  CB  . VAL A 1 253 ? -2.408  13.555  51.848  1.00 90.05  ? 232 VAL A CB  1 
ATOM   1676 N  N   . VAL A 1 254 ? -2.004  10.678  50.173  1.00 91.72  ? 233 VAL A N   1 
ATOM   1677 C  CA  . VAL A 1 254 ? -1.497  10.048  48.960  1.00 90.92  ? 233 VAL A CA  1 
ATOM   1678 C  C   . VAL A 1 254 ? -2.098  10.813  47.786  1.00 92.25  ? 233 VAL A C   1 
ATOM   1679 O  O   . VAL A 1 254 ? -3.237  10.567  47.382  1.00 93.19  ? 233 VAL A O   1 
ATOM   1680 C  CB  . VAL A 1 254 ? -1.841  8.558   48.909  1.00 76.36  ? 233 VAL A CB  1 
ATOM   1681 C  CG1 . VAL A 1 254 ? -1.356  7.948   47.610  1.00 84.36  ? 233 VAL A CG1 1 
ATOM   1682 C  CG2 . VAL A 1 254 ? -1.234  7.835   50.103  1.00 73.93  ? 233 VAL A CG2 1 
ATOM   1683 N  N   . ARG A 1 255 ? -1.322  11.739  47.229  1.00 82.62  ? 234 ARG A N   1 
ATOM   1684 C  CA  . ARG A 1 255 ? -1.807  12.628  46.183  1.00 86.74  ? 234 ARG A CA  1 
ATOM   1685 C  C   . ARG A 1 255 ? -0.626  13.053  45.324  1.00 83.11  ? 234 ARG A C   1 
ATOM   1686 O  O   . ARG A 1 255 ? 0.445   13.377  45.843  1.00 81.57  ? 234 ARG A O   1 
ATOM   1687 C  CB  . ARG A 1 255 ? -2.517  13.844  46.790  1.00 82.66  ? 234 ARG A CB  1 
ATOM   1688 C  CG  . ARG A 1 255 ? -2.901  14.937  45.802  1.00 84.99  ? 234 ARG A CG  1 
ATOM   1689 C  CD  . ARG A 1 255 ? -2.204  16.247  46.147  1.00 87.03  ? 234 ARG A CD  1 
ATOM   1690 N  NE  . ARG A 1 255 ? -2.424  16.633  47.537  1.00 89.07  ? 234 ARG A NE  1 
ATOM   1691 C  CZ  . ARG A 1 255 ? -1.791  17.621  48.153  1.00 87.17  ? 234 ARG A CZ  1 
ATOM   1692 N  NH1 . ARG A 1 255 ? -0.890  18.363  47.528  1.00 82.54  ? 234 ARG A NH1 1 
ATOM   1693 N  NH2 . ARG A 1 255 ? -2.064  17.869  49.431  1.00 92.14  ? 234 ARG A NH2 1 
ATOM   1694 N  N   . TYR A 1 256 ? -0.833  13.049  44.009  1.00 77.55  ? 235 TYR A N   1 
ATOM   1695 C  CA  . TYR A 1 256 ? 0.238   13.322  43.055  1.00 73.49  ? 235 TYR A CA  1 
ATOM   1696 C  C   . TYR A 1 256 ? 0.497   14.821  43.013  1.00 80.12  ? 235 TYR A C   1 
ATOM   1697 O  O   . TYR A 1 256 ? -0.269  15.586  42.422  1.00 89.18  ? 235 TYR A O   1 
ATOM   1698 C  CB  . TYR A 1 256 ? -0.123  12.787  41.674  1.00 79.95  ? 235 TYR A CB  1 
ATOM   1699 C  CG  . TYR A 1 256 ? 1.025   12.824  40.692  1.00 75.22  ? 235 TYR A CG  1 
ATOM   1700 C  CD1 . TYR A 1 256 ? 2.040   11.877  40.746  1.00 63.85  ? 235 TYR A CD1 1 
ATOM   1701 C  CD2 . TYR A 1 256 ? 1.096   13.804  39.710  1.00 77.48  ? 235 TYR A CD2 1 
ATOM   1702 C  CE1 . TYR A 1 256 ? 3.091   11.905  39.851  1.00 66.76  ? 235 TYR A CE1 1 
ATOM   1703 C  CE2 . TYR A 1 256 ? 2.147   13.839  38.811  1.00 72.89  ? 235 TYR A CE2 1 
ATOM   1704 C  CZ  . TYR A 1 256 ? 3.140   12.889  38.887  1.00 72.24  ? 235 TYR A CZ  1 
ATOM   1705 O  OH  . TYR A 1 256 ? 4.184   12.923  37.994  1.00 70.00  ? 235 TYR A OH  1 
ATOM   1706 N  N   . ASP A 1 257 ? 1.585   15.242  43.652  1.00 76.14  ? 236 ASP A N   1 
ATOM   1707 C  CA  . ASP A 1 257 ? 2.080   16.615  43.565  1.00 75.83  ? 236 ASP A CA  1 
ATOM   1708 C  C   . ASP A 1 257 ? 3.601   16.511  43.601  1.00 74.58  ? 236 ASP A C   1 
ATOM   1709 O  O   . ASP A 1 257 ? 4.188   16.305  44.667  1.00 79.51  ? 236 ASP A O   1 
ATOM   1710 C  CB  . ASP A 1 257 ? 1.547   17.482  44.696  1.00 75.74  ? 236 ASP A CB  1 
ATOM   1711 C  CG  . ASP A 1 257 ? 2.205   18.850  44.744  1.00 77.23  ? 236 ASP A CG  1 
ATOM   1712 O  OD1 . ASP A 1 257 ? 2.919   19.212  43.783  1.00 71.93  ? 236 ASP A OD1 1 
ATOM   1713 O  OD2 . ASP A 1 257 ? 2.008   19.562  45.750  1.00 79.32  ? 236 ASP A OD2 1 
ATOM   1714 N  N   . VAL A 1 258 ? 4.232   16.643  42.435  1.00 75.38  ? 237 VAL A N   1 
ATOM   1715 C  CA  . VAL A 1 258 ? 5.669   16.412  42.350  1.00 84.38  ? 237 VAL A CA  1 
ATOM   1716 C  C   . VAL A 1 258 ? 6.461   17.511  43.045  1.00 74.88  ? 237 VAL A C   1 
ATOM   1717 O  O   . VAL A 1 258 ? 7.593   17.276  43.482  1.00 62.71  ? 237 VAL A O   1 
ATOM   1718 C  CB  . VAL A 1 258 ? 6.087   16.268  40.875  1.00 78.73  ? 237 VAL A CB  1 
ATOM   1719 C  CG1 . VAL A 1 258 ? 6.352   17.636  40.248  1.00 78.42  ? 237 VAL A CG1 1 
ATOM   1720 C  CG2 . VAL A 1 258 ? 7.302   15.361  40.755  1.00 70.75  ? 237 VAL A CG2 1 
ATOM   1721 N  N   . GLN A 1 259 ? 5.899   18.719  43.160  1.00 76.89  ? 238 GLN A N   1 
ATOM   1722 C  CA  . GLN A 1 259 ? 6.648   19.836  43.730  1.00 66.34  ? 238 GLN A CA  1 
ATOM   1723 C  C   . GLN A 1 259 ? 6.873   19.653  45.228  1.00 66.53  ? 238 GLN A C   1 
ATOM   1724 O  O   . GLN A 1 259 ? 7.997   19.810  45.719  1.00 65.77  ? 238 GLN A O   1 
ATOM   1725 C  CB  . GLN A 1 259 ? 5.914   21.149  43.456  1.00 70.08  ? 238 GLN A CB  1 
ATOM   1726 N  N   . ASN A 1 260 ? 5.817   19.313  45.971  1.00 68.52  ? 239 ASN A N   1 
ATOM   1727 C  CA  . ASN A 1 260 ? 5.883   19.271  47.427  1.00 69.00  ? 239 ASN A CA  1 
ATOM   1728 C  C   . ASN A 1 260 ? 6.000   17.866  47.998  1.00 69.35  ? 239 ASN A C   1 
ATOM   1729 O  O   . ASN A 1 260 ? 6.401   17.721  49.158  1.00 68.02  ? 239 ASN A O   1 
ATOM   1730 C  CB  . ASN A 1 260 ? 4.638   19.933  48.031  1.00 70.59  ? 239 ASN A CB  1 
ATOM   1731 C  CG  . ASN A 1 260 ? 4.430   21.345  47.534  1.00 72.04  ? 239 ASN A CG  1 
ATOM   1732 O  OD1 . ASN A 1 260 ? 5.360   22.151  47.509  1.00 71.87  ? 239 ASN A OD1 1 
ATOM   1733 N  ND2 . ASN A 1 260 ? 3.204   21.653  47.127  1.00 76.83  ? 239 ASN A ND2 1 
ATOM   1734 N  N   . LYS A 1 261 ? 5.656   16.839  47.227  1.00 69.72  ? 240 LYS A N   1 
ATOM   1735 C  CA  . LYS A 1 261 ? 5.603   15.456  47.695  1.00 68.64  ? 240 LYS A CA  1 
ATOM   1736 C  C   . LYS A 1 261 ? 6.319   14.538  46.714  1.00 67.76  ? 240 LYS A C   1 
ATOM   1737 O  O   . LYS A 1 261 ? 5.789   13.514  46.279  1.00 65.77  ? 240 LYS A O   1 
ATOM   1738 C  CB  . LYS A 1 261 ? 4.156   15.015  47.891  1.00 66.45  ? 240 LYS A CB  1 
ATOM   1739 C  CG  . LYS A 1 261 ? 3.363   15.904  48.837  1.00 74.05  ? 240 LYS A CG  1 
ATOM   1740 C  CD  . LYS A 1 261 ? 1.876   15.598  48.774  1.00 72.75  ? 240 LYS A CD  1 
ATOM   1741 C  CE  . LYS A 1 261 ? 1.562   14.205  49.287  1.00 74.12  ? 240 LYS A CE  1 
ATOM   1742 N  NZ  . LYS A 1 261 ? 0.175   13.816  48.939  1.00 83.65  ? 240 LYS A NZ  1 
ATOM   1743 N  N   . ALA A 1 262 ? 7.549   14.908  46.349  1.00 64.91  ? 241 ALA A N   1 
ATOM   1744 C  CA  . ALA A 1 262 ? 8.272   14.180  45.311  1.00 63.19  ? 241 ALA A CA  1 
ATOM   1745 C  C   . ALA A 1 262 ? 8.342   12.686  45.605  1.00 58.77  ? 241 ALA A C   1 
ATOM   1746 O  O   . ALA A 1 262 ? 8.279   11.862  44.686  1.00 57.74  ? 241 ALA A O   1 
ATOM   1747 C  CB  . ALA A 1 262 ? 9.681   14.756  45.159  1.00 59.00  ? 241 ALA A CB  1 
ATOM   1748 N  N   . GLY A 1 263 ? 8.476   12.315  46.880  1.00 58.97  ? 242 GLY A N   1 
ATOM   1749 C  CA  . GLY A 1 263 ? 8.607   10.906  47.218  1.00 57.93  ? 242 GLY A CA  1 
ATOM   1750 C  C   . GLY A 1 263 ? 7.356   10.102  46.918  1.00 60.59  ? 242 GLY A C   1 
ATOM   1751 O  O   . GLY A 1 263 ? 7.435   8.989   46.390  1.00 61.67  ? 242 GLY A O   1 
ATOM   1752 N  N   . VAL A 1 264 ? 6.186   10.645  47.261  1.00 60.33  ? 243 VAL A N   1 
ATOM   1753 C  CA  . VAL A 1 264 ? 4.933   9.926   47.047  1.00 61.11  ? 243 VAL A CA  1 
ATOM   1754 C  C   . VAL A 1 264 ? 4.531   9.957   45.576  1.00 60.80  ? 243 VAL A C   1 
ATOM   1755 O  O   . VAL A 1 264 ? 3.992   8.977   45.050  1.00 60.47  ? 243 VAL A O   1 
ATOM   1756 C  CB  . VAL A 1 264 ? 3.828   10.504  47.949  1.00 63.33  ? 243 VAL A CB  1 
ATOM   1757 C  CG1 . VAL A 1 264 ? 2.477   9.919   47.571  1.00 64.32  ? 243 VAL A CG1 1 
ATOM   1758 C  CG2 . VAL A 1 264 ? 4.141   10.225  49.412  1.00 63.65  ? 243 VAL A CG2 1 
ATOM   1759 N  N   . SER A 1 265 ? 4.773   11.080  44.895  1.00 61.00  ? 244 SER A N   1 
ATOM   1760 C  CA  . SER A 1 265 ? 4.455   11.164  43.473  1.00 60.76  ? 244 SER A CA  1 
ATOM   1761 C  C   . SER A 1 265 ? 5.254   10.143  42.677  1.00 58.75  ? 244 SER A C   1 
ATOM   1762 O  O   . SER A 1 265 ? 4.736   9.537   41.730  1.00 58.96  ? 244 SER A O   1 
ATOM   1763 C  CB  . SER A 1 265 ? 4.729   12.577  42.957  1.00 61.34  ? 244 SER A CB  1 
ATOM   1764 O  OG  . SER A 1 265 ? 3.858   13.519  43.556  1.00 68.68  ? 244 SER A OG  1 
ATOM   1765 N  N   . ASN A 1 266 ? 6.520   9.939   43.046  1.00 57.94  ? 245 ASN A N   1 
ATOM   1766 C  CA  . ASN A 1 266 ? 7.348   8.968   42.342  1.00 61.26  ? 245 ASN A CA  1 
ATOM   1767 C  C   . ASN A 1 266 ? 6.778   7.561   42.472  1.00 59.24  ? 245 ASN A C   1 
ATOM   1768 O  O   . ASN A 1 266 ? 6.717   6.814   41.488  1.00 56.10  ? 245 ASN A O   1 
ATOM   1769 C  CB  . ASN A 1 266 ? 8.779   9.013   42.877  1.00 54.30  ? 245 ASN A CB  1 
ATOM   1770 C  CG  . ASN A 1 266 ? 9.717   8.119   42.097  1.00 62.33  ? 245 ASN A CG  1 
ATOM   1771 O  OD1 . ASN A 1 266 ? 9.535   7.907   40.897  1.00 56.72  ? 245 ASN A OD1 1 
ATOM   1772 N  ND2 . ASN A 1 266 ? 10.724  7.580   42.775  1.00 62.41  ? 245 ASN A ND2 1 
ATOM   1773 N  N   . LEU A 1 267 ? 6.356   7.180   43.680  1.00 57.58  ? 246 LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 267 ? 5.772   5.857   43.875  1.00 59.28  ? 246 LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 267 ? 4.457   5.707   43.118  1.00 59.05  ? 246 LEU A C   1 
ATOM   1776 O  O   . LEU A 1 267 ? 4.086   4.588   42.743  1.00 57.26  ? 246 LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 267 ? 5.565   5.595   45.367  1.00 66.92  ? 246 LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 267 ? 6.845   5.424   46.191  1.00 64.18  ? 246 LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 267 ? 6.579   5.689   47.665  1.00 61.69  ? 246 LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 267 ? 7.426   4.029   45.997  1.00 54.63  ? 246 LEU A CD2 1 
ATOM   1781 N  N   . LEU A 1 268 ? 3.742   6.811   42.883  1.00 58.49  ? 247 LEU A N   1 
ATOM   1782 C  CA  . LEU A 1 268 ? 2.514   6.739   42.100  1.00 59.37  ? 247 LEU A CA  1 
ATOM   1783 C  C   . LEU A 1 268 ? 2.797   6.598   40.610  1.00 61.58  ? 247 LEU A C   1 
ATOM   1784 O  O   . LEU A 1 268 ? 2.028   5.944   39.899  1.00 61.46  ? 247 LEU A O   1 
ATOM   1785 C  CB  . LEU A 1 268 ? 1.645   7.975   42.347  1.00 61.33  ? 247 LEU A CB  1 
ATOM   1786 C  CG  . LEU A 1 268 ? 1.029   8.136   43.740  1.00 63.20  ? 247 LEU A CG  1 
ATOM   1787 C  CD1 . LEU A 1 268 ? 0.010   9.264   43.750  1.00 69.36  ? 247 LEU A CD1 1 
ATOM   1788 C  CD2 . LEU A 1 268 ? 0.374   6.849   44.214  1.00 67.71  ? 247 LEU A CD2 1 
ATOM   1789 N  N   . ASP A 1 269 ? 3.874   7.210   40.116  1.00 57.80  ? 248 ASP A N   1 
ATOM   1790 C  CA  . ASP A 1 269 ? 4.240   7.020   38.717  1.00 66.12  ? 248 ASP A CA  1 
ATOM   1791 C  C   . ASP A 1 269 ? 4.684   5.586   38.458  1.00 59.98  ? 248 ASP A C   1 
ATOM   1792 O  O   . ASP A 1 269 ? 4.311   4.988   37.443  1.00 56.04  ? 248 ASP A O   1 
ATOM   1793 C  CB  . ASP A 1 269 ? 5.340   8.003   38.327  1.00 58.74  ? 248 ASP A CB  1 
ATOM   1794 C  CG  . ASP A 1 269 ? 4.851   9.433   38.287  1.00 72.10  ? 248 ASP A CG  1 
ATOM   1795 O  OD1 . ASP A 1 269 ? 3.792   9.685   37.672  1.00 67.90  ? 248 ASP A OD1 1 
ATOM   1796 O  OD2 . ASP A 1 269 ? 5.520   10.302  38.880  1.00 70.48  ? 248 ASP A OD2 1 
ATOM   1797 N  N   . ILE A 1 270 ? 5.480   5.020   39.368  1.00 60.53  ? 249 ILE A N   1 
ATOM   1798 C  CA  . ILE A 1 270 ? 5.907   3.631   39.226  1.00 63.52  ? 249 ILE A CA  1 
ATOM   1799 C  C   . ILE A 1 270 ? 4.696   2.708   39.243  1.00 58.32  ? 249 ILE A C   1 
ATOM   1800 O  O   . ILE A 1 270 ? 4.568   1.802   38.412  1.00 60.46  ? 249 ILE A O   1 
ATOM   1801 C  CB  . ILE A 1 270 ? 6.909   3.263   40.336  1.00 55.19  ? 249 ILE A CB  1 
ATOM   1802 C  CG1 . ILE A 1 270 ? 8.145   4.161   40.255  1.00 61.14  ? 249 ILE A CG1 1 
ATOM   1803 C  CG2 . ILE A 1 270 ? 7.294   1.792   40.239  1.00 50.43  ? 249 ILE A CG2 1 
ATOM   1804 C  CD1 . ILE A 1 270 ? 9.150   3.936   41.370  1.00 70.19  ? 249 ILE A CD1 1 
ATOM   1805 N  N   . LEU A 1 271 ? 3.787   2.930   40.193  1.00 61.49  ? 250 LEU A N   1 
ATOM   1806 C  CA  . LEU A 1 271 ? 2.595   2.094   40.291  1.00 63.12  ? 250 LEU A CA  1 
ATOM   1807 C  C   . LEU A 1 271 ? 1.727   2.234   39.047  1.00 64.67  ? 250 LEU A C   1 
ATOM   1808 O  O   . LEU A 1 271 ? 1.168   1.248   38.556  1.00 67.38  ? 250 LEU A O   1 
ATOM   1809 C  CB  . LEU A 1 271 ? 1.812   2.465   41.551  1.00 62.72  ? 250 LEU A CB  1 
ATOM   1810 C  CG  . LEU A 1 271 ? 0.865   1.423   42.149  1.00 59.55  ? 250 LEU A CG  1 
ATOM   1811 C  CD1 . LEU A 1 271 ? 1.564   0.085   42.340  1.00 65.50  ? 250 LEU A CD1 1 
ATOM   1812 C  CD2 . LEU A 1 271 ? 0.318   1.930   43.475  1.00 60.22  ? 250 LEU A CD2 1 
ATOM   1813 N  N   . SER A 1 272 ? 1.607   3.454   38.521  1.00 62.35  ? 251 SER A N   1 
ATOM   1814 C  CA  . SER A 1 272 ? 0.832   3.662   37.305  1.00 66.08  ? 251 SER A CA  1 
ATOM   1815 C  C   . SER A 1 272 ? 1.478   2.983   36.107  1.00 66.16  ? 251 SER A C   1 
ATOM   1816 O  O   . SER A 1 272 ? 0.778   2.586   35.168  1.00 73.68  ? 251 SER A O   1 
ATOM   1817 C  CB  . SER A 1 272 ? 0.676   5.159   37.036  1.00 70.09  ? 251 SER A CB  1 
ATOM   1818 O  OG  . SER A 1 272 ? 0.119   5.389   35.753  1.00 79.53  ? 251 SER A OG  1 
ATOM   1819 N  N   . ALA A 1 273 ? 2.804   2.846   36.118  1.00 60.89  ? 252 ALA A N   1 
ATOM   1820 C  CA  . ALA A 1 273 ? 3.506   2.269   34.978  1.00 65.79  ? 252 ALA A CA  1 
ATOM   1821 C  C   . ALA A 1 273 ? 3.360   0.751   34.939  1.00 70.17  ? 252 ALA A C   1 
ATOM   1822 O  O   . ALA A 1 273 ? 3.061   0.177   33.886  1.00 68.15  ? 252 ALA A O   1 
ATOM   1823 C  CB  . ALA A 1 273 ? 4.982   2.668   35.023  1.00 67.42  ? 252 ALA A CB  1 
ATOM   1824 N  N   . VAL A 1 274 ? 3.561   0.087   36.079  1.00 66.11  ? 253 VAL A N   1 
ATOM   1825 C  CA  . VAL A 1 274 ? 3.495   -1.372  36.112  1.00 63.79  ? 253 VAL A CA  1 
ATOM   1826 C  C   . VAL A 1 274 ? 2.093   -1.849  35.756  1.00 69.60  ? 253 VAL A C   1 
ATOM   1827 O  O   . VAL A 1 274 ? 1.916   -2.779  34.961  1.00 77.51  ? 253 VAL A O   1 
ATOM   1828 C  CB  . VAL A 1 274 ? 3.925   -1.898  37.494  1.00 60.23  ? 253 VAL A CB  1 
ATOM   1829 C  CG1 . VAL A 1 274 ? 3.822   -3.422  37.543  1.00 59.29  ? 253 VAL A CG1 1 
ATOM   1830 C  CG2 . VAL A 1 274 ? 5.334   -1.442  37.833  1.00 60.71  ? 253 VAL A CG2 1 
ATOM   1831 N  N   . THR A 1 275 ? 1.076   -1.212  36.335  1.00 67.12  ? 254 THR A N   1 
ATOM   1832 C  CA  . THR A 1 275 ? -0.283  -1.734  36.294  1.00 79.57  ? 254 THR A CA  1 
ATOM   1833 C  C   . THR A 1 275 ? -1.154  -1.094  35.221  1.00 81.72  ? 254 THR A C   1 
ATOM   1834 O  O   . THR A 1 275 ? -2.162  -1.692  34.830  1.00 82.49  ? 254 THR A O   1 
ATOM   1835 C  CB  . THR A 1 275 ? -0.966  -1.539  37.656  1.00 71.15  ? 254 THR A CB  1 
ATOM   1836 O  OG1 . THR A 1 275 ? -1.599  -0.255  37.693  1.00 80.58  ? 254 THR A OG1 1 
ATOM   1837 C  CG2 . THR A 1 275 ? 0.049   -1.630  38.797  1.00 71.10  ? 254 THR A CG2 1 
ATOM   1838 N  N   . GLY A 1 276 ? -0.802  0.099   34.746  1.00 81.14  ? 255 GLY A N   1 
ATOM   1839 C  CA  . GLY A 1 276 ? -1.579  0.787   33.739  1.00 78.79  ? 255 GLY A CA  1 
ATOM   1840 C  C   . GLY A 1 276 ? -2.711  1.636   34.274  1.00 85.96  ? 255 GLY A C   1 
ATOM   1841 O  O   . GLY A 1 276 ? -3.323  2.384   33.499  1.00 88.78  ? 255 GLY A O   1 
ATOM   1842 N  N   . GLN A 1 277 ? -3.012  1.547   35.568  1.00 91.64  ? 256 GLN A N   1 
ATOM   1843 C  CA  . GLN A 1 277 ? -4.069  2.365   36.146  1.00 97.38  ? 256 GLN A CA  1 
ATOM   1844 C  C   . GLN A 1 277 ? -3.703  3.840   36.053  1.00 96.01  ? 256 GLN A C   1 
ATOM   1845 O  O   . GLN A 1 277 ? -2.568  4.235   36.331  1.00 87.91  ? 256 GLN A O   1 
ATOM   1846 C  CB  . GLN A 1 277 ? -4.301  1.982   37.608  1.00 94.30  ? 256 GLN A CB  1 
ATOM   1847 C  CG  . GLN A 1 277 ? -4.688  0.531   37.829  1.00 93.65  ? 256 GLN A CG  1 
ATOM   1848 C  CD  . GLN A 1 277 ? -4.842  0.193   39.300  1.00 91.22  ? 256 GLN A CD  1 
ATOM   1849 O  OE1 . GLN A 1 277 ? -5.701  0.745   39.988  1.00 93.22  ? 256 GLN A OE1 1 
ATOM   1850 N  NE2 . GLN A 1 277 ? -4.002  -0.710  39.791  1.00 89.27  ? 256 GLN A NE2 1 
ATOM   1851 N  N   . SER A 1 278 ? -4.675  4.660   35.661  1.00 92.31  ? 257 SER A N   1 
ATOM   1852 C  CA  . SER A 1 278 ? -4.456  6.097   35.635  1.00 88.99  ? 257 SER A CA  1 
ATOM   1853 C  C   . SER A 1 278 ? -4.244  6.612   37.054  1.00 88.28  ? 257 SER A C   1 
ATOM   1854 O  O   . SER A 1 278 ? -4.820  6.101   38.018  1.00 87.55  ? 257 SER A O   1 
ATOM   1855 C  CB  . SER A 1 278 ? -5.636  6.811   34.978  1.00 96.82  ? 257 SER A CB  1 
ATOM   1856 O  OG  . SER A 1 278 ? -5.245  8.080   34.484  1.00 95.33  ? 257 SER A OG  1 
ATOM   1857 N  N   . ILE A 1 279 ? -3.391  7.632   37.177  1.00 91.53  ? 258 ILE A N   1 
ATOM   1858 C  CA  . ILE A 1 279 ? -2.989  8.101   38.505  1.00 87.56  ? 258 ILE A CA  1 
ATOM   1859 C  C   . ILE A 1 279 ? -4.187  8.547   39.329  1.00 88.58  ? 258 ILE A C   1 
ATOM   1860 O  O   . ILE A 1 279 ? -4.255  8.200   40.517  1.00 87.63  ? 258 ILE A O   1 
ATOM   1861 C  CB  . ILE A 1 279 ? -1.903  9.178   38.380  1.00 81.84  ? 258 ILE A CB  1 
ATOM   1862 C  CG1 . ILE A 1 279 ? -0.637  8.559   37.776  1.00 84.62  ? 258 ILE A CG1 1 
ATOM   1863 C  CG2 . ILE A 1 279 ? -1.609  9.804   39.742  1.00 89.49  ? 258 ILE A CG2 1 
ATOM   1864 C  CD1 . ILE A 1 279 ? 0.535   9.506   37.660  1.00 68.26  ? 258 ILE A CD1 1 
ATOM   1865 N  N   . PRO A 1 280 ? -5.155  9.300   38.797  1.00 91.24  ? 259 PRO A N   1 
ATOM   1866 C  CA  . PRO A 1 280 ? -6.312  9.672   39.629  1.00 99.85  ? 259 PRO A CA  1 
ATOM   1867 C  C   . PRO A 1 280 ? -7.062  8.474   40.182  1.00 93.36  ? 259 PRO A C   1 
ATOM   1868 O  O   . PRO A 1 280 ? -7.694  8.585   41.240  1.00 91.81  ? 259 PRO A O   1 
ATOM   1869 C  CB  . PRO A 1 280 ? -7.182  10.498  38.671  1.00 92.09  ? 259 PRO A CB  1 
ATOM   1870 C  CG  . PRO A 1 280 ? -6.223  11.046  37.672  1.00 106.39 ? 259 PRO A CG  1 
ATOM   1871 C  CD  . PRO A 1 280 ? -5.171  9.984   37.491  1.00 90.40  ? 259 PRO A CD  1 
ATOM   1872 N  N   . GLU A 1 281 ? -7.015  7.327   39.495  1.00 98.42  ? 260 GLU A N   1 
ATOM   1873 C  CA  . GLU A 1 281 ? -7.626  6.120   40.041  1.00 95.16  ? 260 GLU A CA  1 
ATOM   1874 C  C   . GLU A 1 281 ? -6.945  5.711   41.340  1.00 92.23  ? 260 GLU A C   1 
ATOM   1875 O  O   . GLU A 1 281 ? -7.610  5.301   42.297  1.00 91.87  ? 260 GLU A O   1 
ATOM   1876 C  CB  . GLU A 1 281 ? -7.549  4.970   39.034  1.00 95.21  ? 260 GLU A CB  1 
ATOM   1877 C  CG  . GLU A 1 281 ? -7.826  5.348   37.591  1.00 97.24  ? 260 GLU A CG  1 
ATOM   1878 C  CD  . GLU A 1 281 ? -7.773  4.151   36.657  1.00 97.66  ? 260 GLU A CD  1 
ATOM   1879 O  OE1 . GLU A 1 281 ? -7.579  3.018   37.147  1.00 91.53  ? 260 GLU A OE1 1 
ATOM   1880 O  OE2 . GLU A 1 281 ? -7.922  4.343   35.432  1.00 103.30 ? 260 GLU A OE2 1 
ATOM   1881 N  N   . LEU A 1 282 ? -5.613  5.803   41.383  1.00 111.67 ? 261 LEU A N   1 
ATOM   1882 C  CA  . LEU A 1 282 ? -4.881  5.450   42.594  1.00 116.77 ? 261 LEU A CA  1 
ATOM   1883 C  C   . LEU A 1 282 ? -5.071  6.490   43.689  1.00 106.55 ? 261 LEU A C   1 
ATOM   1884 O  O   . LEU A 1 282 ? -5.082  6.141   44.874  1.00 99.68  ? 261 LEU A O   1 
ATOM   1885 C  CB  . LEU A 1 282 ? -3.396  5.281   42.276  1.00 89.96  ? 261 LEU A CB  1 
ATOM   1886 C  CG  . LEU A 1 282 ? -3.052  4.163   41.290  1.00 91.21  ? 261 LEU A CG  1 
ATOM   1887 C  CD1 . LEU A 1 282 ? -1.590  4.247   40.888  1.00 94.68  ? 261 LEU A CD1 1 
ATOM   1888 C  CD2 . LEU A 1 282 ? -3.367  2.801   41.886  1.00 92.31  ? 261 LEU A CD2 1 
ATOM   1889 N  N   . GLU A 1 283 ? -5.206  7.767   43.322  1.00 98.23  ? 262 GLU A N   1 
ATOM   1890 C  CA  . GLU A 1 283 ? -5.566  8.775   44.311  1.00 96.22  ? 262 GLU A CA  1 
ATOM   1891 C  C   . GLU A 1 283 ? -6.896  8.441   44.967  1.00 97.85  ? 262 GLU A C   1 
ATOM   1892 O  O   . GLU A 1 283 ? -7.096  8.720   46.154  1.00 100.68 ? 262 GLU A O   1 
ATOM   1893 C  CB  . GLU A 1 283 ? -5.636  10.156  43.660  1.00 94.72  ? 262 GLU A CB  1 
ATOM   1894 C  CG  . GLU A 1 283 ? -4.294  10.846  43.491  1.00 89.83  ? 262 GLU A CG  1 
ATOM   1895 C  CD  . GLU A 1 283 ? -4.423  12.190  42.800  1.00 93.56  ? 262 GLU A CD  1 
ATOM   1896 O  OE1 . GLU A 1 283 ? -5.274  12.312  41.894  1.00 93.78  ? 262 GLU A OE1 1 
ATOM   1897 O  OE2 . GLU A 1 283 ? -3.684  13.126  43.167  1.00 89.58  ? 262 GLU A OE2 1 
ATOM   1898 N  N   . GLN A 1 284 ? -7.815  7.845   44.208  1.00 101.23 ? 263 GLN A N   1 
ATOM   1899 C  CA  . GLN A 1 284 ? -9.113  7.462   44.746  1.00 107.31 ? 263 GLN A CA  1 
ATOM   1900 C  C   . GLN A 1 284 ? -9.050  6.129   45.479  1.00 105.71 ? 263 GLN A C   1 
ATOM   1901 O  O   . GLN A 1 284 ? -9.835  5.896   46.405  1.00 108.38 ? 263 GLN A O   1 
ATOM   1902 C  CB  . GLN A 1 284 ? -10.129 7.400   43.609  1.00 108.79 ? 263 GLN A CB  1 
ATOM   1903 C  CG  . GLN A 1 284 ? -11.573 7.362   44.049  1.00 114.57 ? 263 GLN A CG  1 
ATOM   1904 C  CD  . GLN A 1 284 ? -12.522 7.506   42.878  1.00 119.47 ? 263 GLN A CD  1 
ATOM   1905 O  OE1 . GLN A 1 284 ? -12.407 8.438   42.082  1.00 123.30 ? 263 GLN A OE1 1 
ATOM   1906 N  NE2 . GLN A 1 284 ? -13.456 6.572   42.754  1.00 119.31 ? 263 GLN A NE2 1 
ATOM   1907 N  N   . HIS A 1 285 ? -8.130  5.248   45.077  1.00 93.41  ? 264 HIS A N   1 
ATOM   1908 C  CA  . HIS A 1 285 ? -7.943  3.970   45.755  1.00 90.15  ? 264 HIS A CA  1 
ATOM   1909 C  C   . HIS A 1 285 ? -7.221  4.134   47.085  1.00 87.52  ? 264 HIS A C   1 
ATOM   1910 O  O   . HIS A 1 285 ? -7.422  3.327   47.999  1.00 86.00  ? 264 HIS A O   1 
ATOM   1911 C  CB  . HIS A 1 285 ? -7.162  3.014   44.846  1.00 87.45  ? 264 HIS A CB  1 
ATOM   1912 C  CG  . HIS A 1 285 ? -6.733  1.745   45.517  1.00 84.90  ? 264 HIS A CG  1 
ATOM   1913 N  ND1 . HIS A 1 285 ? -7.516  0.611   45.537  1.00 80.18  ? 264 HIS A ND1 1 
ATOM   1914 C  CD2 . HIS A 1 285 ? -5.595  1.427   46.180  1.00 84.35  ? 264 HIS A CD2 1 
ATOM   1915 C  CE1 . HIS A 1 285 ? -6.882  -0.348  46.189  1.00 80.21  ? 264 HIS A CE1 1 
ATOM   1916 N  NE2 . HIS A 1 285 ? -5.715  0.121   46.590  1.00 78.74  ? 264 HIS A NE2 1 
ATOM   1917 N  N   . PHE A 1 286 ? -6.388  5.168   47.208  1.00 90.02  ? 265 PHE A N   1 
ATOM   1918 C  CA  . PHE A 1 286 ? -5.602  5.423   48.408  1.00 84.81  ? 265 PHE A CA  1 
ATOM   1919 C  C   . PHE A 1 286 ? -6.152  6.581   49.232  1.00 107.92 ? 265 PHE A C   1 
ATOM   1920 O  O   . PHE A 1 286 ? -5.455  7.083   50.121  1.00 105.42 ? 265 PHE A O   1 
ATOM   1921 C  CB  . PHE A 1 286 ? -4.141  5.690   48.031  1.00 85.91  ? 265 PHE A CB  1 
ATOM   1922 C  CG  . PHE A 1 286 ? -3.377  4.451   47.659  1.00 84.98  ? 265 PHE A CG  1 
ATOM   1923 C  CD1 . PHE A 1 286 ? -2.931  3.581   48.639  1.00 82.76  ? 265 PHE A CD1 1 
ATOM   1924 C  CD2 . PHE A 1 286 ? -3.108  4.155   46.333  1.00 89.24  ? 265 PHE A CD2 1 
ATOM   1925 C  CE1 . PHE A 1 286 ? -2.233  2.439   48.306  1.00 75.76  ? 265 PHE A CE1 1 
ATOM   1926 C  CE2 . PHE A 1 286 ? -2.409  3.012   45.994  1.00 87.02  ? 265 PHE A CE2 1 
ATOM   1927 C  CZ  . PHE A 1 286 ? -1.970  2.154   46.982  1.00 74.82  ? 265 PHE A CZ  1 
ATOM   1928 N  N   . GLU A 1 287 ? -7.374  7.030   48.948  1.00 95.48  ? 266 GLU A N   1 
ATOM   1929 C  CA  . GLU A 1 287 ? -8.030  8.021   49.791  1.00 95.18  ? 266 GLU A CA  1 
ATOM   1930 C  C   . GLU A 1 287 ? -8.186  7.465   51.201  1.00 98.63  ? 266 GLU A C   1 
ATOM   1931 O  O   . GLU A 1 287 ? -8.918  6.493   51.412  1.00 100.32 ? 266 GLU A O   1 
ATOM   1932 C  CB  . GLU A 1 287 ? -9.393  8.411   49.210  1.00 101.12 ? 266 GLU A CB  1 
ATOM   1933 C  CG  . GLU A 1 287 ? -9.357  9.634   48.309  1.00 103.49 ? 266 GLU A CG  1 
ATOM   1934 C  CD  . GLU A 1 287 ? -10.492 9.652   47.301  1.00 102.46 ? 266 GLU A CD  1 
ATOM   1935 O  OE1 . GLU A 1 287 ? -11.515 8.974   47.534  1.00 94.61  ? 266 GLU A OE1 1 
ATOM   1936 O  OE2 . GLU A 1 287 ? -10.354 10.337  46.266  1.00 103.84 ? 266 GLU A OE2 1 
ATOM   1937 N  N   . GLY A 1 288 ? -7.500  8.066   52.171  1.00 97.87  ? 267 GLY A N   1 
ATOM   1938 C  CA  . GLY A 1 288 ? -7.539  7.599   53.540  1.00 92.65  ? 267 GLY A CA  1 
ATOM   1939 C  C   . GLY A 1 288 ? -6.546  6.508   53.878  1.00 99.39  ? 267 GLY A C   1 
ATOM   1940 O  O   . GLY A 1 288 ? -6.481  6.093   55.043  1.00 93.55  ? 267 GLY A O   1 
ATOM   1941 N  N   . LYS A 1 289 ? -5.779  6.027   52.905  1.00 92.05  ? 268 LYS A N   1 
ATOM   1942 C  CA  . LYS A 1 289 ? -4.747  5.031   53.147  1.00 86.66  ? 268 LYS A CA  1 
ATOM   1943 C  C   . LYS A 1 289 ? -3.425  5.711   53.489  1.00 89.36  ? 268 LYS A C   1 
ATOM   1944 O  O   . LYS A 1 289 ? -3.184  6.870   53.142  1.00 84.64  ? 268 LYS A O   1 
ATOM   1945 C  CB  . LYS A 1 289 ? -4.575  4.127   51.925  1.00 87.86  ? 268 LYS A CB  1 
ATOM   1946 N  N   . MET A 1 290 ? -2.563  4.969   54.182  1.00 82.55  ? 269 MET A N   1 
ATOM   1947 C  CA  . MET A 1 290 ? -1.285  5.495   54.633  1.00 80.62  ? 269 MET A CA  1 
ATOM   1948 C  C   . MET A 1 290 ? -0.211  5.268   53.567  1.00 78.76  ? 269 MET A C   1 
ATOM   1949 O  O   . MET A 1 290 ? -0.450  4.661   52.521  1.00 75.86  ? 269 MET A O   1 
ATOM   1950 C  CB  . MET A 1 290 ? -0.886  4.854   55.963  1.00 83.11  ? 269 MET A CB  1 
ATOM   1951 C  CG  . MET A 1 290 ? -0.401  3.412   55.855  1.00 86.80  ? 269 MET A CG  1 
ATOM   1952 S  SD  . MET A 1 290 ? 0.069   2.700   57.446  1.00 112.86 ? 269 MET A SD  1 
ATOM   1953 C  CE  . MET A 1 290 ? 1.079   1.316   56.922  1.00 82.72  ? 269 MET A CE  1 
ATOM   1954 N  N   . TYR A 1 291 ? 0.997   5.769   53.840  1.00 81.08  ? 270 TYR A N   1 
ATOM   1955 C  CA  . TYR A 1 291 ? 2.098   5.589   52.897  1.00 80.83  ? 270 TYR A CA  1 
ATOM   1956 C  C   . TYR A 1 291 ? 2.568   4.140   52.863  1.00 78.17  ? 270 TYR A C   1 
ATOM   1957 O  O   . TYR A 1 291 ? 2.950   3.633   51.804  1.00 72.85  ? 270 TYR A O   1 
ATOM   1958 C  CB  . TYR A 1 291 ? 3.260   6.518   53.253  1.00 76.46  ? 270 TYR A CB  1 
ATOM   1959 C  CG  . TYR A 1 291 ? 2.978   7.988   53.025  1.00 80.39  ? 270 TYR A CG  1 
ATOM   1960 C  CD1 . TYR A 1 291 ? 2.040   8.401   52.088  1.00 80.52  ? 270 TYR A CD1 1 
ATOM   1961 C  CD2 . TYR A 1 291 ? 3.651   8.962   53.748  1.00 73.74  ? 270 TYR A CD2 1 
ATOM   1962 C  CE1 . TYR A 1 291 ? 1.779   9.738   51.879  1.00 75.80  ? 270 TYR A CE1 1 
ATOM   1963 C  CE2 . TYR A 1 291 ? 3.396   10.305  53.546  1.00 82.22  ? 270 TYR A CE2 1 
ATOM   1964 C  CZ  . TYR A 1 291 ? 2.458   10.687  52.610  1.00 78.16  ? 270 TYR A CZ  1 
ATOM   1965 O  OH  . TYR A 1 291 ? 2.193   12.020  52.398  1.00 84.05  ? 270 TYR A OH  1 
ATOM   1966 N  N   . GLY A 1 292 ? 2.556   3.459   54.011  1.00 76.92  ? 271 GLY A N   1 
ATOM   1967 C  CA  . GLY A 1 292 ? 2.954   2.062   54.036  1.00 72.29  ? 271 GLY A CA  1 
ATOM   1968 C  C   . GLY A 1 292 ? 2.061   1.175   53.191  1.00 79.92  ? 271 GLY A C   1 
ATOM   1969 O  O   . GLY A 1 292 ? 2.515   0.160   52.655  1.00 82.12  ? 271 GLY A O   1 
ATOM   1970 N  N   . HIS A 1 293 ? 0.778   1.525   53.079  1.00 77.14  ? 272 HIS A N   1 
ATOM   1971 C  CA  . HIS A 1 293 ? -0.101  0.797   52.170  1.00 75.06  ? 272 HIS A CA  1 
ATOM   1972 C  C   . HIS A 1 293 ? 0.359   0.957   50.727  1.00 76.30  ? 272 HIS A C   1 
ATOM   1973 O  O   . HIS A 1 293 ? 0.372   -0.010  49.958  1.00 73.70  ? 272 HIS A O   1 
ATOM   1974 C  CB  . HIS A 1 293 ? -1.541  1.285   52.324  1.00 78.81  ? 272 HIS A CB  1 
ATOM   1975 C  CG  . HIS A 1 293 ? -2.105  1.081   53.694  1.00 90.01  ? 272 HIS A CG  1 
ATOM   1976 N  ND1 . HIS A 1 293 ? -3.229  1.742   54.142  1.00 92.02  ? 272 HIS A ND1 1 
ATOM   1977 C  CD2 . HIS A 1 293 ? -1.701  0.291   54.717  1.00 94.12  ? 272 HIS A CD2 1 
ATOM   1978 C  CE1 . HIS A 1 293 ? -3.493  1.367   55.381  1.00 87.89  ? 272 HIS A CE1 1 
ATOM   1979 N  NE2 . HIS A 1 293 ? -2.580  0.488   55.754  1.00 88.95  ? 272 HIS A NE2 1 
ATOM   1980 N  N   . LEU A 1 294 ? 0.742   2.177   50.345  1.00 74.40  ? 273 LEU A N   1 
ATOM   1981 C  CA  . LEU A 1 294 ? 1.190   2.420   48.979  1.00 73.72  ? 273 LEU A CA  1 
ATOM   1982 C  C   . LEU A 1 294 ? 2.521   1.733   48.700  1.00 71.30  ? 273 LEU A C   1 
ATOM   1983 O  O   . LEU A 1 294 ? 2.740   1.228   47.595  1.00 64.16  ? 273 LEU A O   1 
ATOM   1984 C  CB  . LEU A 1 294 ? 1.290   3.924   48.735  1.00 73.32  ? 273 LEU A CB  1 
ATOM   1985 C  CG  . LEU A 1 294 ? 1.736   4.419   47.360  1.00 71.71  ? 273 LEU A CG  1 
ATOM   1986 C  CD1 . LEU A 1 294 ? 1.240   3.546   46.219  1.00 69.95  ? 273 LEU A CD1 1 
ATOM   1987 C  CD2 . LEU A 1 294 ? 1.219   5.830   47.199  1.00 79.97  ? 273 LEU A CD2 1 
ATOM   1988 N  N   . LYS A 1 295 ? 3.424   1.706   49.684  1.00 63.12  ? 274 LYS A N   1 
ATOM   1989 C  CA  . LYS A 1 295 ? 4.698   1.022   49.491  1.00 63.00  ? 274 LYS A CA  1 
ATOM   1990 C  C   . LYS A 1 295 ? 4.499   -0.480  49.338  1.00 67.20  ? 274 LYS A C   1 
ATOM   1991 O  O   . LYS A 1 295 ? 5.215   -1.131  48.568  1.00 57.32  ? 274 LYS A O   1 
ATOM   1992 C  CB  . LYS A 1 295 ? 5.640   1.319   50.656  1.00 65.31  ? 274 LYS A CB  1 
ATOM   1993 C  CG  . LYS A 1 295 ? 6.268   2.700   50.603  1.00 64.01  ? 274 LYS A CG  1 
ATOM   1994 C  CD  . LYS A 1 295 ? 7.213   2.913   51.767  1.00 66.46  ? 274 LYS A CD  1 
ATOM   1995 C  CE  . LYS A 1 295 ? 7.904   4.257   51.685  1.00 66.50  ? 274 LYS A CE  1 
ATOM   1996 N  NZ  . LYS A 1 295 ? 8.867   4.430   52.804  1.00 67.55  ? 274 LYS A NZ  1 
ATOM   1997 N  N   . GLY A 1 296 ? 3.549   -1.052  50.080  1.00 67.03  ? 275 GLY A N   1 
ATOM   1998 C  CA  . GLY A 1 296 ? 3.208   -2.449  49.883  1.00 73.17  ? 275 GLY A CA  1 
ATOM   1999 C  C   . GLY A 1 296 ? 2.602   -2.717  48.521  1.00 63.65  ? 275 GLY A C   1 
ATOM   2000 O  O   . GLY A 1 296 ? 2.795   -3.796  47.952  1.00 57.73  ? 275 GLY A O   1 
ATOM   2001 N  N   . GLU A 1 297 ? 1.858   -1.747  47.982  1.00 61.96  ? 276 GLU A N   1 
ATOM   2002 C  CA  . GLU A 1 297 ? 1.241   -1.922  46.672  1.00 60.66  ? 276 GLU A CA  1 
ATOM   2003 C  C   . GLU A 1 297 ? 2.274   -1.827  45.555  1.00 59.77  ? 276 GLU A C   1 
ATOM   2004 O  O   . GLU A 1 297 ? 2.241   -2.615  44.602  1.00 58.21  ? 276 GLU A O   1 
ATOM   2005 C  CB  . GLU A 1 297 ? 0.137   -0.883  46.481  1.00 62.14  ? 276 GLU A CB  1 
ATOM   2006 C  CG  . GLU A 1 297 ? -0.717  -1.109  45.245  1.00 67.68  ? 276 GLU A CG  1 
ATOM   2007 C  CD  . GLU A 1 297 ? -2.200  -0.911  45.502  1.00 74.38  ? 276 GLU A CD  1 
ATOM   2008 O  OE1 . GLU A 1 297 ? -2.624  -0.947  46.677  1.00 72.82  ? 276 GLU A OE1 1 
ATOM   2009 O  OE2 . GLU A 1 297 ? -2.947  -0.723  44.518  1.00 79.50  ? 276 GLU A OE2 1 
ATOM   2010 N  N   . VAL A 1 298 ? 3.197   -0.867  45.652  1.00 61.58  ? 277 VAL A N   1 
ATOM   2011 C  CA  . VAL A 1 298 ? 4.256   -0.753  44.653  1.00 62.58  ? 277 VAL A CA  1 
ATOM   2012 C  C   . VAL A 1 298 ? 5.173   -1.964  44.713  1.00 53.88  ? 277 VAL A C   1 
ATOM   2013 O  O   . VAL A 1 298 ? 5.543   -2.529  43.680  1.00 52.18  ? 277 VAL A O   1 
ATOM   2014 C  CB  . VAL A 1 298 ? 5.037   0.560   44.851  1.00 69.08  ? 277 VAL A CB  1 
ATOM   2015 C  CG1 . VAL A 1 298 ? 6.392   0.520   44.128  1.00 55.15  ? 277 VAL A CG1 1 
ATOM   2016 C  CG2 . VAL A 1 298 ? 4.216   1.738   44.353  1.00 69.82  ? 277 VAL A CG2 1 
ATOM   2017 N  N   . ALA A 1 299 ? 5.558   -2.382  45.920  1.00 55.88  ? 278 ALA A N   1 
ATOM   2018 C  CA  . ALA A 1 299 ? 6.482   -3.503  46.047  1.00 61.26  ? 278 ALA A CA  1 
ATOM   2019 C  C   . ALA A 1 299 ? 5.872   -4.780  45.487  1.00 58.42  ? 278 ALA A C   1 
ATOM   2020 O  O   . ALA A 1 299 ? 6.559   -5.563  44.822  1.00 55.02  ? 278 ALA A O   1 
ATOM   2021 C  CB  . ALA A 1 299 ? 6.883   -3.691  47.511  1.00 62.00  ? 278 ALA A CB  1 
ATOM   2022 N  N   . GLU A 1 300 ? 4.583   -5.008  45.747  1.00 60.79  ? 279 GLU A N   1 
ATOM   2023 C  CA  . GLU A 1 300 ? 3.924   -6.205  45.234  1.00 64.07  ? 279 GLU A CA  1 
ATOM   2024 C  C   . GLU A 1 300 ? 3.818   -6.169  43.713  1.00 64.66  ? 279 GLU A C   1 
ATOM   2025 O  O   . GLU A 1 300 ? 4.116   -7.161  43.038  1.00 61.77  ? 279 GLU A O   1 
ATOM   2026 C  CB  . GLU A 1 300 ? 2.539   -6.351  45.868  1.00 56.36  ? 279 GLU A CB  1 
ATOM   2027 N  N   . ALA A 1 301 ? 3.391   -5.033  43.153  1.00 57.66  ? 280 ALA A N   1 
ATOM   2028 C  CA  . ALA A 1 301 ? 3.221   -4.937  41.706  1.00 57.19  ? 280 ALA A CA  1 
ATOM   2029 C  C   . ALA A 1 301 ? 4.561   -5.028  40.987  1.00 56.02  ? 280 ALA A C   1 
ATOM   2030 O  O   . ALA A 1 301 ? 4.730   -5.828  40.060  1.00 55.19  ? 280 ALA A O   1 
ATOM   2031 C  CB  . ALA A 1 301 ? 2.513   -3.630  41.352  1.00 54.29  ? 280 ALA A CB  1 
ATOM   2032 N  N   . VAL A 1 302 ? 5.529   -4.217  41.415  1.00 55.45  ? 281 VAL A N   1 
ATOM   2033 C  CA  . VAL A 1 302 ? 6.875   -4.280  40.849  1.00 56.35  ? 281 VAL A CA  1 
ATOM   2034 C  C   . VAL A 1 302 ? 7.413   -5.699  40.948  1.00 55.06  ? 281 VAL A C   1 
ATOM   2035 O  O   . VAL A 1 302 ? 7.968   -6.243  39.988  1.00 49.82  ? 281 VAL A O   1 
ATOM   2036 C  CB  . VAL A 1 302 ? 7.797   -3.278  41.571  1.00 56.05  ? 281 VAL A CB  1 
ATOM   2037 C  CG1 . VAL A 1 302 ? 9.271   -3.663  41.427  1.00 59.31  ? 281 VAL A CG1 1 
ATOM   2038 C  CG2 . VAL A 1 302 ? 7.563   -1.868  41.048  1.00 51.55  ? 281 VAL A CG2 1 
ATOM   2039 N  N   . SER A 1 303 ? 7.247   -6.320  42.116  1.00 52.44  ? 282 SER A N   1 
ATOM   2040 C  CA  . SER A 1 303 ? 7.790   -7.657  42.322  1.00 51.78  ? 282 SER A CA  1 
ATOM   2041 C  C   . SER A 1 303 ? 7.161   -8.654  41.360  1.00 57.68  ? 282 SER A C   1 
ATOM   2042 O  O   . SER A 1 303 ? 7.850   -9.527  40.819  1.00 56.77  ? 282 SER A O   1 
ATOM   2043 C  CB  . SER A 1 303 ? 7.571   -8.088  43.772  1.00 61.25  ? 282 SER A CB  1 
ATOM   2044 O  OG  . SER A 1 303 ? 8.074   -9.391  44.006  1.00 68.35  ? 282 SER A OG  1 
ATOM   2045 N  N   . GLY A 1 304 ? 5.853   -8.535  41.125  1.00 54.47  ? 283 GLY A N   1 
ATOM   2046 C  CA  . GLY A 1 304 ? 5.197   -9.438  40.195  1.00 58.86  ? 283 GLY A CA  1 
ATOM   2047 C  C   . GLY A 1 304 ? 5.703   -9.277  38.775  1.00 57.58  ? 283 GLY A C   1 
ATOM   2048 O  O   . GLY A 1 304 ? 5.896   -10.262 38.058  1.00 53.88  ? 283 GLY A O   1 
ATOM   2049 N  N   . MET A 1 305 ? 5.917   -8.031  38.347  1.00 54.31  ? 284 MET A N   1 
ATOM   2050 C  CA  . MET A 1 305 ? 6.446   -7.794  37.008  1.00 56.89  ? 284 MET A CA  1 
ATOM   2051 C  C   . MET A 1 305 ? 7.848   -8.370  36.862  1.00 54.27  ? 284 MET A C   1 
ATOM   2052 O  O   . MET A 1 305 ? 8.180   -8.965  35.829  1.00 50.84  ? 284 MET A O   1 
ATOM   2053 C  CB  . MET A 1 305 ? 6.449   -6.296  36.704  1.00 57.07  ? 284 MET A CB  1 
ATOM   2054 C  CG  . MET A 1 305 ? 7.001   -5.953  35.329  1.00 59.19  ? 284 MET A CG  1 
ATOM   2055 S  SD  . MET A 1 305 ? 6.623   -4.269  34.807  1.00 63.19  ? 284 MET A SD  1 
ATOM   2056 C  CE  . MET A 1 305 ? 8.120   -3.428  35.298  1.00 53.62  ? 284 MET A CE  1 
ATOM   2057 N  N   . LEU A 1 306 ? 8.686   -8.206  37.887  1.00 53.57  ? 285 LEU A N   1 
ATOM   2058 C  CA  . LEU A 1 306 ? 10.056  -8.695  37.817  1.00 50.65  ? 285 LEU A CA  1 
ATOM   2059 C  C   . LEU A 1 306 ? 10.145  -10.210 37.925  1.00 54.34  ? 285 LEU A C   1 
ATOM   2060 O  O   . LEU A 1 306 ? 11.141  -10.789 37.481  1.00 52.17  ? 285 LEU A O   1 
ATOM   2061 C  CB  . LEU A 1 306 ? 10.903  -8.064  38.921  1.00 44.88  ? 285 LEU A CB  1 
ATOM   2062 C  CG  . LEU A 1 306 ? 11.618  -6.758  38.573  1.00 59.18  ? 285 LEU A CG  1 
ATOM   2063 C  CD1 . LEU A 1 306 ? 10.631  -5.617  38.418  1.00 64.91  ? 285 LEU A CD1 1 
ATOM   2064 C  CD2 . LEU A 1 306 ? 12.659  -6.434  39.633  1.00 53.45  ? 285 LEU A CD2 1 
ATOM   2065 N  N   . THR A 1 307 ? 9.147   -10.866 38.521  1.00 51.19  ? 286 THR A N   1 
ATOM   2066 C  CA  . THR A 1 307 ? 9.215   -12.316 38.658  1.00 52.35  ? 286 THR A CA  1 
ATOM   2067 C  C   . THR A 1 307 ? 8.867   -13.026 37.356  1.00 53.83  ? 286 THR A C   1 
ATOM   2068 O  O   . THR A 1 307 ? 9.424   -14.093 37.074  1.00 53.57  ? 286 THR A O   1 
ATOM   2069 C  CB  . THR A 1 307 ? 8.300   -12.789 39.790  1.00 58.09  ? 286 THR A CB  1 
ATOM   2070 O  OG1 . THR A 1 307 ? 6.990   -12.231 39.631  1.00 60.77  ? 286 THR A OG1 1 
ATOM   2071 C  CG2 . THR A 1 307 ? 8.878   -12.371 41.140  1.00 56.76  ? 286 THR A CG2 1 
ATOM   2072 N  N   . GLU A 1 308 ? 7.960   -12.462 36.554  1.00 52.53  ? 287 GLU A N   1 
ATOM   2073 C  CA  . GLU A 1 308 ? 7.713   -13.026 35.231  1.00 56.17  ? 287 GLU A CA  1 
ATOM   2074 C  C   . GLU A 1 308 ? 8.896   -12.773 34.304  1.00 50.88  ? 287 GLU A C   1 
ATOM   2075 O  O   . GLU A 1 308 ? 9.313   -13.666 33.559  1.00 45.08  ? 287 GLU A O   1 
ATOM   2076 C  CB  . GLU A 1 308 ? 6.436   -12.439 34.629  1.00 57.91  ? 287 GLU A CB  1 
ATOM   2077 C  CG  . GLU A 1 308 ? 5.897   -13.241 33.448  1.00 65.23  ? 287 GLU A CG  1 
ATOM   2078 C  CD  . GLU A 1 308 ? 5.449   -12.367 32.291  1.00 69.29  ? 287 GLU A CD  1 
ATOM   2079 O  OE1 . GLU A 1 308 ? 4.607   -11.471 32.507  1.00 96.56  ? 287 GLU A OE1 1 
ATOM   2080 O  OE2 . GLU A 1 308 ? 5.946   -12.574 31.163  1.00 68.28  ? 287 GLU A OE2 1 
ATOM   2081 N  N   . LEU A 1 309 ? 9.446   -11.558 34.337  1.00 46.27  ? 288 LEU A N   1 
ATOM   2082 C  CA  . LEU A 1 309 ? 10.597  -11.241 33.500  1.00 53.00  ? 288 LEU A CA  1 
ATOM   2083 C  C   . LEU A 1 309 ? 11.806  -12.085 33.880  1.00 42.18  ? 288 LEU A C   1 
ATOM   2084 O  O   . LEU A 1 309 ? 12.526  -12.579 33.006  1.00 39.73  ? 288 LEU A O   1 
ATOM   2085 C  CB  . LEU A 1 309 ? 10.928  -9.754  33.613  1.00 52.87  ? 288 LEU A CB  1 
ATOM   2086 C  CG  . LEU A 1 309 ? 10.607  -8.888  32.394  1.00 58.08  ? 288 LEU A CG  1 
ATOM   2087 C  CD1 . LEU A 1 309 ? 9.163   -9.066  31.942  1.00 61.06  ? 288 LEU A CD1 1 
ATOM   2088 C  CD2 . LEU A 1 309 ? 10.889  -7.426  32.713  1.00 55.55  ? 288 LEU A CD2 1 
ATOM   2089 N  N   . GLN A 1 310 ? 12.050  -12.254 35.180  1.00 44.39  ? 289 GLN A N   1 
ATOM   2090 C  CA  . GLN A 1 310 ? 13.203  -13.035 35.613  1.00 44.72  ? 289 GLN A CA  1 
ATOM   2091 C  C   . GLN A 1 310 ? 13.014  -14.517 35.326  1.00 42.07  ? 289 GLN A C   1 
ATOM   2092 O  O   . GLN A 1 310 ? 13.997  -15.234 35.113  1.00 38.57  ? 289 GLN A O   1 
ATOM   2093 C  CB  . GLN A 1 310 ? 13.458  -12.818 37.103  1.00 41.21  ? 289 GLN A CB  1 
ATOM   2094 C  CG  . GLN A 1 310 ? 13.989  -11.439 37.446  1.00 50.50  ? 289 GLN A CG  1 
ATOM   2095 C  CD  . GLN A 1 310 ? 13.936  -11.153 38.935  1.00 61.23  ? 289 GLN A CD  1 
ATOM   2096 O  OE1 . GLN A 1 310 ? 13.913  -12.070 39.756  1.00 63.46  ? 289 GLN A OE1 1 
ATOM   2097 N  NE2 . GLN A 1 310 ? 13.902  -9.875  39.289  1.00 63.40  ? 289 GLN A NE2 1 
ATOM   2098 N  N   . GLU A 1 311 ? 11.771  -14.996 35.329  1.00 41.17  ? 290 GLU A N   1 
ATOM   2099 C  CA  . GLU A 1 311 ? 11.523  -16.390 34.984  1.00 42.26  ? 290 GLU A CA  1 
ATOM   2100 C  C   . GLU A 1 311 ? 11.932  -16.666 33.542  1.00 43.61  ? 290 GLU A C   1 
ATOM   2101 O  O   . GLU A 1 311 ? 12.607  -17.661 33.252  1.00 42.54  ? 290 GLU A O   1 
ATOM   2102 C  CB  . GLU A 1 311 ? 10.048  -16.724 35.214  1.00 48.78  ? 290 GLU A CB  1 
ATOM   2103 C  CG  . GLU A 1 311 ? 9.742   -18.211 35.268  1.00 56.61  ? 290 GLU A CG  1 
ATOM   2104 C  CD  . GLU A 1 311 ? 9.735   -18.853 33.897  1.00 64.36  ? 290 GLU A CD  1 
ATOM   2105 O  OE1 . GLU A 1 311 ? 9.202   -18.230 32.953  1.00 60.44  ? 290 GLU A OE1 1 
ATOM   2106 O  OE2 . GLU A 1 311 ? 10.270  -19.975 33.761  1.00 68.24  ? 290 GLU A OE2 1 
ATOM   2107 N  N   . ARG A 1 312 ? 11.543  -15.780 32.623  1.00 45.56  ? 291 ARG A N   1 
ATOM   2108 C  CA  . ARG A 1 312 ? 11.953  -15.928 31.231  1.00 39.16  ? 291 ARG A CA  1 
ATOM   2109 C  C   . ARG A 1 312 ? 13.455  -15.731 31.074  1.00 37.59  ? 291 ARG A C   1 
ATOM   2110 O  O   . ARG A 1 312 ? 14.102  -16.429 30.286  1.00 37.39  ? 291 ARG A O   1 
ATOM   2111 C  CB  . ARG A 1 312 ? 11.197  -14.931 30.356  1.00 39.51  ? 291 ARG A CB  1 
ATOM   2112 C  CG  . ARG A 1 312 ? 9.684   -14.982 30.499  1.00 44.45  ? 291 ARG A CG  1 
ATOM   2113 C  CD  . ARG A 1 312 ? 9.020   -14.026 29.524  1.00 42.02  ? 291 ARG A CD  1 
ATOM   2114 N  NE  . ARG A 1 312 ? 9.343   -14.364 28.143  1.00 48.81  ? 291 ARG A NE  1 
ATOM   2115 C  CZ  . ARG A 1 312 ? 9.200   -13.541 27.112  1.00 43.89  ? 291 ARG A CZ  1 
ATOM   2116 N  NH1 . ARG A 1 312 ? 8.749   -12.308 27.269  1.00 52.84  ? 291 ARG A NH1 1 
ATOM   2117 N  NH2 . ARG A 1 312 ? 9.518   -13.968 25.894  1.00 46.35  ? 291 ARG A NH2 1 
ATOM   2118 N  N   . TYR A 1 313 ? 14.025  -14.780 31.813  1.00 37.44  ? 292 TYR A N   1 
ATOM   2119 C  CA  . TYR A 1 313 ? 15.446  -14.489 31.675  1.00 36.07  ? 292 TYR A CA  1 
ATOM   2120 C  C   . TYR A 1 313 ? 16.297  -15.699 32.035  1.00 35.43  ? 292 TYR A C   1 
ATOM   2121 O  O   . TYR A 1 313 ? 17.207  -16.072 31.292  1.00 34.61  ? 292 TYR A O   1 
ATOM   2122 C  CB  . TYR A 1 313 ? 15.827  -13.299 32.551  1.00 36.01  ? 292 TYR A CB  1 
ATOM   2123 C  CG  . TYR A 1 313 ? 17.319  -13.125 32.674  1.00 34.91  ? 292 TYR A CG  1 
ATOM   2124 C  CD1 . TYR A 1 313 ? 18.039  -12.453 31.698  1.00 34.30  ? 292 TYR A CD1 1 
ATOM   2125 C  CD2 . TYR A 1 313 ? 18.011  -13.645 33.759  1.00 34.59  ? 292 TYR A CD2 1 
ATOM   2126 C  CE1 . TYR A 1 313 ? 19.402  -12.297 31.801  1.00 33.40  ? 292 TYR A CE1 1 
ATOM   2127 C  CE2 . TYR A 1 313 ? 19.373  -13.494 33.870  1.00 33.83  ? 292 TYR A CE2 1 
ATOM   2128 C  CZ  . TYR A 1 313 ? 20.064  -12.819 32.885  1.00 34.47  ? 292 TYR A CZ  1 
ATOM   2129 O  OH  . TYR A 1 313 ? 21.423  -12.662 32.984  1.00 32.66  ? 292 TYR A OH  1 
ATOM   2130 N  N   . HIS A 1 314 ? 16.032  -16.314 33.188  1.00 35.89  ? 293 HIS A N   1 
ATOM   2131 C  CA  . HIS A 1 314 ? 16.849  -17.445 33.610  1.00 37.29  ? 293 HIS A CA  1 
ATOM   2132 C  C   . HIS A 1 314 ? 16.681  -18.629 32.670  1.00 40.19  ? 293 HIS A C   1 
ATOM   2133 O  O   . HIS A 1 314 ? 17.619  -19.412 32.485  1.00 39.34  ? 293 HIS A O   1 
ATOM   2134 C  CB  . HIS A 1 314 ? 16.502  -17.837 35.046  1.00 37.86  ? 293 HIS A CB  1 
ATOM   2135 C  CG  . HIS A 1 314 ? 17.042  -16.888 36.070  1.00 41.96  ? 293 HIS A CG  1 
ATOM   2136 N  ND1 . HIS A 1 314 ? 16.253  -16.311 37.042  1.00 45.48  ? 293 HIS A ND1 1 
ATOM   2137 C  CD2 . HIS A 1 314 ? 18.294  -16.412 36.271  1.00 42.21  ? 293 HIS A CD2 1 
ATOM   2138 C  CE1 . HIS A 1 314 ? 16.995  -15.520 37.796  1.00 48.36  ? 293 HIS A CE1 1 
ATOM   2139 N  NE2 . HIS A 1 314 ? 18.237  -15.564 37.350  1.00 45.58  ? 293 HIS A NE2 1 
ATOM   2140 N  N   . ARG A 1 315 ? 15.504  -18.771 32.065  1.00 38.38  ? 294 ARG A N   1 
ATOM   2141 C  CA  . ARG A 1 315 ? 15.298  -19.830 31.086  1.00 37.44  ? 294 ARG A CA  1 
ATOM   2142 C  C   . ARG A 1 315 ? 16.151  -19.600 29.844  1.00 37.70  ? 294 ARG A C   1 
ATOM   2143 O  O   . ARG A 1 315 ? 16.851  -20.508 29.384  1.00 40.41  ? 294 ARG A O   1 
ATOM   2144 C  CB  . ARG A 1 315 ? 13.817  -19.910 30.725  1.00 42.28  ? 294 ARG A CB  1 
ATOM   2145 C  CG  . ARG A 1 315 ? 13.462  -21.049 29.802  1.00 46.19  ? 294 ARG A CG  1 
ATOM   2146 C  CD  . ARG A 1 315 ? 12.160  -21.718 30.219  1.00 55.99  ? 294 ARG A CD  1 
ATOM   2147 N  NE  . ARG A 1 315 ? 11.122  -20.757 30.576  1.00 58.30  ? 294 ARG A NE  1 
ATOM   2148 C  CZ  . ARG A 1 315 ? 10.487  -19.978 29.710  1.00 54.78  ? 294 ARG A CZ  1 
ATOM   2149 N  NH1 . ARG A 1 315 ? 10.785  -19.990 28.421  1.00 50.00  ? 294 ARG A NH1 1 
ATOM   2150 N  NH2 . ARG A 1 315 ? 9.531   -19.165 30.150  1.00 51.28  ? 294 ARG A NH2 1 
ATOM   2151 N  N   . PHE A 1 316 ? 16.106  -18.385 29.289  1.00 35.22  ? 295 PHE A N   1 
ATOM   2152 C  CA  . PHE A 1 316 ? 16.920  -18.073 28.120  1.00 34.46  ? 295 PHE A CA  1 
ATOM   2153 C  C   . PHE A 1 316 ? 18.406  -18.131 28.451  1.00 34.02  ? 295 PHE A C   1 
ATOM   2154 O  O   . PHE A 1 316 ? 19.201  -18.688 27.686  1.00 32.86  ? 295 PHE A O   1 
ATOM   2155 C  CB  . PHE A 1 316 ? 16.564  -16.685 27.585  1.00 37.71  ? 295 PHE A CB  1 
ATOM   2156 C  CG  . PHE A 1 316 ? 15.171  -16.577 27.031  1.00 37.93  ? 295 PHE A CG  1 
ATOM   2157 C  CD1 . PHE A 1 316 ? 14.618  -17.603 26.286  1.00 45.36  ? 295 PHE A CD1 1 
ATOM   2158 C  CD2 . PHE A 1 316 ? 14.420  -15.436 27.247  1.00 36.34  ? 295 PHE A CD2 1 
ATOM   2159 C  CE1 . PHE A 1 316 ? 13.340  -17.494 25.771  1.00 49.61  ? 295 PHE A CE1 1 
ATOM   2160 C  CE2 . PHE A 1 316 ? 13.142  -15.322 26.736  1.00 37.59  ? 295 PHE A CE2 1 
ATOM   2161 C  CZ  . PHE A 1 316 ? 12.602  -16.351 25.998  1.00 45.67  ? 295 PHE A CZ  1 
ATOM   2162 N  N   . ARG A 1 317 ? 18.794  -17.568 29.597  1.00 34.53  ? 296 ARG A N   1 
ATOM   2163 C  CA  . ARG A 1 317 ? 20.210  -17.397 29.901  1.00 37.46  ? 296 ARG A CA  1 
ATOM   2164 C  C   . ARG A 1 317 ? 20.877  -18.726 30.205  1.00 36.90  ? 296 ARG A C   1 
ATOM   2165 O  O   . ARG A 1 317 ? 22.093  -18.863 30.028  1.00 39.55  ? 296 ARG A O   1 
ATOM   2166 C  CB  . ARG A 1 317 ? 20.379  -16.438 31.081  1.00 34.78  ? 296 ARG A CB  1 
ATOM   2167 C  CG  . ARG A 1 317 ? 21.826  -16.114 31.428  1.00 35.88  ? 296 ARG A CG  1 
ATOM   2168 C  CD  . ARG A 1 317 ? 22.532  -15.411 30.277  1.00 36.10  ? 296 ARG A CD  1 
ATOM   2169 N  NE  . ARG A 1 317 ? 23.941  -15.162 30.560  1.00 32.53  ? 296 ARG A NE  1 
ATOM   2170 C  CZ  . ARG A 1 317 ? 24.912  -16.044 30.366  1.00 35.01  ? 296 ARG A CZ  1 
ATOM   2171 N  NH1 . ARG A 1 317 ? 24.664  -17.255 29.892  1.00 40.07  ? 296 ARG A NH1 1 
ATOM   2172 N  NH2 . ARG A 1 317 ? 26.165  -15.702 30.653  1.00 31.61  ? 296 ARG A NH2 1 
ATOM   2173 N  N   . ASN A 1 318 ? 20.105  -19.704 30.665  1.00 40.45  ? 297 ASN A N   1 
ATOM   2174 C  CA  . ASN A 1 318 ? 20.614  -21.034 30.956  1.00 38.39  ? 297 ASN A CA  1 
ATOM   2175 C  C   . ASN A 1 318 ? 20.639  -21.928 29.724  1.00 48.02  ? 297 ASN A C   1 
ATOM   2176 O  O   . ASN A 1 318 ? 21.108  -23.067 29.813  1.00 50.80  ? 297 ASN A O   1 
ATOM   2177 C  CB  . ASN A 1 318 ? 19.764  -21.690 32.047  1.00 41.77  ? 297 ASN A CB  1 
ATOM   2178 C  CG  . ASN A 1 318 ? 20.487  -22.819 32.745  1.00 50.24  ? 297 ASN A CG  1 
ATOM   2179 O  OD1 . ASN A 1 318 ? 21.675  -22.714 33.056  1.00 52.54  ? 297 ASN A OD1 1 
ATOM   2180 N  ND2 . ASN A 1 318 ? 19.775  -23.911 32.996  1.00 50.97  ? 297 ASN A ND2 1 
ATOM   2181 N  N   . ASP A 1 319 ? 20.143  -21.446 28.588  1.00 35.73  ? 298 ASP A N   1 
ATOM   2182 C  CA  . ASP A 1 319 ? 20.158  -22.191 27.334  1.00 38.93  ? 298 ASP A CA  1 
ATOM   2183 C  C   . ASP A 1 319 ? 21.126  -21.480 26.391  1.00 42.88  ? 298 ASP A C   1 
ATOM   2184 O  O   . ASP A 1 319 ? 20.729  -20.689 25.533  1.00 38.21  ? 298 ASP A O   1 
ATOM   2185 C  CB  . ASP A 1 319 ? 18.751  -22.287 26.747  1.00 39.11  ? 298 ASP A CB  1 
ATOM   2186 C  CG  . ASP A 1 319 ? 18.655  -23.302 25.625  1.00 43.42  ? 298 ASP A CG  1 
ATOM   2187 O  OD1 . ASP A 1 319 ? 19.706  -23.850 25.226  1.00 43.23  ? 298 ASP A OD1 1 
ATOM   2188 O  OD2 . ASP A 1 319 ? 17.528  -23.557 25.148  1.00 41.28  ? 298 ASP A OD2 1 
ATOM   2189 N  N   . GLU A 1 320 ? 22.415  -21.795 26.544  1.00 44.66  ? 299 GLU A N   1 
ATOM   2190 C  CA  . GLU A 1 320 ? 23.439  -21.131 25.747  1.00 44.97  ? 299 GLU A CA  1 
ATOM   2191 C  C   . GLU A 1 320 ? 23.376  -21.555 24.287  1.00 44.89  ? 299 GLU A C   1 
ATOM   2192 O  O   . GLU A 1 320 ? 23.767  -20.784 23.405  1.00 42.91  ? 299 GLU A O   1 
ATOM   2193 C  CB  . GLU A 1 320 ? 24.828  -21.418 26.318  1.00 52.36  ? 299 GLU A CB  1 
ATOM   2194 C  CG  . GLU A 1 320 ? 25.479  -20.210 26.983  1.00 60.51  ? 299 GLU A CG  1 
ATOM   2195 C  CD  . GLU A 1 320 ? 26.920  -20.466 27.387  1.00 71.84  ? 299 GLU A CD  1 
ATOM   2196 O  OE1 . GLU A 1 320 ? 27.747  -19.537 27.269  1.00 88.75  ? 299 GLU A OE1 1 
ATOM   2197 O  OE2 . GLU A 1 320 ? 27.226  -21.598 27.818  1.00 82.43  ? 299 GLU A OE2 1 
ATOM   2198 N  N   . ALA A 1 321 ? 22.904  -22.772 24.013  1.00 41.47  ? 300 ALA A N   1 
ATOM   2199 C  CA  . ALA A 1 321 ? 22.709  -23.181 22.627  1.00 36.53  ? 300 ALA A CA  1 
ATOM   2200 C  C   . ALA A 1 321 ? 21.677  -22.296 21.943  1.00 33.55  ? 300 ALA A C   1 
ATOM   2201 O  O   . ALA A 1 321 ? 21.863  -21.887 20.791  1.00 33.00  ? 300 ALA A O   1 
ATOM   2202 C  CB  . ALA A 1 321 ? 22.286  -24.647 22.564  1.00 38.78  ? 300 ALA A CB  1 
ATOM   2203 N  N   . PHE A 1 322 ? 20.581  -21.987 22.641  1.00 38.79  ? 301 PHE A N   1 
ATOM   2204 C  CA  . PHE A 1 322 ? 19.573  -21.097 22.077  1.00 40.27  ? 301 PHE A CA  1 
ATOM   2205 C  C   . PHE A 1 322 ? 20.144  -19.708 21.823  1.00 34.93  ? 301 PHE A C   1 
ATOM   2206 O  O   . PHE A 1 322 ? 19.885  -19.106 20.776  1.00 35.24  ? 301 PHE A O   1 
ATOM   2207 C  CB  . PHE A 1 322 ? 18.365  -21.014 23.011  1.00 43.01  ? 301 PHE A CB  1 
ATOM   2208 C  CG  . PHE A 1 322 ? 17.346  -19.994 22.591  1.00 44.26  ? 301 PHE A CG  1 
ATOM   2209 C  CD1 . PHE A 1 322 ? 16.701  -20.102 21.372  1.00 44.52  ? 301 PHE A CD1 1 
ATOM   2210 C  CD2 . PHE A 1 322 ? 17.030  -18.929 23.417  1.00 43.44  ? 301 PHE A CD2 1 
ATOM   2211 C  CE1 . PHE A 1 322 ? 15.763  -19.163 20.982  1.00 50.83  ? 301 PHE A CE1 1 
ATOM   2212 C  CE2 . PHE A 1 322 ? 16.089  -17.992 23.033  1.00 45.61  ? 301 PHE A CE2 1 
ATOM   2213 C  CZ  . PHE A 1 322 ? 15.456  -18.110 21.814  1.00 45.83  ? 301 PHE A CZ  1 
ATOM   2214 N  N   . LEU A 1 323 ? 20.921  -19.179 22.770  1.00 34.92  ? 302 LEU A N   1 
ATOM   2215 C  CA  . LEU A 1 323 ? 21.505  -17.856 22.581  1.00 35.38  ? 302 LEU A CA  1 
ATOM   2216 C  C   . LEU A 1 323 ? 22.470  -17.852 21.404  1.00 34.79  ? 302 LEU A C   1 
ATOM   2217 O  O   . LEU A 1 323 ? 22.537  -16.875 20.649  1.00 33.32  ? 302 LEU A O   1 
ATOM   2218 C  CB  . LEU A 1 323 ? 22.217  -17.404 23.855  1.00 36.25  ? 302 LEU A CB  1 
ATOM   2219 C  CG  . LEU A 1 323 ? 21.366  -17.329 25.125  1.00 41.98  ? 302 LEU A CG  1 
ATOM   2220 C  CD1 . LEU A 1 323 ? 22.245  -17.020 26.327  1.00 35.84  ? 302 LEU A CD1 1 
ATOM   2221 C  CD2 . LEU A 1 323 ? 20.269  -16.288 24.987  1.00 37.67  ? 302 LEU A CD2 1 
ATOM   2222 N  N   . ASN A 1 324 ? 23.235  -18.932 21.240  1.00 34.96  ? 303 ASN A N   1 
ATOM   2223 C  CA  . ASN A 1 324 ? 24.175  -19.008 20.128  1.00 37.95  ? 303 ASN A CA  1 
ATOM   2224 C  C   . ASN A 1 324 ? 23.448  -18.986 18.791  1.00 38.13  ? 303 ASN A C   1 
ATOM   2225 O  O   . ASN A 1 324 ? 23.895  -18.330 17.845  1.00 33.59  ? 303 ASN A O   1 
ATOM   2226 C  CB  . ASN A 1 324 ? 25.033  -20.268 20.243  1.00 36.83  ? 303 ASN A CB  1 
ATOM   2227 C  CG  . ASN A 1 324 ? 26.365  -20.011 20.927  1.00 45.66  ? 303 ASN A CG  1 
ATOM   2228 O  OD1 . ASN A 1 324 ? 26.753  -18.864 21.160  1.00 46.01  ? 303 ASN A OD1 1 
ATOM   2229 N  ND2 . ASN A 1 324 ? 27.080  -21.084 21.241  1.00 55.47  ? 303 ASN A ND2 1 
ATOM   2230 N  N   . GLN A 1 325 ? 22.329  -19.705 18.688  1.00 35.61  ? 304 GLN A N   1 
ATOM   2231 C  CA  . GLN A 1 325 ? 21.593  -19.722 17.430  1.00 34.37  ? 304 GLN A CA  1 
ATOM   2232 C  C   . GLN A 1 325 ? 20.919  -18.383 17.162  1.00 35.77  ? 304 GLN A C   1 
ATOM   2233 O  O   . GLN A 1 325 ? 20.790  -17.980 16.001  1.00 31.11  ? 304 GLN A O   1 
ATOM   2234 C  CB  . GLN A 1 325 ? 20.559  -20.844 17.434  1.00 33.19  ? 304 GLN A CB  1 
ATOM   2235 C  CG  . GLN A 1 325 ? 20.330  -21.457 16.054  1.00 51.18  ? 304 GLN A CG  1 
ATOM   2236 C  CD  . GLN A 1 325 ? 21.559  -22.187 15.519  1.00 54.12  ? 304 GLN A CD  1 
ATOM   2237 O  OE1 . GLN A 1 325 ? 21.991  -21.951 14.391  1.00 49.05  ? 304 GLN A OE1 1 
ATOM   2238 N  NE2 . GLN A 1 325 ? 22.122  -23.080 16.330  1.00 67.05  ? 304 GLN A NE2 1 
ATOM   2239 N  N   . VAL A 1 326 ? 20.480  -17.685 18.212  1.00 29.40  ? 305 VAL A N   1 
ATOM   2240 C  CA  . VAL A 1 326 ? 19.931  -16.346 18.023  1.00 33.36  ? 305 VAL A CA  1 
ATOM   2241 C  C   . VAL A 1 326 ? 21.010  -15.397 17.521  1.00 27.83  ? 305 VAL A C   1 
ATOM   2242 O  O   . VAL A 1 326 ? 20.765  -14.570 16.636  1.00 27.12  ? 305 VAL A O   1 
ATOM   2243 C  CB  . VAL A 1 326 ? 19.291  -15.838 19.327  1.00 35.78  ? 305 VAL A CB  1 
ATOM   2244 C  CG1 . VAL A 1 326 ? 19.026  -14.340 19.242  1.00 32.44  ? 305 VAL A CG1 1 
ATOM   2245 C  CG2 . VAL A 1 326 ? 18.001  -16.591 19.611  1.00 42.36  ? 305 VAL A CG2 1 
ATOM   2246 N  N   . MET A 1 327 ? 22.217  -15.486 18.087  1.00 31.43  ? 306 MET A N   1 
ATOM   2247 C  CA  . MET A 1 327 ? 23.305  -14.619 17.644  1.00 28.78  ? 306 MET A CA  1 
ATOM   2248 C  C   . MET A 1 327 ? 23.736  -14.960 16.224  1.00 30.46  ? 306 MET A C   1 
ATOM   2249 O  O   . MET A 1 327 ? 24.112  -14.070 15.452  1.00 27.28  ? 306 MET A O   1 
ATOM   2250 C  CB  . MET A 1 327 ? 24.494  -14.731 18.597  1.00 29.14  ? 306 MET A CB  1 
ATOM   2251 C  CG  . MET A 1 327 ? 24.310  -13.998 19.924  1.00 31.69  ? 306 MET A CG  1 
ATOM   2252 S  SD  . MET A 1 327 ? 25.748  -14.157 21.007  1.00 28.16  ? 306 MET A SD  1 
ATOM   2253 C  CE  . MET A 1 327 ? 25.881  -15.939 21.158  1.00 38.79  ? 306 MET A CE  1 
ATOM   2254 N  N   . LYS A 1 328 ? 23.714  -16.244 15.868  1.00 30.76  ? 307 LYS A N   1 
ATOM   2255 C  CA  . LYS A 1 328 ? 24.050  -16.626 14.503  1.00 28.99  ? 307 LYS A CA  1 
ATOM   2256 C  C   . LYS A 1 328 ? 23.055  -16.025 13.521  1.00 27.78  ? 307 LYS A C   1 
ATOM   2257 O  O   . LYS A 1 328 ? 23.436  -15.274 12.621  1.00 30.60  ? 307 LYS A O   1 
ATOM   2258 C  CB  . LYS A 1 328 ? 24.087  -18.147 14.382  1.00 32.85  ? 307 LYS A CB  1 
ATOM   2259 C  CG  . LYS A 1 328 ? 24.637  -18.644 13.055  1.00 41.21  ? 307 LYS A CG  1 
ATOM   2260 C  CD  . LYS A 1 328 ? 24.657  -20.165 13.005  1.00 43.89  ? 307 LYS A CD  1 
ATOM   2261 C  CE  . LYS A 1 328 ? 25.235  -20.675 11.687  1.00 51.15  ? 307 LYS A CE  1 
ATOM   2262 N  NZ  . LYS A 1 328 ? 26.720  -20.526 11.625  1.00 50.64  ? 307 LYS A NZ  1 
ATOM   2263 N  N   . GLU A 1 329 ? 21.761  -16.298 13.725  1.00 30.02  ? 308 GLU A N   1 
ATOM   2264 C  CA  . GLU A 1 329 ? 20.728  -15.792 12.823  1.00 35.51  ? 308 GLU A CA  1 
ATOM   2265 C  C   . GLU A 1 329 ? 20.734  -14.270 12.776  1.00 32.30  ? 308 GLU A C   1 
ATOM   2266 O  O   . GLU A 1 329 ? 20.645  -13.668 11.700  1.00 29.52  ? 308 GLU A O   1 
ATOM   2267 C  CB  . GLU A 1 329 ? 19.353  -16.301 13.268  1.00 37.36  ? 308 GLU A CB  1 
ATOM   2268 C  CG  . GLU A 1 329 ? 18.174  -15.740 12.464  1.00 56.51  ? 308 GLU A CG  1 
ATOM   2269 C  CD  . GLU A 1 329 ? 16.830  -15.930 13.158  1.00 70.91  ? 308 GLU A CD  1 
ATOM   2270 O  OE1 . GLU A 1 329 ? 16.812  -16.255 14.367  1.00 61.18  ? 308 GLU A OE1 1 
ATOM   2271 O  OE2 . GLU A 1 329 ? 15.788  -15.745 12.492  1.00 69.94  ? 308 GLU A OE2 1 
ATOM   2272 N  N   . GLY A 1 330 ? 20.820  -13.630 13.943  1.00 33.53  ? 309 GLY A N   1 
ATOM   2273 C  CA  . GLY A 1 330 ? 20.806  -12.177 13.977  1.00 29.97  ? 309 GLY A CA  1 
ATOM   2274 C  C   . GLY A 1 330 ? 21.974  -11.568 13.230  1.00 26.66  ? 309 GLY A C   1 
ATOM   2275 O  O   . GLY A 1 330 ? 21.826  -10.552 12.548  1.00 29.08  ? 309 GLY A O   1 
ATOM   2276 N  N   . ALA A 1 331 ? 23.155  -12.177 13.350  1.00 28.71  ? 310 ALA A N   1 
ATOM   2277 C  CA  . ALA A 1 331 ? 24.317  -11.639 12.651  1.00 29.88  ? 310 ALA A CA  1 
ATOM   2278 C  C   . ALA A 1 331 ? 24.233  -11.875 11.147  1.00 29.62  ? 310 ALA A C   1 
ATOM   2279 O  O   . ALA A 1 331 ? 24.731  -11.052 10.373  1.00 27.83  ? 310 ALA A O   1 
ATOM   2280 C  CB  . ALA A 1 331 ? 25.603  -12.242 13.216  1.00 26.42  ? 310 ALA A CB  1 
ATOM   2281 N  N   . GLU A 1 332 ? 23.621  -12.985 10.708  1.00 30.25  ? 311 GLU A N   1 
ATOM   2282 C  CA  . GLU A 1 332 ? 23.462  -13.205 9.271   1.00 30.81  ? 311 GLU A CA  1 
ATOM   2283 C  C   . GLU A 1 332 ? 22.502  -12.187 8.667   1.00 29.53  ? 311 GLU A C   1 
ATOM   2284 O  O   . GLU A 1 332 ? 22.766  -11.638 7.592   1.00 29.14  ? 311 GLU A O   1 
ATOM   2285 C  CB  . GLU A 1 332 ? 22.959  -14.622 8.975   1.00 30.15  ? 311 GLU A CB  1 
ATOM   2286 C  CG  . GLU A 1 332 ? 23.475  -15.699 9.904   1.00 41.44  ? 311 GLU A CG  1 
ATOM   2287 C  CD  . GLU A 1 332 ? 23.298  -17.103 9.353   1.00 53.60  ? 311 GLU A CD  1 
ATOM   2288 O  OE1 . GLU A 1 332 ? 22.185  -17.427 8.890   1.00 54.51  ? 311 GLU A OE1 1 
ATOM   2289 O  OE2 . GLU A 1 332 ? 24.275  -17.885 9.395   1.00 54.59  ? 311 GLU A OE2 1 
ATOM   2290 N  N   . LYS A 1 333 ? 21.377  -11.932 9.340   1.00 32.88  ? 312 LYS A N   1 
ATOM   2291 C  CA  . LYS A 1 333 ? 20.447  -10.917 8.859   1.00 33.66  ? 312 LYS A CA  1 
ATOM   2292 C  C   . LYS A 1 333 ? 21.096  -9.540  8.856   1.00 32.93  ? 312 LYS A C   1 
ATOM   2293 O  O   . LYS A 1 333 ? 20.951  -8.778  7.894   1.00 33.73  ? 312 LYS A O   1 
ATOM   2294 C  CB  . LYS A 1 333 ? 19.186  -10.900 9.721   1.00 35.31  ? 312 LYS A CB  1 
ATOM   2295 C  CG  . LYS A 1 333 ? 18.243  -12.069 9.480   1.00 43.87  ? 312 LYS A CG  1 
ATOM   2296 C  CD  . LYS A 1 333 ? 16.833  -11.775 9.997   1.00 47.46  ? 312 LYS A CD  1 
ATOM   2297 C  CE  . LYS A 1 333 ? 16.695  -12.041 11.490  1.00 49.36  ? 312 LYS A CE  1 
ATOM   2298 N  NZ  . LYS A 1 333 ? 15.362  -11.600 12.012  1.00 47.46  ? 312 LYS A NZ  1 
ATOM   2299 N  N   . ALA A 1 334 ? 21.812  -9.200  9.928   1.00 30.39  ? 313 ALA A N   1 
ATOM   2300 C  CA  . ALA A 1 334 ? 22.436  -7.885  10.008  1.00 29.45  ? 313 ALA A CA  1 
ATOM   2301 C  C   . ALA A 1 334 ? 23.480  -7.709  8.916   1.00 31.14  ? 313 ALA A C   1 
ATOM   2302 O  O   . ALA A 1 334 ? 23.550  -6.653  8.280   1.00 28.03  ? 313 ALA A O   1 
ATOM   2303 C  CB  . ALA A 1 334 ? 23.063  -7.680  11.388  1.00 23.72  ? 313 ALA A CB  1 
ATOM   2304 N  N   . SER A 1 335 ? 24.299  -8.736  8.682   1.00 30.39  ? 314 SER A N   1 
ATOM   2305 C  CA  . SER A 1 335 ? 25.308  -8.648  7.633   1.00 34.37  ? 314 SER A CA  1 
ATOM   2306 C  C   . SER A 1 335 ? 24.675  -8.554  6.253   1.00 31.14  ? 314 SER A C   1 
ATOM   2307 O  O   . SER A 1 335 ? 25.219  -7.882  5.373   1.00 28.37  ? 314 SER A O   1 
ATOM   2308 C  CB  . SER A 1 335 ? 26.248  -9.852  7.698   1.00 31.68  ? 314 SER A CB  1 
ATOM   2309 O  OG  . SER A 1 335 ? 27.265  -9.640  8.661   1.00 38.90  ? 314 SER A OG  1 
ATOM   2310 N  N   . ALA A 1 336 ? 23.538  -9.216  6.041   1.00 27.43  ? 315 ALA A N   1 
ATOM   2311 C  CA  . ALA A 1 336 ? 22.900  -9.172  4.730   1.00 30.80  ? 315 ALA A CA  1 
ATOM   2312 C  C   . ALA A 1 336 ? 22.468  -7.754  4.375   1.00 27.78  ? 315 ALA A C   1 
ATOM   2313 O  O   . ALA A 1 336 ? 22.659  -7.306  3.238   1.00 33.20  ? 315 ALA A O   1 
ATOM   2314 C  CB  . ALA A 1 336 ? 21.706  -10.123 4.692   1.00 30.30  ? 315 ALA A CB  1 
ATOM   2315 N  N   . HIS A 1 337 ? 21.878  -7.033  5.330   1.00 28.51  ? 316 HIS A N   1 
ATOM   2316 C  CA  . HIS A 1 337 ? 21.504  -5.645  5.074   1.00 31.36  ? 316 HIS A CA  1 
ATOM   2317 C  C   . HIS A 1 337 ? 22.723  -4.732  5.074   1.00 26.28  ? 316 HIS A C   1 
ATOM   2318 O  O   . HIS A 1 337 ? 22.862  -3.872  4.197   1.00 27.08  ? 316 HIS A O   1 
ATOM   2319 C  CB  . HIS A 1 337 ? 20.489  -5.169  6.114   1.00 34.09  ? 316 HIS A CB  1 
ATOM   2320 C  CG  . HIS A 1 337 ? 19.131  -5.780  5.958   1.00 42.83  ? 316 HIS A CG  1 
ATOM   2321 N  ND1 . HIS A 1 337 ? 18.762  -6.947  6.591   1.00 48.28  ? 316 HIS A ND1 1 
ATOM   2322 C  CD2 . HIS A 1 337 ? 18.055  -5.388  5.235   1.00 55.15  ? 316 HIS A CD2 1 
ATOM   2323 C  CE1 . HIS A 1 337 ? 17.516  -7.246  6.268   1.00 49.51  ? 316 HIS A CE1 1 
ATOM   2324 N  NE2 . HIS A 1 337 ? 17.065  -6.316  5.445   1.00 54.69  ? 316 HIS A NE2 1 
ATOM   2325 N  N   . ALA A 1 338 ? 23.623  -4.916  6.044   1.00 27.59  ? 317 ALA A N   1 
ATOM   2326 C  CA  . ALA A 1 338 ? 24.750  -4.002  6.193   1.00 25.74  ? 317 ALA A CA  1 
ATOM   2327 C  C   . ALA A 1 338 ? 25.669  -4.058  4.983   1.00 25.31  ? 317 ALA A C   1 
ATOM   2328 O  O   . ALA A 1 338 ? 26.210  -3.033  4.558   1.00 22.88  ? 317 ALA A O   1 
ATOM   2329 C  CB  . ALA A 1 338 ? 25.527  -4.330  7.469   1.00 21.95  ? 317 ALA A CB  1 
ATOM   2330 N  N   . SER A 1 339 ? 25.864  -5.249  4.416   1.00 23.51  ? 318 SER A N   1 
ATOM   2331 C  CA  . SER A 1 339 ? 26.779  -5.376  3.288   1.00 21.94  ? 318 SER A CA  1 
ATOM   2332 C  C   . SER A 1 339 ? 26.271  -4.625  2.066   1.00 21.01  ? 318 SER A C   1 
ATOM   2333 O  O   . SER A 1 339 ? 27.073  -4.099  1.287   1.00 23.99  ? 318 SER A O   1 
ATOM   2334 C  CB  . SER A 1 339 ? 27.003  -6.850  2.955   1.00 23.84  ? 318 SER A CB  1 
ATOM   2335 O  OG  . SER A 1 339 ? 25.792  -7.474  2.577   1.00 35.12  ? 318 SER A OG  1 
ATOM   2336 N  N   . LYS A 1 340 ? 24.956  -4.565  1.870   1.00 25.47  ? 319 LYS A N   1 
ATOM   2337 C  CA  . LYS A 1 340 ? 24.428  -3.795  0.751   1.00 30.79  ? 319 LYS A CA  1 
ATOM   2338 C  C   . LYS A 1 340 ? 24.846  -2.336  0.863   1.00 28.77  ? 319 LYS A C   1 
ATOM   2339 O  O   . LYS A 1 340 ? 25.329  -1.738  -0.105  1.00 24.69  ? 319 LYS A O   1 
ATOM   2340 C  CB  . LYS A 1 340 ? 22.906  -3.916  0.701   1.00 32.47  ? 319 LYS A CB  1 
ATOM   2341 C  CG  . LYS A 1 340 ? 22.403  -5.332  0.476   1.00 35.58  ? 319 LYS A CG  1 
ATOM   2342 C  CD  . LYS A 1 340 ? 20.889  -5.359  0.319   1.00 41.05  ? 319 LYS A CD  1 
ATOM   2343 C  CE  . LYS A 1 340 ? 20.352  -6.780  0.304   1.00 52.56  ? 319 LYS A CE  1 
ATOM   2344 N  NZ  . LYS A 1 340 ? 18.911  -6.829  -0.076  1.00 59.48  ? 319 LYS A NZ  1 
ATOM   2345 N  N   . THR A 1 341 ? 24.688  -1.750  2.051   1.00 23.94  ? 320 THR A N   1 
ATOM   2346 C  CA  . THR A 1 341 ? 25.064  -0.353  2.226   1.00 24.35  ? 320 THR A CA  1 
ATOM   2347 C  C   . THR A 1 341 ? 26.572  -0.164  2.121   1.00 19.71  ? 320 THR A C   1 
ATOM   2348 O  O   . THR A 1 341 ? 27.036  0.797   1.501   1.00 20.59  ? 320 THR A O   1 
ATOM   2349 C  CB  . THR A 1 341 ? 24.554  0.169   3.568   1.00 25.03  ? 320 THR A CB  1 
ATOM   2350 O  OG1 . THR A 1 341 ? 23.123  0.204   3.548   1.00 24.91  ? 320 THR A OG1 1 
ATOM   2351 C  CG2 . THR A 1 341 ? 25.102  1.570   3.841   1.00 21.96  ? 320 THR A CG2 1 
ATOM   2352 N  N   . LEU A 1 342 ? 27.356  -1.057  2.729   1.00 21.04  ? 321 LEU A N   1 
ATOM   2353 C  CA  . LEU A 1 342 ? 28.806  -0.889  2.698   1.00 22.45  ? 321 LEU A CA  1 
ATOM   2354 C  C   . LEU A 1 342 ? 29.340  -0.972  1.273   1.00 25.37  ? 321 LEU A C   1 
ATOM   2355 O  O   . LEU A 1 342 ? 30.233  -0.207  0.892   1.00 17.66  ? 321 LEU A O   1 
ATOM   2356 C  CB  . LEU A 1 342 ? 29.487  -1.939  3.573   1.00 20.90  ? 321 LEU A CB  1 
ATOM   2357 C  CG  . LEU A 1 342 ? 31.017  -1.836  3.614   1.00 20.29  ? 321 LEU A CG  1 
ATOM   2358 C  CD1 . LEU A 1 342 ? 31.456  -0.669  4.492   1.00 21.17  ? 321 LEU A CD1 1 
ATOM   2359 C  CD2 . LEU A 1 342 ? 31.642  -3.134  4.088   1.00 22.36  ? 321 LEU A CD2 1 
ATOM   2360 N  N   . LYS A 1 343 ? 28.822  -1.909  0.479   1.00 21.24  ? 322 LYS A N   1 
ATOM   2361 C  CA  . LYS A 1 343 ? 29.300  -2.048  -0.892  1.00 28.42  ? 322 LYS A CA  1 
ATOM   2362 C  C   . LYS A 1 343 ? 28.947  -0.823  -1.722  1.00 22.55  ? 322 LYS A C   1 
ATOM   2363 O  O   . LYS A 1 343 ? 29.719  -0.420  -2.597  1.00 26.96  ? 322 LYS A O   1 
ATOM   2364 C  CB  . LYS A 1 343 ? 28.729  -3.314  -1.524  1.00 23.03  ? 322 LYS A CB  1 
ATOM   2365 C  CG  . LYS A 1 343 ? 29.343  -4.590  -0.976  1.00 35.22  ? 322 LYS A CG  1 
ATOM   2366 C  CD  . LYS A 1 343 ? 28.816  -5.826  -1.692  1.00 36.87  ? 322 LYS A CD  1 
ATOM   2367 C  CE  . LYS A 1 343 ? 29.336  -7.106  -1.045  1.00 44.03  ? 322 LYS A CE  1 
ATOM   2368 N  NZ  . LYS A 1 343 ? 30.826  -7.104  -0.894  1.00 41.47  ? 322 LYS A NZ  1 
ATOM   2369 N  N   . ALA A 1 344 ? 27.782  -0.221  -1.467  1.00 26.37  ? 323 ALA A N   1 
ATOM   2370 C  CA  . ALA A 1 344 ? 27.435  1.025   -2.144  1.00 26.06  ? 323 ALA A CA  1 
ATOM   2371 C  C   . ALA A 1 344 ? 28.365  2.156   -1.721  1.00 26.35  ? 323 ALA A C   1 
ATOM   2372 O  O   . ALA A 1 344 ? 28.726  3.009   -2.539  1.00 24.05  ? 323 ALA A O   1 
ATOM   2373 C  CB  . ALA A 1 344 ? 25.979  1.395   -1.861  1.00 23.03  ? 323 ALA A CB  1 
ATOM   2374 N  N   . VAL A 1 345 ? 28.754  2.184   -0.443  1.00 18.95  ? 324 VAL A N   1 
ATOM   2375 C  CA  . VAL A 1 345 ? 29.686  3.200   0.034   1.00 24.93  ? 324 VAL A CA  1 
ATOM   2376 C  C   . VAL A 1 345 ? 31.043  3.032   -0.638  1.00 24.13  ? 324 VAL A C   1 
ATOM   2377 O  O   . VAL A 1 345 ? 31.659  4.004   -1.089  1.00 21.88  ? 324 VAL A O   1 
ATOM   2378 C  CB  . VAL A 1 345 ? 29.805  3.133   1.567   1.00 20.79  ? 324 VAL A CB  1 
ATOM   2379 C  CG1 . VAL A 1 345 ? 30.957  3.985   2.048   1.00 19.95  ? 324 VAL A CG1 1 
ATOM   2380 C  CG2 . VAL A 1 345 ? 28.511  3.580   2.211   1.00 22.59  ? 324 VAL A CG2 1 
ATOM   2381 N  N   . TYR A 1 346 ? 31.529  1.792   -0.710  1.00 21.39  ? 325 TYR A N   1 
ATOM   2382 C  CA  . TYR A 1 346 ? 32.823  1.529   -1.328  1.00 21.42  ? 325 TYR A CA  1 
ATOM   2383 C  C   . TYR A 1 346 ? 32.806  1.844   -2.819  1.00 21.48  ? 325 TYR A C   1 
ATOM   2384 O  O   . TYR A 1 346 ? 33.820  2.290   -3.368  1.00 19.40  ? 325 TYR A O   1 
ATOM   2385 C  CB  . TYR A 1 346 ? 33.224  0.069   -1.098  1.00 20.06  ? 325 TYR A CB  1 
ATOM   2386 C  CG  . TYR A 1 346 ? 33.791  -0.237  0.277   1.00 22.34  ? 325 TYR A CG  1 
ATOM   2387 C  CD1 . TYR A 1 346 ? 33.853  0.736   1.267   1.00 25.47  ? 325 TYR A CD1 1 
ATOM   2388 C  CD2 . TYR A 1 346 ? 34.286  -1.502  0.575   1.00 23.02  ? 325 TYR A CD2 1 
ATOM   2389 C  CE1 . TYR A 1 346 ? 34.381  0.458   2.515   1.00 21.17  ? 325 TYR A CE1 1 
ATOM   2390 C  CE2 . TYR A 1 346 ? 34.816  -1.789  1.822   1.00 22.95  ? 325 TYR A CE2 1 
ATOM   2391 C  CZ  . TYR A 1 346 ? 34.861  -0.804  2.788   1.00 20.66  ? 325 TYR A CZ  1 
ATOM   2392 O  OH  . TYR A 1 346 ? 35.385  -1.079  4.032   1.00 22.13  ? 325 TYR A OH  1 
ATOM   2393 N  N   . GLU A 1 347 ? 31.676  1.608   -3.489  1.00 20.54  ? 326 GLU A N   1 
ATOM   2394 C  CA  . GLU A 1 347 ? 31.582  1.906   -4.915  1.00 22.72  ? 326 GLU A CA  1 
ATOM   2395 C  C   . GLU A 1 347 ? 31.584  3.411   -5.168  1.00 22.12  ? 326 GLU A C   1 
ATOM   2396 O  O   . GLU A 1 347 ? 32.155  3.879   -6.160  1.00 24.92  ? 326 GLU A O   1 
ATOM   2397 C  CB  . GLU A 1 347 ? 30.324  1.260   -5.496  1.00 24.45  ? 326 GLU A CB  1 
ATOM   2398 C  CG  . GLU A 1 347 ? 30.092  1.544   -6.973  1.00 36.89  ? 326 GLU A CG  1 
ATOM   2399 C  CD  . GLU A 1 347 ? 31.209  1.023   -7.864  1.00 45.24  ? 326 GLU A CD  1 
ATOM   2400 O  OE1 . GLU A 1 347 ? 31.738  -0.077  -7.597  1.00 40.77  ? 326 GLU A OE1 1 
ATOM   2401 O  OE2 . GLU A 1 347 ? 31.561  1.723   -8.836  1.00 47.24  ? 326 GLU A OE2 1 
ATOM   2402 N  N   . ALA A 1 348 ? 30.932  4.182   -4.297  1.00 23.21  ? 327 ALA A N   1 
ATOM   2403 C  CA  . ALA A 1 348 ? 30.937  5.634   -4.447  1.00 23.69  ? 327 ALA A CA  1 
ATOM   2404 C  C   . ALA A 1 348 ? 32.317  6.213   -4.168  1.00 25.09  ? 327 ALA A C   1 
ATOM   2405 O  O   . ALA A 1 348 ? 32.763  7.138   -4.858  1.00 25.40  ? 327 ALA A O   1 
ATOM   2406 C  CB  . ALA A 1 348 ? 29.900  6.259   -3.517  1.00 30.07  ? 327 ALA A CB  1 
ATOM   2407 N  N   . ILE A 1 349 ? 33.008  5.677   -3.162  1.00 21.34  ? 328 ILE A N   1 
ATOM   2408 C  CA  . ILE A 1 349 ? 34.306  6.213   -2.774  1.00 19.87  ? 328 ILE A CA  1 
ATOM   2409 C  C   . ILE A 1 349 ? 35.337  5.979   -3.868  1.00 24.39  ? 328 ILE A C   1 
ATOM   2410 O  O   . ILE A 1 349 ? 36.238  6.801   -4.071  1.00 26.32  ? 328 ILE A O   1 
ATOM   2411 C  CB  . ILE A 1 349 ? 34.752  5.598   -1.436  1.00 23.52  ? 328 ILE A CB  1 
ATOM   2412 C  CG1 . ILE A 1 349 ? 33.904  6.155   -0.291  1.00 26.24  ? 328 ILE A CG1 1 
ATOM   2413 C  CG2 . ILE A 1 349 ? 36.228  5.874   -1.191  1.00 25.12  ? 328 ILE A CG2 1 
ATOM   2414 C  CD1 . ILE A 1 349 ? 34.136  5.451   1.038   1.00 28.18  ? 328 ILE A CD1 1 
ATOM   2415 N  N   . GLY A 1 350 ? 35.242  4.850   -4.569  1.00 22.80  ? 329 GLY A N   1 
ATOM   2416 C  CA  . GLY A 1 350 ? 36.178  4.539   -5.631  1.00 24.28  ? 329 GLY A CA  1 
ATOM   2417 C  C   . GLY A 1 350 ? 36.994  3.283   -5.393  1.00 26.17  ? 329 GLY A C   1 
ATOM   2418 O  O   . GLY A 1 350 ? 37.910  2.991   -6.163  1.00 24.69  ? 329 GLY A O   1 
ATOM   2419 N  N   . PHE A 1 351 ? 36.686  2.535   -4.334  1.00 21.69  ? 330 PHE A N   1 
ATOM   2420 C  CA  . PHE A 1 351 ? 37.353  1.260   -4.113  1.00 23.23  ? 330 PHE A CA  1 
ATOM   2421 C  C   . PHE A 1 351 ? 37.010  0.274   -5.224  1.00 18.70  ? 330 PHE A C   1 
ATOM   2422 O  O   . PHE A 1 351 ? 35.899  0.264   -5.762  1.00 17.58  ? 330 PHE A O   1 
ATOM   2423 C  CB  . PHE A 1 351 ? 36.941  0.642   -2.774  1.00 21.23  ? 330 PHE A CB  1 
ATOM   2424 C  CG  . PHE A 1 351 ? 37.443  1.383   -1.563  1.00 17.51  ? 330 PHE A CG  1 
ATOM   2425 C  CD1 . PHE A 1 351 ? 38.329  2.442   -1.678  1.00 23.19  ? 330 PHE A CD1 1 
ATOM   2426 C  CD2 . PHE A 1 351 ? 37.027  1.002   -0.297  1.00 22.78  ? 330 PHE A CD2 1 
ATOM   2427 C  CE1 . PHE A 1 351 ? 38.782  3.110   -0.554  1.00 24.79  ? 330 PHE A CE1 1 
ATOM   2428 C  CE2 . PHE A 1 351 ? 37.476  1.668   0.830   1.00 20.72  ? 330 PHE A CE2 1 
ATOM   2429 C  CZ  . PHE A 1 351 ? 38.354  2.720   0.702   1.00 22.61  ? 330 PHE A CZ  1 
ATOM   2430 N  N   . VAL A 1 352 ? 37.978  -0.578  -5.552  1.00 20.06  ? 331 VAL A N   1 
ATOM   2431 C  CA  . VAL A 1 352 ? 37.698  -1.729  -6.397  1.00 18.43  ? 331 VAL A CA  1 
ATOM   2432 C  C   . VAL A 1 352 ? 36.754  -2.657  -5.648  1.00 18.72  ? 331 VAL A C   1 
ATOM   2433 O  O   . VAL A 1 352 ? 36.977  -2.978  -4.473  1.00 19.25  ? 331 VAL A O   1 
ATOM   2434 C  CB  . VAL A 1 352 ? 39.000  -2.445  -6.779  1.00 21.47  ? 331 VAL A CB  1 
ATOM   2435 C  CG1 . VAL A 1 352 ? 38.705  -3.684  -7.614  1.00 24.21  ? 331 VAL A CG1 1 
ATOM   2436 C  CG2 . VAL A 1 352 ? 39.919  -1.497  -7.534  1.00 28.24  ? 331 VAL A CG2 1 
ATOM   2437 N  N   . ALA A 1 353 ? 35.680  -3.068  -6.313  1.00 20.32  ? 332 ALA A N   1 
ATOM   2438 C  CA  . ALA A 1 353 ? 34.725  -3.972  -5.695  1.00 24.39  ? 332 ALA A CA  1 
ATOM   2439 C  C   . ALA A 1 353 ? 35.391  -5.304  -5.374  1.00 29.39  ? 332 ALA A C   1 
ATOM   2440 O  O   . ALA A 1 353 ? 36.116  -5.866  -6.200  1.00 21.45  ? 332 ALA A O   1 
ATOM   2441 C  CB  . ALA A 1 353 ? 33.530  -4.189  -6.621  1.00 29.20  ? 332 ALA A CB  1 
ATOM   2442 N  N   . LYS A 1 354 ? 35.140  -5.811  -4.175  1.00 22.35  ? 333 LYS A N   1 
ATOM   2443 C  CA  . LYS A 1 354 ? 35.677  -7.107  -3.790  1.00 29.61  ? 333 LYS A CA  1 
ATOM   2444 C  C   . LYS A 1 354 ? 35.105  -8.180  -4.709  1.00 25.37  ? 333 LYS A C   1 
ATOM   2445 O  O   . LYS A 1 354 ? 33.876  -8.310  -4.802  1.00 28.06  ? 333 LYS A O   1 
ATOM   2446 C  CB  . LYS A 1 354 ? 35.331  -7.415  -2.339  1.00 21.99  ? 333 LYS A CB  1 
ATOM   2447 C  CG  . LYS A 1 354 ? 35.815  -8.770  -1.862  1.00 26.48  ? 333 LYS A CG  1 
ATOM   2448 C  CD  . LYS A 1 354 ? 35.406  -9.015  -0.427  1.00 29.64  ? 333 LYS A CD  1 
ATOM   2449 C  CE  . LYS A 1 354 ? 35.499  -10.483 -0.074  1.00 35.78  ? 333 LYS A CE  1 
ATOM   2450 N  NZ  . LYS A 1 354 ? 36.853  -11.028 -0.331  1.00 42.35  ? 333 LYS A NZ  1 
ATOM   2451 N  N   . PRO A 1 355 ? 35.941  -8.961  -5.408  1.00 29.77  ? 334 PRO A N   1 
ATOM   2452 C  CA  . PRO A 1 355 ? 35.394  -9.978  -6.314  1.00 31.66  ? 334 PRO A CA  1 
ATOM   2453 C  C   . PRO A 1 355 ? 34.866  -11.215 -5.592  1.00 36.16  ? 334 PRO A C   1 
ATOM   2454 O  O   . PRO A 1 355 ? 34.907  -11.318 -4.362  1.00 37.41  ? 334 PRO A O   1 
ATOM   2455 C  CB  . PRO A 1 355 ? 36.592  -10.330 -7.204  1.00 35.47  ? 334 PRO A CB  1 
ATOM   2456 C  CG  . PRO A 1 355 ? 37.785  -10.013 -6.375  1.00 30.19  ? 334 PRO A CG  1 
ATOM   2457 C  CD  . PRO A 1 355 ? 37.409  -8.849  -5.518  1.00 32.49  ? 334 PRO A CD  1 
ATOM   2458 O  OXT . PRO A 1 355 ? 34.369  -12.143 -6.230  1.00 46.42  ? 334 PRO A OXT 1 
ATOM   2459 N  N   . THR B 1 23  ? 57.695  -22.696 8.265   1.00 58.64  ? 2   THR B N   1 
ATOM   2460 C  CA  . THR B 1 23  ? 57.152  -21.344 8.183   1.00 59.80  ? 2   THR B CA  1 
ATOM   2461 C  C   . THR B 1 23  ? 58.283  -20.321 8.115   1.00 57.37  ? 2   THR B C   1 
ATOM   2462 O  O   . THR B 1 23  ? 59.173  -20.306 8.964   1.00 57.86  ? 2   THR B O   1 
ATOM   2463 C  CB  . THR B 1 23  ? 56.253  -21.029 9.385   1.00 65.63  ? 2   THR B CB  1 
ATOM   2464 O  OG1 . THR B 1 23  ? 55.536  -22.209 9.768   1.00 76.44  ? 2   THR B OG1 1 
ATOM   2465 C  CG2 . THR B 1 23  ? 55.261  -19.930 9.036   1.00 56.73  ? 2   THR B CG2 1 
ATOM   2466 N  N   . LYS B 1 24  ? 58.237  -19.466 7.100   1.00 45.95  ? 3   LYS B N   1 
ATOM   2467 C  CA  . LYS B 1 24  ? 59.287  -18.495 6.842   1.00 44.13  ? 3   LYS B CA  1 
ATOM   2468 C  C   . LYS B 1 24  ? 59.014  -17.191 7.574   1.00 41.23  ? 3   LYS B C   1 
ATOM   2469 O  O   . LYS B 1 24  ? 57.892  -16.937 8.023   1.00 35.69  ? 3   LYS B O   1 
ATOM   2470 C  CB  . LYS B 1 24  ? 59.395  -18.238 5.342   1.00 44.89  ? 3   LYS B CB  1 
ATOM   2471 C  CG  . LYS B 1 24  ? 59.734  -19.480 4.542   1.00 44.75  ? 3   LYS B CG  1 
ATOM   2472 C  CD  . LYS B 1 24  ? 59.540  -19.263 3.054   1.00 50.34  ? 3   LYS B CD  1 
ATOM   2473 C  CE  . LYS B 1 24  ? 59.122  -20.557 2.360   1.00 68.63  ? 3   LYS B CE  1 
ATOM   2474 N  NZ  . LYS B 1 24  ? 59.975  -21.725 2.747   1.00 68.43  ? 3   LYS B NZ  1 
ATOM   2475 N  N   . PRO B 1 25  ? 60.032  -16.345 7.732   1.00 44.26  ? 4   PRO B N   1 
ATOM   2476 C  CA  . PRO B 1 25  ? 59.790  -15.012 8.295   1.00 44.35  ? 4   PRO B CA  1 
ATOM   2477 C  C   . PRO B 1 25  ? 58.796  -14.242 7.441   1.00 33.95  ? 4   PRO B C   1 
ATOM   2478 O  O   . PRO B 1 25  ? 58.872  -14.244 6.212   1.00 31.53  ? 4   PRO B O   1 
ATOM   2479 C  CB  . PRO B 1 25  ? 61.177  -14.358 8.277   1.00 43.27  ? 4   PRO B CB  1 
ATOM   2480 C  CG  . PRO B 1 25  ? 62.138  -15.488 8.232   1.00 50.75  ? 4   PRO B CG  1 
ATOM   2481 C  CD  . PRO B 1 25  ? 61.461  -16.583 7.463   1.00 49.49  ? 4   PRO B CD  1 
ATOM   2482 N  N   . ILE B 1 26  ? 57.869  -13.563 8.109   1.00 33.64  ? 5   ILE B N   1 
ATOM   2483 C  CA  . ILE B 1 26  ? 56.793  -12.830 7.452   1.00 31.51  ? 5   ILE B CA  1 
ATOM   2484 C  C   . ILE B 1 26  ? 57.217  -11.375 7.310   1.00 27.44  ? 5   ILE B C   1 
ATOM   2485 O  O   . ILE B 1 26  ? 57.643  -10.744 8.286   1.00 28.18  ? 5   ILE B O   1 
ATOM   2486 C  CB  . ILE B 1 26  ? 55.478  -12.957 8.241   1.00 29.72  ? 5   ILE B CB  1 
ATOM   2487 C  CG1 . ILE B 1 26  ? 55.023  -14.420 8.271   1.00 33.30  ? 5   ILE B CG1 1 
ATOM   2488 C  CG2 . ILE B 1 26  ? 54.403  -12.075 7.635   1.00 29.99  ? 5   ILE B CG2 1 
ATOM   2489 C  CD1 . ILE B 1 26  ? 53.960  -14.718 9.310   1.00 32.16  ? 5   ILE B CD1 1 
ATOM   2490 N  N   . VAL B 1 27  ? 57.125  -10.853 6.089   1.00 25.61  ? 6   VAL B N   1 
ATOM   2491 C  CA  . VAL B 1 27  ? 57.483  -9.476  5.772   1.00 28.88  ? 6   VAL B CA  1 
ATOM   2492 C  C   . VAL B 1 27  ? 56.247  -8.791  5.210   1.00 21.78  ? 6   VAL B C   1 
ATOM   2493 O  O   . VAL B 1 27  ? 55.611  -9.314  4.291   1.00 26.21  ? 6   VAL B O   1 
ATOM   2494 C  CB  . VAL B 1 27  ? 58.647  -9.409  4.765   1.00 27.65  ? 6   VAL B CB  1 
ATOM   2495 C  CG1 . VAL B 1 27  ? 59.027  -7.966  4.483   1.00 28.23  ? 6   VAL B CG1 1 
ATOM   2496 C  CG2 . VAL B 1 27  ? 59.845  -10.192 5.285   1.00 30.30  ? 6   VAL B CG2 1 
ATOM   2497 N  N   . PHE B 1 28  ? 55.907  -7.630  5.759   1.00 21.88  ? 7   PHE B N   1 
ATOM   2498 C  CA  . PHE B 1 28  ? 54.723  -6.889  5.348   1.00 22.59  ? 7   PHE B CA  1 
ATOM   2499 C  C   . PHE B 1 28  ? 55.143  -5.543  4.780   1.00 21.71  ? 7   PHE B C   1 
ATOM   2500 O  O   . PHE B 1 28  ? 55.940  -4.826  5.391   1.00 27.23  ? 7   PHE B O   1 
ATOM   2501 C  CB  . PHE B 1 28  ? 53.761  -6.690  6.523   1.00 19.73  ? 7   PHE B CB  1 
ATOM   2502 C  CG  . PHE B 1 28  ? 52.457  -6.048  6.136   1.00 21.21  ? 7   PHE B CG  1 
ATOM   2503 C  CD1 . PHE B 1 28  ? 52.379  -4.678  5.924   1.00 22.51  ? 7   PHE B CD1 1 
ATOM   2504 C  CD2 . PHE B 1 28  ? 51.311  -6.812  5.981   1.00 24.92  ? 7   PHE B CD2 1 
ATOM   2505 C  CE1 . PHE B 1 28  ? 51.182  -4.082  5.563   1.00 21.71  ? 7   PHE B CE1 1 
ATOM   2506 C  CE2 . PHE B 1 28  ? 50.106  -6.220  5.620   1.00 24.21  ? 7   PHE B CE2 1 
ATOM   2507 C  CZ  . PHE B 1 28  ? 50.045  -4.853  5.412   1.00 21.32  ? 7   PHE B CZ  1 
ATOM   2508 N  N   . SER B 1 29  ? 54.600  -5.200  3.617   1.00 22.84  ? 8   SER B N   1 
ATOM   2509 C  CA  . SER B 1 29  ? 54.864  -3.913  2.995   1.00 26.02  ? 8   SER B CA  1 
ATOM   2510 C  C   . SER B 1 29  ? 53.555  -3.330  2.493   1.00 22.31  ? 8   SER B C   1 
ATOM   2511 O  O   . SER B 1 29  ? 52.739  -4.040  1.902   1.00 26.36  ? 8   SER B O   1 
ATOM   2512 C  CB  . SER B 1 29  ? 55.861  -4.039  1.840   1.00 32.61  ? 8   SER B CB  1 
ATOM   2513 O  OG  . SER B 1 29  ? 56.248  -2.756  1.382   1.00 44.72  ? 8   SER B OG  1 
ATOM   2514 N  N   . GLY B 1 30  ? 53.356  -2.040  2.745   1.00 26.87  ? 9   GLY B N   1 
ATOM   2515 C  CA  . GLY B 1 30  ? 52.202  -1.316  2.240   1.00 27.35  ? 9   GLY B CA  1 
ATOM   2516 C  C   . GLY B 1 30  ? 52.554  -0.593  0.951   1.00 29.57  ? 9   GLY B C   1 
ATOM   2517 O  O   . GLY B 1 30  ? 53.667  -0.091  0.794   1.00 33.84  ? 9   GLY B O   1 
ATOM   2518 N  N   . ALA B 1 31  ? 51.590  -0.551  0.032   1.00 30.92  ? 10  ALA B N   1 
ATOM   2519 C  CA  . ALA B 1 31  ? 51.768  0.050   -1.287  1.00 31.39  ? 10  ALA B CA  1 
ATOM   2520 C  C   . ALA B 1 31  ? 50.644  1.049   -1.520  1.00 29.92  ? 10  ALA B C   1 
ATOM   2521 O  O   . ALA B 1 31  ? 49.475  0.663   -1.632  1.00 27.63  ? 10  ALA B O   1 
ATOM   2522 C  CB  . ALA B 1 31  ? 51.778  -1.017  -2.382  1.00 28.72  ? 10  ALA B CB  1 
ATOM   2523 N  N   . GLN B 1 32  ? 50.997  2.316   -1.602  1.00 31.58  ? 11  GLN B N   1 
ATOM   2524 C  CA  . GLN B 1 32  ? 50.008  3.352   -1.858  1.00 31.11  ? 11  GLN B CA  1 
ATOM   2525 C  C   . GLN B 1 32  ? 49.434  3.181   -3.262  1.00 32.25  ? 11  GLN B C   1 
ATOM   2526 O  O   . GLN B 1 32  ? 50.194  2.970   -4.214  1.00 30.39  ? 11  GLN B O   1 
ATOM   2527 C  CB  . GLN B 1 32  ? 50.661  4.725   -1.700  1.00 39.53  ? 11  GLN B CB  1 
ATOM   2528 C  CG  . GLN B 1 32  ? 49.712  5.828   -1.297  1.00 46.80  ? 11  GLN B CG  1 
ATOM   2529 C  CD  . GLN B 1 32  ? 49.028  5.554   0.024   1.00 37.93  ? 11  GLN B CD  1 
ATOM   2530 O  OE1 . GLN B 1 32  ? 47.801  5.574   0.112   1.00 43.95  ? 11  GLN B OE1 1 
ATOM   2531 N  NE2 . GLN B 1 32  ? 49.819  5.301   1.061   1.00 44.36  ? 11  GLN B NE2 1 
ATOM   2532 N  N   . PRO B 1 33  ? 48.109  3.238   -3.435  1.00 27.52  ? 12  PRO B N   1 
ATOM   2533 C  CA  . PRO B 1 33  ? 47.562  3.115   -4.798  1.00 28.10  ? 12  PRO B CA  1 
ATOM   2534 C  C   . PRO B 1 33  ? 48.077  4.181   -5.750  1.00 36.31  ? 12  PRO B C   1 
ATOM   2535 O  O   . PRO B 1 33  ? 48.333  3.890   -6.925  1.00 35.38  ? 12  PRO B O   1 
ATOM   2536 C  CB  . PRO B 1 33  ? 46.045  3.233   -4.582  1.00 32.02  ? 12  PRO B CB  1 
ATOM   2537 C  CG  . PRO B 1 33  ? 45.826  2.896   -3.144  1.00 28.70  ? 12  PRO B CG  1 
ATOM   2538 C  CD  . PRO B 1 33  ? 47.047  3.352   -2.418  1.00 25.51  ? 12  PRO B CD  1 
ATOM   2539 N  N   . SER B 1 34  ? 48.238  5.414   -5.277  1.00 36.24  ? 13  SER B N   1 
ATOM   2540 C  CA  . SER B 1 34  ? 48.751  6.481   -6.122  1.00 45.67  ? 13  SER B CA  1 
ATOM   2541 C  C   . SER B 1 34  ? 50.268  6.456   -6.238  1.00 50.43  ? 13  SER B C   1 
ATOM   2542 O  O   . SER B 1 34  ? 50.822  7.182   -7.071  1.00 56.68  ? 13  SER B O   1 
ATOM   2543 C  CB  . SER B 1 34  ? 48.313  7.841   -5.580  1.00 49.29  ? 13  SER B CB  1 
ATOM   2544 O  OG  . SER B 1 34  ? 49.209  8.288   -4.576  1.00 67.91  ? 13  SER B OG  1 
ATOM   2545 N  N   . GLY B 1 35  ? 50.945  5.645   -5.430  1.00 56.88  ? 14  GLY B N   1 
ATOM   2546 C  CA  . GLY B 1 35  ? 52.392  5.607   -5.424  1.00 57.03  ? 14  GLY B CA  1 
ATOM   2547 C  C   . GLY B 1 35  ? 52.987  5.369   -6.794  1.00 65.19  ? 14  GLY B C   1 
ATOM   2548 O  O   . GLY B 1 35  ? 52.440  4.606   -7.596  1.00 71.37  ? 14  GLY B O   1 
ATOM   2549 N  N   . GLU B 1 36  ? 54.105  6.031   -7.075  1.00 69.84  ? 15  GLU B N   1 
ATOM   2550 C  CA  . GLU B 1 36  ? 54.838  5.871   -8.325  1.00 65.59  ? 15  GLU B CA  1 
ATOM   2551 C  C   . GLU B 1 36  ? 56.187  5.246   -7.990  1.00 67.96  ? 15  GLU B C   1 
ATOM   2552 O  O   . GLU B 1 36  ? 57.030  5.884   -7.350  1.00 68.04  ? 15  GLU B O   1 
ATOM   2553 C  CB  . GLU B 1 36  ? 55.010  7.211   -9.035  1.00 62.38  ? 15  GLU B CB  1 
ATOM   2554 N  N   . LEU B 1 37  ? 56.382  3.998   -8.407  1.00 61.99  ? 16  LEU B N   1 
ATOM   2555 C  CA  . LEU B 1 37  ? 57.642  3.309   -8.169  1.00 55.33  ? 16  LEU B CA  1 
ATOM   2556 C  C   . LEU B 1 37  ? 58.704  3.831   -9.126  1.00 49.43  ? 16  LEU B C   1 
ATOM   2557 O  O   . LEU B 1 37  ? 58.485  3.887   -10.340 1.00 45.37  ? 16  LEU B O   1 
ATOM   2558 C  CB  . LEU B 1 37  ? 57.471  1.800   -8.338  1.00 51.03  ? 16  LEU B CB  1 
ATOM   2559 C  CG  . LEU B 1 37  ? 56.666  1.078   -7.255  1.00 44.02  ? 16  LEU B CG  1 
ATOM   2560 C  CD1 . LEU B 1 37  ? 56.555  -0.404  -7.582  1.00 46.73  ? 16  LEU B CD1 1 
ATOM   2561 C  CD2 . LEU B 1 37  ? 57.291  1.276   -5.883  1.00 46.75  ? 16  LEU B CD2 1 
ATOM   2562 N  N   . THR B 1 38  ? 59.851  4.212   -8.579  1.00 51.89  ? 17  THR B N   1 
ATOM   2563 C  CA  . THR B 1 38  ? 60.959  4.699   -9.383  1.00 47.33  ? 17  THR B CA  1 
ATOM   2564 C  C   . THR B 1 38  ? 61.931  3.566   -9.684  1.00 49.10  ? 17  THR B C   1 
ATOM   2565 O  O   . THR B 1 38  ? 61.812  2.448   -9.179  1.00 42.71  ? 17  THR B O   1 
ATOM   2566 C  CB  . THR B 1 38  ? 61.708  5.829   -8.674  1.00 49.11  ? 17  THR B CB  1 
ATOM   2567 O  OG1 . THR B 1 38  ? 62.496  5.281   -7.608  1.00 44.39  ? 17  THR B OG1 1 
ATOM   2568 C  CG2 . THR B 1 38  ? 60.740  6.860   -8.118  1.00 53.83  ? 17  THR B CG2 1 
ATOM   2569 N  N   . ILE B 1 39  ? 62.918  3.882   -10.521 1.00 53.00  ? 18  ILE B N   1 
ATOM   2570 C  CA  . ILE B 1 39  ? 64.000  2.941   -10.776 1.00 46.61  ? 18  ILE B CA  1 
ATOM   2571 C  C   . ILE B 1 39  ? 64.778  2.677   -9.496  1.00 46.73  ? 18  ILE B C   1 
ATOM   2572 O  O   . ILE B 1 39  ? 65.330  1.587   -9.307  1.00 41.75  ? 18  ILE B O   1 
ATOM   2573 C  CB  . ILE B 1 39  ? 64.896  3.484   -11.909 1.00 45.29  ? 18  ILE B CB  1 
ATOM   2574 C  CG1 . ILE B 1 39  ? 65.295  2.347   -12.843 1.00 63.55  ? 18  ILE B CG1 1 
ATOM   2575 C  CG2 . ILE B 1 39  ? 66.117  4.239   -11.365 1.00 45.80  ? 18  ILE B CG2 1 
ATOM   2576 C  CD1 . ILE B 1 39  ? 64.159  1.886   -13.717 1.00 63.47  ? 18  ILE B CD1 1 
ATOM   2577 N  N   . GLY B 1 40  ? 64.834  3.663   -8.598  1.00 47.49  ? 19  GLY B N   1 
ATOM   2578 C  CA  . GLY B 1 40  ? 65.449  3.430   -7.303  1.00 50.59  ? 19  GLY B CA  1 
ATOM   2579 C  C   . GLY B 1 40  ? 64.674  2.429   -6.468  1.00 46.19  ? 19  GLY B C   1 
ATOM   2580 O  O   . GLY B 1 40  ? 65.262  1.553   -5.829  1.00 46.52  ? 19  GLY B O   1 
ATOM   2581 N  N   . ASN B 1 41  ? 63.344  2.541   -6.464  1.00 45.11  ? 20  ASN B N   1 
ATOM   2582 C  CA  . ASN B 1 41  ? 62.530  1.570   -5.741  1.00 47.89  ? 20  ASN B CA  1 
ATOM   2583 C  C   . ASN B 1 41  ? 62.730  0.163   -6.284  1.00 46.69  ? 20  ASN B C   1 
ATOM   2584 O  O   . ASN B 1 41  ? 62.654  -0.810  -5.527  1.00 44.12  ? 20  ASN B O   1 
ATOM   2585 C  CB  . ASN B 1 41  ? 61.050  1.952   -5.819  1.00 43.79  ? 20  ASN B CB  1 
ATOM   2586 C  CG  . ASN B 1 41  ? 60.727  3.206   -5.032  1.00 49.30  ? 20  ASN B CG  1 
ATOM   2587 O  OD1 . ASN B 1 41  ? 60.231  4.189   -5.582  1.00 54.88  ? 20  ASN B OD1 1 
ATOM   2588 N  ND2 . ASN B 1 41  ? 61.004  3.176   -3.733  1.00 51.70  ? 20  ASN B ND2 1 
ATOM   2589 N  N   . TYR B 1 42  ? 62.983  0.034   -7.587  1.00 38.99  ? 21  TYR B N   1 
ATOM   2590 C  CA  . TYR B 1 42  ? 63.070  -1.288  -8.204  1.00 43.38  ? 21  TYR B CA  1 
ATOM   2591 C  C   . TYR B 1 42  ? 64.450  -1.911  -8.008  1.00 48.32  ? 21  TYR B C   1 
ATOM   2592 O  O   . TYR B 1 42  ? 64.596  -2.916  -7.308  1.00 42.64  ? 21  TYR B O   1 
ATOM   2593 C  CB  . TYR B 1 42  ? 62.725  -1.178  -9.692  1.00 40.39  ? 21  TYR B CB  1 
ATOM   2594 C  CG  . TYR B 1 42  ? 62.717  -2.498  -10.413 1.00 41.45  ? 21  TYR B CG  1 
ATOM   2595 C  CD1 . TYR B 1 42  ? 61.818  -3.494  -10.061 1.00 42.06  ? 21  TYR B CD1 1 
ATOM   2596 C  CD2 . TYR B 1 42  ? 63.601  -2.748  -11.451 1.00 46.35  ? 21  TYR B CD2 1 
ATOM   2597 C  CE1 . TYR B 1 42  ? 61.803  -4.704  -10.716 1.00 36.09  ? 21  TYR B CE1 1 
ATOM   2598 C  CE2 . TYR B 1 42  ? 63.593  -3.954  -12.115 1.00 44.11  ? 21  TYR B CE2 1 
ATOM   2599 C  CZ  . TYR B 1 42  ? 62.691  -4.929  -11.741 1.00 43.73  ? 21  TYR B CZ  1 
ATOM   2600 O  OH  . TYR B 1 42  ? 62.676  -6.136  -12.398 1.00 47.24  ? 21  TYR B OH  1 
ATOM   2601 N  N   . MET B 1 43  ? 65.484  -1.305  -8.595  1.00 52.37  ? 22  MET B N   1 
ATOM   2602 C  CA  . MET B 1 43  ? 66.810  -1.912  -8.536  1.00 51.85  ? 22  MET B CA  1 
ATOM   2603 C  C   . MET B 1 43  ? 67.341  -1.961  -7.111  1.00 45.32  ? 22  MET B C   1 
ATOM   2604 O  O   . MET B 1 43  ? 68.107  -2.868  -6.766  1.00 47.54  ? 22  MET B O   1 
ATOM   2605 C  CB  . MET B 1 43  ? 67.779  -1.151  -9.442  1.00 53.81  ? 22  MET B CB  1 
ATOM   2606 C  CG  . MET B 1 43  ? 67.334  -1.098  -10.895 1.00 51.12  ? 22  MET B CG  1 
ATOM   2607 S  SD  . MET B 1 43  ? 68.611  -0.512  -12.024 1.00 49.77  ? 22  MET B SD  1 
ATOM   2608 C  CE  . MET B 1 43  ? 68.604  1.248   -11.703 1.00 58.49  ? 22  MET B CE  1 
ATOM   2609 N  N   . GLY B 1 44  ? 66.950  -1.006  -6.274  1.00 55.20  ? 23  GLY B N   1 
ATOM   2610 C  CA  . GLY B 1 44  ? 67.379  -0.996  -4.893  1.00 52.91  ? 23  GLY B CA  1 
ATOM   2611 C  C   . GLY B 1 44  ? 66.751  -2.099  -4.066  1.00 56.68  ? 23  GLY B C   1 
ATOM   2612 O  O   . GLY B 1 44  ? 67.466  -2.907  -3.465  1.00 63.54  ? 23  GLY B O   1 
ATOM   2613 N  N   . ALA B 1 45  ? 65.417  -2.149  -4.028  1.00 49.72  ? 24  ALA B N   1 
ATOM   2614 C  CA  . ALA B 1 45  ? 64.705  -3.046  -3.123  1.00 48.05  ? 24  ALA B CA  1 
ATOM   2615 C  C   . ALA B 1 45  ? 63.870  -4.096  -3.844  1.00 45.16  ? 24  ALA B C   1 
ATOM   2616 O  O   . ALA B 1 45  ? 64.103  -5.293  -3.652  1.00 45.33  ? 24  ALA B O   1 
ATOM   2617 C  CB  . ALA B 1 45  ? 63.812  -2.215  -2.188  1.00 44.84  ? 24  ALA B CB  1 
ATOM   2618 N  N   . LEU B 1 46  ? 62.919  -3.688  -4.687  1.00 46.20  ? 25  LEU B N   1 
ATOM   2619 C  CA  . LEU B 1 46  ? 61.869  -4.611  -5.115  1.00 43.42  ? 25  LEU B CA  1 
ATOM   2620 C  C   . LEU B 1 46  ? 62.409  -5.714  -6.013  1.00 42.44  ? 25  LEU B C   1 
ATOM   2621 O  O   . LEU B 1 46  ? 61.841  -6.812  -6.051  1.00 37.87  ? 25  LEU B O   1 
ATOM   2622 C  CB  . LEU B 1 46  ? 60.753  -3.839  -5.823  1.00 35.29  ? 25  LEU B CB  1 
ATOM   2623 C  CG  . LEU B 1 46  ? 59.508  -4.630  -6.232  1.00 37.28  ? 25  LEU B CG  1 
ATOM   2624 C  CD1 . LEU B 1 46  ? 58.919  -5.387  -5.053  1.00 39.80  ? 25  LEU B CD1 1 
ATOM   2625 C  CD2 . LEU B 1 46  ? 58.460  -3.705  -6.832  1.00 34.66  ? 25  LEU B CD2 1 
ATOM   2626 N  N   . ARG B 1 47  ? 63.495  -5.449  -6.738  1.00 39.56  ? 26  ARG B N   1 
ATOM   2627 C  CA  . ARG B 1 47  ? 64.078  -6.479  -7.590  1.00 42.10  ? 26  ARG B CA  1 
ATOM   2628 C  C   . ARG B 1 47  ? 64.660  -7.608  -6.753  1.00 37.95  ? 26  ARG B C   1 
ATOM   2629 O  O   . ARG B 1 47  ? 64.586  -8.779  -7.141  1.00 37.10  ? 26  ARG B O   1 
ATOM   2630 C  CB  . ARG B 1 47  ? 65.146  -5.865  -8.494  1.00 39.05  ? 26  ARG B CB  1 
ATOM   2631 C  CG  . ARG B 1 47  ? 65.777  -6.846  -9.467  1.00 45.67  ? 26  ARG B CG  1 
ATOM   2632 C  CD  . ARG B 1 47  ? 66.670  -6.133  -10.480 1.00 40.71  ? 26  ARG B CD  1 
ATOM   2633 N  NE  . ARG B 1 47  ? 67.776  -5.422  -9.847  1.00 49.89  ? 26  ARG B NE  1 
ATOM   2634 C  CZ  . ARG B 1 47  ? 68.731  -4.780  -10.507 1.00 44.95  ? 26  ARG B CZ  1 
ATOM   2635 N  NH1 . ARG B 1 47  ? 68.750  -4.739  -11.829 1.00 49.24  ? 26  ARG B NH1 1 
ATOM   2636 N  NH2 . ARG B 1 47  ? 69.693  -4.166  -9.824  1.00 50.35  ? 26  ARG B NH2 1 
ATOM   2637 N  N   . GLN B 1 48  ? 65.240  -7.276  -5.598  1.00 40.36  ? 27  GLN B N   1 
ATOM   2638 C  CA  . GLN B 1 48  ? 65.735  -8.311  -4.697  1.00 47.46  ? 27  GLN B CA  1 
ATOM   2639 C  C   . GLN B 1 48  ? 64.586  -9.041  -4.008  1.00 35.24  ? 27  GLN B C   1 
ATOM   2640 O  O   . GLN B 1 48  ? 64.611  -10.271 -3.893  1.00 39.02  ? 27  GLN B O   1 
ATOM   2641 C  CB  . GLN B 1 48  ? 66.680  -7.696  -3.664  1.00 50.25  ? 27  GLN B CB  1 
ATOM   2642 N  N   . TRP B 1 49  ? 63.563  -8.305  -3.556  1.00 36.65  ? 28  TRP B N   1 
ATOM   2643 C  CA  . TRP B 1 49  ? 62.438  -8.939  -2.871  1.00 37.12  ? 28  TRP B CA  1 
ATOM   2644 C  C   . TRP B 1 49  ? 61.789  -10.011 -3.739  1.00 38.30  ? 28  TRP B C   1 
ATOM   2645 O  O   . TRP B 1 49  ? 61.330  -11.037 -3.227  1.00 37.46  ? 28  TRP B O   1 
ATOM   2646 C  CB  . TRP B 1 49  ? 61.393  -7.894  -2.469  1.00 39.81  ? 28  TRP B CB  1 
ATOM   2647 C  CG  . TRP B 1 49  ? 61.872  -6.874  -1.475  1.00 44.88  ? 28  TRP B CG  1 
ATOM   2648 C  CD1 . TRP B 1 49  ? 63.051  -6.887  -0.788  1.00 49.93  ? 28  TRP B CD1 1 
ATOM   2649 C  CD2 . TRP B 1 49  ? 61.182  -5.685  -1.063  1.00 47.38  ? 28  TRP B CD2 1 
ATOM   2650 N  NE1 . TRP B 1 49  ? 63.137  -5.782  0.027   1.00 54.80  ? 28  TRP B NE1 1 
ATOM   2651 C  CE2 . TRP B 1 49  ? 62.004  -5.028  -0.124  1.00 49.22  ? 28  TRP B CE2 1 
ATOM   2652 C  CE3 . TRP B 1 49  ? 59.951  -5.112  -1.398  1.00 51.30  ? 28  TRP B CE3 1 
ATOM   2653 C  CZ2 . TRP B 1 49  ? 61.633  -3.827  0.485   1.00 48.06  ? 28  TRP B CZ2 1 
ATOM   2654 C  CZ3 . TRP B 1 49  ? 59.584  -3.919  -0.791  1.00 51.22  ? 28  TRP B CZ3 1 
ATOM   2655 C  CH2 . TRP B 1 49  ? 60.422  -3.291  0.138   1.00 47.38  ? 28  TRP B CH2 1 
ATOM   2656 N  N   . VAL B 1 50  ? 61.742  -9.790  -5.056  1.00 33.98  ? 29  VAL B N   1 
ATOM   2657 C  CA  . VAL B 1 50  ? 61.151  -10.772 -5.962  1.00 30.74  ? 29  VAL B CA  1 
ATOM   2658 C  C   . VAL B 1 50  ? 61.924  -12.082 -5.912  1.00 34.24  ? 29  VAL B C   1 
ATOM   2659 O  O   . VAL B 1 50  ? 61.334  -13.170 -5.926  1.00 32.82  ? 29  VAL B O   1 
ATOM   2660 C  CB  . VAL B 1 50  ? 61.097  -10.203 -7.392  1.00 34.18  ? 29  VAL B CB  1 
ATOM   2661 C  CG1 . VAL B 1 50  ? 60.835  -11.312 -8.403  1.00 28.68  ? 29  VAL B CG1 1 
ATOM   2662 C  CG2 . VAL B 1 50  ? 60.031  -9.122  -7.486  1.00 31.15  ? 29  VAL B CG2 1 
ATOM   2663 N  N   . ASN B 1 51  ? 63.252  -12.004 -5.870  1.00 37.20  ? 30  ASN B N   1 
ATOM   2664 C  CA  . ASN B 1 51  ? 64.073  -13.205 -5.859  1.00 36.06  ? 30  ASN B CA  1 
ATOM   2665 C  C   . ASN B 1 51  ? 64.071  -13.917 -4.514  1.00 38.65  ? 30  ASN B C   1 
ATOM   2666 O  O   . ASN B 1 51  ? 64.588  -15.035 -4.426  1.00 45.15  ? 30  ASN B O   1 
ATOM   2667 C  CB  . ASN B 1 51  ? 65.504  -12.851 -6.256  1.00 42.38  ? 30  ASN B CB  1 
ATOM   2668 C  CG  . ASN B 1 51  ? 65.611  -12.424 -7.707  1.00 52.62  ? 30  ASN B CG  1 
ATOM   2669 O  OD1 . ASN B 1 51  ? 64.923  -12.967 -8.574  1.00 54.56  ? 30  ASN B OD1 1 
ATOM   2670 N  ND2 . ASN B 1 51  ? 66.470  -11.446 -7.980  1.00 49.93  ? 30  ASN B ND2 1 
ATOM   2671 N  N   . MET B 1 52  ? 63.497  -13.309 -3.474  1.00 40.33  ? 31  MET B N   1 
ATOM   2672 C  CA  . MET B 1 52  ? 63.492  -13.884 -2.135  1.00 39.73  ? 31  MET B CA  1 
ATOM   2673 C  C   . MET B 1 52  ? 62.089  -14.256 -1.663  1.00 38.92  ? 31  MET B C   1 
ATOM   2674 O  O   . MET B 1 52  ? 61.850  -14.356 -0.454  1.00 38.12  ? 31  MET B O   1 
ATOM   2675 C  CB  . MET B 1 52  ? 64.150  -12.909 -1.156  1.00 42.29  ? 31  MET B CB  1 
ATOM   2676 C  CG  . MET B 1 52  ? 65.593  -12.571 -1.525  1.00 47.97  ? 31  MET B CG  1 
ATOM   2677 S  SD  . MET B 1 52  ? 66.427  -11.523 -0.319  1.00 69.65  ? 31  MET B SD  1 
ATOM   2678 C  CE  . MET B 1 52  ? 65.423  -10.040 -0.396  1.00 54.02  ? 31  MET B CE  1 
ATOM   2679 N  N   . GLN B 1 53  ? 61.155  -14.476 -2.593  1.00 29.00  ? 32  GLN B N   1 
ATOM   2680 C  CA  . GLN B 1 53  ? 59.810  -14.890 -2.208  1.00 33.76  ? 32  GLN B CA  1 
ATOM   2681 C  C   . GLN B 1 53  ? 59.759  -16.336 -1.735  1.00 34.59  ? 32  GLN B C   1 
ATOM   2682 O  O   . GLN B 1 53  ? 58.771  -16.736 -1.111  1.00 35.06  ? 32  GLN B O   1 
ATOM   2683 C  CB  . GLN B 1 53  ? 58.842  -14.705 -3.374  1.00 24.97  ? 32  GLN B CB  1 
ATOM   2684 C  CG  . GLN B 1 53  ? 58.724  -13.270 -3.849  1.00 33.93  ? 32  GLN B CG  1 
ATOM   2685 C  CD  . GLN B 1 53  ? 57.770  -13.123 -5.013  1.00 27.10  ? 32  GLN B CD  1 
ATOM   2686 O  OE1 . GLN B 1 53  ? 56.554  -13.051 -4.832  1.00 28.22  ? 32  GLN B OE1 1 
ATOM   2687 N  NE2 . GLN B 1 53  ? 58.315  -13.075 -6.215  1.00 27.91  ? 32  GLN B NE2 1 
ATOM   2688 N  N   . ASP B 1 54  ? 60.782  -17.133 -2.036  1.00 36.51  ? 33  ASP B N   1 
ATOM   2689 C  CA  . ASP B 1 54  ? 60.878  -18.479 -1.493  1.00 46.04  ? 33  ASP B CA  1 
ATOM   2690 C  C   . ASP B 1 54  ? 61.527  -18.510 -0.118  1.00 47.32  ? 33  ASP B C   1 
ATOM   2691 O  O   . ASP B 1 54  ? 61.370  -19.502 0.604   1.00 38.63  ? 33  ASP B O   1 
ATOM   2692 C  CB  . ASP B 1 54  ? 61.669  -19.380 -2.447  1.00 51.68  ? 33  ASP B CB  1 
ATOM   2693 C  CG  . ASP B 1 54  ? 60.874  -19.763 -3.678  1.00 58.45  ? 33  ASP B CG  1 
ATOM   2694 O  OD1 . ASP B 1 54  ? 59.640  -19.927 -3.566  1.00 61.79  ? 33  ASP B OD1 1 
ATOM   2695 O  OD2 . ASP B 1 54  ? 61.485  -19.904 -4.758  1.00 80.03  ? 33  ASP B OD2 1 
ATOM   2696 N  N   . ASP B 1 55  ? 62.240  -17.450 0.260   1.00 42.03  ? 34  ASP B N   1 
ATOM   2697 C  CA  . ASP B 1 55  ? 62.899  -17.377 1.557   1.00 42.77  ? 34  ASP B CA  1 
ATOM   2698 C  C   . ASP B 1 55  ? 62.048  -16.695 2.616   1.00 41.00  ? 34  ASP B C   1 
ATOM   2699 O  O   . ASP B 1 55  ? 62.246  -16.951 3.810   1.00 44.73  ? 34  ASP B O   1 
ATOM   2700 C  CB  . ASP B 1 55  ? 64.229  -16.629 1.424   1.00 41.01  ? 34  ASP B CB  1 
ATOM   2701 C  CG  . ASP B 1 55  ? 65.123  -17.219 0.348   1.00 51.28  ? 34  ASP B CG  1 
ATOM   2702 O  OD1 . ASP B 1 55  ? 65.078  -18.452 0.148   1.00 52.85  ? 34  ASP B OD1 1 
ATOM   2703 O  OD2 . ASP B 1 55  ? 65.868  -16.451 -0.299  1.00 54.12  ? 34  ASP B OD2 1 
ATOM   2704 N  N   . TYR B 1 56  ? 61.116  -15.838 2.208   1.00 38.45  ? 35  TYR B N   1 
ATOM   2705 C  CA  . TYR B 1 56  ? 60.231  -15.131 3.116   1.00 37.12  ? 35  TYR B CA  1 
ATOM   2706 C  C   . TYR B 1 56  ? 58.792  -15.328 2.663   1.00 34.02  ? 35  TYR B C   1 
ATOM   2707 O  O   . TYR B 1 56  ? 58.521  -15.601 1.490   1.00 37.91  ? 35  TYR B O   1 
ATOM   2708 C  CB  . TYR B 1 56  ? 60.539  -13.627 3.159   1.00 35.57  ? 35  TYR B CB  1 
ATOM   2709 C  CG  . TYR B 1 56  ? 61.947  -13.283 3.576   1.00 36.66  ? 35  TYR B CG  1 
ATOM   2710 C  CD1 . TYR B 1 56  ? 63.009  -13.432 2.695   1.00 41.19  ? 35  TYR B CD1 1 
ATOM   2711 C  CD2 . TYR B 1 56  ? 62.215  -12.794 4.846   1.00 41.83  ? 35  TYR B CD2 1 
ATOM   2712 C  CE1 . TYR B 1 56  ? 64.300  -13.114 3.071   1.00 40.74  ? 35  TYR B CE1 1 
ATOM   2713 C  CE2 . TYR B 1 56  ? 63.502  -12.473 5.231   1.00 51.96  ? 35  TYR B CE2 1 
ATOM   2714 C  CZ  . TYR B 1 56  ? 64.540  -12.635 4.339   1.00 43.72  ? 35  TYR B CZ  1 
ATOM   2715 O  OH  . TYR B 1 56  ? 65.823  -12.317 4.717   1.00 57.38  ? 35  TYR B OH  1 
ATOM   2716 N  N   . HIS B 1 57  ? 57.867  -15.193 3.609   1.00 31.40  ? 36  HIS B N   1 
ATOM   2717 C  CA  . HIS B 1 57  ? 56.449  -15.053 3.283   1.00 31.44  ? 36  HIS B CA  1 
ATOM   2718 C  C   . HIS B 1 57  ? 56.180  -13.558 3.163   1.00 25.79  ? 36  HIS B C   1 
ATOM   2719 O  O   . HIS B 1 57  ? 55.954  -12.873 4.162   1.00 31.87  ? 36  HIS B O   1 
ATOM   2720 C  CB  . HIS B 1 57  ? 55.562  -15.709 4.334   1.00 30.72  ? 36  HIS B CB  1 
ATOM   2721 C  CG  . HIS B 1 57  ? 54.109  -15.726 3.966   1.00 41.93  ? 36  HIS B CG  1 
ATOM   2722 N  ND1 . HIS B 1 57  ? 53.158  -16.386 4.714   1.00 48.39  ? 36  HIS B ND1 1 
ATOM   2723 C  CD2 . HIS B 1 57  ? 53.445  -15.167 2.925   1.00 48.91  ? 36  HIS B CD2 1 
ATOM   2724 C  CE1 . HIS B 1 57  ? 51.972  -16.231 4.153   1.00 39.72  ? 36  HIS B CE1 1 
ATOM   2725 N  NE2 . HIS B 1 57  ? 52.118  -15.495 3.066   1.00 46.31  ? 36  HIS B NE2 1 
ATOM   2726 N  N   . CYS B 1 58  ? 56.225  -13.051 1.936   1.00 24.35  ? 37  CYS B N   1 
ATOM   2727 C  CA  . CYS B 1 58  ? 56.084  -11.629 1.673   1.00 24.83  ? 37  CYS B CA  1 
ATOM   2728 C  C   . CYS B 1 58  ? 54.619  -11.267 1.490   1.00 28.64  ? 37  CYS B C   1 
ATOM   2729 O  O   . CYS B 1 58  ? 53.861  -11.996 0.843   1.00 26.37  ? 37  CYS B O   1 
ATOM   2730 C  CB  . CYS B 1 58  ? 56.878  -11.240 0.426   1.00 26.78  ? 37  CYS B CB  1 
ATOM   2731 S  SG  . CYS B 1 58  ? 58.647  -11.572 0.555   1.00 33.58  ? 37  CYS B SG  1 
ATOM   2732 N  N   . ILE B 1 59  ? 54.235  -10.123 2.055   1.00 26.81  ? 38  ILE B N   1 
ATOM   2733 C  CA  . ILE B 1 59  ? 52.858  -9.644  2.053   1.00 25.49  ? 38  ILE B CA  1 
ATOM   2734 C  C   . ILE B 1 59  ? 52.870  -8.227  1.506   1.00 25.55  ? 38  ILE B C   1 
ATOM   2735 O  O   . ILE B 1 59  ? 53.562  -7.359  2.048   1.00 26.62  ? 38  ILE B O   1 
ATOM   2736 C  CB  . ILE B 1 59  ? 52.235  -9.675  3.460   1.00 25.75  ? 38  ILE B CB  1 
ATOM   2737 C  CG1 . ILE B 1 59  ? 52.267  -11.102 4.017   1.00 31.48  ? 38  ILE B CG1 1 
ATOM   2738 C  CG2 . ILE B 1 59  ? 50.810  -9.136  3.423   1.00 28.98  ? 38  ILE B CG2 1 
ATOM   2739 C  CD1 . ILE B 1 59  ? 51.729  -11.226 5.422   1.00 29.36  ? 38  ILE B CD1 1 
ATOM   2740 N  N   . TYR B 1 60  ? 52.114  -7.996  0.434   1.00 24.20  ? 39  TYR B N   1 
ATOM   2741 C  CA  . TYR B 1 60  ? 51.986  -6.683  -0.186  1.00 22.84  ? 39  TYR B CA  1 
ATOM   2742 C  C   . TYR B 1 60  ? 50.528  -6.260  -0.114  1.00 20.10  ? 39  TYR B C   1 
ATOM   2743 O  O   . TYR B 1 60  ? 49.664  -6.893  -0.729  1.00 25.08  ? 39  TYR B O   1 
ATOM   2744 C  CB  . TYR B 1 60  ? 52.472  -6.712  -1.636  1.00 23.87  ? 39  TYR B CB  1 
ATOM   2745 C  CG  . TYR B 1 60  ? 53.931  -7.059  -1.770  1.00 23.48  ? 39  TYR B CG  1 
ATOM   2746 C  CD1 . TYR B 1 60  ? 54.343  -8.380  -1.882  1.00 25.69  ? 39  TYR B CD1 1 
ATOM   2747 C  CD2 . TYR B 1 60  ? 54.899  -6.067  -1.776  1.00 23.27  ? 39  TYR B CD2 1 
ATOM   2748 C  CE1 . TYR B 1 60  ? 55.682  -8.701  -1.999  1.00 29.45  ? 39  TYR B CE1 1 
ATOM   2749 C  CE2 . TYR B 1 60  ? 56.236  -6.376  -1.891  1.00 28.37  ? 39  TYR B CE2 1 
ATOM   2750 C  CZ  . TYR B 1 60  ? 56.623  -7.693  -2.005  1.00 31.82  ? 39  TYR B CZ  1 
ATOM   2751 O  OH  . TYR B 1 60  ? 57.959  -7.997  -2.123  1.00 39.05  ? 39  TYR B OH  1 
ATOM   2752 N  N   . CYS B 1 61  ? 50.260  -5.196  0.632   1.00 25.92  ? 40  CYS B N   1 
ATOM   2753 C  CA  . CYS B 1 61  ? 48.909  -4.696  0.854   1.00 20.83  ? 40  CYS B CA  1 
ATOM   2754 C  C   . CYS B 1 61  ? 48.763  -3.356  0.146   1.00 20.17  ? 40  CYS B C   1 
ATOM   2755 O  O   . CYS B 1 61  ? 49.505  -2.415  0.440   1.00 22.66  ? 40  CYS B O   1 
ATOM   2756 C  CB  . CYS B 1 61  ? 48.639  -4.555  2.353   1.00 24.33  ? 40  CYS B CB  1 
ATOM   2757 S  SG  . CYS B 1 61  ? 47.024  -3.883  2.780   1.00 24.79  ? 40  CYS B SG  1 
ATOM   2758 N  N   . ILE B 1 62  ? 47.814  -3.273  -0.782  1.00 24.72  ? 41  ILE B N   1 
ATOM   2759 C  CA  . ILE B 1 62  ? 47.528  -2.032  -1.497  1.00 25.53  ? 41  ILE B CA  1 
ATOM   2760 C  C   . ILE B 1 62  ? 46.518  -1.264  -0.648  1.00 23.26  ? 41  ILE B C   1 
ATOM   2761 O  O   . ILE B 1 62  ? 45.346  -1.640  -0.570  1.00 20.86  ? 41  ILE B O   1 
ATOM   2762 C  CB  . ILE B 1 62  ? 47.005  -2.301  -2.913  1.00 22.54  ? 41  ILE B CB  1 
ATOM   2763 C  CG1 . ILE B 1 62  ? 48.029  -3.120  -3.708  1.00 21.36  ? 41  ILE B CG1 1 
ATOM   2764 C  CG2 . ILE B 1 62  ? 46.725  -0.994  -3.639  1.00 26.06  ? 41  ILE B CG2 1 
ATOM   2765 C  CD1 . ILE B 1 62  ? 47.602  -3.432  -5.122  1.00 24.14  ? 41  ILE B CD1 1 
ATOM   2766 N  N   . VAL B 1 63  ? 46.977  -0.193  -0.005  1.00 24.04  ? 42  VAL B N   1 
ATOM   2767 C  CA  . VAL B 1 63  ? 46.258  0.383   1.147   1.00 20.93  ? 42  VAL B CA  1 
ATOM   2768 C  C   . VAL B 1 63  ? 45.323  1.458   0.608   1.00 21.93  ? 42  VAL B C   1 
ATOM   2769 O  O   . VAL B 1 63  ? 45.550  2.663   0.748   1.00 25.79  ? 42  VAL B O   1 
ATOM   2770 C  CB  . VAL B 1 63  ? 47.224  0.927   2.205   1.00 25.83  ? 42  VAL B CB  1 
ATOM   2771 C  CG1 . VAL B 1 63  ? 47.902  -0.212  2.928   1.00 23.76  ? 42  VAL B CG1 1 
ATOM   2772 C  CG2 . VAL B 1 63  ? 48.270  1.846   1.560   1.00 24.60  ? 42  VAL B CG2 1 
ATOM   2773 N  N   . ASP B 1 64  ? 44.181  1.016   0.073   1.00 19.58  ? 43  ASP B N   1 
ATOM   2774 C  CA  . ASP B 1 64  ? 43.187  1.982   -0.383  1.00 22.41  ? 43  ASP B CA  1 
ATOM   2775 C  C   . ASP B 1 64  ? 42.410  2.612   0.771   1.00 21.78  ? 43  ASP B C   1 
ATOM   2776 O  O   . ASP B 1 64  ? 41.889  3.722   0.611   1.00 22.17  ? 43  ASP B O   1 
ATOM   2777 C  CB  . ASP B 1 64  ? 42.219  1.350   -1.397  1.00 19.53  ? 43  ASP B CB  1 
ATOM   2778 C  CG  . ASP B 1 64  ? 41.514  0.111   -0.875  1.00 20.65  ? 43  ASP B CG  1 
ATOM   2779 O  OD1 . ASP B 1 64  ? 41.893  -0.410  0.190   1.00 20.30  ? 43  ASP B OD1 1 
ATOM   2780 O  OD2 . ASP B 1 64  ? 40.564  -0.345  -1.551  1.00 19.26  ? 43  ASP B OD2 1 
ATOM   2781 N  N   . GLN B 1 65  ? 42.338  1.957   1.934   1.00 20.40  ? 44  GLN B N   1 
ATOM   2782 C  CA  . GLN B 1 65  ? 41.668  2.583   3.071   1.00 24.05  ? 44  GLN B CA  1 
ATOM   2783 C  C   . GLN B 1 65  ? 42.516  3.690   3.687   1.00 18.47  ? 44  GLN B C   1 
ATOM   2784 O  O   . GLN B 1 65  ? 41.968  4.645   4.248   1.00 24.07  ? 44  GLN B O   1 
ATOM   2785 C  CB  . GLN B 1 65  ? 41.315  1.535   4.124   1.00 23.26  ? 44  GLN B CB  1 
ATOM   2786 C  CG  . GLN B 1 65  ? 40.159  0.641   3.725   1.00 19.23  ? 44  GLN B CG  1 
ATOM   2787 C  CD  . GLN B 1 65  ? 39.951  -0.496  4.702   1.00 25.26  ? 44  GLN B CD  1 
ATOM   2788 O  OE1 . GLN B 1 65  ? 40.763  -1.415  4.783   1.00 29.24  ? 44  GLN B OE1 1 
ATOM   2789 N  NE2 . GLN B 1 65  ? 38.863  -0.434  5.456   1.00 25.66  ? 44  GLN B NE2 1 
ATOM   2790 N  N   . HIS B 1 66  ? 43.845  3.577   3.608   1.00 18.68  ? 45  HIS B N   1 
ATOM   2791 C  CA  . HIS B 1 66  ? 44.704  4.692   3.993   1.00 23.61  ? 45  HIS B CA  1 
ATOM   2792 C  C   . HIS B 1 66  ? 44.633  5.829   2.982   1.00 23.79  ? 45  HIS B C   1 
ATOM   2793 O  O   . HIS B 1 66  ? 44.779  6.999   3.356   1.00 22.77  ? 45  HIS B O   1 
ATOM   2794 C  CB  . HIS B 1 66  ? 46.150  4.220   4.144   1.00 20.22  ? 45  HIS B CB  1 
ATOM   2795 C  CG  . HIS B 1 66  ? 46.403  3.454   5.402   1.00 24.51  ? 45  HIS B CG  1 
ATOM   2796 N  ND1 . HIS B 1 66  ? 46.415  4.052   6.643   1.00 20.91  ? 45  HIS B ND1 1 
ATOM   2797 C  CD2 . HIS B 1 66  ? 46.654  2.140   5.613   1.00 27.03  ? 45  HIS B CD2 1 
ATOM   2798 C  CE1 . HIS B 1 66  ? 46.659  3.139   7.566   1.00 27.15  ? 45  HIS B CE1 1 
ATOM   2799 N  NE2 . HIS B 1 66  ? 46.808  1.970   6.967   1.00 28.93  ? 45  HIS B NE2 1 
ATOM   2800 N  N   . ALA B 1 67  ? 44.404  5.508   1.707   1.00 21.31  ? 46  ALA B N   1 
ATOM   2801 C  CA  . ALA B 1 67  ? 44.427  6.526   0.663   1.00 22.27  ? 46  ALA B CA  1 
ATOM   2802 C  C   . ALA B 1 67  ? 43.295  7.532   0.819   1.00 23.61  ? 46  ALA B C   1 
ATOM   2803 O  O   . ALA B 1 67  ? 43.474  8.712   0.500   1.00 22.61  ? 46  ALA B O   1 
ATOM   2804 C  CB  . ALA B 1 67  ? 44.353  5.867   -0.717  1.00 22.99  ? 46  ALA B CB  1 
ATOM   2805 N  N   . ILE B 1 68  ? 42.127  7.096   1.303   1.00 26.43  ? 47  ILE B N   1 
ATOM   2806 C  CA  . ILE B 1 68  ? 40.976  7.994   1.382   1.00 27.68  ? 47  ILE B CA  1 
ATOM   2807 C  C   . ILE B 1 68  ? 41.026  8.920   2.586   1.00 24.77  ? 47  ILE B C   1 
ATOM   2808 O  O   . ILE B 1 68  ? 40.059  9.654   2.824   1.00 24.02  ? 47  ILE B O   1 
ATOM   2809 C  CB  . ILE B 1 68  ? 39.640  7.223   1.411   1.00 22.33  ? 47  ILE B CB  1 
ATOM   2810 C  CG1 . ILE B 1 68  ? 39.538  6.331   2.653   1.00 25.14  ? 47  ILE B CG1 1 
ATOM   2811 C  CG2 . ILE B 1 68  ? 39.487  6.401   0.138   1.00 23.22  ? 47  ILE B CG2 1 
ATOM   2812 C  CD1 . ILE B 1 68  ? 38.150  5.734   2.862   1.00 21.54  ? 47  ILE B CD1 1 
ATOM   2813 N  N   . THR B 1 69  ? 42.108  8.898   3.369   1.00 22.59  ? 48  THR B N   1 
ATOM   2814 C  CA  . THR B 1 69  ? 42.335  9.971   4.329   1.00 23.01  ? 48  THR B CA  1 
ATOM   2815 C  C   . THR B 1 69  ? 42.586  11.298  3.631   1.00 28.81  ? 48  THR B C   1 
ATOM   2816 O  O   . THR B 1 69  ? 42.577  12.342  4.288   1.00 25.76  ? 48  THR B O   1 
ATOM   2817 C  CB  . THR B 1 69  ? 43.519  9.658   5.240   1.00 20.81  ? 48  THR B CB  1 
ATOM   2818 O  OG1 . THR B 1 69  ? 44.692  9.425   4.449   1.00 25.48  ? 48  THR B OG1 1 
ATOM   2819 C  CG2 . THR B 1 69  ? 43.225  8.452   6.097   1.00 23.92  ? 48  THR B CG2 1 
ATOM   2820 N  N   . VAL B 1 70  ? 42.843  11.264  2.327   1.00 27.39  ? 49  VAL B N   1 
ATOM   2821 C  CA  . VAL B 1 70  ? 42.874  12.440  1.470   1.00 28.98  ? 49  VAL B CA  1 
ATOM   2822 C  C   . VAL B 1 70  ? 41.751  12.284  0.457   1.00 29.96  ? 49  VAL B C   1 
ATOM   2823 O  O   . VAL B 1 70  ? 41.589  11.208  -0.130  1.00 30.63  ? 49  VAL B O   1 
ATOM   2824 C  CB  . VAL B 1 70  ? 44.231  12.590  0.758   1.00 31.76  ? 49  VAL B CB  1 
ATOM   2825 C  CG1 . VAL B 1 70  ? 44.172  13.711  -0.267  1.00 31.52  ? 49  VAL B CG1 1 
ATOM   2826 C  CG2 . VAL B 1 70  ? 45.333  12.839  1.772   1.00 28.27  ? 49  VAL B CG2 1 
ATOM   2827 N  N   . ARG B 1 71  ? 40.970  13.344  0.262   1.00 32.51  ? 50  ARG B N   1 
ATOM   2828 C  CA  . ARG B 1 71  ? 39.881  13.290  -0.702  1.00 38.22  ? 50  ARG B CA  1 
ATOM   2829 C  C   . ARG B 1 71  ? 40.398  12.785  -2.039  1.00 34.73  ? 50  ARG B C   1 
ATOM   2830 O  O   . ARG B 1 71  ? 41.418  13.257  -2.544  1.00 36.71  ? 50  ARG B O   1 
ATOM   2831 C  CB  . ARG B 1 71  ? 39.247  14.667  -0.877  1.00 41.93  ? 50  ARG B CB  1 
ATOM   2832 C  CG  . ARG B 1 71  ? 38.221  15.004  0.172   1.00 44.40  ? 50  ARG B CG  1 
ATOM   2833 C  CD  . ARG B 1 71  ? 36.949  14.187  0.009   1.00 38.05  ? 50  ARG B CD  1 
ATOM   2834 N  NE  . ARG B 1 71  ? 35.973  14.571  1.020   1.00 37.38  ? 50  ARG B NE  1 
ATOM   2835 C  CZ  . ARG B 1 71  ? 36.100  14.310  2.314   1.00 45.29  ? 50  ARG B CZ  1 
ATOM   2836 N  NH1 . ARG B 1 71  ? 37.135  13.632  2.785   1.00 44.08  ? 50  ARG B NH1 1 
ATOM   2837 N  NH2 . ARG B 1 71  ? 35.171  14.748  3.158   1.00 44.03  ? 50  ARG B NH2 1 
ATOM   2838 N  N   . GLN B 1 72  ? 39.685  11.819  -2.605  1.00 31.19  ? 51  GLN B N   1 
ATOM   2839 C  CA  . GLN B 1 72  ? 40.106  11.114  -3.804  1.00 31.97  ? 51  GLN B CA  1 
ATOM   2840 C  C   . GLN B 1 72  ? 38.993  11.190  -4.837  1.00 28.90  ? 51  GLN B C   1 
ATOM   2841 O  O   . GLN B 1 72  ? 37.816  11.040  -4.500  1.00 31.12  ? 51  GLN B O   1 
ATOM   2842 C  CB  . GLN B 1 72  ? 40.431  9.647   -3.478  1.00 35.05  ? 51  GLN B CB  1 
ATOM   2843 C  CG  . GLN B 1 72  ? 41.667  9.089   -4.172  1.00 38.84  ? 51  GLN B CG  1 
ATOM   2844 C  CD  . GLN B 1 72  ? 42.953  9.427   -3.453  1.00 37.97  ? 51  GLN B CD  1 
ATOM   2845 O  OE1 . GLN B 1 72  ? 42.943  9.997   -2.360  1.00 37.27  ? 51  GLN B OE1 1 
ATOM   2846 N  NE2 . GLN B 1 72  ? 44.075  9.066   -4.060  1.00 46.21  ? 51  GLN B NE2 1 
ATOM   2847 N  N   . ASP B 1 73  ? 39.359  11.440  -6.083  1.00 29.95  ? 52  ASP B N   1 
ATOM   2848 C  CA  . ASP B 1 73  ? 38.407  11.262  -7.172  1.00 28.13  ? 52  ASP B CA  1 
ATOM   2849 C  C   . ASP B 1 73  ? 38.113  9.771   -7.297  1.00 28.76  ? 52  ASP B C   1 
ATOM   2850 O  O   . ASP B 1 73  ? 39.054  8.981   -7.438  1.00 24.42  ? 52  ASP B O   1 
ATOM   2851 C  CB  . ASP B 1 73  ? 38.964  11.809  -8.476  1.00 31.47  ? 52  ASP B CB  1 
ATOM   2852 C  CG  . ASP B 1 73  ? 38.098  11.456  -9.661  1.00 32.98  ? 52  ASP B CG  1 
ATOM   2853 O  OD1 . ASP B 1 73  ? 37.015  12.059  -9.810  1.00 38.89  ? 52  ASP B OD1 1 
ATOM   2854 O  OD2 . ASP B 1 73  ? 38.493  10.565  -10.437 1.00 35.11  ? 52  ASP B OD2 1 
ATOM   2855 N  N   . PRO B 1 74  ? 36.849  9.334   -7.233  1.00 28.61  ? 53  PRO B N   1 
ATOM   2856 C  CA  . PRO B 1 74  ? 36.598  7.881   -7.182  1.00 27.09  ? 53  PRO B CA  1 
ATOM   2857 C  C   . PRO B 1 74  ? 37.149  7.119   -8.375  1.00 26.32  ? 53  PRO B C   1 
ATOM   2858 O  O   . PRO B 1 74  ? 37.741  6.046   -8.202  1.00 25.71  ? 53  PRO B O   1 
ATOM   2859 C  CB  . PRO B 1 74  ? 35.065  7.794   -7.114  1.00 32.42  ? 53  PRO B CB  1 
ATOM   2860 C  CG  . PRO B 1 74  ? 34.623  9.121   -6.589  1.00 29.83  ? 53  PRO B CG  1 
ATOM   2861 C  CD  . PRO B 1 74  ? 35.605  10.117  -7.115  1.00 23.46  ? 53  PRO B CD  1 
ATOM   2862 N  N   . GLN B 1 75  ? 36.981  7.648   -9.587  1.00 26.93  ? 54  GLN B N   1 
ATOM   2863 C  CA  . GLN B 1 75  ? 37.439  6.937   -10.775 1.00 31.15  ? 54  GLN B CA  1 
ATOM   2864 C  C   . GLN B 1 75  ? 38.955  6.794   -10.782 1.00 28.18  ? 54  GLN B C   1 
ATOM   2865 O  O   . GLN B 1 75  ? 39.487  5.749   -11.177 1.00 24.30  ? 54  GLN B O   1 
ATOM   2866 C  CB  . GLN B 1 75  ? 36.957  7.662   -12.030 1.00 36.97  ? 54  GLN B CB  1 
ATOM   2867 C  CG  . GLN B 1 75  ? 37.185  6.896   -13.317 1.00 45.79  ? 54  GLN B CG  1 
ATOM   2868 C  CD  . GLN B 1 75  ? 38.336  7.448   -14.135 1.00 59.58  ? 54  GLN B CD  1 
ATOM   2869 O  OE1 . GLN B 1 75  ? 39.476  7.503   -13.669 1.00 53.42  ? 54  GLN B OE1 1 
ATOM   2870 N  NE2 . GLN B 1 75  ? 38.042  7.866   -15.364 1.00 52.40  ? 54  GLN B NE2 1 
ATOM   2871 N  N   . ASN B 1 76  ? 39.671  7.834   -10.346 1.00 26.44  ? 55  ASN B N   1 
ATOM   2872 C  CA  . ASN B 1 76  ? 41.125  7.753   -10.294 1.00 22.88  ? 55  ASN B CA  1 
ATOM   2873 C  C   . ASN B 1 76  ? 41.601  6.812   -9.194  1.00 24.57  ? 55  ASN B C   1 
ATOM   2874 O  O   . ASN B 1 76  ? 42.636  6.155   -9.352  1.00 24.89  ? 55  ASN B O   1 
ATOM   2875 C  CB  . ASN B 1 76  ? 41.720  9.145   -10.096 1.00 30.10  ? 55  ASN B CB  1 
ATOM   2876 C  CG  . ASN B 1 76  ? 43.237  9.125   -10.033 1.00 37.77  ? 55  ASN B CG  1 
ATOM   2877 O  OD1 . ASN B 1 76  ? 43.827  9.251   -8.958  1.00 43.38  ? 55  ASN B OD1 1 
ATOM   2878 N  ND2 . ASN B 1 76  ? 43.877  8.951   -11.185 1.00 42.45  ? 55  ASN B ND2 1 
ATOM   2879 N  N   . LEU B 1 77  ? 40.878  6.741   -8.074  1.00 24.24  ? 56  LEU B N   1 
ATOM   2880 C  CA  . LEU B 1 77  ? 41.255  5.816   -7.011  1.00 21.89  ? 56  LEU B CA  1 
ATOM   2881 C  C   . LEU B 1 77  ? 41.147  4.373   -7.486  1.00 21.47  ? 56  LEU B C   1 
ATOM   2882 O  O   . LEU B 1 77  ? 42.060  3.567   -7.277  1.00 20.39  ? 56  LEU B O   1 
ATOM   2883 C  CB  . LEU B 1 77  ? 40.374  6.044   -5.783  1.00 22.07  ? 56  LEU B CB  1 
ATOM   2884 C  CG  . LEU B 1 77  ? 40.569  5.082   -4.608  1.00 20.74  ? 56  LEU B CG  1 
ATOM   2885 C  CD1 . LEU B 1 77  ? 42.033  4.970   -4.209  1.00 18.79  ? 56  LEU B CD1 1 
ATOM   2886 C  CD2 . LEU B 1 77  ? 39.732  5.540   -3.423  1.00 29.03  ? 56  LEU B CD2 1 
ATOM   2887 N  N   . ARG B 1 78  ? 40.029  4.035   -8.132  1.00 19.15  ? 57  ARG B N   1 
ATOM   2888 C  CA  . ARG B 1 78  ? 39.829  2.678   -8.632  1.00 21.23  ? 57  ARG B CA  1 
ATOM   2889 C  C   . ARG B 1 78  ? 40.878  2.319   -9.677  1.00 23.51  ? 57  ARG B C   1 
ATOM   2890 O  O   . ARG B 1 78  ? 41.465  1.231   -9.640  1.00 23.38  ? 57  ARG B O   1 
ATOM   2891 C  CB  . ARG B 1 78  ? 38.418  2.551   -9.210  1.00 22.69  ? 57  ARG B CB  1 
ATOM   2892 C  CG  . ARG B 1 78  ? 38.081  1.168   -9.734  1.00 27.54  ? 57  ARG B CG  1 
ATOM   2893 C  CD  . ARG B 1 78  ? 36.595  1.029   -10.036 1.00 30.64  ? 57  ARG B CD  1 
ATOM   2894 N  NE  . ARG B 1 78  ? 35.780  1.157   -8.831  1.00 36.76  ? 57  ARG B NE  1 
ATOM   2895 C  CZ  . ARG B 1 78  ? 35.038  2.213   -8.519  1.00 35.13  ? 57  ARG B CZ  1 
ATOM   2896 N  NH1 . ARG B 1 78  ? 34.955  3.265   -9.318  1.00 35.65  ? 57  ARG B NH1 1 
ATOM   2897 N  NH2 . ARG B 1 78  ? 34.364  2.214   -7.373  1.00 23.07  ? 57  ARG B NH2 1 
ATOM   2898 N  N   . LYS B 1 79  ? 41.131  3.232   -10.617 1.00 21.66  ? 58  LYS B N   1 
ATOM   2899 C  CA  . LYS B 1 79  ? 42.132  2.985   -11.649 1.00 24.03  ? 58  LYS B CA  1 
ATOM   2900 C  C   . LYS B 1 79  ? 43.525  2.831   -11.050 1.00 23.50  ? 58  LYS B C   1 
ATOM   2901 O  O   . LYS B 1 79  ? 44.306  1.976   -11.484 1.00 21.08  ? 58  LYS B O   1 
ATOM   2902 C  CB  . LYS B 1 79  ? 42.108  4.129   -12.668 1.00 29.22  ? 58  LYS B CB  1 
ATOM   2903 C  CG  . LYS B 1 79  ? 43.291  4.149   -13.618 1.00 30.56  ? 58  LYS B CG  1 
ATOM   2904 C  CD  . LYS B 1 79  ? 43.255  5.362   -14.536 1.00 38.01  ? 58  LYS B CD  1 
ATOM   2905 C  CE  . LYS B 1 79  ? 44.440  6.285   -14.274 1.00 46.54  ? 58  LYS B CE  1 
ATOM   2906 N  NZ  . LYS B 1 79  ? 45.747  5.601   -14.524 1.00 43.79  ? 58  LYS B NZ  1 
ATOM   2907 N  N   . ALA B 1 80  ? 43.864  3.663   -10.065 1.00 23.33  ? 59  ALA B N   1 
ATOM   2908 C  CA  . ALA B 1 80  ? 45.208  3.621   -9.498  1.00 22.39  ? 59  ALA B CA  1 
ATOM   2909 C  C   . ALA B 1 80  ? 45.438  2.351   -8.693  1.00 28.30  ? 59  ALA B C   1 
ATOM   2910 O  O   . ALA B 1 80  ? 46.579  1.882   -8.590  1.00 22.58  ? 59  ALA B O   1 
ATOM   2911 C  CB  . ALA B 1 80  ? 45.447  4.850   -8.622  1.00 23.08  ? 59  ALA B CB  1 
ATOM   2912 N  N   . THR B 1 81  ? 44.379  1.795   -8.095  1.00 19.20  ? 60  THR B N   1 
ATOM   2913 C  CA  . THR B 1 81  ? 44.519  0.529   -7.386  1.00 23.28  ? 60  THR B CA  1 
ATOM   2914 C  C   . THR B 1 81  ? 44.883  -0.591  -8.351  1.00 19.68  ? 60  THR B C   1 
ATOM   2915 O  O   . THR B 1 81  ? 45.750  -1.419  -8.055  1.00 21.01  ? 60  THR B O   1 
ATOM   2916 C  CB  . THR B 1 81  ? 43.225  0.190   -6.642  1.00 17.61  ? 60  THR B CB  1 
ATOM   2917 O  OG1 . THR B 1 81  ? 42.952  1.200   -5.664  1.00 24.73  ? 60  THR B OG1 1 
ATOM   2918 C  CG2 . THR B 1 81  ? 43.345  -1.165  -5.947  1.00 19.03  ? 60  THR B CG2 1 
ATOM   2919 N  N   . LEU B 1 82  ? 44.229  -0.627  -9.513  1.00 20.19  ? 61  LEU B N   1 
ATOM   2920 C  CA  . LEU B 1 82  ? 44.551  -1.633  -10.521 1.00 23.62  ? 61  LEU B CA  1 
ATOM   2921 C  C   . LEU B 1 82  ? 45.926  -1.391  -11.132 1.00 22.63  ? 61  LEU B C   1 
ATOM   2922 O  O   . LEU B 1 82  ? 46.666  -2.346  -11.390 1.00 21.97  ? 61  LEU B O   1 
ATOM   2923 C  CB  . LEU B 1 82  ? 43.472  -1.648  -11.602 1.00 22.09  ? 61  LEU B CB  1 
ATOM   2924 C  CG  . LEU B 1 82  ? 42.062  -1.934  -11.083 1.00 25.86  ? 61  LEU B CG  1 
ATOM   2925 C  CD1 . LEU B 1 82  ? 41.036  -1.860  -12.200 1.00 28.75  ? 61  LEU B CD1 1 
ATOM   2926 C  CD2 . LEU B 1 82  ? 42.004  -3.292  -10.394 1.00 27.66  ? 61  LEU B CD2 1 
ATOM   2927 N  N   . ASP B 1 83  ? 46.290  -0.124  -11.373 1.00 24.77  ? 62  ASP B N   1 
ATOM   2928 C  CA  . ASP B 1 83  ? 47.634  0.186   -11.854 1.00 20.02  ? 62  ASP B CA  1 
ATOM   2929 C  C   . ASP B 1 83  ? 48.688  -0.401  -10.925 1.00 22.40  ? 62  ASP B C   1 
ATOM   2930 O  O   . ASP B 1 83  ? 49.643  -1.049  -11.368 1.00 22.28  ? 62  ASP B O   1 
ATOM   2931 C  CB  . ASP B 1 83  ? 47.843  1.704   -11.949 1.00 24.55  ? 62  ASP B CB  1 
ATOM   2932 C  CG  . ASP B 1 83  ? 46.971  2.367   -12.998 1.00 28.81  ? 62  ASP B CG  1 
ATOM   2933 O  OD1 . ASP B 1 83  ? 46.265  1.659   -13.735 1.00 33.51  ? 62  ASP B OD1 1 
ATOM   2934 O  OD2 . ASP B 1 83  ? 46.992  3.614   -13.080 1.00 29.69  ? 62  ASP B OD2 1 
ATOM   2935 N  N   . THR B 1 84  ? 48.531  -0.162  -9.620  1.00 20.23  ? 63  THR B N   1 
ATOM   2936 C  CA  . THR B 1 84  ? 49.523  -0.614  -8.651  1.00 17.57  ? 63  THR B CA  1 
ATOM   2937 C  C   . THR B 1 84  ? 49.596  -2.132  -8.602  1.00 20.61  ? 63  THR B C   1 
ATOM   2938 O  O   . THR B 1 84  ? 50.690  -2.705  -8.556  1.00 18.27  ? 63  THR B O   1 
ATOM   2939 C  CB  . THR B 1 84  ? 49.191  -0.042  -7.273  1.00 22.53  ? 63  THR B CB  1 
ATOM   2940 O  OG1 . THR B 1 84  ? 49.387  1.378   -7.295  1.00 29.39  ? 63  THR B OG1 1 
ATOM   2941 C  CG2 . THR B 1 84  ? 50.066  -0.660  -6.197  1.00 22.01  ? 63  THR B CG2 1 
ATOM   2942 N  N   . LEU B 1 85  ? 48.443  -2.803  -8.610  1.00 21.07  ? 64  LEU B N   1 
ATOM   2943 C  CA  . LEU B 1 85  ? 48.445  -4.262  -8.596  1.00 23.39  ? 64  LEU B CA  1 
ATOM   2944 C  C   . LEU B 1 85  ? 49.189  -4.814  -9.805  1.00 19.81  ? 64  LEU B C   1 
ATOM   2945 O  O   . LEU B 1 85  ? 50.065  -5.676  -9.675  1.00 23.93  ? 64  LEU B O   1 
ATOM   2946 C  CB  . LEU B 1 85  ? 47.009  -4.790  -8.566  1.00 22.81  ? 64  LEU B CB  1 
ATOM   2947 C  CG  . LEU B 1 85  ? 46.841  -6.308  -8.715  1.00 22.23  ? 64  LEU B CG  1 
ATOM   2948 C  CD1 . LEU B 1 85  ? 47.572  -7.049  -7.604  1.00 21.37  ? 64  LEU B CD1 1 
ATOM   2949 C  CD2 . LEU B 1 85  ? 45.367  -6.693  -8.732  1.00 22.34  ? 64  LEU B CD2 1 
ATOM   2950 N  N   . ALA B 1 86  ? 48.858  -4.312  -10.995 1.00 21.48  ? 65  ALA B N   1 
ATOM   2951 C  CA  . ALA B 1 86  ? 49.476  -4.824  -12.211 1.00 18.37  ? 65  ALA B CA  1 
ATOM   2952 C  C   . ALA B 1 86  ? 50.974  -4.559  -12.235 1.00 18.89  ? 65  ALA B C   1 
ATOM   2953 O  O   . ALA B 1 86  ? 51.736  -5.368  -12.774 1.00 22.33  ? 65  ALA B O   1 
ATOM   2954 C  CB  . ALA B 1 86  ? 48.804  -4.202  -13.431 1.00 19.13  ? 65  ALA B CB  1 
ATOM   2955 N  N   . LEU B 1 87  ? 51.415  -3.433  -11.671 1.00 21.64  ? 66  LEU B N   1 
ATOM   2956 C  CA  . LEU B 1 87  ? 52.837  -3.110  -11.691 1.00 23.13  ? 66  LEU B CA  1 
ATOM   2957 C  C   . LEU B 1 87  ? 53.637  -4.056  -10.801 1.00 25.19  ? 66  LEU B C   1 
ATOM   2958 O  O   . LEU B 1 87  ? 54.715  -4.513  -11.191 1.00 22.11  ? 66  LEU B O   1 
ATOM   2959 C  CB  . LEU B 1 87  ? 53.046  -1.661  -11.262 1.00 21.71  ? 66  LEU B CB  1 
ATOM   2960 C  CG  . LEU B 1 87  ? 54.487  -1.153  -11.296 1.00 27.64  ? 66  LEU B CG  1 
ATOM   2961 C  CD1 . LEU B 1 87  ? 55.086  -1.296  -12.686 1.00 34.00  ? 66  LEU B CD1 1 
ATOM   2962 C  CD2 . LEU B 1 87  ? 54.543  0.296   -10.840 1.00 32.26  ? 66  LEU B CD2 1 
ATOM   2963 N  N   . TYR B 1 88  ? 53.133  -4.352  -9.599  1.00 24.81  ? 67  TYR B N   1 
ATOM   2964 C  CA  . TYR B 1 88  ? 53.823  -5.296  -8.723  1.00 24.48  ? 67  TYR B CA  1 
ATOM   2965 C  C   . TYR B 1 88  ? 53.850  -6.694  -9.330  1.00 20.36  ? 67  TYR B C   1 
ATOM   2966 O  O   . TYR B 1 88  ? 54.856  -7.405  -9.225  1.00 17.59  ? 67  TYR B O   1 
ATOM   2967 C  CB  . TYR B 1 88  ? 53.155  -5.321  -7.349  1.00 25.60  ? 67  TYR B CB  1 
ATOM   2968 C  CG  . TYR B 1 88  ? 53.631  -4.228  -6.419  1.00 25.97  ? 67  TYR B CG  1 
ATOM   2969 C  CD1 . TYR B 1 88  ? 53.121  -2.941  -6.508  1.00 30.54  ? 67  TYR B CD1 1 
ATOM   2970 C  CD2 . TYR B 1 88  ? 54.586  -4.487  -5.448  1.00 30.20  ? 67  TYR B CD2 1 
ATOM   2971 C  CE1 . TYR B 1 88  ? 53.553  -1.938  -5.654  1.00 31.17  ? 67  TYR B CE1 1 
ATOM   2972 C  CE2 . TYR B 1 88  ? 55.023  -3.493  -4.592  1.00 36.56  ? 67  TYR B CE2 1 
ATOM   2973 C  CZ  . TYR B 1 88  ? 54.503  -2.221  -4.700  1.00 31.15  ? 67  TYR B CZ  1 
ATOM   2974 O  OH  . TYR B 1 88  ? 54.937  -1.231  -3.849  1.00 28.60  ? 67  TYR B OH  1 
ATOM   2975 N  N   . LEU B 1 89  ? 52.746  -7.113  -9.952  1.00 20.02  ? 68  LEU B N   1 
ATOM   2976 C  CA  . LEU B 1 89  ? 52.751  -8.368  -10.696 1.00 19.68  ? 68  LEU B CA  1 
ATOM   2977 C  C   . LEU B 1 89  ? 53.761  -8.322  -11.838 1.00 21.33  ? 68  LEU B C   1 
ATOM   2978 O  O   . LEU B 1 89  ? 54.415  -9.326  -12.141 1.00 23.64  ? 68  LEU B O   1 
ATOM   2979 C  CB  . LEU B 1 89  ? 51.356  -8.664  -11.246 1.00 24.04  ? 68  LEU B CB  1 
ATOM   2980 C  CG  . LEU B 1 89  ? 50.203  -8.854  -10.259 1.00 21.47  ? 68  LEU B CG  1 
ATOM   2981 C  CD1 . LEU B 1 89  ? 48.884  -8.929  -11.013 1.00 22.73  ? 68  LEU B CD1 1 
ATOM   2982 C  CD2 . LEU B 1 89  ? 50.388  -10.100 -9.404  1.00 26.63  ? 68  LEU B CD2 1 
ATOM   2983 N  N   . ALA B 1 90  ? 53.888  -7.167  -12.494 1.00 21.47  ? 69  ALA B N   1 
ATOM   2984 C  CA  . ALA B 1 90  ? 54.860  -7.028  -13.573 1.00 29.82  ? 69  ALA B CA  1 
ATOM   2985 C  C   . ALA B 1 90  ? 56.284  -7.163  -13.051 1.00 29.78  ? 69  ALA B C   1 
ATOM   2986 O  O   . ALA B 1 90  ? 57.149  -7.740  -13.719 1.00 26.74  ? 69  ALA B O   1 
ATOM   2987 C  CB  . ALA B 1 90  ? 54.672  -5.683  -14.273 1.00 29.15  ? 69  ALA B CB  1 
ATOM   2988 N  N   . CYS B 1 91  ? 56.551  -6.622  -11.864 1.00 22.40  ? 70  CYS B N   1 
ATOM   2989 C  CA  . CYS B 1 91  ? 57.874  -6.748  -11.270 1.00 25.84  ? 70  CYS B CA  1 
ATOM   2990 C  C   . CYS B 1 91  ? 58.184  -8.177  -10.851 1.00 25.71  ? 70  CYS B C   1 
ATOM   2991 O  O   . CYS B 1 91  ? 59.351  -8.491  -10.595 1.00 30.05  ? 70  CYS B O   1 
ATOM   2992 C  CB  . CYS B 1 91  ? 57.987  -5.796  -10.079 1.00 26.04  ? 70  CYS B CB  1 
ATOM   2993 S  SG  . CYS B 1 91  ? 57.958  -4.039  -10.547 1.00 31.40  ? 70  CYS B SG  1 
ATOM   2994 N  N   . GLY B 1 92  ? 57.183  -9.050  -10.798 1.00 23.89  ? 71  GLY B N   1 
ATOM   2995 C  CA  . GLY B 1 92  ? 57.397  -10.447 -10.498 1.00 25.82  ? 71  GLY B CA  1 
ATOM   2996 C  C   . GLY B 1 92  ? 56.812  -10.939 -9.194  1.00 26.06  ? 71  GLY B C   1 
ATOM   2997 O  O   . GLY B 1 92  ? 57.098  -12.075 -8.803  1.00 28.15  ? 71  GLY B O   1 
ATOM   2998 N  N   . ILE B 1 93  ? 56.014  -10.127 -8.496  1.00 27.92  ? 72  ILE B N   1 
ATOM   2999 C  CA  . ILE B 1 93  ? 55.347  -10.619 -7.299  1.00 25.64  ? 72  ILE B CA  1 
ATOM   3000 C  C   . ILE B 1 93  ? 54.390  -11.733 -7.698  1.00 22.72  ? 72  ILE B C   1 
ATOM   3001 O  O   . ILE B 1 93  ? 53.535  -11.560 -8.577  1.00 19.28  ? 72  ILE B O   1 
ATOM   3002 C  CB  . ILE B 1 93  ? 54.623  -9.479  -6.570  1.00 26.06  ? 72  ILE B CB  1 
ATOM   3003 C  CG1 . ILE B 1 93  ? 55.620  -8.399  -6.142  1.00 28.29  ? 72  ILE B CG1 1 
ATOM   3004 C  CG2 . ILE B 1 93  ? 53.890  -10.011 -5.350  1.00 23.99  ? 72  ILE B CG2 1 
ATOM   3005 C  CD1 . ILE B 1 93  ? 56.779  -8.918  -5.308  1.00 30.19  ? 72  ILE B CD1 1 
ATOM   3006 N  N   . ASP B 1 94  ? 54.532  -12.884 -7.042  1.00 25.45  ? 73  ASP B N   1 
ATOM   3007 C  CA  . ASP B 1 94  ? 53.835  -14.107 -7.418  1.00 25.91  ? 73  ASP B CA  1 
ATOM   3008 C  C   . ASP B 1 94  ? 52.629  -14.277 -6.513  1.00 26.44  ? 73  ASP B C   1 
ATOM   3009 O  O   . ASP B 1 94  ? 52.810  -14.425 -5.297  1.00 24.55  ? 73  ASP B O   1 
ATOM   3010 C  CB  . ASP B 1 94  ? 54.780  -15.303 -7.288  1.00 25.26  ? 73  ASP B CB  1 
ATOM   3011 C  CG  . ASP B 1 94  ? 54.188  -16.599 -7.835  1.00 27.90  ? 73  ASP B CG  1 
ATOM   3012 O  OD1 . ASP B 1 94  ? 53.017  -16.912 -7.530  1.00 24.07  ? 73  ASP B OD1 1 
ATOM   3013 O  OD2 . ASP B 1 94  ? 54.904  -17.315 -8.571  1.00 25.70  ? 73  ASP B OD2 1 
ATOM   3014 N  N   . PRO B 1 95  ? 51.397  -14.249 -7.030  1.00 20.75  ? 74  PRO B N   1 
ATOM   3015 C  CA  . PRO B 1 95  ? 50.230  -14.308 -6.131  1.00 20.76  ? 74  PRO B CA  1 
ATOM   3016 C  C   . PRO B 1 95  ? 50.133  -15.595 -5.327  1.00 24.79  ? 74  PRO B C   1 
ATOM   3017 O  O   . PRO B 1 95  ? 49.439  -15.618 -4.304  1.00 19.90  ? 74  PRO B O   1 
ATOM   3018 C  CB  . PRO B 1 95  ? 49.034  -14.163 -7.084  1.00 24.64  ? 74  PRO B CB  1 
ATOM   3019 C  CG  . PRO B 1 95  ? 49.593  -13.606 -8.347  1.00 22.23  ? 74  PRO B CG  1 
ATOM   3020 C  CD  . PRO B 1 95  ? 51.001  -14.106 -8.441  1.00 22.45  ? 74  PRO B CD  1 
ATOM   3021 N  N   . GLN B 1 96  ? 50.785  -16.672 -5.761  1.00 26.90  ? 75  GLN B N   1 
ATOM   3022 C  CA  . GLN B 1 96  ? 50.744  -17.922 -5.013  1.00 27.53  ? 75  GLN B CA  1 
ATOM   3023 C  C   . GLN B 1 96  ? 51.852  -18.020 -3.968  1.00 27.94  ? 75  GLN B C   1 
ATOM   3024 O  O   . GLN B 1 96  ? 51.617  -18.541 -2.872  1.00 32.93  ? 75  GLN B O   1 
ATOM   3025 C  CB  . GLN B 1 96  ? 50.824  -19.108 -5.975  1.00 23.75  ? 75  GLN B CB  1 
ATOM   3026 C  CG  . GLN B 1 96  ? 49.645  -19.201 -6.929  1.00 25.92  ? 75  GLN B CG  1 
ATOM   3027 C  CD  . GLN B 1 96  ? 49.824  -18.363 -8.183  1.00 26.60  ? 75  GLN B CD  1 
ATOM   3028 O  OE1 . GLN B 1 96  ? 50.923  -18.265 -8.731  1.00 25.28  ? 75  GLN B OE1 1 
ATOM   3029 N  NE2 . GLN B 1 96  ? 48.739  -17.762 -8.648  1.00 29.90  ? 75  GLN B NE2 1 
ATOM   3030 N  N   . LYS B 1 97  ? 53.062  -17.547 -4.276  1.00 31.22  ? 76  LYS B N   1 
ATOM   3031 C  CA  . LYS B 1 97  ? 54.117  -17.554 -3.266  1.00 28.68  ? 76  LYS B CA  1 
ATOM   3032 C  C   . LYS B 1 97  ? 53.876  -16.483 -2.212  1.00 27.01  ? 76  LYS B C   1 
ATOM   3033 O  O   . LYS B 1 97  ? 54.039  -16.731 -1.012  1.00 33.56  ? 76  LYS B O   1 
ATOM   3034 C  CB  . LYS B 1 97  ? 55.483  -17.335 -3.908  1.00 29.45  ? 76  LYS B CB  1 
ATOM   3035 C  CG  . LYS B 1 97  ? 55.844  -18.286 -5.025  1.00 34.36  ? 76  LYS B CG  1 
ATOM   3036 C  CD  . LYS B 1 97  ? 57.322  -18.138 -5.357  1.00 33.01  ? 76  LYS B CD  1 
ATOM   3037 C  CE  . LYS B 1 97  ? 57.711  -18.919 -6.585  1.00 39.37  ? 76  LYS B CE  1 
ATOM   3038 N  NZ  . LYS B 1 97  ? 59.185  -18.875 -6.799  1.00 50.22  ? 76  LYS B NZ  1 
ATOM   3039 N  N   . SER B 1 98  ? 53.507  -15.283 -2.645  1.00 24.38  ? 77  SER B N   1 
ATOM   3040 C  CA  . SER B 1 98  ? 53.284  -14.145 -1.774  1.00 25.97  ? 77  SER B CA  1 
ATOM   3041 C  C   . SER B 1 98  ? 51.791  -13.883 -1.624  1.00 25.99  ? 77  SER B C   1 
ATOM   3042 O  O   . SER B 1 98  ? 50.955  -14.482 -2.302  1.00 26.32  ? 77  SER B O   1 
ATOM   3043 C  CB  . SER B 1 98  ? 53.991  -12.903 -2.329  1.00 24.27  ? 77  SER B CB  1 
ATOM   3044 O  OG  . SER B 1 98  ? 55.390  -13.112 -2.429  1.00 30.93  ? 77  SER B OG  1 
ATOM   3045 N  N   . THR B 1 99  ? 51.468  -12.966 -0.720  1.00 24.72  ? 78  THR B N   1 
ATOM   3046 C  CA  . THR B 1 99  ? 50.096  -12.549 -0.457  1.00 26.73  ? 78  THR B CA  1 
ATOM   3047 C  C   . THR B 1 99  ? 49.985  -11.087 -0.876  1.00 26.13  ? 78  THR B C   1 
ATOM   3048 O  O   . THR B 1 99  ? 50.441  -10.195 -0.160  1.00 29.86  ? 78  THR B O   1 
ATOM   3049 C  CB  . THR B 1 99  ? 49.737  -12.731 1.016   1.00 23.87  ? 78  THR B CB  1 
ATOM   3050 O  OG1 . THR B 1 99  ? 50.099  -14.049 1.447   1.00 28.86  ? 78  THR B OG1 1 
ATOM   3051 C  CG2 . THR B 1 99  ? 48.251  -12.529 1.223   1.00 26.08  ? 78  THR B CG2 1 
ATOM   3052 N  N   . ILE B 1 100 ? 49.379  -10.844 -2.032  1.00 24.30  ? 79  ILE B N   1 
ATOM   3053 C  CA  . ILE B 1 100 ? 49.165  -9.496  -2.544  1.00 24.09  ? 79  ILE B CA  1 
ATOM   3054 C  C   . ILE B 1 100 ? 47.665  -9.296  -2.719  1.00 24.20  ? 79  ILE B C   1 
ATOM   3055 O  O   . ILE B 1 100 ? 46.985  -10.138 -3.318  1.00 17.55  ? 79  ILE B O   1 
ATOM   3056 C  CB  . ILE B 1 100 ? 49.940  -9.263  -3.856  1.00 24.44  ? 79  ILE B CB  1 
ATOM   3057 C  CG1 . ILE B 1 100 ? 49.704  -7.843  -4.369  1.00 25.21  ? 79  ILE B CG1 1 
ATOM   3058 C  CG2 . ILE B 1 100 ? 49.576  -10.310 -4.912  1.00 23.46  ? 79  ILE B CG2 1 
ATOM   3059 C  CD1 . ILE B 1 100 ? 50.774  -7.375  -5.325  1.00 25.48  ? 79  ILE B CD1 1 
ATOM   3060 N  N   . PHE B 1 101 ? 47.148  -8.202  -2.161  1.00 18.60  ? 80  PHE B N   1 
ATOM   3061 C  CA  . PHE B 1 101 ? 45.708  -8.004  -2.054  1.00 15.65  ? 80  PHE B CA  1 
ATOM   3062 C  C   . PHE B 1 101 ? 45.423  -6.522  -1.857  1.00 17.12  ? 80  PHE B C   1 
ATOM   3063 O  O   . PHE B 1 101 ? 46.316  -5.733  -1.539  1.00 18.07  ? 80  PHE B O   1 
ATOM   3064 C  CB  . PHE B 1 101 ? 45.131  -8.814  -0.887  1.00 18.33  ? 80  PHE B CB  1 
ATOM   3065 C  CG  . PHE B 1 101 ? 45.609  -8.345  0.460   1.00 19.52  ? 80  PHE B CG  1 
ATOM   3066 C  CD1 . PHE B 1 101 ? 46.876  -8.678  0.912   1.00 20.32  ? 80  PHE B CD1 1 
ATOM   3067 C  CD2 . PHE B 1 101 ? 44.801  -7.562  1.267   1.00 23.83  ? 80  PHE B CD2 1 
ATOM   3068 C  CE1 . PHE B 1 101 ? 47.328  -8.245  2.144   1.00 20.75  ? 80  PHE B CE1 1 
ATOM   3069 C  CE2 . PHE B 1 101 ? 45.248  -7.124  2.508   1.00 22.60  ? 80  PHE B CE2 1 
ATOM   3070 C  CZ  . PHE B 1 101 ? 46.516  -7.465  2.942   1.00 19.89  ? 80  PHE B CZ  1 
ATOM   3071 N  N   . VAL B 1 102 ? 44.155  -6.162  -2.041  1.00 15.19  ? 81  VAL B N   1 
ATOM   3072 C  CA  . VAL B 1 102 ? 43.660  -4.814  -1.783  1.00 18.26  ? 81  VAL B CA  1 
ATOM   3073 C  C   . VAL B 1 102 ? 43.125  -4.756  -0.354  1.00 18.54  ? 81  VAL B C   1 
ATOM   3074 O  O   . VAL B 1 102 ? 42.371  -5.636  0.077   1.00 19.71  ? 81  VAL B O   1 
ATOM   3075 C  CB  . VAL B 1 102 ? 42.574  -4.426  -2.800  1.00 16.94  ? 81  VAL B CB  1 
ATOM   3076 C  CG1 . VAL B 1 102 ? 42.028  -3.040  -2.512  1.00 18.04  ? 81  VAL B CG1 1 
ATOM   3077 C  CG2 . VAL B 1 102 ? 43.128  -4.488  -4.221  1.00 18.57  ? 81  VAL B CG2 1 
ATOM   3078 N  N   . GLN B 1 103 ? 43.505  -3.707  0.374   1.00 15.19  ? 82  GLN B N   1 
ATOM   3079 C  CA  . GLN B 1 103 ? 43.249  -3.650  1.811   1.00 16.83  ? 82  GLN B CA  1 
ATOM   3080 C  C   . GLN B 1 103 ? 41.759  -3.731  2.128   1.00 18.15  ? 82  GLN B C   1 
ATOM   3081 O  O   . GLN B 1 103 ? 41.352  -4.466  3.035   1.00 20.01  ? 82  GLN B O   1 
ATOM   3082 C  CB  . GLN B 1 103 ? 43.849  -2.362  2.373   1.00 17.88  ? 82  GLN B CB  1 
ATOM   3083 C  CG  . GLN B 1 103 ? 43.874  -2.251  3.891   1.00 19.21  ? 82  GLN B CG  1 
ATOM   3084 C  CD  . GLN B 1 103 ? 44.291  -0.863  4.333   1.00 21.29  ? 82  GLN B CD  1 
ATOM   3085 O  OE1 . GLN B 1 103 ? 44.299  0.074   3.534   1.00 21.01  ? 82  GLN B OE1 1 
ATOM   3086 N  NE2 . GLN B 1 103 ? 44.643  -0.723  5.601   1.00 24.72  ? 82  GLN B NE2 1 
ATOM   3087 N  N   . SER B 1 104 ? 40.930  -2.987  1.395   1.00 16.42  ? 83  SER B N   1 
ATOM   3088 C  CA  . SER B 1 104 ? 39.499  -2.936  1.669   1.00 16.74  ? 83  SER B CA  1 
ATOM   3089 C  C   . SER B 1 104 ? 38.791  -4.267  1.437   1.00 17.60  ? 83  SER B C   1 
ATOM   3090 O  O   . SER B 1 104 ? 37.653  -4.420  1.887   1.00 18.33  ? 83  SER B O   1 
ATOM   3091 C  CB  . SER B 1 104 ? 38.844  -1.847  0.809   1.00 18.73  ? 83  SER B CB  1 
ATOM   3092 O  OG  . SER B 1 104 ? 38.837  -2.201  -0.569  1.00 19.55  ? 83  SER B OG  1 
ATOM   3093 N  N   . HIS B 1 105 ? 39.423  -5.222  0.750   1.00 19.20  ? 84  HIS B N   1 
ATOM   3094 C  CA  . HIS B 1 105 ? 38.824  -6.531  0.515   1.00 14.80  ? 84  HIS B CA  1 
ATOM   3095 C  C   . HIS B 1 105 ? 38.932  -7.451  1.723   1.00 22.90  ? 84  HIS B C   1 
ATOM   3096 O  O   . HIS B 1 105 ? 38.335  -8.533  1.715   1.00 25.75  ? 84  HIS B O   1 
ATOM   3097 C  CB  . HIS B 1 105 ? 39.491  -7.218  -0.684  1.00 14.39  ? 84  HIS B CB  1 
ATOM   3098 C  CG  . HIS B 1 105 ? 39.279  -6.517  -1.990  1.00 15.15  ? 84  HIS B CG  1 
ATOM   3099 N  ND1 . HIS B 1 105 ? 39.813  -6.982  -3.174  1.00 16.51  ? 84  HIS B ND1 1 
ATOM   3100 C  CD2 . HIS B 1 105 ? 38.590  -5.393  -2.303  1.00 16.55  ? 84  HIS B CD2 1 
ATOM   3101 C  CE1 . HIS B 1 105 ? 39.466  -6.171  -4.158  1.00 20.54  ? 84  HIS B CE1 1 
ATOM   3102 N  NE2 . HIS B 1 105 ? 38.721  -5.202  -3.658  1.00 20.38  ? 84  HIS B NE2 1 
ATOM   3103 N  N   . VAL B 1 106 ? 39.676  -7.054  2.744   1.00 16.71  ? 85  VAL B N   1 
ATOM   3104 C  CA  . VAL B 1 106 ? 39.931  -7.873  3.919   1.00 21.27  ? 85  VAL B CA  1 
ATOM   3105 C  C   . VAL B 1 106 ? 39.347  -7.156  5.129   1.00 22.35  ? 85  VAL B C   1 
ATOM   3106 O  O   . VAL B 1 106 ? 39.971  -6.257  5.694   1.00 18.94  ? 85  VAL B O   1 
ATOM   3107 C  CB  . VAL B 1 106 ? 41.440  -8.130  4.097   1.00 18.79  ? 85  VAL B CB  1 
ATOM   3108 C  CG1 . VAL B 1 106 ? 41.695  -9.080  5.249   1.00 21.12  ? 85  VAL B CG1 1 
ATOM   3109 C  CG2 . VAL B 1 106 ? 42.039  -8.666  2.800   1.00 24.36  ? 85  VAL B CG2 1 
ATOM   3110 N  N   . PRO B 1 107 ? 38.135  -7.523  5.555   1.00 23.60  ? 86  PRO B N   1 
ATOM   3111 C  CA  . PRO B 1 107 ? 37.509  -6.800  6.674   1.00 23.56  ? 86  PRO B CA  1 
ATOM   3112 C  C   . PRO B 1 107 ? 38.357  -6.779  7.932   1.00 19.48  ? 86  PRO B C   1 
ATOM   3113 O  O   . PRO B 1 107 ? 38.252  -5.832  8.725   1.00 20.02  ? 86  PRO B O   1 
ATOM   3114 C  CB  . PRO B 1 107 ? 36.199  -7.563  6.910   1.00 21.06  ? 86  PRO B CB  1 
ATOM   3115 C  CG  . PRO B 1 107 ? 35.974  -8.404  5.704   1.00 24.20  ? 86  PRO B CG  1 
ATOM   3116 C  CD  . PRO B 1 107 ? 37.192  -8.408  4.847   1.00 23.07  ? 86  PRO B CD  1 
ATOM   3117 N  N   . GLU B 1 108 ? 39.199  -7.795  8.132   1.00 19.78  ? 87  GLU B N   1 
ATOM   3118 C  CA  . GLU B 1 108 ? 39.949  -7.912  9.377   1.00 22.83  ? 87  GLU B CA  1 
ATOM   3119 C  C   . GLU B 1 108 ? 40.821  -6.692  9.642   1.00 18.64  ? 87  GLU B C   1 
ATOM   3120 O  O   . GLU B 1 108 ? 41.158  -6.416  10.797  1.00 17.66  ? 87  GLU B O   1 
ATOM   3121 C  CB  . GLU B 1 108 ? 40.813  -9.175  9.349   1.00 18.46  ? 87  GLU B CB  1 
ATOM   3122 C  CG  . GLU B 1 108 ? 40.019  -10.466 9.469   1.00 18.65  ? 87  GLU B CG  1 
ATOM   3123 C  CD  . GLU B 1 108 ? 39.474  -10.966 8.141   1.00 25.57  ? 87  GLU B CD  1 
ATOM   3124 O  OE1 . GLU B 1 108 ? 39.828  -10.408 7.083   1.00 23.87  ? 87  GLU B OE1 1 
ATOM   3125 O  OE2 . GLU B 1 108 ? 38.692  -11.937 8.157   1.00 29.20  ? 87  GLU B OE2 1 
ATOM   3126 N  N   . HIS B 1 109 ? 41.222  -5.964  8.602   1.00 19.21  ? 88  HIS B N   1 
ATOM   3127 C  CA  . HIS B 1 109 ? 42.052  -4.785  8.836   1.00 21.30  ? 88  HIS B CA  1 
ATOM   3128 C  C   . HIS B 1 109 ? 41.283  -3.725  9.612   1.00 20.70  ? 88  HIS B C   1 
ATOM   3129 O  O   . HIS B 1 109 ? 41.798  -3.157  10.581  1.00 17.07  ? 88  HIS B O   1 
ATOM   3130 C  CB  . HIS B 1 109 ? 42.564  -4.221  7.511   1.00 23.05  ? 88  HIS B CB  1 
ATOM   3131 C  CG  . HIS B 1 109 ? 43.604  -5.077  6.862   1.00 24.07  ? 88  HIS B CG  1 
ATOM   3132 N  ND1 . HIS B 1 109 ? 44.950  -4.780  6.907   1.00 19.33  ? 88  HIS B ND1 1 
ATOM   3133 C  CD2 . HIS B 1 109 ? 43.497  -6.235  6.172   1.00 18.15  ? 88  HIS B CD2 1 
ATOM   3134 C  CE1 . HIS B 1 109 ? 45.626  -5.714  6.264   1.00 23.06  ? 88  HIS B CE1 1 
ATOM   3135 N  NE2 . HIS B 1 109 ? 44.768  -6.610  5.810   1.00 20.94  ? 88  HIS B NE2 1 
ATOM   3136 N  N   . ALA B 1 110 ? 40.037  -3.457  9.212   1.00 22.79  ? 89  ALA B N   1 
ATOM   3137 C  CA  . ALA B 1 110 ? 39.240  -2.464  9.926   1.00 18.46  ? 89  ALA B CA  1 
ATOM   3138 C  C   . ALA B 1 110 ? 38.842  -2.967  11.307  1.00 18.79  ? 89  ALA B C   1 
ATOM   3139 O  O   . ALA B 1 110 ? 38.821  -2.194  12.270  1.00 20.11  ? 89  ALA B O   1 
ATOM   3140 C  CB  . ALA B 1 110 ? 37.998  -2.095  9.112   1.00 19.51  ? 89  ALA B CB  1 
ATOM   3141 N  N   . GLN B 1 111 ? 38.529  -4.260  11.426  1.00 20.98  ? 90  GLN B N   1 
ATOM   3142 C  CA  . GLN B 1 111 ? 38.137  -4.811  12.721  1.00 17.51  ? 90  GLN B CA  1 
ATOM   3143 C  C   . GLN B 1 111 ? 39.255  -4.658  13.744  1.00 21.84  ? 90  GLN B C   1 
ATOM   3144 O  O   . GLN B 1 111 ? 39.038  -4.138  14.845  1.00 23.50  ? 90  GLN B O   1 
ATOM   3145 C  CB  . GLN B 1 111 ? 37.750  -6.282  12.569  1.00 21.52  ? 90  GLN B CB  1 
ATOM   3146 C  CG  . GLN B 1 111 ? 36.483  -6.523  11.761  1.00 16.84  ? 90  GLN B CG  1 
ATOM   3147 C  CD  . GLN B 1 111 ? 36.262  -7.995  11.457  1.00 22.10  ? 90  GLN B CD  1 
ATOM   3148 O  OE1 . GLN B 1 111 ? 36.746  -8.511  10.450  1.00 20.69  ? 90  GLN B OE1 1 
ATOM   3149 N  NE2 . GLN B 1 111 ? 35.531  -8.678  12.329  1.00 23.55  ? 90  GLN B NE2 1 
ATOM   3150 N  N   . LEU B 1 112 ? 40.466  -5.110  13.400  1.00 20.01  ? 91  LEU B N   1 
ATOM   3151 C  CA  . LEU B 1 112 ? 41.586  -4.951  14.323  1.00 19.04  ? 91  LEU B CA  1 
ATOM   3152 C  C   . LEU B 1 112 ? 41.953  -3.483  14.492  1.00 19.63  ? 91  LEU B C   1 
ATOM   3153 O  O   . LEU B 1 112 ? 42.412  -3.079  15.567  1.00 21.75  ? 91  LEU B O   1 
ATOM   3154 C  CB  . LEU B 1 112 ? 42.797  -5.751  13.842  1.00 19.71  ? 91  LEU B CB  1 
ATOM   3155 C  CG  . LEU B 1 112 ? 44.000  -5.733  14.791  1.00 23.00  ? 91  LEU B CG  1 
ATOM   3156 C  CD1 . LEU B 1 112 ? 43.608  -6.277  16.166  1.00 24.93  ? 91  LEU B CD1 1 
ATOM   3157 C  CD2 . LEU B 1 112 ? 45.178  -6.519  14.225  1.00 21.22  ? 91  LEU B CD2 1 
ATOM   3158 N  N   . GLY B 1 113 ? 41.752  -2.672  13.454  1.00 19.74  ? 92  GLY B N   1 
ATOM   3159 C  CA  . GLY B 1 113 ? 42.012  -1.250  13.587  1.00 18.68  ? 92  GLY B CA  1 
ATOM   3160 C  C   . GLY B 1 113 ? 41.176  -0.614  14.678  1.00 19.55  ? 92  GLY B C   1 
ATOM   3161 O  O   . GLY B 1 113 ? 41.674  0.196   15.463  1.00 18.52  ? 92  GLY B O   1 
ATOM   3162 N  N   . TRP B 1 114 ? 39.893  -0.969  14.745  1.00 24.20  ? 93  TRP B N   1 
ATOM   3163 C  CA  . TRP B 1 114 ? 39.054  -0.430  15.805  1.00 24.55  ? 93  TRP B CA  1 
ATOM   3164 C  C   . TRP B 1 114 ? 39.504  -0.931  17.176  1.00 22.98  ? 93  TRP B C   1 
ATOM   3165 O  O   . TRP B 1 114 ? 39.604  -0.153  18.131  1.00 21.56  ? 93  TRP B O   1 
ATOM   3166 C  CB  . TRP B 1 114 ? 37.586  -0.791  15.586  1.00 22.75  ? 93  TRP B CB  1 
ATOM   3167 C  CG  . TRP B 1 114 ? 36.850  -0.464  16.823  1.00 24.39  ? 93  TRP B CG  1 
ATOM   3168 C  CD1 . TRP B 1 114 ? 36.383  -1.336  17.761  1.00 22.80  ? 93  TRP B CD1 1 
ATOM   3169 C  CD2 . TRP B 1 114 ? 36.562  0.849   17.312  1.00 19.89  ? 93  TRP B CD2 1 
ATOM   3170 N  NE1 . TRP B 1 114 ? 35.804  -0.645  18.797  1.00 26.27  ? 93  TRP B NE1 1 
ATOM   3171 C  CE2 . TRP B 1 114 ? 35.901  0.699   18.543  1.00 22.05  ? 93  TRP B CE2 1 
ATOM   3172 C  CE3 . TRP B 1 114 ? 36.794  2.138   16.820  1.00 25.21  ? 93  TRP B CE3 1 
ATOM   3173 C  CZ2 . TRP B 1 114 ? 35.459  1.792   19.291  1.00 26.03  ? 93  TRP B CZ2 1 
ATOM   3174 C  CZ3 . TRP B 1 114 ? 36.354  3.221   17.564  1.00 25.23  ? 93  TRP B CZ3 1 
ATOM   3175 C  CH2 . TRP B 1 114 ? 35.699  3.041   18.785  1.00 21.22  ? 93  TRP B CH2 1 
ATOM   3176 N  N   . ALA B 1 115 ? 39.761  -2.234  17.296  1.00 18.98  ? 94  ALA B N   1 
ATOM   3177 C  CA  . ALA B 1 115 ? 40.124  -2.797  18.592  1.00 17.44  ? 94  ALA B CA  1 
ATOM   3178 C  C   . ALA B 1 115 ? 41.404  -2.171  19.126  1.00 19.81  ? 94  ALA B C   1 
ATOM   3179 O  O   . ALA B 1 115 ? 41.516  -1.897  20.328  1.00 20.53  ? 94  ALA B O   1 
ATOM   3180 C  CB  . ALA B 1 115 ? 40.274  -4.313  18.484  1.00 21.45  ? 94  ALA B CB  1 
ATOM   3181 N  N   . LEU B 1 116 ? 42.385  -1.940  18.252  1.00 19.86  ? 95  LEU B N   1 
ATOM   3182 C  CA  . LEU B 1 116 ? 43.638  -1.341  18.694  1.00 18.65  ? 95  LEU B CA  1 
ATOM   3183 C  C   . LEU B 1 116 ? 43.496  0.144   19.007  1.00 19.17  ? 95  LEU B C   1 
ATOM   3184 O  O   . LEU B 1 116 ? 44.383  0.709   19.652  1.00 20.79  ? 95  LEU B O   1 
ATOM   3185 C  CB  . LEU B 1 116 ? 44.727  -1.550  17.638  1.00 23.14  ? 95  LEU B CB  1 
ATOM   3186 C  CG  . LEU B 1 116 ? 45.158  -3.002  17.407  1.00 23.10  ? 95  LEU B CG  1 
ATOM   3187 C  CD1 . LEU B 1 116 ? 46.210  -3.091  16.306  1.00 22.88  ? 95  LEU B CD1 1 
ATOM   3188 C  CD2 . LEU B 1 116 ? 45.679  -3.621  18.696  1.00 26.83  ? 95  LEU B CD2 1 
ATOM   3189 N  N   . ASN B 1 117 ? 42.413  0.793   18.568  1.00 18.41  ? 96  ASN B N   1 
ATOM   3190 C  CA  . ASN B 1 117 ? 42.154  2.156   19.024  1.00 20.12  ? 96  ASN B CA  1 
ATOM   3191 C  C   . ASN B 1 117 ? 42.018  2.211   20.538  1.00 19.00  ? 96  ASN B C   1 
ATOM   3192 O  O   . ASN B 1 117 ? 42.412  3.199   21.168  1.00 22.11  ? 96  ASN B O   1 
ATOM   3193 C  CB  . ASN B 1 117 ? 40.882  2.714   18.386  1.00 21.60  ? 96  ASN B CB  1 
ATOM   3194 C  CG  . ASN B 1 117 ? 41.153  3.491   17.119  1.00 24.70  ? 96  ASN B CG  1 
ATOM   3195 O  OD1 . ASN B 1 117 ? 42.253  3.993   16.902  1.00 24.62  ? 96  ASN B OD1 1 
ATOM   3196 N  ND2 . ASN B 1 117 ? 40.136  3.611   16.281  1.00 26.36  ? 96  ASN B ND2 1 
ATOM   3197 N  N   . CYS B 1 118 ? 41.457  1.166   21.135  1.00 20.91  ? 97  CYS B N   1 
ATOM   3198 C  CA  . CYS B 1 118 ? 41.228  1.132   22.571  1.00 22.30  ? 97  CYS B CA  1 
ATOM   3199 C  C   . CYS B 1 118 ? 42.490  0.831   23.362  1.00 22.00  ? 97  CYS B C   1 
ATOM   3200 O  O   . CYS B 1 118 ? 42.461  0.910   24.595  1.00 24.20  ? 97  CYS B O   1 
ATOM   3201 C  CB  . CYS B 1 118 ? 40.148  0.098   22.878  1.00 21.83  ? 97  CYS B CB  1 
ATOM   3202 S  SG  . CYS B 1 118 ? 38.635  0.378   21.933  1.00 22.72  ? 97  CYS B SG  1 
ATOM   3203 N  N   . TYR B 1 119 ? 43.590  0.497   22.690  1.00 19.08  ? 98  TYR B N   1 
ATOM   3204 C  CA  . TYR B 1 119 ? 44.879  0.277   23.337  1.00 19.80  ? 98  TYR B CA  1 
ATOM   3205 C  C   . TYR B 1 119 ? 45.932  1.250   22.824  1.00 23.59  ? 98  TYR B C   1 
ATOM   3206 O  O   . TYR B 1 119 ? 47.130  1.037   23.032  1.00 26.37  ? 98  TYR B O   1 
ATOM   3207 C  CB  . TYR B 1 119 ? 45.314  -1.173  23.134  1.00 23.62  ? 98  TYR B CB  1 
ATOM   3208 C  CG  . TYR B 1 119 ? 44.287  -2.128  23.682  1.00 26.80  ? 98  TYR B CG  1 
ATOM   3209 C  CD1 . TYR B 1 119 ? 43.211  -2.536  22.907  1.00 22.26  ? 98  TYR B CD1 1 
ATOM   3210 C  CD2 . TYR B 1 119 ? 44.364  -2.585  24.993  1.00 23.84  ? 98  TYR B CD2 1 
ATOM   3211 C  CE1 . TYR B 1 119 ? 42.253  -3.391  23.415  1.00 25.15  ? 98  TYR B CE1 1 
ATOM   3212 C  CE2 . TYR B 1 119 ? 43.413  -3.441  25.505  1.00 29.12  ? 98  TYR B CE2 1 
ATOM   3213 C  CZ  . TYR B 1 119 ? 42.362  -3.839  24.712  1.00 27.76  ? 98  TYR B CZ  1 
ATOM   3214 O  OH  . TYR B 1 119 ? 41.411  -4.689  25.217  1.00 33.83  ? 98  TYR B OH  1 
ATOM   3215 N  N   . THR B 1 120 ? 45.500  2.312   22.154  1.00 24.36  ? 99  THR B N   1 
ATOM   3216 C  CA  . THR B 1 120 ? 46.367  3.383   21.688  1.00 21.89  ? 99  THR B CA  1 
ATOM   3217 C  C   . THR B 1 120 ? 45.975  4.648   22.433  1.00 24.57  ? 99  THR B C   1 
ATOM   3218 O  O   . THR B 1 120 ? 44.784  4.946   22.560  1.00 22.16  ? 99  THR B O   1 
ATOM   3219 C  CB  . THR B 1 120 ? 46.230  3.586   20.177  1.00 20.57  ? 99  THR B CB  1 
ATOM   3220 O  OG1 . THR B 1 120 ? 46.588  2.378   19.492  1.00 24.56  ? 99  THR B OG1 1 
ATOM   3221 C  CG2 . THR B 1 120 ? 47.122  4.720   19.703  1.00 23.98  ? 99  THR B CG2 1 
ATOM   3222 N  N   . TYR B 1 121 ? 46.963  5.374   22.945  1.00 24.53  ? 100 TYR B N   1 
ATOM   3223 C  CA  . TYR B 1 121 ? 46.689  6.625   23.638  1.00 30.56  ? 100 TYR B CA  1 
ATOM   3224 C  C   . TYR B 1 121 ? 46.444  7.749   22.638  1.00 31.63  ? 100 TYR B C   1 
ATOM   3225 O  O   . TYR B 1 121 ? 47.115  7.844   21.606  1.00 28.15  ? 100 TYR B O   1 
ATOM   3226 C  CB  . TYR B 1 121 ? 47.851  7.000   24.560  1.00 28.78  ? 100 TYR B CB  1 
ATOM   3227 C  CG  . TYR B 1 121 ? 48.000  6.115   25.781  1.00 39.50  ? 100 TYR B CG  1 
ATOM   3228 C  CD1 . TYR B 1 121 ? 47.237  6.335   26.921  1.00 48.56  ? 100 TYR B CD1 1 
ATOM   3229 C  CD2 . TYR B 1 121 ? 48.916  5.072   25.799  1.00 39.70  ? 100 TYR B CD2 1 
ATOM   3230 C  CE1 . TYR B 1 121 ? 47.375  5.532   28.043  1.00 55.13  ? 100 TYR B CE1 1 
ATOM   3231 C  CE2 . TYR B 1 121 ? 49.060  4.263   26.913  1.00 43.52  ? 100 TYR B CE2 1 
ATOM   3232 C  CZ  . TYR B 1 121 ? 48.288  4.498   28.033  1.00 49.08  ? 100 TYR B CZ  1 
ATOM   3233 O  OH  . TYR B 1 121 ? 48.431  3.696   29.146  1.00 52.47  ? 100 TYR B OH  1 
ATOM   3234 N  N   . PHE B 1 122 ? 45.462  8.598   22.950  1.00 30.29  ? 101 PHE B N   1 
ATOM   3235 C  CA  . PHE B 1 122 ? 45.246  9.813   22.168  1.00 34.72  ? 101 PHE B CA  1 
ATOM   3236 C  C   . PHE B 1 122 ? 46.529  10.629  22.073  1.00 33.07  ? 101 PHE B C   1 
ATOM   3237 O  O   . PHE B 1 122 ? 46.823  11.223  21.030  1.00 29.70  ? 101 PHE B O   1 
ATOM   3238 C  CB  . PHE B 1 122 ? 44.120  10.636  22.805  1.00 29.04  ? 101 PHE B CB  1 
ATOM   3239 C  CG  . PHE B 1 122 ? 43.847  11.950  22.120  1.00 30.66  ? 101 PHE B CG  1 
ATOM   3240 C  CD1 . PHE B 1 122 ? 44.655  13.050  22.348  1.00 34.48  ? 101 PHE B CD1 1 
ATOM   3241 C  CD2 . PHE B 1 122 ? 42.761  12.091  21.275  1.00 31.82  ? 101 PHE B CD2 1 
ATOM   3242 C  CE1 . PHE B 1 122 ? 44.401  14.254  21.727  1.00 35.73  ? 101 PHE B CE1 1 
ATOM   3243 C  CE2 . PHE B 1 122 ? 42.504  13.296  20.653  1.00 33.56  ? 101 PHE B CE2 1 
ATOM   3244 C  CZ  . PHE B 1 122 ? 43.325  14.376  20.881  1.00 34.60  ? 101 PHE B CZ  1 
ATOM   3245 N  N   . GLY B 1 123 ? 47.309  10.663  23.155  1.00 29.15  ? 102 GLY B N   1 
ATOM   3246 C  CA  . GLY B 1 123 ? 48.537  11.441  23.145  1.00 33.53  ? 102 GLY B CA  1 
ATOM   3247 C  C   . GLY B 1 123 ? 49.547  10.934  22.135  1.00 29.67  ? 102 GLY B C   1 
ATOM   3248 O  O   . GLY B 1 123 ? 50.281  11.718  21.531  1.00 32.26  ? 102 GLY B O   1 
ATOM   3249 N  N   . GLU B 1 124 ? 49.612  9.613   21.948  1.00 33.54  ? 103 GLU B N   1 
ATOM   3250 C  CA  . GLU B 1 124 ? 50.533  9.056   20.963  1.00 36.11  ? 103 GLU B CA  1 
ATOM   3251 C  C   . GLU B 1 124 ? 50.192  9.541   19.561  1.00 34.98  ? 103 GLU B C   1 
ATOM   3252 O  O   . GLU B 1 124 ? 51.083  9.909   18.788  1.00 36.16  ? 103 GLU B O   1 
ATOM   3253 C  CB  . GLU B 1 124 ? 50.508  7.527   21.021  1.00 31.62  ? 103 GLU B CB  1 
ATOM   3254 C  CG  . GLU B 1 124 ? 51.118  6.942   22.287  1.00 39.44  ? 103 GLU B CG  1 
ATOM   3255 C  CD  . GLU B 1 124 ? 50.925  5.437   22.393  1.00 37.70  ? 103 GLU B CD  1 
ATOM   3256 O  OE1 . GLU B 1 124 ? 49.773  4.970   22.259  1.00 33.40  ? 103 GLU B OE1 1 
ATOM   3257 O  OE2 . GLU B 1 124 ? 51.926  4.718   22.604  1.00 38.40  ? 103 GLU B OE2 1 
ATOM   3258 N  N   . LEU B 1 125 ? 48.902  9.555   19.217  1.00 26.82  ? 104 LEU B N   1 
ATOM   3259 C  CA  . LEU B 1 125 ? 48.492  10.015  17.897  1.00 23.88  ? 104 LEU B CA  1 
ATOM   3260 C  C   . LEU B 1 125 ? 48.695  11.517  17.735  1.00 28.75  ? 104 LEU B C   1 
ATOM   3261 O  O   . LEU B 1 125 ? 48.933  11.989  16.618  1.00 31.06  ? 104 LEU B O   1 
ATOM   3262 C  CB  . LEU B 1 125 ? 47.033  9.641   17.653  1.00 25.56  ? 104 LEU B CB  1 
ATOM   3263 C  CG  . LEU B 1 125 ? 46.742  8.140   17.585  1.00 25.47  ? 104 LEU B CG  1 
ATOM   3264 C  CD1 . LEU B 1 125 ? 45.247  7.891   17.500  1.00 23.36  ? 104 LEU B CD1 1 
ATOM   3265 C  CD2 . LEU B 1 125 ? 47.448  7.497   16.403  1.00 25.48  ? 104 LEU B CD2 1 
ATOM   3266 N  N   . SER B 1 126 ? 48.600  12.279  18.827  1.00 34.40  ? 105 SER B N   1 
ATOM   3267 C  CA  . SER B 1 126 ? 48.871  13.712  18.755  1.00 36.46  ? 105 SER B CA  1 
ATOM   3268 C  C   . SER B 1 126 ? 50.332  13.979  18.414  1.00 35.37  ? 105 SER B C   1 
ATOM   3269 O  O   . SER B 1 126 ? 50.638  14.915  17.668  1.00 39.43  ? 105 SER B O   1 
ATOM   3270 C  CB  . SER B 1 126 ? 48.503  14.384  20.079  1.00 41.73  ? 105 SER B CB  1 
ATOM   3271 O  OG  . SER B 1 126 ? 47.137  14.181  20.390  1.00 42.59  ? 105 SER B OG  1 
ATOM   3272 N  N   . ARG B 1 127 ? 51.249  13.179  18.962  1.00 40.23  ? 106 ARG B N   1 
ATOM   3273 C  CA  . ARG B 1 127 ? 52.662  13.340  18.639  1.00 41.54  ? 106 ARG B CA  1 
ATOM   3274 C  C   . ARG B 1 127 ? 52.960  13.015  17.180  1.00 44.09  ? 106 ARG B C   1 
ATOM   3275 O  O   . ARG B 1 127 ? 54.009  13.420  16.672  1.00 48.62  ? 106 ARG B O   1 
ATOM   3276 C  CB  . ARG B 1 127 ? 53.516  12.457  19.550  1.00 38.08  ? 106 ARG B CB  1 
ATOM   3277 N  N   . MET B 1 128 ? 52.071  12.286  16.502  1.00 42.07  ? 107 MET B N   1 
ATOM   3278 C  CA  . MET B 1 128 ? 52.212  12.049  15.072  1.00 43.37  ? 107 MET B CA  1 
ATOM   3279 C  C   . MET B 1 128 ? 51.791  13.253  14.239  1.00 48.35  ? 107 MET B C   1 
ATOM   3280 O  O   . MET B 1 128 ? 51.974  13.235  13.017  1.00 54.39  ? 107 MET B O   1 
ATOM   3281 C  CB  . MET B 1 128 ? 51.370  10.845  14.634  1.00 44.51  ? 107 MET B CB  1 
ATOM   3282 C  CG  . MET B 1 128 ? 51.439  9.617   15.536  1.00 38.45  ? 107 MET B CG  1 
ATOM   3283 S  SD  . MET B 1 128 ? 53.006  8.727   15.505  1.00 55.03  ? 107 MET B SD  1 
ATOM   3284 C  CE  . MET B 1 128 ? 53.171  8.349   13.762  1.00 47.66  ? 107 MET B CE  1 
ATOM   3285 N  N   . THR B 1 129 ? 51.222  14.278  14.869  1.00 61.57  ? 108 THR B N   1 
ATOM   3286 C  CA  . THR B 1 129 ? 50.659  15.432  14.174  1.00 58.56  ? 108 THR B CA  1 
ATOM   3287 C  C   . THR B 1 129 ? 49.425  15.013  13.384  1.00 56.23  ? 108 THR B C   1 
ATOM   3288 O  O   . THR B 1 129 ? 48.406  14.640  13.965  1.00 56.01  ? 108 THR B O   1 
ATOM   3289 C  CB  . THR B 1 129 ? 51.673  16.091  13.227  1.00 67.22  ? 108 THR B CB  1 
ATOM   3290 O  OG1 . THR B 1 129 ? 52.927  16.246  13.902  1.00 64.51  ? 108 THR B OG1 1 
ATOM   3291 C  CG2 . THR B 1 129 ? 51.168  17.458  12.782  1.00 68.58  ? 108 THR B CG2 1 
ATOM   3292 N  N   . GLU B 1 140 ? 40.980  21.006  15.001  1.00 47.16  ? 119 GLU B N   1 
ATOM   3293 C  CA  . GLU B 1 140 ? 41.463  21.469  13.707  1.00 35.39  ? 119 GLU B CA  1 
ATOM   3294 C  C   . GLU B 1 140 ? 40.615  20.854  12.597  1.00 39.45  ? 119 GLU B C   1 
ATOM   3295 O  O   . GLU B 1 140 ? 39.834  19.930  12.835  1.00 37.04  ? 119 GLU B O   1 
ATOM   3296 C  CB  . GLU B 1 140 ? 42.943  21.120  13.527  1.00 42.38  ? 119 GLU B CB  1 
ATOM   3297 C  CG  . GLU B 1 140 ? 43.594  21.764  12.307  1.00 54.63  ? 119 GLU B CG  1 
ATOM   3298 C  CD  . GLU B 1 140 ? 45.104  21.628  12.302  1.00 59.97  ? 119 GLU B CD  1 
ATOM   3299 O  OE1 . GLU B 1 140 ? 45.630  20.778  13.051  1.00 59.34  ? 119 GLU B OE1 1 
ATOM   3300 O  OE2 . GLU B 1 140 ? 45.763  22.375  11.548  1.00 67.75  ? 119 GLU B OE2 1 
ATOM   3301 N  N   . ASN B 1 141 ? 40.773  21.372  11.380  1.00 40.66  ? 120 ASN B N   1 
ATOM   3302 C  CA  . ASN B 1 141 ? 39.931  21.000  10.255  1.00 39.17  ? 120 ASN B CA  1 
ATOM   3303 C  C   . ASN B 1 141 ? 40.485  19.823  9.454   1.00 39.01  ? 120 ASN B C   1 
ATOM   3304 O  O   . ASN B 1 141 ? 40.146  19.679  8.274   1.00 39.51  ? 120 ASN B O   1 
ATOM   3305 C  CB  . ASN B 1 141 ? 39.732  22.210  9.343   1.00 40.08  ? 120 ASN B CB  1 
ATOM   3306 C  CG  . ASN B 1 141 ? 39.341  23.454  10.110  1.00 34.21  ? 120 ASN B CG  1 
ATOM   3307 O  OD1 . ASN B 1 141 ? 38.491  23.408  11.000  1.00 43.93  ? 120 ASN B OD1 1 
ATOM   3308 N  ND2 . ASN B 1 141 ? 39.974  24.575  9.780   1.00 37.27  ? 120 ASN B ND2 1 
ATOM   3309 N  N   . ILE B 1 142 ? 41.333  18.987  10.059  1.00 31.90  ? 121 ILE B N   1 
ATOM   3310 C  CA  . ILE B 1 142 ? 41.679  17.707  9.451   1.00 30.97  ? 121 ILE B CA  1 
ATOM   3311 C  C   . ILE B 1 142 ? 40.575  16.698  9.745   1.00 25.41  ? 121 ILE B C   1 
ATOM   3312 O  O   . ILE B 1 142 ? 39.776  16.871  10.663  1.00 25.17  ? 121 ILE B O   1 
ATOM   3313 C  CB  . ILE B 1 142 ? 43.042  17.196  9.952   1.00 35.34  ? 121 ILE B CB  1 
ATOM   3314 C  CG1 . ILE B 1 142 ? 43.006  16.953  11.465  1.00 31.96  ? 121 ILE B CG1 1 
ATOM   3315 C  CG2 . ILE B 1 142 ? 44.138  18.187  9.599   1.00 38.71  ? 121 ILE B CG2 1 
ATOM   3316 C  CD1 . ILE B 1 142 ? 44.048  15.976  11.951  1.00 30.02  ? 121 ILE B CD1 1 
ATOM   3317 N  N   . ASN B 1 143 ? 40.538  15.620  8.972   1.00 25.37  ? 122 ASN B N   1 
ATOM   3318 C  CA  . ASN B 1 143 ? 39.546  14.590  9.241   1.00 26.20  ? 122 ASN B CA  1 
ATOM   3319 C  C   . ASN B 1 143 ? 40.111  13.550  10.206  1.00 26.58  ? 122 ASN B C   1 
ATOM   3320 O  O   . ASN B 1 143 ? 41.326  13.419  10.384  1.00 22.71  ? 122 ASN B O   1 
ATOM   3321 C  CB  . ASN B 1 143 ? 39.062  13.921  7.950   1.00 25.41  ? 122 ASN B CB  1 
ATOM   3322 C  CG  . ASN B 1 143 ? 40.141  13.120  7.258   1.00 26.52  ? 122 ASN B CG  1 
ATOM   3323 O  OD1 . ASN B 1 143 ? 40.541  12.054  7.725   1.00 26.55  ? 122 ASN B OD1 1 
ATOM   3324 N  ND2 . ASN B 1 143 ? 40.592  13.612  6.116   1.00 25.78  ? 122 ASN B ND2 1 
ATOM   3325 N  N   . ALA B 1 144 ? 39.196  12.821  10.846  1.00 26.00  ? 123 ALA B N   1 
ATOM   3326 C  CA  . ALA B 1 144 ? 39.587  11.847  11.857  1.00 26.18  ? 123 ALA B CA  1 
ATOM   3327 C  C   . ALA B 1 144 ? 40.450  10.737  11.279  1.00 27.85  ? 123 ALA B C   1 
ATOM   3328 O  O   . ALA B 1 144 ? 41.218  10.110  12.018  1.00 26.45  ? 123 ALA B O   1 
ATOM   3329 C  CB  . ALA B 1 144 ? 38.341  11.253  12.513  1.00 27.53  ? 123 ALA B CB  1 
ATOM   3330 N  N   . GLY B 1 145 ? 40.330  10.468  9.974   1.00 25.52  ? 124 GLY B N   1 
ATOM   3331 C  CA  . GLY B 1 145 ? 41.160  9.444   9.357   1.00 21.51  ? 124 GLY B CA  1 
ATOM   3332 C  C   . GLY B 1 145 ? 42.635  9.803   9.364   1.00 23.54  ? 124 GLY B C   1 
ATOM   3333 O  O   . GLY B 1 145 ? 43.486  8.967   9.679   1.00 17.77  ? 124 GLY B O   1 
ATOM   3334 N  N   . LEU B 1 146 ? 42.961  11.048  9.006   1.00 22.22  ? 125 LEU B N   1 
ATOM   3335 C  CA  . LEU B 1 146 ? 44.353  11.483  9.065   1.00 29.93  ? 125 LEU B CA  1 
ATOM   3336 C  C   . LEU B 1 146 ? 44.908  11.346  10.476  1.00 29.26  ? 125 LEU B C   1 
ATOM   3337 O  O   . LEU B 1 146 ? 46.078  10.989  10.663  1.00 32.88  ? 125 LEU B O   1 
ATOM   3338 C  CB  . LEU B 1 146 ? 44.478  12.932  8.598   1.00 26.99  ? 125 LEU B CB  1 
ATOM   3339 C  CG  . LEU B 1 146 ? 44.680  13.194  7.112   1.00 31.04  ? 125 LEU B CG  1 
ATOM   3340 C  CD1 . LEU B 1 146 ? 44.669  14.692  6.866   1.00 34.15  ? 125 LEU B CD1 1 
ATOM   3341 C  CD2 . LEU B 1 146 ? 45.977  12.578  6.616   1.00 33.86  ? 125 LEU B CD2 1 
ATOM   3342 N  N   . PHE B 1 147 ? 44.089  11.651  11.483  1.00 24.59  ? 126 PHE B N   1 
ATOM   3343 C  CA  . PHE B 1 147 ? 44.553  11.561  12.861  1.00 22.29  ? 126 PHE B CA  1 
ATOM   3344 C  C   . PHE B 1 147 ? 44.736  10.112  13.293  1.00 22.04  ? 126 PHE B C   1 
ATOM   3345 O  O   . PHE B 1 147 ? 45.667  9.797   14.043  1.00 26.04  ? 126 PHE B O   1 
ATOM   3346 C  CB  . PHE B 1 147 ? 43.569  12.275  13.784  1.00 26.14  ? 126 PHE B CB  1 
ATOM   3347 C  CG  . PHE B 1 147 ? 43.969  12.252  15.229  1.00 23.25  ? 126 PHE B CG  1 
ATOM   3348 C  CD1 . PHE B 1 147 ? 44.962  13.092  15.696  1.00 26.21  ? 126 PHE B CD1 1 
ATOM   3349 C  CD2 . PHE B 1 147 ? 43.345  11.397  16.123  1.00 28.64  ? 126 PHE B CD2 1 
ATOM   3350 C  CE1 . PHE B 1 147 ? 45.331  13.078  17.026  1.00 36.36  ? 126 PHE B CE1 1 
ATOM   3351 C  CE2 . PHE B 1 147 ? 43.708  11.383  17.457  1.00 31.97  ? 126 PHE B CE2 1 
ATOM   3352 C  CZ  . PHE B 1 147 ? 44.700  12.223  17.908  1.00 28.11  ? 126 PHE B CZ  1 
ATOM   3353 N  N   . ASP B 1 148 ? 43.871  9.213   12.818  1.00 23.31  ? 127 ASP B N   1 
ATOM   3354 C  CA  . ASP B 1 148 ? 43.802  7.854   13.339  1.00 26.25  ? 127 ASP B CA  1 
ATOM   3355 C  C   . ASP B 1 148 ? 44.502  6.813   12.474  1.00 22.23  ? 127 ASP B C   1 
ATOM   3356 O  O   . ASP B 1 148 ? 44.656  5.671   12.922  1.00 21.65  ? 127 ASP B O   1 
ATOM   3357 C  CB  . ASP B 1 148 ? 42.334  7.435   13.519  1.00 26.37  ? 127 ASP B CB  1 
ATOM   3358 C  CG  . ASP B 1 148 ? 42.186  6.148   14.315  1.00 31.25  ? 127 ASP B CG  1 
ATOM   3359 O  OD1 . ASP B 1 148 ? 42.661  6.113   15.470  1.00 27.64  ? 127 ASP B OD1 1 
ATOM   3360 O  OD2 . ASP B 1 148 ? 41.604  5.172   13.790  1.00 34.33  ? 127 ASP B OD2 1 
ATOM   3361 N  N   . TYR B 1 149 ? 44.943  7.161   11.266  1.00 19.34  ? 128 TYR B N   1 
ATOM   3362 C  CA  . TYR B 1 149 ? 45.489  6.137   10.384  1.00 20.02  ? 128 TYR B CA  1 
ATOM   3363 C  C   . TYR B 1 149 ? 46.708  5.419   10.964  1.00 22.84  ? 128 TYR B C   1 
ATOM   3364 O  O   . TYR B 1 149 ? 46.929  4.259   10.581  1.00 22.34  ? 128 TYR B O   1 
ATOM   3365 C  CB  . TYR B 1 149 ? 45.812  6.736   8.999   1.00 19.21  ? 128 TYR B CB  1 
ATOM   3366 C  CG  . TYR B 1 149 ? 47.139  7.458   8.879   1.00 21.62  ? 128 TYR B CG  1 
ATOM   3367 C  CD1 . TYR B 1 149 ? 48.331  6.754   8.755   1.00 28.26  ? 128 TYR B CD1 1 
ATOM   3368 C  CD2 . TYR B 1 149 ? 47.197  8.845   8.861   1.00 25.31  ? 128 TYR B CD2 1 
ATOM   3369 C  CE1 . TYR B 1 149 ? 49.544  7.413   8.640   1.00 29.66  ? 128 TYR B CE1 1 
ATOM   3370 C  CE2 . TYR B 1 149 ? 48.403  9.509   8.747   1.00 25.66  ? 128 TYR B CE2 1 
ATOM   3371 C  CZ  . TYR B 1 149 ? 49.572  8.788   8.634   1.00 31.30  ? 128 TYR B CZ  1 
ATOM   3372 O  OH  . TYR B 1 149 ? 50.773  9.447   8.518   1.00 43.42  ? 128 TYR B OH  1 
ATOM   3373 N  N   . PRO B 1 150 ? 47.510  6.001   11.863  1.00 25.36  ? 129 PRO B N   1 
ATOM   3374 C  CA  . PRO B 1 150 ? 48.600  5.204   12.451  1.00 26.93  ? 129 PRO B CA  1 
ATOM   3375 C  C   . PRO B 1 150 ? 48.114  3.951   13.168  1.00 25.89  ? 129 PRO B C   1 
ATOM   3376 O  O   . PRO B 1 150 ? 48.848  2.955   13.214  1.00 22.03  ? 129 PRO B O   1 
ATOM   3377 C  CB  . PRO B 1 150 ? 49.273  6.190   13.417  1.00 24.04  ? 129 PRO B CB  1 
ATOM   3378 C  CG  . PRO B 1 150 ? 48.967  7.522   12.857  1.00 26.41  ? 129 PRO B CG  1 
ATOM   3379 C  CD  . PRO B 1 150 ? 47.586  7.411   12.287  1.00 23.06  ? 129 PRO B CD  1 
ATOM   3380 N  N   . VAL B 1 151 ? 46.905  3.969   13.737  1.00 23.09  ? 130 VAL B N   1 
ATOM   3381 C  CA  . VAL B 1 151 ? 46.374  2.766   14.371  1.00 23.81  ? 130 VAL B CA  1 
ATOM   3382 C  C   . VAL B 1 151 ? 46.017  1.720   13.322  1.00 23.93  ? 130 VAL B C   1 
ATOM   3383 O  O   . VAL B 1 151 ? 46.227  0.519   13.529  1.00 21.82  ? 130 VAL B O   1 
ATOM   3384 C  CB  . VAL B 1 151 ? 45.161  3.101   15.256  1.00 19.92  ? 130 VAL B CB  1 
ATOM   3385 C  CG1 . VAL B 1 151 ? 44.632  1.833   15.935  1.00 20.86  ? 130 VAL B CG1 1 
ATOM   3386 C  CG2 . VAL B 1 151 ? 45.531  4.140   16.289  1.00 22.47  ? 130 VAL B CG2 1 
ATOM   3387 N  N   . LEU B 1 152 ? 45.451  2.148   12.193  1.00 24.04  ? 131 LEU B N   1 
ATOM   3388 C  CA  . LEU B 1 152 ? 45.148  1.196   11.130  1.00 26.05  ? 131 LEU B CA  1 
ATOM   3389 C  C   . LEU B 1 152 ? 46.426  0.583   10.571  1.00 27.73  ? 131 LEU B C   1 
ATOM   3390 O  O   . LEU B 1 152 ? 46.455  -0.607  10.235  1.00 23.62  ? 131 LEU B O   1 
ATOM   3391 C  CB  . LEU B 1 152 ? 44.343  1.872   10.020  1.00 26.77  ? 131 LEU B CB  1 
ATOM   3392 C  CG  . LEU B 1 152 ? 43.890  0.952   8.881   1.00 24.79  ? 131 LEU B CG  1 
ATOM   3393 C  CD1 . LEU B 1 152 ? 43.098  -0.237  9.422   1.00 21.21  ? 131 LEU B CD1 1 
ATOM   3394 C  CD2 . LEU B 1 152 ? 43.071  1.720   7.861   1.00 24.76  ? 131 LEU B CD2 1 
ATOM   3395 N  N   . MET B 1 153 ? 47.496  1.380   10.464  1.00 22.37  ? 132 MET B N   1 
ATOM   3396 C  CA  . MET B 1 153 ? 48.780  0.829   10.041  1.00 24.16  ? 132 MET B CA  1 
ATOM   3397 C  C   . MET B 1 153 ? 49.239  -0.262  10.994  1.00 23.22  ? 132 MET B C   1 
ATOM   3398 O  O   . MET B 1 153 ? 49.720  -1.318  10.565  1.00 21.68  ? 132 MET B O   1 
ATOM   3399 C  CB  . MET B 1 153 ? 49.851  1.918   9.986   1.00 23.90  ? 132 MET B CB  1 
ATOM   3400 C  CG  . MET B 1 153 ? 49.631  3.028   8.974   1.00 37.80  ? 132 MET B CG  1 
ATOM   3401 S  SD  . MET B 1 153 ? 51.166  3.861   8.462   1.00 41.00  ? 132 MET B SD  1 
ATOM   3402 C  CE  . MET B 1 153 ? 52.452  2.701   8.944   1.00 39.23  ? 132 MET B CE  1 
ATOM   3403 N  N   . ALA B 1 154 ? 49.121  -0.012  12.297  1.00 24.91  ? 133 ALA B N   1 
ATOM   3404 C  CA  . ALA B 1 154 ? 49.506  -1.023  13.272  1.00 26.11  ? 133 ALA B CA  1 
ATOM   3405 C  C   . ALA B 1 154 ? 48.712  -2.301  13.062  1.00 20.92  ? 133 ALA B C   1 
ATOM   3406 O  O   . ALA B 1 154 ? 49.272  -3.400  13.101  1.00 24.21  ? 133 ALA B O   1 
ATOM   3407 C  CB  . ALA B 1 154 ? 49.305  -0.488  14.687  1.00 27.44  ? 133 ALA B CB  1 
ATOM   3408 N  N   . ALA B 1 155 ? 47.403  -2.175  12.821  1.00 23.46  ? 134 ALA B N   1 
ATOM   3409 C  CA  . ALA B 1 155 ? 46.577  -3.354  12.585  1.00 22.65  ? 134 ALA B CA  1 
ATOM   3410 C  C   . ALA B 1 155 ? 47.010  -4.086  11.320  1.00 23.63  ? 134 ALA B C   1 
ATOM   3411 O  O   . ALA B 1 155 ? 47.068  -5.323  11.301  1.00 25.05  ? 134 ALA B O   1 
ATOM   3412 C  CB  . ALA B 1 155 ? 45.102  -2.953  12.499  1.00 21.92  ? 134 ALA B CB  1 
ATOM   3413 N  N   . ASP B 1 156 ? 47.326  -3.339  10.256  1.00 25.85  ? 135 ASP B N   1 
ATOM   3414 C  CA  . ASP B 1 156 ? 47.784  -3.958  9.017   1.00 26.71  ? 135 ASP B CA  1 
ATOM   3415 C  C   . ASP B 1 156 ? 48.924  -4.931  9.290   1.00 25.85  ? 135 ASP B C   1 
ATOM   3416 O  O   . ASP B 1 156 ? 48.942  -6.056  8.779   1.00 28.38  ? 135 ASP B O   1 
ATOM   3417 C  CB  . ASP B 1 156 ? 48.260  -2.888  8.025   1.00 24.23  ? 135 ASP B CB  1 
ATOM   3418 C  CG  . ASP B 1 156 ? 47.145  -1.975  7.532   1.00 27.07  ? 135 ASP B CG  1 
ATOM   3419 O  OD1 . ASP B 1 156 ? 45.956  -2.349  7.581   1.00 26.67  ? 135 ASP B OD1 1 
ATOM   3420 O  OD2 . ASP B 1 156 ? 47.477  -0.861  7.071   1.00 29.53  ? 135 ASP B OD2 1 
ATOM   3421 N  N   . ILE B 1 157 ? 49.890  -4.502  10.100  1.00 25.75  ? 136 ILE B N   1 
ATOM   3422 C  CA  . ILE B 1 157 ? 51.094  -5.289  10.333  1.00 29.24  ? 136 ILE B CA  1 
ATOM   3423 C  C   . ILE B 1 157 ? 50.822  -6.427  11.308  1.00 24.44  ? 136 ILE B C   1 
ATOM   3424 O  O   . ILE B 1 157 ? 51.141  -7.589  11.033  1.00 18.94  ? 136 ILE B O   1 
ATOM   3425 C  CB  . ILE B 1 157 ? 52.219  -4.365  10.838  1.00 27.51  ? 136 ILE B CB  1 
ATOM   3426 C  CG1 . ILE B 1 157 ? 52.577  -3.338  9.762   1.00 31.56  ? 136 ILE B CG1 1 
ATOM   3427 C  CG2 . ILE B 1 157 ? 53.448  -5.167  11.224  1.00 29.15  ? 136 ILE B CG2 1 
ATOM   3428 C  CD1 . ILE B 1 157 ? 53.227  -2.081  10.306  1.00 32.12  ? 136 ILE B CD1 1 
ATOM   3429 N  N   . LEU B 1 158 ? 50.225  -6.111  12.460  1.00 21.81  ? 137 LEU B N   1 
ATOM   3430 C  CA  . LEU B 1 158 ? 50.063  -7.102  13.518  1.00 24.03  ? 137 LEU B CA  1 
ATOM   3431 C  C   . LEU B 1 158 ? 49.090  -8.209  13.136  1.00 23.20  ? 137 LEU B C   1 
ATOM   3432 O  O   . LEU B 1 158 ? 49.138  -9.290  13.733  1.00 26.41  ? 137 LEU B O   1 
ATOM   3433 C  CB  . LEU B 1 158 ? 49.595  -6.416  14.806  1.00 20.76  ? 137 LEU B CB  1 
ATOM   3434 C  CG  . LEU B 1 158 ? 50.508  -5.324  15.370  1.00 24.87  ? 137 LEU B CG  1 
ATOM   3435 C  CD1 . LEU B 1 158 ? 49.906  -4.743  16.645  1.00 29.30  ? 137 LEU B CD1 1 
ATOM   3436 C  CD2 . LEU B 1 158 ? 51.919  -5.840  15.634  1.00 26.57  ? 137 LEU B CD2 1 
ATOM   3437 N  N   . LEU B 1 159 ? 48.218  -7.968  12.157  1.00 22.15  ? 138 LEU B N   1 
ATOM   3438 C  CA  . LEU B 1 159 ? 47.258  -8.985  11.746  1.00 22.77  ? 138 LEU B CA  1 
ATOM   3439 C  C   . LEU B 1 159 ? 47.952  -10.261 11.290  1.00 25.90  ? 138 LEU B C   1 
ATOM   3440 O  O   . LEU B 1 159 ? 47.462  -11.368 11.538  1.00 26.37  ? 138 LEU B O   1 
ATOM   3441 C  CB  . LEU B 1 159 ? 46.383  -8.454  10.613  1.00 26.29  ? 138 LEU B CB  1 
ATOM   3442 C  CG  . LEU B 1 159 ? 44.982  -7.956  10.935  1.00 27.45  ? 138 LEU B CG  1 
ATOM   3443 C  CD1 . LEU B 1 159 ? 44.310  -7.525  9.646   1.00 23.51  ? 138 LEU B CD1 1 
ATOM   3444 C  CD2 . LEU B 1 159 ? 44.176  -9.030  11.630  1.00 23.87  ? 138 LEU B CD2 1 
ATOM   3445 N  N   . TYR B 1 160 ? 49.082  -10.130 10.600  1.00 24.54  ? 139 TYR B N   1 
ATOM   3446 C  CA  . TYR B 1 160 ? 49.702  -11.257 9.919   1.00 22.32  ? 139 TYR B CA  1 
ATOM   3447 C  C   . TYR B 1 160 ? 50.888  -11.817 10.683  1.00 22.57  ? 139 TYR B C   1 
ATOM   3448 O  O   . TYR B 1 160 ? 51.687  -12.565 10.113  1.00 27.29  ? 139 TYR B O   1 
ATOM   3449 C  CB  . TYR B 1 160 ? 50.098  -10.836 8.504   1.00 19.76  ? 139 TYR B CB  1 
ATOM   3450 C  CG  . TYR B 1 160 ? 48.887  -10.381 7.735   1.00 18.67  ? 139 TYR B CG  1 
ATOM   3451 C  CD1 . TYR B 1 160 ? 47.996  -11.306 7.212   1.00 20.01  ? 139 TYR B CD1 1 
ATOM   3452 C  CD2 . TYR B 1 160 ? 48.602  -9.030  7.573   1.00 22.09  ? 139 TYR B CD2 1 
ATOM   3453 C  CE1 . TYR B 1 160 ? 46.872  -10.905 6.528   1.00 19.00  ? 139 TYR B CE1 1 
ATOM   3454 C  CE2 . TYR B 1 160 ? 47.474  -8.619  6.888   1.00 18.75  ? 139 TYR B CE2 1 
ATOM   3455 C  CZ  . TYR B 1 160 ? 46.613  -9.565  6.369   1.00 16.34  ? 139 TYR B CZ  1 
ATOM   3456 O  OH  . TYR B 1 160 ? 45.485  -9.186  5.687   1.00 19.06  ? 139 TYR B OH  1 
ATOM   3457 N  N   . GLN B 1 161 ? 50.997  -11.501 11.973  1.00 22.50  ? 140 GLN B N   1 
ATOM   3458 C  CA  . GLN B 1 161 ? 52.107  -11.980 12.791  1.00 26.47  ? 140 GLN B CA  1 
ATOM   3459 C  C   . GLN B 1 161 ? 53.435  -11.560 12.170  1.00 25.91  ? 140 GLN B C   1 
ATOM   3460 O  O   . GLN B 1 161 ? 54.417  -12.305 12.184  1.00 29.07  ? 140 GLN B O   1 
ATOM   3461 C  CB  . GLN B 1 161 ? 52.033  -13.497 12.974  1.00 30.06  ? 140 GLN B CB  1 
ATOM   3462 C  CG  . GLN B 1 161 ? 50.807  -13.955 13.747  1.00 31.83  ? 140 GLN B CG  1 
ATOM   3463 C  CD  . GLN B 1 161 ? 50.802  -13.448 15.178  1.00 29.24  ? 140 GLN B CD  1 
ATOM   3464 O  OE1 . GLN B 1 161 ? 51.738  -13.691 15.936  1.00 28.51  ? 140 GLN B OE1 1 
ATOM   3465 N  NE2 . GLN B 1 161 ? 49.751  -12.730 15.549  1.00 27.47  ? 140 GLN B NE2 1 
ATOM   3466 N  N   . THR B 1 162 ? 53.458  -10.343 11.631  1.00 25.28  ? 141 THR B N   1 
ATOM   3467 C  CA  . THR B 1 162 ? 54.603  -9.867  10.870  1.00 21.53  ? 141 THR B CA  1 
ATOM   3468 C  C   . THR B 1 162 ? 55.867  -9.856  11.719  1.00 27.17  ? 141 THR B C   1 
ATOM   3469 O  O   . THR B 1 162 ? 55.863  -9.407  12.870  1.00 28.57  ? 141 THR B O   1 
ATOM   3470 C  CB  . THR B 1 162 ? 54.325  -8.460  10.337  1.00 25.36  ? 141 THR B CB  1 
ATOM   3471 O  OG1 . THR B 1 162 ? 53.172  -8.490  9.484   1.00 22.36  ? 141 THR B OG1 1 
ATOM   3472 C  CG2 . THR B 1 162 ? 55.531  -7.922  9.560   1.00 23.19  ? 141 THR B CG2 1 
ATOM   3473 N  N   . ASN B 1 163 ? 56.961  -10.342 11.129  1.00 26.34  ? 142 ASN B N   1 
ATOM   3474 C  CA  . ASN B 1 163 ? 58.273  -10.322 11.761  1.00 28.65  ? 142 ASN B CA  1 
ATOM   3475 C  C   . ASN B 1 163 ? 59.097  -9.102  11.363  1.00 30.18  ? 142 ASN B C   1 
ATOM   3476 O  O   . ASN B 1 163 ? 59.818  -8.549  12.199  1.00 31.58  ? 142 ASN B O   1 
ATOM   3477 C  CB  . ASN B 1 163 ? 59.052  -11.592 11.401  1.00 34.93  ? 142 ASN B CB  1 
ATOM   3478 C  CG  . ASN B 1 163 ? 58.298  -12.857 11.748  1.00 39.23  ? 142 ASN B CG  1 
ATOM   3479 O  OD1 . ASN B 1 163 ? 58.078  -13.711 10.896  1.00 31.06  ? 142 ASN B OD1 1 
ATOM   3480 N  ND2 . ASN B 1 163 ? 57.898  -12.983 13.006  1.00 45.47  ? 142 ASN B ND2 1 
ATOM   3481 N  N   . GLN B 1 164 ? 59.021  -8.674  10.102  1.00 31.75  ? 143 GLN B N   1 
ATOM   3482 C  CA  . GLN B 1 164 ? 59.867  -7.598  9.605   1.00 36.82  ? 143 GLN B CA  1 
ATOM   3483 C  C   . GLN B 1 164 ? 59.069  -6.684  8.689   1.00 33.34  ? 143 GLN B C   1 
ATOM   3484 O  O   . GLN B 1 164 ? 58.197  -7.132  7.943   1.00 32.01  ? 143 GLN B O   1 
ATOM   3485 C  CB  . GLN B 1 164 ? 61.086  -8.151  8.854   1.00 39.19  ? 143 GLN B CB  1 
ATOM   3486 C  CG  . GLN B 1 164 ? 62.055  -8.921  9.738   1.00 42.62  ? 143 GLN B CG  1 
ATOM   3487 C  CD  . GLN B 1 164 ? 62.993  -9.811  8.946   1.00 59.05  ? 143 GLN B CD  1 
ATOM   3488 O  OE1 . GLN B 1 164 ? 63.505  -9.420  7.894   1.00 59.81  ? 143 GLN B OE1 1 
ATOM   3489 N  NE2 . GLN B 1 164 ? 63.218  -11.022 9.446   1.00 56.09  ? 143 GLN B NE2 1 
ATOM   3490 N  N   . VAL B 1 165 ? 59.393  -5.391  8.739   1.00 31.14  ? 144 VAL B N   1 
ATOM   3491 C  CA  . VAL B 1 165 ? 58.699  -4.375  7.964   1.00 38.64  ? 144 VAL B CA  1 
ATOM   3492 C  C   . VAL B 1 165 ? 59.737  -3.481  7.298   1.00 39.34  ? 144 VAL B C   1 
ATOM   3493 O  O   . VAL B 1 165 ? 60.583  -2.902  7.985   1.00 38.65  ? 144 VAL B O   1 
ATOM   3494 C  CB  . VAL B 1 165 ? 57.755  -3.526  8.835   1.00 42.60  ? 144 VAL B CB  1 
ATOM   3495 C  CG1 . VAL B 1 165 ? 57.027  -2.494  7.981   1.00 40.54  ? 144 VAL B CG1 1 
ATOM   3496 C  CG2 . VAL B 1 165 ? 56.763  -4.407  9.586   1.00 31.85  ? 144 VAL B CG2 1 
ATOM   3497 N  N   . PRO B 1 166 ? 59.727  -3.333  5.965   1.00 44.83  ? 145 PRO B N   1 
ATOM   3498 C  CA  . PRO B 1 166 ? 60.527  -2.275  5.330   1.00 50.59  ? 145 PRO B CA  1 
ATOM   3499 C  C   . PRO B 1 166 ? 59.850  -0.927  5.512   1.00 56.86  ? 145 PRO B C   1 
ATOM   3500 O  O   . PRO B 1 166 ? 58.820  -0.642  4.894   1.00 63.87  ? 145 PRO B O   1 
ATOM   3501 C  CB  . PRO B 1 166 ? 60.567  -2.706  3.856   1.00 44.65  ? 145 PRO B CB  1 
ATOM   3502 C  CG  . PRO B 1 166 ? 59.342  -3.505  3.661   1.00 42.89  ? 145 PRO B CG  1 
ATOM   3503 C  CD  . PRO B 1 166 ? 59.083  -4.209  4.968   1.00 42.72  ? 145 PRO B CD  1 
ATOM   3504 N  N   . VAL B 1 167 ? 60.425  -0.094  6.373   1.00 65.32  ? 146 VAL B N   1 
ATOM   3505 C  CA  . VAL B 1 167 ? 59.868  1.210   6.704   1.00 66.23  ? 146 VAL B CA  1 
ATOM   3506 C  C   . VAL B 1 167 ? 60.759  2.278   6.092   1.00 67.35  ? 146 VAL B C   1 
ATOM   3507 O  O   . VAL B 1 167 ? 61.981  2.263   6.287   1.00 70.09  ? 146 VAL B O   1 
ATOM   3508 C  CB  . VAL B 1 167 ? 59.747  1.405   8.226   1.00 58.50  ? 146 VAL B CB  1 
ATOM   3509 N  N   . GLY B 1 168 ? 60.153  3.189   5.338   1.00 71.56  ? 147 GLY B N   1 
ATOM   3510 C  CA  . GLY B 1 168 ? 60.861  4.387   4.940   1.00 86.21  ? 147 GLY B CA  1 
ATOM   3511 C  C   . GLY B 1 168 ? 61.218  5.242   6.139   1.00 77.31  ? 147 GLY B C   1 
ATOM   3512 O  O   . GLY B 1 168 ? 60.670  5.093   7.231   1.00 74.17  ? 147 GLY B O   1 
ATOM   3513 N  N   . GLU B 1 169 ? 62.176  6.149   5.934   1.00 90.76  ? 148 GLU B N   1 
ATOM   3514 C  CA  . GLU B 1 169 ? 62.541  7.068   7.006   1.00 94.82  ? 148 GLU B CA  1 
ATOM   3515 C  C   . GLU B 1 169 ? 61.338  7.884   7.462   1.00 95.01  ? 148 GLU B C   1 
ATOM   3516 O  O   . GLU B 1 169 ? 61.218  8.211   8.649   1.00 82.82  ? 148 GLU B O   1 
ATOM   3517 C  CB  . GLU B 1 169 ? 63.669  7.992   6.546   1.00 89.54  ? 148 GLU B CB  1 
ATOM   3518 N  N   . ASP B 1 170 ? 60.436  8.210   6.534   1.00 86.77  ? 149 ASP B N   1 
ATOM   3519 C  CA  . ASP B 1 170 ? 59.229  8.957   6.866   1.00 75.44  ? 149 ASP B CA  1 
ATOM   3520 C  C   . ASP B 1 170 ? 58.268  8.171   7.751   1.00 69.31  ? 149 ASP B C   1 
ATOM   3521 O  O   . ASP B 1 170 ? 57.408  8.778   8.397   1.00 64.15  ? 149 ASP B O   1 
ATOM   3522 C  CB  . ASP B 1 170 ? 58.515  9.379   5.577   1.00 74.27  ? 149 ASP B CB  1 
ATOM   3523 C  CG  . ASP B 1 170 ? 58.382  8.237   4.576   1.00 80.21  ? 149 ASP B CG  1 
ATOM   3524 O  OD1 . ASP B 1 170 ? 58.561  7.065   4.968   1.00 74.23  ? 149 ASP B OD1 1 
ATOM   3525 O  OD2 . ASP B 1 170 ? 58.114  8.517   3.388   1.00 93.36  ? 149 ASP B OD2 1 
ATOM   3526 N  N   . GLN B 1 171 ? 58.388  6.845   7.795   1.00 67.04  ? 150 GLN B N   1 
ATOM   3527 C  CA  . GLN B 1 171 ? 57.452  6.000   8.526   1.00 62.13  ? 150 GLN B CA  1 
ATOM   3528 C  C   . GLN B 1 171 ? 58.047  5.426   9.807   1.00 56.64  ? 150 GLN B C   1 
ATOM   3529 O  O   . GLN B 1 171 ? 57.459  4.513   10.396  1.00 48.61  ? 150 GLN B O   1 
ATOM   3530 C  CB  . GLN B 1 171 ? 56.963  4.863   7.623   1.00 65.81  ? 150 GLN B CB  1 
ATOM   3531 C  CG  . GLN B 1 171 ? 56.485  5.314   6.245   1.00 78.14  ? 150 GLN B CG  1 
ATOM   3532 C  CD  . GLN B 1 171 ? 54.995  5.115   6.041   1.00 76.95  ? 150 GLN B CD  1 
ATOM   3533 O  OE1 . GLN B 1 171 ? 54.175  5.804   6.647   1.00 69.53  ? 150 GLN B OE1 1 
ATOM   3534 N  NE2 . GLN B 1 171 ? 54.637  4.167   5.181   1.00 73.72  ? 150 GLN B NE2 1 
ATOM   3535 N  N   . LYS B 1 172 ? 59.192  5.939   10.260  1.00 64.23  ? 151 LYS B N   1 
ATOM   3536 C  CA  . LYS B 1 172 ? 59.839  5.371   11.439  1.00 57.67  ? 151 LYS B CA  1 
ATOM   3537 C  C   . LYS B 1 172 ? 58.935  5.461   12.664  1.00 48.84  ? 151 LYS B C   1 
ATOM   3538 O  O   . LYS B 1 172 ? 58.773  4.482   13.401  1.00 40.03  ? 151 LYS B O   1 
ATOM   3539 C  CB  . LYS B 1 172 ? 61.165  6.084   11.699  1.00 50.23  ? 151 LYS B CB  1 
ATOM   3540 C  CG  . LYS B 1 172 ? 62.262  5.734   10.709  1.00 65.50  ? 151 LYS B CG  1 
ATOM   3541 C  CD  . LYS B 1 172 ? 63.129  4.596   11.223  1.00 73.96  ? 151 LYS B CD  1 
ATOM   3542 C  CE  . LYS B 1 172 ? 64.236  4.254   10.237  1.00 82.55  ? 151 LYS B CE  1 
ATOM   3543 N  NZ  . LYS B 1 172 ? 65.221  3.295   10.814  1.00 89.52  ? 151 LYS B NZ  1 
ATOM   3544 N  N   . GLN B 1 173 ? 58.332  6.630   12.896  1.00 47.62  ? 152 GLN B N   1 
ATOM   3545 C  CA  . GLN B 1 173 ? 57.487  6.798   14.075  1.00 45.80  ? 152 GLN B CA  1 
ATOM   3546 C  C   . GLN B 1 173 ? 56.302  5.845   14.040  1.00 45.25  ? 152 GLN B C   1 
ATOM   3547 O  O   . GLN B 1 173 ? 55.907  5.292   15.073  1.00 39.73  ? 152 GLN B O   1 
ATOM   3548 C  CB  . GLN B 1 173 ? 56.993  8.241   14.179  1.00 47.55  ? 152 GLN B CB  1 
ATOM   3549 C  CG  . GLN B 1 173 ? 57.735  9.090   15.198  1.00 57.50  ? 152 GLN B CG  1 
ATOM   3550 C  CD  . GLN B 1 173 ? 56.861  10.181  15.789  1.00 62.75  ? 152 GLN B CD  1 
ATOM   3551 O  OE1 . GLN B 1 173 ? 56.566  11.184  15.135  1.00 54.08  ? 152 GLN B OE1 1 
ATOM   3552 N  NE2 . GLN B 1 173 ? 56.433  9.985   17.034  1.00 62.37  ? 152 GLN B NE2 1 
ATOM   3553 N  N   . HIS B 1 174 ? 55.714  5.650   12.861  1.00 39.32  ? 153 HIS B N   1 
ATOM   3554 C  CA  . HIS B 1 174 ? 54.559  4.770   12.752  1.00 41.54  ? 153 HIS B CA  1 
ATOM   3555 C  C   . HIS B 1 174 ? 54.921  3.342   13.135  1.00 39.63  ? 153 HIS B C   1 
ATOM   3556 O  O   . HIS B 1 174 ? 54.152  2.663   13.825  1.00 37.19  ? 153 HIS B O   1 
ATOM   3557 C  CB  . HIS B 1 174 ? 53.999  4.832   11.334  1.00 43.34  ? 153 HIS B CB  1 
ATOM   3558 C  CG  . HIS B 1 174 ? 53.642  6.218   10.892  1.00 44.82  ? 153 HIS B CG  1 
ATOM   3559 N  ND1 . HIS B 1 174 ? 54.586  7.134   10.480  1.00 56.54  ? 153 HIS B ND1 1 
ATOM   3560 C  CD2 . HIS B 1 174 ? 52.447  6.849   10.814  1.00 44.86  ? 153 HIS B CD2 1 
ATOM   3561 C  CE1 . HIS B 1 174 ? 53.986  8.266   10.156  1.00 57.04  ? 153 HIS B CE1 1 
ATOM   3562 N  NE2 . HIS B 1 174 ? 52.688  8.120   10.352  1.00 45.60  ? 153 HIS B NE2 1 
ATOM   3563 N  N   . LEU B 1 175 ? 56.093  2.870   12.708  1.00 35.39  ? 154 LEU B N   1 
ATOM   3564 C  CA  . LEU B 1 175 ? 56.499  1.510   13.049  1.00 41.06  ? 154 LEU B CA  1 
ATOM   3565 C  C   . LEU B 1 175 ? 56.722  1.368   14.551  1.00 35.96  ? 154 LEU B C   1 
ATOM   3566 O  O   . LEU B 1 175 ? 56.409  0.324   15.133  1.00 36.87  ? 154 LEU B O   1 
ATOM   3567 C  CB  . LEU B 1 175 ? 57.758  1.128   12.268  1.00 42.95  ? 154 LEU B CB  1 
ATOM   3568 C  CG  . LEU B 1 175 ? 58.115  -0.356  12.104  1.00 49.93  ? 154 LEU B CG  1 
ATOM   3569 C  CD1 . LEU B 1 175 ? 58.854  -0.898  13.318  1.00 49.28  ? 154 LEU B CD1 1 
ATOM   3570 C  CD2 . LEU B 1 175 ? 56.881  -1.213  11.820  1.00 51.43  ? 154 LEU B CD2 1 
ATOM   3571 N  N   . GLU B 1 176 ? 57.262  2.404   15.198  1.00 35.90  ? 155 GLU B N   1 
ATOM   3572 C  CA  . GLU B 1 176 ? 57.507  2.320   16.633  1.00 37.97  ? 155 GLU B CA  1 
ATOM   3573 C  C   . GLU B 1 176 ? 56.209  2.356   17.429  1.00 33.86  ? 155 GLU B C   1 
ATOM   3574 O  O   . GLU B 1 176 ? 56.144  1.788   18.525  1.00 35.63  ? 155 GLU B O   1 
ATOM   3575 C  CB  . GLU B 1 176 ? 58.440  3.446   17.075  1.00 43.02  ? 155 GLU B CB  1 
ATOM   3576 C  CG  . GLU B 1 176 ? 59.791  3.431   16.364  1.00 48.19  ? 155 GLU B CG  1 
ATOM   3577 C  CD  . GLU B 1 176 ? 60.416  2.045   16.318  1.00 57.16  ? 155 GLU B CD  1 
ATOM   3578 O  OE1 . GLU B 1 176 ? 60.481  1.381   17.377  1.00 55.81  ? 155 GLU B OE1 1 
ATOM   3579 O  OE2 . GLU B 1 176 ? 60.826  1.612   15.218  1.00 59.66  ? 155 GLU B OE2 1 
ATOM   3580 N  N   . LEU B 1 177 ? 55.173  3.020   16.910  1.00 31.97  ? 156 LEU B N   1 
ATOM   3581 C  CA  . LEU B 1 177 ? 53.858  2.923   17.535  1.00 34.18  ? 156 LEU B CA  1 
ATOM   3582 C  C   . LEU B 1 177 ? 53.321  1.501   17.446  1.00 35.65  ? 156 LEU B C   1 
ATOM   3583 O  O   . LEU B 1 177 ? 52.738  0.988   18.407  1.00 31.59  ? 156 LEU B O   1 
ATOM   3584 C  CB  . LEU B 1 177 ? 52.882  3.900   16.879  1.00 40.44  ? 156 LEU B CB  1 
ATOM   3585 C  CG  . LEU B 1 177 ? 51.441  3.868   17.401  1.00 40.62  ? 156 LEU B CG  1 
ATOM   3586 C  CD1 . LEU B 1 177 ? 51.334  4.528   18.766  1.00 40.69  ? 156 LEU B CD1 1 
ATOM   3587 C  CD2 . LEU B 1 177 ? 50.497  4.532   16.411  1.00 37.52  ? 156 LEU B CD2 1 
ATOM   3588 N  N   . SER B 1 178 ? 53.507  0.848   16.297  1.00 31.07  ? 157 SER B N   1 
ATOM   3589 C  CA  . SER B 1 178 ? 53.053  -0.530  16.149  1.00 31.07  ? 157 SER B CA  1 
ATOM   3590 C  C   . SER B 1 178 ? 53.758  -1.451  17.136  1.00 31.56  ? 157 SER B C   1 
ATOM   3591 O  O   . SER B 1 178 ? 53.136  -2.355  17.706  1.00 35.58  ? 157 SER B O   1 
ATOM   3592 C  CB  . SER B 1 178 ? 53.289  -1.006  14.716  1.00 34.28  ? 157 SER B CB  1 
ATOM   3593 O  OG  . SER B 1 178 ? 52.750  -0.082  13.788  1.00 36.66  ? 157 SER B OG  1 
ATOM   3594 N  N   . ARG B 1 179 ? 55.062  -1.253  17.332  1.00 26.21  ? 158 ARG B N   1 
ATOM   3595 C  CA  . ARG B 1 179 ? 55.787  -2.033  18.329  1.00 27.09  ? 158 ARG B CA  1 
ATOM   3596 C  C   . ARG B 1 179 ? 55.247  -1.766  19.729  1.00 24.69  ? 158 ARG B C   1 
ATOM   3597 O  O   . ARG B 1 179 ? 55.009  -2.699  20.502  1.00 29.11  ? 158 ARG B O   1 
ATOM   3598 C  CB  . ARG B 1 179 ? 57.282  -1.712  18.254  1.00 38.67  ? 158 ARG B CB  1 
ATOM   3599 C  CG  . ARG B 1 179 ? 57.992  -2.332  17.054  1.00 43.31  ? 158 ARG B CG  1 
ATOM   3600 C  CD  . ARG B 1 179 ? 59.435  -1.850  16.929  1.00 42.28  ? 158 ARG B CD  1 
ATOM   3601 N  NE  . ARG B 1 179 ? 60.143  -1.861  18.204  1.00 57.35  ? 158 ARG B NE  1 
ATOM   3602 C  CZ  . ARG B 1 179 ? 60.782  -2.909  18.707  1.00 58.50  ? 158 ARG B CZ  1 
ATOM   3603 N  NH1 . ARG B 1 179 ? 60.817  -4.070  18.072  1.00 54.89  ? 158 ARG B NH1 1 
ATOM   3604 N  NH2 . ARG B 1 179 ? 61.403  -2.789  19.877  1.00 68.66  ? 158 ARG B NH2 1 
ATOM   3605 N  N   . ASP B 1 180 ? 55.024  -0.494  20.066  1.00 26.79  ? 159 ASP B N   1 
ATOM   3606 C  CA  . ASP B 1 180 ? 54.585  -0.155  21.417  1.00 30.10  ? 159 ASP B CA  1 
ATOM   3607 C  C   . ASP B 1 180 ? 53.194  -0.708  21.701  1.00 29.89  ? 159 ASP B C   1 
ATOM   3608 O  O   . ASP B 1 180 ? 52.908  -1.141  22.824  1.00 29.39  ? 159 ASP B O   1 
ATOM   3609 C  CB  . ASP B 1 180 ? 54.609  1.360   21.615  1.00 32.56  ? 159 ASP B CB  1 
ATOM   3610 C  CG  . ASP B 1 180 ? 56.016  1.933   21.588  1.00 39.15  ? 159 ASP B CG  1 
ATOM   3611 O  OD1 . ASP B 1 180 ? 56.979  1.180   21.848  1.00 41.28  ? 159 ASP B OD1 1 
ATOM   3612 O  OD2 . ASP B 1 180 ? 56.161  3.141   21.309  1.00 49.93  ? 159 ASP B OD2 1 
ATOM   3613 N  N   . VAL B 1 181 ? 52.313  -0.687  20.701  1.00 31.70  ? 160 VAL B N   1 
ATOM   3614 C  CA  . VAL B 1 181 ? 50.963  -1.202  20.895  1.00 33.47  ? 160 VAL B CA  1 
ATOM   3615 C  C   . VAL B 1 181 ? 50.985  -2.718  21.029  1.00 34.15  ? 160 VAL B C   1 
ATOM   3616 O  O   . VAL B 1 181 ? 50.259  -3.292  21.847  1.00 31.64  ? 160 VAL B O   1 
ATOM   3617 C  CB  . VAL B 1 181 ? 50.047  -0.750  19.745  1.00 33.15  ? 160 VAL B CB  1 
ATOM   3618 C  CG1 . VAL B 1 181 ? 48.681  -1.399  19.879  1.00 34.77  ? 160 VAL B CG1 1 
ATOM   3619 C  CG2 . VAL B 1 181 ? 49.919  0.768   19.732  1.00 33.21  ? 160 VAL B CG2 1 
ATOM   3620 N  N   . ALA B 1 182 ? 51.804  -3.393  20.221  1.00 27.91  ? 161 ALA B N   1 
ATOM   3621 C  CA  . ALA B 1 182 ? 51.890  -4.845  20.318  1.00 28.70  ? 161 ALA B CA  1 
ATOM   3622 C  C   . ALA B 1 182 ? 52.399  -5.271  21.688  1.00 27.09  ? 161 ALA B C   1 
ATOM   3623 O  O   . ALA B 1 182 ? 51.851  -6.191  22.303  1.00 30.58  ? 161 ALA B O   1 
ATOM   3624 C  CB  . ALA B 1 182 ? 52.797  -5.395  19.218  1.00 32.38  ? 161 ALA B CB  1 
ATOM   3625 N  N   . GLN B 1 183 ? 53.441  -4.608  22.189  1.00 26.68  ? 162 GLN B N   1 
ATOM   3626 C  CA  . GLN B 1 183 ? 53.970  -4.961  23.501  1.00 30.45  ? 162 GLN B CA  1 
ATOM   3627 C  C   . GLN B 1 183 ? 52.958  -4.663  24.601  1.00 28.68  ? 162 GLN B C   1 
ATOM   3628 O  O   . GLN B 1 183 ? 52.803  -5.452  25.540  1.00 28.57  ? 162 GLN B O   1 
ATOM   3629 C  CB  . GLN B 1 183 ? 55.282  -4.217  23.748  1.00 30.93  ? 162 GLN B CB  1 
ATOM   3630 C  CG  . GLN B 1 183 ? 56.370  -4.578  22.746  1.00 40.23  ? 162 GLN B CG  1 
ATOM   3631 C  CD  . GLN B 1 183 ? 57.704  -3.931  23.064  1.00 45.80  ? 162 GLN B CD  1 
ATOM   3632 O  OE1 . GLN B 1 183 ? 57.776  -2.741  23.366  1.00 46.80  ? 162 GLN B OE1 1 
ATOM   3633 N  NE2 . GLN B 1 183 ? 58.770  -4.720  23.002  1.00 51.14  ? 162 GLN B NE2 1 
ATOM   3634 N  N   . ARG B 1 184 ? 52.261  -3.531  24.499  1.00 30.66  ? 163 ARG B N   1 
ATOM   3635 C  CA  . ARG B 1 184 ? 51.268  -3.165  25.505  1.00 33.88  ? 163 ARG B CA  1 
ATOM   3636 C  C   . ARG B 1 184 ? 50.128  -4.172  25.542  1.00 29.66  ? 163 ARG B C   1 
ATOM   3637 O  O   . ARG B 1 184 ? 49.695  -4.600  26.619  1.00 31.83  ? 163 ARG B O   1 
ATOM   3638 C  CB  . ARG B 1 184 ? 50.747  -1.761  25.201  1.00 32.50  ? 163 ARG B CB  1 
ATOM   3639 C  CG  . ARG B 1 184 ? 49.641  -1.258  26.102  1.00 36.99  ? 163 ARG B CG  1 
ATOM   3640 C  CD  . ARG B 1 184 ? 49.248  0.148   25.674  1.00 31.57  ? 163 ARG B CD  1 
ATOM   3641 N  NE  . ARG B 1 184 ? 50.415  1.022   25.635  1.00 32.40  ? 163 ARG B NE  1 
ATOM   3642 C  CZ  . ARG B 1 184 ? 50.588  2.023   24.782  1.00 34.25  ? 163 ARG B CZ  1 
ATOM   3643 N  NH1 . ARG B 1 184 ? 49.685  2.309   23.857  1.00 32.59  ? 163 ARG B NH1 1 
ATOM   3644 N  NH2 . ARG B 1 184 ? 51.698  2.750   24.854  1.00 35.07  ? 163 ARG B NH2 1 
ATOM   3645 N  N   . PHE B 1 185 ? 49.638  -4.568  24.371  1.00 26.60  ? 164 PHE B N   1 
ATOM   3646 C  CA  . PHE B 1 185 ? 48.579  -5.566  24.301  1.00 27.31  ? 164 PHE B CA  1 
ATOM   3647 C  C   . PHE B 1 185 ? 49.043  -6.903  24.864  1.00 28.78  ? 164 PHE B C   1 
ATOM   3648 O  O   . PHE B 1 185 ? 48.326  -7.544  25.639  1.00 26.68  ? 164 PHE B O   1 
ATOM   3649 C  CB  . PHE B 1 185 ? 48.125  -5.725  22.855  1.00 28.46  ? 164 PHE B CB  1 
ATOM   3650 C  CG  . PHE B 1 185 ? 46.877  -6.526  22.701  1.00 22.18  ? 164 PHE B CG  1 
ATOM   3651 C  CD1 . PHE B 1 185 ? 46.931  -7.900  22.535  1.00 25.49  ? 164 PHE B CD1 1 
ATOM   3652 C  CD2 . PHE B 1 185 ? 45.646  -5.905  22.724  1.00 22.20  ? 164 PHE B CD2 1 
ATOM   3653 C  CE1 . PHE B 1 185 ? 45.773  -8.638  22.395  1.00 23.42  ? 164 PHE B CE1 1 
ATOM   3654 C  CE2 . PHE B 1 185 ? 44.495  -6.628  22.583  1.00 22.05  ? 164 PHE B CE2 1 
ATOM   3655 C  CZ  . PHE B 1 185 ? 44.551  -8.000  22.418  1.00 26.16  ? 164 PHE B CZ  1 
ATOM   3656 N  N   . ASN B 1 186 ? 50.250  -7.337  24.486  1.00 29.64  ? 165 ASN B N   1 
ATOM   3657 C  CA  . ASN B 1 186 ? 50.748  -8.627  24.951  1.00 32.30  ? 165 ASN B CA  1 
ATOM   3658 C  C   . ASN B 1 186 ? 50.986  -8.624  26.454  1.00 26.56  ? 165 ASN B C   1 
ATOM   3659 O  O   . ASN B 1 186 ? 50.863  -9.668  27.102  1.00 29.17  ? 165 ASN B O   1 
ATOM   3660 C  CB  . ASN B 1 186 ? 52.043  -8.997  24.228  1.00 29.57  ? 165 ASN B CB  1 
ATOM   3661 C  CG  . ASN B 1 186 ? 51.845  -9.233  22.743  1.00 29.62  ? 165 ASN B CG  1 
ATOM   3662 O  OD1 . ASN B 1 186 ? 50.731  -9.468  22.275  1.00 30.41  ? 165 ASN B OD1 1 
ATOM   3663 N  ND2 . ASN B 1 186 ? 52.939  -9.184  21.994  1.00 30.15  ? 165 ASN B ND2 1 
ATOM   3664 N  N   . ALA B 1 187 ? 51.347  -7.473  27.022  1.00 27.25  ? 166 ALA B N   1 
ATOM   3665 C  CA  . ALA B 1 187 ? 51.562  -7.401  28.461  1.00 34.23  ? 166 ALA B CA  1 
ATOM   3666 C  C   . ALA B 1 187 ? 50.265  -7.610  29.228  1.00 28.55  ? 166 ALA B C   1 
ATOM   3667 O  O   . ALA B 1 187 ? 50.297  -8.032  30.388  1.00 40.11  ? 166 ALA B O   1 
ATOM   3668 C  CB  . ALA B 1 187 ? 52.186  -6.054  28.830  1.00 25.48  ? 166 ALA B CB  1 
ATOM   3669 N  N   . ILE B 1 188 ? 49.129  -7.329  28.599  1.00 30.85  ? 167 ILE B N   1 
ATOM   3670 C  CA  . ILE B 1 188 ? 47.833  -7.490  29.243  1.00 32.25  ? 167 ILE B CA  1 
ATOM   3671 C  C   . ILE B 1 188 ? 47.269  -8.888  29.026  1.00 31.76  ? 167 ILE B C   1 
ATOM   3672 O  O   . ILE B 1 188 ? 46.741  -9.498  29.958  1.00 31.43  ? 167 ILE B O   1 
ATOM   3673 C  CB  . ILE B 1 188 ? 46.862  -6.413  28.719  1.00 30.85  ? 167 ILE B CB  1 
ATOM   3674 C  CG1 . ILE B 1 188 ? 47.343  -5.015  29.117  1.00 29.48  ? 167 ILE B CG1 1 
ATOM   3675 C  CG2 . ILE B 1 188 ? 45.456  -6.664  29.247  1.00 30.34  ? 167 ILE B CG2 1 
ATOM   3676 C  CD1 . ILE B 1 188 ? 46.747  -3.905  28.275  1.00 31.88  ? 167 ILE B CD1 1 
ATOM   3677 N  N   . TYR B 1 189 ? 47.381  -9.418  27.804  1.00 27.68  ? 168 TYR B N   1 
ATOM   3678 C  CA  . TYR B 1 189 ? 46.640  -10.602 27.398  1.00 27.14  ? 168 TYR B CA  1 
ATOM   3679 C  C   . TYR B 1 189 ? 47.504  -11.818 27.096  1.00 27.45  ? 168 TYR B C   1 
ATOM   3680 O  O   . TYR B 1 189 ? 46.953  -12.904 26.888  1.00 30.00  ? 168 TYR B O   1 
ATOM   3681 C  CB  . TYR B 1 189 ? 45.798  -10.282 26.155  1.00 27.45  ? 168 TYR B CB  1 
ATOM   3682 C  CG  . TYR B 1 189 ? 44.742  -9.235  26.400  1.00 28.35  ? 168 TYR B CG  1 
ATOM   3683 C  CD1 . TYR B 1 189 ? 43.598  -9.536  27.129  1.00 28.43  ? 168 TYR B CD1 1 
ATOM   3684 C  CD2 . TYR B 1 189 ? 44.886  -7.946  25.907  1.00 28.33  ? 168 TYR B CD2 1 
ATOM   3685 C  CE1 . TYR B 1 189 ? 42.624  -8.581  27.357  1.00 25.02  ? 168 TYR B CE1 1 
ATOM   3686 C  CE2 . TYR B 1 189 ? 43.919  -6.985  26.130  1.00 29.95  ? 168 TYR B CE2 1 
ATOM   3687 C  CZ  . TYR B 1 189 ? 42.791  -7.307  26.858  1.00 26.70  ? 168 TYR B CZ  1 
ATOM   3688 O  OH  . TYR B 1 189 ? 41.827  -6.348  27.079  1.00 27.53  ? 168 TYR B OH  1 
ATOM   3689 N  N   . GLY B 1 190 ? 48.822  -11.677 27.073  1.00 27.92  ? 169 GLY B N   1 
ATOM   3690 C  CA  . GLY B 1 190 ? 49.699  -12.740 26.623  1.00 32.87  ? 169 GLY B CA  1 
ATOM   3691 C  C   . GLY B 1 190 ? 50.208  -12.486 25.216  1.00 32.51  ? 169 GLY B C   1 
ATOM   3692 O  O   . GLY B 1 190 ? 49.839  -11.519 24.544  1.00 31.45  ? 169 GLY B O   1 
ATOM   3693 N  N   . ASP B 1 191 ? 51.067  -13.397 24.757  1.00 40.54  ? 170 ASP B N   1 
ATOM   3694 C  CA  . ASP B 1 191 ? 51.758  -13.238 23.476  1.00 42.76  ? 170 ASP B CA  1 
ATOM   3695 C  C   . ASP B 1 191 ? 50.792  -13.542 22.332  1.00 37.99  ? 170 ASP B C   1 
ATOM   3696 O  O   . ASP B 1 191 ? 50.765  -14.634 21.760  1.00 40.99  ? 170 ASP B O   1 
ATOM   3697 C  CB  . ASP B 1 191 ? 52.988  -14.136 23.425  1.00 45.69  ? 170 ASP B CB  1 
ATOM   3698 C  CG  . ASP B 1 191 ? 54.022  -13.772 24.476  1.00 51.02  ? 170 ASP B CG  1 
ATOM   3699 O  OD1 . ASP B 1 191 ? 54.503  -12.618 24.467  1.00 51.55  ? 170 ASP B OD1 1 
ATOM   3700 O  OD2 . ASP B 1 191 ? 54.347  -14.637 25.317  1.00 61.43  ? 170 ASP B OD2 1 
ATOM   3701 N  N   . ILE B 1 192 ? 49.994  -12.537 21.985  1.00 28.00  ? 171 ILE B N   1 
ATOM   3702 C  CA  . ILE B 1 192 ? 49.085  -12.651 20.850  1.00 26.50  ? 171 ILE B CA  1 
ATOM   3703 C  C   . ILE B 1 192 ? 49.742  -12.138 19.575  1.00 24.28  ? 171 ILE B C   1 
ATOM   3704 O  O   . ILE B 1 192 ? 49.606  -12.747 18.513  1.00 22.77  ? 171 ILE B O   1 
ATOM   3705 C  CB  . ILE B 1 192 ? 47.772  -11.894 21.138  1.00 30.79  ? 171 ILE B CB  1 
ATOM   3706 C  CG1 . ILE B 1 192 ? 47.194  -12.277 22.507  1.00 30.91  ? 171 ILE B CG1 1 
ATOM   3707 C  CG2 . ILE B 1 192 ? 46.756  -12.178 20.044  1.00 22.95  ? 171 ILE B CG2 1 
ATOM   3708 C  CD1 . ILE B 1 192 ? 46.582  -13.647 22.555  1.00 34.24  ? 171 ILE B CD1 1 
ATOM   3709 N  N   . PHE B 1 193 ? 50.460  -11.021 19.670  1.00 27.16  ? 172 PHE B N   1 
ATOM   3710 C  CA  . PHE B 1 193 ? 51.122  -10.396 18.536  1.00 25.19  ? 172 PHE B CA  1 
ATOM   3711 C  C   . PHE B 1 193 ? 52.618  -10.683 18.566  1.00 27.62  ? 172 PHE B C   1 
ATOM   3712 O  O   . PHE B 1 193 ? 53.226  -10.792 19.633  1.00 23.18  ? 172 PHE B O   1 
ATOM   3713 C  CB  . PHE B 1 193 ? 50.931  -8.875  18.539  1.00 21.54  ? 172 PHE B CB  1 
ATOM   3714 C  CG  . PHE B 1 193 ? 49.503  -8.429  18.475  1.00 22.05  ? 172 PHE B CG  1 
ATOM   3715 C  CD1 . PHE B 1 193 ? 48.702  -8.767  17.404  1.00 23.26  ? 172 PHE B CD1 1 
ATOM   3716 C  CD2 . PHE B 1 193 ? 48.969  -7.640  19.479  1.00 24.47  ? 172 PHE B CD2 1 
ATOM   3717 C  CE1 . PHE B 1 193 ? 47.388  -8.339  17.345  1.00 21.19  ? 172 PHE B CE1 1 
ATOM   3718 C  CE2 . PHE B 1 193 ? 47.664  -7.213  19.423  1.00 19.55  ? 172 PHE B CE2 1 
ATOM   3719 C  CZ  . PHE B 1 193 ? 46.871  -7.562  18.358  1.00 21.79  ? 172 PHE B CZ  1 
ATOM   3720 N  N   . LYS B 1 194 ? 53.207  -10.804 17.379  1.00 24.28  ? 173 LYS B N   1 
ATOM   3721 C  CA  . LYS B 1 194 ? 54.645  -10.626 17.239  1.00 31.09  ? 173 LYS B CA  1 
ATOM   3722 C  C   . LYS B 1 194 ? 54.961  -9.137  17.251  1.00 24.53  ? 173 LYS B C   1 
ATOM   3723 O  O   . LYS B 1 194 ? 54.191  -8.325  16.733  1.00 28.11  ? 173 LYS B O   1 
ATOM   3724 C  CB  . LYS B 1 194 ? 55.163  -11.243 15.941  1.00 31.52  ? 173 LYS B CB  1 
ATOM   3725 C  CG  . LYS B 1 194 ? 55.693  -12.654 16.081  1.00 41.82  ? 173 LYS B CG  1 
ATOM   3726 C  CD  . LYS B 1 194 ? 54.580  -13.661 15.919  1.00 45.77  ? 173 LYS B CD  1 
ATOM   3727 C  CE  . LYS B 1 194 ? 55.087  -15.088 16.021  1.00 49.42  ? 173 LYS B CE  1 
ATOM   3728 N  NZ  . LYS B 1 194 ? 54.046  -16.063 15.579  1.00 59.17  ? 173 LYS B NZ  1 
ATOM   3729 N  N   . VAL B 1 195 ? 56.097  -8.778  17.841  1.00 27.23  ? 174 VAL B N   1 
ATOM   3730 C  CA  . VAL B 1 195 ? 56.568  -7.396  17.856  1.00 32.93  ? 174 VAL B CA  1 
ATOM   3731 C  C   . VAL B 1 195 ? 57.383  -7.179  16.584  1.00 34.08  ? 174 VAL B C   1 
ATOM   3732 O  O   . VAL B 1 195 ? 58.483  -7.746  16.464  1.00 31.35  ? 174 VAL B O   1 
ATOM   3733 C  CB  . VAL B 1 195 ? 57.398  -7.098  19.111  1.00 34.51  ? 174 VAL B CB  1 
ATOM   3734 C  CG1 . VAL B 1 195 ? 57.881  -5.655  19.100  1.00 34.93  ? 174 VAL B CG1 1 
ATOM   3735 C  CG2 . VAL B 1 195 ? 56.577  -7.379  20.360  1.00 36.08  ? 174 VAL B CG2 1 
ATOM   3736 N  N   . PRO B 1 196 ? 56.902  -6.385  15.628  1.00 36.72  ? 175 PRO B N   1 
ATOM   3737 C  CA  . PRO B 1 196 ? 57.603  -6.275  14.346  1.00 38.63  ? 175 PRO B CA  1 
ATOM   3738 C  C   . PRO B 1 196 ? 58.918  -5.529  14.479  1.00 42.40  ? 175 PRO B C   1 
ATOM   3739 O  O   . PRO B 1 196 ? 59.093  -4.674  15.351  1.00 44.45  ? 175 PRO B O   1 
ATOM   3740 C  CB  . PRO B 1 196 ? 56.611  -5.504  13.468  1.00 32.80  ? 175 PRO B CB  1 
ATOM   3741 C  CG  . PRO B 1 196 ? 55.844  -4.669  14.439  1.00 37.10  ? 175 PRO B CG  1 
ATOM   3742 C  CD  . PRO B 1 196 ? 55.725  -5.497  15.691  1.00 33.70  ? 175 PRO B CD  1 
ATOM   3743 N  N   . GLU B 1 197 ? 59.851  -5.861  13.586  1.00 32.54  ? 176 GLU B N   1 
ATOM   3744 C  CA  . GLU B 1 197 ? 61.148  -5.214  13.535  1.00 44.78  ? 176 GLU B CA  1 
ATOM   3745 C  C   . GLU B 1 197 ? 61.328  -4.507  12.198  1.00 44.16  ? 176 GLU B C   1 
ATOM   3746 O  O   . GLU B 1 197 ? 60.941  -5.051  11.160  1.00 38.55  ? 176 GLU B O   1 
ATOM   3747 C  CB  . GLU B 1 197 ? 62.285  -6.231  13.718  1.00 44.64  ? 176 GLU B CB  1 
ATOM   3748 C  CG  . GLU B 1 197 ? 62.152  -7.113  14.950  1.00 54.75  ? 176 GLU B CG  1 
ATOM   3749 C  CD  . GLU B 1 197 ? 62.116  -6.317  16.241  1.00 58.63  ? 176 GLU B CD  1 
ATOM   3750 O  OE1 . GLU B 1 197 ? 62.648  -5.186  16.257  1.00 60.12  ? 176 GLU B OE1 1 
ATOM   3751 O  OE2 . GLU B 1 197 ? 61.555  -6.823  17.238  1.00 61.71  ? 176 GLU B OE2 1 
ATOM   3752 N  N   . PRO B 1 198 ? 61.899  -3.306  12.182  1.00 52.05  ? 177 PRO B N   1 
ATOM   3753 C  CA  . PRO B 1 198 ? 62.257  -2.686  10.902  1.00 53.59  ? 177 PRO B CA  1 
ATOM   3754 C  C   . PRO B 1 198 ? 63.339  -3.487  10.195  1.00 58.29  ? 177 PRO B C   1 
ATOM   3755 O  O   . PRO B 1 198 ? 64.146  -4.176  10.823  1.00 54.90  ? 177 PRO B O   1 
ATOM   3756 C  CB  . PRO B 1 198 ? 62.757  -1.295  11.305  1.00 54.53  ? 177 PRO B CB  1 
ATOM   3757 C  CG  . PRO B 1 198 ? 63.163  -1.443  12.731  1.00 53.31  ? 177 PRO B CG  1 
ATOM   3758 C  CD  . PRO B 1 198 ? 62.220  -2.433  13.324  1.00 58.03  ? 177 PRO B CD  1 
ATOM   3759 N  N   . PHE B 1 199 ? 63.345  -3.393  8.868   1.00 61.22  ? 178 PHE B N   1 
ATOM   3760 C  CA  . PHE B 1 199 ? 64.174  -4.241  8.020   1.00 71.62  ? 178 PHE B CA  1 
ATOM   3761 C  C   . PHE B 1 199 ? 65.016  -3.378  7.092   1.00 70.03  ? 178 PHE B C   1 
ATOM   3762 O  O   . PHE B 1 199 ? 64.559  -2.336  6.612   1.00 59.02  ? 178 PHE B O   1 
ATOM   3763 C  CB  . PHE B 1 199 ? 63.274  -5.235  7.253   1.00 65.21  ? 178 PHE B CB  1 
ATOM   3764 C  CG  . PHE B 1 199 ? 63.692  -5.496  5.835   1.00 72.25  ? 178 PHE B CG  1 
ATOM   3765 C  CD1 . PHE B 1 199 ? 64.870  -6.162  5.544   1.00 76.19  ? 178 PHE B CD1 1 
ATOM   3766 C  CD2 . PHE B 1 199 ? 62.872  -5.115  4.790   1.00 70.43  ? 178 PHE B CD2 1 
ATOM   3767 C  CE1 . PHE B 1 199 ? 65.232  -6.413  4.230   1.00 76.97  ? 178 PHE B CE1 1 
ATOM   3768 C  CE2 . PHE B 1 199 ? 63.229  -5.361  3.479   1.00 78.80  ? 178 PHE B CE2 1 
ATOM   3769 C  CZ  . PHE B 1 199 ? 64.411  -6.009  3.198   1.00 76.09  ? 178 PHE B CZ  1 
ATOM   3770 N  N   . ILE B 1 200 ? 66.250  -3.813  6.861   1.00 93.94  ? 179 ILE B N   1 
ATOM   3771 C  CA  . ILE B 1 200 ? 67.257  -3.024  6.155   1.00 97.45  ? 179 ILE B CA  1 
ATOM   3772 C  C   . ILE B 1 200 ? 67.633  -3.766  4.881   1.00 96.13  ? 179 ILE B C   1 
ATOM   3773 O  O   . ILE B 1 200 ? 67.488  -4.997  4.798   1.00 95.28  ? 179 ILE B O   1 
ATOM   3774 C  CB  . ILE B 1 200 ? 68.504  -2.767  7.031   1.00 102.37 ? 179 ILE B CB  1 
ATOM   3775 C  CG1 . ILE B 1 200 ? 69.342  -4.042  7.186   1.00 104.88 ? 179 ILE B CG1 1 
ATOM   3776 C  CG2 . ILE B 1 200 ? 68.098  -2.274  8.395   1.00 96.70  ? 179 ILE B CG2 1 
ATOM   3777 C  CD1 . ILE B 1 200 ? 70.481  -4.164  6.187   1.00 103.85 ? 179 ILE B CD1 1 
ATOM   3778 N  N   . PRO B 1 201 ? 68.168  -3.053  3.872   1.00 98.51  ? 180 PRO B N   1 
ATOM   3779 C  CA  . PRO B 1 201 ? 68.494  -3.648  2.567   1.00 97.69  ? 180 PRO B CA  1 
ATOM   3780 C  C   . PRO B 1 201 ? 69.228  -4.985  2.670   1.00 97.73  ? 180 PRO B C   1 
ATOM   3781 O  O   . PRO B 1 201 ? 69.182  -5.775  1.726   1.00 91.62  ? 180 PRO B O   1 
ATOM   3782 C  CB  . PRO B 1 201 ? 69.396  -2.592  1.916   1.00 98.59  ? 180 PRO B CB  1 
ATOM   3783 C  CG  . PRO B 1 201 ? 69.002  -1.310  2.552   1.00 97.12  ? 180 PRO B CG  1 
ATOM   3784 C  CD  . PRO B 1 201 ? 68.613  -1.649  3.964   1.00 98.14  ? 180 PRO B CD  1 
ATOM   3785 N  N   . GLY B 1 204 ? 71.377  -3.986  -2.604  1.00 73.75  ? 183 GLY B N   1 
ATOM   3786 C  CA  . GLY B 1 204 ? 71.104  -2.618  -2.209  1.00 72.25  ? 183 GLY B CA  1 
ATOM   3787 C  C   . GLY B 1 204 ? 71.721  -1.606  -3.154  1.00 77.09  ? 183 GLY B C   1 
ATOM   3788 O  O   . GLY B 1 204 ? 72.621  -0.857  -2.774  1.00 87.14  ? 183 GLY B O   1 
ATOM   3789 N  N   . ALA B 1 205 ? 71.233  -1.585  -4.392  1.00 77.81  ? 184 ALA B N   1 
ATOM   3790 C  CA  . ALA B 1 205 ? 71.763  -0.668  -5.391  1.00 75.01  ? 184 ALA B CA  1 
ATOM   3791 C  C   . ALA B 1 205 ? 71.476  0.774   -4.991  1.00 76.77  ? 184 ALA B C   1 
ATOM   3792 O  O   . ALA B 1 205 ? 70.350  1.115   -4.614  1.00 76.19  ? 184 ALA B O   1 
ATOM   3793 C  CB  . ALA B 1 205 ? 71.156  -0.966  -6.761  1.00 73.83  ? 184 ALA B CB  1 
ATOM   3794 N  N   . ARG B 1 206 ? 72.498  1.620   -5.082  1.00 77.52  ? 185 ARG B N   1 
ATOM   3795 C  CA  . ARG B 1 206 ? 72.370  3.033   -4.753  1.00 74.99  ? 185 ARG B CA  1 
ATOM   3796 C  C   . ARG B 1 206 ? 72.018  3.811   -6.015  1.00 72.42  ? 185 ARG B C   1 
ATOM   3797 O  O   . ARG B 1 206 ? 72.784  3.813   -6.985  1.00 76.83  ? 185 ARG B O   1 
ATOM   3798 C  CB  . ARG B 1 206 ? 73.667  3.561   -4.140  1.00 78.92  ? 185 ARG B CB  1 
ATOM   3799 N  N   . VAL B 1 207 ? 70.860  4.465   -6.003  1.00 69.24  ? 186 VAL B N   1 
ATOM   3800 C  CA  . VAL B 1 207 ? 70.409  5.313   -7.100  1.00 68.23  ? 186 VAL B CA  1 
ATOM   3801 C  C   . VAL B 1 207 ? 70.150  6.703   -6.538  1.00 72.27  ? 186 VAL B C   1 
ATOM   3802 O  O   . VAL B 1 207 ? 69.391  6.854   -5.573  1.00 67.31  ? 186 VAL B O   1 
ATOM   3803 C  CB  . VAL B 1 207 ? 69.146  4.749   -7.775  1.00 68.12  ? 186 VAL B CB  1 
ATOM   3804 C  CG1 . VAL B 1 207 ? 68.687  5.669   -8.895  1.00 66.74  ? 186 VAL B CG1 1 
ATOM   3805 C  CG2 . VAL B 1 207 ? 69.409  3.350   -8.304  1.00 54.24  ? 186 VAL B CG2 1 
ATOM   3806 N  N   . MET B 1 208 ? 70.775  7.710   -7.140  1.00 70.07  ? 187 MET B N   1 
ATOM   3807 C  CA  . MET B 1 208 ? 70.695  9.079   -6.661  1.00 70.10  ? 187 MET B CA  1 
ATOM   3808 C  C   . MET B 1 208 ? 69.828  9.924   -7.586  1.00 66.69  ? 187 MET B C   1 
ATOM   3809 O  O   . MET B 1 208 ? 69.695  9.640   -8.781  1.00 68.98  ? 187 MET B O   1 
ATOM   3810 C  CB  . MET B 1 208 ? 72.086  9.720   -6.557  1.00 67.91  ? 187 MET B CB  1 
ATOM   3811 C  CG  . MET B 1 208 ? 72.893  9.411   -5.287  1.00 72.51  ? 187 MET B CG  1 
ATOM   3812 S  SD  . MET B 1 208 ? 71.976  9.245   -3.740  1.00 83.42  ? 187 MET B SD  1 
ATOM   3813 C  CE  . MET B 1 208 ? 72.366  7.553   -3.290  1.00 76.30  ? 187 MET B CE  1 
ATOM   3814 N  N   . SER B 1 209 ? 69.242  10.970  -7.011  1.00 65.93  ? 188 SER B N   1 
ATOM   3815 C  CA  . SER B 1 209 ? 68.453  11.916  -7.786  1.00 71.45  ? 188 SER B CA  1 
ATOM   3816 C  C   . SER B 1 209 ? 69.308  12.530  -8.889  1.00 77.11  ? 188 SER B C   1 
ATOM   3817 O  O   . SER B 1 209 ? 70.452  12.929  -8.660  1.00 74.88  ? 188 SER B O   1 
ATOM   3818 C  CB  . SER B 1 209 ? 67.905  13.002  -6.862  1.00 76.63  ? 188 SER B CB  1 
ATOM   3819 O  OG  . SER B 1 209 ? 67.301  12.427  -5.714  1.00 85.78  ? 188 SER B OG  1 
ATOM   3820 N  N   . LEU B 1 210 ? 68.741  12.606  -10.097 1.00 69.98  ? 189 LEU B N   1 
ATOM   3821 C  CA  . LEU B 1 210 ? 69.529  12.991  -11.265 1.00 71.54  ? 189 LEU B CA  1 
ATOM   3822 C  C   . LEU B 1 210 ? 70.012  14.434  -11.166 1.00 76.45  ? 189 LEU B C   1 
ATOM   3823 O  O   . LEU B 1 210 ? 71.219  14.701  -11.196 1.00 76.93  ? 189 LEU B O   1 
ATOM   3824 C  CB  . LEU B 1 210 ? 68.708  12.787  -12.540 1.00 66.88  ? 189 LEU B CB  1 
ATOM   3825 C  CG  . LEU B 1 210 ? 68.386  11.341  -12.926 1.00 74.49  ? 189 LEU B CG  1 
ATOM   3826 C  CD1 . LEU B 1 210 ? 67.740  11.298  -14.302 1.00 69.01  ? 189 LEU B CD1 1 
ATOM   3827 C  CD2 . LEU B 1 210 ? 69.633  10.469  -12.893 1.00 59.69  ? 189 LEU B CD2 1 
ATOM   3828 N  N   . LEU B 1 211 ? 69.083  15.383  -11.054 1.00 73.98  ? 190 LEU B N   1 
ATOM   3829 C  CA  . LEU B 1 211 ? 69.437  16.797  -11.031 1.00 74.89  ? 190 LEU B CA  1 
ATOM   3830 C  C   . LEU B 1 211 ? 69.911  17.266  -9.663  1.00 72.52  ? 190 LEU B C   1 
ATOM   3831 O  O   . LEU B 1 211 ? 70.191  18.459  -9.496  1.00 77.12  ? 190 LEU B O   1 
ATOM   3832 C  CB  . LEU B 1 211 ? 68.247  17.649  -11.483 1.00 72.59  ? 190 LEU B CB  1 
ATOM   3833 C  CG  . LEU B 1 211 ? 67.561  17.227  -12.787 1.00 81.21  ? 190 LEU B CG  1 
ATOM   3834 C  CD1 . LEU B 1 211 ? 66.673  18.343  -13.324 1.00 73.84  ? 190 LEU B CD1 1 
ATOM   3835 C  CD2 . LEU B 1 211 ? 68.579  16.801  -13.836 1.00 81.72  ? 190 LEU B CD2 1 
ATOM   3836 N  N   . GLU B 1 212 ? 70.008  16.372  -8.681  1.00 75.08  ? 191 GLU B N   1 
ATOM   3837 C  CA  . GLU B 1 212 ? 70.538  16.727  -7.365  1.00 77.94  ? 191 GLU B CA  1 
ATOM   3838 C  C   . GLU B 1 212 ? 71.098  15.492  -6.676  1.00 73.76  ? 191 GLU B C   1 
ATOM   3839 O  O   . GLU B 1 212 ? 70.585  15.054  -5.648  1.00 69.91  ? 191 GLU B O   1 
ATOM   3840 C  CB  . GLU B 1 212 ? 69.443  17.361  -6.504  1.00 77.04  ? 191 GLU B CB  1 
ATOM   3841 N  N   . PRO B 1 213 ? 72.181  14.899  -7.224  1.00 79.40  ? 192 PRO B N   1 
ATOM   3842 C  CA  . PRO B 1 213 ? 72.756  13.689  -6.612  1.00 78.35  ? 192 PRO B CA  1 
ATOM   3843 C  C   . PRO B 1 213 ? 73.249  13.925  -5.186  1.00 81.12  ? 192 PRO B C   1 
ATOM   3844 O  O   . PRO B 1 213 ? 73.540  12.957  -4.484  1.00 84.00  ? 192 PRO B O   1 
ATOM   3845 C  CB  . PRO B 1 213 ? 73.926  13.344  -7.542  1.00 74.74  ? 192 PRO B CB  1 
ATOM   3846 C  CG  . PRO B 1 213 ? 73.606  14.014  -8.834  1.00 78.38  ? 192 PRO B CG  1 
ATOM   3847 C  CD  . PRO B 1 213 ? 72.882  15.271  -8.463  1.00 76.70  ? 192 PRO B CD  1 
ATOM   3848 N  N   . LYS B 1 216 ? 69.034  11.146  -2.404  1.00 67.82  ? 195 LYS B N   1 
ATOM   3849 C  CA  . LYS B 1 216 ? 68.692  9.832   -2.933  1.00 79.38  ? 195 LYS B CA  1 
ATOM   3850 C  C   . LYS B 1 216 ? 67.374  9.880   -3.685  1.00 78.38  ? 195 LYS B C   1 
ATOM   3851 O  O   . LYS B 1 216 ? 66.413  10.505  -3.238  1.00 65.02  ? 195 LYS B O   1 
ATOM   3852 C  CB  . LYS B 1 216 ? 68.615  8.801   -1.806  1.00 68.04  ? 195 LYS B CB  1 
ATOM   3853 N  N   . MET B 1 217 ? 67.338  9.215   -4.837  1.00 68.90  ? 196 MET B N   1 
ATOM   3854 C  CA  . MET B 1 217 ? 66.117  9.171   -5.627  1.00 70.35  ? 196 MET B CA  1 
ATOM   3855 C  C   . MET B 1 217 ? 64.982  8.623   -4.775  1.00 72.91  ? 196 MET B C   1 
ATOM   3856 O  O   . MET B 1 217 ? 65.092  7.540   -4.192  1.00 75.61  ? 196 MET B O   1 
ATOM   3857 C  CB  . MET B 1 217 ? 66.316  8.309   -6.874  1.00 63.48  ? 196 MET B CB  1 
ATOM   3858 C  CG  . MET B 1 217 ? 65.146  8.382   -7.844  1.00 61.54  ? 196 MET B CG  1 
ATOM   3859 S  SD  . MET B 1 217 ? 65.335  7.374   -9.325  1.00 54.27  ? 196 MET B SD  1 
ATOM   3860 C  CE  . MET B 1 217 ? 66.442  8.388   -10.302 1.00 56.23  ? 196 MET B CE  1 
ATOM   3861 N  N   . SER B 1 218 ? 63.890  9.378   -4.699  1.00 80.64  ? 197 SER B N   1 
ATOM   3862 C  CA  . SER B 1 218 ? 62.763  9.037   -3.846  1.00 87.75  ? 197 SER B CA  1 
ATOM   3863 C  C   . SER B 1 218 ? 61.464  9.183   -4.624  1.00 85.97  ? 197 SER B C   1 
ATOM   3864 O  O   . SER B 1 218 ? 61.333  10.052  -5.489  1.00 85.39  ? 197 SER B O   1 
ATOM   3865 C  CB  . SER B 1 218 ? 62.720  9.930   -2.596  1.00 88.63  ? 197 SER B CB  1 
ATOM   3866 O  OG  . SER B 1 218 ? 62.515  11.287  -2.948  1.00 97.18  ? 197 SER B OG  1 
ATOM   3867 N  N   . LYS B 1 219 ? 60.501  8.315   -4.305  1.00 81.83  ? 198 LYS B N   1 
ATOM   3868 C  CA  . LYS B 1 219 ? 59.173  8.428   -4.894  1.00 78.42  ? 198 LYS B CA  1 
ATOM   3869 C  C   . LYS B 1 219 ? 58.416  9.637   -4.362  1.00 104.04 ? 198 LYS B C   1 
ATOM   3870 O  O   . LYS B 1 219 ? 57.409  10.034  -4.956  1.00 88.06  ? 198 LYS B O   1 
ATOM   3871 C  CB  . LYS B 1 219 ? 58.369  7.155   -4.628  1.00 99.67  ? 198 LYS B CB  1 
ATOM   3872 N  N   . SER B 1 220 ? 58.882  10.226  -3.264  1.00 83.15  ? 199 SER B N   1 
ATOM   3873 C  CA  . SER B 1 220 ? 58.259  11.398  -2.667  1.00 78.33  ? 199 SER B CA  1 
ATOM   3874 C  C   . SER B 1 220 ? 58.825  12.706  -3.203  1.00 79.93  ? 199 SER B C   1 
ATOM   3875 O  O   . SER B 1 220 ? 58.433  13.775  -2.725  1.00 78.08  ? 199 SER B O   1 
ATOM   3876 C  CB  . SER B 1 220 ? 58.428  11.356  -1.145  1.00 79.31  ? 199 SER B CB  1 
ATOM   3877 O  OG  . SER B 1 220 ? 59.797  11.255  -0.791  1.00 88.29  ? 199 SER B OG  1 
ATOM   3878 N  N   . ASP B 1 221 ? 59.732  12.646  -4.176  1.00 83.57  ? 200 ASP B N   1 
ATOM   3879 C  CA  . ASP B 1 221 ? 60.410  13.846  -4.651  1.00 79.25  ? 200 ASP B CA  1 
ATOM   3880 C  C   . ASP B 1 221 ? 59.399  14.858  -5.174  1.00 80.92  ? 200 ASP B C   1 
ATOM   3881 O  O   . ASP B 1 221 ? 58.582  14.545  -6.044  1.00 70.46  ? 200 ASP B O   1 
ATOM   3882 C  CB  . ASP B 1 221 ? 61.409  13.474  -5.750  1.00 80.09  ? 200 ASP B CB  1 
ATOM   3883 C  CG  . ASP B 1 221 ? 62.678  14.309  -5.700  1.00 80.15  ? 200 ASP B CG  1 
ATOM   3884 O  OD1 . ASP B 1 221 ? 62.580  15.546  -5.552  1.00 79.32  ? 200 ASP B OD1 1 
ATOM   3885 O  OD2 . ASP B 1 221 ? 63.777  13.723  -5.804  1.00 86.86  ? 200 ASP B OD2 1 
ATOM   3886 N  N   . ASP B 1 222 ? 59.455  16.077  -4.631  1.00 79.96  ? 201 ASP B N   1 
ATOM   3887 C  CA  . ASP B 1 222 ? 58.636  17.164  -5.154  1.00 82.99  ? 201 ASP B CA  1 
ATOM   3888 C  C   . ASP B 1 222 ? 59.122  17.633  -6.519  1.00 83.65  ? 201 ASP B C   1 
ATOM   3889 O  O   . ASP B 1 222 ? 58.379  18.322  -7.226  1.00 78.67  ? 201 ASP B O   1 
ATOM   3890 C  CB  . ASP B 1 222 ? 58.628  18.337  -4.173  1.00 86.57  ? 201 ASP B CB  1 
ATOM   3891 N  N   . ASN B 1 223 ? 60.351  17.277  -6.898  1.00 78.60  ? 202 ASN B N   1 
ATOM   3892 C  CA  . ASN B 1 223 ? 60.912  17.607  -8.204  1.00 74.93  ? 202 ASN B CA  1 
ATOM   3893 C  C   . ASN B 1 223 ? 60.891  16.341  -9.054  1.00 75.24  ? 202 ASN B C   1 
ATOM   3894 O  O   . ASN B 1 223 ? 61.640  15.395  -8.789  1.00 72.98  ? 202 ASN B O   1 
ATOM   3895 C  CB  . ASN B 1 223 ? 62.331  18.153  -8.064  1.00 73.33  ? 202 ASN B CB  1 
ATOM   3896 C  CG  . ASN B 1 223 ? 62.777  18.940  -9.281  1.00 73.58  ? 202 ASN B CG  1 
ATOM   3897 O  OD1 . ASN B 1 223 ? 62.352  18.667  -10.404 1.00 71.55  ? 202 ASN B OD1 1 
ATOM   3898 N  ND2 . ASN B 1 223 ? 63.635  19.929  -9.061  1.00 69.05  ? 202 ASN B ND2 1 
ATOM   3899 N  N   . ARG B 1 224 ? 60.033  16.326  -10.076 1.00 80.48  ? 203 ARG B N   1 
ATOM   3900 C  CA  . ARG B 1 224 ? 59.858  15.119  -10.876 1.00 69.89  ? 203 ARG B CA  1 
ATOM   3901 C  C   . ARG B 1 224 ? 61.111  14.779  -11.673 1.00 64.72  ? 203 ARG B C   1 
ATOM   3902 O  O   . ARG B 1 224 ? 61.426  13.598  -11.851 1.00 57.11  ? 203 ARG B O   1 
ATOM   3903 C  CB  . ARG B 1 224 ? 58.663  15.282  -11.817 1.00 63.61  ? 203 ARG B CB  1 
ATOM   3904 N  N   . ASN B 1 225 ? 61.845  15.789  -12.142 1.00 66.38  ? 204 ASN B N   1 
ATOM   3905 C  CA  . ASN B 1 225 ? 62.997  15.554  -13.004 1.00 62.37  ? 204 ASN B CA  1 
ATOM   3906 C  C   . ASN B 1 225 ? 64.120  14.806  -12.297 1.00 63.29  ? 204 ASN B C   1 
ATOM   3907 O  O   . ASN B 1 225 ? 65.049  14.341  -12.967 1.00 59.76  ? 204 ASN B O   1 
ATOM   3908 C  CB  . ASN B 1 225 ? 63.516  16.889  -13.539 1.00 64.37  ? 204 ASN B CB  1 
ATOM   3909 C  CG  . ASN B 1 225 ? 62.417  17.729  -14.161 1.00 71.43  ? 204 ASN B CG  1 
ATOM   3910 O  OD1 . ASN B 1 225 ? 62.035  18.770  -13.624 1.00 69.72  ? 204 ASN B OD1 1 
ATOM   3911 N  ND2 . ASN B 1 225 ? 61.894  17.275  -15.294 1.00 65.43  ? 204 ASN B ND2 1 
ATOM   3912 N  N   . ASN B 1 226 ? 64.059  14.684  -10.972 1.00 59.49  ? 205 ASN B N   1 
ATOM   3913 C  CA  . ASN B 1 226 ? 65.070  13.967  -10.209 1.00 64.93  ? 205 ASN B CA  1 
ATOM   3914 C  C   . ASN B 1 226 ? 64.904  12.451  -10.250 1.00 63.71  ? 205 ASN B C   1 
ATOM   3915 O  O   . ASN B 1 226 ? 65.776  11.741  -9.737  1.00 63.87  ? 205 ASN B O   1 
ATOM   3916 C  CB  . ASN B 1 226 ? 65.043  14.434  -8.748  1.00 73.32  ? 205 ASN B CB  1 
ATOM   3917 C  CG  . ASN B 1 226 ? 66.040  15.545  -8.464  1.00 74.81  ? 205 ASN B CG  1 
ATOM   3918 O  OD1 . ASN B 1 226 ? 66.994  15.748  -9.215  1.00 75.12  ? 205 ASN B OD1 1 
ATOM   3919 N  ND2 . ASN B 1 226 ? 65.833  16.257  -7.362  1.00 67.52  ? 205 ASN B ND2 1 
ATOM   3920 N  N   . VAL B 1 227 ? 63.821  11.933  -10.837 1.00 59.17  ? 206 VAL B N   1 
ATOM   3921 C  CA  . VAL B 1 227 ? 63.507  10.511  -10.772 1.00 65.95  ? 206 VAL B CA  1 
ATOM   3922 C  C   . VAL B 1 227 ? 63.086  10.000  -12.143 1.00 56.82  ? 206 VAL B C   1 
ATOM   3923 O  O   . VAL B 1 227 ? 62.748  10.768  -13.045 1.00 57.31  ? 206 VAL B O   1 
ATOM   3924 C  CB  . VAL B 1 227 ? 62.392  10.215  -9.743  1.00 65.35  ? 206 VAL B CB  1 
ATOM   3925 C  CG1 . VAL B 1 227 ? 62.666  10.943  -8.433  1.00 69.82  ? 206 VAL B CG1 1 
ATOM   3926 C  CG2 . VAL B 1 227 ? 61.036  10.608  -10.307 1.00 53.29  ? 206 VAL B CG2 1 
ATOM   3927 N  N   . ILE B 1 228 ? 63.114  8.676   -12.285 1.00 56.31  ? 207 ILE B N   1 
ATOM   3928 C  CA  . ILE B 1 228 ? 62.644  7.984   -13.481 1.00 52.52  ? 207 ILE B CA  1 
ATOM   3929 C  C   . ILE B 1 228 ? 61.628  6.940   -13.039 1.00 55.29  ? 207 ILE B C   1 
ATOM   3930 O  O   . ILE B 1 228 ? 61.964  6.025   -12.278 1.00 52.74  ? 207 ILE B O   1 
ATOM   3931 C  CB  . ILE B 1 228 ? 63.797  7.326   -14.257 1.00 50.26  ? 207 ILE B CB  1 
ATOM   3932 C  CG1 . ILE B 1 228 ? 64.704  8.398   -14.859 1.00 47.43  ? 207 ILE B CG1 1 
ATOM   3933 C  CG2 . ILE B 1 228 ? 63.252  6.411   -15.348 1.00 44.09  ? 207 ILE B CG2 1 
ATOM   3934 C  CD1 . ILE B 1 228 ? 66.118  7.932   -15.094 1.00 51.34  ? 207 ILE B CD1 1 
ATOM   3935 N  N   . GLY B 1 229 ? 60.391  7.077   -13.510 1.00 50.97  ? 208 GLY B N   1 
ATOM   3936 C  CA  . GLY B 1 229 ? 59.356  6.135   -13.140 1.00 49.12  ? 208 GLY B CA  1 
ATOM   3937 C  C   . GLY B 1 229 ? 59.458  4.836   -13.916 1.00 44.56  ? 208 GLY B C   1 
ATOM   3938 O  O   . GLY B 1 229 ? 59.992  4.780   -15.022 1.00 40.38  ? 208 GLY B O   1 
ATOM   3939 N  N   . LEU B 1 230 ? 58.926  3.769   -13.315 1.00 41.12  ? 209 LEU B N   1 
ATOM   3940 C  CA  . LEU B 1 230 ? 58.937  2.476   -13.987 1.00 46.31  ? 209 LEU B CA  1 
ATOM   3941 C  C   . LEU B 1 230 ? 58.058  2.482   -15.231 1.00 42.09  ? 209 LEU B C   1 
ATOM   3942 O  O   . LEU B 1 230 ? 58.287  1.685   -16.146 1.00 39.73  ? 209 LEU B O   1 
ATOM   3943 C  CB  . LEU B 1 230 ? 58.478  1.369   -13.038 1.00 42.66  ? 209 LEU B CB  1 
ATOM   3944 C  CG  . LEU B 1 230 ? 59.400  0.957   -11.889 1.00 43.08  ? 209 LEU B CG  1 
ATOM   3945 C  CD1 . LEU B 1 230 ? 59.033  -0.449  -11.425 1.00 48.78  ? 209 LEU B CD1 1 
ATOM   3946 C  CD2 . LEU B 1 230 ? 60.869  1.026   -12.267 1.00 45.12  ? 209 LEU B CD2 1 
ATOM   3947 N  N   . LEU B 1 231 ? 57.053  3.359   -15.280 1.00 45.43  ? 210 LEU B N   1 
ATOM   3948 C  CA  . LEU B 1 231 ? 56.174  3.494   -16.436 1.00 50.34  ? 210 LEU B CA  1 
ATOM   3949 C  C   . LEU B 1 231 ? 56.582  4.662   -17.329 1.00 53.02  ? 210 LEU B C   1 
ATOM   3950 O  O   . LEU B 1 231 ? 55.728  5.303   -17.949 1.00 56.31  ? 210 LEU B O   1 
ATOM   3951 C  CB  . LEU B 1 231 ? 54.723  3.655   -15.984 1.00 44.18  ? 210 LEU B CB  1 
ATOM   3952 C  CG  . LEU B 1 231 ? 54.161  2.543   -15.095 1.00 50.86  ? 210 LEU B CG  1 
ATOM   3953 C  CD1 . LEU B 1 231 ? 52.643  2.653   -14.992 1.00 46.07  ? 210 LEU B CD1 1 
ATOM   3954 C  CD2 . LEU B 1 231 ? 54.565  1.169   -15.609 1.00 48.01  ? 210 LEU B CD2 1 
ATOM   3955 N  N   . GLU B 1 232 ? 57.881  4.933   -17.413 1.00 51.21  ? 211 GLU B N   1 
ATOM   3956 C  CA  . GLU B 1 232 ? 58.409  6.082   -18.134 1.00 51.99  ? 211 GLU B CA  1 
ATOM   3957 C  C   . GLU B 1 232 ? 58.792  5.662   -19.546 1.00 48.64  ? 211 GLU B C   1 
ATOM   3958 O  O   . GLU B 1 232 ? 59.503  4.670   -19.730 1.00 48.36  ? 211 GLU B O   1 
ATOM   3959 C  CB  . GLU B 1 232 ? 59.625  6.647   -17.398 1.00 50.48  ? 211 GLU B CB  1 
ATOM   3960 C  CG  . GLU B 1 232 ? 60.054  8.024   -17.860 1.00 54.58  ? 211 GLU B CG  1 
ATOM   3961 C  CD  . GLU B 1 232 ? 59.889  9.085   -16.786 1.00 61.70  ? 211 GLU B CD  1 
ATOM   3962 O  OE1 . GLU B 1 232 ? 59.246  8.809   -15.751 1.00 51.94  ? 211 GLU B OE1 1 
ATOM   3963 O  OE2 . GLU B 1 232 ? 60.409  10.203  -16.979 1.00 70.28  ? 211 GLU B OE2 1 
ATOM   3964 N  N   . ASP B 1 233 ? 58.322  6.415   -20.538 1.00 58.74  ? 212 ASP B N   1 
ATOM   3965 C  CA  . ASP B 1 233 ? 58.587  6.070   -21.925 1.00 56.64  ? 212 ASP B CA  1 
ATOM   3966 C  C   . ASP B 1 233 ? 60.056  6.325   -22.258 1.00 59.54  ? 212 ASP B C   1 
ATOM   3967 O  O   . ASP B 1 233 ? 60.726  7.120   -21.594 1.00 67.03  ? 212 ASP B O   1 
ATOM   3968 C  CB  . ASP B 1 233 ? 57.670  6.868   -22.852 1.00 58.21  ? 212 ASP B CB  1 
ATOM   3969 C  CG  . ASP B 1 233 ? 58.260  8.203   -23.260 1.00 71.31  ? 212 ASP B CG  1 
ATOM   3970 O  OD1 . ASP B 1 233 ? 58.192  8.538   -24.463 1.00 77.63  ? 212 ASP B OD1 1 
ATOM   3971 O  OD2 . ASP B 1 233 ? 58.793  8.915   -22.385 1.00 75.18  ? 212 ASP B OD2 1 
ATOM   3972 N  N   . PRO B 1 234 ? 60.586  5.646   -23.281 1.00 58.44  ? 213 PRO B N   1 
ATOM   3973 C  CA  . PRO B 1 234 ? 62.023  5.789   -23.579 1.00 59.75  ? 213 PRO B CA  1 
ATOM   3974 C  C   . PRO B 1 234 ? 62.463  7.217   -23.856 1.00 64.65  ? 213 PRO B C   1 
ATOM   3975 O  O   . PRO B 1 234 ? 63.591  7.584   -23.506 1.00 61.97  ? 213 PRO B O   1 
ATOM   3976 C  CB  . PRO B 1 234 ? 62.211  4.897   -24.815 1.00 59.03  ? 213 PRO B CB  1 
ATOM   3977 C  CG  . PRO B 1 234 ? 61.117  3.890   -24.725 1.00 57.03  ? 213 PRO B CG  1 
ATOM   3978 C  CD  . PRO B 1 234 ? 59.948  4.605   -24.107 1.00 55.32  ? 213 PRO B CD  1 
ATOM   3979 N  N   . LYS B 1 235 ? 61.616  8.029   -24.494 1.00 65.32  ? 214 LYS B N   1 
ATOM   3980 C  CA  . LYS B 1 235 ? 62.006  9.401   -24.810 1.00 63.04  ? 214 LYS B CA  1 
ATOM   3981 C  C   . LYS B 1 235 ? 62.224  10.220  -23.544 1.00 69.01  ? 214 LYS B C   1 
ATOM   3982 O  O   . LYS B 1 235 ? 63.158  11.027  -23.471 1.00 67.48  ? 214 LYS B O   1 
ATOM   3983 C  CB  . LYS B 1 235 ? 60.947  10.060  -25.694 1.00 56.52  ? 214 LYS B CB  1 
ATOM   3984 N  N   . SER B 1 236 ? 61.364  10.033  -22.538 1.00 68.06  ? 215 SER B N   1 
ATOM   3985 C  CA  . SER B 1 236 ? 61.483  10.803  -21.304 1.00 68.44  ? 215 SER B CA  1 
ATOM   3986 C  C   . SER B 1 236 ? 62.681  10.356  -20.480 1.00 62.87  ? 215 SER B C   1 
ATOM   3987 O  O   . SER B 1 236 ? 63.293  11.173  -19.784 1.00 61.76  ? 215 SER B O   1 
ATOM   3988 C  CB  . SER B 1 236 ? 60.199  10.679  -20.483 1.00 70.91  ? 215 SER B CB  1 
ATOM   3989 O  OG  . SER B 1 236 ? 60.288  11.416  -19.276 1.00 63.81  ? 215 SER B OG  1 
ATOM   3990 N  N   . VAL B 1 237 ? 63.019  9.066   -20.533 1.00 64.95  ? 216 VAL B N   1 
ATOM   3991 C  CA  . VAL B 1 237 ? 64.235  8.590   -19.882 1.00 66.56  ? 216 VAL B CA  1 
ATOM   3992 C  C   . VAL B 1 237 ? 65.459  9.208   -20.541 1.00 63.06  ? 216 VAL B C   1 
ATOM   3993 O  O   . VAL B 1 237 ? 66.393  9.649   -19.863 1.00 63.24  ? 216 VAL B O   1 
ATOM   3994 C  CB  . VAL B 1 237 ? 64.291  7.052   -19.915 1.00 63.41  ? 216 VAL B CB  1 
ATOM   3995 C  CG1 . VAL B 1 237 ? 65.670  6.564   -19.515 1.00 50.06  ? 216 VAL B CG1 1 
ATOM   3996 C  CG2 . VAL B 1 237 ? 63.231  6.463   -18.998 1.00 51.52  ? 216 VAL B CG2 1 
ATOM   3997 N  N   . VAL B 1 238 ? 65.474  9.253   -21.874 1.00 61.57  ? 217 VAL B N   1 
ATOM   3998 C  CA  . VAL B 1 238 ? 66.589  9.871   -22.587 1.00 65.34  ? 217 VAL B CA  1 
ATOM   3999 C  C   . VAL B 1 238 ? 66.713  11.338  -22.204 1.00 64.32  ? 217 VAL B C   1 
ATOM   4000 O  O   . VAL B 1 238 ? 67.821  11.870  -22.067 1.00 61.61  ? 217 VAL B O   1 
ATOM   4001 C  CB  . VAL B 1 238 ? 66.407  9.692   -24.107 1.00 60.08  ? 217 VAL B CB  1 
ATOM   4002 C  CG1 . VAL B 1 238 ? 67.075  10.819  -24.880 1.00 62.12  ? 217 VAL B CG1 1 
ATOM   4003 C  CG2 . VAL B 1 238 ? 66.967  8.349   -24.546 1.00 53.95  ? 217 VAL B CG2 1 
ATOM   4004 N  N   . LYS B 1 239 ? 65.578  12.015  -22.028 1.00 64.20  ? 218 LYS B N   1 
ATOM   4005 C  CA  . LYS B 1 239 ? 65.600  13.443  -21.736 1.00 67.99  ? 218 LYS B CA  1 
ATOM   4006 C  C   . LYS B 1 239 ? 66.075  13.716  -20.315 1.00 67.58  ? 218 LYS B C   1 
ATOM   4007 O  O   . LYS B 1 239 ? 66.786  14.697  -20.068 1.00 70.71  ? 218 LYS B O   1 
ATOM   4008 C  CB  . LYS B 1 239 ? 64.207  14.027  -21.963 1.00 67.17  ? 218 LYS B CB  1 
ATOM   4009 C  CG  . LYS B 1 239 ? 64.155  15.543  -21.992 1.00 69.85  ? 218 LYS B CG  1 
ATOM   4010 C  CD  . LYS B 1 239 ? 62.733  16.046  -22.231 1.00 68.54  ? 218 LYS B CD  1 
ATOM   4011 C  CE  . LYS B 1 239 ? 62.182  15.614  -23.589 1.00 58.53  ? 218 LYS B CE  1 
ATOM   4012 N  NZ  . LYS B 1 239 ? 61.910  16.777  -24.477 1.00 62.39  ? 218 LYS B NZ  1 
ATOM   4013 N  N   . LYS B 1 240 ? 65.689  12.865  -19.364 1.00 60.19  ? 219 LYS B N   1 
ATOM   4014 C  CA  . LYS B 1 240 ? 66.102  13.062  -17.981 1.00 73.05  ? 219 LYS B CA  1 
ATOM   4015 C  C   . LYS B 1 240 ? 67.552  12.659  -17.754 1.00 69.27  ? 219 LYS B C   1 
ATOM   4016 O  O   . LYS B 1 240 ? 68.240  13.274  -16.931 1.00 66.41  ? 219 LYS B O   1 
ATOM   4017 C  CB  . LYS B 1 240 ? 65.183  12.277  -17.048 1.00 70.26  ? 219 LYS B CB  1 
ATOM   4018 C  CG  . LYS B 1 240 ? 63.775  12.834  -16.991 1.00 68.99  ? 219 LYS B CG  1 
ATOM   4019 C  CD  . LYS B 1 240 ? 62.910  12.082  -16.002 1.00 58.82  ? 219 LYS B CD  1 
ATOM   4020 C  CE  . LYS B 1 240 ? 61.587  12.794  -15.788 1.00 70.76  ? 219 LYS B CE  1 
ATOM   4021 N  NZ  . LYS B 1 240 ? 61.129  12.669  -14.383 1.00 61.84  ? 219 LYS B NZ  1 
ATOM   4022 N  N   . ILE B 1 241 ? 68.027  11.629  -18.456 1.00 68.40  ? 220 ILE B N   1 
ATOM   4023 C  CA  . ILE B 1 241 ? 69.422  11.223  -18.330 1.00 60.80  ? 220 ILE B CA  1 
ATOM   4024 C  C   . ILE B 1 241 ? 70.335  12.248  -18.991 1.00 63.57  ? 220 ILE B C   1 
ATOM   4025 O  O   . ILE B 1 241 ? 71.386  12.608  -18.448 1.00 65.51  ? 220 ILE B O   1 
ATOM   4026 C  CB  . ILE B 1 241 ? 69.617  9.815   -18.922 1.00 62.46  ? 220 ILE B CB  1 
ATOM   4027 C  CG1 . ILE B 1 241 ? 68.798  8.780   -18.139 1.00 60.59  ? 220 ILE B CG1 1 
ATOM   4028 C  CG2 . ILE B 1 241 ? 71.093  9.439   -18.935 1.00 57.29  ? 220 ILE B CG2 1 
ATOM   4029 C  CD1 . ILE B 1 241 ? 69.169  8.663   -16.673 1.00 57.15  ? 220 ILE B CD1 1 
ATOM   4030 N  N   . LYS B 1 242 ? 69.951  12.732  -20.176 1.00 65.19  ? 221 LYS B N   1 
ATOM   4031 C  CA  . LYS B 1 242 ? 70.742  13.760  -20.844 1.00 68.19  ? 221 LYS B CA  1 
ATOM   4032 C  C   . LYS B 1 242 ? 70.854  15.011  -19.983 1.00 69.72  ? 221 LYS B C   1 
ATOM   4033 O  O   . LYS B 1 242 ? 71.892  15.684  -19.992 1.00 67.72  ? 221 LYS B O   1 
ATOM   4034 C  CB  . LYS B 1 242 ? 70.117  14.101  -22.200 1.00 73.13  ? 221 LYS B CB  1 
ATOM   4035 N  N   . ARG B 1 243 ? 69.806  15.332  -19.232 1.00 70.90  ? 222 ARG B N   1 
ATOM   4036 C  CA  . ARG B 1 243 ? 69.770  16.531  -18.407 1.00 71.38  ? 222 ARG B CA  1 
ATOM   4037 C  C   . ARG B 1 243 ? 70.320  16.317  -17.001 1.00 71.90  ? 222 ARG B C   1 
ATOM   4038 O  O   . ARG B 1 243 ? 70.298  17.255  -16.198 1.00 73.69  ? 222 ARG B O   1 
ATOM   4039 C  CB  . ARG B 1 243 ? 68.331  17.052  -18.312 1.00 75.13  ? 222 ARG B CB  1 
ATOM   4040 N  N   . ALA B 1 244 ? 70.810  15.122  -16.681 1.00 78.14  ? 223 ALA B N   1 
ATOM   4041 C  CA  . ALA B 1 244 ? 71.286  14.850  -15.330 1.00 81.61  ? 223 ALA B CA  1 
ATOM   4042 C  C   . ALA B 1 244 ? 72.496  15.716  -15.000 1.00 72.35  ? 223 ALA B C   1 
ATOM   4043 O  O   . ALA B 1 244 ? 73.372  15.930  -15.837 1.00 82.36  ? 223 ALA B O   1 
ATOM   4044 C  CB  . ALA B 1 244 ? 71.644  13.370  -15.191 1.00 69.82  ? 223 ALA B CB  1 
ATOM   4045 N  N   . VAL B 1 245 ? 72.548  16.220  -13.765 1.00 74.26  ? 224 VAL B N   1 
ATOM   4046 C  CA  . VAL B 1 245 ? 73.670  17.063  -13.375 1.00 87.61  ? 224 VAL B CA  1 
ATOM   4047 C  C   . VAL B 1 245 ? 74.973  16.275  -13.497 1.00 92.06  ? 224 VAL B C   1 
ATOM   4048 O  O   . VAL B 1 245 ? 75.011  15.053  -13.300 1.00 89.46  ? 224 VAL B O   1 
ATOM   4049 C  CB  . VAL B 1 245 ? 73.489  17.601  -11.946 1.00 78.46  ? 224 VAL B CB  1 
ATOM   4050 N  N   . THR B 1 246 ? 76.049  16.983  -13.843 1.00 89.85  ? 225 THR B N   1 
ATOM   4051 C  CA  . THR B 1 246 ? 77.372  16.382  -13.952 1.00 93.16  ? 225 THR B CA  1 
ATOM   4052 C  C   . THR B 1 246 ? 78.417  17.435  -13.599 1.00 91.18  ? 225 THR B C   1 
ATOM   4053 O  O   . THR B 1 246 ? 78.118  18.628  -13.503 1.00 91.41  ? 225 THR B O   1 
ATOM   4054 C  CB  . THR B 1 246 ? 77.623  15.812  -15.355 1.00 94.52  ? 225 THR B CB  1 
ATOM   4055 O  OG1 . THR B 1 246 ? 78.760  14.940  -15.323 1.00 97.23  ? 225 THR B OG1 1 
ATOM   4056 C  CG2 . THR B 1 246 ? 77.877  16.928  -16.362 1.00 91.73  ? 225 THR B CG2 1 
ATOM   4057 N  N   . ASP B 1 247 ? 79.653  16.979  -13.406 1.00 90.51  ? 226 ASP B N   1 
ATOM   4058 C  CA  . ASP B 1 247 ? 80.757  17.838  -12.991 1.00 98.49  ? 226 ASP B CA  1 
ATOM   4059 C  C   . ASP B 1 247 ? 81.617  18.196  -14.195 1.00 108.67 ? 226 ASP B C   1 
ATOM   4060 O  O   . ASP B 1 247 ? 82.002  17.316  -14.971 1.00 100.70 ? 226 ASP B O   1 
ATOM   4061 C  CB  . ASP B 1 247 ? 81.608  17.148  -11.923 1.00 102.39 ? 226 ASP B CB  1 
ATOM   4062 N  N   . SER B 1 248 ? 81.929  19.484  -14.338 1.00 93.95  ? 227 SER B N   1 
ATOM   4063 C  CA  . SER B 1 248 ? 82.670  19.982  -15.498 1.00 99.29  ? 227 SER B CA  1 
ATOM   4064 C  C   . SER B 1 248 ? 84.179  19.932  -15.245 1.00 96.52  ? 227 SER B C   1 
ATOM   4065 O  O   . SER B 1 248 ? 84.875  20.946  -15.201 1.00 95.00  ? 227 SER B O   1 
ATOM   4066 C  CB  . SER B 1 248 ? 82.216  21.397  -15.844 1.00 96.55  ? 227 SER B CB  1 
ATOM   4067 O  OG  . SER B 1 248 ? 82.437  22.287  -14.763 1.00 95.01  ? 227 SER B OG  1 
ATOM   4068 N  N   . ASP B 1 249 ? 84.682  18.711  -15.084 1.00 108.12 ? 228 ASP B N   1 
ATOM   4069 C  CA  . ASP B 1 249 ? 86.117  18.492  -14.980 1.00 114.40 ? 228 ASP B CA  1 
ATOM   4070 C  C   . ASP B 1 249 ? 86.750  18.528  -16.366 1.00 108.17 ? 228 ASP B C   1 
ATOM   4071 O  O   . ASP B 1 249 ? 86.166  18.051  -17.343 1.00 106.84 ? 228 ASP B O   1 
ATOM   4072 C  CB  . ASP B 1 249 ? 86.407  17.153  -14.304 1.00 92.88  ? 228 ASP B CB  1 
ATOM   4073 N  N   . GLU B 1 250 ? 87.947  19.103  -16.447 1.00 109.56 ? 229 GLU B N   1 
ATOM   4074 C  CA  . GLU B 1 250 ? 88.665  19.250  -17.709 1.00 112.28 ? 229 GLU B CA  1 
ATOM   4075 C  C   . GLU B 1 250 ? 89.951  18.436  -17.670 1.00 112.57 ? 229 GLU B C   1 
ATOM   4076 O  O   . GLU B 1 250 ? 90.842  18.741  -16.859 1.00 114.81 ? 229 GLU B O   1 
ATOM   4077 C  CB  . GLU B 1 250 ? 88.978  20.724  -17.983 1.00 106.74 ? 229 GLU B CB  1 
ATOM   4078 C  CG  . GLU B 1 250 ? 87.774  21.562  -18.394 1.00 107.08 ? 229 GLU B CG  1 
ATOM   4079 C  CD  . GLU B 1 250 ? 87.316  21.281  -19.815 1.00 109.10 ? 229 GLU B CD  1 
ATOM   4080 O  OE1 . GLU B 1 250 ? 86.899  20.138  -20.097 1.00 109.21 ? 229 GLU B OE1 1 
ATOM   4081 O  OE2 . GLU B 1 250 ? 87.381  22.205  -20.653 1.00 96.56  ? 229 GLU B OE2 1 
ATOM   4082 N  N   . PRO B 1 251 ? 90.109  17.400  -18.509 1.00 115.19 ? 230 PRO B N   1 
ATOM   4083 C  CA  . PRO B 1 251 ? 89.142  16.856  -19.478 1.00 132.87 ? 230 PRO B CA  1 
ATOM   4084 C  C   . PRO B 1 251 ? 88.054  16.042  -18.784 1.00 129.90 ? 230 PRO B C   1 
ATOM   4085 O  O   . PRO B 1 251 ? 88.305  15.468  -17.728 1.00 97.60  ? 230 PRO B O   1 
ATOM   4086 C  CB  . PRO B 1 251 ? 90.021  15.991  -20.390 1.00 110.35 ? 230 PRO B CB  1 
ATOM   4087 C  CG  . PRO B 1 251 ? 91.131  15.527  -19.496 1.00 92.89  ? 230 PRO B CG  1 
ATOM   4088 C  CD  . PRO B 1 251 ? 91.400  16.688  -18.570 1.00 98.01  ? 230 PRO B CD  1 
ATOM   4089 N  N   . PRO B 1 252 ? 86.839  15.969  -19.331 1.00 114.94 ? 231 PRO B N   1 
ATOM   4090 C  CA  . PRO B 1 252 ? 85.794  15.148  -18.698 1.00 110.55 ? 231 PRO B CA  1 
ATOM   4091 C  C   . PRO B 1 252 ? 86.164  13.673  -18.749 1.00 114.64 ? 231 PRO B C   1 
ATOM   4092 O  O   . PRO B 1 252 ? 86.372  13.109  -19.826 1.00 117.05 ? 231 PRO B O   1 
ATOM   4093 C  CB  . PRO B 1 252 ? 84.543  15.451  -19.532 1.00 108.81 ? 231 PRO B CB  1 
ATOM   4094 C  CG  . PRO B 1 252 ? 84.841  16.733  -20.238 1.00 116.21 ? 231 PRO B CG  1 
ATOM   4095 C  CD  . PRO B 1 252 ? 86.318  16.733  -20.478 1.00 115.56 ? 231 PRO B CD  1 
ATOM   4096 N  N   . VAL B 1 253 ? 86.248  13.049  -17.574 1.00 102.09 ? 232 VAL B N   1 
ATOM   4097 C  CA  . VAL B 1 253 ? 86.574  11.637  -17.452 1.00 99.63  ? 232 VAL B CA  1 
ATOM   4098 C  C   . VAL B 1 253 ? 85.538  10.974  -16.555 1.00 93.32  ? 232 VAL B C   1 
ATOM   4099 O  O   . VAL B 1 253 ? 84.868  11.625  -15.750 1.00 96.94  ? 232 VAL B O   1 
ATOM   4100 C  CB  . VAL B 1 253 ? 87.995  11.410  -16.891 1.00 96.60  ? 232 VAL B CB  1 
ATOM   4101 N  N   . VAL B 1 254 ? 85.421  9.659   -16.697 1.00 105.59 ? 233 VAL B N   1 
ATOM   4102 C  CA  . VAL B 1 254 ? 84.428  8.873   -15.974 1.00 92.42  ? 233 VAL B CA  1 
ATOM   4103 C  C   . VAL B 1 254 ? 85.120  8.253   -14.767 1.00 105.88 ? 233 VAL B C   1 
ATOM   4104 O  O   . VAL B 1 254 ? 85.997  7.394   -14.913 1.00 91.05  ? 233 VAL B O   1 
ATOM   4105 C  CB  . VAL B 1 254 ? 83.795  7.802   -16.872 1.00 98.11  ? 233 VAL B CB  1 
ATOM   4106 C  CG1 . VAL B 1 254 ? 82.572  7.200   -16.198 1.00 98.98  ? 233 VAL B CG1 1 
ATOM   4107 C  CG2 . VAL B 1 254 ? 83.427  8.391   -18.227 1.00 90.93  ? 233 VAL B CG2 1 
ATOM   4108 N  N   . ARG B 1 255 ? 84.722  8.684   -13.571 1.00 91.81  ? 234 ARG B N   1 
ATOM   4109 C  CA  . ARG B 1 255 ? 85.312  8.194   -12.334 1.00 96.22  ? 234 ARG B CA  1 
ATOM   4110 C  C   . ARG B 1 255 ? 84.297  8.342   -11.209 1.00 96.34  ? 234 ARG B C   1 
ATOM   4111 O  O   . ARG B 1 255 ? 83.593  9.352   -11.130 1.00 93.23  ? 234 ARG B O   1 
ATOM   4112 C  CB  . ARG B 1 255 ? 86.598  8.956   -11.990 1.00 92.27  ? 234 ARG B CB  1 
ATOM   4113 N  N   . TYR B 1 256 ? 84.231  7.331   -10.344 1.00 96.37  ? 235 TYR B N   1 
ATOM   4114 C  CA  . TYR B 1 256 ? 83.300  7.344   -9.223  1.00 101.11 ? 235 TYR B CA  1 
ATOM   4115 C  C   . TYR B 1 256 ? 83.863  8.205   -8.098  1.00 103.59 ? 235 TYR B C   1 
ATOM   4116 O  O   . TYR B 1 256 ? 84.989  7.986   -7.642  1.00 103.31 ? 235 TYR B O   1 
ATOM   4117 C  CB  . TYR B 1 256 ? 83.041  5.919   -8.731  1.00 103.91 ? 235 TYR B CB  1 
ATOM   4118 N  N   . ASP B 1 257 ? 83.078  9.185   -7.657  1.00 101.18 ? 236 ASP B N   1 
ATOM   4119 C  CA  . ASP B 1 257 ? 83.493  10.082  -6.585  1.00 99.49  ? 236 ASP B CA  1 
ATOM   4120 C  C   . ASP B 1 257 ? 82.286  10.816  -6.010  1.00 103.31 ? 236 ASP B C   1 
ATOM   4121 O  O   . ASP B 1 257 ? 81.904  11.878  -6.501  1.00 107.29 ? 236 ASP B O   1 
ATOM   4122 C  CB  . ASP B 1 257 ? 84.528  11.085  -7.096  1.00 105.21 ? 236 ASP B CB  1 
ATOM   4123 C  CG  . ASP B 1 257 ? 85.092  11.955  -5.990  1.00 109.25 ? 236 ASP B CG  1 
ATOM   4124 O  OD1 . ASP B 1 257 ? 84.584  11.886  -4.851  1.00 108.08 ? 236 ASP B OD1 1 
ATOM   4125 O  OD2 . ASP B 1 257 ? 86.053  12.706  -6.261  1.00 104.53 ? 236 ASP B OD2 1 
ATOM   4126 N  N   . ALA B 1 262 ? 79.525  13.859  -8.283  1.00 90.10  ? 241 ALA B N   1 
ATOM   4127 C  CA  . ALA B 1 262 ? 78.320  13.201  -7.794  1.00 89.90  ? 241 ALA B CA  1 
ATOM   4128 C  C   . ALA B 1 262 ? 77.354  12.956  -8.937  1.00 81.66  ? 241 ALA B C   1 
ATOM   4129 O  O   . ALA B 1 262 ? 76.497  12.076  -8.861  1.00 88.12  ? 241 ALA B O   1 
ATOM   4130 C  CB  . ALA B 1 262 ? 77.659  14.032  -6.716  1.00 92.94  ? 241 ALA B CB  1 
ATOM   4131 N  N   . GLY B 1 263 ? 77.493  13.739  -10.000 1.00 88.60  ? 242 GLY B N   1 
ATOM   4132 C  CA  . GLY B 1 263 ? 76.668  13.530  -11.168 1.00 83.74  ? 242 GLY B CA  1 
ATOM   4133 C  C   . GLY B 1 263 ? 77.141  12.288  -11.891 1.00 80.18  ? 242 GLY B C   1 
ATOM   4134 O  O   . GLY B 1 263 ? 76.420  11.292  -11.962 1.00 77.14  ? 242 GLY B O   1 
ATOM   4135 N  N   . VAL B 1 264 ? 78.394  12.304  -12.351 1.00 90.74  ? 243 VAL B N   1 
ATOM   4136 C  CA  . VAL B 1 264 ? 78.929  11.167  -13.098 1.00 79.10  ? 243 VAL B CA  1 
ATOM   4137 C  C   . VAL B 1 264 ? 78.797  9.890   -12.283 1.00 84.83  ? 243 VAL B C   1 
ATOM   4138 O  O   . VAL B 1 264 ? 78.533  8.810   -12.827 1.00 85.09  ? 243 VAL B O   1 
ATOM   4139 C  CB  . VAL B 1 264 ? 80.395  11.431  -13.493 1.00 80.41  ? 243 VAL B CB  1 
ATOM   4140 C  CG1 . VAL B 1 264 ? 81.022  10.183  -14.104 1.00 98.86  ? 243 VAL B CG1 1 
ATOM   4141 C  CG2 . VAL B 1 264 ? 80.483  12.602  -14.454 1.00 91.52  ? 243 VAL B CG2 1 
ATOM   4142 N  N   . SER B 1 265 ? 78.975  9.994   -10.965 1.00 83.32  ? 244 SER B N   1 
ATOM   4143 C  CA  . SER B 1 265 ? 78.883  8.822   -10.102 1.00 81.58  ? 244 SER B CA  1 
ATOM   4144 C  C   . SER B 1 265 ? 77.488  8.210   -10.137 1.00 76.41  ? 244 SER B C   1 
ATOM   4145 O  O   . SER B 1 265 ? 77.343  6.982   -10.153 1.00 75.63  ? 244 SER B O   1 
ATOM   4146 C  CB  . SER B 1 265 ? 79.259  9.207   -8.673  1.00 90.90  ? 244 SER B CB  1 
ATOM   4147 O  OG  . SER B 1 265 ? 80.380  10.073  -8.664  1.00 91.80  ? 244 SER B OG  1 
ATOM   4148 N  N   . ASN B 1 266 ? 76.449  9.051   -10.141 1.00 80.36  ? 245 ASN B N   1 
ATOM   4149 C  CA  . ASN B 1 266 ? 75.084  8.536   -10.165 1.00 81.39  ? 245 ASN B CA  1 
ATOM   4150 C  C   . ASN B 1 266 ? 74.860  7.659   -11.388 1.00 71.91  ? 245 ASN B C   1 
ATOM   4151 O  O   . ASN B 1 266 ? 74.200  6.618   -11.304 1.00 69.26  ? 245 ASN B O   1 
ATOM   4152 C  CB  . ASN B 1 266 ? 74.082  9.694   -10.151 1.00 80.24  ? 245 ASN B CB  1 
ATOM   4153 N  N   . LEU B 1 267 ? 75.410  8.066   -12.535 1.00 76.65  ? 246 LEU B N   1 
ATOM   4154 C  CA  . LEU B 1 267 ? 75.156  7.348   -13.778 1.00 69.17  ? 246 LEU B CA  1 
ATOM   4155 C  C   . LEU B 1 267 ? 75.909  6.030   -13.797 1.00 67.15  ? 246 LEU B C   1 
ATOM   4156 O  O   . LEU B 1 267 ? 75.463  5.065   -14.426 1.00 68.25  ? 246 LEU B O   1 
ATOM   4157 C  CB  . LEU B 1 267 ? 75.546  8.215   -14.984 1.00 69.67  ? 246 LEU B CB  1 
ATOM   4158 C  CG  . LEU B 1 267 ? 74.722  9.467   -15.310 1.00 71.21  ? 246 LEU B CG  1 
ATOM   4159 C  CD1 . LEU B 1 267 ? 74.863  10.510  -14.262 1.00 82.07  ? 246 LEU B CD1 1 
ATOM   4160 C  CD2 . LEU B 1 267 ? 75.181  10.106  -16.595 1.00 68.58  ? 246 LEU B CD2 1 
ATOM   4161 N  N   . LEU B 1 268 ? 77.047  5.976   -13.103 1.00 76.97  ? 247 LEU B N   1 
ATOM   4162 C  CA  . LEU B 1 268 ? 77.785  4.728   -12.968 1.00 74.76  ? 247 LEU B CA  1 
ATOM   4163 C  C   . LEU B 1 268 ? 77.050  3.751   -12.059 1.00 74.68  ? 247 LEU B C   1 
ATOM   4164 O  O   . LEU B 1 268 ? 77.046  2.542   -12.317 1.00 68.15  ? 247 LEU B O   1 
ATOM   4165 C  CB  . LEU B 1 268 ? 79.188  5.017   -12.437 1.00 93.13  ? 247 LEU B CB  1 
ATOM   4166 C  CG  . LEU B 1 268 ? 80.131  5.706   -13.425 1.00 92.90  ? 247 LEU B CG  1 
ATOM   4167 C  CD1 . LEU B 1 268 ? 81.441  6.074   -12.745 1.00 94.72  ? 247 LEU B CD1 1 
ATOM   4168 C  CD2 . LEU B 1 268 ? 80.384  4.808   -14.627 1.00 86.14  ? 247 LEU B CD2 1 
ATOM   4169 N  N   . ASP B 1 269 ? 76.429  4.253   -10.987 1.00 86.29  ? 248 ASP B N   1 
ATOM   4170 C  CA  . ASP B 1 269 ? 75.646  3.385   -10.113 1.00 83.70  ? 248 ASP B CA  1 
ATOM   4171 C  C   . ASP B 1 269 ? 74.434  2.821   -10.846 1.00 78.84  ? 248 ASP B C   1 
ATOM   4172 O  O   . ASP B 1 269 ? 74.125  1.630   -10.728 1.00 78.91  ? 248 ASP B O   1 
ATOM   4173 C  CB  . ASP B 1 269 ? 75.197  4.150   -8.865  1.00 85.73  ? 248 ASP B CB  1 
ATOM   4174 C  CG  . ASP B 1 269 ? 76.331  4.909   -8.193  1.00 92.23  ? 248 ASP B CG  1 
ATOM   4175 O  OD1 . ASP B 1 269 ? 77.504  4.702   -8.568  1.00 93.01  ? 248 ASP B OD1 1 
ATOM   4176 O  OD2 . ASP B 1 269 ? 76.044  5.721   -7.287  1.00 95.17  ? 248 ASP B OD2 1 
ATOM   4177 N  N   . ILE B 1 270 ? 73.740  3.666   -11.610 1.00 71.50  ? 249 ILE B N   1 
ATOM   4178 C  CA  . ILE B 1 270 ? 72.522  3.238   -12.292 1.00 72.60  ? 249 ILE B CA  1 
ATOM   4179 C  C   . ILE B 1 270 ? 72.851  2.239   -13.395 1.00 67.83  ? 249 ILE B C   1 
ATOM   4180 O  O   . ILE B 1 270 ? 72.205  1.192   -13.521 1.00 59.61  ? 249 ILE B O   1 
ATOM   4181 C  CB  . ILE B 1 270 ? 71.769  4.466   -12.836 1.00 65.37  ? 249 ILE B CB  1 
ATOM   4182 C  CG1 . ILE B 1 270 ? 71.112  5.228   -11.682 1.00 69.61  ? 249 ILE B CG1 1 
ATOM   4183 C  CG2 . ILE B 1 270 ? 70.737  4.053   -13.868 1.00 59.64  ? 249 ILE B CG2 1 
ATOM   4184 C  CD1 . ILE B 1 270 ? 71.065  6.729   -11.876 1.00 74.60  ? 249 ILE B CD1 1 
ATOM   4185 N  N   . LEU B 1 271 ? 73.863  2.547   -14.210 1.00 70.96  ? 250 LEU B N   1 
ATOM   4186 C  CA  . LEU B 1 271 ? 74.228  1.654   -15.305 1.00 63.15  ? 250 LEU B CA  1 
ATOM   4187 C  C   . LEU B 1 271 ? 74.714  0.309   -14.782 1.00 67.55  ? 250 LEU B C   1 
ATOM   4188 O  O   . LEU B 1 271 ? 74.354  -0.742  -15.324 1.00 57.87  ? 250 LEU B O   1 
ATOM   4189 C  CB  . LEU B 1 271 ? 75.300  2.307   -16.176 1.00 71.01  ? 250 LEU B CB  1 
ATOM   4190 C  CG  . LEU B 1 271 ? 75.771  1.521   -17.402 1.00 68.96  ? 250 LEU B CG  1 
ATOM   4191 C  CD1 . LEU B 1 271 ? 74.596  1.058   -18.249 1.00 53.87  ? 250 LEU B CD1 1 
ATOM   4192 C  CD2 . LEU B 1 271 ? 76.723  2.372   -18.232 1.00 72.31  ? 250 LEU B CD2 1 
ATOM   4193 N  N   . SER B 1 272 ? 75.534  0.323   -13.729 1.00 66.20  ? 251 SER B N   1 
ATOM   4194 C  CA  . SER B 1 272 ? 76.041  -0.928  -13.177 1.00 70.59  ? 251 SER B CA  1 
ATOM   4195 C  C   . SER B 1 272 ? 74.903  -1.803  -12.666 1.00 70.72  ? 251 SER B C   1 
ATOM   4196 O  O   . SER B 1 272 ? 74.904  -3.021  -12.877 1.00 73.33  ? 251 SER B O   1 
ATOM   4197 C  CB  . SER B 1 272 ? 77.042  -0.641  -12.058 1.00 74.29  ? 251 SER B CB  1 
ATOM   4198 O  OG  . SER B 1 272 ? 76.413  -0.002  -10.961 1.00 80.48  ? 251 SER B OG  1 
ATOM   4199 N  N   . ALA B 1 273 ? 73.920  -1.200  -11.994 1.00 59.20  ? 252 ALA B N   1 
ATOM   4200 C  CA  . ALA B 1 273 ? 72.801  -1.979  -11.473 1.00 65.91  ? 252 ALA B CA  1 
ATOM   4201 C  C   . ALA B 1 273 ? 72.033  -2.660  -12.598 1.00 64.76  ? 252 ALA B C   1 
ATOM   4202 O  O   . ALA B 1 273 ? 71.634  -3.824  -12.473 1.00 62.54  ? 252 ALA B O   1 
ATOM   4203 C  CB  . ALA B 1 273 ? 71.870  -1.080  -10.660 1.00 54.02  ? 252 ALA B CB  1 
ATOM   4204 N  N   . VAL B 1 274 ? 71.813  -1.950  -13.705 1.00 64.85  ? 253 VAL B N   1 
ATOM   4205 C  CA  . VAL B 1 274 ? 71.044  -2.513  -14.809 1.00 59.07  ? 253 VAL B CA  1 
ATOM   4206 C  C   . VAL B 1 274 ? 71.796  -3.672  -15.453 1.00 61.72  ? 253 VAL B C   1 
ATOM   4207 O  O   . VAL B 1 274 ? 71.234  -4.750  -15.676 1.00 60.59  ? 253 VAL B O   1 
ATOM   4208 C  CB  . VAL B 1 274 ? 70.714  -1.419  -15.841 1.00 60.46  ? 253 VAL B CB  1 
ATOM   4209 C  CG1 . VAL B 1 274 ? 70.004  -2.020  -17.047 1.00 51.77  ? 253 VAL B CG1 1 
ATOM   4210 C  CG2 . VAL B 1 274 ? 69.869  -0.322  -15.205 1.00 59.39  ? 253 VAL B CG2 1 
ATOM   4211 N  N   . THR B 1 275 ? 73.076  -3.470  -15.758 1.00 65.08  ? 254 THR B N   1 
ATOM   4212 C  CA  . THR B 1 275 ? 73.844  -4.434  -16.533 1.00 66.39  ? 254 THR B CA  1 
ATOM   4213 C  C   . THR B 1 275 ? 74.561  -5.468  -15.677 1.00 68.73  ? 254 THR B C   1 
ATOM   4214 O  O   . THR B 1 275 ? 75.121  -6.422  -16.228 1.00 66.92  ? 254 THR B O   1 
ATOM   4215 C  CB  . THR B 1 275 ? 74.878  -3.705  -17.399 1.00 66.39  ? 254 THR B CB  1 
ATOM   4216 O  OG1 . THR B 1 275 ? 75.840  -3.059  -16.555 1.00 65.40  ? 254 THR B OG1 1 
ATOM   4217 C  CG2 . THR B 1 275 ? 74.201  -2.663  -18.286 1.00 61.30  ? 254 THR B CG2 1 
ATOM   4218 N  N   . GLY B 1 276 ? 74.554  -5.312  -14.356 1.00 62.77  ? 255 GLY B N   1 
ATOM   4219 C  CA  . GLY B 1 276 ? 75.298  -6.220  -13.502 1.00 73.81  ? 255 GLY B CA  1 
ATOM   4220 C  C   . GLY B 1 276 ? 76.792  -6.186  -13.729 1.00 72.43  ? 255 GLY B C   1 
ATOM   4221 O  O   . GLY B 1 276 ? 77.480  -7.173  -13.445 1.00 77.89  ? 255 GLY B O   1 
ATOM   4222 N  N   . GLN B 1 277 ? 77.317  -5.071  -14.229 1.00 70.32  ? 256 GLN B N   1 
ATOM   4223 C  CA  . GLN B 1 277 ? 78.737  -4.924  -14.504 1.00 70.38  ? 256 GLN B CA  1 
ATOM   4224 C  C   . GLN B 1 277 ? 79.414  -4.139  -13.389 1.00 76.08  ? 256 GLN B C   1 
ATOM   4225 O  O   . GLN B 1 277 ? 78.783  -3.339  -12.694 1.00 71.57  ? 256 GLN B O   1 
ATOM   4226 C  CB  . GLN B 1 277 ? 78.964  -4.210  -15.839 1.00 70.51  ? 256 GLN B CB  1 
ATOM   4227 C  CG  . GLN B 1 277 ? 78.348  -4.913  -17.035 1.00 73.45  ? 256 GLN B CG  1 
ATOM   4228 C  CD  . GLN B 1 277 ? 78.490  -4.114  -18.319 1.00 78.14  ? 256 GLN B CD  1 
ATOM   4229 O  OE1 . GLN B 1 277 ? 78.478  -2.883  -18.304 1.00 82.79  ? 256 GLN B OE1 1 
ATOM   4230 N  NE2 . GLN B 1 277 ? 78.626  -4.815  -19.439 1.00 82.98  ? 256 GLN B NE2 1 
ATOM   4231 N  N   . SER B 1 278 ? 80.712  -4.379  -13.225 1.00 88.01  ? 257 SER B N   1 
ATOM   4232 C  CA  . SER B 1 278 ? 81.495  -3.623  -12.260 1.00 96.38  ? 257 SER B CA  1 
ATOM   4233 C  C   . SER B 1 278 ? 81.690  -2.193  -12.748 1.00 106.59 ? 257 SER B C   1 
ATOM   4234 O  O   . SER B 1 278 ? 81.767  -1.928  -13.950 1.00 109.00 ? 257 SER B O   1 
ATOM   4235 C  CB  . SER B 1 278 ? 82.853  -4.286  -12.033 1.00 86.64  ? 257 SER B CB  1 
ATOM   4236 O  OG  . SER B 1 278 ? 83.627  -4.284  -13.220 1.00 84.42  ? 257 SER B OG  1 
ATOM   4237 N  N   . ILE B 1 279 ? 81.762  -1.261  -11.796 1.00 92.45  ? 258 ILE B N   1 
ATOM   4238 C  CA  . ILE B 1 279 ? 82.020  0.131   -12.157 1.00 91.19  ? 258 ILE B CA  1 
ATOM   4239 C  C   . ILE B 1 279 ? 83.325  0.270   -12.927 1.00 93.82  ? 258 ILE B C   1 
ATOM   4240 O  O   . ILE B 1 279 ? 83.321  0.900   -13.997 1.00 97.64  ? 258 ILE B O   1 
ATOM   4241 C  CB  . ILE B 1 279 ? 81.985  1.018   -10.892 1.00 93.77  ? 258 ILE B CB  1 
ATOM   4242 N  N   . PRO B 1 280 ? 84.453  -0.284  -12.473 1.00 108.33 ? 259 PRO B N   1 
ATOM   4243 C  CA  . PRO B 1 280 ? 85.694  -0.144  -13.254 1.00 108.35 ? 259 PRO B CA  1 
ATOM   4244 C  C   . PRO B 1 280 ? 85.627  -0.777  -14.633 1.00 106.09 ? 259 PRO B C   1 
ATOM   4245 O  O   . PRO B 1 280 ? 86.142  -0.197  -15.596 1.00 107.91 ? 259 PRO B O   1 
ATOM   4246 C  CB  . PRO B 1 280 ? 86.744  -0.832  -12.369 1.00 107.73 ? 259 PRO B CB  1 
ATOM   4247 C  CG  . PRO B 1 280 ? 86.178  -0.814  -11.001 1.00 109.87 ? 259 PRO B CG  1 
ATOM   4248 C  CD  . PRO B 1 280 ? 84.690  -0.911  -11.163 1.00 111.20 ? 259 PRO B CD  1 
ATOM   4249 N  N   . GLU B 1 281 ? 85.018  -1.961  -14.758 1.00 95.02  ? 260 GLU B N   1 
ATOM   4250 C  CA  . GLU B 1 281 ? 84.862  -2.564  -16.077 1.00 91.10  ? 260 GLU B CA  1 
ATOM   4251 C  C   . GLU B 1 281 ? 84.020  -1.680  -16.986 1.00 95.00  ? 260 GLU B C   1 
ATOM   4252 O  O   . GLU B 1 281 ? 84.193  -1.700  -18.210 1.00 91.16  ? 260 GLU B O   1 
ATOM   4253 C  CB  . GLU B 1 281 ? 84.235  -3.952  -15.956 1.00 86.94  ? 260 GLU B CB  1 
ATOM   4254 N  N   . LEU B 1 282 ? 83.101  -0.905  -16.405 1.00 99.53  ? 261 LEU B N   1 
ATOM   4255 C  CA  . LEU B 1 282 ? 82.353  0.074   -17.186 1.00 103.10 ? 261 LEU B CA  1 
ATOM   4256 C  C   . LEU B 1 282 ? 83.249  1.225   -17.627 1.00 97.14  ? 261 LEU B C   1 
ATOM   4257 O  O   . LEU B 1 282 ? 83.174  1.671   -18.778 1.00 97.95  ? 261 LEU B O   1 
ATOM   4258 C  CB  . LEU B 1 282 ? 81.168  0.593   -16.370 1.00 97.29  ? 261 LEU B CB  1 
ATOM   4259 C  CG  . LEU B 1 282 ? 79.906  -0.269  -16.407 1.00 100.71 ? 261 LEU B CG  1 
ATOM   4260 C  CD1 . LEU B 1 282 ? 79.011  0.030   -15.216 1.00 108.38 ? 261 LEU B CD1 1 
ATOM   4261 C  CD2 . LEU B 1 282 ? 79.158  -0.039  -17.709 1.00 89.44  ? 261 LEU B CD2 1 
ATOM   4262 N  N   . GLU B 1 283 ? 84.110  1.713   -16.729 1.00 100.89 ? 262 GLU B N   1 
ATOM   4263 C  CA  . GLU B 1 283 ? 85.009  2.804   -17.091 1.00 97.07  ? 262 GLU B CA  1 
ATOM   4264 C  C   . GLU B 1 283 ? 85.964  2.383   -18.198 1.00 90.11  ? 262 GLU B C   1 
ATOM   4265 O  O   . GLU B 1 283 ? 86.355  3.210   -19.029 1.00 96.61  ? 262 GLU B O   1 
ATOM   4266 C  CB  . GLU B 1 283 ? 85.790  3.277   -15.865 1.00 97.01  ? 262 GLU B CB  1 
ATOM   4267 C  CG  . GLU B 1 283 ? 84.940  3.426   -14.615 1.00 98.61  ? 262 GLU B CG  1 
ATOM   4268 C  CD  . GLU B 1 283 ? 85.529  4.396   -13.612 1.00 98.31  ? 262 GLU B CD  1 
ATOM   4269 O  OE1 . GLU B 1 283 ? 86.770  4.437   -13.475 1.00 94.04  ? 262 GLU B OE1 1 
ATOM   4270 O  OE2 . GLU B 1 283 ? 84.746  5.120   -12.962 1.00 99.28  ? 262 GLU B OE2 1 
ATOM   4271 N  N   . GLN B 1 284 ? 86.351  1.105   -18.223 1.00 81.93  ? 263 GLN B N   1 
ATOM   4272 C  CA  . GLN B 1 284 ? 87.142  0.595   -19.337 1.00 87.11  ? 263 GLN B CA  1 
ATOM   4273 C  C   . GLN B 1 284 ? 86.435  0.847   -20.662 1.00 90.00  ? 263 GLN B C   1 
ATOM   4274 O  O   . GLN B 1 284 ? 87.071  1.208   -21.659 1.00 87.30  ? 263 GLN B O   1 
ATOM   4275 C  CB  . GLN B 1 284 ? 87.404  -0.901  -19.155 1.00 90.66  ? 263 GLN B CB  1 
ATOM   4276 C  CG  . GLN B 1 284 ? 88.835  -1.261  -18.767 1.00 94.10  ? 263 GLN B CG  1 
ATOM   4277 C  CD  . GLN B 1 284 ? 89.046  -1.317  -17.264 1.00 86.92  ? 263 GLN B CD  1 
ATOM   4278 O  OE1 . GLN B 1 284 ? 89.819  -0.540  -16.703 1.00 81.27  ? 263 GLN B OE1 1 
ATOM   4279 N  NE2 . GLN B 1 284 ? 88.366  -2.249  -16.606 1.00 88.25  ? 263 GLN B NE2 1 
ATOM   4280 N  N   . HIS B 1 285 ? 85.114  0.656   -20.687 1.00 87.51  ? 264 HIS B N   1 
ATOM   4281 C  CA  . HIS B 1 285 ? 84.343  0.868   -21.907 1.00 83.18  ? 264 HIS B CA  1 
ATOM   4282 C  C   . HIS B 1 285 ? 84.287  2.343   -22.290 1.00 81.37  ? 264 HIS B C   1 
ATOM   4283 O  O   . HIS B 1 285 ? 84.296  2.675   -23.481 1.00 82.21  ? 264 HIS B O   1 
ATOM   4284 C  CB  . HIS B 1 285 ? 82.935  0.298   -21.727 1.00 86.65  ? 264 HIS B CB  1 
ATOM   4285 C  CG  . HIS B 1 285 ? 81.996  0.626   -22.845 1.00 86.70  ? 264 HIS B CG  1 
ATOM   4286 N  ND1 . HIS B 1 285 ? 82.082  0.040   -24.089 1.00 94.85  ? 264 HIS B ND1 1 
ATOM   4287 C  CD2 . HIS B 1 285 ? 80.944  1.477   -22.902 1.00 89.81  ? 264 HIS B CD2 1 
ATOM   4288 C  CE1 . HIS B 1 285 ? 81.126  0.518   -24.866 1.00 94.68  ? 264 HIS B CE1 1 
ATOM   4289 N  NE2 . HIS B 1 285 ? 80.421  1.391   -24.169 1.00 92.32  ? 264 HIS B NE2 1 
ATOM   4290 N  N   . PHE B 1 286 ? 84.229  3.240   -21.307 1.00 84.09  ? 265 PHE B N   1 
ATOM   4291 C  CA  . PHE B 1 286 ? 84.172  4.676   -21.580 1.00 84.41  ? 265 PHE B CA  1 
ATOM   4292 C  C   . PHE B 1 286 ? 85.569  5.281   -21.660 1.00 82.46  ? 265 PHE B C   1 
ATOM   4293 O  O   . PHE B 1 286 ? 86.122  5.444   -22.746 1.00 93.15  ? 265 PHE B O   1 
ATOM   4294 C  CB  . PHE B 1 286 ? 83.356  5.397   -20.504 1.00 78.56  ? 265 PHE B CB  1 
ATOM   4295 C  CG  . PHE B 1 286 ? 81.950  4.890   -20.373 1.00 79.05  ? 265 PHE B CG  1 
ATOM   4296 C  CD1 . PHE B 1 286 ? 81.006  5.173   -21.345 1.00 77.56  ? 265 PHE B CD1 1 
ATOM   4297 C  CD2 . PHE B 1 286 ? 81.572  4.131   -19.278 1.00 85.46  ? 265 PHE B CD2 1 
ATOM   4298 C  CE1 . PHE B 1 286 ? 79.713  4.705   -21.229 1.00 76.94  ? 265 PHE B CE1 1 
ATOM   4299 C  CE2 . PHE B 1 286 ? 80.279  3.662   -19.156 1.00 78.30  ? 265 PHE B CE2 1 
ATOM   4300 C  CZ  . PHE B 1 286 ? 79.348  3.950   -20.133 1.00 80.05  ? 265 PHE B CZ  1 
ATOM   4301 N  N   . GLY B 1 288 ? 87.998  7.449   -22.783 1.00 83.83  ? 267 GLY B N   1 
ATOM   4302 C  CA  . GLY B 1 288 ? 88.082  8.109   -24.072 1.00 80.47  ? 267 GLY B CA  1 
ATOM   4303 C  C   . GLY B 1 288 ? 86.771  8.739   -24.499 1.00 84.25  ? 267 GLY B C   1 
ATOM   4304 O  O   . GLY B 1 288 ? 86.754  9.820   -25.086 1.00 79.73  ? 267 GLY B O   1 
ATOM   4305 N  N   . LYS B 1 289 ? 85.667  8.054   -24.213 1.00 82.49  ? 268 LYS B N   1 
ATOM   4306 C  CA  . LYS B 1 289 ? 84.353  8.603   -24.502 1.00 81.72  ? 268 LYS B CA  1 
ATOM   4307 C  C   . LYS B 1 289 ? 84.037  9.750   -23.546 1.00 79.91  ? 268 LYS B C   1 
ATOM   4308 O  O   . LYS B 1 289 ? 84.599  9.857   -22.452 1.00 83.64  ? 268 LYS B O   1 
ATOM   4309 C  CB  . LYS B 1 289 ? 83.284  7.516   -24.395 1.00 77.12  ? 268 LYS B CB  1 
ATOM   4310 N  N   . MET B 1 290 ? 83.125  10.618  -23.976 1.00 79.40  ? 269 MET B N   1 
ATOM   4311 C  CA  . MET B 1 290 ? 82.743  11.779  -23.191 1.00 78.39  ? 269 MET B CA  1 
ATOM   4312 C  C   . MET B 1 290 ? 81.538  11.456  -22.307 1.00 75.87  ? 269 MET B C   1 
ATOM   4313 O  O   . MET B 1 290 ? 80.988  10.351  -22.331 1.00 74.72  ? 269 MET B O   1 
ATOM   4314 C  CB  . MET B 1 290 ? 82.430  12.969  -24.101 1.00 83.49  ? 269 MET B CB  1 
ATOM   4315 C  CG  . MET B 1 290 ? 83.623  13.854  -24.469 1.00 91.01  ? 269 MET B CG  1 
ATOM   4316 S  SD  . MET B 1 290 ? 84.694  14.328  -23.093 1.00 113.29 ? 269 MET B SD  1 
ATOM   4317 C  CE  . MET B 1 290 ? 86.010  13.123  -23.261 1.00 96.88  ? 269 MET B CE  1 
ATOM   4318 N  N   . TYR B 1 291 ? 81.119  12.445  -21.513 1.00 76.79  ? 270 TYR B N   1 
ATOM   4319 C  CA  . TYR B 1 291 ? 79.935  12.284  -20.679 1.00 75.40  ? 270 TYR B CA  1 
ATOM   4320 C  C   . TYR B 1 291 ? 78.680  12.043  -21.506 1.00 79.36  ? 270 TYR B C   1 
ATOM   4321 O  O   . TYR B 1 291 ? 77.696  11.512  -20.979 1.00 74.65  ? 270 TYR B O   1 
ATOM   4322 C  CB  . TYR B 1 291 ? 79.728  13.517  -19.799 1.00 76.48  ? 270 TYR B CB  1 
ATOM   4323 C  CG  . TYR B 1 291 ? 80.755  13.712  -18.702 1.00 89.45  ? 270 TYR B CG  1 
ATOM   4324 C  CD1 . TYR B 1 291 ? 81.756  12.776  -18.470 1.00 84.59  ? 270 TYR B CD1 1 
ATOM   4325 C  CD2 . TYR B 1 291 ? 80.713  14.836  -17.890 1.00 88.63  ? 270 TYR B CD2 1 
ATOM   4326 C  CE1 . TYR B 1 291 ? 82.689  12.963  -17.463 1.00 92.05  ? 270 TYR B CE1 1 
ATOM   4327 C  CE2 . TYR B 1 291 ? 81.637  15.029  -16.884 1.00 93.25  ? 270 TYR B CE2 1 
ATOM   4328 C  CZ  . TYR B 1 291 ? 82.623  14.093  -16.674 1.00 96.20  ? 270 TYR B CZ  1 
ATOM   4329 O  OH  . TYR B 1 291 ? 83.541  14.293  -15.667 1.00 95.13  ? 270 TYR B OH  1 
ATOM   4330 N  N   . GLY B 1 292 ? 78.681  12.440  -22.782 1.00 72.46  ? 271 GLY B N   1 
ATOM   4331 C  CA  . GLY B 1 292 ? 77.546  12.153  -23.639 1.00 68.93  ? 271 GLY B CA  1 
ATOM   4332 C  C   . GLY B 1 292 ? 77.495  10.707  -24.071 1.00 71.89  ? 271 GLY B C   1 
ATOM   4333 O  O   . GLY B 1 292 ? 76.409  10.164  -24.298 1.00 69.33  ? 271 GLY B O   1 
ATOM   4334 N  N   . HIS B 1 293 ? 78.657  10.066  -24.204 1.00 77.06  ? 272 HIS B N   1 
ATOM   4335 C  CA  . HIS B 1 293 ? 78.670  8.621   -24.379 1.00 71.08  ? 272 HIS B CA  1 
ATOM   4336 C  C   . HIS B 1 293 ? 78.039  7.942   -23.172 1.00 66.98  ? 272 HIS B C   1 
ATOM   4337 O  O   . HIS B 1 293 ? 77.191  7.057   -23.317 1.00 60.01  ? 272 HIS B O   1 
ATOM   4338 C  CB  . HIS B 1 293 ? 80.099  8.121   -24.594 1.00 68.91  ? 272 HIS B CB  1 
ATOM   4339 N  N   . LEU B 1 294 ? 78.415  8.371   -21.967 1.00 64.83  ? 273 LEU B N   1 
ATOM   4340 C  CA  . LEU B 1 294 ? 77.869  7.754   -20.764 1.00 65.52  ? 273 LEU B CA  1 
ATOM   4341 C  C   . LEU B 1 294 ? 76.356  7.911   -20.707 1.00 66.99  ? 273 LEU B C   1 
ATOM   4342 O  O   . LEU B 1 294 ? 75.627  6.931   -20.529 1.00 67.29  ? 273 LEU B O   1 
ATOM   4343 C  CB  . LEU B 1 294 ? 78.519  8.367   -19.525 1.00 65.75  ? 273 LEU B CB  1 
ATOM   4344 C  CG  . LEU B 1 294 ? 78.054  7.817   -18.175 1.00 59.30  ? 273 LEU B CG  1 
ATOM   4345 C  CD1 . LEU B 1 294 ? 78.272  6.321   -18.101 1.00 59.25  ? 273 LEU B CD1 1 
ATOM   4346 C  CD2 . LEU B 1 294 ? 78.771  8.516   -17.027 1.00 71.48  ? 273 LEU B CD2 1 
ATOM   4347 N  N   . LYS B 1 295 ? 75.862  9.141   -20.867 1.00 62.36  ? 274 LYS B N   1 
ATOM   4348 C  CA  . LYS B 1 295 ? 74.431  9.378   -20.714 1.00 63.20  ? 274 LYS B CA  1 
ATOM   4349 C  C   . LYS B 1 295 ? 73.630  8.588   -21.739 1.00 61.35  ? 274 LYS B C   1 
ATOM   4350 O  O   . LYS B 1 295 ? 72.569  8.041   -21.419 1.00 58.01  ? 274 LYS B O   1 
ATOM   4351 C  CB  . LYS B 1 295 ? 74.138  10.873  -20.819 1.00 65.86  ? 274 LYS B CB  1 
ATOM   4352 C  CG  . LYS B 1 295 ? 74.612  11.643  -19.603 1.00 68.33  ? 274 LYS B CG  1 
ATOM   4353 C  CD  . LYS B 1 295 ? 74.432  13.136  -19.769 1.00 75.90  ? 274 LYS B CD  1 
ATOM   4354 C  CE  . LYS B 1 295 ? 74.760  13.859  -18.486 1.00 69.35  ? 274 LYS B CE  1 
ATOM   4355 N  NZ  . LYS B 1 295 ? 73.966  15.089  -18.351 1.00 69.78  ? 274 LYS B NZ  1 
ATOM   4356 N  N   . GLY B 1 296 ? 74.121  8.515   -22.976 1.00 66.56  ? 275 GLY B N   1 
ATOM   4357 C  CA  . GLY B 1 296 ? 73.453  7.690   -23.968 1.00 60.87  ? 275 GLY B CA  1 
ATOM   4358 C  C   . GLY B 1 296 ? 73.410  6.230   -23.561 1.00 57.52  ? 275 GLY B C   1 
ATOM   4359 O  O   . GLY B 1 296 ? 72.358  5.591   -23.610 1.00 53.91  ? 275 GLY B O   1 
ATOM   4360 N  N   . GLU B 1 297 ? 74.553  5.693   -23.123 1.00 56.98  ? 276 GLU B N   1 
ATOM   4361 C  CA  . GLU B 1 297 ? 74.613  4.288   -22.733 1.00 61.72  ? 276 GLU B CA  1 
ATOM   4362 C  C   . GLU B 1 297 ? 73.624  3.992   -21.612 1.00 60.33  ? 276 GLU B C   1 
ATOM   4363 O  O   . GLU B 1 297 ? 72.866  3.016   -21.674 1.00 52.96  ? 276 GLU B O   1 
ATOM   4364 C  CB  . GLU B 1 297 ? 76.033  3.917   -22.296 1.00 57.75  ? 276 GLU B CB  1 
ATOM   4365 C  CG  . GLU B 1 297 ? 77.108  4.002   -23.384 1.00 71.15  ? 276 GLU B CG  1 
ATOM   4366 C  CD  . GLU B 1 297 ? 76.561  3.878   -24.796 1.00 71.03  ? 276 GLU B CD  1 
ATOM   4367 O  OE1 . GLU B 1 297 ? 75.981  2.823   -25.130 1.00 74.54  ? 276 GLU B OE1 1 
ATOM   4368 O  OE2 . GLU B 1 297 ? 76.701  4.847   -25.571 1.00 76.83  ? 276 GLU B OE2 1 
ATOM   4369 N  N   . VAL B 1 298 ? 73.625  4.829   -20.572 1.00 56.21  ? 277 VAL B N   1 
ATOM   4370 C  CA  . VAL B 1 298 ? 72.687  4.655   -19.465 1.00 54.74  ? 277 VAL B CA  1 
ATOM   4371 C  C   . VAL B 1 298 ? 71.266  4.591   -20.003 1.00 54.97  ? 277 VAL B C   1 
ATOM   4372 O  O   . VAL B 1 298 ? 70.564  3.586   -19.849 1.00 51.65  ? 277 VAL B O   1 
ATOM   4373 C  CB  . VAL B 1 298 ? 72.843  5.796   -18.444 1.00 57.25  ? 277 VAL B CB  1 
ATOM   4374 C  CG1 . VAL B 1 298 ? 71.769  5.707   -17.364 1.00 56.85  ? 277 VAL B CG1 1 
ATOM   4375 C  CG2 . VAL B 1 298 ? 74.224  5.768   -17.820 1.00 52.79  ? 277 VAL B CG2 1 
ATOM   4376 N  N   . ALA B 1 299 ? 70.844  5.660   -20.684 1.00 53.46  ? 278 ALA B N   1 
ATOM   4377 C  CA  . ALA B 1 299 ? 69.456  5.779   -21.116 1.00 53.10  ? 278 ALA B CA  1 
ATOM   4378 C  C   . ALA B 1 299 ? 69.008  4.562   -21.912 1.00 49.05  ? 278 ALA B C   1 
ATOM   4379 O  O   . ALA B 1 299 ? 67.856  4.127   -21.800 1.00 46.93  ? 278 ALA B O   1 
ATOM   4380 C  CB  . ALA B 1 299 ? 69.282  7.053   -21.944 1.00 58.53  ? 278 ALA B CB  1 
ATOM   4381 N  N   . GLU B 1 300 ? 69.901  3.998   -22.728 1.00 49.70  ? 279 GLU B N   1 
ATOM   4382 C  CA  . GLU B 1 300 ? 69.527  2.828   -23.514 1.00 54.32  ? 279 GLU B CA  1 
ATOM   4383 C  C   . GLU B 1 300 ? 69.301  1.617   -22.619 1.00 49.03  ? 279 GLU B C   1 
ATOM   4384 O  O   . GLU B 1 300 ? 68.365  0.841   -22.843 1.00 48.12  ? 279 GLU B O   1 
ATOM   4385 C  CB  . GLU B 1 300 ? 70.600  2.517   -24.558 1.00 55.72  ? 279 GLU B CB  1 
ATOM   4386 C  CG  . GLU B 1 300 ? 71.062  3.723   -25.356 1.00 63.53  ? 279 GLU B CG  1 
ATOM   4387 C  CD  . GLU B 1 300 ? 71.062  3.477   -26.854 1.00 83.72  ? 279 GLU B CD  1 
ATOM   4388 O  OE1 . GLU B 1 300 ? 71.852  2.628   -27.320 1.00 93.78  ? 279 GLU B OE1 1 
ATOM   4389 O  OE2 . GLU B 1 300 ? 70.269  4.132   -27.565 1.00 82.04  ? 279 GLU B OE2 1 
ATOM   4390 N  N   . ALA B 1 301 ? 70.153  1.435   -21.608 1.00 49.46  ? 280 ALA B N   1 
ATOM   4391 C  CA  . ALA B 1 301 ? 70.032  0.272   -20.736 1.00 48.92  ? 280 ALA B CA  1 
ATOM   4392 C  C   . ALA B 1 301 ? 68.772  0.350   -19.881 1.00 46.76  ? 280 ALA B C   1 
ATOM   4393 O  O   . ALA B 1 301 ? 68.002  -0.615  -19.806 1.00 45.90  ? 280 ALA B O   1 
ATOM   4394 C  CB  . ALA B 1 301 ? 71.275  0.151   -19.853 1.00 50.09  ? 280 ALA B CB  1 
ATOM   4395 N  N   . VAL B 1 302 ? 68.539  1.496   -19.233 1.00 45.96  ? 281 VAL B N   1 
ATOM   4396 C  CA  . VAL B 1 302 ? 67.359  1.637   -18.384 1.00 43.96  ? 281 VAL B CA  1 
ATOM   4397 C  C   . VAL B 1 302 ? 66.088  1.453   -19.203 1.00 47.23  ? 281 VAL B C   1 
ATOM   4398 O  O   . VAL B 1 302 ? 65.128  0.826   -18.745 1.00 42.79  ? 281 VAL B O   1 
ATOM   4399 C  CB  . VAL B 1 302 ? 67.358  2.995   -17.650 1.00 47.04  ? 281 VAL B CB  1 
ATOM   4400 C  CG1 . VAL B 1 302 ? 68.251  2.937   -16.419 1.00 49.28  ? 281 VAL B CG1 1 
ATOM   4401 C  CG2 . VAL B 1 302 ? 67.779  4.136   -18.571 1.00 56.64  ? 281 VAL B CG2 1 
ATOM   4402 N  N   . SER B 1 303 ? 66.051  2.004   -20.417 1.00 48.32  ? 282 SER B N   1 
ATOM   4403 C  CA  . SER B 1 303 ? 64.866  1.829   -21.250 1.00 50.36  ? 282 SER B CA  1 
ATOM   4404 C  C   . SER B 1 303 ? 64.714  0.387   -21.716 1.00 46.50  ? 282 SER B C   1 
ATOM   4405 O  O   . SER B 1 303 ? 63.587  -0.086  -21.897 1.00 50.99  ? 282 SER B O   1 
ATOM   4406 C  CB  . SER B 1 303 ? 64.915  2.775   -22.449 1.00 46.23  ? 282 SER B CB  1 
ATOM   4407 O  OG  . SER B 1 303 ? 64.707  4.116   -22.037 1.00 49.04  ? 282 SER B OG  1 
ATOM   4408 N  N   . GLY B 1 304 ? 65.823  -0.325  -21.920 1.00 44.58  ? 283 GLY B N   1 
ATOM   4409 C  CA  . GLY B 1 304 ? 65.722  -1.734  -22.260 1.00 44.97  ? 283 GLY B CA  1 
ATOM   4410 C  C   . GLY B 1 304 ? 65.113  -2.550  -21.137 1.00 46.90  ? 283 GLY B C   1 
ATOM   4411 O  O   . GLY B 1 304 ? 64.310  -3.455  -21.374 1.00 47.56  ? 283 GLY B O   1 
ATOM   4412 N  N   . MET B 1 305 ? 65.485  -2.236  -19.897 1.00 48.14  ? 284 MET B N   1 
ATOM   4413 C  CA  . MET B 1 305 ? 64.950  -2.961  -18.752 1.00 42.70  ? 284 MET B CA  1 
ATOM   4414 C  C   . MET B 1 305 ? 63.500  -2.579  -18.485 1.00 45.48  ? 284 MET B C   1 
ATOM   4415 O  O   . MET B 1 305 ? 62.665  -3.446  -18.204 1.00 48.95  ? 284 MET B O   1 
ATOM   4416 C  CB  . MET B 1 305 ? 65.818  -2.679  -17.531 1.00 42.32  ? 284 MET B CB  1 
ATOM   4417 C  CG  . MET B 1 305 ? 65.417  -3.439  -16.280 1.00 51.17  ? 284 MET B CG  1 
ATOM   4418 S  SD  . MET B 1 305 ? 66.077  -2.689  -14.780 1.00 52.45  ? 284 MET B SD  1 
ATOM   4419 C  CE  . MET B 1 305 ? 65.442  -1.029  -14.925 1.00 50.28  ? 284 MET B CE  1 
ATOM   4420 N  N   . LEU B 1 306 ? 63.182  -1.285  -18.569 1.00 47.26  ? 285 LEU B N   1 
ATOM   4421 C  CA  . LEU B 1 306 ? 61.813  -0.841  -18.335 1.00 40.83  ? 285 LEU B CA  1 
ATOM   4422 C  C   . LEU B 1 306 ? 60.861  -1.387  -19.389 1.00 45.95  ? 285 LEU B C   1 
ATOM   4423 O  O   . LEU B 1 306 ? 59.683  -1.618  -19.098 1.00 42.22  ? 285 LEU B O   1 
ATOM   4424 C  CB  . LEU B 1 306 ? 61.749  0.689   -18.315 1.00 38.24  ? 285 LEU B CB  1 
ATOM   4425 C  CG  . LEU B 1 306 ? 62.451  1.413   -17.162 1.00 43.69  ? 285 LEU B CG  1 
ATOM   4426 C  CD1 . LEU B 1 306 ? 62.274  2.922   -17.286 1.00 48.47  ? 285 LEU B CD1 1 
ATOM   4427 C  CD2 . LEU B 1 306 ? 61.936  0.924   -15.820 1.00 50.86  ? 285 LEU B CD2 1 
ATOM   4428 N  N   . THR B 1 307 ? 61.346  -1.588  -20.617 1.00 42.47  ? 286 THR B N   1 
ATOM   4429 C  CA  . THR B 1 307 ? 60.479  -2.083  -21.681 1.00 39.60  ? 286 THR B CA  1 
ATOM   4430 C  C   . THR B 1 307 ? 59.978  -3.487  -21.373 1.00 42.79  ? 286 THR B C   1 
ATOM   4431 O  O   . THR B 1 307 ? 58.805  -3.801  -21.606 1.00 43.28  ? 286 THR B O   1 
ATOM   4432 C  CB  . THR B 1 307 ? 61.225  -2.059  -23.015 1.00 49.21  ? 286 THR B CB  1 
ATOM   4433 O  OG1 . THR B 1 307 ? 61.514  -0.702  -23.376 1.00 47.52  ? 286 THR B OG1 1 
ATOM   4434 C  CG2 . THR B 1 307 ? 60.392  -2.706  -24.110 1.00 42.63  ? 286 THR B CG2 1 
ATOM   4435 N  N   . GLU B 1 308 ? 60.854  -4.347  -20.850 1.00 44.75  ? 287 GLU B N   1 
ATOM   4436 C  CA  . GLU B 1 308 ? 60.430  -5.688  -20.462 1.00 51.12  ? 287 GLU B CA  1 
ATOM   4437 C  C   . GLU B 1 308 ? 59.425  -5.635  -19.317 1.00 50.11  ? 287 GLU B C   1 
ATOM   4438 O  O   . GLU B 1 308 ? 58.468  -6.418  -19.280 1.00 47.52  ? 287 GLU B O   1 
ATOM   4439 C  CB  . GLU B 1 308 ? 61.651  -6.523  -20.076 1.00 54.28  ? 287 GLU B CB  1 
ATOM   4440 C  CG  . GLU B 1 308 ? 61.555  -7.989  -20.470 1.00 63.39  ? 287 GLU B CG  1 
ATOM   4441 C  CD  . GLU B 1 308 ? 60.663  -8.788  -19.542 1.00 66.63  ? 287 GLU B CD  1 
ATOM   4442 O  OE1 . GLU B 1 308 ? 61.003  -8.905  -18.345 1.00 65.36  ? 287 GLU B OE1 1 
ATOM   4443 O  OE2 . GLU B 1 308 ? 59.619  -9.294  -20.006 1.00 63.38  ? 287 GLU B OE2 1 
ATOM   4444 N  N   . LEU B 1 309 ? 59.635  -4.725  -18.363 1.00 40.54  ? 288 LEU B N   1 
ATOM   4445 C  CA  . LEU B 1 309 ? 58.676  -4.554  -17.277 1.00 39.87  ? 288 LEU B CA  1 
ATOM   4446 C  C   . LEU B 1 309 ? 57.338  -4.049  -17.800 1.00 35.39  ? 288 LEU B C   1 
ATOM   4447 O  O   . LEU B 1 309 ? 56.276  -4.483  -17.341 1.00 32.10  ? 288 LEU B O   1 
ATOM   4448 C  CB  . LEU B 1 309 ? 59.233  -3.583  -16.238 1.00 40.02  ? 288 LEU B CB  1 
ATOM   4449 C  CG  . LEU B 1 309 ? 59.813  -4.179  -14.959 1.00 46.66  ? 288 LEU B CG  1 
ATOM   4450 C  CD1 . LEU B 1 309 ? 60.615  -3.131  -14.205 1.00 48.06  ? 288 LEU B CD1 1 
ATOM   4451 C  CD2 . LEU B 1 309 ? 58.699  -4.730  -14.085 1.00 44.62  ? 288 LEU B CD2 1 
ATOM   4452 N  N   . GLN B 1 310 ? 57.374  -3.131  -18.766 1.00 38.70  ? 289 GLN B N   1 
ATOM   4453 C  CA  . GLN B 1 310 ? 56.166  -2.422  -19.169 1.00 34.41  ? 289 GLN B CA  1 
ATOM   4454 C  C   . GLN B 1 310 ? 55.245  -3.293  -20.010 1.00 33.20  ? 289 GLN B C   1 
ATOM   4455 O  O   . GLN B 1 310 ? 54.021  -3.189  -19.894 1.00 34.85  ? 289 GLN B O   1 
ATOM   4456 C  CB  . GLN B 1 310 ? 56.541  -1.150  -19.927 1.00 38.78  ? 289 GLN B CB  1 
ATOM   4457 C  CG  . GLN B 1 310 ? 57.041  -0.036  -19.025 1.00 41.17  ? 289 GLN B CG  1 
ATOM   4458 C  CD  . GLN B 1 310 ? 57.573  1.146   -19.800 1.00 49.99  ? 289 GLN B CD  1 
ATOM   4459 O  OE1 . GLN B 1 310 ? 57.594  1.138   -21.031 1.00 48.67  ? 289 GLN B OE1 1 
ATOM   4460 N  NE2 . GLN B 1 310 ? 58.009  2.173   -19.082 1.00 46.93  ? 289 GLN B NE2 1 
ATOM   4461 N  N   . GLU B 1 311 ? 55.799  -4.146  -20.870 1.00 40.47  ? 290 GLU B N   1 
ATOM   4462 C  CA  . GLU B 1 311 ? 54.940  -5.042  -21.636 1.00 41.23  ? 290 GLU B CA  1 
ATOM   4463 C  C   . GLU B 1 311 ? 54.220  -6.022  -20.715 1.00 33.96  ? 290 GLU B C   1 
ATOM   4464 O  O   . GLU B 1 311 ? 53.031  -6.295  -20.900 1.00 32.54  ? 290 GLU B O   1 
ATOM   4465 C  CB  . GLU B 1 311 ? 55.751  -5.769  -22.708 1.00 46.88  ? 290 GLU B CB  1 
ATOM   4466 C  CG  . GLU B 1 311 ? 56.961  -6.536  -22.195 1.00 51.48  ? 290 GLU B CG  1 
ATOM   4467 C  CD  . GLU B 1 311 ? 56.666  -8.001  -21.931 1.00 56.04  ? 290 GLU B CD  1 
ATOM   4468 O  OE1 . GLU B 1 311 ? 57.399  -8.624  -21.135 1.00 54.46  ? 290 GLU B OE1 1 
ATOM   4469 O  OE2 . GLU B 1 311 ? 55.701  -8.530  -22.519 1.00 58.44  ? 290 GLU B OE2 1 
ATOM   4470 N  N   . ARG B 1 312 ? 54.911  -6.541  -19.700 1.00 33.08  ? 291 ARG B N   1 
ATOM   4471 C  CA  . ARG B 1 312 ? 54.220  -7.332  -18.688 1.00 34.62  ? 291 ARG B CA  1 
ATOM   4472 C  C   . ARG B 1 312 ? 53.152  -6.501  -17.989 1.00 30.91  ? 291 ARG B C   1 
ATOM   4473 O  O   . ARG B 1 312 ? 52.051  -6.992  -17.716 1.00 29.24  ? 291 ARG B O   1 
ATOM   4474 C  CB  . ARG B 1 312 ? 55.218  -7.879  -17.671 1.00 32.37  ? 291 ARG B CB  1 
ATOM   4475 C  CG  . ARG B 1 312 ? 56.107  -8.977  -18.217 1.00 40.61  ? 291 ARG B CG  1 
ATOM   4476 C  CD  . ARG B 1 312 ? 57.285  -9.234  -17.299 1.00 46.62  ? 291 ARG B CD  1 
ATOM   4477 N  NE  . ARG B 1 312 ? 56.864  -9.495  -15.927 1.00 38.00  ? 291 ARG B NE  1 
ATOM   4478 C  CZ  . ARG B 1 312 ? 56.460  -10.676 -15.481 1.00 40.16  ? 291 ARG B CZ  1 
ATOM   4479 N  NH1 . ARG B 1 312 ? 56.366  -11.723 -16.285 1.00 44.02  ? 291 ARG B NH1 1 
ATOM   4480 N  NH2 . ARG B 1 312 ? 56.145  -10.812 -14.197 1.00 35.93  ? 291 ARG B NH2 1 
ATOM   4481 N  N   . TYR B 1 313 ? 53.460  -5.235  -17.696 1.00 30.02  ? 292 TYR B N   1 
ATOM   4482 C  CA  . TYR B 1 313 ? 52.492  -4.375  -17.026 1.00 28.72  ? 292 TYR B CA  1 
ATOM   4483 C  C   . TYR B 1 313 ? 51.209  -4.262  -17.835 1.00 30.38  ? 292 TYR B C   1 
ATOM   4484 O  O   . TYR B 1 313 ? 50.109  -4.426  -17.299 1.00 26.66  ? 292 TYR B O   1 
ATOM   4485 C  CB  . TYR B 1 313 ? 53.091  -2.988  -16.790 1.00 29.74  ? 292 TYR B CB  1 
ATOM   4486 C  CG  . TYR B 1 313 ? 52.064  -1.967  -16.355 1.00 29.80  ? 292 TYR B CG  1 
ATOM   4487 C  CD1 . TYR B 1 313 ? 51.672  -1.877  -15.026 1.00 27.42  ? 292 TYR B CD1 1 
ATOM   4488 C  CD2 . TYR B 1 313 ? 51.483  -1.100  -17.271 1.00 28.13  ? 292 TYR B CD2 1 
ATOM   4489 C  CE1 . TYR B 1 313 ? 50.733  -0.957  -14.622 1.00 25.25  ? 292 TYR B CE1 1 
ATOM   4490 C  CE2 . TYR B 1 313 ? 50.544  -0.172  -16.875 1.00 33.52  ? 292 TYR B CE2 1 
ATOM   4491 C  CZ  . TYR B 1 313 ? 50.171  -0.109  -15.544 1.00 32.40  ? 292 TYR B CZ  1 
ATOM   4492 O  OH  . TYR B 1 313 ? 49.237  0.807   -15.133 1.00 28.11  ? 292 TYR B OH  1 
ATOM   4493 N  N   . HIS B 1 314 ? 51.330  -3.980  -19.135 1.00 29.83  ? 293 HIS B N   1 
ATOM   4494 C  CA  . HIS B 1 314 ? 50.139  -3.770  -19.951 1.00 31.43  ? 293 HIS B CA  1 
ATOM   4495 C  C   . HIS B 1 314 ? 49.371  -5.064  -20.171 1.00 28.53  ? 293 HIS B C   1 
ATOM   4496 O  O   . HIS B 1 314 ? 48.138  -5.043  -20.246 1.00 30.65  ? 293 HIS B O   1 
ATOM   4497 C  CB  . HIS B 1 314 ? 50.524  -3.141  -21.291 1.00 37.47  ? 293 HIS B CB  1 
ATOM   4498 C  CG  . HIS B 1 314 ? 50.959  -1.715  -21.177 1.00 35.49  ? 293 HIS B CG  1 
ATOM   4499 N  ND1 . HIS B 1 314 ? 50.105  -0.709  -20.778 1.00 37.06  ? 293 HIS B ND1 1 
ATOM   4500 C  CD2 . HIS B 1 314 ? 52.158  -1.127  -21.397 1.00 33.28  ? 293 HIS B CD2 1 
ATOM   4501 C  CE1 . HIS B 1 314 ? 50.759  0.439   -20.761 1.00 35.01  ? 293 HIS B CE1 1 
ATOM   4502 N  NE2 . HIS B 1 314 ? 52.006  0.213   -21.133 1.00 35.88  ? 293 HIS B NE2 1 
ATOM   4503 N  N   . ARG B 1 315 ? 50.076  -6.191  -20.287 1.00 32.73  ? 294 ARG B N   1 
ATOM   4504 C  CA  A ARG B 1 315 ? 49.393  -7.466  -20.473 0.50 31.79  ? 294 ARG B CA  1 
ATOM   4505 C  CA  B ARG B 1 315 ? 49.397  -7.470  -20.471 0.50 32.78  ? 294 ARG B CA  1 
ATOM   4506 C  C   . ARG B 1 315 ? 48.528  -7.810  -19.266 1.00 33.03  ? 294 ARG B C   1 
ATOM   4507 O  O   . ARG B 1 315 ? 47.390  -8.269  -19.420 1.00 37.56  ? 294 ARG B O   1 
ATOM   4508 C  CB  A ARG B 1 315 ? 50.415  -8.571  -20.742 0.50 34.47  ? 294 ARG B CB  1 
ATOM   4509 C  CB  B ARG B 1 315 ? 50.429  -8.570  -20.726 0.50 34.48  ? 294 ARG B CB  1 
ATOM   4510 C  CG  A ARG B 1 315 ? 49.801  -9.949  -20.930 0.50 36.66  ? 294 ARG B CG  1 
ATOM   4511 C  CG  B ARG B 1 315 ? 49.839  -9.957  -20.920 0.50 36.65  ? 294 ARG B CG  1 
ATOM   4512 C  CD  A ARG B 1 315 ? 50.733  -10.884 -21.695 0.50 42.73  ? 294 ARG B CD  1 
ATOM   4513 C  CD  B ARG B 1 315 ? 50.859  -10.912 -21.528 0.50 42.77  ? 294 ARG B CD  1 
ATOM   4514 N  NE  A ARG B 1 315 ? 52.073  -10.935 -21.120 0.50 39.66  ? 294 ARG B NE  1 
ATOM   4515 N  NE  B ARG B 1 315 ? 52.140  -10.877 -20.830 0.50 39.77  ? 294 ARG B NE  1 
ATOM   4516 C  CZ  A ARG B 1 315 ? 53.102  -10.204 -21.530 0.50 40.32  ? 294 ARG B CZ  1 
ATOM   4517 C  CZ  B ARG B 1 315 ? 52.476  -11.675 -19.824 0.50 38.41  ? 294 ARG B CZ  1 
ATOM   4518 N  NH1 A ARG B 1 315 ? 52.990  -9.346  -22.532 0.50 40.89  ? 294 ARG B NH1 1 
ATOM   4519 N  NH1 B ARG B 1 315 ? 51.645  -12.594 -19.361 0.50 34.65  ? 294 ARG B NH1 1 
ATOM   4520 N  NH2 A ARG B 1 315 ? 54.276  -10.337 -20.919 0.50 40.12  ? 294 ARG B NH2 1 
ATOM   4521 N  NH2 B ARG B 1 315 ? 53.678  -11.546 -19.270 0.50 39.63  ? 294 ARG B NH2 1 
ATOM   4522 N  N   . PHE B 1 316 ? 49.046  -7.589  -18.055 1.00 31.37  ? 295 PHE B N   1 
ATOM   4523 C  CA  . PHE B 1 316 ? 48.245  -7.833  -16.859 1.00 32.91  ? 295 PHE B CA  1 
ATOM   4524 C  C   . PHE B 1 316 ? 47.177  -6.758  -16.681 1.00 32.70  ? 295 PHE B C   1 
ATOM   4525 O  O   . PHE B 1 316 ? 46.035  -7.062  -16.322 1.00 26.56  ? 295 PHE B O   1 
ATOM   4526 C  CB  . PHE B 1 316 ? 49.142  -7.886  -15.623 1.00 28.98  ? 295 PHE B CB  1 
ATOM   4527 C  CG  . PHE B 1 316 ? 50.154  -8.994  -15.649 1.00 31.84  ? 295 PHE B CG  1 
ATOM   4528 C  CD1 . PHE B 1 316 ? 49.853  -10.220 -16.218 1.00 36.79  ? 295 PHE B CD1 1 
ATOM   4529 C  CD2 . PHE B 1 316 ? 51.410  -8.807  -15.101 1.00 32.06  ? 295 PHE B CD2 1 
ATOM   4530 C  CE1 . PHE B 1 316 ? 50.785  -11.237 -16.236 1.00 38.00  ? 295 PHE B CE1 1 
ATOM   4531 C  CE2 . PHE B 1 316 ? 52.345  -9.821  -15.117 1.00 32.19  ? 295 PHE B CE2 1 
ATOM   4532 C  CZ  . PHE B 1 316 ? 52.033  -11.035 -15.684 1.00 38.83  ? 295 PHE B CZ  1 
ATOM   4533 N  N   . ARG B 1 317 ? 47.530  -5.498  -16.944 1.00 31.24  ? 296 ARG B N   1 
ATOM   4534 C  CA  . ARG B 1 317 ? 46.641  -4.389  -16.611 1.00 28.34  ? 296 ARG B CA  1 
ATOM   4535 C  C   . ARG B 1 317 ? 45.383  -4.401  -17.469 1.00 30.03  ? 296 ARG B C   1 
ATOM   4536 O  O   . ARG B 1 317 ? 44.295  -4.064  -16.987 1.00 29.50  ? 296 ARG B O   1 
ATOM   4537 C  CB  . ARG B 1 317 ? 47.384  -3.063  -16.769 1.00 24.01  ? 296 ARG B CB  1 
ATOM   4538 C  CG  . ARG B 1 317 ? 46.551  -1.840  -16.451 1.00 25.35  ? 296 ARG B CG  1 
ATOM   4539 C  CD  . ARG B 1 317 ? 46.066  -1.859  -15.012 1.00 28.39  ? 296 ARG B CD  1 
ATOM   4540 N  NE  . ARG B 1 317 ? 45.258  -0.689  -14.701 1.00 31.17  ? 296 ARG B NE  1 
ATOM   4541 C  CZ  . ARG B 1 317 ? 43.938  -0.628  -14.821 1.00 29.39  ? 296 ARG B CZ  1 
ATOM   4542 N  NH1 . ARG B 1 317 ? 43.235  -1.649  -15.285 1.00 23.83  ? 296 ARG B NH1 1 
ATOM   4543 N  NH2 . ARG B 1 317 ? 43.307  0.489   -14.471 1.00 27.73  ? 296 ARG B NH2 1 
ATOM   4544 N  N   . ASN B 1 318 ? 45.511  -4.773  -18.744 1.00 33.65  ? 297 ASN B N   1 
ATOM   4545 C  CA  . ASN B 1 318 ? 44.366  -4.807  -19.643 1.00 28.69  ? 297 ASN B CA  1 
ATOM   4546 C  C   . ASN B 1 318 ? 43.517  -6.062  -19.480 1.00 35.01  ? 297 ASN B C   1 
ATOM   4547 O  O   . ASN B 1 318 ? 42.424  -6.127  -20.056 1.00 34.13  ? 297 ASN B O   1 
ATOM   4548 C  CB  . ASN B 1 318 ? 44.846  -4.688  -21.091 1.00 35.32  ? 297 ASN B CB  1 
ATOM   4549 C  CG  . ASN B 1 318 ? 45.411  -3.314  -21.402 1.00 35.08  ? 297 ASN B CG  1 
ATOM   4550 O  OD1 . ASN B 1 318 ? 44.920  -2.305  -20.897 1.00 38.53  ? 297 ASN B OD1 1 
ATOM   4551 N  ND2 . ASN B 1 318 ? 46.449  -3.269  -22.232 1.00 32.87  ? 297 ASN B ND2 1 
ATOM   4552 N  N   . ASP B 1 319 ? 43.980  -7.051  -18.712 1.00 31.98  ? 298 ASP B N   1 
ATOM   4553 C  CA  . ASP B 1 319 ? 43.228  -8.286  -18.488 1.00 26.08  ? 298 ASP B CA  1 
ATOM   4554 C  C   . ASP B 1 319 ? 42.518  -8.166  -17.143 1.00 31.70  ? 298 ASP B C   1 
ATOM   4555 O  O   . ASP B 1 319 ? 42.933  -8.731  -16.130 1.00 26.52  ? 298 ASP B O   1 
ATOM   4556 C  CB  . ASP B 1 319 ? 44.153  -9.496  -18.541 1.00 29.28  ? 298 ASP B CB  1 
ATOM   4557 C  CG  . ASP B 1 319 ? 43.395  -10.811 -18.524 1.00 33.84  ? 298 ASP B CG  1 
ATOM   4558 O  OD1 . ASP B 1 319 ? 42.159  -10.794 -18.333 1.00 34.98  ? 298 ASP B OD1 1 
ATOM   4559 O  OD2 . ASP B 1 319 ? 44.040  -11.863 -18.706 1.00 34.39  ? 298 ASP B OD2 1 
ATOM   4560 N  N   . GLU B 1 320 ? 41.409  -7.422  -17.150 1.00 29.56  ? 299 GLU B N   1 
ATOM   4561 C  CA  . GLU B 1 320 ? 40.703  -7.134  -15.906 1.00 36.17  ? 299 GLU B CA  1 
ATOM   4562 C  C   . GLU B 1 320 ? 40.188  -8.409  -15.244 1.00 35.11  ? 299 GLU B C   1 
ATOM   4563 O  O   . GLU B 1 320 ? 40.145  -8.494  -14.012 1.00 29.69  ? 299 GLU B O   1 
ATOM   4564 C  CB  . GLU B 1 320 ? 39.552  -6.163  -16.176 1.00 39.49  ? 299 GLU B CB  1 
ATOM   4565 C  CG  . GLU B 1 320 ? 39.961  -4.884  -16.929 1.00 47.83  ? 299 GLU B CG  1 
ATOM   4566 C  CD  . GLU B 1 320 ? 40.333  -3.736  -15.999 1.00 56.70  ? 299 GLU B CD  1 
ATOM   4567 O  OE1 . GLU B 1 320 ? 40.439  -3.969  -14.778 1.00 60.71  ? 299 GLU B OE1 1 
ATOM   4568 O  OE2 . GLU B 1 320 ? 40.517  -2.597  -16.486 1.00 48.35  ? 299 GLU B OE2 1 
ATOM   4569 N  N   . ALA B 1 321 ? 39.800  -9.409  -16.038 1.00 27.41  ? 300 ALA B N   1 
ATOM   4570 C  CA  . ALA B 1 321 ? 39.360  -10.674 -15.459 1.00 22.89  ? 300 ALA B CA  1 
ATOM   4571 C  C   . ALA B 1 321 ? 40.486  -11.339 -14.680 1.00 23.59  ? 300 ALA B C   1 
ATOM   4572 O  O   . ALA B 1 321 ? 40.264  -11.874 -13.587 1.00 27.63  ? 300 ALA B O   1 
ATOM   4573 C  CB  . ALA B 1 321 ? 38.847  -11.607 -16.555 1.00 32.66  ? 300 ALA B CB  1 
ATOM   4574 N  N   . PHE B 1 322 ? 41.704  -11.315 -15.226 1.00 23.13  ? 301 PHE B N   1 
ATOM   4575 C  CA  . PHE B 1 322 ? 42.841  -11.870 -14.501 1.00 17.99  ? 301 PHE B CA  1 
ATOM   4576 C  C   . PHE B 1 322 ? 43.097  -11.111 -13.206 1.00 21.51  ? 301 PHE B C   1 
ATOM   4577 O  O   . PHE B 1 322 ? 43.355  -11.723 -12.163 1.00 17.47  ? 301 PHE B O   1 
ATOM   4578 C  CB  . PHE B 1 322 ? 44.092  -11.844 -15.374 1.00 21.92  ? 301 PHE B CB  1 
ATOM   4579 C  CG  . PHE B 1 322 ? 45.334  -12.260 -14.648 1.00 17.37  ? 301 PHE B CG  1 
ATOM   4580 C  CD1 . PHE B 1 322 ? 45.483  -13.562 -14.199 1.00 19.56  ? 301 PHE B CD1 1 
ATOM   4581 C  CD2 . PHE B 1 322 ? 46.346  -11.352 -14.407 1.00 18.45  ? 301 PHE B CD2 1 
ATOM   4582 C  CE1 . PHE B 1 322 ? 46.623  -13.950 -13.528 1.00 24.78  ? 301 PHE B CE1 1 
ATOM   4583 C  CE2 . PHE B 1 322 ? 47.485  -11.732 -13.733 1.00 22.73  ? 301 PHE B CE2 1 
ATOM   4584 C  CZ  . PHE B 1 322 ? 47.625  -13.035 -13.294 1.00 30.80  ? 301 PHE B CZ  1 
ATOM   4585 N  N   . LEU B 1 323 ? 43.044  -9.776  -13.253 1.00 19.84  ? 302 LEU B N   1 
ATOM   4586 C  CA  . LEU B 1 323 ? 43.297  -8.995  -12.047 1.00 19.99  ? 302 LEU B CA  1 
ATOM   4587 C  C   . LEU B 1 323 ? 42.248  -9.289  -10.981 1.00 21.06  ? 302 LEU B C   1 
ATOM   4588 O  O   . LEU B 1 323 ? 42.558  -9.315  -9.786  1.00 17.40  ? 302 LEU B O   1 
ATOM   4589 C  CB  . LEU B 1 323 ? 43.324  -7.500  -12.369 1.00 16.50  ? 302 LEU B CB  1 
ATOM   4590 C  CG  . LEU B 1 323 ? 44.424  -6.982  -13.295 1.00 22.83  ? 302 LEU B CG  1 
ATOM   4591 C  CD1 . LEU B 1 323 ? 44.218  -5.493  -13.536 1.00 28.33  ? 302 LEU B CD1 1 
ATOM   4592 C  CD2 . LEU B 1 323 ? 45.801  -7.243  -12.722 1.00 20.26  ? 302 LEU B CD2 1 
ATOM   4593 N  N   . ASN B 1 324 ? 40.996  -9.495  -11.396 1.00 25.12  ? 303 ASN B N   1 
ATOM   4594 C  CA  . ASN B 1 324 ? 39.960  -9.876  -10.443 1.00 24.88  ? 303 ASN B CA  1 
ATOM   4595 C  C   . ASN B 1 324 ? 40.280  -11.215 -9.793  1.00 24.84  ? 303 ASN B C   1 
ATOM   4596 O  O   . ASN B 1 324 ? 40.061  -11.399 -8.590  1.00 24.99  ? 303 ASN B O   1 
ATOM   4597 C  CB  . ASN B 1 324 ? 38.599  -9.931  -11.134 1.00 31.54  ? 303 ASN B CB  1 
ATOM   4598 C  CG  . ASN B 1 324 ? 37.852  -8.618  -11.056 1.00 30.22  ? 303 ASN B CG  1 
ATOM   4599 O  OD1 . ASN B 1 324 ? 38.214  -7.727  -10.287 1.00 35.08  ? 303 ASN B OD1 1 
ATOM   4600 N  ND2 . ASN B 1 324 ? 36.796  -8.493  -11.847 1.00 39.28  ? 303 ASN B ND2 1 
ATOM   4601 N  N   . GLN B 1 325 ? 40.790  -12.168 -10.573 1.00 16.89  ? 304 GLN B N   1 
ATOM   4602 C  CA  . GLN B 1 325 ? 41.194  -13.442 -9.991  1.00 19.91  ? 304 GLN B CA  1 
ATOM   4603 C  C   . GLN B 1 325 ? 42.316  -13.248 -8.981  1.00 23.29  ? 304 GLN B C   1 
ATOM   4604 O  O   . GLN B 1 325 ? 42.317  -13.876 -7.914  1.00 18.46  ? 304 GLN B O   1 
ATOM   4605 C  CB  . GLN B 1 325 ? 41.630  -14.409 -11.090 1.00 17.88  ? 304 GLN B CB  1 
ATOM   4606 C  CG  . GLN B 1 325 ? 42.058  -15.775 -10.580 1.00 25.28  ? 304 GLN B CG  1 
ATOM   4607 C  CD  . GLN B 1 325 ? 42.868  -16.545 -11.599 1.00 21.44  ? 304 GLN B CD  1 
ATOM   4608 O  OE1 . GLN B 1 325 ? 42.361  -16.931 -12.649 1.00 25.05  ? 304 GLN B OE1 1 
ATOM   4609 N  NE2 . GLN B 1 325 ? 44.140  -16.765 -11.295 1.00 25.87  ? 304 GLN B NE2 1 
ATOM   4610 N  N   . VAL B 1 326 ? 43.287  -12.391 -9.302  1.00 17.58  ? 305 VAL B N   1 
ATOM   4611 C  CA  . VAL B 1 326 ? 44.409  -12.175 -8.393  1.00 17.97  ? 305 VAL B CA  1 
ATOM   4612 C  C   . VAL B 1 326 ? 43.926  -11.566 -7.085  1.00 21.51  ? 305 VAL B C   1 
ATOM   4613 O  O   . VAL B 1 326 ? 44.364  -11.963 -5.999  1.00 16.53  ? 305 VAL B O   1 
ATOM   4614 C  CB  . VAL B 1 326 ? 45.477  -11.293 -9.061  1.00 19.89  ? 305 VAL B CB  1 
ATOM   4615 C  CG1 . VAL B 1 326 ? 46.563  -10.934 -8.057  1.00 23.04  ? 305 VAL B CG1 1 
ATOM   4616 C  CG2 . VAL B 1 326 ? 46.081  -12.004 -10.266 1.00 23.58  ? 305 VAL B CG2 1 
ATOM   4617 N  N   . MET B 1 327 ? 43.029  -10.581 -7.165  1.00 19.26  ? 306 MET B N   1 
ATOM   4618 C  CA  . MET B 1 327 ? 42.527  -9.948  -5.952  1.00 25.79  ? 306 MET B CA  1 
ATOM   4619 C  C   . MET B 1 327 ? 41.683  -10.913 -5.131  1.00 22.02  ? 306 MET B C   1 
ATOM   4620 O  O   . MET B 1 327 ? 41.684  -10.838 -3.898  1.00 18.39  ? 306 MET B O   1 
ATOM   4621 C  CB  . MET B 1 327 ? 41.724  -8.696  -6.308  1.00 20.51  ? 306 MET B CB  1 
ATOM   4622 C  CG  . MET B 1 327 ? 42.585  -7.539  -6.804  1.00 19.34  ? 306 MET B CG  1 
ATOM   4623 S  SD  . MET B 1 327 ? 41.644  -6.063  -7.261  1.00 18.88  ? 306 MET B SD  1 
ATOM   4624 C  CE  . MET B 1 327 ? 40.591  -6.702  -8.563  1.00 25.37  ? 306 MET B CE  1 
ATOM   4625 N  N   . LYS B 1 328 ? 40.954  -11.816 -5.790  1.00 25.70  ? 307 LYS B N   1 
ATOM   4626 C  CA  . LYS B 1 328 ? 40.183  -12.814 -5.057  1.00 32.31  ? 307 LYS B CA  1 
ATOM   4627 C  C   . LYS B 1 328 ? 41.105  -13.784 -4.328  1.00 29.13  ? 307 LYS B C   1 
ATOM   4628 O  O   . LYS B 1 328 ? 40.908  -14.071 -3.143  1.00 23.76  ? 307 LYS B O   1 
ATOM   4629 C  CB  . LYS B 1 328 ? 39.254  -13.562 -6.012  1.00 32.94  ? 307 LYS B CB  1 
ATOM   4630 C  CG  . LYS B 1 328 ? 38.349  -14.565 -5.323  1.00 26.68  ? 307 LYS B CG  1 
ATOM   4631 C  CD  . LYS B 1 328 ? 36.945  -14.547 -5.906  1.00 40.61  ? 307 LYS B CD  1 
ATOM   4632 C  CE  . LYS B 1 328 ? 36.042  -15.569 -5.223  1.00 41.89  ? 307 LYS B CE  1 
ATOM   4633 N  NZ  . LYS B 1 328 ? 36.570  -16.960 -5.358  1.00 47.67  ? 307 LYS B NZ  1 
ATOM   4634 N  N   . GLU B 1 329 ? 42.133  -14.284 -5.019  1.00 19.68  ? 308 GLU B N   1 
ATOM   4635 C  CA  . GLU B 1 329 ? 43.073  -15.201 -4.381  1.00 25.27  ? 308 GLU B CA  1 
ATOM   4636 C  C   . GLU B 1 329 ? 43.802  -14.523 -3.230  1.00 25.82  ? 308 GLU B C   1 
ATOM   4637 O  O   . GLU B 1 329 ? 43.976  -15.114 -2.159  1.00 20.31  ? 308 GLU B O   1 
ATOM   4638 C  CB  . GLU B 1 329 ? 44.076  -15.731 -5.409  1.00 25.19  ? 308 GLU B CB  1 
ATOM   4639 C  CG  . GLU B 1 329 ? 45.208  -16.550 -4.797  1.00 26.50  ? 308 GLU B CG  1 
ATOM   4640 C  CD  . GLU B 1 329 ? 45.953  -17.406 -5.812  1.00 30.27  ? 308 GLU B CD  1 
ATOM   4641 O  OE1 . GLU B 1 329 ? 45.940  -17.076 -7.017  1.00 24.01  ? 308 GLU B OE1 1 
ATOM   4642 O  OE2 . GLU B 1 329 ? 46.552  -18.421 -5.398  1.00 29.81  ? 308 GLU B OE2 1 
ATOM   4643 N  N   . GLY B 1 330 ? 44.237  -13.279 -3.433  1.00 17.87  ? 309 GLY B N   1 
ATOM   4644 C  CA  . GLY B 1 330 ? 44.983  -12.594 -2.394  1.00 18.75  ? 309 GLY B CA  1 
ATOM   4645 C  C   . GLY B 1 330 ? 44.129  -12.258 -1.190  1.00 21.68  ? 309 GLY B C   1 
ATOM   4646 O  O   . GLY B 1 330 ? 44.573  -12.395 -0.048  1.00 23.06  ? 309 GLY B O   1 
ATOM   4647 N  N   . ALA B 1 331 ? 42.896  -11.804 -1.429  1.00 18.96  ? 310 ALA B N   1 
ATOM   4648 C  CA  . ALA B 1 331 ? 42.020  -11.424 -0.328  1.00 20.81  ? 310 ALA B CA  1 
ATOM   4649 C  C   . ALA B 1 331 ? 41.633  -12.637 0.505   1.00 22.17  ? 310 ALA B C   1 
ATOM   4650 O  O   . ALA B 1 331 ? 41.600  -12.567 1.738   1.00 19.44  ? 310 ALA B O   1 
ATOM   4651 C  CB  . ALA B 1 331 ? 40.773  -10.725 -0.872  1.00 19.94  ? 310 ALA B CB  1 
ATOM   4652 N  N   . GLU B 1 332 ? 41.337  -13.759 -0.153  1.00 20.75  ? 311 GLU B N   1 
ATOM   4653 C  CA  . GLU B 1 332 ? 40.965  -14.966 0.573   1.00 22.34  ? 311 GLU B CA  1 
ATOM   4654 C  C   . GLU B 1 332 ? 42.135  -15.511 1.380   1.00 23.14  ? 311 GLU B C   1 
ATOM   4655 O  O   . GLU B 1 332 ? 41.969  -15.883 2.548   1.00 20.48  ? 311 GLU B O   1 
ATOM   4656 C  CB  . GLU B 1 332 ? 40.433  -16.011 -0.403  1.00 23.74  ? 311 GLU B CB  1 
ATOM   4657 C  CG  . GLU B 1 332 ? 38.933  -15.880 -0.643  1.00 35.13  ? 311 GLU B CG  1 
ATOM   4658 C  CD  . GLU B 1 332 ? 38.500  -14.446 -0.937  1.00 39.62  ? 311 GLU B CD  1 
ATOM   4659 O  OE1 . GLU B 1 332 ? 38.560  -14.029 -2.114  1.00 39.00  ? 311 GLU B OE1 1 
ATOM   4660 O  OE2 . GLU B 1 332 ? 38.106  -13.726 0.012   1.00 40.69  ? 311 GLU B OE2 1 
ATOM   4661 N  N   . LYS B 1 333 ? 43.328  -15.556 0.786   1.00 19.09  ? 312 LYS B N   1 
ATOM   4662 C  CA  . LYS B 1 333 ? 44.502  -15.985 1.540   1.00 20.53  ? 312 LYS B CA  1 
ATOM   4663 C  C   . LYS B 1 333 ? 44.793  -15.026 2.688   1.00 21.56  ? 312 LYS B C   1 
ATOM   4664 O  O   . LYS B 1 333 ? 45.157  -15.455 3.791   1.00 17.50  ? 312 LYS B O   1 
ATOM   4665 C  CB  . LYS B 1 333 ? 45.710  -16.100 0.608   1.00 20.25  ? 312 LYS B CB  1 
ATOM   4666 C  CG  . LYS B 1 333 ? 47.001  -16.524 1.293   1.00 22.78  ? 312 LYS B CG  1 
ATOM   4667 C  CD  . LYS B 1 333 ? 47.990  -17.178 0.317   1.00 25.50  ? 312 LYS B CD  1 
ATOM   4668 C  CE  . LYS B 1 333 ? 48.301  -16.289 -0.877  1.00 27.77  ? 312 LYS B CE  1 
ATOM   4669 N  NZ  . LYS B 1 333 ? 49.307  -16.922 -1.768  1.00 29.34  ? 312 LYS B NZ  1 
ATOM   4670 N  N   . ALA B 1 334 ? 44.637  -13.721 2.447   1.00 15.41  ? 313 ALA B N   1 
ATOM   4671 C  CA  . ALA B 1 334 ? 44.897  -12.744 3.496   1.00 17.61  ? 313 ALA B CA  1 
ATOM   4672 C  C   . ALA B 1 334 ? 43.922  -12.904 4.655   1.00 18.49  ? 313 ALA B C   1 
ATOM   4673 O  O   . ALA B 1 334 ? 44.329  -12.886 5.818   1.00 16.24  ? 313 ALA B O   1 
ATOM   4674 C  CB  . ALA B 1 334 ? 44.823  -11.329 2.926   1.00 18.38  ? 313 ALA B CB  1 
ATOM   4675 N  N   . SER B 1 335 ? 42.632  -13.073 4.354   1.00 21.39  ? 314 SER B N   1 
ATOM   4676 C  CA  . SER B 1 335 ? 41.630  -13.181 5.410   1.00 20.10  ? 314 SER B CA  1 
ATOM   4677 C  C   . SER B 1 335 ? 41.806  -14.457 6.219   1.00 22.13  ? 314 SER B C   1 
ATOM   4678 O  O   . SER B 1 335 ? 41.579  -14.463 7.432   1.00 21.14  ? 314 SER B O   1 
ATOM   4679 C  CB  . SER B 1 335 ? 40.226  -13.129 4.812   1.00 23.55  ? 314 SER B CB  1 
ATOM   4680 O  OG  . SER B 1 335 ? 39.881  -11.803 4.459   1.00 25.73  ? 314 SER B OG  1 
ATOM   4681 N  N   . ALA B 1 336 ? 42.187  -15.555 5.562   1.00 20.25  ? 315 ALA B N   1 
ATOM   4682 C  CA  . ALA B 1 336 ? 42.434  -16.796 6.290   1.00 22.82  ? 315 ALA B CA  1 
ATOM   4683 C  C   . ALA B 1 336 ? 43.545  -16.614 7.316   1.00 24.32  ? 315 ALA B C   1 
ATOM   4684 O  O   . ALA B 1 336 ? 43.425  -17.060 8.463   1.00 30.25  ? 315 ALA B O   1 
ATOM   4685 C  CB  . ALA B 1 336 ? 42.792  -17.917 5.312   1.00 21.41  ? 315 ALA B CB  1 
ATOM   4686 N  N   . HIS B 1 337 ? 44.635  -15.961 6.918   1.00 20.52  ? 316 HIS B N   1 
ATOM   4687 C  CA  . HIS B 1 337 ? 45.734  -15.699 7.840   1.00 22.73  ? 316 HIS B CA  1 
ATOM   4688 C  C   . HIS B 1 337 ? 45.313  -14.692 8.905   1.00 25.77  ? 316 HIS B C   1 
ATOM   4689 O  O   . HIS B 1 337 ? 45.533  -14.906 10.105  1.00 21.86  ? 316 HIS B O   1 
ATOM   4690 C  CB  . HIS B 1 337 ? 46.943  -15.203 7.039   1.00 27.47  ? 316 HIS B CB  1 
ATOM   4691 C  CG  . HIS B 1 337 ? 48.219  -15.134 7.820   1.00 30.13  ? 316 HIS B CG  1 
ATOM   4692 N  ND1 . HIS B 1 337 ? 48.323  -15.556 9.128   1.00 36.84  ? 316 HIS B ND1 1 
ATOM   4693 C  CD2 . HIS B 1 337 ? 49.450  -14.688 7.469   1.00 32.74  ? 316 HIS B CD2 1 
ATOM   4694 C  CE1 . HIS B 1 337 ? 49.562  -15.371 9.551   1.00 35.96  ? 316 HIS B CE1 1 
ATOM   4695 N  NE2 . HIS B 1 337 ? 50.265  -14.844 8.565   1.00 33.26  ? 316 HIS B NE2 1 
ATOM   4696 N  N   . ALA B 1 338 ? 44.648  -13.613 8.483   1.00 21.23  ? 317 ALA B N   1 
ATOM   4697 C  CA  . ALA B 1 338 ? 44.310  -12.526 9.394   1.00 22.78  ? 317 ALA B CA  1 
ATOM   4698 C  C   . ALA B 1 338 ? 43.290  -12.963 10.436  1.00 23.22  ? 317 ALA B C   1 
ATOM   4699 O  O   . ALA B 1 338 ? 43.340  -12.514 11.586  1.00 21.78  ? 317 ALA B O   1 
ATOM   4700 C  CB  . ALA B 1 338 ? 43.778  -11.333 8.600   1.00 23.18  ? 317 ALA B CB  1 
ATOM   4701 N  N   . SER B 1 339 ? 42.348  -13.826 10.050  1.00 23.49  ? 318 SER B N   1 
ATOM   4702 C  CA  . SER B 1 339 ? 41.299  -14.238 10.972  1.00 26.37  ? 318 SER B CA  1 
ATOM   4703 C  C   . SER B 1 339 ? 41.858  -15.051 12.131  1.00 28.85  ? 318 SER B C   1 
ATOM   4704 O  O   . SER B 1 339 ? 41.295  -15.030 13.228  1.00 26.09  ? 318 SER B O   1 
ATOM   4705 C  CB  . SER B 1 339 ? 40.230  -15.036 10.225  1.00 29.81  ? 318 SER B CB  1 
ATOM   4706 O  OG  . SER B 1 339 ? 40.785  -16.185 9.613   1.00 37.23  ? 318 SER B OG  1 
ATOM   4707 N  N   . LYS B 1 340 ? 42.961  -15.768 11.919  1.00 31.57  ? 319 LYS B N   1 
ATOM   4708 C  CA  . LYS B 1 340 ? 43.587  -16.472 13.032  1.00 24.44  ? 319 LYS B CA  1 
ATOM   4709 C  C   . LYS B 1 340 ? 44.002  -15.496 14.126  1.00 31.63  ? 319 LYS B C   1 
ATOM   4710 O  O   . LYS B 1 340 ? 43.759  -15.742 15.313  1.00 26.58  ? 319 LYS B O   1 
ATOM   4711 C  CB  . LYS B 1 340 ? 44.786  -17.278 12.533  1.00 32.13  ? 319 LYS B CB  1 
ATOM   4712 C  CG  . LYS B 1 340 ? 44.406  -18.401 11.581  1.00 34.85  ? 319 LYS B CG  1 
ATOM   4713 C  CD  . LYS B 1 340 ? 45.624  -19.023 10.912  1.00 40.02  ? 319 LYS B CD  1 
ATOM   4714 C  CE  . LYS B 1 340 ? 45.221  -20.180 9.999   1.00 45.79  ? 319 LYS B CE  1 
ATOM   4715 N  NZ  . LYS B 1 340 ? 46.263  -20.492 8.981   1.00 56.83  ? 319 LYS B NZ  1 
ATOM   4716 N  N   . THR B 1 341 ? 44.608  -14.369 13.747  1.00 22.82  ? 320 THR B N   1 
ATOM   4717 C  CA  . THR B 1 341 ? 45.033  -13.397 14.751  1.00 24.44  ? 320 THR B CA  1 
ATOM   4718 C  C   . THR B 1 341 ? 43.846  -12.641 15.336  1.00 22.64  ? 320 THR B C   1 
ATOM   4719 O  O   . THR B 1 341 ? 43.792  -12.409 16.551  1.00 20.65  ? 320 THR B O   1 
ATOM   4720 C  CB  . THR B 1 341 ? 46.039  -12.415 14.149  1.00 25.58  ? 320 THR B CB  1 
ATOM   4721 O  OG1 . THR B 1 341 ? 47.270  -13.096 13.884  1.00 31.62  ? 320 THR B OG1 1 
ATOM   4722 C  CG2 . THR B 1 341 ? 46.308  -11.259 15.108  1.00 26.66  ? 320 THR B CG2 1 
ATOM   4723 N  N   . LEU B 1 342 ? 42.888  -12.242 14.494  1.00 24.55  ? 321 LEU B N   1 
ATOM   4724 C  CA  . LEU B 1 342 ? 41.761  -11.462 14.994  1.00 21.36  ? 321 LEU B CA  1 
ATOM   4725 C  C   . LEU B 1 342 ? 40.937  -12.265 15.988  1.00 21.72  ? 321 LEU B C   1 
ATOM   4726 O  O   . LEU B 1 342 ? 40.486  -11.730 17.004  1.00 18.67  ? 321 LEU B O   1 
ATOM   4727 C  CB  . LEU B 1 342 ? 40.868  -10.991 13.850  1.00 20.60  ? 321 LEU B CB  1 
ATOM   4728 C  CG  . LEU B 1 342 ? 39.789  -9.996  14.296  1.00 23.24  ? 321 LEU B CG  1 
ATOM   4729 C  CD1 . LEU B 1 342 ? 40.406  -8.637  14.593  1.00 24.60  ? 321 LEU B CD1 1 
ATOM   4730 C  CD2 . LEU B 1 342 ? 38.677  -9.870  13.269  1.00 24.06  ? 321 LEU B CD2 1 
ATOM   4731 N  N   . LYS B 1 343 ? 40.712  -13.546 15.703  1.00 25.25  ? 322 LYS B N   1 
ATOM   4732 C  CA  . LYS B 1 343 ? 39.899  -14.356 16.600  1.00 25.29  ? 322 LYS B CA  1 
ATOM   4733 C  C   . LYS B 1 343 ? 40.588  -14.562 17.942  1.00 26.18  ? 322 LYS B C   1 
ATOM   4734 O  O   . LYS B 1 343 ? 39.912  -14.656 18.974  1.00 23.53  ? 322 LYS B O   1 
ATOM   4735 C  CB  . LYS B 1 343 ? 39.574  -15.691 15.936  1.00 30.29  ? 322 LYS B CB  1 
ATOM   4736 C  CG  . LYS B 1 343 ? 38.149  -15.781 15.357  1.00 40.35  ? 322 LYS B CG  1 
ATOM   4737 C  CD  . LYS B 1 343 ? 37.718  -14.560 14.512  1.00 43.41  ? 322 LYS B CD  1 
ATOM   4738 C  CE  . LYS B 1 343 ? 38.303  -14.584 13.104  1.00 42.83  ? 322 LYS B CE  1 
ATOM   4739 N  NZ  . LYS B 1 343 ? 37.635  -13.621 12.180  1.00 43.12  ? 322 LYS B NZ  1 
ATOM   4740 N  N   . ALA B 1 344 ? 41.920  -14.636 17.948  1.00 20.89  ? 323 ALA B N   1 
ATOM   4741 C  CA  . ALA B 1 344 ? 42.653  -14.697 19.207  1.00 24.30  ? 323 ALA B CA  1 
ATOM   4742 C  C   . ALA B 1 344 ? 42.583  -13.369 19.951  1.00 25.96  ? 323 ALA B C   1 
ATOM   4743 O  O   . ALA B 1 344 ? 42.558  -13.347 21.189  1.00 25.36  ? 323 ALA B O   1 
ATOM   4744 C  CB  . ALA B 1 344 ? 44.109  -15.084 18.944  1.00 21.83  ? 323 ALA B CB  1 
ATOM   4745 N  N   . VAL B 1 345 ? 42.567  -12.257 19.217  1.00 20.08  ? 324 VAL B N   1 
ATOM   4746 C  CA  . VAL B 1 345 ? 42.411  -10.950 19.844  1.00 19.58  ? 324 VAL B CA  1 
ATOM   4747 C  C   . VAL B 1 345 ? 41.023  -10.825 20.466  1.00 23.55  ? 324 VAL B C   1 
ATOM   4748 O  O   . VAL B 1 345 ? 40.874  -10.380 21.608  1.00 22.46  ? 324 VAL B O   1 
ATOM   4749 C  CB  . VAL B 1 345 ? 42.671  -9.833  18.814  1.00 18.36  ? 324 VAL B CB  1 
ATOM   4750 C  CG1 . VAL B 1 345 ? 42.271  -8.478  19.373  1.00 21.21  ? 324 VAL B CG1 1 
ATOM   4751 C  CG2 . VAL B 1 345 ? 44.131  -9.818  18.403  1.00 22.72  ? 324 VAL B CG2 1 
ATOM   4752 N  N   . TYR B 1 346 ? 39.987  -11.214 19.722  1.00 20.48  ? 325 TYR B N   1 
ATOM   4753 C  CA  . TYR B 1 346 ? 38.629  -11.119 20.248  1.00 21.51  ? 325 TYR B CA  1 
ATOM   4754 C  C   . TYR B 1 346 ? 38.447  -12.040 21.448  1.00 26.48  ? 325 TYR B C   1 
ATOM   4755 O  O   . TYR B 1 346 ? 37.778  -11.676 22.423  1.00 23.33  ? 325 TYR B O   1 
ATOM   4756 C  CB  . TYR B 1 346 ? 37.617  -11.446 19.149  1.00 21.28  ? 325 TYR B CB  1 
ATOM   4757 C  CG  . TYR B 1 346 ? 37.305  -10.295 18.203  1.00 22.73  ? 325 TYR B CG  1 
ATOM   4758 C  CD1 . TYR B 1 346 ? 37.994  -9.089  18.275  1.00 25.74  ? 325 TYR B CD1 1 
ATOM   4759 C  CD2 . TYR B 1 346 ? 36.304  -10.416 17.248  1.00 25.14  ? 325 TYR B CD2 1 
ATOM   4760 C  CE1 . TYR B 1 346 ? 37.700  -8.042  17.415  1.00 29.17  ? 325 TYR B CE1 1 
ATOM   4761 C  CE2 . TYR B 1 346 ? 36.004  -9.376  16.386  1.00 21.40  ? 325 TYR B CE2 1 
ATOM   4762 C  CZ  . TYR B 1 346 ? 36.703  -8.190  16.476  1.00 24.95  ? 325 TYR B CZ  1 
ATOM   4763 O  OH  . TYR B 1 346 ? 36.412  -7.150  15.623  1.00 24.54  ? 325 TYR B OH  1 
ATOM   4764 N  N   . GLU B 1 347 ? 39.046  -13.233 21.400  1.00 28.80  ? 326 GLU B N   1 
ATOM   4765 C  CA  . GLU B 1 347 ? 38.997  -14.139 22.542  1.00 29.42  ? 326 GLU B CA  1 
ATOM   4766 C  C   . GLU B 1 347 ? 39.576  -13.479 23.787  1.00 30.93  ? 326 GLU B C   1 
ATOM   4767 O  O   . GLU B 1 347 ? 38.985  -13.541 24.871  1.00 23.22  ? 326 GLU B O   1 
ATOM   4768 C  CB  . GLU B 1 347 ? 39.775  -15.420 22.231  1.00 30.98  ? 326 GLU B CB  1 
ATOM   4769 C  CG  . GLU B 1 347 ? 38.930  -16.638 21.903  1.00 44.40  ? 326 GLU B CG  1 
ATOM   4770 C  CD  . GLU B 1 347 ? 37.880  -16.926 22.951  1.00 49.52  ? 326 GLU B CD  1 
ATOM   4771 O  OE1 . GLU B 1 347 ? 38.185  -16.783 24.152  1.00 56.33  ? 326 GLU B OE1 1 
ATOM   4772 O  OE2 . GLU B 1 347 ? 36.751  -17.299 22.572  1.00 53.97  ? 326 GLU B OE2 1 
ATOM   4773 N  N   . ALA B 1 348 ? 40.748  -12.854 23.647  1.00 26.17  ? 327 ALA B N   1 
ATOM   4774 C  CA  . ALA B 1 348 ? 41.429  -12.279 24.801  1.00 28.29  ? 327 ALA B CA  1 
ATOM   4775 C  C   . ALA B 1 348 ? 40.684  -11.065 25.341  1.00 26.30  ? 327 ALA B C   1 
ATOM   4776 O  O   . ALA B 1 348 ? 40.654  -10.840 26.557  1.00 26.15  ? 327 ALA B O   1 
ATOM   4777 C  CB  . ALA B 1 348 ? 42.864  -11.910 24.423  1.00 28.91  ? 327 ALA B CB  1 
ATOM   4778 N  N   . ILE B 1 349 ? 40.078  -10.271 24.456  1.00 26.02  ? 328 ILE B N   1 
ATOM   4779 C  CA  . ILE B 1 349 ? 39.363  -9.073  24.890  1.00 30.41  ? 328 ILE B CA  1 
ATOM   4780 C  C   . ILE B 1 349 ? 38.136  -9.448  25.707  1.00 24.90  ? 328 ILE B C   1 
ATOM   4781 O  O   . ILE B 1 349 ? 37.772  -8.746  26.656  1.00 25.79  ? 328 ILE B O   1 
ATOM   4782 C  CB  . ILE B 1 349 ? 38.989  -8.208  23.673  1.00 28.52  ? 328 ILE B CB  1 
ATOM   4783 C  CG1 . ILE B 1 349 ? 40.124  -7.253  23.315  1.00 36.25  ? 328 ILE B CG1 1 
ATOM   4784 C  CG2 . ILE B 1 349 ? 37.754  -7.363  23.949  1.00 33.60  ? 328 ILE B CG2 1 
ATOM   4785 C  CD1 . ILE B 1 349 ? 41.487  -7.861  23.348  1.00 35.90  ? 328 ILE B CD1 1 
ATOM   4786 N  N   . GLY B 1 350 ? 37.471  -10.542 25.343  1.00 23.86  ? 329 GLY B N   1 
ATOM   4787 C  CA  . GLY B 1 350 ? 36.287  -10.976 26.054  1.00 25.29  ? 329 GLY B CA  1 
ATOM   4788 C  C   . GLY B 1 350 ? 35.025  -10.962 25.219  1.00 25.86  ? 329 GLY B C   1 
ATOM   4789 O  O   . GLY B 1 350 ? 33.930  -11.175 25.749  1.00 25.90  ? 329 GLY B O   1 
ATOM   4790 N  N   . PHE B 1 351 ? 35.156  -10.708 23.918  1.00 24.03  ? 330 PHE B N   1 
ATOM   4791 C  CA  . PHE B 1 351 ? 34.002  -10.769 23.032  1.00 22.98  ? 330 PHE B CA  1 
ATOM   4792 C  C   . PHE B 1 351 ? 33.451  -12.189 22.984  1.00 22.24  ? 330 PHE B C   1 
ATOM   4793 O  O   . PHE B 1 351 ? 34.204  -13.164 23.022  1.00 25.04  ? 330 PHE B O   1 
ATOM   4794 C  CB  . PHE B 1 351 ? 34.381  -10.331 21.615  1.00 23.71  ? 330 PHE B CB  1 
ATOM   4795 C  CG  . PHE B 1 351 ? 34.695  -8.863  21.475  1.00 23.32  ? 330 PHE B CG  1 
ATOM   4796 C  CD1 . PHE B 1 351 ? 34.447  -7.965  22.500  1.00 24.96  ? 330 PHE B CD1 1 
ATOM   4797 C  CD2 . PHE B 1 351 ? 35.233  -8.384  20.294  1.00 28.41  ? 330 PHE B CD2 1 
ATOM   4798 C  CE1 . PHE B 1 351 ? 34.739  -6.617  22.345  1.00 22.80  ? 330 PHE B CE1 1 
ATOM   4799 C  CE2 . PHE B 1 351 ? 35.523  -7.043  20.136  1.00 25.40  ? 330 PHE B CE2 1 
ATOM   4800 C  CZ  . PHE B 1 351 ? 35.274  -6.162  21.161  1.00 26.44  ? 330 PHE B CZ  1 
ATOM   4801 N  N   . VAL B 1 352 ? 32.124  -12.303 22.895  1.00 26.79  ? 331 VAL B N   1 
ATOM   4802 C  CA  . VAL B 1 352 ? 31.516  -13.573 22.530  1.00 25.28  ? 331 VAL B CA  1 
ATOM   4803 C  C   . VAL B 1 352 ? 31.979  -13.948 21.130  1.00 31.67  ? 331 VAL B C   1 
ATOM   4804 O  O   . VAL B 1 352 ? 31.871  -13.153 20.188  1.00 32.52  ? 331 VAL B O   1 
ATOM   4805 C  CB  . VAL B 1 352 ? 29.985  -13.477 22.603  1.00 31.88  ? 331 VAL B CB  1 
ATOM   4806 C  CG1 . VAL B 1 352 ? 29.345  -14.733 22.018  1.00 30.11  ? 331 VAL B CG1 1 
ATOM   4807 C  CG2 . VAL B 1 352 ? 29.524  -13.263 24.038  1.00 33.96  ? 331 VAL B CG2 1 
ATOM   4808 N  N   . ALA B 1 353 ? 32.511  -15.158 20.988  1.00 25.24  ? 332 ALA B N   1 
ATOM   4809 C  CA  . ALA B 1 353 ? 32.941  -15.625 19.680  1.00 25.71  ? 332 ALA B CA  1 
ATOM   4810 C  C   . ALA B 1 353 ? 31.751  -15.726 18.736  1.00 28.05  ? 332 ALA B C   1 
ATOM   4811 O  O   . ALA B 1 353 ? 30.680  -16.213 19.106  1.00 25.99  ? 332 ALA B O   1 
ATOM   4812 C  CB  . ALA B 1 353 ? 33.633  -16.981 19.803  1.00 30.82  ? 332 ALA B CB  1 
ATOM   4813 N  N   . LYS B 1 354 ? 31.944  -15.266 17.510  1.00 31.51  ? 333 LYS B N   1 
ATOM   4814 C  CA  . LYS B 1 354 ? 30.894  -15.328 16.506  1.00 29.88  ? 333 LYS B CA  1 
ATOM   4815 C  C   . LYS B 1 354 ? 30.516  -16.784 16.264  1.00 33.01  ? 333 LYS B C   1 
ATOM   4816 O  O   . LYS B 1 354 ? 31.382  -17.581 15.875  1.00 26.76  ? 333 LYS B O   1 
ATOM   4817 C  CB  . LYS B 1 354 ? 31.382  -14.684 15.214  1.00 34.98  ? 333 LYS B CB  1 
ATOM   4818 C  CG  . LYS B 1 354 ? 30.348  -14.605 14.108  1.00 31.03  ? 333 LYS B CG  1 
ATOM   4819 C  CD  . LYS B 1 354 ? 30.993  -14.113 12.818  1.00 40.04  ? 333 LYS B CD  1 
ATOM   4820 C  CE  . LYS B 1 354 ? 29.970  -13.906 11.718  1.00 45.07  ? 333 LYS B CE  1 
ATOM   4821 N  NZ  . LYS B 1 354 ? 30.588  -13.245 10.531  1.00 57.82  ? 333 LYS B NZ  1 
ATOM   4822 N  N   . PRO B 1 355 ? 29.249  -17.178 16.468  1.00 35.83  ? 334 PRO B N   1 
ATOM   4823 C  CA  . PRO B 1 355 ? 28.869  -18.586 16.306  1.00 34.32  ? 334 PRO B CA  1 
ATOM   4824 C  C   . PRO B 1 355 ? 28.667  -18.999 14.854  1.00 41.28  ? 334 PRO B C   1 
ATOM   4825 O  O   . PRO B 1 355 ? 28.623  -18.169 13.945  1.00 44.69  ? 334 PRO B O   1 
ATOM   4826 C  CB  . PRO B 1 355 ? 27.553  -18.679 17.080  1.00 41.83  ? 334 PRO B CB  1 
ATOM   4827 C  CG  . PRO B 1 355 ? 26.966  -17.312 16.973  1.00 47.16  ? 334 PRO B CG  1 
ATOM   4828 C  CD  . PRO B 1 355 ? 28.130  -16.356 16.967  1.00 42.32  ? 334 PRO B CD  1 
ATOM   4829 O  OXT . PRO B 1 355 ? 28.544  -20.187 14.559  1.00 55.96  ? 334 PRO B OXT 1 
HETATM 4830 N  N1  . IMD C 2 .   ? 25.185  3.162   18.010  1.00 30.12  ? 401 IMD A N1  1 
HETATM 4831 C  C2  . IMD C 2 .   ? 24.345  4.171   17.846  1.00 31.47  ? 401 IMD A C2  1 
HETATM 4832 N  N3  . IMD C 2 .   ? 23.564  4.216   18.914  1.00 38.77  ? 401 IMD A N3  1 
HETATM 4833 C  C4  . IMD C 2 .   ? 23.914  3.219   19.786  1.00 31.58  ? 401 IMD A C4  1 
HETATM 4834 C  C5  . IMD C 2 .   ? 24.943  2.548   19.211  1.00 35.31  ? 401 IMD A C5  1 
HETATM 4835 CA CA  . CA  D 3 .   ? 53.016  -18.538 -9.215  1.00 22.18  ? 401 CA  B CA  1 
HETATM 4836 N  N1  . IMD E 2 .   ? 50.558  -11.945 30.976  1.00 58.82  ? 402 IMD B N1  1 
HETATM 4837 C  C2  . IMD E 2 .   ? 49.483  -11.470 31.584  1.00 51.40  ? 402 IMD B C2  1 
HETATM 4838 N  N3  . IMD E 2 .   ? 48.465  -12.248 31.255  1.00 45.86  ? 402 IMD B N3  1 
HETATM 4839 C  C4  . IMD E 2 .   ? 48.893  -13.243 30.417  1.00 44.59  ? 402 IMD B C4  1 
HETATM 4840 C  C5  . IMD E 2 .   ? 50.224  -13.052 30.240  1.00 52.87  ? 402 IMD B C5  1 
HETATM 4841 O  O   . HOH F 4 .   ? 36.241  -19.419 31.940  1.00 52.97  ? 501 HOH A O   1 
HETATM 4842 O  O   . HOH F 4 .   ? 21.498  -1.645  4.164   1.00 36.66  ? 502 HOH A O   1 
HETATM 4843 O  O   . HOH F 4 .   ? 34.097  11.185  22.933  1.00 31.59  ? 503 HOH A O   1 
HETATM 4844 O  O   . HOH F 4 .   ? 32.352  -7.483  5.278   1.00 30.13  ? 504 HOH A O   1 
HETATM 4845 O  O   . HOH F 4 .   ? 27.932  15.308  25.165  1.00 55.68  ? 505 HOH A O   1 
HETATM 4846 O  O   . HOH F 4 .   ? 38.416  -0.040  33.102  1.00 37.00  ? 506 HOH A O   1 
HETATM 4847 O  O   . HOH F 4 .   ? 17.909  13.599  -3.176  1.00 54.11  ? 507 HOH A O   1 
HETATM 4848 O  O   . HOH F 4 .   ? 33.538  -0.776  -5.691  1.00 25.10  ? 508 HOH A O   1 
HETATM 4849 O  O   . HOH F 4 .   ? 36.390  1.026   5.302   1.00 24.55  ? 509 HOH A O   1 
HETATM 4850 O  O   . HOH F 4 .   ? 16.208  -23.029 29.484  1.00 45.22  ? 510 HOH A O   1 
HETATM 4851 O  O   . HOH F 4 .   ? 40.344  -8.083  34.429  1.00 37.35  ? 511 HOH A O   1 
HETATM 4852 O  O   . HOH F 4 .   ? 24.544  -12.949 6.194   1.00 31.02  ? 512 HOH A O   1 
HETATM 4853 O  O   . HOH F 4 .   ? 37.160  19.635  4.290   1.00 35.53  ? 513 HOH A O   1 
HETATM 4854 O  O   . HOH F 4 .   ? 36.192  -6.170  -8.804  1.00 34.14  ? 514 HOH A O   1 
HETATM 4855 O  O   . HOH F 4 .   ? 34.312  -6.159  32.422  1.00 38.16  ? 515 HOH A O   1 
HETATM 4856 O  O   . HOH F 4 .   ? 29.707  -3.842  30.186  1.00 45.58  ? 516 HOH A O   1 
HETATM 4857 O  O   . HOH F 4 .   ? 23.407  16.406  2.067   1.00 29.31  ? 517 HOH A O   1 
HETATM 4858 O  O   . HOH F 4 .   ? 21.795  4.849   6.084   1.00 28.50  ? 518 HOH A O   1 
HETATM 4859 O  O   . HOH F 4 .   ? 33.342  -11.293 18.595  1.00 23.96  ? 519 HOH A O   1 
HETATM 4860 O  O   . HOH F 4 .   ? 15.004  3.076   5.489   1.00 42.80  ? 520 HOH A O   1 
HETATM 4861 O  O   . HOH F 4 .   ? -12.055 6.414   47.975  1.00 91.46  ? 521 HOH A O   1 
HETATM 4862 O  O   . HOH F 4 .   ? 34.813  12.400  20.605  1.00 25.31  ? 522 HOH A O   1 
HETATM 4863 O  O   . HOH F 4 .   ? 36.420  9.313   -3.014  1.00 23.24  ? 523 HOH A O   1 
HETATM 4864 O  O   . HOH F 4 .   ? 7.395   18.409  51.553  1.00 46.76  ? 524 HOH A O   1 
HETATM 4865 O  O   . HOH F 4 .   ? 10.781  -5.357  14.541  1.00 37.05  ? 525 HOH A O   1 
HETATM 4866 O  O   . HOH F 4 .   ? 25.159  -11.817 16.880  1.00 18.23  ? 526 HOH A O   1 
HETATM 4867 O  O   . HOH F 4 .   ? 20.589  5.931   8.594   1.00 20.43  ? 527 HOH A O   1 
HETATM 4868 O  O   . HOH F 4 .   ? 28.417  -11.614 10.132  1.00 31.63  ? 528 HOH A O   1 
HETATM 4869 O  O   . HOH F 4 .   ? 44.567  -2.773  31.395  1.00 44.38  ? 529 HOH A O   1 
HETATM 4870 O  O   . HOH F 4 .   ? 28.601  8.321   -6.293  1.00 30.48  ? 530 HOH A O   1 
HETATM 4871 O  O   . HOH F 4 .   ? 30.921  -9.681  23.245  1.00 21.35  ? 531 HOH A O   1 
HETATM 4872 O  O   . HOH F 4 .   ? 6.971   -10.333 27.956  1.00 58.14  ? 532 HOH A O   1 
HETATM 4873 O  O   . HOH F 4 .   ? 21.952  18.341  10.511  1.00 27.78  ? 533 HOH A O   1 
HETATM 4874 O  O   . HOH F 4 .   ? 31.786  -6.811  -3.807  1.00 30.02  ? 534 HOH A O   1 
HETATM 4875 O  O   . HOH F 4 .   ? 32.482  -4.860  13.474  1.00 19.93  ? 535 HOH A O   1 
HETATM 4876 O  O   . HOH F 4 .   ? 30.326  -10.126 6.093   1.00 37.25  ? 536 HOH A O   1 
HETATM 4877 O  O   . HOH F 4 .   ? 32.761  5.457   -8.352  1.00 41.14  ? 537 HOH A O   1 
HETATM 4878 O  O   . HOH F 4 .   ? 27.712  9.587   17.010  1.00 30.63  ? 538 HOH A O   1 
HETATM 4879 O  O   . HOH F 4 .   ? 46.185  9.992   25.867  1.00 28.98  ? 539 HOH A O   1 
HETATM 4880 O  O   . HOH F 4 .   ? 31.526  -2.253  -3.715  1.00 27.03  ? 540 HOH A O   1 
HETATM 4881 O  O   . HOH F 4 .   ? 35.706  4.518   13.659  1.00 30.22  ? 541 HOH A O   1 
HETATM 4882 O  O   . HOH F 4 .   ? 6.666   -12.347 25.366  1.00 56.34  ? 542 HOH A O   1 
HETATM 4883 O  O   . HOH F 4 .   ? 23.144  14.739  -2.781  1.00 43.52  ? 543 HOH A O   1 
HETATM 4884 O  O   . HOH F 4 .   ? 40.023  -2.173  26.242  1.00 31.16  ? 544 HOH A O   1 
HETATM 4885 O  O   . HOH F 4 .   ? 10.331  8.134   46.684  1.00 59.92  ? 545 HOH A O   1 
HETATM 4886 O  O   . HOH F 4 .   ? 26.813  3.550   -4.646  1.00 29.21  ? 546 HOH A O   1 
HETATM 4887 O  O   . HOH F 4 .   ? 6.348   -6.117  32.288  1.00 65.15  ? 547 HOH A O   1 
HETATM 4888 O  O   . HOH F 4 .   ? 30.117  17.265  1.637   1.00 29.90  ? 548 HOH A O   1 
HETATM 4889 O  O   . HOH F 4 .   ? 38.581  -4.175  27.355  1.00 29.87  ? 549 HOH A O   1 
HETATM 4890 O  O   . HOH F 4 .   ? 22.756  -24.671 26.899  1.00 52.90  ? 550 HOH A O   1 
HETATM 4891 O  O   . HOH F 4 .   ? -2.740  9.528   34.878  1.00 68.33  ? 551 HOH A O   1 
HETATM 4892 O  O   . HOH F 4 .   ? 15.681  4.888   28.936  1.00 64.21  ? 552 HOH A O   1 
HETATM 4893 O  O   . HOH F 4 .   ? 35.866  -2.713  -9.225  1.00 40.25  ? 553 HOH A O   1 
HETATM 4894 O  O   . HOH F 4 .   ? 9.397   -13.243 23.011  1.00 48.26  ? 554 HOH A O   1 
HETATM 4895 O  O   . HOH F 4 .   ? 17.436  -5.218  8.622   1.00 52.64  ? 555 HOH A O   1 
HETATM 4896 O  O   . HOH F 4 .   ? 18.427  15.707  6.478   1.00 48.82  ? 556 HOH A O   1 
HETATM 4897 O  O   . HOH F 4 .   ? 17.639  -11.528 15.104  1.00 37.40  ? 557 HOH A O   1 
HETATM 4898 O  O   . HOH F 4 .   ? 41.941  2.718   28.535  1.00 42.91  ? 558 HOH A O   1 
HETATM 4899 O  O   . HOH F 4 .   ? 41.410  5.721   28.402  1.00 42.09  ? 559 HOH A O   1 
HETATM 4900 O  O   . HOH F 4 .   ? 26.112  -7.241  -0.456  1.00 39.33  ? 560 HOH A O   1 
HETATM 4901 O  O   . HOH F 4 .   ? 17.289  10.578  3.928   1.00 43.90  ? 561 HOH A O   1 
HETATM 4902 O  O   . HOH F 4 .   ? 17.973  -3.596  42.419  1.00 52.80  ? 562 HOH A O   1 
HETATM 4903 O  O   . HOH F 4 .   ? 21.747  -2.472  28.045  1.00 35.57  ? 563 HOH A O   1 
HETATM 4904 O  O   . HOH F 4 .   ? 21.522  -1.826  51.892  1.00 37.15  ? 564 HOH A O   1 
HETATM 4905 O  O   . HOH F 4 .   ? 22.492  0.948   26.602  1.00 49.39  ? 565 HOH A O   1 
HETATM 4906 O  O   . HOH F 4 .   ? 22.238  2.670   -0.753  1.00 42.50  ? 566 HOH A O   1 
HETATM 4907 O  O   . HOH F 4 .   ? 5.536   -12.927 28.053  1.00 54.87  ? 567 HOH A O   1 
HETATM 4908 O  O   . HOH F 4 .   ? 26.413  -15.830 11.542  1.00 34.08  ? 568 HOH A O   1 
HETATM 4909 O  O   . HOH F 4 .   ? 21.574  -0.286  0.723   1.00 44.73  ? 569 HOH A O   1 
HETATM 4910 O  O   . HOH F 4 .   ? 13.169  7.313   18.114  1.00 54.10  ? 570 HOH A O   1 
HETATM 4911 O  O   . HOH F 4 .   ? 32.661  -4.271  -2.566  1.00 28.39  ? 571 HOH A O   1 
HETATM 4912 O  O   . HOH F 4 .   ? 38.102  3.087   13.278  1.00 33.43  ? 572 HOH A O   1 
HETATM 4913 O  O   . HOH F 4 .   ? 24.132  3.206   24.637  1.00 48.34  ? 573 HOH A O   1 
HETATM 4914 O  O   . HOH F 4 .   ? 19.478  -5.475  36.757  1.00 62.20  ? 574 HOH A O   1 
HETATM 4915 O  O   . HOH F 4 .   ? 18.478  -2.337  5.468   1.00 49.56  ? 575 HOH A O   1 
HETATM 4916 O  O   . HOH F 4 .   ? 31.234  -0.652  43.669  1.00 43.53  ? 576 HOH A O   1 
HETATM 4917 O  O   . HOH F 4 .   ? 14.769  -4.854  8.778   1.00 52.29  ? 577 HOH A O   1 
HETATM 4918 O  O   . HOH F 4 .   ? 30.248  -3.365  -5.729  1.00 39.48  ? 578 HOH A O   1 
HETATM 4919 O  O   . HOH F 4 .   ? 32.942  -10.163 5.966   1.00 41.46  ? 579 HOH A O   1 
HETATM 4920 O  O   . HOH F 4 .   ? 26.807  -14.118 7.161   1.00 33.14  ? 580 HOH A O   1 
HETATM 4921 O  O   . HOH G 4 .   ? 39.985  -16.859 -13.014 1.00 31.95  ? 501 HOH B O   1 
HETATM 4922 O  O   . HOH G 4 .   ? 34.401  -17.225 23.107  1.00 41.36  ? 502 HOH B O   1 
HETATM 4923 O  O   . HOH G 4 .   ? 47.456  -13.976 11.535  1.00 29.40  ? 503 HOH B O   1 
HETATM 4924 O  O   . HOH G 4 .   ? 57.539  -20.712 -2.384  1.00 49.83  ? 504 HOH B O   1 
HETATM 4925 O  O   . HOH G 4 .   ? 37.052  -12.798 6.416   1.00 39.15  ? 505 HOH B O   1 
HETATM 4926 O  O   . HOH G 4 .   ? 38.387  -11.119 2.508   1.00 28.89  ? 506 HOH B O   1 
HETATM 4927 O  O   . HOH G 4 .   ? 53.902  -8.267  14.043  1.00 24.75  ? 507 HOH B O   1 
HETATM 4928 O  O   . HOH G 4 .   ? 59.160  2.424   22.352  1.00 62.74  ? 508 HOH B O   1 
HETATM 4929 O  O   . HOH G 4 .   ? 51.682  3.105   13.288  1.00 38.50  ? 509 HOH B O   1 
HETATM 4930 O  O   . HOH G 4 .   ? 41.578  -13.293 -17.966 1.00 37.94  ? 510 HOH B O   1 
HETATM 4931 O  O   . HOH G 4 .   ? 45.506  -15.411 -8.959  1.00 27.44  ? 511 HOH B O   1 
HETATM 4932 O  O   . HOH G 4 .   ? 55.382  -11.972 20.509  1.00 39.03  ? 512 HOH B O   1 
HETATM 4933 O  O   . HOH G 4 .   ? 54.398  1.326   -3.739  1.00 42.77  ? 513 HOH B O   1 
HETATM 4934 O  O   . HOH G 4 .   ? 46.787  -12.288 -5.042  1.00 22.29  ? 514 HOH B O   1 
HETATM 4935 O  O   . HOH G 4 .   ? 36.133  14.088  -8.394  1.00 36.98  ? 515 HOH B O   1 
HETATM 4936 O  O   . HOH G 4 .   ? 47.883  -18.797 -3.164  1.00 23.05  ? 516 HOH B O   1 
HETATM 4937 O  O   . HOH G 4 .   ? 37.975  10.323  1.359   1.00 30.02  ? 517 HOH B O   1 
HETATM 4938 O  O   . HOH G 4 .   ? 34.131  -6.993  14.312  1.00 25.27  ? 518 HOH B O   1 
HETATM 4939 O  O   . HOH G 4 .   ? 48.133  10.669  14.378  1.00 28.20  ? 519 HOH B O   1 
HETATM 4940 O  O   . HOH G 4 .   ? 36.041  -10.985 9.804   1.00 31.80  ? 520 HOH B O   1 
HETATM 4941 O  O   . HOH G 4 .   ? 44.373  -13.462 27.224  1.00 32.01  ? 521 HOH B O   1 
HETATM 4942 O  O   . HOH G 4 .   ? 52.150  17.756  15.955  1.00 57.25  ? 522 HOH B O   1 
HETATM 4943 O  O   . HOH G 4 .   ? 58.313  -14.379 -9.366  1.00 32.19  ? 523 HOH B O   1 
HETATM 4944 O  O   . HOH G 4 .   ? 36.474  -2.550  -1.793  1.00 18.38  ? 524 HOH B O   1 
HETATM 4945 O  O   . HOH G 4 .   ? 39.119  -6.730  27.809  1.00 23.82  ? 525 HOH B O   1 
HETATM 4946 O  O   . HOH G 4 .   ? 67.663  -4.989  -5.151  1.00 53.04  ? 526 HOH B O   1 
HETATM 4947 O  O   . HOH G 4 .   ? 36.983  -4.689  16.600  1.00 20.54  ? 527 HOH B O   1 
HETATM 4948 O  O   . HOH G 4 .   ? 40.767  -2.225  -19.158 1.00 49.59  ? 528 HOH B O   1 
HETATM 4949 O  O   . HOH G 4 .   ? 52.619  2.405   -5.287  1.00 40.27  ? 529 HOH B O   1 
HETATM 4950 O  O   . HOH G 4 .   ? 51.664  -16.882 20.523  1.00 52.09  ? 530 HOH B O   1 
HETATM 4951 O  O   . HOH G 4 .   ? 40.507  0.073   -4.241  1.00 14.45  ? 531 HOH B O   1 
HETATM 4952 O  O   . HOH G 4 .   ? 50.016  -3.024  28.840  1.00 31.08  ? 532 HOH B O   1 
HETATM 4953 O  O   . HOH G 4 .   ? 43.090  15.033  4.056   1.00 30.17  ? 533 HOH B O   1 
HETATM 4954 O  O   . HOH G 4 .   ? 39.350  -3.605  6.117   1.00 19.93  ? 534 HOH B O   1 
HETATM 4955 O  O   . HOH G 4 .   ? 35.674  -14.849 21.398  1.00 30.69  ? 535 HOH B O   1 
HETATM 4956 O  O   . HOH G 4 .   ? 55.189  -14.802 13.092  1.00 44.33  ? 536 HOH B O   1 
HETATM 4957 O  O   . HOH G 4 .   ? 41.800  -12.693 28.263  1.00 25.15  ? 537 HOH B O   1 
HETATM 4958 O  O   . HOH G 4 .   ? 42.312  -8.203  -3.182  1.00 19.90  ? 538 HOH B O   1 
HETATM 4959 O  O   . HOH G 4 .   ? 52.685  -7.950  31.820  1.00 50.83  ? 539 HOH B O   1 
HETATM 4960 O  O   . HOH G 4 .   ? 62.669  -21.302 3.321   1.00 62.58  ? 540 HOH B O   1 
HETATM 4961 O  O   . HOH G 4 .   ? 37.158  -3.241  4.370   1.00 19.62  ? 541 HOH B O   1 
HETATM 4962 O  O   . HOH G 4 .   ? 38.128  3.796   -12.646 1.00 35.11  ? 542 HOH B O   1 
HETATM 4963 O  O   . HOH G 4 .   ? 30.137  -11.789 8.173   1.00 44.75  ? 543 HOH B O   1 
HETATM 4964 O  O   . HOH G 4 .   ? 35.566  -10.385 -10.176 1.00 40.69  ? 544 HOH B O   1 
HETATM 4965 O  O   . HOH G 4 .   ? 51.595  -9.727  15.067  1.00 29.22  ? 545 HOH B O   1 
HETATM 4966 O  O   . HOH G 4 .   ? 38.429  9.679   -1.234  1.00 32.39  ? 546 HOH B O   1 
HETATM 4967 O  O   . HOH G 4 .   ? 40.574  2.549   13.464  1.00 38.32  ? 547 HOH B O   1 
HETATM 4968 O  O   . HOH G 4 .   ? 34.222  -17.305 15.903  1.00 37.39  ? 548 HOH B O   1 
HETATM 4969 O  O   . HOH G 4 .   ? 51.994  -14.288 18.791  1.00 39.55  ? 549 HOH B O   1 
HETATM 4970 O  O   . HOH G 4 .   ? 48.055  -13.455 -3.049  1.00 23.27  ? 550 HOH B O   1 
HETATM 4971 O  O   . HOH G 4 .   ? 62.004  3.826   -20.902 1.00 48.12  ? 551 HOH B O   1 
HETATM 4972 O  O   . HOH G 4 .   ? 47.088  7.179   -2.181  1.00 49.78  ? 552 HOH B O   1 
HETATM 4973 O  O   . HOH G 4 .   ? 37.060  -15.118 18.902  1.00 24.43  ? 553 HOH B O   1 
HETATM 4974 O  O   . HOH G 4 .   ? 56.460  -14.902 -0.427  1.00 28.20  ? 554 HOH B O   1 
HETATM 4975 O  O   . HOH G 4 .   ? 59.207  1.279   19.972  1.00 51.56  ? 555 HOH B O   1 
HETATM 4976 O  O   . HOH G 4 .   ? 61.164  -16.198 -4.919  1.00 41.57  ? 556 HOH B O   1 
HETATM 4977 O  O   . HOH G 4 .   ? 39.575  -9.720  -19.072 1.00 32.49  ? 557 HOH B O   1 
HETATM 4978 O  O   . HOH G 4 .   ? 52.702  8.509   6.573   1.00 47.63  ? 558 HOH B O   1 
HETATM 4979 O  O   . HOH G 4 .   ? 45.629  6.619   -4.186  1.00 43.00  ? 559 HOH B O   1 
HETATM 4980 O  O   . HOH G 4 .   ? 39.333  -16.822 3.346   1.00 29.01  ? 560 HOH B O   1 
HETATM 4981 O  O   . HOH G 4 .   ? 46.918  -11.457 -19.082 1.00 37.51  ? 561 HOH B O   1 
HETATM 4982 O  O   . HOH G 4 .   ? 52.676  -16.723 -10.536 1.00 26.17  ? 562 HOH B O   1 
HETATM 4983 O  O   . HOH G 4 .   ? 51.525  -17.051 0.512   1.00 34.11  ? 563 HOH B O   1 
HETATM 4984 O  O   . HOH G 4 .   ? 57.705  -16.870 -9.429  1.00 30.42  ? 564 HOH B O   1 
HETATM 4985 O  O   . HOH G 4 .   ? 47.537  -15.909 -10.625 1.00 35.05  ? 565 HOH B O   1 
HETATM 4986 O  O   . HOH G 4 .   ? 35.593  3.748   -12.183 1.00 37.40  ? 566 HOH B O   1 
HETATM 4987 O  O   . HOH G 4 .   ? 32.066  -17.117 23.184  1.00 32.48  ? 567 HOH B O   1 
HETATM 4988 O  O   . HOH G 4 .   ? 53.773  3.430   -1.564  1.00 41.62  ? 568 HOH B O   1 
HETATM 4989 O  O   . HOH G 4 .   ? 40.387  0.727   -15.090 1.00 42.69  ? 569 HOH B O   1 
HETATM 4990 O  O   . HOH G 4 .   ? 37.930  0.664   12.190  1.00 30.19  ? 570 HOH B O   1 
HETATM 4991 O  O   . HOH G 4 .   ? 54.617  2.212   25.348  1.00 40.80  ? 571 HOH B O   1 
HETATM 4992 O  O   . HOH G 4 .   ? 75.727  5.713   -4.293  1.00 65.91  ? 572 HOH B O   1 
HETATM 4993 O  O   . HOH G 4 .   ? 51.170  -15.982 26.438  1.00 41.30  ? 573 HOH B O   1 
HETATM 4994 O  O   . HOH G 4 .   ? 50.887  4.228   -10.266 1.00 73.07  ? 574 HOH B O   1 
HETATM 4995 O  O   . HOH G 4 .   ? 42.123  16.440  6.223   1.00 31.16  ? 575 HOH B O   1 
HETATM 4996 O  O   . HOH G 4 .   ? 53.411  4.052   2.184   1.00 60.54  ? 576 HOH B O   1 
HETATM 4997 O  O   . HOH G 4 .   ? 55.522  -19.752 5.326   1.00 34.74  ? 577 HOH B O   1 
HETATM 4998 O  O   . HOH G 4 .   ? 54.852  -0.521  25.394  1.00 38.26  ? 578 HOH B O   1 
HETATM 4999 O  O   . HOH G 4 .   ? 54.714  0.733   3.914   1.00 53.13  ? 579 HOH B O   1 
HETATM 5000 O  O   . HOH G 4 .   ? 33.842  17.773  3.886   1.00 42.85  ? 580 HOH B O   1 
HETATM 5001 O  O   . HOH G 4 .   ? 55.860  -8.614  23.647  1.00 39.56  ? 581 HOH B O   1 
HETATM 5002 O  O   . HOH G 4 .   ? 27.122  -13.778 9.768   1.00 28.63  ? 582 HOH B O   1 
HETATM 5003 O  O   . HOH G 4 .   ? 35.474  -14.835 16.714  1.00 37.82  ? 583 HOH B O   1 
HETATM 5004 O  O   . HOH G 4 .   ? 39.004  1.320   -13.039 1.00 33.74  ? 584 HOH B O   1 
HETATM 5005 O  O   . HOH G 4 .   ? 50.551  -16.949 12.017  1.00 39.81  ? 585 HOH B O   1 
HETATM 5006 O  O   . HOH G 4 .   ? 49.691  -5.113  -24.242 1.00 34.30  ? 586 HOH B O   1 
HETATM 5007 O  O   . HOH G 4 .   ? 48.171  -13.499 -17.264 1.00 38.90  ? 587 HOH B O   1 
HETATM 5008 O  O   . HOH G 4 .   ? 43.842  -15.352 25.509  1.00 35.40  ? 588 HOH B O   1 
HETATM 5009 O  O   . HOH G 4 .   ? 39.055  -19.669 2.406   1.00 39.86  ? 589 HOH B 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   . LYS A 24  ? 0.4661 0.6501 0.8262 -0.0290 -0.0076 0.0522  3   LYS A N   
2    C CA  . LYS A 24  ? 0.4259 0.5984 0.7926 -0.0295 0.0044  0.0451  3   LYS A CA  
3    C C   . LYS A 24  ? 0.3800 0.5284 0.7435 -0.0251 -0.0009 0.0541  3   LYS A C   
4    O O   . LYS A 24  ? 0.3591 0.4928 0.7012 -0.0282 -0.0074 0.0649  3   LYS A O   
5    C CB  . LYS A 24  ? 0.3589 0.5256 0.7048 -0.0426 0.0197  0.0368  3   LYS A CB  
6    C CG  . LYS A 24  ? 0.4875 0.6759 0.8436 -0.0473 0.0296  0.0243  3   LYS A CG  
7    C CD  . LYS A 24  ? 0.4743 0.6507 0.8117 -0.0564 0.0489  0.0158  3   LYS A CD  
8    C CE  . LYS A 24  ? 0.6466 0.8217 0.9569 -0.0685 0.0523  0.0155  3   LYS A CE  
9    N NZ  . LYS A 24  ? 0.6175 0.7841 0.9127 -0.0745 0.0715  0.0074  3   LYS A NZ  
10   N N   . PRO A 25  ? 0.3596 0.4985 0.7356 -0.0174 0.0025  0.0484  4   PRO A N   
11   C CA  . PRO A 25  ? 0.3743 0.4840 0.7363 -0.0146 -0.0032 0.0531  4   PRO A CA  
12   C C   . PRO A 25  ? 0.3566 0.4474 0.6850 -0.0255 0.0016  0.0525  4   PRO A C   
13   O O   . PRO A 25  ? 0.3059 0.3986 0.6208 -0.0321 0.0145  0.0436  4   PRO A O   
14   C CB  . PRO A 25  ? 0.3914 0.4920 0.7663 -0.0057 0.0032  0.0421  4   PRO A CB  
15   C CG  . PRO A 25  ? 0.3983 0.5271 0.8008 -0.0001 0.0099  0.0365  4   PRO A CG  
16   C CD  . PRO A 25  ? 0.4172 0.5666 0.8142 -0.0111 0.0130  0.0360  4   PRO A CD  
17   N N   . ILE A 26  ? 0.3674 0.4404 0.6837 -0.0265 -0.0080 0.0632  5   ILE A N   
18   C CA  . ILE A 26  ? 0.3316 0.3885 0.6181 -0.0352 -0.0057 0.0660  5   ILE A CA  
19   C C   . ILE A 26  ? 0.2914 0.3283 0.5685 -0.0342 -0.0060 0.0565  5   ILE A C   
20   O O   . ILE A 26  ? 0.2422 0.2687 0.5328 -0.0289 -0.0144 0.0566  5   ILE A O   
21   C CB  . ILE A 26  ? 0.3430 0.3949 0.6237 -0.0374 -0.0159 0.0848  5   ILE A CB  
22   C CG1 . ILE A 26  ? 0.3969 0.4641 0.6769 -0.0380 -0.0147 0.0915  5   ILE A CG1 
23   C CG2 . ILE A 26  ? 0.3314 0.3690 0.5846 -0.0448 -0.0138 0.0896  5   ILE A CG2 
24   C CD1 . ILE A 26  ? 0.3073 0.3644 0.5703 -0.0332 -0.0234 0.1069  5   ILE A CD1 
25   N N   . VAL A 27  ? 0.3055 0.3357 0.5579 -0.0394 0.0042  0.0478  6   VAL A N   
26   C CA  . VAL A 27  ? 0.3098 0.3210 0.5456 -0.0396 0.0043  0.0369  6   VAL A CA  
27   C C   . VAL A 27  ? 0.3036 0.3072 0.5103 -0.0470 0.0016  0.0445  6   VAL A C   
28   O O   . VAL A 27  ? 0.2972 0.3080 0.4885 -0.0507 0.0115  0.0493  6   VAL A O   
29   C CB  . VAL A 27  ? 0.3921 0.4023 0.6222 -0.0364 0.0203  0.0194  6   VAL A CB  
30   C CG1 . VAL A 27  ? 0.4135 0.4009 0.6222 -0.0362 0.0197  0.0069  6   VAL A CG1 
31   C CG2 . VAL A 27  ? 0.3860 0.4095 0.6488 -0.0284 0.0244  0.0146  6   VAL A CG2 
32   N N   . PHE A 28  ? 0.2787 0.2684 0.4794 -0.0493 -0.0111 0.0460  7   PHE A N   
33   C CA  . PHE A 28  ? 0.3144 0.3004 0.4911 -0.0557 -0.0164 0.0547  7   PHE A CA  
34   C C   . PHE A 28  ? 0.3674 0.3395 0.5203 -0.0575 -0.0175 0.0394  7   PHE A C   
35   O O   . PHE A 28  ? 0.3512 0.3104 0.5119 -0.0564 -0.0236 0.0270  7   PHE A O   
36   C CB  . PHE A 28  ? 0.2978 0.2826 0.4891 -0.0583 -0.0324 0.0715  7   PHE A CB  
37   C CG  . PHE A 28  ? 0.3111 0.2971 0.4830 -0.0642 -0.0378 0.0843  7   PHE A CG  
38   C CD1 . PHE A 28  ? 0.3081 0.2861 0.4686 -0.0690 -0.0492 0.0790  7   PHE A CD1 
39   C CD2 . PHE A 28  ? 0.2687 0.2641 0.4341 -0.0648 -0.0312 0.1019  7   PHE A CD2 
40   C CE1 . PHE A 28  ? 0.3134 0.2973 0.4590 -0.0737 -0.0553 0.0925  7   PHE A CE1 
41   C CE2 . PHE A 28  ? 0.2675 0.2654 0.4174 -0.0683 -0.0346 0.1162  7   PHE A CE2 
42   C CZ  . PHE A 28  ? 0.2955 0.2897 0.4366 -0.0724 -0.0474 0.1122  7   PHE A CZ  
43   N N   . SER A 29  ? 0.2709 0.2446 0.3933 -0.0597 -0.0107 0.0404  8   SER A N   
44   C CA  . SER A 29  ? 0.3047 0.2667 0.3979 -0.0611 -0.0128 0.0272  8   SER A CA  
45   C C   . SER A 29  ? 0.3177 0.2861 0.3874 -0.0653 -0.0188 0.0410  8   SER A C   
46   O O   . SER A 29  ? 0.3349 0.3138 0.3969 -0.0640 -0.0078 0.0547  8   SER A O   
47   C CB  . SER A 29  ? 0.3883 0.3452 0.4635 -0.0555 0.0069  0.0114  8   SER A CB  
48   O OG  . SER A 29  ? 0.6436 0.5852 0.6895 -0.0558 0.0043  -0.0037 8   SER A OG  
49   N N   . GLY A 30  ? 0.3284 0.2911 0.3876 -0.0706 -0.0358 0.0377  9   GLY A N   
50   C CA  . GLY A 30  ? 0.3850 0.3570 0.4221 -0.0739 -0.0436 0.0503  9   GLY A CA  
51   C C   . GLY A 30  ? 0.4563 0.4229 0.4519 -0.0714 -0.0376 0.0373  9   GLY A C   
52   O O   . GLY A 30  ? 0.5098 0.4609 0.4935 -0.0717 -0.0393 0.0157  9   GLY A O   
53   N N   . ALA A 31  ? 0.3729 0.3507 0.3447 -0.0680 -0.0292 0.0512  10  ALA A N   
54   C CA  . ALA A 31  ? 0.4269 0.4014 0.3557 -0.0634 -0.0218 0.0431  10  ALA A CA  
55   C C   . ALA A 31  ? 0.4198 0.4090 0.3308 -0.0661 -0.0378 0.0581  10  ALA A C   
56   O O   . ALA A 31  ? 0.3969 0.4013 0.3171 -0.0650 -0.0359 0.0821  10  ALA A O   
57   C CB  . ALA A 31  ? 0.4722 0.4468 0.3871 -0.0546 0.0072  0.0469  10  ALA A CB  
58   N N   . GLN A 32  ? 0.5240 0.5091 0.4096 -0.0695 -0.0532 0.0442  11  GLN A N   
59   C CA  . GLN A 32  ? 0.4733 0.4766 0.3408 -0.0719 -0.0702 0.0576  11  GLN A CA  
60   C C   . GLN A 32  ? 0.5483 0.5616 0.3844 -0.0601 -0.0506 0.0736  11  GLN A C   
61   O O   . GLN A 32  ? 0.5770 0.5775 0.3894 -0.0516 -0.0282 0.0636  11  GLN A O   
62   C CB  . GLN A 32  ? 0.5679 0.5636 0.4098 -0.0786 -0.0906 0.0355  11  GLN A CB  
63   C CG  . GLN A 32  ? 0.6609 0.6782 0.5050 -0.0878 -0.1193 0.0462  11  GLN A CG  
64   C CD  . GLN A 32  ? 0.5820 0.6022 0.4752 -0.1000 -0.1374 0.0505  11  GLN A CD  
65   O OE1 . GLN A 32  ? 0.5970 0.5990 0.5166 -0.1023 -0.1319 0.0396  11  GLN A OE1 
66   N NE2 . GLN A 32  ? 0.5429 0.5871 0.4498 -0.1069 -0.1584 0.0677  11  GLN A NE2 
67   N N   . PRO A 33  ? 0.4817 0.5172 0.3188 -0.0586 -0.0562 0.0998  12  PRO A N   
68   C CA  . PRO A 33  ? 0.5195 0.5633 0.3234 -0.0459 -0.0363 0.1161  12  PRO A CA  
69   C C   . PRO A 33  ? 0.6535 0.7010 0.4105 -0.0417 -0.0454 0.1071  12  PRO A C   
70   O O   . PRO A 33  ? 0.6836 0.7533 0.4254 -0.0393 -0.0582 0.1240  12  PRO A O   
71   C CB  . PRO A 33  ? 0.4890 0.5545 0.3152 -0.0456 -0.0399 0.1483  12  PRO A CB  
72   C CG  . PRO A 33  ? 0.5126 0.5878 0.3682 -0.0584 -0.0712 0.1469  12  PRO A CG  
73   C CD  . PRO A 33  ? 0.5007 0.5535 0.3727 -0.0665 -0.0758 0.1188  12  PRO A CD  
74   N N   . SER A 34  ? 0.6713 0.6972 0.4038 -0.0400 -0.0385 0.0805  13  SER A N   
75   C CA  . SER A 34  ? 0.9356 0.9591 0.6178 -0.0354 -0.0453 0.0676  13  SER A CA  
76   C C   . SER A 34  ? 1.1172 1.1285 0.7608 -0.0194 -0.0131 0.0671  13  SER A C   
77   O O   . SER A 34  ? 1.0290 1.0482 0.6290 -0.0099 -0.0128 0.0730  13  SER A O   
78   C CB  . SER A 34  ? 1.0004 1.0042 0.6786 -0.0459 -0.0629 0.0353  13  SER A CB  
79   O OG  . SER A 34  ? 1.1074 1.0853 0.7971 -0.0438 -0.0418 0.0179  13  SER A OG  
80   N N   . GLY A 35  ? 1.1784 1.1719 0.8378 -0.0157 0.0142  0.0609  14  GLY A N   
81   C CA  . GLY A 35  ? 1.1817 1.1626 0.8098 -0.0013 0.0473  0.0606  14  GLY A CA  
82   C C   . GLY A 35  ? 1.3428 1.3034 0.9279 0.0041  0.0504  0.0359  14  GLY A C   
83   O O   . GLY A 35  ? 1.3801 1.3332 0.9275 0.0182  0.0742  0.0386  14  GLY A O   
84   N N   . GLU A 36  ? 1.4792 1.4279 1.0677 -0.0061 0.0292  0.0119  15  GLU A N   
85   C CA  . GLU A 36  ? 1.5161 1.4418 1.0607 -0.0020 0.0304  -0.0135 15  GLU A CA  
86   C C   . GLU A 36  ? 1.4446 1.3451 1.0137 -0.0075 0.0365  -0.0379 15  GLU A C   
87   O O   . GLU A 36  ? 1.5436 1.4275 1.0996 -0.0143 0.0205  -0.0608 15  GLU A O   
88   C CB  . GLU A 36  ? 1.6198 1.5536 1.1326 -0.0089 -0.0037 -0.0210 15  GLU A CB  
89   C CG  . GLU A 36  ? 1.6516 1.5937 1.2043 -0.0279 -0.0365 -0.0265 15  GLU A CG  
90   C CD  . GLU A 36  ? 1.8487 1.7840 1.3697 -0.0379 -0.0659 -0.0488 15  GLU A CD  
91   O OE1 . GLU A 36  ? 1.8635 1.7819 1.3303 -0.0300 -0.0595 -0.0647 15  GLU A OE1 
92   O OE2 . GLU A 36  ? 1.8133 1.7592 1.3632 -0.0539 -0.0947 -0.0510 15  GLU A OE2 
93   N N   . LEU A 37  ? 1.2106 1.1082 0.8163 -0.0048 0.0603  -0.0330 16  LEU A N   
94   C CA  . LEU A 37  ? 1.0831 0.9595 0.7119 -0.0067 0.0701  -0.0536 16  LEU A CA  
95   C C   . LEU A 37  ? 1.0701 0.9193 0.6519 0.0027  0.0843  -0.0749 16  LEU A C   
96   O O   . LEU A 37  ? 1.0520 0.8978 0.5937 0.0153  0.1035  -0.0698 16  LEU A O   
97   C CB  . LEU A 37  ? 0.9521 0.8337 0.6219 -0.0035 0.0959  -0.0438 16  LEU A CB  
98   C CG  . LEU A 37  ? 1.0750 0.9681 0.8029 -0.0142 0.0841  -0.0385 16  LEU A CG  
99   C CD1 . LEU A 37  ? 1.0484 0.9495 0.8079 -0.0108 0.1097  -0.0280 16  LEU A CD1 
100  C CD2 . LEU A 37  ? 1.0268 0.9031 0.7725 -0.0197 0.0731  -0.0599 16  LEU A CD2 
101  N N   . THR A 38  ? 1.0242 0.8517 0.6092 -0.0026 0.0765  -0.0982 17  THR A N   
102  C CA  . THR A 38  ? 1.0499 0.8465 0.5930 0.0064  0.0925  -0.1200 17  THR A CA  
103  C C   . THR A 38  ? 0.9622 0.7457 0.5366 0.0137  0.1229  -0.1259 17  THR A C   
104  O O   . THR A 38  ? 0.9012 0.6966 0.5308 0.0082  0.1230  -0.1196 17  THR A O   
105  C CB  . THR A 38  ? 1.1737 0.9502 0.6965 -0.0035 0.0677  -0.1437 17  THR A CB  
106  O OG1 . THR A 38  ? 1.1152 0.8825 0.6865 -0.0115 0.0643  -0.1532 17  THR A OG1 
107  C CG2 . THR A 38  ? 1.1710 0.9681 0.6807 -0.0151 0.0323  -0.1366 17  THR A CG2 
108  N N   . ILE A 39  ? 0.9839 0.7436 0.5219 0.0268  0.1489  -0.1374 18  ILE A N   
109  C CA  . ILE A 39  ? 0.9815 0.7305 0.5496 0.0347  0.1796  -0.1422 18  ILE A CA  
110  C C   . ILE A 39  ? 0.9591 0.6978 0.5666 0.0271  0.1699  -0.1562 18  ILE A C   
111  O O   . ILE A 39  ? 0.9787 0.7226 0.6334 0.0295  0.1861  -0.1539 18  ILE A O   
112  C CB  . ILE A 39  ? 0.9667 0.6887 0.4857 0.0510  0.2098  -0.1525 18  ILE A CB  
113  C CG1 . ILE A 39  ? 1.0546 0.7461 0.5172 0.0512  0.1968  -0.1749 18  ILE A CG1 
114  C CG2 . ILE A 39  ? 1.0569 0.7912 0.5468 0.0608  0.2258  -0.1345 18  ILE A CG2 
115  C CD1 . ILE A 39  ? 1.1010 0.7646 0.5784 0.0499  0.2013  -0.1964 18  ILE A CD1 
116  N N   . GLY A 40  ? 0.9964 0.7213 0.5867 0.0178  0.1437  -0.1705 19  GLY A N   
117  C CA  . GLY A 40  ? 0.9754 0.6899 0.6048 0.0106  0.1347  -0.1817 19  GLY A CA  
118  C C   . GLY A 40  ? 1.0223 0.7672 0.7138 0.0017  0.1212  -0.1643 19  GLY A C   
119  O O   . GLY A 40  ? 0.9907 0.7365 0.7286 0.0027  0.1288  -0.1648 19  GLY A O   
120  N N   . ASN A 41  ? 0.9669 0.7371 0.6593 -0.0060 0.1014  -0.1477 20  ASN A N   
121  C CA  . ASN A 41  ? 0.9592 0.7568 0.7058 -0.0135 0.0902  -0.1297 20  ASN A CA  
122  C C   . ASN A 41  ? 0.9371 0.7496 0.7171 -0.0059 0.1158  -0.1181 20  ASN A C   
123  O O   . ASN A 41  ? 0.9016 0.7256 0.7313 -0.0086 0.1149  -0.1130 20  ASN A O   
124  C CB  . ASN A 41  ? 1.0075 0.8277 0.7442 -0.0213 0.0682  -0.1128 20  ASN A CB  
125  C CG  . ASN A 41  ? 1.0303 0.8439 0.7530 -0.0331 0.0373  -0.1220 20  ASN A CG  
126  O OD1 . ASN A 41  ? 1.1153 0.9154 0.8607 -0.0397 0.0271  -0.1341 20  ASN A OD1 
127  N ND2 . ASN A 41  ? 1.0520 0.8760 0.7386 -0.0357 0.0225  -0.1159 20  ASN A ND2 
128  N N   . TYR A 42  ? 0.9431 0.7564 0.6966 0.0034  0.1387  -0.1135 21  TYR A N   
129  C CA  . TYR A 42  ? 0.9195 0.7476 0.7048 0.0086  0.1637  -0.1031 21  TYR A CA  
130  C C   . TYR A 42  ? 0.9252 0.7439 0.7421 0.0139  0.1805  -0.1151 21  TYR A C   
131  O O   . TYR A 42  ? 0.8965 0.7320 0.7643 0.0102  0.1782  -0.1096 21  TYR A O   
132  C CB  . TYR A 42  ? 0.9224 0.7486 0.6700 0.0180  0.1875  -0.0968 21  TYR A CB  
133  C CG  . TYR A 42  ? 0.9033 0.7421 0.6825 0.0222  0.2162  -0.0883 21  TYR A CG  
134  C CD1 . TYR A 42  ? 0.9143 0.7783 0.7331 0.0142  0.2124  -0.0726 21  TYR A CD1 
135  C CD2 . TYR A 42  ? 0.9491 0.7737 0.7182 0.0336  0.2478  -0.0963 21  TYR A CD2 
136  C CE1 . TYR A 42  ? 0.8822 0.7578 0.7300 0.0157  0.2377  -0.0669 21  TYR A CE1 
137  C CE2 . TYR A 42  ? 0.9015 0.7391 0.7032 0.0357  0.2741  -0.0892 21  TYR A CE2 
138  C CZ  . TYR A 42  ? 0.8823 0.7458 0.7233 0.0258  0.2681  -0.0753 21  TYR A CZ  
139  O OH  . TYR A 42  ? 0.9258 0.8053 0.8035 0.0245  0.2836  -0.0678 21  TYR A OH  
140  N N   . MET A 43  ? 0.9849 0.7770 0.7712 0.0236  0.1975  -0.1310 22  MET A N   
141  C CA  . MET A 43  ? 0.9722 0.7564 0.7882 0.0315  0.2195  -0.1398 22  MET A CA  
142  C C   . MET A 43  ? 0.8959 0.6820 0.7544 0.0262  0.2029  -0.1441 22  MET A C   
143  O O   . MET A 43  ? 0.9662 0.7643 0.8716 0.0298  0.2144  -0.1417 22  MET A O   
144  C CB  . MET A 43  ? 0.9614 0.7116 0.7312 0.0433  0.2400  -0.1563 22  MET A CB  
145  C CG  . MET A 43  ? 0.9525 0.6979 0.6741 0.0507  0.2569  -0.1518 22  MET A CG  
146  S SD  . MET A 43  ? 1.0226 0.7479 0.7322 0.0679  0.2964  -0.1589 22  MET A SD  
147  C CE  . MET A 43  ? 1.0612 0.7450 0.6994 0.0731  0.2890  -0.1795 22  MET A CE  
148  N N   . GLY A 44  ? 0.9352 0.7104 0.7792 0.0180  0.1763  -0.1498 23  GLY A N   
149  C CA  . GLY A 44  ? 0.9680 0.7423 0.8507 0.0136  0.1616  -0.1527 23  GLY A CA  
150  C C   . GLY A 44  ? 1.1146 0.9221 1.0460 0.0062  0.1468  -0.1344 23  GLY A C   
151  O O   . GLY A 44  ? 1.1926 1.0141 1.1705 0.0097  0.1536  -0.1298 23  GLY A O   
152  N N   . ALA A 45  ? 1.2050 1.0261 1.1251 -0.0033 0.1270  -0.1232 24  ALA A N   
153  C CA  . ALA A 45  ? 1.1356 0.9827 1.0954 -0.0110 0.1100  -0.1065 24  ALA A CA  
154  C C   . ALA A 45  ? 1.0417 0.9156 1.0160 -0.0110 0.1211  -0.0904 24  ALA A C   
155  O O   . ALA A 45  ? 1.0348 0.9271 1.0512 -0.0102 0.1264  -0.0837 24  ALA A O   
156  C CB  . ALA A 45  ? 1.1446 0.9900 1.0878 -0.0217 0.0820  -0.1025 24  ALA A CB  
157  N N   . LEU A 46  ? 0.8634 0.8547 0.8897 -0.0071 0.1308  -0.0140 25  LEU A N   
158  C CA  . LEU A 46  ? 0.7990 0.7935 0.8322 -0.0143 0.1239  -0.0093 25  LEU A CA  
159  C C   . LEU A 46  ? 0.8173 0.8289 0.8761 -0.0185 0.1309  -0.0072 25  LEU A C   
160  O O   . LEU A 46  ? 0.8483 0.8695 0.9253 -0.0218 0.1230  -0.0057 25  LEU A O   
161  C CB  . LEU A 46  ? 0.7597 0.7387 0.7671 -0.0197 0.1238  -0.0059 25  LEU A CB  
162  C CG  . LEU A 46  ? 0.7469 0.7247 0.7575 -0.0269 0.1173  -0.0011 25  LEU A CG  
163  C CD1 . LEU A 46  ? 0.6541 0.6346 0.6745 -0.0254 0.1030  -0.0022 25  LEU A CD1 
164  C CD2 . LEU A 46  ? 0.7520 0.7133 0.7357 -0.0302 0.1174  0.0027  25  LEU A CD2 
165  N N   . ARG A 47  ? 0.7160 0.7319 0.7764 -0.0190 0.1458  -0.0073 26  ARG A N   
166  C CA  . ARG A 47  ? 0.7956 0.8293 0.8818 -0.0237 0.1536  -0.0051 26  ARG A CA  
167  C C   . ARG A 47  ? 0.7735 0.8267 0.8910 -0.0191 0.1484  -0.0071 26  ARG A C   
168  O O   . ARG A 47  ? 0.7308 0.7992 0.8720 -0.0245 0.1462  -0.0049 26  ARG A O   
169  C CB  . ARG A 47  ? 0.8162 0.8512 0.8977 -0.0238 0.1719  -0.0053 26  ARG A CB  
170  C CG  . ARG A 47  ? 0.8358 0.8902 0.9446 -0.0293 0.1818  -0.0027 26  ARG A CG  
171  C CD  . ARG A 47  ? 0.9818 1.0364 1.0835 -0.0294 0.2011  -0.0027 26  ARG A CD  
172  N NE  . ARG A 47  ? 0.9874 1.0454 1.0916 -0.0189 0.2084  -0.0083 26  ARG A NE  
173  C CZ  . ARG A 47  ? 0.9402 0.9983 1.0382 -0.0166 0.2258  -0.0101 26  ARG A CZ  
174  N NH1 . ARG A 47  ? 0.8531 0.9086 0.9413 -0.0244 0.2380  -0.0063 26  ARG A NH1 
175  N NH2 . ARG A 47  ? 1.0057 1.0655 1.1064 -0.0063 0.2315  -0.0159 26  ARG A NH2 
176  N N   . GLN A 48  ? 0.9380 0.9907 1.0560 -0.0093 0.1463  -0.0111 27  GLN A N   
177  C CA  . GLN A 48  ? 0.8507 0.9210 0.9973 -0.0037 0.1405  -0.0123 27  GLN A CA  
178  C C   . GLN A 48  ? 0.7959 0.8690 0.9499 -0.0076 0.1238  -0.0104 27  GLN A C   
179  O O   . GLN A 48  ? 0.7524 0.8440 0.9331 -0.0094 0.1195  -0.0091 27  GLN A O   
180  C CB  . GLN A 48  ? 0.8590 0.9234 1.0003 0.0076  0.1409  -0.0165 27  GLN A CB  
181  C CG  . GLN A 48  ? 0.8954 0.9779 1.0664 0.0153  0.1375  -0.0172 27  GLN A CG  
182  C CD  . GLN A 48  ? 0.9446 1.0480 1.1426 0.0162  0.1505  -0.0166 27  GLN A CD  
183  O OE1 . GLN A 48  ? 0.9656 1.0662 1.1559 0.0154  0.1658  -0.0177 27  GLN A OE1 
184  N NE2 . GLN A 48  ? 0.9634 1.0887 1.1932 0.0176  0.1446  -0.0147 27  GLN A NE2 
185  N N   . TRP A 49  ? 0.8045 0.8599 0.9349 -0.0092 0.1145  -0.0103 28  TRP A N   
186  C CA  A TRP A 49  ? 0.7948 0.8507 0.9289 -0.0121 0.0992  -0.0092 28  TRP A CA  
187  C CA  B TRP A 49  ? 0.7943 0.8508 0.9292 -0.0120 0.0993  -0.0092 28  TRP A CA  
188  C C   . TRP A 49  ? 0.7571 0.8188 0.9002 -0.0227 0.0978  -0.0062 28  TRP A C   
189  O O   . TRP A 49  ? 0.7099 0.7795 0.8663 -0.0257 0.0872  -0.0058 28  TRP A O   
190  C CB  A TRP A 49  ? 0.7974 0.8331 0.9040 -0.0108 0.0913  -0.0098 28  TRP A CB  
191  C CB  B TRP A 49  ? 0.7966 0.8334 0.9050 -0.0102 0.0908  -0.0100 28  TRP A CB  
192  C CG  A TRP A 49  ? 0.7859 0.8119 0.8786 -0.0025 0.0939  -0.0129 28  TRP A CG  
193  C CG  B TRP A 49  ? 0.7790 0.8125 0.8844 -0.0007 0.0875  -0.0129 28  TRP A CG  
194  C CD1 A TRP A 49  ? 0.7706 0.8033 0.8743 0.0055  0.0993  -0.0154 28  TRP A CD1 
195  C CD1 B TRP A 49  ? 0.7819 0.8030 0.8694 0.0044  0.0932  -0.0154 28  TRP A CD1 
196  C CD2 A TRP A 49  ? 0.8035 0.8107 0.8686 -0.0016 0.0912  -0.0139 28  TRP A CD2 
197  C CD2 B TRP A 49  ? 0.7227 0.7644 0.8428 0.0043  0.0776  -0.0133 28  TRP A CD2 
198  N NE1 A TRP A 49  ? 0.7732 0.7908 0.8568 0.0107  0.1003  -0.0184 28  TRP A NE1 
199  N NE1 B TRP A 49  ? 0.7690 0.7891 0.8597 0.0122  0.0879  -0.0175 28  TRP A NE1 
200  C CE2 A TRP A 49  ? 0.7930 0.7956 0.8531 0.0061  0.0951  -0.0175 28  TRP A CE2 
201  C CE2 B TRP A 49  ? 0.7310 0.7636 0.8414 0.0126  0.0784  -0.0158 28  TRP A CE2 
202  C CE3 A TRP A 49  ? 0.8128 0.8069 0.8581 -0.0064 0.0858  -0.0121 28  TRP A CE3 
203  C CE3 B TRP A 49  ? 0.6946 0.7497 0.8339 0.0024  0.0679  -0.0117 28  TRP A CE3 
204  C CZ2 A TRP A 49  ? 0.8052 0.7912 0.8410 0.0079  0.0932  -0.0196 28  TRP A CZ2 
205  C CZ2 B TRP A 49  ? 0.7496 0.7856 0.8691 0.0193  0.0702  -0.0161 28  TRP A CZ2 
206  C CZ3 A TRP A 49  ? 0.8509 0.8303 0.8734 -0.0038 0.0839  -0.0137 28  TRP A CZ3 
207  C CZ3 B TRP A 49  ? 0.6908 0.7502 0.8384 0.0091  0.0593  -0.0119 28  TRP A CZ3 
208  C CH2 A TRP A 49  ? 0.9166 0.8922 0.9343 0.0027  0.0873  -0.0176 28  TRP A CH2 
209  C CH2 B TRP A 49  ? 0.7304 0.7800 0.8682 0.0177  0.0607  -0.0137 28  TRP A CH2 
210  N N   . VAL A 50  ? 0.7161 0.7727 0.8510 -0.0288 0.1084  -0.0041 29  VAL A N   
211  C CA  . VAL A 50  ? 0.6641 0.7232 0.8059 -0.0395 0.1079  -0.0012 29  VAL A CA  
212  C C   . VAL A 50  ? 0.6847 0.7673 0.8597 -0.0427 0.1067  -0.0012 29  VAL A C   
213  O O   . VAL A 50  ? 0.6257 0.7121 0.8100 -0.0507 0.0993  -0.0003 29  VAL A O   
214  C CB  . VAL A 50  ? 0.6360 0.6859 0.7636 -0.0449 0.1212  0.0018  29  VAL A CB  
215  C CG1 . VAL A 50  ? 0.6085 0.6650 0.7502 -0.0562 0.1240  0.0050  29  VAL A CG1 
216  C CG2 . VAL A 50  ? 0.6462 0.6727 0.7413 -0.0441 0.1183  0.0029  29  VAL A CG2 
217  N N   . ASN A 51  ? 0.6617 0.7607 0.8555 -0.0366 0.1139  -0.0024 30  ASN A N   
218  C CA  . ASN A 51  ? 0.6574 0.7818 0.8856 -0.0391 0.1132  -0.0020 30  ASN A CA  
219  C C   . ASN A 51  ? 0.5392 0.6734 0.7811 -0.0348 0.0976  -0.0034 30  ASN A C   
220  O O   . ASN A 51  ? 0.6018 0.7576 0.8721 -0.0377 0.0938  -0.0028 30  ASN A O   
221  C CB  . ASN A 51  ? 0.6893 0.8284 0.9338 -0.0334 0.1280  -0.0024 30  ASN A CB  
222  C CG  . ASN A 51  ? 0.7189 0.8458 0.9444 -0.0359 0.1442  -0.0014 30  ASN A CG  
223  O OD1 . ASN A 51  ? 0.8519 0.9737 1.0674 -0.0278 0.1537  -0.0034 30  ASN A OD1 
224  N ND2 . ASN A 51  ? 0.6502 0.7713 0.8696 -0.0472 0.1475  0.0017  30  ASN A ND2 
225  N N   . MET A 52  ? 0.5682 0.6876 0.7909 -0.0284 0.0884  -0.0049 31  MET A N   
226  C CA  . MET A 52  ? 0.5436 0.6699 0.7756 -0.0237 0.0739  -0.0057 31  MET A CA  
227  C C   . MET A 52  ? 0.5706 0.6847 0.7879 -0.0299 0.0608  -0.0059 31  MET A C   
228  O O   . MET A 52  ? 0.6172 0.7299 0.8318 -0.0255 0.0489  -0.0066 31  MET A O   
229  C CB  . MET A 52  ? 0.6142 0.7340 0.8376 -0.0111 0.0739  -0.0072 31  MET A CB  
230  C CG  . MET A 52  ? 0.6226 0.7554 0.8632 -0.0034 0.0860  -0.0077 31  MET A CG  
231  S SD  . MET A 52  ? 0.7937 0.9069 1.0103 0.0075  0.0943  -0.0105 31  MET A SD  
232  C CE  . MET A 52  ? 0.7924 0.9150 1.0260 0.0200  0.0859  -0.0107 31  MET A CE  
233  N N   . GLN A 53  ? 0.5210 0.6256 0.7283 -0.0398 0.0632  -0.0051 32  GLN A N   
234  C CA  . GLN A 53  ? 0.5110 0.6027 0.7040 -0.0453 0.0521  -0.0056 32  GLN A CA  
235  C C   . GLN A 53  ? 0.4574 0.5638 0.6696 -0.0505 0.0404  -0.0065 32  GLN A C   
236  O O   . GLN A 53  ? 0.4851 0.5821 0.6859 -0.0527 0.0294  -0.0079 32  GLN A O   
237  C CB  . GLN A 53  ? 0.4889 0.5657 0.6670 -0.0539 0.0585  -0.0042 32  GLN A CB  
238  C CG  . GLN A 53  ? 0.5566 0.6141 0.7082 -0.0492 0.0652  -0.0033 32  GLN A CG  
239  C CD  . GLN A 53  ? 0.5727 0.6152 0.7095 -0.0571 0.0705  -0.0009 32  GLN A CD  
240  O OE1 . GLN A 53  ? 0.4174 0.4447 0.5383 -0.0591 0.0639  -0.0008 32  GLN A OE1 
241  N NE2 . GLN A 53  ? 0.5199 0.5662 0.6620 -0.0613 0.0830  0.0015  32  GLN A NE2 
242  N N   . ASP A 54  ? 0.5190 0.6484 0.7597 -0.0526 0.0423  -0.0059 33  ASP A N   
243  C CA  . ASP A 54  ? 0.4919 0.6374 0.7519 -0.0578 0.0302  -0.0067 33  ASP A CA  
244  C C   . ASP A 54  ? 0.5142 0.6696 0.7816 -0.0481 0.0196  -0.0069 33  ASP A C   
245  O O   . ASP A 54  ? 0.4922 0.6552 0.7665 -0.0515 0.0063  -0.0077 33  ASP A O   
246  C CB  . ASP A 54  ? 0.5198 0.6878 0.8095 -0.0653 0.0364  -0.0056 33  ASP A CB  
247  C CG  . ASP A 54  ? 0.6165 0.7744 0.8998 -0.0772 0.0451  -0.0050 33  ASP A CG  
248  O OD1 . ASP A 54  ? 0.6253 0.7709 0.8973 -0.0858 0.0379  -0.0064 33  ASP A OD1 
249  O OD2 . ASP A 54  ? 0.6789 0.8400 0.9673 -0.0778 0.0596  -0.0030 33  ASP A OD2 
250  N N   . ASP A 55  ? 0.4697 0.6241 0.7347 -0.0363 0.0249  -0.0060 34  ASP A N   
251  C CA  . ASP A 55  ? 0.5365 0.6988 0.8085 -0.0261 0.0160  -0.0054 34  ASP A CA  
252  C C   . ASP A 55  ? 0.5374 0.6780 0.7815 -0.0199 0.0105  -0.0061 34  ASP A C   
253  O O   . ASP A 55  ? 0.5585 0.7023 0.8045 -0.0127 0.0015  -0.0052 34  ASP A O   
254  C CB  . ASP A 55  ? 0.5894 0.7657 0.8803 -0.0164 0.0258  -0.0040 34  ASP A CB  
255  C CG  . ASP A 55  ? 0.6473 0.8494 0.9703 -0.0214 0.0309  -0.0029 34  ASP A CG  
256  O OD1 . ASP A 55  ? 0.5600 0.7754 0.8975 -0.0299 0.0211  -0.0027 34  ASP A OD1 
257  O OD2 . ASP A 55  ? 0.6908 0.8999 1.0246 -0.0173 0.0449  -0.0024 34  ASP A OD2 
258  N N   . TYR A 56  ? 0.5032 0.6225 0.7221 -0.0227 0.0155  -0.0073 35  TYR A N   
259  C CA  . TYR A 56  ? 0.4846 0.5843 0.6780 -0.0177 0.0110  -0.0079 35  TYR A CA  
260  C C   . TYR A 56  ? 0.4699 0.5534 0.6435 -0.0259 0.0084  -0.0092 35  TYR A C   
261  O O   . TYR A 56  ? 0.5069 0.5889 0.6814 -0.0339 0.0141  -0.0093 35  TYR A O   
262  C CB  . TYR A 56  ? 0.5120 0.6010 0.6936 -0.0098 0.0214  -0.0081 35  TYR A CB  
263  C CG  . TYR A 56  ? 0.5546 0.6558 0.7531 -0.0002 0.0252  -0.0074 35  TYR A CG  
264  C CD1 . TYR A 56  ? 0.5414 0.6573 0.7598 0.0001  0.0357  -0.0070 35  TYR A CD1 
265  C CD2 . TYR A 56  ? 0.5538 0.6514 0.7487 0.0088  0.0189  -0.0068 35  TYR A CD2 
266  C CE1 . TYR A 56  ? 0.5955 0.7225 0.8304 0.0099  0.0400  -0.0065 35  TYR A CE1 
267  C CE2 . TYR A 56  ? 0.6534 0.7606 0.8640 0.0184  0.0226  -0.0060 35  TYR A CE2 
268  C CZ  . TYR A 56  ? 0.6747 0.7968 0.9056 0.0193  0.0332  -0.0060 35  TYR A CZ  
269  O OH  . TYR A 56  ? 0.8050 0.9365 1.0524 0.0298  0.0378  -0.0053 35  TYR A OH  
270  N N   . HIS A 57  ? 0.4404 0.5113 0.5962 -0.0236 0.0002  -0.0099 36  HIS A N   
271  C CA  . HIS A 57  ? 0.4049 0.4576 0.5389 -0.0284 -0.0008 -0.0110 36  HIS A CA  
272  C C   . HIS A 57  ? 0.3672 0.4058 0.4840 -0.0235 0.0076  -0.0105 36  HIS A C   
273  O O   . HIS A 57  ? 0.3641 0.3952 0.4695 -0.0171 0.0050  -0.0105 36  HIS A O   
274  C CB  . HIS A 57  ? 0.4538 0.5008 0.5775 -0.0282 -0.0127 -0.0121 36  HIS A CB  
275  C CG  . HIS A 57  ? 0.5604 0.6160 0.6939 -0.0359 -0.0211 -0.0135 36  HIS A CG  
276  N ND1 . HIS A 57  ? 0.5986 0.6675 0.7437 -0.0343 -0.0311 -0.0133 36  HIS A ND1 
277  C CD2 . HIS A 57  ? 0.6198 0.6718 0.7527 -0.0455 -0.0213 -0.0153 36  HIS A CD2 
278  C CE1 . HIS A 57  ? 0.5390 0.6130 0.6899 -0.0431 -0.0376 -0.0153 36  HIS A CE1 
279  N NE2 . HIS A 57  ? 0.6604 0.7237 0.8041 -0.0502 -0.0315 -0.0168 36  HIS A NE2 
280  N N   . CYS A 58  ? 0.3322 0.3673 0.4469 -0.0271 0.0175  -0.0098 37  CYS A N   
281  C CA  . CYS A 58  ? 0.2773 0.2996 0.3749 -0.0235 0.0253  -0.0093 37  CYS A CA  
282  C C   . CYS A 58  ? 0.3795 0.3848 0.4561 -0.0262 0.0225  -0.0091 37  CYS A C   
283  O O   . CYS A 58  ? 0.3548 0.3565 0.4306 -0.0329 0.0210  -0.0089 37  CYS A O   
284  C CB  . CYS A 58  ? 0.4128 0.4388 0.5160 -0.0259 0.0375  -0.0081 37  CYS A CB  
285  S SG  . CYS A 58  ? 0.4580 0.5047 0.5869 -0.0214 0.0434  -0.0084 37  CYS A SG  
286  N N   . ILE A 59  ? 0.3242 0.3190 0.3846 -0.0209 0.0221  -0.0092 38  ILE A N   
287  C CA  . ILE A 59  ? 0.3358 0.3160 0.3773 -0.0218 0.0196  -0.0087 38  ILE A CA  
288  C C   . ILE A 59  ? 0.3310 0.3028 0.3588 -0.0195 0.0268  -0.0076 38  ILE A C   
289  O O   . ILE A 59  ? 0.3870 0.3586 0.4113 -0.0142 0.0283  -0.0086 38  ILE A O   
290  C CB  . ILE A 59  ? 0.3139 0.2906 0.3488 -0.0183 0.0106  -0.0099 38  ILE A CB  
291  C CG1 . ILE A 59  ? 0.3577 0.3420 0.4035 -0.0210 0.0028  -0.0111 38  ILE A CG1 
292  C CG2 . ILE A 59  ? 0.3614 0.3247 0.3785 -0.0185 0.0092  -0.0092 38  ILE A CG2 
293  C CD1 . ILE A 59  ? 0.3790 0.3631 0.4211 -0.0167 -0.0052 -0.0118 38  ILE A CD1 
294  N N   . TYR A 60  ? 0.3386 0.3024 0.3575 -0.0234 0.0310  -0.0055 39  TYR A N   
295  C CA  . TYR A 60  ? 0.3622 0.3175 0.3657 -0.0219 0.0370  -0.0039 39  TYR A CA  
296  C C   . TYR A 60  ? 0.3598 0.3033 0.3476 -0.0216 0.0321  -0.0024 39  TYR A C   
297  O O   . TYR A 60  ? 0.4181 0.3565 0.4047 -0.0252 0.0306  -0.0007 39  TYR A O   
298  C CB  . TYR A 60  ? 0.3505 0.3063 0.3559 -0.0263 0.0465  -0.0016 39  TYR A CB  
299  C CG  . TYR A 60  ? 0.3701 0.3391 0.3921 -0.0260 0.0528  -0.0030 39  TYR A CG  
300  C CD1 . TYR A 60  ? 0.4020 0.3720 0.4201 -0.0219 0.0598  -0.0041 39  TYR A CD1 
301  C CD2 . TYR A 60  ? 0.4009 0.3816 0.4430 -0.0298 0.0517  -0.0034 39  TYR A CD2 
302  C CE1 . TYR A 60  ? 0.4292 0.4116 0.4637 -0.0206 0.0665  -0.0055 39  TYR A CE1 
303  C CE2 . TYR A 60  ? 0.3925 0.3873 0.4523 -0.0290 0.0574  -0.0043 39  TYR A CE2 
304  C CZ  . TYR A 60  ? 0.4536 0.4492 0.5099 -0.0239 0.0652  -0.0053 39  TYR A CZ  
305  O OH  . TYR A 60  ? 0.6281 0.6382 0.7032 -0.0222 0.0718  -0.0063 39  TYR A OH  
306  N N   . CYS A 61  ? 0.4100 0.3492 0.3866 -0.0173 0.0297  -0.0030 40  CYS A N   
307  C CA  . CYS A 61  ? 0.3468 0.2775 0.3108 -0.0162 0.0246  -0.0017 40  CYS A CA  
308  C C   . CYS A 61  ? 0.3672 0.2913 0.3159 -0.0153 0.0281  0.0005  40  CYS A C   
309  O O   . CYS A 61  ? 0.3539 0.2787 0.2976 -0.0131 0.0299  -0.0013 40  CYS A O   
310  C CB  . CYS A 61  ? 0.3440 0.2766 0.3086 -0.0127 0.0177  -0.0041 40  CYS A CB  
311  S SG  . CYS A 61  ? 0.3905 0.3155 0.3416 -0.0108 0.0123  -0.0026 40  CYS A SG  
312  N N   . ILE A 62  ? 0.3297 0.2466 0.2702 -0.0171 0.0287  0.0043  41  ILE A N   
313  C CA  . ILE A 62  ? 0.3635 0.2740 0.2881 -0.0163 0.0306  0.0073  41  ILE A CA  
314  C C   . ILE A 62  ? 0.3923 0.3011 0.3097 -0.0130 0.0233  0.0070  41  ILE A C   
315  O O   . ILE A 62  ? 0.3376 0.2439 0.2554 -0.0121 0.0186  0.0087  41  ILE A O   
316  C CB  . ILE A 62  ? 0.4014 0.3044 0.3202 -0.0190 0.0339  0.0126  41  ILE A CB  
317  C CG1 . ILE A 62  ? 0.3782 0.2840 0.3069 -0.0234 0.0414  0.0127  41  ILE A CG1 
318  C CG2 . ILE A 62  ? 0.4419 0.3388 0.3430 -0.0181 0.0353  0.0162  41  ILE A CG2 
319  C CD1 . ILE A 62  ? 0.4357 0.3329 0.3590 -0.0270 0.0457  0.0182  41  ILE A CD1 
320  N N   . VAL A 63  ? 0.3391 0.2494 0.2503 -0.0114 0.0226  0.0045  42  VAL A N   
321  C CA  . VAL A 63  ? 0.3931 0.3043 0.3018 -0.0092 0.0157  0.0031  42  VAL A CA  
322  C C   . VAL A 63  ? 0.3866 0.2936 0.2817 -0.0088 0.0129  0.0067  42  VAL A C   
323  O O   . VAL A 63  ? 0.4235 0.3295 0.3082 -0.0090 0.0123  0.0058  42  VAL A O   
324  C CB  . VAL A 63  ? 0.4160 0.3299 0.3257 -0.0082 0.0159  -0.0016 42  VAL A CB  
325  C CG1 . VAL A 63  ? 0.3918 0.3109 0.3164 -0.0074 0.0162  -0.0042 42  VAL A CG1 
326  C CG2 . VAL A 63  ? 0.3578 0.2690 0.2586 -0.0090 0.0223  -0.0029 42  VAL A CG2 
327  N N   . ASP A 64  ? 0.3384 0.2428 0.2338 -0.0080 0.0106  0.0109  43  ASP A N   
328  C CA  . ASP A 64  ? 0.4304 0.3321 0.3148 -0.0067 0.0069  0.0152  43  ASP A CA  
329  C C   . ASP A 64  ? 0.3775 0.2841 0.2626 -0.0048 -0.0001 0.0139  43  ASP A C   
330  O O   . ASP A 64  ? 0.3427 0.2497 0.2186 -0.0043 -0.0039 0.0163  43  ASP A O   
331  C CB  . ASP A 64  ? 0.3950 0.2911 0.2797 -0.0056 0.0073  0.0207  43  ASP A CB  
332  C CG  . ASP A 64  ? 0.3990 0.2957 0.2956 -0.0043 0.0053  0.0194  43  ASP A CG  
333  O OD1 . ASP A 64  ? 0.3425 0.2443 0.2475 -0.0046 0.0042  0.0146  43  ASP A OD1 
334  O OD2 . ASP A 64  ? 0.3865 0.2775 0.2832 -0.0027 0.0051  0.0233  43  ASP A OD2 
335  N N   . GLN A 65  ? 0.3156 0.2262 0.2110 -0.0042 -0.0019 0.0104  44  GLN A N   
336  C CA  . GLN A 65  ? 0.3312 0.2467 0.2277 -0.0032 -0.0075 0.0091  44  GLN A CA  
337  C C   . GLN A 65  ? 0.3191 0.2355 0.2091 -0.0053 -0.0081 0.0057  44  GLN A C   
338  O O   . GLN A 65  ? 0.2800 0.1995 0.1665 -0.0059 -0.0129 0.0057  44  GLN A O   
339  C CB  . GLN A 65  ? 0.3434 0.2616 0.2509 -0.0021 -0.0087 0.0068  44  GLN A CB  
340  C CG  . GLN A 65  ? 0.2964 0.2125 0.2086 0.0000  -0.0087 0.0093  44  GLN A CG  
341  C CD  . GLN A 65  ? 0.3352 0.2534 0.2559 0.0007  -0.0096 0.0065  44  GLN A CD  
342  O OE1 . GLN A 65  ? 0.3566 0.2737 0.2819 -0.0008 -0.0076 0.0040  44  GLN A OE1 
343  N NE2 . GLN A 65  ? 0.3472 0.2688 0.2698 0.0027  -0.0127 0.0070  44  GLN A NE2 
344  N N   . HIS A 66  ? 0.3149 0.2288 0.2040 -0.0067 -0.0031 0.0025  45  HIS A N   
345  C CA  . HIS A 66  ? 0.3571 0.2693 0.2381 -0.0085 -0.0024 -0.0012 45  HIS A CA  
346  C C   . HIS A 66  ? 0.3140 0.2232 0.1801 -0.0100 -0.0027 0.0008  45  HIS A C   
347  O O   . HIS A 66  ? 0.3874 0.2960 0.2445 -0.0121 -0.0057 -0.0014 45  HIS A O   
348  C CB  . HIS A 66  ? 0.3651 0.2754 0.2503 -0.0084 0.0039  -0.0050 45  HIS A CB  
349  C CG  . HIS A 66  ? 0.3831 0.2961 0.2801 -0.0072 0.0027  -0.0075 45  HIS A CG  
350  N ND1 . HIS A 66  ? 0.3581 0.2708 0.2546 -0.0076 -0.0010 -0.0099 45  HIS A ND1 
351  C CD2 . HIS A 66  ? 0.3745 0.2901 0.2834 -0.0058 0.0043  -0.0077 45  HIS A CD2 
352  C CE1 . HIS A 66  ? 0.4046 0.3192 0.3114 -0.0061 -0.0013 -0.0110 45  HIS A CE1 
353  N NE2 . HIS A 66  ? 0.3786 0.2954 0.2929 -0.0049 0.0014  -0.0098 45  HIS A NE2 
354  N N   . ALA A 67  ? 0.3553 0.2620 0.2175 -0.0096 0.0003  0.0051  46  ALA A N   
355  C CA  . ALA A 67  ? 0.3649 0.2678 0.2107 -0.0110 0.0004  0.0076  46  ALA A CA  
356  C C   . ALA A 67  ? 0.4170 0.3232 0.2567 -0.0111 -0.0082 0.0102  46  ALA A C   
357  O O   . ALA A 67  ? 0.3889 0.2934 0.2141 -0.0133 -0.0104 0.0099  46  ALA A O   
358  C CB  . ALA A 67  ? 0.4032 0.3021 0.2465 -0.0105 0.0051  0.0129  46  ALA A CB  
359  N N   . ILE A 68  ? 0.3911 0.3028 0.2420 -0.0087 -0.0133 0.0125  47  ILE A N   
360  C CA  . ILE A 68  ? 0.3417 0.2588 0.1897 -0.0081 -0.0213 0.0160  47  ILE A CA  
361  C C   . ILE A 68  ? 0.3335 0.2554 0.1813 -0.0112 -0.0262 0.0114  47  ILE A C   
362  O O   . ILE A 68  ? 0.3603 0.2888 0.2074 -0.0116 -0.0334 0.0137  47  ILE A O   
363  C CB  . ILE A 68  ? 0.3336 0.2548 0.1940 -0.0038 -0.0239 0.0205  47  ILE A CB  
364  C CG1 . ILE A 68  ? 0.3654 0.2881 0.2399 -0.0030 -0.0213 0.0167  47  ILE A CG1 
365  C CG2 . ILE A 68  ? 0.3808 0.2956 0.2376 -0.0013 -0.0208 0.0264  47  ILE A CG2 
366  C CD1 . ILE A 68  ? 0.3484 0.2762 0.2342 0.0008  -0.0243 0.0195  47  ILE A CD1 
367  N N   . THR A 69  ? 0.3117 0.2305 0.1604 -0.0135 -0.0225 0.0051  48  THR A N   
368  C CA  . THR A 69  ? 0.3746 0.2945 0.2192 -0.0175 -0.0262 0.0004  48  THR A CA  
369  C C   . THR A 69  ? 0.3854 0.3025 0.2120 -0.0210 -0.0290 0.0000  48  THR A C   
370  O O   . THR A 69  ? 0.3742 0.2932 0.1960 -0.0251 -0.0342 -0.0032 48  THR A O   
371  C CB  . THR A 69  ? 0.4046 0.3191 0.2523 -0.0186 -0.0209 -0.0059 48  THR A CB  
372  O OG1 . THR A 69  ? 0.3693 0.2760 0.2075 -0.0187 -0.0140 -0.0082 48  THR A OG1 
373  C CG2 . THR A 69  ? 0.3049 0.2219 0.1685 -0.0155 -0.0188 -0.0053 48  THR A CG2 
374  N N   . VAL A 70  ? 0.4197 0.3320 0.2354 -0.0199 -0.0255 0.0029  49  VAL A N   
375  C CA  . VAL A 70  ? 0.4214 0.3315 0.2182 -0.0225 -0.0291 0.0044  49  VAL A CA  
376  C C   . VAL A 70  ? 0.4501 0.3640 0.2470 -0.0190 -0.0328 0.0134  49  VAL A C   
377  O O   . VAL A 70  ? 0.4483 0.3598 0.2521 -0.0152 -0.0277 0.0171  49  VAL A O   
378  C CB  . VAL A 70  ? 0.4955 0.3952 0.2764 -0.0244 -0.0210 0.0006  49  VAL A CB  
379  C CG1 . VAL A 70  ? 0.4657 0.3606 0.2445 -0.0276 -0.0182 -0.0084 49  VAL A CG1 
380  C CG2 . VAL A 70  ? 0.5421 0.4382 0.3292 -0.0209 -0.0118 0.0030  49  VAL A CG2 
381  N N   . ARG A 71  ? 0.4408 0.3605 0.2307 -0.0201 -0.0419 0.0169  50  ARG A N   
382  C CA  . ARG A 71  ? 0.4906 0.4142 0.2818 -0.0156 -0.0464 0.0261  50  ARG A CA  
383  C C   . ARG A 71  ? 0.5454 0.4589 0.3240 -0.0141 -0.0399 0.0304  50  ARG A C   
384  O O   . ARG A 71  ? 0.5522 0.4584 0.3126 -0.0176 -0.0365 0.0280  50  ARG A O   
385  C CB  . ARG A 71  ? 0.5239 0.4561 0.3082 -0.0174 -0.0579 0.0290  50  ARG A CB  
386  C CG  . ARG A 71  ? 0.6009 0.5404 0.3926 -0.0115 -0.0642 0.0388  50  ARG A CG  
387  C CD  . ARG A 71  ? 0.6356 0.5848 0.4514 -0.0077 -0.0655 0.0392  50  ARG A CD  
388  N NE  . ARG A 71  ? 0.6225 0.5860 0.4455 -0.0098 -0.0753 0.0389  50  ARG A NE  
389  C CZ  . ARG A 71  ? 0.5550 0.5241 0.3871 -0.0143 -0.0761 0.0323  50  ARG A CZ  
390  N NH1 . ARG A 71  ? 0.6443 0.6060 0.4796 -0.0163 -0.0682 0.0256  50  ARG A NH1 
391  N NH2 . ARG A 71  ? 0.7016 0.6846 0.5405 -0.0168 -0.0853 0.0329  50  ARG A NH2 
392  N N   . GLN A 72  ? 0.5237 0.4359 0.3115 -0.0090 -0.0375 0.0367  51  GLN A N   
393  C CA  . GLN A 72  ? 0.5090 0.4111 0.2879 -0.0078 -0.0304 0.0415  51  GLN A CA  
394  C C   . GLN A 72  ? 0.5553 0.4573 0.3300 -0.0034 -0.0360 0.0519  51  GLN A C   
395  O O   . GLN A 72  ? 0.5719 0.4821 0.3578 0.0004  -0.0434 0.0553  51  GLN A O   
396  C CB  . GLN A 72  ? 0.5486 0.4468 0.3423 -0.0062 -0.0216 0.0397  51  GLN A CB  
397  C CG  . GLN A 72  ? 0.5702 0.4689 0.3708 -0.0092 -0.0161 0.0306  51  GLN A CG  
398  C CD  . GLN A 72  ? 0.4850 0.3766 0.2718 -0.0127 -0.0083 0.0273  51  GLN A CD  
399  O OE1 . GLN A 72  ? 0.6652 0.5505 0.4381 -0.0132 -0.0050 0.0321  51  GLN A OE1 
400  N NE2 . GLN A 72  ? 0.5435 0.4355 0.3335 -0.0149 -0.0046 0.0193  51  GLN A NE2 
401  N N   . ASP A 73  ? 0.4436 0.3359 0.2023 -0.0038 -0.0319 0.0572  52  ASP A N   
402  C CA  . ASP A 73  ? 0.5245 0.4132 0.2805 0.0012  -0.0349 0.0680  52  ASP A CA  
403  C C   . ASP A 73  ? 0.4453 0.3295 0.2187 0.0048  -0.0287 0.0695  52  ASP A C   
404  O O   . ASP A 73  ? 0.4185 0.2961 0.1940 0.0020  -0.0191 0.0659  52  ASP A O   
405  C CB  . ASP A 73  ? 0.5164 0.3948 0.2485 -0.0008 -0.0317 0.0736  52  ASP A CB  
406  C CG  . ASP A 73  ? 0.5161 0.3878 0.2454 0.0045  -0.0333 0.0854  52  ASP A CG  
407  O OD1 . ASP A 73  ? 0.5494 0.4276 0.2811 0.0092  -0.0436 0.0915  52  ASP A OD1 
408  O OD2 . ASP A 73  ? 0.5973 0.4573 0.3231 0.0040  -0.0241 0.0889  52  ASP A OD2 
409  N N   . PRO A 74  ? 0.4925 0.3801 0.2787 0.0108  -0.0338 0.0744  53  PRO A N   
410  C CA  . PRO A 74  ? 0.5371 0.4198 0.3395 0.0136  -0.0278 0.0739  53  PRO A CA  
411  C C   . PRO A 74  ? 0.4394 0.3077 0.2355 0.0119  -0.0184 0.0771  53  PRO A C   
412  O O   . PRO A 74  ? 0.4489 0.3142 0.2535 0.0089  -0.0109 0.0715  53  PRO A O   
413  C CB  . PRO A 74  ? 0.4839 0.3707 0.2959 0.0213  -0.0349 0.0804  53  PRO A CB  
414  C CG  . PRO A 74  ? 0.4720 0.3724 0.2815 0.0213  -0.0451 0.0804  53  PRO A CG  
415  C CD  . PRO A 74  ? 0.4419 0.3396 0.2304 0.0153  -0.0451 0.0794  53  PRO A CD  
416  N N   . GLN A 75  ? 0.4410 0.3006 0.2221 0.0133  -0.0188 0.0863  54  GLN A N   
417  C CA  . GLN A 75  ? 0.5080 0.3533 0.2835 0.0113  -0.0095 0.0904  54  GLN A CA  
418  C C   . GLN A 75  ? 0.5027 0.3466 0.2728 0.0039  -0.0005 0.0839  54  GLN A C   
419  O O   . GLN A 75  ? 0.4412 0.2788 0.2184 0.0010  0.0082  0.0821  54  GLN A O   
420  C CB  . GLN A 75  ? 0.5200 0.3559 0.2779 0.0141  -0.0120 0.1023  54  GLN A CB  
421  C CG  . GLN A 75  ? 0.7880 0.6198 0.5540 0.0222  -0.0169 0.1103  54  GLN A CG  
422  C CD  . GLN A 75  ? 0.9365 0.7530 0.7088 0.0222  -0.0083 0.1129  54  GLN A CD  
423  O OE1 . GLN A 75  ? 0.8746 0.6772 0.6341 0.0215  -0.0040 0.1211  54  GLN A OE1 
424  N NE2 . GLN A 75  ? 0.8394 0.6578 0.6307 0.0225  -0.0056 0.1058  54  GLN A NE2 
425  N N   . ASN A 76  ? 0.4995 0.3492 0.2573 0.0008  -0.0024 0.0801  55  ASN A N   
426  C CA  . ASN A 76  ? 0.4947 0.3432 0.2473 -0.0052 0.0069  0.0738  55  ASN A CA  
427  C C   . ASN A 76  ? 0.5281 0.3828 0.3010 -0.0067 0.0107  0.0645  55  ASN A C   
428  O O   . ASN A 76  ? 0.4718 0.3238 0.2488 -0.0104 0.0201  0.0613  55  ASN A O   
429  C CB  . ASN A 76  ? 0.5399 0.3921 0.2743 -0.0078 0.0038  0.0708  55  ASN A CB  
430  C CG  . ASN A 76  ? 0.5758 0.4263 0.3046 -0.0131 0.0142  0.0639  55  ASN A CG  
431  O OD1 . ASN A 76  ? 0.6436 0.4859 0.3601 -0.0158 0.0227  0.0675  55  ASN A OD1 
432  N ND2 . ASN A 76  ? 0.6296 0.4877 0.3680 -0.0144 0.0142  0.0541  55  ASN A ND2 
433  N N   . LEU A 77  ? 0.4897 0.3533 0.2757 -0.0040 0.0036  0.0602  56  LEU A N   
434  C CA  . LEU A 77  ? 0.4369 0.3058 0.2411 -0.0050 0.0065  0.0522  56  LEU A CA  
435  C C   . LEU A 77  ? 0.4239 0.2868 0.2402 -0.0051 0.0121  0.0539  56  LEU A C   
436  O O   . LEU A 77  ? 0.3957 0.2595 0.2208 -0.0084 0.0187  0.0490  56  LEU A O   
437  C CB  . LEU A 77  ? 0.4329 0.3114 0.2477 -0.0021 -0.0021 0.0488  56  LEU A CB  
438  C CG  . LEU A 77  ? 0.4539 0.3371 0.2869 -0.0024 -0.0002 0.0419  56  LEU A CG  
439  C CD1 . LEU A 77  ? 0.4007 0.2856 0.2336 -0.0064 0.0056  0.0349  56  LEU A CD1 
440  C CD2 . LEU A 77  ? 0.4286 0.3205 0.2706 0.0005  -0.0081 0.0398  56  LEU A CD2 
441  N N   . ARG A 78  ? 0.4339 0.2905 0.2509 -0.0015 0.0095  0.0609  57  ARG A N   
442  C CA  . ARG A 78  ? 0.4946 0.3431 0.3213 -0.0022 0.0148  0.0623  57  ARG A CA  
443  C C   . ARG A 78  ? 0.5077 0.3491 0.3282 -0.0077 0.0245  0.0640  57  ARG A C   
444  O O   . ARG A 78  ? 0.4301 0.2710 0.2620 -0.0115 0.0304  0.0602  57  ARG A O   
445  C CB  . ARG A 78  ? 0.4576 0.2984 0.2837 0.0034  0.0108  0.0700  57  ARG A CB  
446  C CG  . ARG A 78  ? 0.5071 0.3381 0.3436 0.0030  0.0152  0.0705  57  ARG A CG  
447  C CD  . ARG A 78  ? 0.6277 0.4562 0.4714 0.0101  0.0097  0.0729  57  ARG A CD  
448  N NE  . ARG A 78  ? 0.6629 0.4932 0.4977 0.0162  0.0028  0.0801  57  ARG A NE  
449  C CZ  . ARG A 78  ? 0.5909 0.4323 0.4311 0.0212  -0.0048 0.0789  57  ARG A CZ  
450  N NH1 . ARG A 78  ? 0.5408 0.3910 0.3945 0.0215  -0.0061 0.0712  57  ARG A NH1 
451  N NH2 . ARG A 78  ? 0.6683 0.5126 0.5003 0.0259  -0.0114 0.0861  57  ARG A NH2 
452  N N   . LYS A 79  ? 0.4706 0.3070 0.2728 -0.0086 0.0262  0.0698  58  LYS A N   
453  C CA  . LYS A 79  ? 0.4388 0.2685 0.2340 -0.0141 0.0365  0.0720  58  LYS A CA  
454  C C   . LYS A 79  ? 0.4410 0.2796 0.2430 -0.0184 0.0426  0.0633  58  LYS A C   
455  O O   . LYS A 79  ? 0.4231 0.2605 0.2325 -0.0230 0.0513  0.0620  58  LYS A O   
456  C CB  . LYS A 79  ? 0.5600 0.3828 0.3317 -0.0140 0.0367  0.0799  58  LYS A CB  
457  C CG  . LYS A 79  ? 0.6314 0.4447 0.3943 -0.0194 0.0481  0.0845  58  LYS A CG  
458  C CD  . LYS A 79  ? 0.7755 0.5801 0.5126 -0.0188 0.0477  0.0938  58  LYS A CD  
459  C CE  . LYS A 79  ? 0.8320 0.6429 0.5533 -0.0204 0.0480  0.0894  58  LYS A CE  
460  N NZ  . LYS A 79  ? 0.8488 0.6616 0.5712 -0.0263 0.0607  0.0841  58  LYS A NZ  
461  N N   . ALA A 80  ? 0.4326 0.2804 0.2329 -0.0170 0.0382  0.0573  59  ALA A N   
462  C CA  . ALA A 80  ? 0.4938 0.3488 0.2991 -0.0199 0.0441  0.0494  59  ALA A CA  
463  C C   . ALA A 80  ? 0.4229 0.2845 0.2512 -0.0205 0.0449  0.0435  59  ALA A C   
464  O O   . ALA A 80  ? 0.4558 0.3222 0.2923 -0.0233 0.0519  0.0389  59  ALA A O   
465  C CB  . ALA A 80  ? 0.5386 0.3991 0.3345 -0.0184 0.0390  0.0446  59  ALA A CB  
466  N N   . THR A 81  ? 0.4107 0.2730 0.2492 -0.0176 0.0378  0.0434  60  THR A N   
467  C CA  . THR A 81  ? 0.4141 0.2816 0.2723 -0.0185 0.0380  0.0383  60  THR A CA  
468  C C   . THR A 81  ? 0.3702 0.2330 0.2356 -0.0231 0.0456  0.0404  60  THR A C   
469  O O   . THR A 81  ? 0.3790 0.2483 0.2573 -0.0263 0.0500  0.0358  60  THR A O   
470  C CB  . THR A 81  ? 0.3693 0.2371 0.2341 -0.0144 0.0296  0.0381  60  THR A CB  
471  O OG1 . THR A 81  ? 0.4503 0.3240 0.3103 -0.0111 0.0230  0.0360  60  THR A OG1 
472  C CG2 . THR A 81  ? 0.3807 0.2528 0.2631 -0.0156 0.0293  0.0328  60  THR A CG2 
473  N N   . LEU A 82  ? 0.4286 0.2801 0.2859 -0.0238 0.0472  0.0478  61  LEU A N   
474  C CA  . LEU A 82  ? 0.4397 0.2853 0.3026 -0.0293 0.0549  0.0503  61  LEU A CA  
475  C C   . LEU A 82  ? 0.4210 0.2696 0.2799 -0.0339 0.0647  0.0504  61  LEU A C   
476  O O   . LEU A 82  ? 0.4133 0.2653 0.2847 -0.0392 0.0715  0.0486  61  LEU A O   
477  C CB  . LEU A 82  ? 0.4946 0.3251 0.3484 -0.0285 0.0544  0.0588  61  LEU A CB  
478  C CG  . LEU A 82  ? 0.5493 0.3755 0.4082 -0.0236 0.0463  0.0588  61  LEU A CG  
479  C CD1 . LEU A 82  ? 0.6819 0.4922 0.5306 -0.0216 0.0465  0.0679  61  LEU A CD1 
480  C CD2 . LEU A 82  ? 0.5462 0.3756 0.4233 -0.0264 0.0461  0.0522  61  LEU A CD2 
481  N N   . ASP A 83  ? 0.4620 0.3103 0.3038 -0.0321 0.0658  0.0522  62  ASP A N   
482  C CA  . ASP A 83  ? 0.4867 0.3381 0.3234 -0.0358 0.0759  0.0513  62  ASP A CA  
483  C C   . ASP A 83  ? 0.4922 0.3571 0.3472 -0.0367 0.0787  0.0427  62  ASP A C   
484  O O   . ASP A 83  ? 0.4993 0.3687 0.3635 -0.0410 0.0880  0.0417  62  ASP A O   
485  C CB  . ASP A 83  ? 0.5022 0.3511 0.3162 -0.0333 0.0751  0.0527  62  ASP A CB  
486  C CG  . ASP A 83  ? 0.5861 0.4221 0.3799 -0.0334 0.0751  0.0626  62  ASP A CG  
487  O OD1 . ASP A 83  ? 0.6183 0.4461 0.4142 -0.0366 0.0799  0.0685  62  ASP A OD1 
488  O OD2 . ASP A 83  ? 0.5928 0.4264 0.3679 -0.0305 0.0700  0.0645  62  ASP A OD2 
489  N N   . THR A 84  ? 0.4851 0.3568 0.3459 -0.0324 0.0707  0.0369  63  THR A N   
490  C CA  . THR A 84  ? 0.4671 0.3508 0.3443 -0.0321 0.0723  0.0294  63  THR A CA  
491  C C   . THR A 84  ? 0.4095 0.2983 0.3081 -0.0357 0.0738  0.0283  63  THR A C   
492  O O   . THR A 84  ? 0.4036 0.3016 0.3155 -0.0381 0.0803  0.0252  63  THR A O   
493  C CB  . THR A 84  ? 0.5090 0.3967 0.3870 -0.0271 0.0628  0.0246  63  THR A CB  
494  O OG1 . THR A 84  ? 0.5287 0.4132 0.3880 -0.0250 0.0622  0.0243  63  THR A OG1 
495  C CG2 . THR A 84  ? 0.4638 0.3628 0.3601 -0.0263 0.0632  0.0178  63  THR A CG2 
496  N N   . LEU A 85  ? 0.4139 0.2971 0.3163 -0.0361 0.0677  0.0305  64  LEU A N   
497  C CA  . LEU A 85  ? 0.3980 0.2849 0.3190 -0.0404 0.0681  0.0289  64  LEU A CA  
498  C C   . LEU A 85  ? 0.4081 0.2941 0.3331 -0.0472 0.0786  0.0322  64  LEU A C   
499  O O   . LEU A 85  ? 0.4124 0.3091 0.3550 -0.0509 0.0826  0.0290  64  LEU A O   
500  C CB  . LEU A 85  ? 0.3918 0.2695 0.3122 -0.0397 0.0608  0.0307  64  LEU A CB  
501  C CG  . LEU A 85  ? 0.5197 0.3976 0.4558 -0.0453 0.0611  0.0291  64  LEU A CG  
502  C CD1 . LEU A 85  ? 0.3453 0.2383 0.2992 -0.0456 0.0582  0.0222  64  LEU A CD1 
503  C CD2 . LEU A 85  ? 0.4784 0.3442 0.4107 -0.0440 0.0551  0.0308  64  LEU A CD2 
504  N N   . ALA A 86  ? 0.4625 0.3362 0.3718 -0.0489 0.0830  0.0391  65  ALA A N   
505  C CA  . ALA A 86  ? 0.4439 0.3157 0.3556 -0.0559 0.0939  0.0431  65  ALA A CA  
506  C C   . ALA A 86  ? 0.4362 0.3206 0.3533 -0.0569 0.1029  0.0399  65  ALA A C   
507  O O   . ALA A 86  ? 0.3858 0.2771 0.3170 -0.0629 0.1111  0.0399  65  ALA A O   
508  C CB  . ALA A 86  ? 0.4592 0.3146 0.3493 -0.0565 0.0971  0.0518  65  ALA A CB  
509  N N   . LEU A 87  ? 0.4337 0.3214 0.3405 -0.0511 0.1018  0.0370  66  LEU A N   
510  C CA  . LEU A 87  ? 0.3935 0.2911 0.3033 -0.0510 0.1112  0.0336  66  LEU A CA  
511  C C   . LEU A 87  ? 0.4076 0.3216 0.3438 -0.0508 0.1106  0.0272  66  LEU A C   
512  O O   . LEU A 87  ? 0.4341 0.3581 0.3837 -0.0540 0.1202  0.0262  66  LEU A O   
513  C CB  . LEU A 87  ? 0.4795 0.3738 0.3695 -0.0452 0.1095  0.0316  66  LEU A CB  
514  C CG  . LEU A 87  ? 0.5507 0.4515 0.4382 -0.0440 0.1199  0.0277  66  LEU A CG  
515  C CD1 . LEU A 87  ? 0.6353 0.5360 0.5223 -0.0499 0.1339  0.0320  66  LEU A CD1 
516  C CD2 . LEU A 87  ? 0.6844 0.5774 0.5470 -0.0397 0.1173  0.0264  66  LEU A CD2 
517  N N   . TYR A 88  ? 0.4314 0.3489 0.3756 -0.0469 0.0995  0.0231  67  TYR A N   
518  C CA  . TYR A 88  ? 0.4370 0.3695 0.4055 -0.0466 0.0975  0.0179  67  TYR A CA  
519  C C   . TYR A 88  ? 0.4117 0.3494 0.3986 -0.0541 0.0996  0.0195  67  TYR A C   
520  O O   . TYR A 88  ? 0.4374 0.3901 0.4453 -0.0558 0.1030  0.0168  67  TYR A O   
521  C CB  . TYR A 88  ? 0.4641 0.3973 0.4344 -0.0414 0.0850  0.0141  67  TYR A CB  
522  C CG  . TYR A 88  ? 0.4266 0.3613 0.3889 -0.0347 0.0838  0.0102  67  TYR A CG  
523  C CD1 . TYR A 88  ? 0.4833 0.4077 0.4228 -0.0323 0.0846  0.0117  67  TYR A CD1 
524  C CD2 . TYR A 88  ? 0.5153 0.4613 0.4927 -0.0309 0.0815  0.0052  67  TYR A CD2 
525  C CE1 . TYR A 88  ? 0.5297 0.4542 0.4614 -0.0272 0.0834  0.0076  67  TYR A CE1 
526  C CE2 . TYR A 88  ? 0.5214 0.4666 0.4911 -0.0250 0.0808  0.0016  67  TYR A CE2 
527  C CZ  . TYR A 88  ? 0.5098 0.4440 0.4566 -0.0236 0.0819  0.0025  67  TYR A CZ  
528  O OH  . TYR A 88  ? 0.4838 0.4160 0.4224 -0.0188 0.0811  -0.0017 67  TYR A OH  
529  N N   . LEU A 89  ? 0.4621 0.3876 0.4421 -0.0585 0.0974  0.0238  68  LEU A N   
530  C CA  . LEU A 89  ? 0.4163 0.3443 0.4118 -0.0671 0.1002  0.0254  68  LEU A CA  
531  C C   . LEU A 89  ? 0.4404 0.3745 0.4416 -0.0725 0.1140  0.0281  68  LEU A C   
532  O O   . LEU A 89  ? 0.4309 0.3785 0.4545 -0.0779 0.1175  0.0265  68  LEU A O   
533  C CB  . LEU A 89  ? 0.4664 0.3765 0.4503 -0.0702 0.0964  0.0298  68  LEU A CB  
534  C CG  . LEU A 89  ? 0.4674 0.3719 0.4491 -0.0662 0.0838  0.0269  68  LEU A CG  
535  C CD1 . LEU A 89  ? 0.4521 0.3370 0.4193 -0.0675 0.0820  0.0320  68  LEU A CD1 
536  C CD2 . LEU A 89  ? 0.5124 0.4284 0.5157 -0.0697 0.0783  0.0215  68  LEU A CD2 
537  N N   . ALA A 90  ? 0.4165 0.3413 0.3976 -0.0713 0.1220  0.0324  69  ALA A N   
538  C CA  . ALA A 90  ? 0.4793 0.4087 0.4631 -0.0765 0.1364  0.0354  69  ALA A CA  
539  C C   . ALA A 90  ? 0.4936 0.4426 0.4947 -0.0735 0.1423  0.0300  69  ALA A C   
540  O O   . ALA A 90  ? 0.4299 0.3901 0.4468 -0.0789 0.1528  0.0308  69  ALA A O   
541  C CB  . ALA A 90  ? 0.4435 0.3576 0.3984 -0.0752 0.1428  0.0410  69  ALA A CB  
542  N N   . CYS A 91  ? 0.4407 0.3939 0.4396 -0.0649 0.1362  0.0248  70  CYS A N   
543  C CA  . CYS A 91  ? 0.5065 0.4770 0.5226 -0.0608 0.1411  0.0197  70  CYS A CA  
544  C C   . CYS A 91  ? 0.5136 0.5020 0.5614 -0.0639 0.1373  0.0172  70  CYS A C   
545  O O   . CYS A 91  ? 0.5347 0.5400 0.6020 -0.0625 0.1439  0.0147  70  CYS A O   
546  C CB  . CYS A 91  ? 0.5224 0.4905 0.5278 -0.0513 0.1345  0.0150  70  CYS A CB  
547  S SG  . CYS A 91  ? 0.5822 0.5344 0.5532 -0.0476 0.1409  0.0162  70  CYS A SG  
548  N N   . GLY A 92  ? 0.5291 0.5141 0.5823 -0.0680 0.1267  0.0177  71  GLY A N   
549  C CA  . GLY A 92  ? 0.4562 0.4571 0.5376 -0.0727 0.1226  0.0157  71  GLY A CA  
550  C C   . GLY A 92  ? 0.4848 0.4872 0.5718 -0.0697 0.1073  0.0119  71  GLY A C   
551  O O   . GLY A 92  ? 0.4540 0.4698 0.5631 -0.0736 0.1021  0.0099  71  GLY A O   
552  N N   . ILE A 93  ? 0.4170 0.4066 0.4843 -0.0632 0.0997  0.0109  72  ILE A N   
553  C CA  . ILE A 93  ? 0.4231 0.4128 0.4937 -0.0607 0.0860  0.0077  72  ILE A CA  
554  C C   . ILE A 93  ? 0.4547 0.4381 0.5282 -0.0690 0.0810  0.0089  72  ILE A C   
555  O O   . ILE A 93  ? 0.4694 0.4369 0.5280 -0.0728 0.0838  0.0126  72  ILE A O   
556  C CB  . ILE A 93  ? 0.4080 0.3850 0.4568 -0.0529 0.0801  0.0070  72  ILE A CB  
557  C CG1 . ILE A 93  ? 0.4742 0.4567 0.5205 -0.0452 0.0847  0.0049  72  ILE A CG1 
558  C CG2 . ILE A 93  ? 0.4499 0.4263 0.5011 -0.0510 0.0670  0.0041  72  ILE A CG2 
559  C CD1 . ILE A 93  ? 0.5251 0.5256 0.5941 -0.0417 0.0829  0.0013  72  ILE A CD1 
560  N N   . ASP A 94  ? 0.3707 0.3657 0.4629 -0.0720 0.0734  0.0057  73  ASP A N   
561  C CA  . ASP A 94  ? 0.4565 0.4469 0.5540 -0.0812 0.0690  0.0055  73  ASP A CA  
562  C C   . ASP A 94  ? 0.4856 0.4660 0.5726 -0.0782 0.0569  0.0027  73  ASP A C   
563  O O   . ASP A 94  ? 0.4245 0.4149 0.5191 -0.0740 0.0486  -0.0008 73  ASP A O   
564  C CB  . ASP A 94  ? 0.5168 0.5279 0.6424 -0.0877 0.0685  0.0036  73  ASP A CB  
565  C CG  . ASP A 94  ? 0.5756 0.5816 0.7071 -0.0994 0.0658  0.0033  73  ASP A CG  
566  O OD1 . ASP A 94  ? 0.5618 0.5485 0.6764 -0.1007 0.0612  0.0032  73  ASP A OD1 
567  O OD2 . ASP A 94  ? 0.6242 0.6456 0.7778 -0.1073 0.0683  0.0030  73  ASP A OD2 
568  N N   . PRO A 95  ? 0.5101 0.4708 0.5799 -0.0799 0.0556  0.0044  74  PRO A N   
569  C CA  . PRO A 95  ? 0.5327 0.4840 0.5921 -0.0763 0.0452  0.0014  74  PRO A CA  
570  C C   . PRO A 95  ? 0.5095 0.4680 0.5822 -0.0816 0.0364  -0.0033 74  PRO A C   
571  O O   . PRO A 95  ? 0.5567 0.5099 0.6217 -0.0783 0.0278  -0.0063 74  PRO A O   
572  C CB  . PRO A 95  ? 0.6297 0.5590 0.6708 -0.0776 0.0477  0.0049  74  PRO A CB  
573  C CG  . PRO A 95  ? 0.5102 0.4375 0.5559 -0.0855 0.0575  0.0089  74  PRO A CG  
574  C CD  . PRO A 95  ? 0.5334 0.4789 0.5918 -0.0846 0.0640  0.0094  74  PRO A CD  
575  N N   . GLN A 96  ? 0.5727 0.5434 0.6645 -0.0900 0.0382  -0.0040 75  GLN A N   
576  C CA  . GLN A 96  ? 0.5366 0.5162 0.6416 -0.0958 0.0289  -0.0087 75  GLN A CA  
577  C C   . GLN A 96  ? 0.5422 0.5438 0.6630 -0.0910 0.0233  -0.0107 75  GLN A C   
578  O O   . GLN A 96  ? 0.5438 0.5505 0.6683 -0.0917 0.0128  -0.0144 75  GLN A O   
579  C CB  . GLN A 96  ? 0.5962 0.5783 0.7150 -0.1086 0.0325  -0.0085 75  GLN A CB  
580  C CG  . GLN A 96  ? 0.6987 0.6568 0.8029 -0.1150 0.0342  -0.0081 75  GLN A CG  
581  C CD  . GLN A 96  ? 0.7573 0.7029 0.8488 -0.1133 0.0240  -0.0129 75  GLN A CD  
582  O OE1 . GLN A 96  ? 0.8304 0.7556 0.9027 -0.1095 0.0251  -0.0119 75  GLN A OE1 
583  N NE2 . GLN A 96  ? 0.7974 0.7557 0.8995 -0.1158 0.0142  -0.0180 75  GLN A NE2 
584  N N   . LYS A 97  ? 0.5150 0.5290 0.6444 -0.0860 0.0302  -0.0082 76  LYS A N   
585  C CA  . LYS A 97  ? 0.5114 0.5444 0.6549 -0.0795 0.0256  -0.0094 76  LYS A CA  
586  C C   . LYS A 97  ? 0.4780 0.5038 0.6054 -0.0683 0.0223  -0.0097 76  LYS A C   
587  O O   . LYS A 97  ? 0.4589 0.4927 0.5907 -0.0636 0.0137  -0.0115 76  LYS A O   
588  C CB  . LYS A 97  ? 0.4819 0.5320 0.6439 -0.0790 0.0355  -0.0071 76  LYS A CB  
589  C CG  . LYS A 97  ? 0.5378 0.6000 0.7208 -0.0903 0.0390  -0.0067 76  LYS A CG  
590  C CD  . LYS A 97  ? 0.4902 0.5712 0.6928 -0.0885 0.0494  -0.0045 76  LYS A CD  
591  C CE  . LYS A 97  ? 0.5671 0.6618 0.7924 -0.1005 0.0536  -0.0038 76  LYS A CE  
592  N NZ  . LYS A 97  ? 0.4761 0.5896 0.7208 -0.0984 0.0655  -0.0015 76  LYS A NZ  
593  N N   . SER A 98  ? 0.4956 0.5064 0.6043 -0.0643 0.0288  -0.0075 77  SER A N   
594  C CA  . SER A 98  ? 0.4432 0.4470 0.5368 -0.0547 0.0269  -0.0076 77  SER A CA  
595  C C   . SER A 98  ? 0.4444 0.4288 0.5168 -0.0544 0.0234  -0.0076 77  SER A C   
596  O O   . SER A 98  ? 0.4957 0.4704 0.5640 -0.0609 0.0238  -0.0073 77  SER A O   
597  C CB  . SER A 98  ? 0.4223 0.4265 0.5121 -0.0498 0.0372  -0.0053 77  SER A CB  
598  O OG  . SER A 98  ? 0.4830 0.5051 0.5934 -0.0494 0.0420  -0.0053 77  SER A OG  
599  N N   . THR A 99  ? 0.3606 0.3395 0.4203 -0.0468 0.0203  -0.0079 78  THR A N   
600  C CA  . THR A 99  ? 0.4069 0.3698 0.4479 -0.0449 0.0173  -0.0077 78  THR A CA  
601  C C   . THR A 99  ? 0.3501 0.3054 0.3775 -0.0401 0.0235  -0.0048 78  THR A C   
602  O O   . THR A 99  ? 0.3535 0.3129 0.3792 -0.0343 0.0238  -0.0052 78  THR A O   
603  C CB  . THR A 99  ? 0.4072 0.3707 0.4447 -0.0407 0.0080  -0.0103 78  THR A CB  
604  O OG1 . THR A 99  ? 0.4654 0.4363 0.5141 -0.0456 0.0016  -0.0130 78  THR A OG1 
605  C CG2 . THR A 99  ? 0.4218 0.3704 0.4417 -0.0384 0.0058  -0.0101 78  THR A CG2 
606  N N   . ILE A 100 ? 0.3783 0.3220 0.3958 -0.0428 0.0282  -0.0019 79  ILE A N   
607  C CA  . ILE A 100 ? 0.3591 0.2946 0.3616 -0.0390 0.0329  0.0012  79  ILE A CA  
608  C C   . ILE A 100 ? 0.3626 0.2840 0.3509 -0.0376 0.0293  0.0028  79  ILE A C   
609  O O   . ILE A 100 ? 0.3480 0.2618 0.3366 -0.0419 0.0287  0.0033  79  ILE A O   
610  C CB  . ILE A 100 ? 0.3787 0.3138 0.3815 -0.0428 0.0429  0.0046  79  ILE A CB  
611  C CG1 . ILE A 100 ? 0.3523 0.2791 0.3373 -0.0386 0.0467  0.0077  79  ILE A CG1 
612  C CG2 . ILE A 100 ? 0.4518 0.3794 0.4568 -0.0501 0.0451  0.0068  79  ILE A CG2 
613  C CD1 . ILE A 100 ? 0.3844 0.3147 0.3691 -0.0400 0.0568  0.0096  79  ILE A CD1 
614  N N   . PHE A 101 ? 0.3541 0.2720 0.3307 -0.0317 0.0269  0.0034  80  PHE A N   
615  C CA  . PHE A 101 ? 0.3020 0.2094 0.2677 -0.0291 0.0229  0.0047  80  PHE A CA  
616  C C   . PHE A 101 ? 0.3167 0.2220 0.2701 -0.0239 0.0226  0.0069  80  PHE A C   
617  O O   . PHE A 101 ? 0.3368 0.2479 0.2894 -0.0224 0.0247  0.0061  80  PHE A O   
618  C CB  . PHE A 101 ? 0.3549 0.2640 0.3247 -0.0281 0.0157  0.0007  80  PHE A CB  
619  C CG  . PHE A 101 ? 0.3093 0.2272 0.2811 -0.0240 0.0118  -0.0018 80  PHE A CG  
620  C CD1 . PHE A 101 ? 0.3037 0.2326 0.2871 -0.0250 0.0118  -0.0041 80  PHE A CD1 
621  C CD2 . PHE A 101 ? 0.2850 0.2004 0.2481 -0.0192 0.0083  -0.0017 80  PHE A CD2 
622  C CE1 . PHE A 101 ? 0.3416 0.2766 0.3263 -0.0209 0.0083  -0.0059 80  PHE A CE1 
623  C CE2 . PHE A 101 ? 0.3367 0.2587 0.3013 -0.0161 0.0050  -0.0038 80  PHE A CE2 
624  C CZ  . PHE A 101 ? 0.3540 0.2848 0.3287 -0.0168 0.0051  -0.0058 80  PHE A CZ  
625  N N   . VAL A 102 ? 0.3164 0.2130 0.2604 -0.0213 0.0200  0.0094  81  VAL A N   
626  C CA  . VAL A 102 ? 0.2875 0.1830 0.2206 -0.0167 0.0180  0.0114  81  VAL A CA  
627  C C   . VAL A 102 ? 0.3138 0.2140 0.2490 -0.0133 0.0118  0.0081  81  VAL A C   
628  O O   . VAL A 102 ? 0.2866 0.1850 0.2256 -0.0130 0.0088  0.0063  81  VAL A O   
629  C CB  . VAL A 102 ? 0.3193 0.2044 0.2427 -0.0152 0.0183  0.0169  81  VAL A CB  
630  C CG1 . VAL A 102 ? 0.3084 0.1945 0.2222 -0.0105 0.0146  0.0190  81  VAL A CG1 
631  C CG2 . VAL A 102 ? 0.3482 0.2274 0.2677 -0.0189 0.0250  0.0210  81  VAL A CG2 
632  N N   . GLN A 103 ? 0.2914 0.1966 0.2230 -0.0110 0.0104  0.0071  82  GLN A N   
633  C CA  . GLN A 103 ? 0.3491 0.2589 0.2828 -0.0086 0.0054  0.0041  82  GLN A CA  
634  C C   . GLN A 103 ? 0.3073 0.2138 0.2384 -0.0059 0.0016  0.0055  82  GLN A C   
635  O O   . GLN A 103 ? 0.2775 0.1855 0.2130 -0.0052 -0.0012 0.0029  82  GLN A O   
636  C CB  . GLN A 103 ? 0.3311 0.2443 0.2596 -0.0073 0.0051  0.0033  82  GLN A CB  
637  C CG  . GLN A 103 ? 0.3230 0.2406 0.2542 -0.0057 0.0009  0.0003  82  GLN A CG  
638  C CD  . GLN A 103 ? 0.3472 0.2655 0.2713 -0.0051 0.0006  -0.0004 82  GLN A CD  
639  O OE1 . GLN A 103 ? 0.3834 0.2991 0.2988 -0.0055 0.0022  0.0016  82  GLN A OE1 
640  N NE2 . GLN A 103 ? 0.3941 0.3150 0.3207 -0.0044 -0.0015 -0.0032 82  GLN A NE2 
641  N N   . SER A 104 ? 0.3349 0.2369 0.2587 -0.0041 0.0017  0.0096  83  SER A N   
642  C CA  . SER A 104 ? 0.3244 0.2245 0.2470 -0.0005 -0.0015 0.0113  83  SER A CA  
643  C C   . SER A 104 ? 0.3700 0.2638 0.2968 -0.0005 -0.0006 0.0104  83  SER A C   
644  O O   . SER A 104 ? 0.3445 0.2371 0.2718 0.0029  -0.0025 0.0104  83  SER A O   
645  C CB  . SER A 104 ? 0.3399 0.2371 0.2546 0.0020  -0.0020 0.0168  83  SER A CB  
646  O OG  . SER A 104 ? 0.3348 0.2235 0.2461 0.0007  0.0017  0.0205  83  SER A OG  
647  N N   . HIS A 105 ? 0.3267 0.2165 0.2567 -0.0045 0.0025  0.0093  84  HIS A N   
648  C CA  . HIS A 105 ? 0.3534 0.2361 0.2865 -0.0058 0.0032  0.0074  84  HIS A CA  
649  C C   . HIS A 105 ? 0.3495 0.2368 0.2878 -0.0069 0.0003  0.0019  84  HIS A C   
650  O O   . HIS A 105 ? 0.3519 0.2330 0.2911 -0.0080 0.0002  -0.0006 84  HIS A O   
651  C CB  . HIS A 105 ? 0.3668 0.2439 0.3020 -0.0110 0.0073  0.0083  84  HIS A CB  
652  C CG  . HIS A 105 ? 0.3541 0.2239 0.2826 -0.0104 0.0107  0.0143  84  HIS A CG  
653  N ND1 . HIS A 105 ? 0.4021 0.2670 0.3312 -0.0153 0.0156  0.0164  84  HIS A ND1 
654  C CD2 . HIS A 105 ? 0.3921 0.2590 0.3130 -0.0056 0.0098  0.0193  84  HIS A CD2 
655  C CE1 . HIS A 105 ? 0.4452 0.3031 0.3656 -0.0135 0.0178  0.0226  84  HIS A CE1 
656  N NE2 . HIS A 105 ? 0.4376 0.2968 0.3530 -0.0074 0.0138  0.0245  84  HIS A NE2 
657  N N   . VAL A 106 ? 0.3129 0.2096 0.2533 -0.0067 -0.0019 0.0001  85  VAL A N   
658  C CA  . VAL A 106 ? 0.3567 0.2579 0.3008 -0.0075 -0.0050 -0.0042 85  VAL A CA  
659  C C   . VAL A 106 ? 0.2818 0.1873 0.2230 -0.0037 -0.0075 -0.0042 85  VAL A C   
660  O O   . VAL A 106 ? 0.2932 0.2047 0.2345 -0.0032 -0.0084 -0.0036 85  VAL A O   
661  C CB  . VAL A 106 ? 0.3373 0.2455 0.2881 -0.0108 -0.0052 -0.0059 85  VAL A CB  
662  C CG1 . VAL A 106 ? 0.3271 0.2403 0.2808 -0.0111 -0.0094 -0.0093 85  VAL A CG1 
663  C CG2 . VAL A 106 ? 0.3341 0.2396 0.2896 -0.0154 -0.0023 -0.0058 85  VAL A CG2 
664  N N   . PRO A 107 ? 0.3074 0.2097 0.2460 -0.0012 -0.0082 -0.0049 86  PRO A N   
665  C CA  . PRO A 107 ? 0.3314 0.2388 0.2684 0.0021  -0.0098 -0.0043 86  PRO A CA  
666  C C   . PRO A 107 ? 0.3386 0.2523 0.2768 0.0007  -0.0122 -0.0063 86  PRO A C   
667  O O   . PRO A 107 ? 0.2832 0.2016 0.2205 0.0021  -0.0132 -0.0053 86  PRO A O   
668  C CB  . PRO A 107 ? 0.3645 0.2669 0.2996 0.0047  -0.0088 -0.0056 86  PRO A CB  
669  C CG  . PRO A 107 ? 0.4049 0.2978 0.3394 0.0039  -0.0065 -0.0054 86  PRO A CG  
670  C CD  . PRO A 107 ? 0.3557 0.2490 0.2929 -0.0011 -0.0067 -0.0062 86  PRO A CD  
671  N N   . GLU A 108 ? 0.3159 0.2299 0.2564 -0.0021 -0.0134 -0.0089 87  GLU A N   
672  C CA  . GLU A 108 ? 0.3000 0.2191 0.2415 -0.0026 -0.0161 -0.0101 87  GLU A CA  
673  C C   . GLU A 108 ? 0.3143 0.2376 0.2571 -0.0022 -0.0160 -0.0084 87  GLU A C   
674  O O   . GLU A 108 ? 0.3032 0.2291 0.2453 -0.0017 -0.0178 -0.0085 87  GLU A O   
675  C CB  . GLU A 108 ? 0.3097 0.2295 0.2547 -0.0055 -0.0183 -0.0125 87  GLU A CB  
676  C CG  . GLU A 108 ? 0.3156 0.2306 0.2569 -0.0068 -0.0195 -0.0154 87  GLU A CG  
677  C CD  . GLU A 108 ? 0.3877 0.2957 0.3292 -0.0084 -0.0170 -0.0163 87  GLU A CD  
678  O OE1 . GLU A 108 ? 0.4463 0.3537 0.3913 -0.0089 -0.0145 -0.0142 87  GLU A OE1 
679  O OE2 . GLU A 108 ? 0.4543 0.3562 0.3914 -0.0092 -0.0172 -0.0193 87  GLU A OE2 
680  N N   . HIS A 109 ? 0.2899 0.2128 0.2335 -0.0025 -0.0137 -0.0069 88  HIS A N   
681  C CA  . HIS A 109 ? 0.2910 0.2163 0.2338 -0.0022 -0.0132 -0.0062 88  HIS A CA  
682  C C   . HIS A 109 ? 0.2564 0.1829 0.1950 -0.0009 -0.0145 -0.0051 88  HIS A C   
683  O O   . HIS A 109 ? 0.2862 0.2142 0.2243 -0.0011 -0.0156 -0.0057 88  HIS A O   
684  C CB  . HIS A 109 ? 0.2997 0.2236 0.2420 -0.0030 -0.0099 -0.0049 88  HIS A CB  
685  C CG  . HIS A 109 ? 0.2721 0.1971 0.2206 -0.0049 -0.0079 -0.0059 88  HIS A CG  
686  N ND1 . HIS A 109 ? 0.3123 0.2400 0.2639 -0.0052 -0.0055 -0.0066 88  HIS A ND1 
687  C CD2 . HIS A 109 ? 0.2954 0.2195 0.2485 -0.0069 -0.0079 -0.0067 88  HIS A CD2 
688  C CE1 . HIS A 109 ? 0.2737 0.2039 0.2330 -0.0071 -0.0040 -0.0072 88  HIS A CE1 
689  N NE2 . HIS A 109 ? 0.2767 0.2048 0.2369 -0.0086 -0.0058 -0.0074 88  HIS A NE2 
690  N N   . ALA A 110 ? 0.2656 0.1914 0.2020 0.0003  -0.0143 -0.0034 89  ALA A N   
691  C CA  . ALA A 110 ? 0.2427 0.1718 0.1773 0.0011  -0.0158 -0.0022 89  ALA A CA  
692  C C   . ALA A 110 ? 0.3209 0.2518 0.2564 0.0012  -0.0168 -0.0034 89  ALA A C   
693  O O   . ALA A 110 ? 0.2875 0.2213 0.2225 0.0003  -0.0179 -0.0031 89  ALA A O   
694  C CB  . ALA A 110 ? 0.3154 0.2449 0.2493 0.0034  -0.0156 0.0004  89  ALA A CB  
695  N N   . GLN A 111 ? 0.2612 0.1899 0.1973 0.0018  -0.0164 -0.0047 90  GLN A N   
696  C CA  . GLN A 111 ? 0.2663 0.1959 0.2011 0.0018  -0.0170 -0.0057 90  GLN A CA  
697  C C   . GLN A 111 ? 0.3061 0.2364 0.2404 0.0002  -0.0188 -0.0059 90  GLN A C   
698  O O   . GLN A 111 ? 0.3049 0.2368 0.2377 -0.0004 -0.0190 -0.0051 90  GLN A O   
699  C CB  . GLN A 111 ? 0.2532 0.1788 0.1864 0.0021  -0.0166 -0.0079 90  GLN A CB  
700  C CG  . GLN A 111 ? 0.2895 0.2121 0.2226 0.0044  -0.0143 -0.0078 90  GLN A CG  
701  C CD  . GLN A 111 ? 0.3048 0.2212 0.2353 0.0038  -0.0138 -0.0110 90  GLN A CD  
702  O OE1 . GLN A 111 ? 0.3536 0.2661 0.2855 0.0022  -0.0139 -0.0119 90  GLN A OE1 
703  N NE2 . GLN A 111 ? 0.3282 0.2437 0.2545 0.0045  -0.0130 -0.0128 90  GLN A NE2 
704  N N   . LEU A 112 ? 0.2702 0.1991 0.2065 -0.0005 -0.0196 -0.0068 91  LEU A N   
705  C CA  . LEU A 112 ? 0.3122 0.2411 0.2490 -0.0009 -0.0212 -0.0067 91  LEU A CA  
706  C C   . LEU A 112 ? 0.2906 0.2193 0.2267 -0.0015 -0.0203 -0.0060 91  LEU A C   
707  O O   . LEU A 112 ? 0.2932 0.2203 0.2280 -0.0019 -0.0211 -0.0055 91  LEU A O   
708  C CB  . LEU A 112 ? 0.2875 0.2168 0.2289 -0.0008 -0.0221 -0.0077 91  LEU A CB  
709  C CG  . LEU A 112 ? 0.3147 0.2438 0.2578 0.0001  -0.0238 -0.0070 91  LEU A CG  
710  C CD1 . LEU A 112 ? 0.3543 0.2822 0.2929 0.0002  -0.0265 -0.0059 91  LEU A CD1 
711  C CD2 . LEU A 112 ? 0.3572 0.2891 0.3076 0.0008  -0.0245 -0.0078 91  LEU A CD2 
712  N N   . GLY A 113 ? 0.3175 0.2469 0.2533 -0.0017 -0.0189 -0.0058 92  GLY A N   
713  C CA  . GLY A 113 ? 0.3138 0.2427 0.2471 -0.0030 -0.0187 -0.0058 92  GLY A CA  
714  C C   . GLY A 113 ? 0.3776 0.3081 0.3093 -0.0045 -0.0198 -0.0048 92  GLY A C   
715  O O   . GLY A 113 ? 0.3480 0.2762 0.2779 -0.0064 -0.0202 -0.0052 92  GLY A O   
716  N N   . TRP A 114 ? 0.3175 0.2518 0.2504 -0.0039 -0.0199 -0.0036 93  TRP A N   
717  C CA  . TRP A 114 ? 0.3475 0.2850 0.2804 -0.0056 -0.0201 -0.0025 93  TRP A CA  
718  C C   . TRP A 114 ? 0.3516 0.2858 0.2828 -0.0066 -0.0201 -0.0023 93  TRP A C   
719  O O   . TRP A 114 ? 0.3047 0.2381 0.2349 -0.0094 -0.0203 -0.0017 93  TRP A O   
720  C CB  . TRP A 114 ? 0.3302 0.2730 0.2657 -0.0038 -0.0191 -0.0013 93  TRP A CB  
721  C CG  . TRP A 114 ? 0.3123 0.2590 0.2489 -0.0057 -0.0184 -0.0002 93  TRP A CG  
722  C CD1 . TRP A 114 ? 0.3328 0.2789 0.2679 -0.0054 -0.0165 0.0001  93  TRP A CD1 
723  C CD2 . TRP A 114 ? 0.3211 0.2726 0.2600 -0.0092 -0.0194 0.0008  93  TRP A CD2 
724  N NE1 . TRP A 114 ? 0.3821 0.3326 0.3190 -0.0082 -0.0155 0.0016  93  TRP A NE1 
725  C CE2 . TRP A 114 ? 0.3407 0.2949 0.2808 -0.0108 -0.0174 0.0020  93  TRP A CE2 
726  C CE3 . TRP A 114 ? 0.3466 0.3005 0.2862 -0.0115 -0.0218 0.0008  93  TRP A CE3 
727  C CZ2 . TRP A 114 ? 0.3684 0.3282 0.3120 -0.0151 -0.0176 0.0032  93  TRP A CZ2 
728  C CZ3 . TRP A 114 ? 0.3369 0.2962 0.2793 -0.0158 -0.0229 0.0016  93  TRP A CZ3 
729  C CH2 . TRP A 114 ? 0.3649 0.3274 0.3102 -0.0178 -0.0207 0.0028  93  TRP A CH2 
730  N N   . ALA A 115 ? 0.3147 0.2466 0.2449 -0.0047 -0.0202 -0.0027 94  ALA A N   
731  C CA  . ALA A 115 ? 0.3253 0.2539 0.2524 -0.0053 -0.0208 -0.0017 94  ALA A CA  
732  C C   . ALA A 115 ? 0.3022 0.2257 0.2288 -0.0061 -0.0217 -0.0014 94  ALA A C   
733  O O   . ALA A 115 ? 0.2961 0.2162 0.2200 -0.0077 -0.0217 0.0002  94  ALA A O   
734  C CB  . ALA A 115 ? 0.2758 0.2033 0.2014 -0.0033 -0.0219 -0.0024 94  ALA A CB  
735  N N   . LEU A 116 ? 0.3821 0.3043 0.3111 -0.0049 -0.0219 -0.0030 95  LEU A N   
736  C CA  . LEU A 116 ? 0.3256 0.2420 0.2543 -0.0047 -0.0219 -0.0033 95  LEU A CA  
737  C C   . LEU A 116 ? 0.2711 0.1847 0.1973 -0.0081 -0.0210 -0.0040 95  LEU A C   
738  O O   . LEU A 116 ? 0.3156 0.2221 0.2400 -0.0086 -0.0207 -0.0041 95  LEU A O   
739  C CB  . LEU A 116 ? 0.3469 0.2634 0.2794 -0.0023 -0.0212 -0.0051 95  LEU A CB  
740  C CG  . LEU A 116 ? 0.3421 0.2612 0.2787 0.0004  -0.0228 -0.0047 95  LEU A CG  
741  C CD1 . LEU A 116 ? 0.3481 0.2684 0.2902 0.0022  -0.0212 -0.0063 95  LEU A CD1 
742  C CD2 . LEU A 116 ? 0.3774 0.2936 0.3130 0.0017  -0.0253 -0.0024 95  LEU A CD2 
743  N N   . ASN A 117 ? 0.2594 0.1783 0.1856 -0.0104 -0.0209 -0.0042 96  ASN A N   
744  C CA  . ASN A 117 ? 0.2695 0.1872 0.1937 -0.0148 -0.0212 -0.0047 96  ASN A CA  
745  C C   . ASN A 117 ? 0.3167 0.2304 0.2394 -0.0173 -0.0209 -0.0028 96  ASN A C   
746  O O   . ASN A 117 ? 0.2907 0.1975 0.2108 -0.0205 -0.0207 -0.0036 96  ASN A O   
747  C CB  . ASN A 117 ? 0.3232 0.2498 0.2494 -0.0165 -0.0220 -0.0042 96  ASN A CB  
748  C CG  . ASN A 117 ? 0.3779 0.3059 0.3027 -0.0162 -0.0227 -0.0059 96  ASN A CG  
749  O OD1 . ASN A 117 ? 0.3949 0.3165 0.3158 -0.0165 -0.0221 -0.0081 96  ASN A OD1 
750  N ND2 . ASN A 117 ? 0.3580 0.2937 0.2852 -0.0153 -0.0237 -0.0045 96  ASN A ND2 
751  N N   . CYS A 118 ? 0.2759 0.1925 0.1992 -0.0162 -0.0205 -0.0003 97  CYS A N   
752  C CA  . CYS A 118 ? 0.3139 0.2271 0.2347 -0.0188 -0.0196 0.0023  97  CYS A CA  
753  C C   . CYS A 118 ? 0.3052 0.2075 0.2224 -0.0172 -0.0201 0.0035  97  CYS A C   
754  O O   . CYS A 118 ? 0.3673 0.2642 0.2811 -0.0195 -0.0193 0.0062  97  CYS A O   
755  C CB  . CYS A 118 ? 0.2935 0.2125 0.2140 -0.0175 -0.0185 0.0043  97  CYS A CB  
756  S SG  . CYS A 118 ? 0.3545 0.2859 0.2807 -0.0177 -0.0173 0.0035  97  CYS A SG  
757  N N   . TYR A 119 ? 0.3160 0.2153 0.2343 -0.0131 -0.0210 0.0019  98  TYR A N   
758  C CA  . TYR A 119 ? 0.2876 0.1775 0.2045 -0.0103 -0.0216 0.0031  98  TYR A CA  
759  C C   . TYR A 119 ? 0.3272 0.2107 0.2449 -0.0098 -0.0204 -0.0001 98  TYR A C   
760  O O   . TYR A 119 ? 0.3491 0.2265 0.2680 -0.0056 -0.0203 0.0000  98  TYR A O   
761  C CB  . TYR A 119 ? 0.3222 0.2154 0.2412 -0.0052 -0.0237 0.0044  98  TYR A CB  
762  C CG  . TYR A 119 ? 0.3912 0.2885 0.3067 -0.0059 -0.0246 0.0070  98  TYR A CG  
763  C CD1 . TYR A 119 ? 0.3004 0.2062 0.2171 -0.0065 -0.0242 0.0054  98  TYR A CD1 
764  C CD2 . TYR A 119 ? 0.3977 0.2893 0.3078 -0.0058 -0.0256 0.0111  98  TYR A CD2 
765  C CE1 . TYR A 119 ? 0.3475 0.2558 0.2598 -0.0070 -0.0241 0.0070  98  TYR A CE1 
766  C CE2 . TYR A 119 ? 0.3639 0.2586 0.2686 -0.0066 -0.0259 0.0132  98  TYR A CE2 
767  C CZ  . TYR A 119 ? 0.3336 0.2367 0.2395 -0.0072 -0.0249 0.0107  98  TYR A CZ  
768  O OH  . TYR A 119 ? 0.3806 0.2857 0.2802 -0.0078 -0.0242 0.0120  98  TYR A OH  
769  N N   . THR A 120 ? 0.3732 0.2583 0.2899 -0.0137 -0.0194 -0.0031 99  THR A N   
770  C CA  . THR A 120 ? 0.2918 0.1703 0.2065 -0.0143 -0.0180 -0.0070 99  THR A CA  
771  C C   . THR A 120 ? 0.2928 0.1656 0.2031 -0.0211 -0.0178 -0.0082 99  THR A C   
772  O O   . THR A 120 ? 0.3384 0.2187 0.2495 -0.0256 -0.0190 -0.0072 99  THR A O   
773  C CB  . THR A 120 ? 0.3033 0.1891 0.2192 -0.0135 -0.0176 -0.0099 99  THR A CB  
774  O OG1 . THR A 120 ? 0.3635 0.2557 0.2844 -0.0086 -0.0178 -0.0087 99  THR A OG1 
775  C CG2 . THR A 120 ? 0.3179 0.1959 0.2299 -0.0134 -0.0153 -0.0142 99  THR A CG2 
776  N N   . TYR A 121 ? 0.3317 0.1913 0.2379 -0.0218 -0.0162 -0.0103 100 TYR A N   
777  C CA  . TYR A 121 ? 0.3736 0.2262 0.2752 -0.0293 -0.0162 -0.0121 100 TYR A CA  
778  C C   . TYR A 121 ? 0.3210 0.1773 0.2194 -0.0333 -0.0171 -0.0170 100 TYR A C   
779  O O   . TYR A 121 ? 0.3572 0.2127 0.2536 -0.0298 -0.0158 -0.0202 100 TYR A O   
780  C CB  . TYR A 121 ? 0.3700 0.2045 0.2673 -0.0287 -0.0139 -0.0129 100 TYR A CB  
781  C CG  . TYR A 121 ? 0.3974 0.2262 0.2956 -0.0269 -0.0138 -0.0072 100 TYR A CG  
782  C CD1 . TYR A 121 ? 0.4404 0.2683 0.3371 -0.0335 -0.0142 -0.0040 100 TYR A CD1 
783  C CD2 . TYR A 121 ? 0.3785 0.2032 0.2790 -0.0186 -0.0134 -0.0045 100 TYR A CD2 
784  C CE1 . TYR A 121 ? 0.4888 0.3106 0.3844 -0.0321 -0.0138 0.0018  100 TYR A CE1 
785  C CE2 . TYR A 121 ? 0.4164 0.2355 0.3161 -0.0168 -0.0140 0.0014  100 TYR A CE2 
786  C CZ  . TYR A 121 ? 0.4563 0.2732 0.3526 -0.0236 -0.0140 0.0046  100 TYR A CZ  
787  O OH  . TYR A 121 ? 0.5307 0.3412 0.4244 -0.0219 -0.0143 0.0110  100 TYR A OH  
788  N N   . PHE A 122 ? 0.3755 0.2363 0.2734 -0.0410 -0.0193 -0.0172 101 PHE A N   
789  C CA  . PHE A 122 ? 0.3951 0.2591 0.2889 -0.0460 -0.0214 -0.0216 101 PHE A CA  
790  C C   . PHE A 122 ? 0.4233 0.2719 0.3081 -0.0461 -0.0192 -0.0273 101 PHE A C   
791  O O   . PHE A 122 ? 0.4094 0.2595 0.2891 -0.0455 -0.0194 -0.0310 101 PHE A O   
792  C CB  . PHE A 122 ? 0.4101 0.2795 0.3058 -0.0551 -0.0244 -0.0210 101 PHE A CB  
793  C CG  . PHE A 122 ? 0.5086 0.3817 0.3997 -0.0612 -0.0280 -0.0253 101 PHE A CG  
794  C CD1 . PHE A 122 ? 0.5448 0.4038 0.4265 -0.0667 -0.0279 -0.0309 101 PHE A CD1 
795  C CD2 . PHE A 122 ? 0.4905 0.3806 0.3861 -0.0613 -0.0317 -0.0236 101 PHE A CD2 
796  C CE1 . PHE A 122 ? 0.5387 0.4011 0.4145 -0.0729 -0.0321 -0.0351 101 PHE A CE1 
797  C CE2 . PHE A 122 ? 0.4504 0.3445 0.3411 -0.0668 -0.0361 -0.0269 101 PHE A CE2 
798  C CZ  . PHE A 122 ? 0.4796 0.3603 0.3600 -0.0730 -0.0366 -0.0328 101 PHE A CZ  
799  N N   . GLY A 123 ? 0.3995 0.2324 0.2814 -0.0468 -0.0167 -0.0281 102 GLY A N   
800  C CA  . GLY A 123 ? 0.4631 0.2794 0.3361 -0.0466 -0.0137 -0.0340 102 GLY A CA  
801  C C   . GLY A 123 ? 0.4411 0.2561 0.3142 -0.0373 -0.0100 -0.0354 102 GLY A C   
802  O O   . GLY A 123 ? 0.4019 0.2081 0.2672 -0.0368 -0.0071 -0.0412 102 GLY A O   
803  N N   . GLU A 124 ? 0.3963 0.2204 0.2783 -0.0302 -0.0097 -0.0304 103 GLU A N   
804  C CA  . GLU A 124 ? 0.4192 0.2449 0.3037 -0.0221 -0.0063 -0.0313 103 GLU A CA  
805  C C   . GLU A 124 ? 0.4769 0.3120 0.3579 -0.0232 -0.0066 -0.0340 103 GLU A C   
806  O O   . GLU A 124 ? 0.4285 0.2599 0.3061 -0.0197 -0.0025 -0.0376 103 GLU A O   
807  C CB  . GLU A 124 ? 0.4129 0.2471 0.3078 -0.0156 -0.0071 -0.0254 103 GLU A CB  
808  C CG  . GLU A 124 ? 0.4900 0.3135 0.3872 -0.0125 -0.0064 -0.0222 103 GLU A CG  
809  C CD  . GLU A 124 ? 0.4488 0.2810 0.3546 -0.0068 -0.0084 -0.0163 103 GLU A CD  
810  O OE1 . GLU A 124 ? 0.3959 0.2407 0.3044 -0.0087 -0.0114 -0.0136 103 GLU A OE1 
811  O OE2 . GLU A 124 ? 0.4204 0.2468 0.3301 -0.0003 -0.0071 -0.0144 103 GLU A OE2 
812  N N   . LEU A 125 ? 0.3668 0.2139 0.2486 -0.0279 -0.0111 -0.0320 104 LEU A N   
813  C CA  . LEU A 125 ? 0.3571 0.2121 0.2342 -0.0294 -0.0122 -0.0337 104 LEU A CA  
814  C C   . LEU A 125 ? 0.4622 0.3089 0.3268 -0.0358 -0.0128 -0.0395 104 LEU A C   
815  O O   . LEU A 125 ? 0.4509 0.2976 0.3076 -0.0354 -0.0114 -0.0425 104 LEU A O   
816  C CB  . LEU A 125 ? 0.3538 0.2242 0.2367 -0.0312 -0.0169 -0.0291 104 LEU A CB  
817  C CG  . LEU A 125 ? 0.3514 0.2300 0.2447 -0.0256 -0.0165 -0.0242 104 LEU A CG  
818  C CD1 . LEU A 125 ? 0.3242 0.2160 0.2225 -0.0274 -0.0204 -0.0204 104 LEU A CD1 
819  C CD2 . LEU A 125 ? 0.3638 0.2436 0.2584 -0.0196 -0.0131 -0.0245 104 LEU A CD2 
820  N N   . SER A 126 ? 0.4475 0.2866 0.3092 -0.0422 -0.0148 -0.0412 105 SER A N   
821  C CA  . SER A 126 ? 0.4957 0.3257 0.3447 -0.0494 -0.0160 -0.0475 105 SER A CA  
822  C C   . SER A 126 ? 0.5712 0.3853 0.4106 -0.0458 -0.0096 -0.0536 105 SER A C   
823  O O   . SER A 126 ? 0.5124 0.3222 0.3391 -0.0488 -0.0091 -0.0589 105 SER A O   
824  C CB  . SER A 126 ? 0.5302 0.3544 0.3795 -0.0575 -0.0189 -0.0480 105 SER A CB  
825  O OG  . SER A 126 ? 0.6729 0.4876 0.5094 -0.0655 -0.0206 -0.0548 105 SER A OG  
826  N N   . ARG A 127 ? 0.5499 0.3552 0.3949 -0.0391 -0.0045 -0.0527 106 ARG A N   
827  C CA  . ARG A 127 ? 0.5692 0.3602 0.4076 -0.0342 0.0027  -0.0581 106 ARG A CA  
828  C C   . ARG A 127 ? 0.5303 0.3297 0.3691 -0.0280 0.0065  -0.0582 106 ARG A C   
829  O O   . ARG A 127 ? 0.6099 0.3993 0.4425 -0.0241 0.0133  -0.0631 106 ARG A O   
830  C CB  . ARG A 127 ? 0.5826 0.3628 0.4286 -0.0280 0.0065  -0.0562 106 ARG A CB  
831  C CG  . ARG A 127 ? 0.5615 0.3271 0.4037 -0.0342 0.0048  -0.0575 106 ARG A CG  
832  C CD  . ARG A 127 ? 0.6596 0.4111 0.5069 -0.0271 0.0093  -0.0558 106 ARG A CD  
833  N NE  . ARG A 127 ? 0.5873 0.3507 0.4486 -0.0205 0.0077  -0.0476 106 ARG A NE  
834  C CZ  . ARG A 127 ? 0.5594 0.3267 0.4260 -0.0234 0.0034  -0.0416 106 ARG A CZ  
835  N NH1 . ARG A 127 ? 0.5177 0.2794 0.3791 -0.0329 0.0006  -0.0423 106 ARG A NH1 
836  N NH2 . ARG A 127 ? 0.4482 0.2256 0.3255 -0.0170 0.0021  -0.0349 106 ARG A NH2 
837  N N   . MET A 128 ? 0.5713 0.3879 0.4171 -0.0270 0.0031  -0.0529 107 MET A N   
838  C CA  . MET A 128 ? 0.6472 0.4713 0.4920 -0.0230 0.0065  -0.0526 107 MET A CA  
839  C C   . MET A 128 ? 0.6887 0.5089 0.5164 -0.0286 0.0063  -0.0578 107 MET A C   
840  O O   . MET A 128 ? 0.7478 0.5758 0.5711 -0.0344 -0.0003 -0.0562 107 MET A O   
841  C CB  . MET A 128 ? 0.6835 0.5248 0.5390 -0.0213 0.0026  -0.0457 107 MET A CB  
842  C CG  . MET A 128 ? 0.5630 0.4088 0.4337 -0.0162 0.0023  -0.0409 107 MET A CG  
843  S SD  . MET A 128 ? 0.8068 0.6476 0.6853 -0.0071 0.0099  -0.0418 107 MET A SD  
844  C CE  . MET A 128 ? 0.5935 0.4419 0.4694 -0.0053 0.0147  -0.0428 107 MET A CE  
845  N N   . THR A 129 ? 0.8375 0.6454 0.6549 -0.0267 0.0134  -0.0640 108 THR A N   
846  C CA  . THR A 129 ? 0.8269 0.6290 0.6249 -0.0322 0.0135  -0.0696 108 THR A CA  
847  C C   . THR A 129 ? 0.9191 0.7349 0.7142 -0.0326 0.0112  -0.0655 108 THR A C   
848  O O   . THR A 129 ? 1.0044 0.8240 0.7893 -0.0391 0.0046  -0.0654 108 THR A O   
849  C CB  . THR A 129 ? 0.8706 0.6569 0.6584 -0.0287 0.0234  -0.0770 108 THR A CB  
850  O OG1 . THR A 129 ? 0.7983 0.5906 0.5969 -0.0199 0.0309  -0.0744 108 THR A OG1 
851  C CG2 . THR A 129 ? 0.8253 0.5949 0.6133 -0.0289 0.0253  -0.0815 108 THR A CG2 
852  N N   . GLN A 130 ? 1.0388 0.8621 0.8431 -0.0259 0.0164  -0.0617 109 GLN A N   
853  C CA  . GLN A 130 ? 1.0344 0.8693 0.8368 -0.0258 0.0150  -0.0570 109 GLN A CA  
854  C C   . GLN A 130 ? 0.9842 0.8328 0.8054 -0.0223 0.0119  -0.0494 109 GLN A C   
855  O O   . GLN A 130 ? 0.9787 0.8348 0.8048 -0.0251 0.0041  -0.0456 109 GLN A O   
856  C CB  . GLN A 130 ? 1.0604 0.8917 0.8551 -0.0223 0.0247  -0.0595 109 GLN A CB  
857  C CG  . GLN A 130 ? 1.1483 0.9887 0.9378 -0.0231 0.0238  -0.0545 109 GLN A CG  
858  C CD  . GLN A 130 ? 1.2782 1.1126 1.0536 -0.0220 0.0332  -0.0578 109 GLN A CD  
859  O OE1 . GLN A 130 ? 1.2559 1.0876 1.0123 -0.0263 0.0316  -0.0586 109 GLN A OE1 
860  N NE2 . GLN A 130 ? 1.2914 1.1242 1.0760 -0.0162 0.0432  -0.0595 109 GLN A NE2 
861  N N   . ALA A 139 ? 0.9070 0.7545 0.5993 -0.0806 -0.0470 -0.0657 118 ALA A N   
862  C CA  . ALA A 139 ? 1.0927 0.9540 0.8097 -0.0737 -0.0469 -0.0568 118 ALA A CA  
863  C C   . ALA A 139 ? 0.9485 0.8284 0.6731 -0.0756 -0.0590 -0.0492 118 ALA A C   
864  O O   . ALA A 139 ? 1.1686 1.0591 0.9040 -0.0692 -0.0592 -0.0408 118 ALA A O   
865  C CB  . ALA A 139 ? 0.9741 0.8325 0.7093 -0.0728 -0.0434 -0.0588 118 ALA A CB  
866  N N   . GLU A 140 ? 1.0133 0.8969 0.7329 -0.0845 -0.0689 -0.0522 119 GLU A N   
867  C CA  . GLU A 140 ? 0.9712 0.8739 0.6991 -0.0869 -0.0812 -0.0454 119 GLU A CA  
868  C C   . GLU A 140 ? 0.8722 0.7881 0.6282 -0.0840 -0.0823 -0.0402 119 GLU A C   
869  O O   . GLU A 140 ? 0.8982 0.8072 0.6643 -0.0834 -0.0758 -0.0434 119 GLU A O   
870  C CB  . GLU A 140 ? 0.9811 0.8906 0.7008 -0.0815 -0.0837 -0.0377 119 GLU A CB  
871  C CG  . GLU A 140 ? 1.0740 0.9706 0.7639 -0.0841 -0.0820 -0.0420 119 GLU A CG  
872  C CD  . GLU A 140 ? 1.0595 0.9436 0.7430 -0.0769 -0.0683 -0.0424 119 GLU A CD  
873  O OE1 . GLU A 140 ? 1.0003 0.8908 0.6935 -0.0692 -0.0654 -0.0341 119 GLU A OE1 
874  O OE2 . GLU A 140 ? 1.1240 0.9918 0.7936 -0.0789 -0.0602 -0.0510 119 GLU A OE2 
875  N N   . ASN A 141 ? 0.8843 0.8188 0.6525 -0.0819 -0.0904 -0.0320 120 ASN A N   
876  C CA  . ASN A 141 ? 0.8039 0.7523 0.5981 -0.0789 -0.0912 -0.0267 120 ASN A CA  
877  C C   . ASN A 141 ? 0.7746 0.7191 0.5777 -0.0687 -0.0813 -0.0229 120 ASN A C   
878  O O   . ASN A 141 ? 0.8108 0.7629 0.6190 -0.0617 -0.0817 -0.0156 120 ASN A O   
879  C CB  . ASN A 141 ? 0.8022 0.7715 0.6062 -0.0790 -0.1024 -0.0195 120 ASN A CB  
880  N N   . ILE A 142 ? 0.6054 0.5374 0.4105 -0.0681 -0.0726 -0.0279 121 ILE A N   
881  C CA  . ILE A 142 ? 0.5747 0.5026 0.3882 -0.0596 -0.0635 -0.0252 121 ILE A CA  
882  C C   . ILE A 142 ? 0.5583 0.5007 0.3925 -0.0547 -0.0653 -0.0181 121 ILE A C   
883  O O   . ILE A 142 ? 0.5128 0.4665 0.3584 -0.0583 -0.0709 -0.0168 121 ILE A O   
884  C CB  . ILE A 142 ? 0.5127 0.4263 0.3263 -0.0603 -0.0555 -0.0316 121 ILE A CB  
885  C CG1 . ILE A 142 ? 0.6488 0.5614 0.4747 -0.0521 -0.0479 -0.0284 121 ILE A CG1 
886  C CG2 . ILE A 142 ? 0.6787 0.5933 0.4996 -0.0674 -0.0590 -0.0347 121 ILE A CG2 
887  C CD1 . ILE A 142 ? 0.4992 0.3986 0.3263 -0.0513 -0.0403 -0.0334 121 ILE A CD1 
888  N N   . ASN A 143 ? 0.4606 0.4028 0.2997 -0.0468 -0.0600 -0.0138 122 ASN A N   
889  C CA  . ASN A 143 ? 0.4396 0.3920 0.2969 -0.0415 -0.0596 -0.0082 122 ASN A CA  
890  C C   . ASN A 143 ? 0.3945 0.3403 0.2604 -0.0392 -0.0523 -0.0105 122 ASN A C   
891  O O   . ASN A 143 ? 0.4608 0.3943 0.3195 -0.0394 -0.0466 -0.0150 122 ASN A O   
892  C CB  . ASN A 143 ? 0.3948 0.3505 0.2522 -0.0345 -0.0592 -0.0018 122 ASN A CB  
893  C CG  . ASN A 143 ? 0.3945 0.3380 0.2443 -0.0308 -0.0510 -0.0029 122 ASN A CG  
894  O OD1 . ASN A 143 ? 0.3520 0.2913 0.2096 -0.0278 -0.0449 -0.0040 122 ASN A OD1 
895  N ND2 . ASN A 143 ? 0.4728 0.4113 0.3072 -0.0310 -0.0511 -0.0021 122 ASN A ND2 
896  N N   . ALA A 144 ? 0.3962 0.3507 0.2775 -0.0366 -0.0523 -0.0072 123 ALA A N   
897  C CA  . ALA A 144 ? 0.3986 0.3481 0.2875 -0.0355 -0.0468 -0.0089 123 ALA A CA  
898  C C   . ALA A 144 ? 0.4059 0.3464 0.2927 -0.0300 -0.0402 -0.0093 123 ALA A C   
899  O O   . ALA A 144 ? 0.3434 0.2766 0.2318 -0.0296 -0.0358 -0.0120 123 ALA A O   
900  C CB  . ALA A 144 ? 0.3467 0.3076 0.2508 -0.0337 -0.0478 -0.0051 123 ALA A CB  
901  N N   . GLY A 145 ? 0.3086 0.2501 0.1926 -0.0257 -0.0395 -0.0061 124 GLY A N   
902  C CA  . GLY A 145 ? 0.3190 0.2532 0.2020 -0.0216 -0.0332 -0.0065 124 GLY A CA  
903  C C   . GLY A 145 ? 0.3871 0.3106 0.2598 -0.0235 -0.0292 -0.0114 124 GLY A C   
904  O O   . GLY A 145 ? 0.3384 0.2562 0.2142 -0.0212 -0.0239 -0.0134 124 GLY A O   
905  N N   . LEU A 146 ? 0.3851 0.3060 0.2453 -0.0275 -0.0317 -0.0136 125 LEU A N   
906  C CA  . LEU A 146 ? 0.4637 0.3733 0.3126 -0.0293 -0.0272 -0.0192 125 LEU A CA  
907  C C   . LEU A 146 ? 0.4398 0.3434 0.2932 -0.0309 -0.0251 -0.0236 125 LEU A C   
908  O O   . LEU A 146 ? 0.4315 0.3260 0.2825 -0.0291 -0.0191 -0.0271 125 LEU A O   
909  C CB  . LEU A 146 ? 0.4443 0.3521 0.2774 -0.0342 -0.0312 -0.0212 125 LEU A CB  
910  C CG  . LEU A 146 ? 0.5623 0.4585 0.3792 -0.0353 -0.0258 -0.0262 125 LEU A CG  
911  C CD1 . LEU A 146 ? 0.4917 0.3864 0.3080 -0.0302 -0.0191 -0.0234 125 LEU A CD1 
912  C CD2 . LEU A 146 ? 0.5259 0.4215 0.3259 -0.0409 -0.0317 -0.0278 125 LEU A CD2 
913  N N   . PHE A 147 ? 0.3973 0.3058 0.2578 -0.0339 -0.0297 -0.0229 126 PHE A N   
914  C CA  . PHE A 147 ? 0.3894 0.2913 0.2540 -0.0356 -0.0279 -0.0259 126 PHE A CA  
915  C C   . PHE A 147 ? 0.3855 0.2878 0.2614 -0.0299 -0.0239 -0.0235 126 PHE A C   
916  O O   . PHE A 147 ? 0.4029 0.2966 0.2797 -0.0284 -0.0200 -0.0260 126 PHE A O   
917  C CB  . PHE A 147 ? 0.3921 0.3000 0.2607 -0.0415 -0.0338 -0.0254 126 PHE A CB  
918  C CG  . PHE A 147 ? 0.4178 0.3179 0.2896 -0.0442 -0.0321 -0.0278 126 PHE A CG  
919  C CD1 . PHE A 147 ? 0.4163 0.3023 0.2783 -0.0475 -0.0299 -0.0336 126 PHE A CD1 
920  C CD2 . PHE A 147 ? 0.4026 0.3084 0.2861 -0.0436 -0.0325 -0.0242 126 PHE A CD2 
921  C CE1 . PHE A 147 ? 0.4551 0.3322 0.3197 -0.0498 -0.0282 -0.0352 126 PHE A CE1 
922  C CE2 . PHE A 147 ? 0.4153 0.3130 0.3006 -0.0463 -0.0308 -0.0255 126 PHE A CE2 
923  C CZ  . PHE A 147 ? 0.4603 0.3433 0.3364 -0.0493 -0.0289 -0.0307 126 PHE A CZ  
924  N N   . ASP A 148 ? 0.3678 0.2796 0.2521 -0.0266 -0.0251 -0.0187 127 ASP A N   
925  C CA  . ASP A 148 ? 0.3814 0.2949 0.2760 -0.0226 -0.0229 -0.0165 127 ASP A CA  
926  C C   . ASP A 148 ? 0.4245 0.3364 0.3210 -0.0176 -0.0187 -0.0159 127 ASP A C   
927  O O   . ASP A 148 ? 0.3301 0.2429 0.2344 -0.0145 -0.0174 -0.0146 127 ASP A O   
928  C CB  . ASP A 148 ? 0.4085 0.3325 0.3110 -0.0223 -0.0263 -0.0123 127 ASP A CB  
929  C CG  . ASP A 148 ? 0.4453 0.3698 0.3559 -0.0198 -0.0247 -0.0108 127 ASP A CG  
930  O OD1 . ASP A 148 ? 0.3778 0.2963 0.2884 -0.0212 -0.0236 -0.0123 127 ASP A OD1 
931  O OD2 . ASP A 148 ? 0.3921 0.3223 0.3082 -0.0166 -0.0245 -0.0080 127 ASP A OD2 
932  N N   . TYR A 149 ? 0.3841 0.2936 0.2736 -0.0171 -0.0164 -0.0169 128 TYR A N   
933  C CA  . TYR A 149 ? 0.3059 0.2159 0.1989 -0.0131 -0.0123 -0.0157 128 TYR A CA  
934  C C   . TYR A 149 ? 0.2627 0.1685 0.1613 -0.0104 -0.0082 -0.0178 128 TYR A C   
935  O O   . TYR A 149 ? 0.2906 0.1994 0.1966 -0.0075 -0.0061 -0.0162 128 TYR A O   
936  C CB  . TYR A 149 ? 0.3643 0.2723 0.2474 -0.0137 -0.0100 -0.0159 128 TYR A CB  
937  C CG  . TYR A 149 ? 0.3270 0.2268 0.2014 -0.0145 -0.0054 -0.0206 128 TYR A CG  
938  C CD1 . TYR A 149 ? 0.3815 0.2786 0.2604 -0.0113 0.0010  -0.0222 128 TYR A CD1 
939  C CD2 . TYR A 149 ? 0.4094 0.3045 0.2713 -0.0185 -0.0073 -0.0237 128 TYR A CD2 
940  C CE1 . TYR A 149 ? 0.4139 0.3033 0.2853 -0.0112 0.0064  -0.0268 128 TYR A CE1 
941  C CE2 . TYR A 149 ? 0.4239 0.3099 0.2763 -0.0191 -0.0023 -0.0288 128 TYR A CE2 
942  C CZ  . TYR A 149 ? 0.4677 0.3506 0.3250 -0.0151 0.0051  -0.0304 128 TYR A CZ  
943  O OH  . TYR A 149 ? 0.5482 0.4219 0.3965 -0.0149 0.0111  -0.0357 128 TYR A OH  
944  N N   . PRO A 150 ? 0.3147 0.2134 0.2107 -0.0111 -0.0070 -0.0212 129 PRO A N   
945  C CA  . PRO A 150 ? 0.3226 0.2184 0.2261 -0.0073 -0.0038 -0.0221 129 PRO A CA  
946  C C   . PRO A 150 ? 0.3448 0.2456 0.2583 -0.0055 -0.0067 -0.0188 129 PRO A C   
947  O O   . PRO A 150 ? 0.2965 0.1987 0.2178 -0.0019 -0.0050 -0.0182 129 PRO A O   
948  C CB  . PRO A 150 ? 0.3654 0.2510 0.2631 -0.0088 -0.0028 -0.0259 129 PRO A CB  
949  C CG  . PRO A 150 ? 0.3702 0.2528 0.2553 -0.0132 -0.0033 -0.0286 129 PRO A CG  
950  C CD  . PRO A 150 ? 0.3274 0.2195 0.2131 -0.0153 -0.0081 -0.0247 129 PRO A CD  
951  N N   . VAL A 151 ? 0.2515 0.1558 0.1650 -0.0079 -0.0110 -0.0167 130 VAL A N   
952  C CA  . VAL A 151 ? 0.2997 0.2084 0.2204 -0.0063 -0.0132 -0.0138 130 VAL A CA  
953  C C   . VAL A 151 ? 0.2491 0.1639 0.1744 -0.0044 -0.0128 -0.0121 130 VAL A C   
954  O O   . VAL A 151 ? 0.3031 0.2199 0.2347 -0.0021 -0.0130 -0.0112 130 VAL A O   
955  C CB  . VAL A 151 ? 0.2878 0.1988 0.2071 -0.0095 -0.0166 -0.0121 130 VAL A CB  
956  C CG1 . VAL A 151 ? 0.3079 0.2230 0.2326 -0.0078 -0.0181 -0.0094 130 VAL A CG1 
957  C CG2 . VAL A 151 ? 0.3777 0.2817 0.2930 -0.0124 -0.0169 -0.0137 130 VAL A CG2 
958  N N   . LEU A 152 ? 0.3191 0.2364 0.2410 -0.0055 -0.0125 -0.0115 131 LEU A N   
959  C CA  . LEU A 152 ? 0.2942 0.2151 0.2198 -0.0041 -0.0116 -0.0099 131 LEU A CA  
960  C C   . LEU A 152 ? 0.2952 0.2155 0.2251 -0.0024 -0.0078 -0.0111 131 LEU A C   
961  O O   . LEU A 152 ? 0.3516 0.2750 0.2882 -0.0015 -0.0076 -0.0102 131 LEU A O   
962  C CB  . LEU A 152 ? 0.3326 0.2547 0.2526 -0.0052 -0.0119 -0.0083 131 LEU A CB  
963  C CG  . LEU A 152 ? 0.3510 0.2748 0.2737 -0.0040 -0.0107 -0.0061 131 LEU A CG  
964  C CD1 . LEU A 152 ? 0.3616 0.2878 0.2898 -0.0029 -0.0129 -0.0050 131 LEU A CD1 
965  C CD2 . LEU A 152 ? 0.2955 0.2190 0.2113 -0.0046 -0.0111 -0.0038 131 LEU A CD2 
966  N N   . MET A 153 ? 0.3306 0.2471 0.2573 -0.0022 -0.0045 -0.0134 132 MET A N   
967  C CA  . MET A 153 ? 0.3849 0.3021 0.3178 0.0000  -0.0002 -0.0146 132 MET A CA  
968  C C   . MET A 153 ? 0.3137 0.2337 0.2567 0.0025  -0.0021 -0.0142 132 MET A C   
969  O O   . MET A 153 ? 0.3124 0.2375 0.2645 0.0037  -0.0010 -0.0136 132 MET A O   
970  C CB  . MET A 153 ? 0.3747 0.2862 0.3016 0.0004  0.0044  -0.0177 132 MET A CB  
971  C CG  . MET A 153 ? 0.4783 0.3874 0.3945 -0.0019 0.0073  -0.0183 132 MET A CG  
972  S SD  . MET A 153 ? 0.5676 0.4687 0.4755 -0.0011 0.0137  -0.0232 132 MET A SD  
973  C CE  . MET A 153 ? 0.4143 0.3200 0.3370 0.0035  0.0199  -0.0237 132 MET A CE  
974  N N   . ALA A 154 ? 0.3431 0.2597 0.2845 0.0029  -0.0052 -0.0142 133 ALA A N   
975  C CA  . ALA A 154 ? 0.3448 0.2634 0.2939 0.0054  -0.0079 -0.0129 133 ALA A CA  
976  C C   . ALA A 154 ? 0.3130 0.2375 0.2659 0.0045  -0.0113 -0.0109 133 ALA A C   
977  O O   . ALA A 154 ? 0.2984 0.2277 0.2596 0.0060  -0.0127 -0.0103 133 ALA A O   
978  C CB  . ALA A 154 ? 0.3264 0.2388 0.2709 0.0054  -0.0103 -0.0124 133 ALA A CB  
979  N N   . ALA A 155 ? 0.2842 0.2087 0.2315 0.0020  -0.0127 -0.0102 134 ALA A N   
980  C CA  . ALA A 155 ? 0.3279 0.2561 0.2775 0.0012  -0.0151 -0.0092 134 ALA A CA  
981  C C   . ALA A 155 ? 0.3610 0.2928 0.3168 0.0008  -0.0130 -0.0096 134 ALA A C   
982  O O   . ALA A 155 ? 0.3320 0.2672 0.2934 0.0005  -0.0153 -0.0095 134 ALA A O   
983  C CB  . ALA A 155 ? 0.3195 0.2468 0.2629 -0.0005 -0.0158 -0.0084 134 ALA A CB  
984  N N   . ASP A 156 ? 0.3414 0.2723 0.2957 0.0002  -0.0088 -0.0100 135 ASP A N   
985  C CA  . ASP A 156 ? 0.3678 0.3018 0.3280 -0.0010 -0.0059 -0.0099 135 ASP A CA  
986  C C   . ASP A 156 ? 0.3263 0.2660 0.2978 0.0003  -0.0061 -0.0106 135 ASP A C   
987  O O   . ASP A 156 ? 0.3275 0.2718 0.3065 -0.0014 -0.0069 -0.0105 135 ASP A O   
988  C CB  . ASP A 156 ? 0.3368 0.2685 0.2922 -0.0016 -0.0006 -0.0099 135 ASP A CB  
989  C CG  . ASP A 156 ? 0.4132 0.3402 0.3573 -0.0025 -0.0013 -0.0088 135 ASP A CG  
990  O OD1 . ASP A 156 ? 0.4444 0.3710 0.3865 -0.0028 -0.0048 -0.0076 135 ASP A OD1 
991  O OD2 . ASP A 156 ? 0.4112 0.3355 0.3484 -0.0028 0.0017  -0.0093 135 ASP A OD2 
992  N N   . ILE A 157 ? 0.3441 0.2837 0.3177 0.0033  -0.0053 -0.0113 136 ILE A N   
993  C CA  . ILE A 157 ? 0.3282 0.2742 0.3141 0.0057  -0.0054 -0.0114 136 ILE A CA  
994  C C   . ILE A 157 ? 0.2916 0.2412 0.2817 0.0060  -0.0123 -0.0102 136 ILE A C   
995  O O   . ILE A 157 ? 0.3137 0.2711 0.3143 0.0053  -0.0144 -0.0100 136 ILE A O   
996  C CB  . ILE A 157 ? 0.3234 0.2661 0.3094 0.0098  -0.0022 -0.0124 136 ILE A CB  
997  C CG1 . ILE A 157 ? 0.3571 0.2966 0.3380 0.0091  0.0052  -0.0142 136 ILE A CG1 
998  C CG2 . ILE A 157 ? 0.3075 0.2573 0.3075 0.0137  -0.0032 -0.0118 136 ILE A CG2 
999  C CD1 . ILE A 157 ? 0.4197 0.3520 0.3954 0.0122  0.0087  -0.0163 136 ILE A CD1 
1000 N N   . LEU A 158 ? 0.3027 0.2470 0.2844 0.0064  -0.0161 -0.0095 137 LEU A N   
1001 C CA  . LEU A 158 ? 0.3591 0.3056 0.3424 0.0072  -0.0223 -0.0081 137 LEU A CA  
1002 C C   . LEU A 158 ? 0.3131 0.2622 0.2955 0.0037  -0.0258 -0.0085 137 LEU A C   
1003 O O   . LEU A 158 ? 0.3472 0.3001 0.3327 0.0037  -0.0312 -0.0079 137 LEU A O   
1004 C CB  . LEU A 158 ? 0.3276 0.2668 0.3013 0.0084  -0.0241 -0.0069 137 LEU A CB  
1005 C CG  . LEU A 158 ? 0.3427 0.2768 0.3161 0.0117  -0.0213 -0.0067 137 LEU A CG  
1006 C CD1 . LEU A 158 ? 0.3484 0.2748 0.3123 0.0114  -0.0232 -0.0053 137 LEU A CD1 
1007 C CD2 . LEU A 158 ? 0.3611 0.2999 0.3459 0.0161  -0.0221 -0.0057 137 LEU A CD2 
1008 N N   . LEU A 159 ? 0.2894 0.2356 0.2670 0.0007  -0.0232 -0.0096 138 LEU A N   
1009 C CA  . LEU A 159 ? 0.3508 0.2971 0.3267 -0.0025 -0.0257 -0.0106 138 LEU A CA  
1010 C C   . LEU A 159 ? 0.3064 0.2602 0.2933 -0.0045 -0.0282 -0.0114 138 LEU A C   
1011 O O   . LEU A 159 ? 0.3414 0.2959 0.3270 -0.0070 -0.0327 -0.0125 138 LEU A O   
1012 C CB  . LEU A 159 ? 0.3546 0.2963 0.3257 -0.0046 -0.0216 -0.0111 138 LEU A CB  
1013 C CG  . LEU A 159 ? 0.3031 0.2388 0.2639 -0.0036 -0.0207 -0.0105 138 LEU A CG  
1014 C CD1 . LEU A 159 ? 0.3447 0.2771 0.3031 -0.0048 -0.0169 -0.0101 138 LEU A CD1 
1015 C CD2 . LEU A 159 ? 0.3655 0.2992 0.3207 -0.0039 -0.0241 -0.0111 138 LEU A CD2 
1016 N N   . TYR A 160 ? 0.3014 0.2612 0.2990 -0.0039 -0.0251 -0.0111 139 TYR A N   
1017 C CA  . TYR A 160 ? 0.3642 0.3327 0.3744 -0.0068 -0.0264 -0.0118 139 TYR A CA  
1018 C C   . TYR A 160 ? 0.3533 0.3316 0.3752 -0.0037 -0.0306 -0.0107 139 TYR A C   
1019 O O   . TYR A 160 ? 0.3699 0.3583 0.4061 -0.0052 -0.0306 -0.0108 139 TYR A O   
1020 C CB  . TYR A 160 ? 0.3531 0.3228 0.3688 -0.0088 -0.0191 -0.0120 139 TYR A CB  
1021 C CG  . TYR A 160 ? 0.3226 0.2825 0.3269 -0.0113 -0.0159 -0.0123 139 TYR A CG  
1022 C CD1 . TYR A 160 ? 0.3480 0.3045 0.3500 -0.0158 -0.0179 -0.0135 139 TYR A CD1 
1023 C CD2 . TYR A 160 ? 0.2922 0.2457 0.2875 -0.0090 -0.0114 -0.0113 139 TYR A CD2 
1024 C CE1 . TYR A 160 ? 0.2929 0.2399 0.2851 -0.0170 -0.0149 -0.0133 139 TYR A CE1 
1025 C CE2 . TYR A 160 ? 0.3603 0.3059 0.3460 -0.0105 -0.0093 -0.0108 139 TYR A CE2 
1026 C CZ  . TYR A 160 ? 0.3094 0.2517 0.2941 -0.0140 -0.0109 -0.0115 139 TYR A CZ  
1027 O OH  . TYR A 160 ? 0.3872 0.3210 0.3631 -0.0145 -0.0087 -0.0105 139 TYR A OH  
1028 N N   . GLN A 161 ? 0.3451 0.3208 0.3617 0.0004  -0.0343 -0.0091 140 GLN A N   
1029 C CA  . GLN A 161 ? 0.3593 0.3430 0.3861 0.0044  -0.0390 -0.0070 140 GLN A CA  
1030 C C   . GLN A 161 ? 0.3508 0.3420 0.3923 0.0075  -0.0335 -0.0066 140 GLN A C   
1031 O O   . GLN A 161 ? 0.3327 0.3359 0.3898 0.0088  -0.0362 -0.0057 140 GLN A O   
1032 C CB  . GLN A 161 ? 0.4148 0.4065 0.4465 0.0010  -0.0473 -0.0072 140 GLN A CB  
1033 C CG  . GLN A 161 ? 0.3489 0.3325 0.3644 -0.0015 -0.0523 -0.0080 140 GLN A CG  
1034 C CD  . GLN A 161 ? 0.4669 0.4448 0.4730 0.0032  -0.0550 -0.0050 140 GLN A CD  
1035 O OE1 . GLN A 161 ? 0.4248 0.4081 0.4379 0.0075  -0.0591 -0.0019 140 GLN A OE1 
1036 N NE2 . GLN A 161 ? 0.4409 0.4080 0.4319 0.0027  -0.0526 -0.0054 140 GLN A NE2 
1037 N N   . THR A 162 ? 0.3393 0.3236 0.3757 0.0088  -0.0256 -0.0075 141 THR A N   
1038 C CA  . THR A 162 ? 0.3010 0.2908 0.3486 0.0108  -0.0182 -0.0081 141 THR A CA  
1039 C C   . THR A 162 ? 0.3296 0.3243 0.3879 0.0180  -0.0187 -0.0064 141 THR A C   
1040 O O   . THR A 162 ? 0.3235 0.3106 0.3745 0.0222  -0.0211 -0.0051 141 THR A O   
1041 C CB  . THR A 162 ? 0.3009 0.2804 0.3367 0.0103  -0.0103 -0.0096 141 THR A CB  
1042 O OG1 . THR A 162 ? 0.3369 0.3123 0.3642 0.0046  -0.0100 -0.0104 141 THR A OG1 
1043 C CG2 . THR A 162 ? 0.3656 0.3496 0.4106 0.0124  -0.0017 -0.0105 141 THR A CG2 
1044 N N   . ASN A 163 ? 0.3409 0.3483 0.4175 0.0195  -0.0158 -0.0063 142 ASN A N   
1045 C CA  . ASN A 163 ? 0.3744 0.3881 0.4644 0.0273  -0.0152 -0.0046 142 ASN A CA  
1046 C C   . ASN A 163 ? 0.3931 0.4010 0.4823 0.0317  -0.0043 -0.0065 142 ASN A C   
1047 O O   . ASN A 163 ? 0.3647 0.3680 0.4550 0.0389  -0.0031 -0.0057 142 ASN A O   
1048 C CB  . ASN A 163 ? 0.3626 0.3956 0.4755 0.0270  -0.0183 -0.0032 142 ASN A CB  
1049 C CG  . ASN A 163 ? 0.4114 0.4504 0.5252 0.0238  -0.0305 -0.0014 142 ASN A CG  
1050 O OD1 . ASN A 163 ? 0.3838 0.4290 0.5006 0.0164  -0.0333 -0.0027 142 ASN A OD1 
1051 N ND2 . ASN A 163 ? 0.4777 0.5135 0.5876 0.0290  -0.0376 0.0015  142 ASN A ND2 
1052 N N   . GLN A 164 ? 0.3382 0.3452 0.4246 0.0275  0.0039  -0.0089 143 GLN A N   
1053 C CA  . GLN A 164 ? 0.3627 0.3654 0.4481 0.0311  0.0149  -0.0112 143 GLN A CA  
1054 C C   . GLN A 164 ? 0.3331 0.3256 0.4013 0.0254  0.0206  -0.0134 143 GLN A C   
1055 O O   . GLN A 164 ? 0.3338 0.3289 0.4001 0.0188  0.0195  -0.0129 143 GLN A O   
1056 C CB  . GLN A 164 ? 0.4269 0.4457 0.5348 0.0336  0.0209  -0.0110 143 GLN A CB  
1057 C CG  . GLN A 164 ? 0.4527 0.4845 0.5802 0.0393  0.0140  -0.0081 143 GLN A CG  
1058 C CD  . GLN A 164 ? 0.6185 0.6687 0.7711 0.0421  0.0198  -0.0076 143 GLN A CD  
1059 O OE1 . GLN A 164 ? 0.6665 0.7181 0.8212 0.0410  0.0310  -0.0098 143 GLN A OE1 
1060 N NE2 . GLN A 164 ? 0.7392 0.8044 0.9113 0.0458  0.0121  -0.0045 143 GLN A NE2 
1061 N N   . VAL A 165 ? 0.3108 0.2911 0.3660 0.0281  0.0264  -0.0157 144 VAL A N   
1062 C CA  . VAL A 165 ? 0.4040 0.3743 0.4414 0.0234  0.0313  -0.0176 144 VAL A CA  
1063 C C   . VAL A 165 ? 0.4447 0.4127 0.4811 0.0263  0.0428  -0.0205 144 VAL A C   
1064 O O   . VAL A 165 ? 0.4438 0.4034 0.4755 0.0314  0.0456  -0.0228 144 VAL A O   
1065 C CB  . VAL A 165 ? 0.4551 0.4117 0.4739 0.0222  0.0261  -0.0181 144 VAL A CB  
1066 C CG1 . VAL A 165 ? 0.4895 0.4382 0.4914 0.0172  0.0294  -0.0192 144 VAL A CG1 
1067 C CG2 . VAL A 165 ? 0.4868 0.4458 0.5072 0.0205  0.0158  -0.0154 144 VAL A CG2 
1068 N N   . PRO A 166 ? 0.4861 0.4598 0.5255 0.0230  0.0503  -0.0206 145 PRO A N   
1069 C CA  . PRO A 166 ? 0.5310 0.5021 0.5677 0.0257  0.0625  -0.0237 145 PRO A CA  
1070 C C   . PRO A 166 ? 0.5735 0.5285 0.5847 0.0233  0.0657  -0.0263 145 PRO A C   
1071 O O   . PRO A 166 ? 0.7017 0.6542 0.7019 0.0183  0.0700  -0.0259 145 PRO A O   
1072 C CB  . PRO A 166 ? 0.5431 0.5269 0.5921 0.0218  0.0688  -0.0219 145 PRO A CB  
1073 C CG  . PRO A 166 ? 0.5346 0.5281 0.5955 0.0177  0.0593  -0.0185 145 PRO A CG  
1074 C CD  . PRO A 166 ? 0.4922 0.4756 0.5396 0.0169  0.0488  -0.0180 145 PRO A CD  
1075 N N   . VAL A 167 ? 0.5810 0.5246 0.5822 0.0267  0.0634  -0.0289 146 VAL A N   
1076 C CA  . VAL A 167 ? 0.7004 0.6292 0.6778 0.0241  0.0650  -0.0320 146 VAL A CA  
1077 C C   . VAL A 167 ? 0.6155 0.5385 0.5874 0.0275  0.0770  -0.0367 146 VAL A C   
1078 O O   . VAL A 167 ? 0.6363 0.5648 0.6232 0.0336  0.0831  -0.0380 146 VAL A O   
1079 C CB  . VAL A 167 ? 0.6871 0.6055 0.6553 0.0244  0.0564  -0.0327 146 VAL A CB  
1080 C CG1 . VAL A 167 ? 0.6681 0.5907 0.6374 0.0203  0.0460  -0.0285 146 VAL A CG1 
1081 C CG2 . VAL A 167 ? 0.5737 0.4907 0.5531 0.0316  0.0565  -0.0338 146 VAL A CG2 
1082 N N   . GLY A 168 ? 0.8134 0.7253 0.7631 0.0237  0.0802  -0.0394 147 GLY A N   
1083 C CA  . GLY A 168 ? 0.8937 0.7959 0.8322 0.0264  0.0906  -0.0451 147 GLY A CA  
1084 C C   . GLY A 168 ? 0.8662 0.7549 0.7974 0.0296  0.0878  -0.0495 147 GLY A C   
1085 O O   . GLY A 168 ? 0.8029 0.6899 0.7369 0.0294  0.0779  -0.0475 147 GLY A O   
1086 N N   . GLU A 169 ? 0.8399 0.7178 0.7606 0.0325  0.0975  -0.0556 148 GLU A N   
1087 C CA  . GLU A 169 ? 0.7975 0.6600 0.7104 0.0354  0.0962  -0.0605 148 GLU A CA  
1088 C C   . GLU A 169 ? 0.7736 0.6258 0.6676 0.0283  0.0862  -0.0610 148 GLU A C   
1089 O O   . GLU A 169 ? 0.7714 0.6151 0.6649 0.0291  0.0804  -0.0620 148 GLU A O   
1090 C CB  . GLU A 169 ? 0.8809 0.7319 0.7830 0.0391  0.1094  -0.0680 148 GLU A CB  
1091 C CG  . GLU A 169 ? 0.9800 0.8207 0.8891 0.0471  0.1124  -0.0719 148 GLU A CG  
1092 C CD  . GLU A 169 ? 1.0365 0.8911 0.9740 0.0564  0.1174  -0.0687 148 GLU A CD  
1093 O OE1 . GLU A 169 ? 1.1336 0.9833 1.0820 0.0635  0.1161  -0.0689 148 GLU A OE1 
1094 O OE2 . GLU A 169 ? 1.0620 0.9327 1.0114 0.0564  0.1225  -0.0658 148 GLU A OE2 
1095 N N   . ASP A 170 ? 0.6958 0.5492 0.5750 0.0213  0.0840  -0.0598 149 ASP A N   
1096 C CA  . ASP A 170 ? 0.7665 0.6121 0.6284 0.0144  0.0747  -0.0603 149 ASP A CA  
1097 C C   . ASP A 170 ? 0.6629 0.5175 0.5352 0.0121  0.0630  -0.0539 149 ASP A C   
1098 O O   . ASP A 170 ? 0.6754 0.5259 0.5367 0.0067  0.0549  -0.0536 149 ASP A O   
1099 C CB  . ASP A 170 ? 0.7811 0.6241 0.6219 0.0086  0.0767  -0.0613 149 ASP A CB  
1100 C CG  . ASP A 170 ? 0.8813 0.7375 0.7291 0.0078  0.0790  -0.0554 149 ASP A CG  
1101 O OD1 . ASP A 170 ? 0.8883 0.7563 0.7578 0.0113  0.0793  -0.0513 149 ASP A OD1 
1102 O OD2 . ASP A 170 ? 1.1016 0.9560 0.9325 0.0033  0.0804  -0.0548 149 ASP A OD2 
1103 N N   . GLN A 171 ? 0.5846 0.4518 0.4776 0.0157  0.0618  -0.0491 150 GLN A N   
1104 C CA  . GLN A 171 ? 0.6954 0.5695 0.5983 0.0144  0.0516  -0.0439 150 GLN A CA  
1105 C C   . GLN A 171 ? 0.5738 0.4490 0.4929 0.0202  0.0499  -0.0429 150 GLN A C   
1106 O O   . GLN A 171 ? 0.4421 0.3251 0.3721 0.0203  0.0427  -0.0383 150 GLN A O   
1107 C CB  . GLN A 171 ? 0.6039 0.4911 0.5147 0.0124  0.0497  -0.0385 150 GLN A CB  
1108 C CG  . GLN A 171 ? 0.6671 0.5531 0.5630 0.0062  0.0453  -0.0367 150 GLN A CG  
1109 C CD  . GLN A 171 ? 0.7192 0.6153 0.6217 0.0045  0.0449  -0.0317 150 GLN A CD  
1110 O OE1 . GLN A 171 ? 0.8153 0.7194 0.7323 0.0069  0.0492  -0.0302 150 GLN A OE1 
1111 N NE2 . GLN A 171 ? 0.7129 0.6086 0.6053 0.0002  0.0398  -0.0289 150 GLN A NE2 
1112 N N   . LYS A 172 ? 0.5931 0.4600 0.5131 0.0254  0.0564  -0.0472 151 LYS A N   
1113 C CA  . LYS A 172 ? 0.5355 0.4017 0.4697 0.0317  0.0547  -0.0458 151 LYS A CA  
1114 C C   . LYS A 172 ? 0.5495 0.4091 0.4791 0.0288  0.0453  -0.0438 151 LYS A C   
1115 O O   . LYS A 172 ? 0.4685 0.3340 0.4103 0.0312  0.0394  -0.0392 151 LYS A O   
1116 C CB  . LYS A 172 ? 0.5709 0.4263 0.5042 0.0380  0.0643  -0.0511 151 LYS A CB  
1117 C CG  . LYS A 172 ? 0.6162 0.4659 0.5603 0.0450  0.0626  -0.0500 151 LYS A CG  
1118 C CD  . LYS A 172 ? 0.7392 0.5783 0.6834 0.0522  0.0735  -0.0556 151 LYS A CD  
1119 C CE  . LYS A 172 ? 0.9328 0.7563 0.8769 0.0569  0.0718  -0.0563 151 LYS A CE  
1120 N NZ  . LYS A 172 ? 0.8703 0.6801 0.8116 0.0638  0.0832  -0.0627 151 LYS A NZ  
1121 N N   . GLN A 173 ? 0.5418 0.3896 0.4535 0.0231  0.0436  -0.0473 152 GLN A N   
1122 C CA  . GLN A 173 ? 0.5283 0.3705 0.4358 0.0193  0.0354  -0.0455 152 GLN A CA  
1123 C C   . GLN A 173 ? 0.5044 0.3599 0.4188 0.0164  0.0275  -0.0395 152 GLN A C   
1124 O O   . GLN A 173 ? 0.3931 0.2494 0.3134 0.0168  0.0218  -0.0358 152 GLN A O   
1125 C CB  . GLN A 173 ? 0.5715 0.4015 0.4596 0.0123  0.0346  -0.0504 152 GLN A CB  
1126 C CG  . GLN A 173 ? 0.7681 0.5804 0.6468 0.0142  0.0411  -0.0572 152 GLN A CG  
1127 C CD  . GLN A 173 ? 0.8238 0.6240 0.6835 0.0058  0.0383  -0.0620 152 GLN A CD  
1128 O OE1 . GLN A 173 ? 0.8184 0.6246 0.6692 -0.0007 0.0343  -0.0617 152 GLN A OE1 
1129 N NE2 . GLN A 173 ? 0.8888 0.6718 0.7427 0.0057  0.0399  -0.0661 152 GLN A NE2 
1130 N N   . HIS A 174 ? 0.4402 0.3052 0.3528 0.0133  0.0275  -0.0383 153 HIS A N   
1131 C CA  . HIS A 174 ? 0.3900 0.2659 0.3078 0.0107  0.0208  -0.0333 153 HIS A CA  
1132 C C   . HIS A 174 ? 0.3962 0.2810 0.3309 0.0154  0.0189  -0.0293 153 HIS A C   
1133 O O   . HIS A 174 ? 0.3163 0.2045 0.2546 0.0144  0.0124  -0.0258 153 HIS A O   
1134 C CB  . HIS A 174 ? 0.4326 0.3150 0.3455 0.0074  0.0221  -0.0327 153 HIS A CB  
1135 C CG  . HIS A 174 ? 0.4743 0.3495 0.3698 0.0025  0.0224  -0.0358 153 HIS A CG  
1136 N ND1 . HIS A 174 ? 0.5213 0.3878 0.4063 0.0028  0.0290  -0.0409 153 HIS A ND1 
1137 C CD2 . HIS A 174 ? 0.5300 0.4060 0.4167 -0.0027 0.0165  -0.0345 153 HIS A CD2 
1138 C CE1 . HIS A 174 ? 0.5265 0.3883 0.3958 -0.0027 0.0264  -0.0427 153 HIS A CE1 
1139 N NE2 . HIS A 174 ? 0.4859 0.3542 0.3569 -0.0059 0.0186  -0.0387 153 HIS A NE2 
1140 N N   . LEU A 175 ? 0.3929 0.2820 0.3379 0.0204  0.0245  -0.0299 154 LEU A N   
1141 C CA  . LEU A 175 ? 0.3038 0.2025 0.2655 0.0248  0.0218  -0.0261 154 LEU A CA  
1142 C C   . LEU A 175 ? 0.3537 0.2457 0.3176 0.0281  0.0177  -0.0246 154 LEU A C   
1143 O O   . LEU A 175 ? 0.3419 0.2397 0.3129 0.0288  0.0114  -0.0204 154 LEU A O   
1144 C CB  . LEU A 175 ? 0.3495 0.2554 0.3236 0.0296  0.0290  -0.0271 154 LEU A CB  
1145 C CG  . LEU A 175 ? 0.4289 0.3461 0.4224 0.0346  0.0259  -0.0234 154 LEU A CG  
1146 C CD1 . LEU A 175 ? 0.4211 0.3480 0.4182 0.0302  0.0182  -0.0197 154 LEU A CD1 
1147 C CD2 . LEU A 175 ? 0.4592 0.3854 0.4669 0.0392  0.0337  -0.0245 154 LEU A CD2 
1148 N N   . GLU A 176 ? 0.3803 0.2588 0.3369 0.0299  0.0213  -0.0278 155 GLU A N   
1149 C CA  . GLU A 176 ? 0.4332 0.3030 0.3913 0.0333  0.0182  -0.0259 155 GLU A CA  
1150 C C   . GLU A 176 ? 0.4385 0.3059 0.3890 0.0277  0.0107  -0.0230 155 GLU A C   
1151 O O   . GLU A 176 ? 0.4067 0.2735 0.3615 0.0298  0.0060  -0.0188 155 GLU A O   
1152 C CB  . GLU A 176 ? 0.4642 0.3178 0.4149 0.0358  0.0245  -0.0307 155 GLU A CB  
1153 C CG  . GLU A 176 ? 0.7095 0.5529 0.6647 0.0418  0.0233  -0.0284 155 GLU A CG  
1154 C CD  . GLU A 176 ? 0.7161 0.5718 0.6876 0.0474  0.0183  -0.0220 155 GLU A CD  
1155 O OE1 . GLU A 176 ? 0.5327 0.3871 0.5027 0.0459  0.0113  -0.0173 155 GLU A OE1 
1156 O OE2 . GLU A 176 ? 0.6061 0.4732 0.5914 0.0528  0.0213  -0.0216 155 GLU A OE2 
1157 N N   . LEU A 177 ? 0.3818 0.2485 0.3213 0.0207  0.0098  -0.0250 156 LEU A N   
1158 C CA  . LEU A 177 ? 0.4180 0.2852 0.3523 0.0154  0.0035  -0.0222 156 LEU A CA  
1159 C C   . LEU A 177 ? 0.4426 0.3226 0.3855 0.0161  -0.0013 -0.0176 156 LEU A C   
1160 O O   . LEU A 177 ? 0.3800 0.2599 0.3229 0.0153  -0.0060 -0.0141 156 LEU A O   
1161 C CB  . LEU A 177 ? 0.4703 0.3364 0.3932 0.0085  0.0033  -0.0249 156 LEU A CB  
1162 C CG  . LEU A 177 ? 0.5227 0.3924 0.4424 0.0032  -0.0025 -0.0221 156 LEU A CG  
1163 C CD1 . LEU A 177 ? 0.4584 0.3187 0.3757 0.0020  -0.0046 -0.0206 156 LEU A CD1 
1164 C CD2 . LEU A 177 ? 0.4508 0.3222 0.3616 -0.0026 -0.0032 -0.0243 156 LEU A CD2 
1165 N N   . SER A 178 ? 0.3443 0.2346 0.2935 0.0170  0.0003  -0.0178 157 SER A N   
1166 C CA  A SER A 178 ? 0.3271 0.2284 0.2840 0.0171  -0.0042 -0.0143 157 SER A CA  
1167 C CA  B SER A 178 ? 0.3241 0.2255 0.2810 0.0171  -0.0042 -0.0143 157 SER A CA  
1168 C C   . SER A 178 ? 0.3445 0.2474 0.3103 0.0221  -0.0074 -0.0111 157 SER A C   
1169 O O   . SER A 178 ? 0.3684 0.2749 0.3347 0.0212  -0.0129 -0.0078 157 SER A O   
1170 C CB  A SER A 178 ? 0.3696 0.2803 0.3325 0.0168  -0.0013 -0.0153 157 SER A CB  
1171 C CB  B SER A 178 ? 0.4186 0.3294 0.3816 0.0169  -0.0012 -0.0153 157 SER A CB  
1172 O OG  A SER A 178 ? 0.3504 0.2647 0.3242 0.0218  0.0026  -0.0159 157 SER A OG  
1173 O OG  B SER A 178 ? 0.3675 0.2766 0.3212 0.0126  0.0011  -0.0173 157 SER A OG  
1174 N N   . ARG A 179 ? 0.3129 0.2129 0.2852 0.0277  -0.0040 -0.0118 158 ARG A N   
1175 C CA  . ARG A 179 ? 0.3782 0.2795 0.3593 0.0333  -0.0076 -0.0079 158 ARG A CA  
1176 C C   . ARG A 179 ? 0.3303 0.2208 0.3025 0.0325  -0.0114 -0.0051 158 ARG A C   
1177 O O   . ARG A 179 ? 0.3486 0.2419 0.3229 0.0339  -0.0172 -0.0006 158 ARG A O   
1178 C CB  . ARG A 179 ? 0.3827 0.2828 0.3735 0.0404  -0.0023 -0.0093 158 ARG A CB  
1179 C CG  . ARG A 179 ? 0.4131 0.3263 0.4156 0.0416  0.0018  -0.0111 158 ARG A CG  
1180 C CD  . ARG A 179 ? 0.4538 0.3669 0.4674 0.0493  0.0082  -0.0124 158 ARG A CD  
1181 N NE  . ARG A 179 ? 0.4935 0.4116 0.5204 0.0563  0.0036  -0.0078 158 ARG A NE  
1182 C CZ  . ARG A 179 ? 0.5160 0.4229 0.5422 0.0623  0.0034  -0.0061 158 ARG A CZ  
1183 N NH1 . ARG A 179 ? 0.5028 0.3919 0.5158 0.0618  0.0080  -0.0093 158 ARG A NH1 
1184 N NH2 . ARG A 179 ? 0.5041 0.4172 0.5429 0.0689  -0.0019 -0.0008 158 ARG A NH2 
1185 N N   . ASP A 180 ? 0.3644 0.2421 0.3258 0.0297  -0.0083 -0.0077 159 ASP A N   
1186 C CA  . ASP A 180 ? 0.4351 0.3018 0.3882 0.0278  -0.0111 -0.0049 159 ASP A CA  
1187 C C   . ASP A 180 ? 0.4580 0.3307 0.4063 0.0225  -0.0161 -0.0021 159 ASP A C   
1188 O O   . ASP A 180 ? 0.3570 0.2262 0.3025 0.0228  -0.0198 0.0024  159 ASP A O   
1189 C CB  . ASP A 180 ? 0.4274 0.2803 0.3703 0.0241  -0.0067 -0.0091 159 ASP A CB  
1190 C CG  . ASP A 180 ? 0.4838 0.3250 0.4286 0.0300  -0.0018 -0.0113 159 ASP A CG  
1191 O OD1 . ASP A 180 ? 0.4085 0.2529 0.3640 0.0377  -0.0017 -0.0088 159 ASP A OD1 
1192 O OD2 . ASP A 180 ? 0.4853 0.3139 0.4210 0.0269  0.0021  -0.0157 159 ASP A OD2 
1193 N N   . VAL A 181 ? 0.3934 0.2742 0.3400 0.0180  -0.0158 -0.0045 160 VAL A N   
1194 C CA  . VAL A 181 ? 0.3993 0.2852 0.3415 0.0136  -0.0195 -0.0024 160 VAL A CA  
1195 C C   . VAL A 181 ? 0.3851 0.2794 0.3329 0.0163  -0.0240 0.0009  160 VAL A C   
1196 O O   . VAL A 181 ? 0.3747 0.2688 0.3176 0.0147  -0.0274 0.0041  160 VAL A O   
1197 C CB  . VAL A 181 ? 0.4036 0.2952 0.3432 0.0090  -0.0179 -0.0055 160 VAL A CB  
1198 C CG1 . VAL A 181 ? 0.4019 0.3001 0.3393 0.0061  -0.0210 -0.0035 160 VAL A CG1 
1199 C CG2 . VAL A 181 ? 0.3851 0.2689 0.3173 0.0051  -0.0152 -0.0083 160 VAL A CG2 
1200 N N   . ALA A 182 ? 0.3554 0.2573 0.3131 0.0199  -0.0240 0.0002  161 ALA A N   
1201 C CA  . ALA A 182 ? 0.3865 0.2969 0.3500 0.0219  -0.0292 0.0030  161 ALA A CA  
1202 C C   . ALA A 182 ? 0.3160 0.2210 0.2785 0.0258  -0.0331 0.0077  161 ALA A C   
1203 O O   . ALA A 182 ? 0.2981 0.2053 0.2567 0.0250  -0.0383 0.0109  161 ALA A O   
1204 C CB  . ALA A 182 ? 0.3319 0.2523 0.3082 0.0246  -0.0282 0.0013  161 ALA A CB  
1205 N N   . GLN A 183 ? 0.3031 0.2000 0.2681 0.0302  -0.0305 0.0083  162 GLN A N   
1206 C CA  . GLN A 183 ? 0.3502 0.2399 0.3139 0.0346  -0.0339 0.0136  162 GLN A CA  
1207 C C   . GLN A 183 ? 0.3439 0.2246 0.2938 0.0300  -0.0352 0.0164  162 GLN A C   
1208 O O   . GLN A 183 ? 0.3591 0.2386 0.3049 0.0312  -0.0402 0.0216  162 GLN A O   
1209 C CB  . GLN A 183 ? 0.3582 0.2383 0.3264 0.0403  -0.0294 0.0130  162 GLN A CB  
1210 C CG  . GLN A 183 ? 0.4293 0.3189 0.4127 0.0460  -0.0273 0.0110  162 GLN A CG  
1211 C CD  . GLN A 183 ? 0.4427 0.3218 0.4286 0.0506  -0.0203 0.0082  162 GLN A CD  
1212 O OE1 . GLN A 183 ? 0.3632 0.2277 0.3383 0.0478  -0.0166 0.0061  162 GLN A OE1 
1213 N NE2 . GLN A 183 ? 0.4587 0.3452 0.4591 0.0575  -0.0181 0.0077  162 GLN A NE2 
1214 N N   . ARG A 184 ? 0.3546 0.2293 0.2972 0.0245  -0.0309 0.0132  163 ARG A N   
1215 C CA  . ARG A 184 ? 0.3378 0.2052 0.2691 0.0194  -0.0311 0.0156  163 ARG A CA  
1216 C C   . ARG A 184 ? 0.3686 0.2448 0.2957 0.0166  -0.0347 0.0173  163 ARG A C   
1217 O O   . ARG A 184 ? 0.3299 0.2018 0.2492 0.0155  -0.0370 0.0219  163 ARG A O   
1218 C CB  . ARG A 184 ? 0.3138 0.1765 0.2407 0.0137  -0.0263 0.0113  163 ARG A CB  
1219 C CG  . ARG A 184 ? 0.4125 0.2703 0.3302 0.0074  -0.0258 0.0133  163 ARG A CG  
1220 C CD  . ARG A 184 ? 0.3405 0.1959 0.2559 0.0016  -0.0222 0.0088  163 ARG A CD  
1221 N NE  . ARG A 184 ? 0.3176 0.1604 0.2323 0.0024  -0.0194 0.0065  163 ARG A NE  
1222 C CZ  . ARG A 184 ? 0.3689 0.2110 0.2848 0.0017  -0.0166 0.0010  163 ARG A CZ  
1223 N NH1 . ARG A 184 ? 0.3398 0.1932 0.2579 0.0001  -0.0165 -0.0022 163 ARG A NH1 
1224 N NH2 . ARG A 184 ? 0.3515 0.1800 0.2650 0.0025  -0.0137 -0.0013 163 ARG A NH2 
1225 N N   . PHE A 185 ? 0.3293 0.2165 0.2605 0.0151  -0.0348 0.0137  164 PHE A N   
1226 C CA  . PHE A 185 ? 0.3307 0.2249 0.2576 0.0126  -0.0377 0.0143  164 PHE A CA  
1227 C C   . PHE A 185 ? 0.3335 0.2300 0.2602 0.0161  -0.0437 0.0183  164 PHE A C   
1228 O O   . PHE A 185 ? 0.3743 0.2693 0.2915 0.0144  -0.0461 0.0213  164 PHE A O   
1229 C CB  . PHE A 185 ? 0.3263 0.2299 0.2583 0.0108  -0.0365 0.0096  164 PHE A CB  
1230 C CG  . PHE A 185 ? 0.3289 0.2373 0.2553 0.0077  -0.0377 0.0090  164 PHE A CG  
1231 C CD1 . PHE A 185 ? 0.3341 0.2478 0.2608 0.0087  -0.0423 0.0095  164 PHE A CD1 
1232 C CD2 . PHE A 185 ? 0.3336 0.2415 0.2548 0.0039  -0.0343 0.0077  164 PHE A CD2 
1233 C CE1 . PHE A 185 ? 0.3826 0.2989 0.3027 0.0058  -0.0429 0.0080  164 PHE A CE1 
1234 C CE2 . PHE A 185 ? 0.3205 0.2320 0.2368 0.0019  -0.0344 0.0068  164 PHE A CE2 
1235 C CZ  . PHE A 185 ? 0.3182 0.2329 0.2332 0.0029  -0.0384 0.0067  164 PHE A CZ  
1236 N N   . ASN A 186 ? 0.3450 0.2457 0.2821 0.0210  -0.0461 0.0187  165 ASN A N   
1237 C CA  . ASN A 186 ? 0.3321 0.2371 0.2707 0.0246  -0.0531 0.0228  165 ASN A CA  
1238 C C   . ASN A 186 ? 0.4046 0.2990 0.3344 0.0268  -0.0553 0.0292  165 ASN A C   
1239 O O   . ASN A 186 ? 0.3815 0.2773 0.3049 0.0274  -0.0613 0.0333  165 ASN A O   
1240 C CB  . ASN A 186 ? 0.2879 0.2008 0.2421 0.0298  -0.0548 0.0221  165 ASN A CB  
1241 C CG  . ASN A 186 ? 0.3400 0.2647 0.3022 0.0270  -0.0543 0.0172  165 ASN A CG  
1242 O OD1 . ASN A 186 ? 0.3076 0.2332 0.2632 0.0218  -0.0528 0.0141  165 ASN A OD1 
1243 N ND2 . ASN A 186 ? 0.3712 0.3047 0.3482 0.0307  -0.0552 0.0165  165 ASN A ND2 
1244 N N   . ALA A 187 ? 0.3136 0.1965 0.2421 0.0278  -0.0508 0.0302  166 ALA A N   
1245 C CA  . ALA A 187 ? 0.3388 0.2095 0.2585 0.0295  -0.0522 0.0368  166 ALA A CA  
1246 C C   . ALA A 187 ? 0.4028 0.2697 0.3074 0.0235  -0.0518 0.0390  166 ALA A C   
1247 O O   . ALA A 187 ? 0.4185 0.2776 0.3137 0.0245  -0.0544 0.0455  166 ALA A O   
1248 C CB  . ALA A 187 ? 0.3364 0.1939 0.2576 0.0308  -0.0467 0.0364  166 ALA A CB  
1249 N N   . ILE A 188 ? 0.3572 0.2296 0.2594 0.0177  -0.0483 0.0341  167 ILE A N   
1250 C CA  . ILE A 188 ? 0.4558 0.3264 0.3452 0.0124  -0.0468 0.0356  167 ILE A CA  
1251 C C   . ILE A 188 ? 0.4692 0.3481 0.3532 0.0122  -0.0516 0.0356  167 ILE A C   
1252 O O   . ILE A 188 ? 0.4913 0.3664 0.3627 0.0110  -0.0534 0.0399  167 ILE A O   
1253 C CB  . ILE A 188 ? 0.4369 0.3096 0.3275 0.0069  -0.0404 0.0305  167 ILE A CB  
1254 C CG1 . ILE A 188 ? 0.4450 0.3086 0.3388 0.0058  -0.0362 0.0301  167 ILE A CG1 
1255 C CG2 . ILE A 188 ? 0.4513 0.3245 0.3310 0.0019  -0.0379 0.0317  167 ILE A CG2 
1256 C CD1 . ILE A 188 ? 0.4328 0.3008 0.3304 0.0011  -0.0316 0.0245  167 ILE A CD1 
1257 N N   . TYR A 189 ? 0.3685 0.2579 0.2611 0.0129  -0.0536 0.0306  168 TYR A N   
1258 C CA  . TYR A 189 ? 0.3717 0.2683 0.2589 0.0109  -0.0569 0.0285  168 TYR A CA  
1259 C C   . TYR A 189 ? 0.4035 0.3071 0.2959 0.0143  -0.0651 0.0294  168 TYR A C   
1260 O O   . TYR A 189 ? 0.4331 0.3416 0.3195 0.0122  -0.0689 0.0276  168 TYR A O   
1261 C CB  . TYR A 189 ? 0.3752 0.2780 0.2673 0.0077  -0.0524 0.0217  168 TYR A CB  
1262 C CG  . TYR A 189 ? 0.3316 0.2304 0.2194 0.0041  -0.0453 0.0207  168 TYR A CG  
1263 C CD1 . TYR A 189 ? 0.3071 0.2034 0.1827 0.0011  -0.0429 0.0220  168 TYR A CD1 
1264 C CD2 . TYR A 189 ? 0.3381 0.2366 0.2344 0.0036  -0.0410 0.0184  168 TYR A CD2 
1265 C CE1 . TYR A 189 ? 0.3524 0.2474 0.2267 -0.0023 -0.0364 0.0213  168 TYR A CE1 
1266 C CE2 . TYR A 189 ? 0.3502 0.2470 0.2440 -0.0001 -0.0355 0.0177  168 TYR A CE2 
1267 C CZ  . TYR A 189 ? 0.3345 0.2303 0.2185 -0.0029 -0.0332 0.0193  168 TYR A CZ  
1268 O OH  . TYR A 189 ? 0.3527 0.2490 0.2367 -0.0066 -0.0277 0.0188  168 TYR A OH  
1269 N N   . GLY A 190 ? 0.2543 0.2669 0.4349 0.0443  -0.1227 -0.0181 169 GLY A N   
1270 C CA  . GLY A 190 ? 0.2851 0.3249 0.4723 0.0401  -0.1170 -0.0104 169 GLY A CA  
1271 C C   . GLY A 190 ? 0.2882 0.3189 0.4627 0.0359  -0.1137 -0.0099 169 GLY A C   
1272 O O   . GLY A 190 ? 0.3488 0.3502 0.5088 0.0361  -0.1167 -0.0154 169 GLY A O   
1273 N N   . ASP A 191 ? 0.3033 0.3625 0.4827 0.0313  -0.1076 -0.0029 170 ASP A N   
1274 C CA  . ASP A 191 ? 0.3134 0.3698 0.4809 0.0268  -0.1027 -0.0011 170 ASP A CA  
1275 C C   . ASP A 191 ? 0.3371 0.3735 0.4898 0.0105  -0.1079 -0.0069 170 ASP A C   
1276 O O   . ASP A 191 ? 0.4145 0.4678 0.5657 -0.0050 -0.1067 -0.0053 170 ASP A O   
1277 C CB  . ASP A 191 ? 0.2975 0.3971 0.4753 0.0260  -0.0946 0.0079  170 ASP A CB  
1278 C CG  . ASP A 191 ? 0.3979 0.5105 0.5838 0.0465  -0.0879 0.0142  170 ASP A CG  
1279 O OD1 . ASP A 191 ? 0.4304 0.5162 0.6130 0.0583  -0.0897 0.0114  170 ASP A OD1 
1280 O OD2 . ASP A 191 ? 0.5124 0.6616 0.7056 0.0506  -0.0806 0.0220  170 ASP A OD2 
1281 N N   . ILE A 192 ? 0.3272 0.3259 0.4661 0.0141  -0.1133 -0.0137 171 ILE A N   
1282 C CA  . ILE A 192 ? 0.3701 0.3416 0.4895 0.0031  -0.1179 -0.0189 171 ILE A CA  
1283 C C   . ILE A 192 ? 0.3398 0.2976 0.4411 -0.0010 -0.1133 -0.0170 171 ILE A C   
1284 O O   . ILE A 192 ? 0.3596 0.3082 0.4446 -0.0157 -0.1128 -0.0173 171 ILE A O   
1285 C CB  . ILE A 192 ? 0.3565 0.2984 0.4697 0.0113  -0.1266 -0.0268 171 ILE A CB  
1286 C CG1 . ILE A 192 ? 0.3778 0.3348 0.5080 0.0132  -0.1311 -0.0292 171 ILE A CG1 
1287 C CG2 . ILE A 192 ? 0.3711 0.2807 0.4602 0.0045  -0.1310 -0.0314 171 ILE A CG2 
1288 C CD1 . ILE A 192 ? 0.4172 0.3872 0.5495 -0.0008 -0.1321 -0.0292 171 ILE A CD1 
1289 N N   . PHE A 193 ? 0.3011 0.2553 0.4026 0.0109  -0.1094 -0.0152 172 PHE A N   
1290 C CA  . PHE A 193 ? 0.3122 0.2544 0.3972 0.0082  -0.1047 -0.0135 172 PHE A CA  
1291 C C   . PHE A 193 ? 0.3074 0.2858 0.4024 0.0077  -0.0948 -0.0061 172 PHE A C   
1292 O O   . PHE A 193 ? 0.2840 0.2902 0.3979 0.0173  -0.0912 -0.0021 172 PHE A O   
1293 C CB  . PHE A 193 ? 0.2958 0.2107 0.3720 0.0214  -0.1063 -0.0169 172 PHE A CB  
1294 C CG  . PHE A 193 ? 0.3153 0.1993 0.3805 0.0241  -0.1160 -0.0240 172 PHE A CG  
1295 C CD1 . PHE A 193 ? 0.3215 0.1818 0.3668 0.0153  -0.1205 -0.0265 172 PHE A CD1 
1296 C CD2 . PHE A 193 ? 0.2920 0.1701 0.3639 0.0357  -0.1202 -0.0281 172 PHE A CD2 
1297 C CE1 . PHE A 193 ? 0.3295 0.1635 0.3638 0.0214  -0.1292 -0.0326 172 PHE A CE1 
1298 C CE2 . PHE A 193 ? 0.3011 0.1577 0.3637 0.0391  -0.1291 -0.0346 172 PHE A CE2 
1299 C CZ  . PHE A 193 ? 0.3164 0.1521 0.3610 0.0337  -0.1338 -0.0367 172 PHE A CZ  
1300 N N   . LYS A 194 ? 0.4095 0.3878 0.4902 -0.0029 -0.0900 -0.0041 173 LYS A N   
1301 C CA  . LYS A 194 ? 0.3759 0.3839 0.4624 0.0010  -0.0802 0.0019  173 LYS A CA  
1302 C C   . LYS A 194 ? 0.3652 0.3505 0.4455 0.0174  -0.0779 0.0005  173 LYS A C   
1303 O O   . LYS A 194 ? 0.3785 0.3263 0.4411 0.0165  -0.0824 -0.0043 173 LYS A O   
1304 C CB  . LYS A 194 ? 0.3772 0.3956 0.4492 -0.0187 -0.0756 0.0040  173 LYS A CB  
1305 C CG  . LYS A 194 ? 0.3886 0.4389 0.4664 -0.0372 -0.0751 0.0062  173 LYS A CG  
1306 C CD  . LYS A 194 ? 0.4664 0.5690 0.5526 -0.0435 -0.0654 0.0128  173 LYS A CD  
1307 C CE  . LYS A 194 ? 0.5026 0.6414 0.6138 -0.0201 -0.0603 0.0182  173 LYS A CE  
1308 N NZ  . LYS A 194 ? 0.5894 0.7887 0.7114 -0.0243 -0.0513 0.0252  173 LYS A NZ  
1309 N N   . VAL A 195 ? 0.2998 0.3062 0.3925 0.0329  -0.0708 0.0047  174 VAL A N   
1310 C CA  . VAL A 195 ? 0.3094 0.2941 0.3930 0.0470  -0.0667 0.0034  174 VAL A CA  
1311 C C   . VAL A 195 ? 0.3286 0.3214 0.4006 0.0410  -0.0593 0.0058  174 VAL A C   
1312 O O   . VAL A 195 ? 0.3366 0.3696 0.4178 0.0402  -0.0517 0.0115  174 VAL A O   
1313 C CB  . VAL A 195 ? 0.3086 0.3057 0.4042 0.0669  -0.0608 0.0068  174 VAL A CB  
1314 C CG1 . VAL A 195 ? 0.4170 0.3846 0.4982 0.0793  -0.0563 0.0042  174 VAL A CG1 
1315 C CG2 . VAL A 195 ? 0.3112 0.3048 0.4182 0.0699  -0.0677 0.0051  174 VAL A CG2 
1316 N N   . PRO A 196 ? 0.3415 0.3008 0.3934 0.0366  -0.0613 0.0017  175 PRO A N   
1317 C CA  . PRO A 196 ? 0.3965 0.3637 0.4364 0.0302  -0.0538 0.0039  175 PRO A CA  
1318 C C   . PRO A 196 ? 0.4210 0.4097 0.4679 0.0474  -0.0428 0.0077  175 PRO A C   
1319 O O   . PRO A 196 ? 0.4418 0.4217 0.4945 0.0649  -0.0413 0.0072  175 PRO A O   
1320 C CB  . PRO A 196 ? 0.4360 0.3574 0.4525 0.0261  -0.0592 -0.0013 175 PRO A CB  
1321 C CG  . PRO A 196 ? 0.3817 0.2776 0.3982 0.0264  -0.0704 -0.0060 175 PRO A CG  
1322 C CD  . PRO A 196 ? 0.3924 0.3085 0.4313 0.0376  -0.0702 -0.0048 175 PRO A CD  
1323 N N   . GLU A 197 ? 0.4909 0.5076 0.5353 0.0421  -0.0344 0.0113  176 GLU A N   
1324 C CA  . GLU A 197 ? 0.5086 0.5504 0.5592 0.0604  -0.0229 0.0153  176 GLU A CA  
1325 C C   . GLU A 197 ? 0.6202 0.6235 0.6542 0.0721  -0.0198 0.0113  176 GLU A C   
1326 O O   . GLU A 197 ? 0.6363 0.6046 0.6530 0.0617  -0.0251 0.0065  176 GLU A O   
1327 C CB  . GLU A 197 ? 0.5088 0.5969 0.5613 0.0507  -0.0147 0.0198  176 GLU A CB  
1328 C CG  . GLU A 197 ? 0.5275 0.6723 0.6023 0.0540  -0.0112 0.0262  176 GLU A CG  
1329 C CD  . GLU A 197 ? 0.6124 0.8035 0.6877 0.0327  -0.0072 0.0292  176 GLU A CD  
1330 O OE1 . GLU A 197 ? 0.6413 0.8321 0.7020 0.0243  -0.0020 0.0281  176 GLU A OE1 
1331 O OE2 . GLU A 197 ? 0.6638 0.8922 0.7526 0.0226  -0.0092 0.0324  176 GLU A OE2 
1332 N N   . PRO A 198 ? 0.5354 0.5428 0.5721 0.0944  -0.0110 0.0131  177 PRO A N   
1333 C CA  . PRO A 198 ? 0.5584 0.5294 0.5768 0.1049  -0.0063 0.0090  177 PRO A CA  
1334 C C   . PRO A 198 ? 0.4501 0.4300 0.4561 0.1002  0.0016  0.0092  177 PRO A C   
1335 O O   . PRO A 198 ? 0.6050 0.5690 0.5989 0.0820  -0.0039 0.0063  177 PRO A O   
1336 C CB  . PRO A 198 ? 0.5436 0.5181 0.5666 0.1301  0.0020  0.0119  177 PRO A CB  
1337 C CG  . PRO A 198 ? 0.5143 0.5430 0.5580 0.1350  0.0059  0.0195  177 PRO A CG  
1338 C CD  . PRO A 198 ? 0.4677 0.5117 0.5221 0.1115  -0.0048 0.0194  177 PRO A CD  
1339 N N   . ARG A 206 ? 1.1240 1.1143 0.8421 -0.1014 0.0798  -0.0049 185 ARG A N   
1340 C CA  . ARG A 206 ? 1.2010 1.1434 0.9140 -0.0808 0.0760  -0.0086 185 ARG A CA  
1341 C C   . ARG A 206 ? 1.1210 1.0295 0.8019 -0.0935 0.0762  -0.0107 185 ARG A C   
1342 O O   . ARG A 206 ? 1.0865 1.0133 0.7630 -0.0881 0.0880  -0.0135 185 ARG A O   
1343 C CB  . ARG A 206 ? 1.2383 1.2062 0.9734 -0.0492 0.0870  -0.0112 185 ARG A CB  
1344 C CG  . ARG A 206 ? 1.2614 1.1797 0.9916 -0.0291 0.0831  -0.0155 185 ARG A CG  
1345 C CD  . ARG A 206 ? 1.1443 1.0765 0.8785 -0.0043 0.0977  -0.0194 185 ARG A CD  
1346 N NE  . ARG A 206 ? 1.2487 1.1886 0.9632 -0.0132 0.1073  -0.0217 185 ARG A NE  
1347 C CZ  . ARG A 206 ? 1.2775 1.2707 0.9969 -0.0156 0.1199  -0.0207 185 ARG A CZ  
1348 N NH1 . ARG A 206 ? 1.2946 1.3423 1.0384 -0.0095 0.1246  -0.0169 185 ARG A NH1 
1349 N NH2 . ARG A 206 ? 1.1665 1.1619 0.8658 -0.0245 0.1279  -0.0234 185 ARG A NH2 
1350 N N   . VAL A 207 ? 1.1121 0.9710 0.7696 -0.1089 0.0635  -0.0093 186 VAL A N   
1351 C CA  . VAL A 207 ? 1.0994 0.9233 0.7235 -0.1223 0.0619  -0.0102 186 VAL A CA  
1352 C C   . VAL A 207 ? 0.9981 0.7805 0.6176 -0.1034 0.0567  -0.0140 186 VAL A C   
1353 O O   . VAL A 207 ? 1.1263 0.8874 0.7576 -0.0896 0.0474  -0.0145 186 VAL A O   
1354 C CB  . VAL A 207 ? 1.0619 0.8533 0.6575 -0.1496 0.0515  -0.0058 186 VAL A CB  
1355 C CG1 . VAL A 207 ? 1.0698 0.8129 0.6304 -0.1569 0.0463  -0.0060 186 VAL A CG1 
1356 C CG2 . VAL A 207 ? 1.2898 1.1215 0.8804 -0.1752 0.0593  -0.0031 186 VAL A CG2 
1357 N N   . MET A 208 ? 0.9894 0.7617 0.5901 -0.1047 0.0627  -0.0170 187 MET A N   
1358 C CA  . MET A 208 ? 1.0322 0.7696 0.6247 -0.0902 0.0599  -0.0214 187 MET A CA  
1359 C C   . MET A 208 ? 1.0131 0.7092 0.5705 -0.1065 0.0514  -0.0200 187 MET A C   
1360 O O   . MET A 208 ? 0.9912 0.6862 0.5280 -0.1285 0.0510  -0.0161 187 MET A O   
1361 C CB  . MET A 208 ? 0.9759 0.7360 0.5749 -0.0748 0.0757  -0.0268 187 MET A CB  
1362 C CG  . MET A 208 ? 1.0450 0.8565 0.6732 -0.0609 0.0877  -0.0267 187 MET A CG  
1363 S SD  . MET A 208 ? 1.0313 0.8428 0.6901 -0.0390 0.0815  -0.0261 187 MET A SD  
1364 C CE  . MET A 208 ? 1.0752 0.8385 0.7234 -0.0219 0.0790  -0.0326 187 MET A CE  
1365 N N   . SER A 209 ? 1.0165 0.6787 0.5654 -0.0960 0.0448  -0.0231 188 SER A N   
1366 C CA  . SER A 209 ? 1.0427 0.6670 0.5584 -0.1079 0.0363  -0.0216 188 SER A CA  
1367 C C   . SER A 209 ? 1.0194 0.6537 0.5142 -0.1221 0.0473  -0.0224 188 SER A C   
1368 O O   . SER A 209 ? 0.9257 0.5864 0.4299 -0.1146 0.0615  -0.0272 188 SER A O   
1369 C CB  . SER A 209 ? 1.0102 0.6072 0.5231 -0.0936 0.0294  -0.0260 188 SER A CB  
1370 O OG  . SER A 209 ? 1.1082 0.6975 0.6393 -0.0817 0.0189  -0.0255 188 SER A OG  
1371 N N   . LEU A 210 ? 0.9574 0.5686 0.4213 -0.1422 0.0410  -0.0175 189 LEU A N   
1372 C CA  . LEU A 210 ? 1.0158 0.6368 0.4576 -0.1594 0.0511  -0.0176 189 LEU A CA  
1373 C C   . LEU A 210 ? 1.0179 0.6319 0.4508 -0.1511 0.0570  -0.0235 189 LEU A C   
1374 O O   . LEU A 210 ? 0.9851 0.6259 0.4178 -0.1536 0.0716  -0.0273 189 LEU A O   
1375 C CB  . LEU A 210 ? 1.0521 0.6410 0.4574 -0.1826 0.0421  -0.0107 189 LEU A CB  
1376 C CG  . LEU A 210 ? 1.1519 0.7399 0.5577 -0.1946 0.0365  -0.0050 189 LEU A CG  
1377 C CD1 . LEU A 210 ? 1.1621 0.7142 0.5236 -0.2197 0.0308  0.0014  189 LEU A CD1 
1378 C CD2 . LEU A 210 ? 1.0209 0.6636 0.4538 -0.1987 0.0493  -0.0066 189 LEU A CD2 
1379 N N   . LEU A 211 ? 1.0303 0.6102 0.4544 -0.1419 0.0464  -0.0248 190 LEU A N   
1380 C CA  . LEU A 211 ? 1.0262 0.5966 0.4390 -0.1362 0.0513  -0.0308 190 LEU A CA  
1381 C C   . LEU A 211 ? 1.0706 0.6510 0.5079 -0.1144 0.0575  -0.0382 190 LEU A C   
1382 O O   . LEU A 211 ? 1.0584 0.6301 0.4856 -0.1097 0.0634  -0.0444 190 LEU A O   
1383 C CB  . LEU A 211 ? 1.0456 0.5756 0.4302 -0.1409 0.0364  -0.0280 190 LEU A CB  
1384 C CG  . LEU A 211 ? 1.0661 0.5755 0.4178 -0.1613 0.0296  -0.0201 190 LEU A CG  
1385 C CD1 . LEU A 211 ? 1.0633 0.5339 0.3905 -0.1596 0.0130  -0.0163 190 LEU A CD1 
1386 C CD2 . LEU A 211 ? 1.1195 0.6415 0.4524 -0.1771 0.0426  -0.0217 190 LEU A CD2 
1387 N N   . GLU A 212 ? 0.9748 0.5709 0.4412 -0.1020 0.0569  -0.0378 191 GLU A N   
1388 C CA  . GLU A 212 ? 1.0385 0.6411 0.5260 -0.0814 0.0633  -0.0441 191 GLU A CA  
1389 C C   . GLU A 212 ? 1.0562 0.6941 0.5734 -0.0722 0.0708  -0.0426 191 GLU A C   
1390 O O   . GLU A 212 ? 0.9865 0.6251 0.5239 -0.0634 0.0634  -0.0408 191 GLU A O   
1391 C CB  . GLU A 212 ? 1.1070 0.6818 0.5960 -0.0739 0.0489  -0.0451 191 GLU A CB  
1392 C CG  . GLU A 212 ? 1.1945 0.7430 0.6592 -0.0764 0.0462  -0.0499 191 GLU A CG  
1393 C CD  . GLU A 212 ? 1.2241 0.7496 0.6841 -0.0757 0.0280  -0.0482 191 GLU A CD  
1394 O OE1 . GLU A 212 ? 1.3360 0.8436 0.7716 -0.0858 0.0186  -0.0453 191 GLU A OE1 
1395 O OE2 . GLU A 212 ? 1.2699 0.7968 0.7499 -0.0644 0.0231  -0.0496 191 GLU A OE2 
1396 N N   . PRO A 213 ? 0.9993 0.6706 0.5200 -0.0736 0.0857  -0.0432 192 PRO A N   
1397 C CA  . PRO A 213 ? 0.9801 0.6927 0.5277 -0.0676 0.0921  -0.0404 192 PRO A CA  
1398 C C   . PRO A 213 ? 0.9700 0.6929 0.5423 -0.0421 0.0981  -0.0437 192 PRO A C   
1399 O O   . PRO A 213 ? 1.0149 0.7755 0.6100 -0.0344 0.1042  -0.0412 192 PRO A O   
1400 C CB  . PRO A 213 ? 1.0315 0.7794 0.5723 -0.0759 0.1070  -0.0410 192 PRO A CB  
1401 C CG  . PRO A 213 ? 0.9991 0.7238 0.5157 -0.0756 0.1129  -0.0468 192 PRO A CG  
1402 C CD  . PRO A 213 ? 0.9450 0.6212 0.4440 -0.0826 0.0967  -0.0461 192 PRO A CD  
1403 N N   . THR A 214 ? 1.0097 0.7013 0.5764 -0.0295 0.0971  -0.0491 193 THR A N   
1404 C CA  . THR A 214 ? 1.0272 0.7201 0.6125 -0.0068 0.1015  -0.0518 193 THR A CA  
1405 C C   . THR A 214 ? 1.0743 0.7496 0.6725 -0.0057 0.0857  -0.0494 193 THR A C   
1406 O O   . THR A 214 ? 1.1015 0.7759 0.7148 0.0112  0.0878  -0.0511 193 THR A O   
1407 C CB  . THR A 214 ? 0.9207 0.5881 0.4889 0.0053  0.1118  -0.0600 193 THR A CB  
1408 O OG1 . THR A 214 ? 1.0707 0.6995 0.6172 -0.0068 0.1010  -0.0628 193 THR A OG1 
1409 C CG2 . THR A 214 ? 0.9215 0.6087 0.4784 0.0079  0.1293  -0.0629 193 THR A CG2 
1410 N N   . LYS A 215 ? 1.1366 0.7970 0.7273 -0.0223 0.0704  -0.0454 194 LYS A N   
1411 C CA  . LYS A 215 ? 1.1679 0.8151 0.7704 -0.0215 0.0551  -0.0427 194 LYS A CA  
1412 C C   . LYS A 215 ? 1.0590 0.7208 0.6671 -0.0352 0.0475  -0.0354 194 LYS A C   
1413 O O   . LYS A 215 ? 0.9798 0.6411 0.5697 -0.0518 0.0472  -0.0326 194 LYS A O   
1414 C CB  . LYS A 215 ? 1.0412 0.6511 0.6247 -0.0263 0.0427  -0.0452 194 LYS A CB  
1415 N N   . LYS A 216 ? 1.0460 0.7192 0.6767 -0.0296 0.0419  -0.0325 195 LYS A N   
1416 C CA  . LYS A 216 ? 1.0871 0.7744 0.7220 -0.0435 0.0364  -0.0263 195 LYS A CA  
1417 C C   . LYS A 216 ? 1.0614 0.7139 0.6714 -0.0587 0.0223  -0.0232 195 LYS A C   
1418 O O   . LYS A 216 ? 1.0430 0.6653 0.6419 -0.0542 0.0131  -0.0253 195 LYS A O   
1419 C CB  . LYS A 216 ? 1.0881 0.7921 0.7513 -0.0340 0.0326  -0.0243 195 LYS A CB  
1420 C CG  . LYS A 216 ? 1.1384 0.8134 0.8049 -0.0282 0.0179  -0.0250 195 LYS A CG  
1421 C CD  . LYS A 216 ? 1.1377 0.7942 0.7915 -0.0430 0.0045  -0.0202 195 LYS A CD  
1422 C CE  . LYS A 216 ? 1.1719 0.8079 0.8330 -0.0346 -0.0094 -0.0208 195 LYS A CE  
1423 N NZ  . LYS A 216 ? 1.1913 0.7942 0.8265 -0.0439 -0.0222 -0.0180 195 LYS A NZ  
1424 N N   . MET A 217 ? 0.9388 0.8096 0.8313 0.0388  0.1056  -0.1040 196 MET A N   
1425 C CA  . MET A 217 ? 0.9180 0.8117 0.8383 0.0230  0.1134  -0.0973 196 MET A CA  
1426 C C   . MET A 217 ? 0.9304 0.7985 0.8412 0.0236  0.1315  -0.0830 196 MET A C   
1427 O O   . MET A 217 ? 0.9729 0.8167 0.8535 0.0371  0.1343  -0.0824 196 MET A O   
1428 C CB  . MET A 217 ? 0.8912 0.8082 0.8150 0.0223  0.1020  -0.1090 196 MET A CB  
1429 C CG  . MET A 217 ? 0.7372 0.6795 0.6896 0.0034  0.1038  -0.1046 196 MET A CG  
1430 S SD  . MET A 217 ? 0.6955 0.6588 0.6491 -0.0021 0.0915  -0.1176 196 MET A SD  
1431 C CE  . MET A 217 ? 0.6595 0.6671 0.6341 -0.0152 0.0812  -0.1309 196 MET A CE  
1432 N N   . SER A 218 ? 1.2075 1.0842 1.1446 0.0102  0.1432  -0.0736 197 SER A N   
1433 C CA  . SER A 218 ? 1.1617 1.0211 1.0955 0.0095  0.1624  -0.0627 197 SER A CA  
1434 C C   . SER A 218 ? 1.1951 1.0765 1.1561 0.0016  0.1651  -0.0614 197 SER A C   
1435 O O   . SER A 218 ? 1.0939 0.9999 1.0843 -0.0094 0.1586  -0.0631 197 SER A O   
1436 C CB  . SER A 218 ? 1.0581 0.9056 0.9991 0.0015  0.1753  -0.0554 197 SER A CB  
1437 O OG  . SER A 218 ? 1.1475 0.9849 1.0886 -0.0020 0.1965  -0.0468 197 SER A OG  
1438 N N   . LYS A 219 ? 1.2464 1.1167 1.1945 0.0093  0.1735  -0.0590 198 LYS A N   
1439 C CA  . LYS A 219 ? 1.2559 1.1420 1.2268 0.0055  0.1754  -0.0590 198 LYS A CA  
1440 C C   . LYS A 219 ? 1.2364 1.1365 1.2379 -0.0045 0.1881  -0.0557 198 LYS A C   
1441 O O   . LYS A 219 ? 1.2531 1.1715 1.2800 -0.0080 0.1843  -0.0583 198 LYS A O   
1442 C CB  . LYS A 219 ? 1.2566 1.1283 1.2058 0.0188  0.1815  -0.0596 198 LYS A CB  
1443 N N   . SER A 220 ? 1.0769 0.9670 1.0759 -0.0090 0.2017  -0.0511 199 SER A N   
1444 C CA  . SER A 220 ? 1.1123 1.0176 1.1437 -0.0205 0.2148  -0.0502 199 SER A CA  
1445 C C   . SER A 220 ? 1.1050 1.0287 1.1650 -0.0306 0.2031  -0.0533 199 SER A C   
1446 O O   . SER A 220 ? 1.1034 1.0442 1.1957 -0.0396 0.2103  -0.0555 199 SER A O   
1447 C CB  . SER A 220 ? 1.1537 1.0360 1.1678 -0.0244 0.2366  -0.0432 199 SER A CB  
1448 O OG  . SER A 220 ? 1.1772 1.0349 1.1685 -0.0246 0.2305  -0.0397 199 SER A OG  
1449 N N   . ASP A 221 ? 1.0327 0.9569 1.0830 -0.0288 0.1855  -0.0556 200 ASP A N   
1450 C CA  . ASP A 221 ? 1.0042 0.9471 1.0779 -0.0369 0.1746  -0.0595 200 ASP A CA  
1451 C C   . ASP A 221 ? 0.9301 0.8993 1.0379 -0.0424 0.1712  -0.0627 200 ASP A C   
1452 O O   . ASP A 221 ? 0.9451 0.9197 1.0515 -0.0390 0.1645  -0.0634 200 ASP A O   
1453 C CB  . ASP A 221 ? 0.9344 0.8819 0.9930 -0.0339 0.1567  -0.0641 200 ASP A CB  
1454 C CG  . ASP A 221 ? 0.8746 0.8397 0.9506 -0.0398 0.1466  -0.0694 200 ASP A CG  
1455 O OD1 . ASP A 221 ? 0.7802 0.7616 0.8853 -0.0469 0.1477  -0.0702 200 ASP A OD1 
1456 O OD2 . ASP A 221 ? 0.8847 0.8493 0.9457 -0.0355 0.1362  -0.0751 200 ASP A OD2 
1457 N N   . ASP A 222 ? 0.9862 0.9692 1.1232 -0.0499 0.1740  -0.0657 201 ASP A N   
1458 C CA  . ASP A 222 ? 0.9921 1.0002 1.1612 -0.0522 0.1686  -0.0712 201 ASP A CA  
1459 C C   . ASP A 222 ? 1.0332 1.0517 1.1969 -0.0513 0.1488  -0.0724 201 ASP A C   
1460 O O   . ASP A 222 ? 0.9942 1.0180 1.1615 -0.0482 0.1415  -0.0734 201 ASP A O   
1461 C CB  . ASP A 222 ? 0.8781 0.9002 1.0804 -0.0600 0.1731  -0.0767 201 ASP A CB  
1462 N N   . ASN A 223 ? 0.7760 0.7966 0.9287 -0.0540 0.1397  -0.0728 202 ASN A N   
1463 C CA  . ASN A 223 ? 0.7644 0.7964 0.9078 -0.0566 0.1242  -0.0736 202 ASN A CA  
1464 C C   . ASN A 223 ? 0.6463 0.6636 0.7607 -0.0546 0.1227  -0.0702 202 ASN A C   
1465 O O   . ASN A 223 ? 0.5876 0.5987 0.6849 -0.0525 0.1230  -0.0718 202 ASN A O   
1466 C CB  . ASN A 223 ? 0.5885 0.6360 0.7353 -0.0601 0.1162  -0.0789 202 ASN A CB  
1467 C CG  . ASN A 223 ? 0.5403 0.6053 0.6789 -0.0658 0.1030  -0.0802 202 ASN A CG  
1468 O OD1 . ASN A 223 ? 0.5474 0.6058 0.6710 -0.0687 0.0999  -0.0756 202 ASN A OD1 
1469 N ND2 . ASN A 223 ? 0.5300 0.6161 0.6766 -0.0681 0.0956  -0.0869 202 ASN A ND2 
1470 N N   . ARG A 224 ? 0.6732 0.6836 0.7816 -0.0537 0.1189  -0.0671 203 ARG A N   
1471 C CA  . ARG A 224 ? 0.7158 0.7105 0.7991 -0.0521 0.1166  -0.0652 203 ARG A CA  
1472 C C   . ARG A 224 ? 0.6789 0.6828 0.7481 -0.0611 0.1069  -0.0674 203 ARG A C   
1473 O O   . ARG A 224 ? 0.6809 0.6753 0.7319 -0.0608 0.1049  -0.0688 203 ARG A O   
1474 C CB  . ARG A 224 ? 0.7505 0.7323 0.8306 -0.0488 0.1119  -0.0626 203 ARG A CB  
1475 C CG  . ARG A 224 ? 0.7508 0.7224 0.8353 -0.0369 0.1229  -0.0637 203 ARG A CG  
1476 C CD  . ARG A 224 ? 0.8499 0.8363 0.9639 -0.0349 0.1318  -0.0669 203 ARG A CD  
1477 N NE  . ARG A 224 ? 0.8300 0.8275 0.9599 -0.0364 0.1196  -0.0694 203 ARG A NE  
1478 C CZ  . ARG A 224 ? 0.7768 0.7720 0.9137 -0.0279 0.1132  -0.0735 203 ARG A CZ  
1479 N NH1 . ARG A 224 ? 0.8022 0.7882 0.9348 -0.0178 0.1184  -0.0763 203 ARG A NH1 
1480 N NH2 . ARG A 224 ? 0.6924 0.6945 0.8390 -0.0275 0.0998  -0.0762 203 ARG A NH2 
1481 N N   . ASN A 225 ? 0.5736 0.5987 0.6518 -0.0692 0.1011  -0.0697 204 ASN A N   
1482 C CA  . ASN A 225 ? 0.5710 0.6132 0.6387 -0.0789 0.0946  -0.0747 204 ASN A CA  
1483 C C   . ASN A 225 ? 0.5674 0.6168 0.6314 -0.0723 0.0963  -0.0838 204 ASN A C   
1484 O O   . ASN A 225 ? 0.5641 0.6347 0.6234 -0.0783 0.0907  -0.0924 204 ASN A O   
1485 C CB  . ASN A 225 ? 0.5621 0.6275 0.6385 -0.0881 0.0885  -0.0755 204 ASN A CB  
1486 C CG  . ASN A 225 ? 0.5759 0.6301 0.6440 -0.0956 0.0828  -0.0670 204 ASN A CG  
1487 O OD1 . ASN A 225 ? 0.5938 0.6285 0.6442 -0.1008 0.0805  -0.0620 204 ASN A OD1 
1488 N ND2 . ASN A 225 ? 0.5719 0.6353 0.6506 -0.0950 0.0785  -0.0660 204 ASN A ND2 
1489 N N   . ASN A 226 ? 0.5753 0.6075 0.6396 -0.0600 0.1036  -0.0830 205 ASN A N   
1490 C CA  . ASN A 226 ? 0.5980 0.6246 0.6493 -0.0500 0.1034  -0.0906 205 ASN A CA  
1491 C C   . ASN A 226 ? 0.6362 0.6447 0.6660 -0.0431 0.1041  -0.0916 205 ASN A C   
1492 O O   . ASN A 226 ? 0.6697 0.6731 0.6842 -0.0327 0.1008  -0.0999 205 ASN A O   
1493 C CB  . ASN A 226 ? 0.6415 0.6503 0.6962 -0.0415 0.1113  -0.0875 205 ASN A CB  
1494 C CG  . ASN A 226 ? 0.7119 0.7382 0.7851 -0.0447 0.1067  -0.0921 205 ASN A CG  
1495 O OD1 . ASN A 226 ? 0.6317 0.6743 0.7021 -0.0422 0.0968  -0.1029 205 ASN A OD1 
1496 N ND2 . ASN A 226 ? 0.6515 0.6769 0.7455 -0.0487 0.1129  -0.0866 205 ASN A ND2 
1497 N N   . VAL A 227 ? 0.6235 0.6207 0.6504 -0.0464 0.1062  -0.0850 206 VAL A N   
1498 C CA  . VAL A 227 ? 0.6753 0.6507 0.6828 -0.0368 0.1081  -0.0854 206 VAL A CA  
1499 C C   . VAL A 227 ? 0.6749 0.6541 0.6779 -0.0465 0.0996  -0.0879 206 VAL A C   
1500 O O   . VAL A 227 ? 0.6702 0.6534 0.6813 -0.0591 0.0966  -0.0822 206 VAL A O   
1501 C CB  . VAL A 227 ? 0.7415 0.6948 0.7487 -0.0286 0.1197  -0.0763 206 VAL A CB  
1502 C CG1 . VAL A 227 ? 0.7074 0.6379 0.6898 -0.0140 0.1235  -0.0780 206 VAL A CG1 
1503 C CG2 . VAL A 227 ? 0.7930 0.7473 0.8139 -0.0282 0.1294  -0.0722 206 VAL A CG2 
1504 N N   . ILE A 228 ? 0.6354 0.6104 0.6234 -0.0407 0.0949  -0.0970 207 ILE A N   
1505 C CA  . ILE A 228 ? 0.6660 0.6380 0.6482 -0.0494 0.0875  -0.1004 207 ILE A CA  
1506 C C   . ILE A 228 ? 0.6737 0.6175 0.6396 -0.0330 0.0890  -0.1001 207 ILE A C   
1507 O O   . ILE A 228 ? 0.6752 0.6118 0.6271 -0.0164 0.0902  -0.1068 207 ILE A O   
1508 C CB  . ILE A 228 ? 0.6431 0.6414 0.6262 -0.0582 0.0793  -0.1159 207 ILE A CB  
1509 C CG1 . ILE A 228 ? 0.6850 0.7145 0.6831 -0.0781 0.0784  -0.1164 207 ILE A CG1 
1510 C CG2 . ILE A 228 ? 0.6939 0.6836 0.6693 -0.0645 0.0724  -0.1222 207 ILE A CG2 
1511 C CD1 . ILE A 228 ? 0.7168 0.7371 0.7195 -0.0909 0.0809  -0.1005 207 ILE A CD1 
1512 N N   . GLY A 229 ? 0.7083 0.6344 0.6729 -0.0355 0.0875  -0.0934 208 GLY A N   
1513 C CA  . GLY A 229 ? 0.7487 0.6508 0.6986 -0.0193 0.0876  -0.0950 208 GLY A CA  
1514 C C   . GLY A 229 ? 0.7444 0.6404 0.6853 -0.0237 0.0753  -0.1049 208 GLY A C   
1515 O O   . GLY A 229 ? 0.7163 0.6215 0.6637 -0.0443 0.0679  -0.1066 208 GLY A O   
1516 N N   . LEU A 230 ? 0.7549 0.6349 0.6798 -0.0051 0.0737  -0.1118 209 LEU A N   
1517 C CA  . LEU A 230 ? 0.7637 0.6366 0.6820 -0.0076 0.0607  -0.1235 209 LEU A CA  
1518 C C   . LEU A 230 ? 0.7583 0.6149 0.6802 -0.0236 0.0525  -0.1176 209 LEU A C   
1519 O O   . LEU A 230 ? 0.7704 0.6256 0.6927 -0.0396 0.0420  -0.1248 209 LEU A O   
1520 C CB  . LEU A 230 ? 0.7676 0.6226 0.6659 0.0187  0.0597  -0.1313 209 LEU A CB  
1521 C CG  . LEU A 230 ? 0.8218 0.6838 0.7058 0.0362  0.0611  -0.1418 209 LEU A CG  
1522 C CD1 . LEU A 230 ? 0.8162 0.6566 0.6762 0.0614  0.0573  -0.1501 209 LEU A CD1 
1523 C CD2 . LEU A 230 ? 0.8622 0.7507 0.7569 0.0240  0.0511  -0.1570 209 LEU A CD2 
1524 N N   . LEU A 231 ? 0.7747 0.6176 0.6984 -0.0198 0.0562  -0.1056 210 LEU A N   
1525 C CA  . LEU A 231 ? 0.8010 0.6209 0.7224 -0.0302 0.0456  -0.0998 210 LEU A CA  
1526 C C   . LEU A 231 ? 0.9174 0.7450 0.8481 -0.0491 0.0473  -0.0881 210 LEU A C   
1527 O O   . LEU A 231 ? 0.8863 0.6946 0.8145 -0.0485 0.0418  -0.0805 210 LEU A O   
1528 C CB  . LEU A 231 ? 0.8131 0.6113 0.7280 -0.0075 0.0443  -0.0993 210 LEU A CB  
1529 C CG  . LEU A 231 ? 0.8087 0.5982 0.7105 0.0138  0.0426  -0.1110 210 LEU A CG  
1530 C CD1 . LEU A 231 ? 0.8243 0.5985 0.7211 0.0363  0.0426  -0.1120 210 LEU A CD1 
1531 C CD2 . LEU A 231 ? 0.8293 0.6055 0.7234 0.0037  0.0268  -0.1212 210 LEU A CD2 
1532 N N   . GLU A 232 ? 1.0331 0.8890 0.9730 -0.0637 0.0532  -0.0884 211 GLU A N   
1533 C CA  . GLU A 232 ? 1.0434 0.9096 0.9897 -0.0823 0.0542  -0.0789 211 GLU A CA  
1534 C C   . GLU A 232 ? 1.1156 0.9729 1.0519 -0.1094 0.0454  -0.0781 211 GLU A C   
1535 O O   . GLU A 232 ? 1.0282 0.8975 0.9649 -0.1198 0.0439  -0.0888 211 GLU A O   
1536 C CB  . GLU A 232 ? 0.9193 0.8219 0.8800 -0.0836 0.0646  -0.0813 211 GLU A CB  
1537 N N   . ASP A 233 ? 1.1592 0.9949 1.0853 -0.1213 0.0394  -0.0661 212 ASP A N   
1538 C CA  . ASP A 233 ? 1.1620 0.9797 1.0714 -0.1498 0.0319  -0.0621 212 ASP A CA  
1539 C C   . ASP A 233 ? 1.1275 0.9868 1.0468 -0.1732 0.0407  -0.0685 212 ASP A C   
1540 O O   . ASP A 233 ? 1.1105 1.0041 1.0432 -0.1713 0.0494  -0.0687 212 ASP A O   
1541 C CB  . ASP A 233 ? 1.2527 1.0395 1.1440 -0.1568 0.0244  -0.0466 212 ASP A CB  
1542 C CG  . ASP A 233 ? 1.2728 1.0373 1.1401 -0.1906 0.0192  -0.0390 212 ASP A CG  
1543 O OD1 . ASP A 233 ? 1.2818 1.0089 1.1324 -0.1986 0.0089  -0.0397 212 ASP A OD1 
1544 O OD2 . ASP A 233 ? 1.2794 1.0627 1.1431 -0.2100 0.0258  -0.0324 212 ASP A OD2 
1545 N N   . PRO A 234 ? 1.0923 0.9522 1.0073 -0.1954 0.0382  -0.0762 213 PRO A N   
1546 C CA  . PRO A 234 ? 1.0758 0.9853 1.0055 -0.2156 0.0470  -0.0880 213 PRO A CA  
1547 C C   . PRO A 234 ? 1.0525 0.9850 0.9811 -0.2328 0.0549  -0.0790 213 PRO A C   
1548 O O   . PRO A 234 ? 0.9685 0.9494 0.9157 -0.2310 0.0626  -0.0893 213 PRO A O   
1549 C CB  . PRO A 234 ? 0.9862 0.8835 0.9087 -0.2426 0.0423  -0.0951 213 PRO A CB  
1550 C CG  . PRO A 234 ? 1.0818 0.9321 0.9933 -0.2242 0.0301  -0.0945 213 PRO A CG  
1551 C CD  . PRO A 234 ? 1.1451 0.9647 1.0453 -0.2015 0.0267  -0.0783 213 PRO A CD  
1552 N N   . LYS A 235 ? 1.0603 0.9577 0.9650 -0.2474 0.0513  -0.0610 214 LYS A N   
1553 C CA  . LYS A 235 ? 1.0400 0.9574 0.9392 -0.2619 0.0580  -0.0522 214 LYS A CA  
1554 C C   . LYS A 235 ? 1.0365 0.9788 0.9545 -0.2345 0.0612  -0.0531 214 LYS A C   
1555 O O   . LYS A 235 ? 0.9142 0.8989 0.8437 -0.2397 0.0687  -0.0577 214 LYS A O   
1556 C CB  . LYS A 235 ? 1.0239 0.8883 0.8865 -0.2773 0.0507  -0.0318 214 LYS A CB  
1557 N N   . SER A 236 ? 0.9833 0.9008 0.9051 -0.2058 0.0557  -0.0500 215 SER A N   
1558 C CA  . SER A 236 ? 0.9205 0.8593 0.8617 -0.1822 0.0598  -0.0515 215 SER A CA  
1559 C C   . SER A 236 ? 0.9504 0.9330 0.9145 -0.1744 0.0674  -0.0673 215 SER A C   
1560 O O   . SER A 236 ? 0.8880 0.9009 0.8661 -0.1688 0.0721  -0.0705 215 SER A O   
1561 C CB  . SER A 236 ? 0.9352 0.8422 0.8775 -0.1559 0.0546  -0.0474 215 SER A CB  
1562 O OG  . SER A 236 ? 1.1081 1.0322 1.0684 -0.1384 0.0592  -0.0472 215 SER A OG  
1563 N N   . VAL A 237 ? 1.0002 0.9843 0.9666 -0.1719 0.0666  -0.0787 216 VAL A N   
1564 C CA  . VAL A 237 ? 0.9359 0.9560 0.9188 -0.1606 0.0705  -0.0955 216 VAL A CA  
1565 C C   . VAL A 237 ? 0.8435 0.9099 0.8355 -0.1797 0.0741  -0.1054 216 VAL A C   
1566 O O   . VAL A 237 ? 0.7034 0.8020 0.7093 -0.1683 0.0763  -0.1154 216 VAL A O   
1567 C CB  . VAL A 237 ? 0.9504 0.9608 0.9308 -0.1528 0.0663  -0.1075 216 VAL A CB  
1568 C CG1 . VAL A 237 ? 0.8950 0.9328 0.8862 -0.1333 0.0674  -0.1242 216 VAL A CG1 
1569 C CG2 . VAL A 237 ? 0.9486 0.9137 0.9172 -0.1365 0.0623  -0.0981 216 VAL A CG2 
1570 N N   . VAL A 238 ? 0.8817 0.9517 0.8645 -0.2094 0.0750  -0.1034 217 VAL A N   
1571 C CA  . VAL A 238 ? 0.7980 0.9177 0.7894 -0.2303 0.0807  -0.1142 217 VAL A CA  
1572 C C   . VAL A 238 ? 0.7638 0.8980 0.7563 -0.2272 0.0838  -0.1059 217 VAL A C   
1573 O O   . VAL A 238 ? 0.7837 0.9654 0.7906 -0.2272 0.0868  -0.1194 217 VAL A O   
1574 C CB  . VAL A 238 ? 0.7815 0.8973 0.7591 -0.2671 0.0836  -0.1117 217 VAL A CB  
1575 N N   . LYS A 239 ? 0.7668 0.8621 0.7448 -0.2228 0.0812  -0.0860 218 LYS A N   
1576 C CA  . LYS A 239 ? 0.7697 0.8772 0.7494 -0.2181 0.0822  -0.0794 218 LYS A CA  
1577 C C   . LYS A 239 ? 0.7146 0.8452 0.7181 -0.1917 0.0820  -0.0900 218 LYS A C   
1578 O O   . LYS A 239 ? 0.6209 0.7887 0.6353 -0.1909 0.0834  -0.0981 218 LYS A O   
1579 C CB  . LYS A 239 ? 0.8355 0.8948 0.7962 -0.2142 0.0765  -0.0594 218 LYS A CB  
1580 C CG  . LYS A 239 ? 0.8236 0.8613 0.7528 -0.2416 0.0757  -0.0461 218 LYS A CG  
1581 C CD  . LYS A 239 ? 0.9291 0.9052 0.8350 -0.2353 0.0654  -0.0301 218 LYS A CD  
1582 C CE  . LYS A 239 ? 0.9395 0.8845 0.8059 -0.2602 0.0623  -0.0144 218 LYS A CE  
1583 N NZ  . LYS A 239 ? 1.0233 0.9260 0.8655 -0.2796 0.0587  -0.0084 218 LYS A NZ  
1584 N N   . LYS A 240 ? 0.6986 0.8053 0.7081 -0.1700 0.0801  -0.0902 219 LYS A N   
1585 C CA  . LYS A 240 ? 0.7561 0.8749 0.7825 -0.1469 0.0806  -0.0980 219 LYS A CA  
1586 C C   . LYS A 240 ? 0.6714 0.8308 0.7078 -0.1452 0.0798  -0.1185 219 LYS A C   
1587 O O   . LYS A 240 ? 0.6427 0.8253 0.6908 -0.1348 0.0783  -0.1267 219 LYS A O   
1588 C CB  . LYS A 240 ? 0.6479 0.7313 0.6729 -0.1273 0.0811  -0.0934 219 LYS A CB  
1589 C CG  . LYS A 240 ? 0.7592 0.8074 0.7780 -0.1249 0.0805  -0.0777 219 LYS A CG  
1590 C CD  . LYS A 240 ? 0.6868 0.7073 0.7050 -0.1060 0.0829  -0.0759 219 LYS A CD  
1591 C CE  . LYS A 240 ? 0.6222 0.6181 0.6417 -0.0991 0.0823  -0.0651 219 LYS A CE  
1592 N NZ  . LYS A 240 ? 0.6265 0.6015 0.6460 -0.0816 0.0868  -0.0651 219 LYS A NZ  
1593 N N   . ILE A 241 ? 0.6873 0.8562 0.7202 -0.1540 0.0790  -0.1292 220 ILE A N   
1594 C CA  . ILE A 241 ? 0.6574 0.8702 0.7015 -0.1515 0.0762  -0.1531 220 ILE A CA  
1595 C C   . ILE A 241 ? 0.5784 0.8377 0.6307 -0.1670 0.0784  -0.1605 220 ILE A C   
1596 O O   . ILE A 241 ? 0.5697 0.8653 0.6346 -0.1556 0.0743  -0.1787 220 ILE A O   
1597 C CB  . ILE A 241 ? 0.6346 0.8521 0.6764 -0.1607 0.0746  -0.1653 220 ILE A CB  
1598 C CG1 . ILE A 241 ? 0.6798 0.8590 0.7135 -0.1373 0.0704  -0.1644 220 ILE A CG1 
1599 C CG2 . ILE A 241 ? 0.6310 0.9060 0.6879 -0.1652 0.0719  -0.1934 220 ILE A CG2 
1600 C CD1 . ILE A 241 ? 0.7459 0.9218 0.7804 -0.1070 0.0662  -0.1718 220 ILE A CD1 
1601 N N   . LYS A 242 ? 0.5933 0.8500 0.6354 -0.1921 0.0839  -0.1470 221 LYS A N   
1602 C CA  . LYS A 242 ? 0.5893 0.8896 0.6341 -0.2084 0.0878  -0.1525 221 LYS A CA  
1603 C C   . LYS A 242 ? 0.6301 0.9379 0.6832 -0.1895 0.0840  -0.1514 221 LYS A C   
1604 O O   . LYS A 242 ? 0.6339 0.9882 0.6962 -0.1914 0.0837  -0.1656 221 LYS A O   
1605 C CB  . LYS A 242 ? 0.6195 0.9025 0.6422 -0.2385 0.0944  -0.1342 221 LYS A CB  
1606 N N   . ARG A 243 ? 0.6377 0.7781 0.7878 -0.2015 0.1959  -0.2392 222 ARG A N   
1607 C CA  . ARG A 243 ? 0.6500 0.7791 0.7970 -0.1953 0.1895  -0.2423 222 ARG A CA  
1608 C C   . ARG A 243 ? 0.6235 0.7445 0.7987 -0.1785 0.1729  -0.2443 222 ARG A C   
1609 O O   . ARG A 243 ? 0.5677 0.6755 0.7418 -0.1727 0.1651  -0.2444 222 ARG A O   
1610 C CB  . ARG A 243 ? 0.6050 0.7111 0.7154 -0.2014 0.1874  -0.2219 222 ARG A CB  
1611 N N   . ALA A 244 ? 0.6349 0.7626 0.8350 -0.1708 0.1668  -0.2458 223 ALA A N   
1612 C CA  . ALA A 244 ? 0.5760 0.6948 0.8018 -0.1545 0.1506  -0.2472 223 ALA A CA  
1613 C C   . ALA A 244 ? 0.6438 0.7724 0.8909 -0.1475 0.1504  -0.2701 223 ALA A C   
1614 O O   . ALA A 244 ? 0.5994 0.7510 0.8542 -0.1523 0.1629  -0.2898 223 ALA A O   
1615 C CB  . ALA A 244 ? 0.6431 0.7704 0.8917 -0.1476 0.1452  -0.2473 223 ALA A CB  
1616 N N   . VAL A 245 ? 0.6667 0.7774 0.9233 -0.1360 0.1361  -0.2676 224 VAL A N   
1617 C CA  . VAL A 245 ? 0.6458 0.7615 0.9202 -0.1288 0.1342  -0.2884 224 VAL A CA  
1618 C C   . VAL A 245 ? 0.6125 0.7502 0.9221 -0.1194 0.1341  -0.3099 224 VAL A C   
1619 O O   . VAL A 245 ? 0.5975 0.7388 0.9224 -0.1137 0.1285  -0.3058 224 VAL A O   
1620 C CB  . VAL A 245 ? 0.7028 0.7916 0.9792 -0.1193 0.1181  -0.2792 224 VAL A CB  
1621 C CG1 . VAL A 245 ? 0.7080 0.7868 1.0071 -0.1053 0.1028  -0.2727 224 VAL A CG1 
1622 C CG2 . VAL A 245 ? 0.7368 0.8276 1.0229 -0.1152 0.1177  -0.2993 224 VAL A CG2 
1623 N N   . THR A 246 ? 0.6174 0.7707 0.9402 -0.1173 0.1399  -0.3339 225 THR A N   
1624 C CA  . THR A 246 ? 0.6900 0.8654 1.0483 -0.1069 0.1393  -0.3575 225 THR A CA  
1625 C C   . THR A 246 ? 0.7269 0.8978 1.0988 -0.0969 0.1330  -0.3751 225 THR A C   
1626 O O   . THR A 246 ? 0.7856 0.9331 1.1424 -0.0966 0.1260  -0.3661 225 THR A O   
1627 C CB  . THR A 246 ? 0.6872 0.8956 1.0482 -0.1175 0.1582  -0.3721 225 THR A CB  
1628 O OG1 . THR A 246 ? 0.6635 0.8786 1.0018 -0.1294 0.1726  -0.3787 225 THR A OG1 
1629 C CG2 . THR A 246 ? 0.6003 0.8106 0.9496 -0.1269 0.1625  -0.3544 225 THR A CG2 
1630 N N   . ASP A 247 ? 0.7841 0.9776 1.1857 -0.0882 0.1349  -0.4009 226 ASP A N   
1631 C CA  . ASP A 247 ? 0.7546 0.9462 1.1715 -0.0776 0.1292  -0.4209 226 ASP A CA  
1632 C C   . ASP A 247 ? 0.8512 1.0700 1.2645 -0.0854 0.1472  -0.4436 226 ASP A C   
1633 O O   . ASP A 247 ? 0.8649 1.1014 1.2616 -0.0999 0.1641  -0.4417 226 ASP A O   
1634 C CB  . ASP A 247 ? 0.7935 0.9875 1.2481 -0.0589 0.1150  -0.4337 226 ASP A CB  
1635 C CG  . ASP A 247 ? 0.8754 1.1028 1.3534 -0.0577 0.1233  -0.4487 226 ASP A CG  
1636 O OD1 . ASP A 247 ? 0.7826 1.0388 1.2695 -0.0609 0.1372  -0.4717 226 ASP A OD1 
1637 O OD2 . ASP A 247 ? 0.7509 0.9764 1.2386 -0.0536 0.1160  -0.4377 226 ASP A OD2 
1638 N N   . SER A 248 ? 0.8656 1.0868 1.2941 -0.0755 0.1434  -0.4652 227 SER A N   
1639 C CA  . SER A 248 ? 0.8533 1.0967 1.2762 -0.0811 0.1589  -0.4873 227 SER A CA  
1640 C C   . SER A 248 ? 0.8710 1.1433 1.3299 -0.0693 0.1613  -0.5181 227 SER A C   
1641 O O   . SER A 248 ? 0.8695 1.1531 1.3321 -0.0661 0.1665  -0.5404 227 SER A O   
1642 C CB  . SER A 248 ? 0.8662 1.0872 1.2706 -0.0809 0.1534  -0.4872 227 SER A CB  
1643 O OG  . SER A 248 ? 0.8287 1.0255 1.2520 -0.0654 0.1328  -0.4872 227 SER A OG  
1644 N N   . ASP A 249 ? 0.9145 1.1995 1.4003 -0.0621 0.1572  -0.5205 228 ASP A N   
1645 C CA  . ASP A 249 ? 0.8822 1.1975 1.4042 -0.0506 0.1595  -0.5500 228 ASP A CA  
1646 C C   . ASP A 249 ? 0.8930 1.2448 1.4095 -0.0628 0.1835  -0.5682 228 ASP A C   
1647 O O   . ASP A 249 ? 0.9130 1.2752 1.4090 -0.0797 0.1985  -0.5564 228 ASP A O   
1648 C CB  . ASP A 249 ? 0.8273 1.1513 1.3765 -0.0426 0.1516  -0.5472 228 ASP A CB  
1649 C CG  . ASP A 249 ? 0.8436 1.1333 1.4015 -0.0281 0.1274  -0.5324 228 ASP A CG  
1650 O OD1 . ASP A 249 ? 0.8642 1.1236 1.4082 -0.0248 0.1171  -0.5241 228 ASP A OD1 
1651 O OD2 . ASP A 249 ? 0.7293 1.0224 1.3077 -0.0200 0.1187  -0.5290 228 ASP A OD2 
1652 N N   . GLU A 250 ? 0.9696 1.3399 1.5035 -0.0540 0.1870  -0.5970 229 GLU A N   
1653 C CA  . GLU A 250 ? 0.8352 1.2426 1.3666 -0.0637 0.2100  -0.6175 229 GLU A CA  
1654 C C   . GLU A 250 ? 0.8043 1.2480 1.3784 -0.0524 0.2127  -0.6447 229 GLU A C   
1655 O O   . GLU A 250 ? 0.8883 1.3339 1.4873 -0.0348 0.2025  -0.6664 229 GLU A O   
1656 C CB  . GLU A 250 ? 0.9542 1.3559 1.4672 -0.0638 0.2140  -0.6300 229 GLU A CB  
1657 N N   . PRO A 251 ? 0.8269 1.3000 1.4122 -0.0613 0.2255  -0.6456 230 PRO A N   
1658 C CA  . PRO A 251 ? 0.9189 1.3929 1.4794 -0.0816 0.2377  -0.6225 230 PRO A CA  
1659 C C   . PRO A 251 ? 0.9596 1.4052 1.5187 -0.0790 0.2207  -0.5957 230 PRO A C   
1660 O O   . PRO A 251 ? 0.8965 1.3282 1.4791 -0.0614 0.2009  -0.5972 230 PRO A O   
1661 C CB  . PRO A 251 ? 0.8312 1.3523 1.4155 -0.0878 0.2561  -0.6419 230 PRO A CB  
1662 C CG  . PRO A 251 ? 0.8161 1.3523 1.4465 -0.0660 0.2432  -0.6655 230 PRO A CG  
1663 C CD  . PRO A 251 ? 0.8798 1.3904 1.5083 -0.0503 0.2281  -0.6730 230 PRO A CD  
1664 N N   . PRO A 252 ? 0.9587 1.3944 1.4896 -0.0958 0.2276  -0.5709 231 PRO A N   
1665 C CA  . PRO A 252 ? 0.9759 1.3860 1.5048 -0.0931 0.2119  -0.5458 231 PRO A CA  
1666 C C   . PRO A 252 ? 0.9151 1.3438 1.4838 -0.0817 0.2040  -0.5557 231 PRO A C   
1667 O O   . PRO A 252 ? 0.9182 1.3841 1.5085 -0.0854 0.2169  -0.5741 231 PRO A O   
1668 C CB  . PRO A 252 ? 0.9138 1.3198 1.4078 -0.1147 0.2256  -0.5235 231 PRO A CB  
1669 C CG  . PRO A 252 ? 0.9618 1.3750 1.4295 -0.1267 0.2428  -0.5305 231 PRO A CG  
1670 C CD  . PRO A 252 ? 0.9733 1.4168 1.4697 -0.1173 0.2488  -0.5636 231 PRO A CD  
1671 N N   . VAL A 253 ? 0.8203 1.2230 1.3983 -0.0678 0.1823  -0.5433 232 VAL A N   
1672 C CA  . VAL A 253 ? 0.7898 1.2038 1.4019 -0.0557 0.1711  -0.5487 232 VAL A CA  
1673 C C   . VAL A 253 ? 0.9325 1.3178 1.5287 -0.0573 0.1589  -0.5187 232 VAL A C   
1674 O O   . VAL A 253 ? 0.9145 1.2641 1.4865 -0.0561 0.1487  -0.4984 232 VAL A O   
1675 C CB  . VAL A 253 ? 0.7884 1.2001 1.4331 -0.0321 0.1541  -0.5681 232 VAL A CB  
1676 N N   . VAL A 254 ? 0.8245 1.2262 1.4342 -0.0604 0.1602  -0.5161 233 VAL A N   
1677 C CA  . VAL A 254 ? 0.8264 1.2047 1.4234 -0.0611 0.1488  -0.4898 233 VAL A CA  
1678 C C   . VAL A 254 ? 0.8335 1.2087 1.4629 -0.0397 0.1282  -0.4958 233 VAL A C   
1679 O O   . VAL A 254 ? 0.8265 1.2291 1.4853 -0.0357 0.1285  -0.5099 233 VAL A O   
1680 C CB  . VAL A 254 ? 0.6395 1.0351 1.2268 -0.0793 0.1634  -0.4817 233 VAL A CB  
1681 C CG1 . VAL A 254 ? 0.7526 1.1243 1.3282 -0.0781 0.1504  -0.4562 233 VAL A CG1 
1682 C CG2 . VAL A 254 ? 0.6198 1.0162 1.1731 -0.0999 0.1833  -0.4754 233 VAL A CG2 
1683 N N   . ARG A 255 ? 0.7247 1.0660 1.3486 -0.0262 0.1099  -0.4847 234 ARG A N   
1684 C CA  . ARG A 255 ? 0.7700 1.1037 1.4219 -0.0044 0.0889  -0.4902 234 ARG A CA  
1685 C C   . ARG A 255 ? 0.7459 1.0354 1.3766 0.0024  0.0715  -0.4638 234 ARG A C   
1686 O O   . ARG A 255 ? 0.7423 1.0086 1.3485 -0.0026 0.0726  -0.4530 234 ARG A O   
1687 C CB  . ARG A 255 ? 0.7033 1.0522 1.3851 0.0100  0.0860  -0.5195 234 ARG A CB  
1688 C CG  . ARG A 255 ? 0.7285 1.0640 1.4367 0.0341  0.0626  -0.5252 234 ARG A CG  
1689 C CD  . ARG A 255 ? 0.7651 1.0726 1.4690 0.0449  0.0519  -0.5272 234 ARG A CD  
1690 N NE  . ARG A 255 ? 0.7828 1.1102 1.4912 0.0409  0.0658  -0.5502 234 ARG A NE  
1691 C CZ  . ARG A 255 ? 0.7677 1.0753 1.4691 0.0459  0.0613  -0.5545 234 ARG A CZ  
1692 N NH1 . ARG A 255 ? 0.7263 0.9933 1.4167 0.0545  0.0434  -0.5372 234 ARG A NH1 
1693 N NH2 . ARG A 255 ? 0.8223 1.1514 1.5272 0.0418  0.0751  -0.5766 234 ARG A NH2 
1694 N N   . TYR A 256 ? 0.6759 0.9545 1.3161 0.0138  0.0555  -0.4537 235 TYR A N   
1695 C CA  . TYR A 256 ? 0.6448 0.8830 1.2643 0.0196  0.0397  -0.4266 235 TYR A CA  
1696 C C   . TYR A 256 ? 0.7328 0.9486 1.3628 0.0364  0.0242  -0.4324 235 TYR A C   
1697 O O   . TYR A 256 ? 0.8374 1.0555 1.4954 0.0545  0.0101  -0.4451 235 TYR A O   
1698 C CB  . TYR A 256 ? 0.7257 0.9611 1.3509 0.0263  0.0283  -0.4148 235 TYR A CB  
1699 C CG  . TYR A 256 ? 0.6876 0.8840 1.2866 0.0291  0.0152  -0.3844 235 TYR A CG  
1700 C CD1 . TYR A 256 ? 0.5593 0.7428 1.1239 0.0130  0.0239  -0.3612 235 TYR A CD1 
1701 C CD2 . TYR A 256 ? 0.7210 0.8936 1.3295 0.0481  -0.0056 -0.3789 235 TYR A CD2 
1702 C CE1 . TYR A 256 ? 0.6149 0.7651 1.1565 0.0157  0.0128  -0.3341 235 TYR A CE1 
1703 C CE2 . TYR A 256 ? 0.6824 0.8204 1.2667 0.0501  -0.0164 -0.3509 235 TYR A CE2 
1704 C CZ  . TYR A 256 ? 0.6883 0.8164 1.2399 0.0338  -0.0069 -0.3289 235 TYR A CZ  
1705 O OH  . TYR A 256 ? 0.6785 0.7744 1.2069 0.0360  -0.0169 -0.3016 235 TYR A OH  
1706 N N   . ASP A 257 ? 0.6971 0.8908 1.3050 0.0304  0.0264  -0.4234 236 ASP A N   
1707 C CA  . ASP A 257 ? 0.7012 0.8666 1.3134 0.0440  0.0111  -0.4237 236 ASP A CA  
1708 C C   . ASP A 257 ? 0.7078 0.8409 1.2848 0.0334  0.0111  -0.3969 236 ASP A C   
1709 O O   . ASP A 257 ? 0.7753 0.9109 1.3347 0.0201  0.0240  -0.3979 236 ASP A O   
1710 C CB  . ASP A 257 ? 0.6882 0.8696 1.3200 0.0489  0.0157  -0.4527 236 ASP A CB  
1711 C CG  . ASP A 257 ? 0.7176 0.8669 1.3499 0.0602  0.0010  -0.4520 236 ASP A CG  
1712 O OD1 . ASP A 257 ? 0.6650 0.7809 1.2873 0.0663  -0.0141 -0.4302 236 ASP A OD1 
1713 O OD2 . ASP A 257 ? 0.7380 0.8953 1.3804 0.0628  0.0048  -0.4734 236 ASP A OD2 
1714 N N   . VAL A 258 ? 0.7311 0.8350 1.2979 0.0395  -0.0033 -0.3733 237 VAL A N   
1715 C CA  . VAL A 258 ? 0.8653 0.9414 1.3993 0.0290  -0.0029 -0.3464 237 VAL A CA  
1716 C C   . VAL A 258 ? 0.7535 0.8083 1.2833 0.0301  -0.0070 -0.3486 237 VAL A C   
1717 O O   . VAL A 258 ? 0.6126 0.6534 1.1167 0.0177  -0.0013 -0.3337 237 VAL A O   
1718 C CB  . VAL A 258 ? 0.8047 0.8571 1.3297 0.0357  -0.0168 -0.3210 237 VAL A CB  
1719 C CG1 . VAL A 258 ? 0.8074 0.8296 1.3424 0.0518  -0.0362 -0.3171 237 VAL A CG1 
1720 C CG2 . VAL A 258 ? 0.7197 0.7584 1.2101 0.0205  -0.0098 -0.2941 237 VAL A CG2 
1721 N N   . GLN A 259 ? 0.7716 0.8231 1.3265 0.0451  -0.0175 -0.3675 238 GLN A N   
1722 C CA  . GLN A 259 ? 0.6468 0.6749 1.1990 0.0473  -0.0238 -0.3696 238 GLN A CA  
1723 C C   . GLN A 259 ? 0.6469 0.6912 1.1899 0.0343  -0.0075 -0.3838 238 GLN A C   
1724 O O   . GLN A 259 ? 0.6502 0.6761 1.1725 0.0251  -0.0057 -0.3726 238 GLN A O   
1725 C CB  . GLN A 259 ? 0.6869 0.7071 1.2689 0.0675  -0.0399 -0.3874 238 GLN A CB  
1726 N N   . ASN A 260 ? 0.6553 0.7348 1.2133 0.0332  0.0047  -0.4084 239 ASN A N   
1727 C CA  . ASN A 260 ? 0.6580 0.7542 1.2095 0.0232  0.0197  -0.4254 239 ASN A CA  
1728 C C   . ASN A 260 ? 0.6625 0.7805 1.1918 0.0041  0.0398  -0.4194 239 ASN A C   
1729 O O   . ASN A 260 ? 0.6486 0.7733 1.1625 -0.0068 0.0520  -0.4259 239 ASN A O   
1730 C CB  . ASN A 260 ? 0.6591 0.7811 1.2420 0.0348  0.0211  -0.4594 239 ASN A CB  
1731 C CG  . ASN A 260 ? 0.6767 0.7776 1.2828 0.0548  0.0008  -0.4680 239 ASN A CG  
1732 O OD1 . ASN A 260 ? 0.6884 0.7570 1.2853 0.0570  -0.0100 -0.4581 239 ASN A OD1 
1733 N ND2 . ASN A 260 ? 0.7212 0.8399 1.3580 0.0696  -0.0051 -0.4865 239 ASN A ND2 
1734 N N   . LYS A 261 ? 0.6649 0.7930 1.1914 0.0002  0.0431  -0.4076 240 LYS A N   
1735 C CA  . LYS A 261 ? 0.6501 0.7997 1.1581 -0.0173 0.0618  -0.4031 240 LYS A CA  
1736 C C   . LYS A 261 ? 0.6519 0.7848 1.1378 -0.0240 0.0589  -0.3731 240 LYS A C   
1737 O O   . LYS A 261 ? 0.6214 0.7704 1.1070 -0.0292 0.0651  -0.3690 240 LYS A O   
1738 C CB  . LYS A 261 ? 0.6016 0.7895 1.1337 -0.0161 0.0716  -0.4256 240 LYS A CB  
1739 C CG  . LYS A 261 ? 0.6832 0.8910 1.2392 -0.0083 0.0751  -0.4571 240 LYS A CG  
1740 C CD  . LYS A 261 ? 0.6443 0.8895 1.2302 -0.0039 0.0814  -0.4790 240 LYS A CD  
1741 C CE  . LYS A 261 ? 0.6571 0.9294 1.2297 -0.0227 0.1025  -0.4779 240 LYS A CE  
1742 N NZ  . LYS A 261 ? 0.7565 1.0626 1.3594 -0.0188 0.1063  -0.4945 240 LYS A NZ  
1743 N N   . ALA A 262 ? 0.6328 0.7332 1.1003 -0.0241 0.0492  -0.3519 241 ALA A N   
1744 C CA  . ALA A 262 ? 0.6235 0.7062 1.0714 -0.0279 0.0444  -0.3233 241 ALA A CA  
1745 C C   . ALA A 262 ? 0.5694 0.6679 0.9956 -0.0445 0.0604  -0.3150 241 ALA A C   
1746 O O   . ALA A 262 ? 0.5586 0.6563 0.9789 -0.0456 0.0586  -0.3002 241 ALA A O   
1747 C CB  . ALA A 262 ? 0.5878 0.6368 1.0170 -0.0287 0.0354  -0.3036 241 ALA A CB  
1748 N N   . GLY A 263 ? 0.5719 0.6838 0.9849 -0.0572 0.0757  -0.3241 242 GLY A N   
1749 C CA  . GLY A 263 ? 0.5625 0.6864 0.9522 -0.0736 0.0908  -0.3152 242 GLY A CA  
1750 C C   . GLY A 263 ? 0.5817 0.7330 0.9873 -0.0749 0.0980  -0.3252 242 GLY A C   
1751 O O   . GLY A 263 ? 0.5998 0.7518 0.9916 -0.0825 0.1015  -0.3104 242 GLY A O   
1752 N N   . VAL A 264 ? 0.5608 0.7356 0.9960 -0.0676 0.1001  -0.3511 243 VAL A N   
1753 C CA  . VAL A 264 ? 0.5546 0.7588 1.0084 -0.0693 0.1075  -0.3631 243 VAL A CA  
1754 C C   . VAL A 264 ? 0.5473 0.7449 1.0179 -0.0567 0.0920  -0.3552 243 VAL A C   
1755 O O   . VAL A 264 ? 0.5381 0.7488 1.0108 -0.0614 0.0957  -0.3515 243 VAL A O   
1756 C CB  . VAL A 264 ? 0.5638 0.7978 1.0445 -0.0657 0.1156  -0.3946 243 VAL A CB  
1757 C CG1 . VAL A 264 ? 0.5575 0.8226 1.0639 -0.0651 0.1205  -0.4081 243 VAL A CG1 
1758 C CG2 . VAL A 264 ? 0.5713 0.8153 1.0319 -0.0804 0.1335  -0.4019 243 VAL A CG2 
1759 N N   . SER A 265 ? 0.5529 0.7297 1.0353 -0.0404 0.0743  -0.3527 244 SER A N   
1760 C CA  . SER A 265 ? 0.5485 0.7163 1.0440 -0.0274 0.0585  -0.3439 244 SER A CA  
1761 C C   . SER A 265 ? 0.5378 0.6889 1.0057 -0.0351 0.0573  -0.3158 244 SER A C   
1762 O O   . SER A 265 ? 0.5363 0.6930 1.0108 -0.0318 0.0527  -0.3109 244 SER A O   
1763 C CB  . SER A 265 ? 0.5597 0.7035 1.0676 -0.0098 0.0400  -0.3436 244 SER A CB  
1764 O OG  . SER A 265 ? 0.6377 0.7975 1.1743 -0.0001 0.0391  -0.3711 244 SER A OG  
1765 N N   . ASN A 266 ? 0.5444 0.6753 0.9817 -0.0450 0.0610  -0.2979 245 ASN A N   
1766 C CA  . ASN A 266 ? 0.6007 0.7160 1.0109 -0.0520 0.0603  -0.2716 245 ASN A CA  
1767 C C   . ASN A 266 ? 0.5700 0.7069 0.9740 -0.0647 0.0734  -0.2729 245 ASN A C   
1768 O O   . ASN A 266 ? 0.5330 0.6665 0.9320 -0.0638 0.0686  -0.2600 245 ASN A O   
1769 C CB  . ASN A 266 ? 0.5299 0.6233 0.9101 -0.0609 0.0631  -0.2551 245 ASN A CB  
1770 C CG  . ASN A 266 ? 0.6465 0.7222 0.9994 -0.0662 0.0608  -0.2277 245 ASN A CG  
1771 O OD1 . ASN A 266 ? 0.5762 0.6457 0.9331 -0.0581 0.0509  -0.2176 245 ASN A OD1 
1772 N ND2 . ASN A 266 ? 0.6597 0.7275 0.9842 -0.0792 0.0695  -0.2162 245 ASN A ND2 
1773 N N   . LEU A 267 ? 0.5418 0.7007 0.9454 -0.0768 0.0899  -0.2882 246 LEU A N   
1774 C CA  . LEU A 267 ? 0.5581 0.7376 0.9565 -0.0901 0.1033  -0.2901 246 LEU A CA  
1775 C C   . LEU A 267 ? 0.5381 0.7385 0.9672 -0.0823 0.0988  -0.3030 246 LEU A C   
1776 O O   . LEU A 267 ? 0.5135 0.7234 0.9387 -0.0901 0.1036  -0.2981 246 LEU A O   
1777 C CB  . LEU A 267 ? 0.6507 0.8493 1.0426 -0.1043 0.1223  -0.3046 246 LEU A CB  
1778 C CG  . LEU A 267 ? 0.6337 0.8141 0.9908 -0.1151 0.1288  -0.2910 246 LEU A CG  
1779 C CD1 . LEU A 267 ? 0.5964 0.7942 0.9533 -0.1231 0.1435  -0.3101 246 LEU A CD1 
1780 C CD2 . LEU A 267 ? 0.5256 0.6978 0.8523 -0.1286 0.1350  -0.2704 246 LEU A CD2 
1781 N N   . LEU A 268 ? 0.5182 0.7258 0.9785 -0.0667 0.0891  -0.3199 247 LEU A N   
1782 C CA  . LEU A 268 ? 0.5126 0.7397 1.0036 -0.0573 0.0827  -0.3325 247 LEU A CA  
1783 C C   . LEU A 268 ? 0.5488 0.7554 1.0357 -0.0467 0.0657  -0.3136 247 LEU A C   
1784 O O   . LEU A 268 ? 0.5386 0.7586 1.0379 -0.0453 0.0631  -0.3161 247 LEU A O   
1785 C CB  . LEU A 268 ? 0.5211 0.7626 1.0468 -0.0428 0.0770  -0.3576 247 LEU A CB  
1786 C CG  . LEU A 268 ? 0.5314 0.8010 1.0691 -0.0508 0.0937  -0.3819 247 LEU A CG  
1787 C CD1 . LEU A 268 ? 0.5910 0.8774 1.1672 -0.0340 0.0860  -0.4078 247 LEU A CD1 
1788 C CD2 . LEU A 268 ? 0.5796 0.8774 1.1159 -0.0681 0.1118  -0.3877 247 LEU A CD2 
1789 N N   . ASP A 269 ? 0.5171 0.6919 0.9871 -0.0393 0.0540  -0.2952 248 ASP A N   
1790 C CA  . ASP A 269 ? 0.6320 0.7865 1.0937 -0.0302 0.0392  -0.2754 248 ASP A CA  
1791 C C   . ASP A 269 ? 0.5639 0.7159 0.9993 -0.0438 0.0465  -0.2579 248 ASP A C   
1792 O O   . ASP A 269 ? 0.5126 0.6659 0.9509 -0.0394 0.0394  -0.2520 248 ASP A O   
1793 C CB  . ASP A 269 ? 0.5538 0.6754 1.0025 -0.0210 0.0269  -0.2592 248 ASP A CB  
1794 C CG  . ASP A 269 ? 0.7148 0.8342 1.1904 -0.0046 0.0154  -0.2746 248 ASP A CG  
1795 O OD1 . ASP A 269 ? 0.6486 0.7806 1.1507 0.0078  0.0066  -0.2875 248 ASP A OD1 
1796 O OD2 . ASP A 269 ? 0.7009 0.8058 1.1714 -0.0040 0.0148  -0.2742 248 ASP A OD2 
1797 N N   . ILE A 270 ? 0.5809 0.7289 0.9902 -0.0597 0.0600  -0.2500 249 ILE A N   
1798 C CA  . ILE A 270 ? 0.6282 0.7734 1.0117 -0.0730 0.0675  -0.2343 249 ILE A CA  
1799 C C   . ILE A 270 ? 0.5477 0.7207 0.9474 -0.0798 0.0753  -0.2482 249 ILE A C   
1800 O O   . ILE A 270 ? 0.5774 0.7488 0.9711 -0.0809 0.0717  -0.2387 249 ILE A O   
1801 C CB  . ILE A 270 ? 0.5353 0.6725 0.8893 -0.0884 0.0808  -0.2259 249 ILE A CB  
1802 C CG1 . ILE A 270 ? 0.6246 0.7344 0.9640 -0.0820 0.0722  -0.2116 249 ILE A CG1 
1803 C CG2 . ILE A 270 ? 0.4848 0.6190 0.8122 -0.1020 0.0884  -0.2108 249 ILE A CG2 
1804 C CD1 . ILE A 270 ? 0.7508 0.8529 1.0631 -0.0955 0.0835  -0.2049 249 ILE A CD1 
1805 N N   . LEU A 271 ? 0.5720 0.7713 0.9929 -0.0845 0.0861  -0.2714 250 LEU A N   
1806 C CA  . LEU A 271 ? 0.5769 0.8054 1.0159 -0.0923 0.0948  -0.2862 250 LEU A CA  
1807 C C   . LEU A 271 ? 0.5854 0.8209 1.0511 -0.0775 0.0798  -0.2917 250 LEU A C   
1808 O O   . LEU A 271 ? 0.6147 0.8612 1.0842 -0.0828 0.0810  -0.2914 250 LEU A O   
1809 C CB  . LEU A 271 ? 0.5562 0.8126 1.0144 -0.0986 0.1092  -0.3108 250 LEU A CB  
1810 C CG  . LEU A 271 ? 0.5032 0.7897 0.9700 -0.1148 0.1260  -0.3237 250 LEU A CG  
1811 C CD1 . LEU A 271 ? 0.5943 0.8688 1.0257 -0.1327 0.1359  -0.3045 250 LEU A CD1 
1812 C CD2 . LEU A 271 ? 0.4990 0.8097 0.9796 -0.1205 0.1408  -0.3460 250 LEU A CD2 
1813 N N   . SER A 272 ? 0.5523 0.7806 1.0362 -0.0588 0.0649  -0.2968 251 SER A N   
1814 C CA  . SER A 272 ? 0.5903 0.8228 1.0978 -0.0430 0.0488  -0.3013 251 SER A CA  
1815 C C   . SER A 272 ? 0.6065 0.8161 1.0912 -0.0402 0.0383  -0.2774 251 SER A C   
1816 O O   . SER A 272 ? 0.6945 0.9120 1.1929 -0.0334 0.0292  -0.2799 251 SER A O   
1817 C CB  . SER A 272 ? 0.6367 0.8618 1.1645 -0.0232 0.0346  -0.3100 251 SER A CB  
1818 O OG  . SER A 272 ? 0.7515 0.9742 1.2961 -0.0064 0.0167  -0.3102 251 SER A OG  
1819 N N   . ALA A 273 ? 0.5601 0.7425 1.0109 -0.0448 0.0389  -0.2548 252 ALA A N   
1820 C CA  . ALA A 273 ? 0.6373 0.7973 1.0652 -0.0410 0.0289  -0.2316 252 ALA A CA  
1821 C C   . ALA A 273 ? 0.6943 0.8629 1.1089 -0.0556 0.0378  -0.2267 252 ALA A C   
1822 O O   . ALA A 273 ? 0.6689 0.8361 1.0846 -0.0500 0.0285  -0.2214 252 ALA A O   
1823 C CB  . ALA A 273 ? 0.6780 0.8078 1.0758 -0.0410 0.0269  -0.2100 252 ALA A CB  
1824 N N   . VAL A 274 ? 0.6446 0.8212 1.0460 -0.0740 0.0555  -0.2285 253 VAL A N   
1825 C CA  . VAL A 274 ? 0.6186 0.8002 1.0048 -0.0891 0.0644  -0.2226 253 VAL A CA  
1826 C C   . VAL A 274 ? 0.6733 0.8817 1.0893 -0.0891 0.0638  -0.2402 253 VAL A C   
1827 O O   . VAL A 274 ? 0.7758 0.9825 1.1868 -0.0904 0.0590  -0.2335 253 VAL A O   
1828 C CB  . VAL A 274 ? 0.5789 0.7640 0.9457 -0.1086 0.0837  -0.2223 253 VAL A CB  
1829 C CG1 . VAL A 274 ? 0.5712 0.7597 0.9219 -0.1246 0.0927  -0.2161 253 VAL A CG1 
1830 C CG2 . VAL A 274 ? 0.6031 0.7623 0.9412 -0.1083 0.0834  -0.2052 253 VAL A CG2 
1831 N N   . THR A 275 ? 0.6225 0.8568 1.0708 -0.0874 0.0682  -0.2638 254 THR A N   
1832 C CA  . THR A 275 ? 0.7601 1.0253 1.2381 -0.0917 0.0720  -0.2832 254 THR A CA  
1833 C C   . THR A 275 ? 0.7737 1.0478 1.2836 -0.0721 0.0542  -0.2944 254 THR A C   
1834 O O   . THR A 275 ? 0.7691 1.0644 1.3007 -0.0738 0.0530  -0.3060 254 THR A O   
1835 C CB  . THR A 275 ? 0.6381 0.9313 1.1338 -0.1033 0.0898  -0.3043 254 THR A CB  
1836 O OG1 . THR A 275 ? 0.7427 1.0490 1.2699 -0.0879 0.0828  -0.3228 254 THR A OG1 
1837 C CG2 . THR A 275 ? 0.6525 0.9324 1.1167 -0.1168 0.1041  -0.2942 254 THR A CG2 
1838 N N   . GLY A 276 ? 0.7703 1.0287 1.2838 -0.0537 0.0402  -0.2913 255 GLY A N   
1839 C CA  . GLY A 276 ? 0.7294 0.9933 1.2709 -0.0336 0.0222  -0.3011 255 GLY A CA  
1840 C C   . GLY A 276 ? 0.7974 1.0901 1.3786 -0.0272 0.0237  -0.3290 255 GLY A C   
1841 O O   . GLY A 276 ? 0.8241 1.1199 1.4292 -0.0084 0.0075  -0.3380 255 GLY A O   
1842 N N   . GLN A 277 ? 0.8600 1.1737 1.4484 -0.0415 0.0423  -0.3430 256 GLN A N   
1843 C CA  . GLN A 277 ? 0.9103 1.2532 1.5364 -0.0354 0.0449  -0.3705 256 GLN A CA  
1844 C C   . GLN A 277 ? 0.8972 1.2228 1.5280 -0.0167 0.0325  -0.3717 256 GLN A C   
1845 O O   . GLN A 277 ? 0.8127 1.1113 1.4161 -0.0178 0.0331  -0.3558 256 GLN A O   
1846 C CB  . GLN A 277 ? 0.8633 1.2293 1.4902 -0.0552 0.0687  -0.3829 256 GLN A CB  
1847 C CG  . GLN A 277 ? 0.8509 1.2339 1.4733 -0.0757 0.0827  -0.3823 256 GLN A CG  
1848 C CD  . GLN A 277 ? 0.8145 1.2176 1.4338 -0.0956 0.1067  -0.3925 256 GLN A CD  
1849 O OE1 . GLN A 277 ? 0.8205 1.2527 1.4688 -0.0944 0.1142  -0.4161 256 GLN A OE1 
1850 N NE2 . GLN A 277 ? 0.8070 1.1947 1.3902 -0.1133 0.1187  -0.3749 256 GLN A NE2 
1851 N N   . SER A 278 ? 0.8333 1.1745 1.4996 0.0005  0.0207  -0.3910 257 SER A N   
1852 C CA  . SER A 278 ? 0.7937 1.1198 1.4678 0.0184  0.0089  -0.3949 257 SER A CA  
1853 C C   . SER A 278 ? 0.7824 1.1163 1.4557 0.0097  0.0245  -0.4059 257 SER A C   
1854 O O   . SER A 278 ? 0.7598 1.1233 1.4435 -0.0047 0.0425  -0.4213 257 SER A O   
1855 C CB  . SER A 278 ? 0.8738 1.2173 1.5877 0.0386  -0.0068 -0.4155 257 SER A CB  
1856 O OG  . SER A 278 ? 0.8637 1.1810 1.5775 0.0587  -0.0243 -0.4109 257 SER A OG  
1857 N N   . ILE A 279 ? 0.8371 1.1435 1.4970 0.0183  0.0176  -0.3974 258 ILE A N   
1858 C CA  . ILE A 279 ? 0.7884 1.0969 1.4416 0.0098  0.0315  -0.4047 258 ILE A CA  
1859 C C   . ILE A 279 ? 0.7768 1.1224 1.4664 0.0122  0.0394  -0.4369 258 ILE A C   
1860 O O   . ILE A 279 ? 0.7598 1.1240 1.4457 -0.0034 0.0590  -0.4463 258 ILE A O   
1861 C CB  . ILE A 279 ? 0.7342 1.0058 1.3697 0.0200  0.0202  -0.3906 258 ILE A CB  
1862 C CG1 . ILE A 279 ? 0.7930 1.0325 1.3897 0.0131  0.0174  -0.3587 258 ILE A CG1 
1863 C CG2 . ILE A 279 ? 0.8305 1.1059 1.4638 0.0139  0.0323  -0.4021 258 ILE A CG2 
1864 C CD1 . ILE A 279 ? 0.6043 0.8078 1.1816 0.0202  0.0079  -0.3424 258 ILE A CD1 
1865 N N   . PRO A 280 ? 0.7945 1.1530 1.5192 0.0310  0.0257  -0.4550 259 PRO A N   
1866 C CA  . PRO A 280 ? 0.8787 1.2759 1.6391 0.0328  0.0347  -0.4870 259 PRO A CA  
1867 C C   . PRO A 280 ? 0.7811 1.2156 1.5505 0.0137  0.0544  -0.4977 259 PRO A C   
1868 O O   . PRO A 280 ? 0.7454 1.2105 1.5324 0.0073  0.0696  -0.5198 259 PRO A O   
1869 C CB  . PRO A 280 ? 0.7677 1.1694 1.5621 0.0573  0.0133  -0.5005 259 PRO A CB  
1870 C CG  . PRO A 280 ? 0.9711 1.3281 1.7431 0.0701  -0.0063 -0.4763 259 PRO A CG  
1871 C CD  . PRO A 280 ? 0.7887 1.1252 1.5208 0.0528  0.0012  -0.4477 259 PRO A CD  
1872 N N   . GLU A 281 ? 0.8498 1.2825 1.6074 0.0043  0.0547  -0.4828 260 GLU A N   
1873 C CA  . GLU A 281 ? 0.7962 1.2606 1.5588 -0.0163 0.0741  -0.4902 260 GLU A CA  
1874 C C   . GLU A 281 ? 0.7689 1.2320 1.5035 -0.0370 0.0961  -0.4848 260 GLU A C   
1875 O O   . GLU A 281 ? 0.7495 1.2451 1.4962 -0.0506 0.1151  -0.5016 260 GLU A O   
1876 C CB  . GLU A 281 ? 0.8035 1.2599 1.5541 -0.0225 0.0688  -0.4727 260 GLU A CB  
1877 C CG  . GLU A 281 ? 0.8284 1.2730 1.5931 -0.0013 0.0440  -0.4693 260 GLU A CG  
1878 C CD  . GLU A 281 ? 0.8400 1.2785 1.5922 -0.0082 0.0398  -0.4534 260 GLU A CD  
1879 O OE1 . GLU A 281 ? 0.7662 1.2106 1.5010 -0.0298 0.0563  -0.4461 260 GLU A OE1 
1880 O OE2 . GLU A 281 ? 0.9131 1.3399 1.6720 0.0082  0.0196  -0.4482 260 GLU A OE2 
1881 N N   . LEU A 282 ? 1.0402 1.4662 1.7367 -0.0397 0.0939  -0.4612 261 LEU A N   
1882 C CA  . LEU A 282 ? 1.1159 1.5376 1.7832 -0.0580 0.1130  -0.4551 261 LEU A CA  
1883 C C   . LEU A 282 ? 0.9780 1.4124 1.6581 -0.0536 0.1199  -0.4756 261 LEU A C   
1884 O O   . LEU A 282 ? 0.8889 1.3390 1.5596 -0.0693 0.1399  -0.4827 261 LEU A O   
1885 C CB  . LEU A 282 ? 0.8046 1.1840 1.4297 -0.0608 0.1071  -0.4247 261 LEU A CB  
1886 C CG  . LEU A 282 ? 0.8314 1.1962 1.4378 -0.0667 0.1020  -0.4027 261 LEU A CG  
1887 C CD1 . LEU A 282 ? 0.9017 1.2250 1.4708 -0.0650 0.0935  -0.3747 261 LEU A CD1 
1888 C CD2 . LEU A 282 ? 0.8419 1.2263 1.4392 -0.0895 0.1215  -0.4029 261 LEU A CD2 
1889 N N   . GLU A 283 ? 0.8688 1.2951 1.5685 -0.0322 0.1035  -0.4850 262 GLU A N   
1890 C CA  . GLU A 283 ? 0.8323 1.2742 1.5495 -0.0260 0.1090  -0.5085 262 GLU A CA  
1891 C C   . GLU A 283 ? 0.8263 1.3163 1.5752 -0.0325 0.1245  -0.5361 262 GLU A C   
1892 O O   . GLU A 283 ? 0.8548 1.3638 1.6069 -0.0385 0.1397  -0.5527 262 GLU A O   
1893 C CB  . GLU A 283 ? 0.8121 1.2379 1.5490 -0.0006 0.0867  -0.5151 262 GLU A CB  
1894 C CG  . GLU A 283 ? 0.7747 1.1561 1.4825 0.0050  0.0755  -0.4941 262 GLU A CG  
1895 C CD  . GLU A 283 ? 0.8209 1.1853 1.5487 0.0297  0.0531  -0.5001 262 GLU A CD  
1896 O OE1 . GLU A 283 ? 0.8115 1.1860 1.5659 0.0434  0.0403  -0.5080 262 GLU A OE1 
1897 O OE2 . GLU A 283 ? 0.7821 1.1225 1.4991 0.0355  0.0478  -0.4973 262 GLU A OE2 
1898 N N   . GLN A 284 ? 0.8541 1.3653 1.6270 -0.0313 0.1210  -0.5418 263 GLN A N   
1899 C CA  . GLN A 284 ? 0.9043 1.4633 1.7099 -0.0383 0.1357  -0.5676 263 GLN A CA  
1900 C C   . GLN A 284 ? 0.8861 1.4593 1.6712 -0.0658 0.1595  -0.5606 263 GLN A C   
1901 O O   . GLN A 284 ? 0.9021 1.5121 1.7037 -0.0765 0.1783  -0.5807 263 GLN A O   
1902 C CB  . GLN A 284 ? 0.9054 1.4814 1.7469 -0.0254 0.1209  -0.5772 263 GLN A CB  
1903 C CG  . GLN A 284 ? 0.9469 1.5743 1.8321 -0.0261 0.1313  -0.6086 263 GLN A CG  
1904 C CD  . GLN A 284 ? 0.9919 1.6333 1.9140 -0.0092 0.1128  -0.6192 263 GLN A CD  
1905 O OE1 . GLN A 284 ? 1.0446 1.6653 1.9748 0.0134  0.0903  -0.6182 263 GLN A OE1 
1906 N NE2 . GLN A 284 ? 0.9758 1.6449 1.9124 -0.0211 0.1201  -0.6262 263 GLN A NE2 
1907 N N   . HIS A 285 ? 0.7518 1.2962 1.5009 -0.0773 0.1589  -0.5325 264 HIS A N   
1908 C CA  . HIS A 285 ? 0.7164 1.2678 1.4411 -0.1032 0.1800  -0.5230 264 HIS A CA  
1909 C C   . HIS A 285 ? 0.6948 1.2395 1.3910 -0.1144 0.1963  -0.5212 264 HIS A C   
1910 O O   . HIS A 285 ? 0.6729 1.2361 1.3587 -0.1347 0.2179  -0.5241 264 HIS A O   
1911 C CB  . HIS A 285 ? 0.7022 1.2230 1.3975 -0.1097 0.1721  -0.4937 264 HIS A CB  
1912 C CG  . HIS A 285 ? 0.6814 1.1998 1.3446 -0.1352 0.1914  -0.4798 264 HIS A CG  
1913 N ND1 . HIS A 285 ? 0.6101 1.1532 1.2833 -0.1514 0.2034  -0.4841 264 HIS A ND1 
1914 C CD2 . HIS A 285 ? 0.6968 1.1902 1.3179 -0.1470 0.2000  -0.4615 264 HIS A CD2 
1915 C CE1 . HIS A 285 ? 0.6261 1.1580 1.2636 -0.1722 0.2187  -0.4685 264 HIS A CE1 
1916 N NE2 . HIS A 285 ? 0.6281 1.1302 1.2334 -0.1695 0.2167  -0.4548 264 HIS A NE2 
1917 N N   . PHE A 286 ? 0.7397 1.2579 1.4228 -0.1017 0.1861  -0.5165 265 PHE A N   
1918 C CA  . PHE A 286 ? 0.6864 1.1946 1.3413 -0.1102 0.1986  -0.5143 265 PHE A CA  
1919 C C   . PHE A 286 ? 0.9640 1.4934 1.6431 -0.0994 0.2020  -0.5419 265 PHE A C   
1920 O O   . PHE A 286 ? 0.9434 1.4606 1.6017 -0.1011 0.2073  -0.5417 265 PHE A O   
1921 C CB  . PHE A 286 ? 0.7278 1.1893 1.3472 -0.1057 0.1855  -0.4880 265 PHE A CB  
1922 C CG  . PHE A 286 ? 0.7344 1.1750 1.3196 -0.1208 0.1883  -0.4605 265 PHE A CG  
1923 C CD1 . PHE A 286 ? 0.7164 1.1575 1.2707 -0.1418 0.2075  -0.4527 265 PHE A CD1 
1924 C CD2 . PHE A 286 ? 0.7958 1.2160 1.3788 -0.1135 0.1716  -0.4429 265 PHE A CD2 
1925 C CE1 . PHE A 286 ? 0.6449 1.0659 1.1676 -0.1549 0.2094  -0.4280 265 PHE A CE1 
1926 C CE2 . PHE A 286 ? 0.7845 1.1857 1.3362 -0.1266 0.1740  -0.4188 265 PHE A CE2 
1927 C CZ  . PHE A 286 ? 0.6397 1.0412 1.1618 -0.1472 0.1926  -0.4114 265 PHE A CZ  
1928 N N   . GLU A 287 ? 0.7815 1.3420 1.5042 -0.0877 0.1981  -0.5660 266 GLU A N   
1929 C CA  . GLU A 287 ? 0.7607 1.3469 1.5087 -0.0783 0.2035  -0.5950 266 GLU A CA  
1930 C C   . GLU A 287 ? 0.8008 1.4116 1.5351 -0.0987 0.2309  -0.6042 266 GLU A C   
1931 O O   . GLU A 287 ? 0.8101 1.4497 1.5521 -0.1144 0.2466  -0.6089 266 GLU A O   
1932 C CB  . GLU A 287 ? 0.8081 1.4275 1.6065 -0.0637 0.1959  -0.6195 266 GLU A CB  
1933 C CG  . GLU A 287 ? 0.8383 1.4378 1.6560 -0.0366 0.1694  -0.6230 266 GLU A CG  
1934 C CD  . GLU A 287 ? 0.8040 1.4259 1.6630 -0.0237 0.1571  -0.6361 266 GLU A CD  
1935 O OE1 . GLU A 287 ? 0.6874 1.3439 1.5633 -0.0345 0.1687  -0.6484 266 GLU A OE1 
1936 O OE2 . GLU A 287 ? 0.8262 1.4252 1.6941 -0.0039 0.1335  -0.6306 266 GLU A OE2 
1937 N N   . GLY A 288 ? 0.8023 1.4011 1.5151 -0.0989 0.2363  -0.6061 267 GLY A N   
1938 C CA  . GLY A 288 ? 0.7357 1.3541 1.4306 -0.1173 0.2615  -0.6135 267 GLY A CA  
1939 C C   . GLY A 288 ? 0.8445 1.4399 1.4921 -0.1386 0.2722  -0.5865 267 GLY A C   
1940 O O   . GLY A 288 ? 0.7734 1.3807 1.4003 -0.1544 0.2927  -0.5899 267 GLY A O   
1941 N N   . LYS A 289 ? 0.7688 1.3312 1.3976 -0.1391 0.2587  -0.5597 268 LYS A N   
1942 C CA  . LYS A 289 ? 0.7241 1.2611 1.3073 -0.1572 0.2662  -0.5331 268 LYS A CA  
1943 C C   . LYS A 289 ? 0.7809 1.2816 1.3329 -0.1516 0.2579  -0.5205 268 LYS A C   
1944 O O   . LYS A 289 ? 0.7213 1.2081 1.2863 -0.1328 0.2412  -0.5256 268 LYS A O   
1945 C CB  . LYS A 289 ? 0.7465 1.2670 1.3247 -0.1605 0.2561  -0.5112 268 LYS A CB  
1946 N N   . MET A 290 ? 0.7135 1.1988 1.2242 -0.1684 0.2695  -0.5037 269 MET A N   
1947 C CA  . MET A 290 ? 0.7102 1.1636 1.1893 -0.1658 0.2637  -0.4919 269 MET A CA  
1948 C C   . MET A 290 ? 0.7062 1.1205 1.1657 -0.1621 0.2461  -0.4632 269 MET A C   
1949 O O   . MET A 290 ? 0.6677 1.0792 1.1354 -0.1618 0.2390  -0.4524 269 MET A O   
1950 C CB  . MET A 290 ? 0.7524 1.2093 1.1961 -0.1848 0.2845  -0.4894 269 MET A CB  
1951 C CG  . MET A 290 ? 0.8144 1.2585 1.2253 -0.2038 0.2926  -0.4650 269 MET A CG  
1952 S SD  . MET A 290 ? 1.1583 1.6044 1.5255 -0.2251 0.3162  -0.4620 269 MET A SD  
1953 C CE  . MET A 290 ? 0.8010 1.2144 1.1277 -0.2394 0.3139  -0.4270 269 MET A CE  
1954 N N   . TYR A 291 ? 0.7544 1.1387 1.1877 -0.1590 0.2388  -0.4512 270 TYR A N   
1955 C CA  . TYR A 291 ? 0.7699 1.1179 1.1834 -0.1558 0.2231  -0.4239 270 TYR A CA  
1956 C C   . TYR A 291 ? 0.7499 1.0890 1.1312 -0.1738 0.2322  -0.4021 270 TYR A C   
1957 O O   . TYR A 291 ? 0.6905 1.0116 1.0659 -0.1723 0.2216  -0.3828 270 TYR A O   
1958 C CB  . TYR A 291 ? 0.7297 1.0500 1.1255 -0.1486 0.2136  -0.4179 270 TYR A CB  
1959 C CG  . TYR A 291 ? 0.7696 1.0892 1.1957 -0.1288 0.1995  -0.4346 270 TYR A CG  
1960 C CD1 . TYR A 291 ? 0.7551 1.0864 1.2179 -0.1151 0.1891  -0.4449 270 TYR A CD1 
1961 C CD2 . TYR A 291 ? 0.6927 0.9990 1.1103 -0.1235 0.1959  -0.4404 270 TYR A CD2 
1962 C CE1 . TYR A 291 ? 0.6873 1.0160 1.1768 -0.0965 0.1755  -0.4599 270 TYR A CE1 
1963 C CE2 . TYR A 291 ? 0.7918 1.0954 1.2367 -0.1054 0.1825  -0.4557 270 TYR A CE2 
1964 C CZ  . TYR A 291 ? 0.7250 1.0393 1.2053 -0.0918 0.1723  -0.4652 270 TYR A CZ  
1965 O OH  . TYR A 291 ? 0.7923 1.1022 1.2992 -0.0732 0.1582  -0.4802 270 TYR A OH  
1966 N N   . GLY A 292 ? 0.7377 1.0883 1.0967 -0.1906 0.2516  -0.4048 271 GLY A N   
1967 C CA  . GLY A 292 ? 0.6924 1.0340 1.0202 -0.2081 0.2606  -0.3849 271 GLY A CA  
1968 C C   . GLY A 292 ? 0.7782 1.1344 1.1241 -0.2127 0.2621  -0.3833 271 GLY A C   
1969 O O   . GLY A 292 ? 0.8182 1.1581 1.1437 -0.2208 0.2604  -0.3627 271 GLY A O   
1970 N N   . HIS A 293 ? 0.7195 1.1073 1.1043 -0.2076 0.2652  -0.4058 272 HIS A N   
1971 C CA  . HIS A 293 ? 0.6810 1.0832 1.0878 -0.2098 0.2638  -0.4059 272 HIS A CA  
1972 C C   . HIS A 293 ? 0.7033 1.0808 1.1152 -0.1959 0.2415  -0.3899 272 HIS A C   
1973 O O   . HIS A 293 ? 0.6749 1.0451 1.0802 -0.2017 0.2386  -0.3753 272 HIS A O   
1974 C CB  . HIS A 293 ? 0.7006 1.1426 1.1511 -0.2048 0.2698  -0.4348 272 HIS A CB  
1975 C CG  . HIS A 293 ? 0.8341 1.3043 1.2817 -0.2190 0.2932  -0.4515 272 HIS A CG  
1976 N ND1 . HIS A 293 ? 0.8357 1.3420 1.3187 -0.2136 0.3005  -0.4800 272 HIS A ND1 
1977 C CD2 . HIS A 293 ? 0.8987 1.3663 1.3113 -0.2380 0.3110  -0.4437 272 HIS A CD2 
1978 C CE1 . HIS A 293 ? 0.7813 1.3071 1.2512 -0.2291 0.3226  -0.4890 272 HIS A CE1 
1979 N NE2 . HIS A 293 ? 0.8170 1.3191 1.2436 -0.2442 0.3293  -0.4670 272 HIS A NE2 
1980 N N   . LEU A 294 ? 0.6800 1.0438 1.1031 -0.1774 0.2255  -0.3924 273 LEU A N   
1981 C CA  . LEU A 294 ? 0.6779 1.0178 1.1051 -0.1634 0.2043  -0.3771 273 LEU A CA  
1982 C C   . LEU A 294 ? 0.6720 0.9782 1.0590 -0.1701 0.2003  -0.3482 273 LEU A C   
1983 O O   . LEU A 294 ? 0.5874 0.8794 0.9710 -0.1669 0.1896  -0.3323 273 LEU A O   
1984 C CB  . LEU A 294 ? 0.6687 1.0010 1.1160 -0.1431 0.1892  -0.3868 273 LEU A CB  
1985 C CG  . LEU A 294 ? 0.6547 0.9619 1.1080 -0.1265 0.1666  -0.3727 273 LEU A CG  
1986 C CD1 . LEU A 294 ? 0.6285 0.9391 1.0903 -0.1266 0.1609  -0.3644 273 LEU A CD1 
1987 C CD2 . LEU A 294 ? 0.7466 1.0595 1.2324 -0.1073 0.1550  -0.3914 273 LEU A CD2 
1988 N N   . LYS A 295 ? 0.5829 0.8765 0.9390 -0.1788 0.2085  -0.3415 274 LYS A N   
1989 C CA  . LYS A 295 ? 0.6041 0.8675 0.9220 -0.1854 0.2053  -0.3149 274 LYS A CA  
1990 C C   . LYS A 295 ? 0.6617 0.9281 0.9637 -0.2010 0.2146  -0.3039 274 LYS A C   
1991 O O   . LYS A 295 ? 0.5503 0.7945 0.8330 -0.2016 0.2066  -0.2825 274 LYS A O   
1992 C CB  . LYS A 295 ? 0.6467 0.8984 0.9364 -0.1913 0.2122  -0.3123 274 LYS A CB  
1993 C CG  . LYS A 295 ? 0.6329 0.8695 0.9296 -0.1762 0.1988  -0.3148 274 LYS A CG  
1994 C CD  . LYS A 295 ? 0.6772 0.9028 0.9453 -0.1829 0.2054  -0.3124 274 LYS A CD  
1995 C CE  . LYS A 295 ? 0.6812 0.8896 0.9558 -0.1688 0.1913  -0.3137 274 LYS A CE  
1996 N NZ  . LYS A 295 ? 0.7077 0.9050 0.9540 -0.1756 0.1968  -0.3113 274 LYS A NZ  
1997 N N   . GLY A 296 ? 0.6482 0.9415 0.9574 -0.2140 0.2319  -0.3181 275 GLY A N   
1998 C CA  . GLY A 296 ? 0.7280 1.0254 1.0268 -0.2289 0.2403  -0.3095 275 GLY A CA  
1999 C C   . GLY A 296 ? 0.5982 0.8989 0.9214 -0.2210 0.2280  -0.3076 275 GLY A C   
2000 O O   . GLY A 296 ? 0.5320 0.8215 0.8401 -0.2283 0.2267  -0.2922 275 GLY A O   
2001 N N   . GLU A 297 ? 0.5593 0.8749 0.9200 -0.2053 0.2184  -0.3237 276 GLU A N   
2002 C CA  . GLU A 297 ? 0.5334 0.8529 0.9185 -0.1961 0.2054  -0.3234 276 GLU A CA  
2003 C C   . GLU A 297 ? 0.5388 0.8248 0.9074 -0.1844 0.1866  -0.3010 276 GLU A C   
2004 O O   . GLU A 297 ? 0.5225 0.8010 0.8881 -0.1848 0.1796  -0.2894 276 GLU A O   
2005 C CB  . GLU A 297 ? 0.5288 0.8741 0.9582 -0.1820 0.2003  -0.3481 276 GLU A CB  
2006 C CG  . GLU A 297 ? 0.5859 0.9415 1.0441 -0.1735 0.1885  -0.3519 276 GLU A CG  
2007 C CD  . GLU A 297 ? 0.6437 1.0395 1.1431 -0.1735 0.1959  -0.3794 276 GLU A CD  
2008 O OE1 . GLU A 297 ? 0.6157 1.0336 1.1176 -0.1851 0.2141  -0.3937 276 GLU A OE1 
2009 O OE2 . GLU A 297 ? 0.6951 1.1012 1.2244 -0.1615 0.1834  -0.3870 276 GLU A OE2 
2010 N N   . VAL A 298 ? 0.5718 0.8379 0.9300 -0.1742 0.1783  -0.2948 277 VAL A N   
2011 C CA  . VAL A 298 ? 0.6007 0.8355 0.9418 -0.1642 0.1619  -0.2727 277 VAL A CA  
2012 C C   . VAL A 298 ? 0.5098 0.7253 0.8122 -0.1775 0.1669  -0.2506 277 VAL A C   
2013 O O   . VAL A 298 ? 0.4966 0.6964 0.7895 -0.1740 0.1569  -0.2344 277 VAL A O   
2014 C CB  . VAL A 298 ? 0.6889 0.9077 1.0282 -0.1521 0.1533  -0.2718 277 VAL A CB  
2015 C CG1 . VAL A 298 ? 0.5326 0.7178 0.8451 -0.1471 0.1412  -0.2460 277 VAL A CG1 
2016 C CG2 . VAL A 298 ? 0.6817 0.9121 1.0590 -0.1347 0.1422  -0.2891 277 VAL A CG2 
2017 N N   . ALA A 299 ? 0.5428 0.7588 0.8216 -0.1923 0.1820  -0.2499 278 ALA A N   
2018 C CA  . ALA A 299 ? 0.6304 0.8265 0.8709 -0.2043 0.1863  -0.2290 278 ALA A CA  
2019 C C   . ALA A 299 ? 0.5924 0.7944 0.8330 -0.2132 0.1892  -0.2249 278 ALA A C   
2020 O O   . ALA A 299 ? 0.5634 0.7449 0.7821 -0.2142 0.1828  -0.2057 278 ALA A O   
2021 C CB  . ALA A 299 ? 0.6473 0.8447 0.8635 -0.2184 0.2022  -0.2311 278 ALA A CB  
2022 N N   . GLU A 300 ? 0.6044 0.8348 0.8703 -0.2197 0.1987  -0.2433 279 GLU A N   
2023 C CA  . GLU A 300 ? 0.6427 0.8801 0.9117 -0.2290 0.2015  -0.2411 279 GLU A CA  
2024 C C   . GLU A 300 ? 0.6478 0.8773 0.9317 -0.2143 0.1829  -0.2347 279 GLU A C   
2025 O O   . GLU A 300 ? 0.6213 0.8366 0.8889 -0.2180 0.1784  -0.2199 279 GLU A O   
2026 C CB  . GLU A 300 ? 0.5242 0.7966 0.8207 -0.2391 0.2160  -0.2637 279 GLU A CB  
2027 N N   . ALA A 301 ? 0.5463 0.7842 0.8602 -0.1972 0.1714  -0.2459 280 ALA A N   
2028 C CA  . ALA A 301 ? 0.5378 0.7690 0.8662 -0.1823 0.1534  -0.2409 280 ALA A CA  
2029 C C   . ALA A 301 ? 0.5442 0.7418 0.8425 -0.1750 0.1414  -0.2161 280 ALA A C   
2030 O O   . ALA A 301 ? 0.5408 0.7269 0.8292 -0.1739 0.1337  -0.2036 280 ALA A O   
2031 C CB  . ALA A 301 ? 0.4840 0.7298 0.8491 -0.1650 0.1438  -0.2582 280 ALA A CB  
2032 N N   . VAL A 302 ? 0.5470 0.7292 0.8307 -0.1701 0.1397  -0.2094 281 VAL A N   
2033 C CA  . VAL A 302 ? 0.5781 0.7300 0.8328 -0.1646 0.1300  -0.1860 281 VAL A CA  
2034 C C   . VAL A 302 ? 0.5764 0.7164 0.7992 -0.1784 0.1365  -0.1705 281 VAL A C   
2035 O O   . VAL A 302 ? 0.5208 0.6434 0.7288 -0.1736 0.1267  -0.1541 281 VAL A O   
2036 C CB  . VAL A 302 ? 0.5818 0.7222 0.8258 -0.1614 0.1306  -0.1833 281 VAL A CB  
2037 C CG1 . VAL A 302 ? 0.6444 0.7569 0.8521 -0.1630 0.1270  -0.1593 281 VAL A CG1 
2038 C CG2 . VAL A 302 ? 0.5155 0.6569 0.7862 -0.1435 0.1180  -0.1916 281 VAL A CG2 
2039 N N   . SER A 303 ? 0.5441 0.6930 0.7553 -0.1956 0.1530  -0.1757 282 SER A N   
2040 C CA  . SER A 303 ? 0.5512 0.6866 0.7298 -0.2093 0.1595  -0.1609 282 SER A CA  
2041 C C   . SER A 303 ? 0.6229 0.7607 0.8082 -0.2106 0.1547  -0.1586 282 SER A C   
2042 O O   . SER A 303 ? 0.6261 0.7441 0.7867 -0.2119 0.1498  -0.1414 282 SER A O   
2043 C CB  . SER A 303 ? 0.6715 0.8175 0.8384 -0.2275 0.1786  -0.1686 282 SER A CB  
2044 O OG  . SER A 303 ? 0.7770 0.9084 0.9115 -0.2409 0.1846  -0.1543 282 SER A OG  
2045 N N   . GLY A 304 ? 0.5628 0.7250 0.7819 -0.2099 0.1556  -0.1765 283 GLY A N   
2046 C CA  . GLY A 304 ? 0.6141 0.7799 0.8423 -0.2108 0.1501  -0.1761 283 GLY A CA  
2047 C C   . GLY A 304 ? 0.6047 0.7528 0.8305 -0.1935 0.1309  -0.1633 283 GLY A C   
2048 O O   . GLY A 304 ? 0.5665 0.7025 0.7781 -0.1951 0.1255  -0.1520 283 GLY A O   
2049 N N   . MET A 305 ? 0.5595 0.7053 0.7986 -0.1767 0.1202  -0.1648 284 MET A N   
2050 C CA  . MET A 305 ? 0.5994 0.7276 0.8345 -0.1599 0.1024  -0.1517 284 MET A CA  
2051 C C   . MET A 305 ? 0.5886 0.6891 0.7844 -0.1616 0.1005  -0.1282 284 MET A C   
2052 O O   . MET A 305 ? 0.5536 0.6406 0.7377 -0.1555 0.0904  -0.1158 284 MET A O   
2053 C CB  . MET A 305 ? 0.5946 0.7240 0.8497 -0.1429 0.0926  -0.1573 284 MET A CB  
2054 C CG  . MET A 305 ? 0.6293 0.7401 0.8794 -0.1253 0.0746  -0.1431 284 MET A CG  
2055 S SD  . MET A 305 ? 0.6687 0.7835 0.9489 -0.1049 0.0616  -0.1529 284 MET A SD  
2056 C CE  . MET A 305 ? 0.5631 0.6548 0.8194 -0.1028 0.0621  -0.1374 284 MET A CE  
2057 N N   . LEU A 306 ? 0.5893 0.6815 0.7645 -0.1693 0.1097  -0.1226 285 LEU A N   
2058 C CA  . LEU A 306 ? 0.5726 0.6400 0.7118 -0.1704 0.1078  -0.1012 285 LEU A CA  
2059 C C   . LEU A 306 ? 0.6294 0.6899 0.7454 -0.1837 0.1138  -0.0934 285 LEU A C   
2060 O O   . LEU A 306 ? 0.6178 0.6577 0.7067 -0.1815 0.1085  -0.0756 285 LEU A O   
2061 C CB  . LEU A 306 ? 0.5063 0.5678 0.6313 -0.1747 0.1153  -0.0987 285 LEU A CB  
2062 C CG  . LEU A 306 ? 0.6887 0.7409 0.8188 -0.1602 0.1053  -0.0937 285 LEU A CG  
2063 C CD1 . LEU A 306 ? 0.7436 0.8126 0.9100 -0.1507 0.1013  -0.1115 285 LEU A CD1 
2064 C CD2 . LEU A 306 ? 0.6264 0.6690 0.7355 -0.1664 0.1123  -0.0878 285 LEU A CD2 
2065 N N   . THR A 307 ? 0.5808 0.6576 0.7066 -0.1975 0.1248  -0.1061 286 THR A N   
2066 C CA  . THR A 307 ? 0.6058 0.6740 0.7091 -0.2111 0.1305  -0.0985 286 THR A CA  
2067 C C   . THR A 307 ? 0.6244 0.6884 0.7326 -0.2046 0.1188  -0.0946 286 THR A C   
2068 O O   . THR A 307 ? 0.6356 0.6821 0.7178 -0.2087 0.1168  -0.0812 286 THR A O   
2069 C CB  . THR A 307 ? 0.6700 0.7564 0.7806 -0.2298 0.1475  -0.1126 286 THR A CB  
2070 O OG1 . THR A 307 ? 0.6819 0.7951 0.8320 -0.2272 0.1480  -0.1326 286 THR A OG1 
2071 C CG2 . THR A 307 ? 0.6591 0.7441 0.7535 -0.2379 0.1596  -0.1126 286 THR A CG2 
2072 N N   . GLU A 308 ? 0.5921 0.6713 0.7325 -0.1938 0.1101  -0.1063 287 GLU A N   
2073 C CA  . GLU A 308 ? 0.6388 0.7127 0.7827 -0.1850 0.0968  -0.1022 287 GLU A CA  
2074 C C   . GLU A 308 ? 0.5864 0.6374 0.7095 -0.1694 0.0835  -0.0836 287 GLU A C   
2075 O O   . GLU A 308 ? 0.5242 0.5601 0.6285 -0.1672 0.0766  -0.0719 287 GLU A O   
2076 C CB  . GLU A 308 ? 0.6400 0.7365 0.8238 -0.1766 0.0902  -0.1201 287 GLU A CB  
2077 C CG  . GLU A 308 ? 0.7307 0.8266 0.9210 -0.1719 0.0789  -0.1201 287 GLU A CG  
2078 C CD  . GLU A 308 ? 0.7720 0.8741 0.9865 -0.1517 0.0628  -0.1257 287 GLU A CD  
2079 O OE1 . GLU A 308 ? 1.1001 1.2229 1.3459 -0.1477 0.0635  -0.1422 287 GLU A OE1 
2080 O OE2 . GLU A 308 ? 0.7689 0.8550 0.9704 -0.1392 0.0492  -0.1136 287 GLU A OE2 
2081 N N   . LEU A 309 ? 0.5277 0.5760 0.6543 -0.1586 0.0799  -0.0810 288 LEU A N   
2082 C CA  . LEU A 309 ? 0.6260 0.6539 0.7338 -0.1446 0.0685  -0.0631 288 LEU A CA  
2083 C C   . LEU A 309 ? 0.5081 0.5162 0.5784 -0.1522 0.0731  -0.0459 288 LEU A C   
2084 O O   . LEU A 309 ? 0.4888 0.4809 0.5399 -0.1445 0.0643  -0.0314 288 LEU A O   
2085 C CB  . LEU A 309 ? 0.6201 0.6490 0.7399 -0.1341 0.0653  -0.0643 288 LEU A CB  
2086 C CG  . LEU A 309 ? 0.6792 0.7090 0.8185 -0.1153 0.0502  -0.0655 288 LEU A CG  
2087 C CD1 . LEU A 309 ? 0.7008 0.7497 0.8694 -0.1134 0.0466  -0.0826 288 LEU A CD1 
2088 C CD2 . LEU A 309 ? 0.6431 0.6732 0.7943 -0.1076 0.0488  -0.0679 288 LEU A CD2 
2089 N N   . GLN A 310 ? 0.5395 0.5486 0.5985 -0.1665 0.0866  -0.0477 289 GLN A N   
2090 C CA  . GLN A 310 ? 0.5618 0.5522 0.5850 -0.1733 0.0905  -0.0320 289 GLN A CA  
2091 C C   . GLN A 310 ? 0.5362 0.5188 0.5436 -0.1811 0.0908  -0.0277 289 GLN A C   
2092 O O   . GLN A 310 ? 0.5078 0.4716 0.4862 -0.1803 0.0878  -0.0124 289 GLN A O   
2093 C CB  . GLN A 310 ? 0.5192 0.5127 0.5339 -0.1863 0.1044  -0.0359 289 GLN A CB  
2094 C CG  . GLN A 310 ? 0.6337 0.6289 0.6562 -0.1788 0.1034  -0.0367 289 GLN A CG  
2095 C CD  . GLN A 310 ? 0.7678 0.7708 0.7879 -0.1915 0.1172  -0.0454 289 GLN A CD  
2096 O OE1 . GLN A 310 ? 0.8027 0.8037 0.8048 -0.2059 0.1275  -0.0451 289 GLN A OE1 
2097 N NE2 . GLN A 310 ? 0.7868 0.7979 0.8243 -0.1860 0.1172  -0.0536 289 GLN A NE2 
2098 N N   . GLU A 311 ? 0.5136 0.5106 0.5401 -0.1888 0.0942  -0.0413 290 GLU A N   
2099 C CA  . GLU A 311 ? 0.5342 0.5233 0.5481 -0.1962 0.0933  -0.0380 290 GLU A CA  
2100 C C   . GLU A 311 ? 0.5579 0.5343 0.5649 -0.1806 0.0775  -0.0276 290 GLU A C   
2101 O O   . GLU A 311 ? 0.5594 0.5175 0.5393 -0.1816 0.0743  -0.0152 290 GLU A O   
2102 C CB  . GLU A 311 ? 0.6010 0.6106 0.6417 -0.2072 0.0996  -0.0560 290 GLU A CB  
2103 C CG  . GLU A 311 ? 0.7075 0.7092 0.7342 -0.2209 0.1031  -0.0540 290 GLU A CG  
2104 C CD  . GLU A 311 ? 0.8099 0.8015 0.8341 -0.2103 0.0882  -0.0485 290 GLU A CD  
2105 O OE1 . GLU A 311 ? 0.7484 0.7509 0.7970 -0.1968 0.0777  -0.0554 290 GLU A OE1 
2106 O OE2 . GLU A 311 ? 0.8745 0.8467 0.8717 -0.2148 0.0866  -0.0374 290 GLU A OE2 
2107 N N   . ARG A 312 ? 0.5718 0.5572 0.6019 -0.1655 0.0671  -0.0325 291 ARG A N   
2108 C CA  . ARG A 312 ? 0.4972 0.4710 0.5198 -0.1494 0.0519  -0.0224 291 ARG A CA  
2109 C C   . ARG A 312 ? 0.4929 0.4479 0.4873 -0.1413 0.0487  -0.0036 291 ARG A C   
2110 O O   . ARG A 312 ? 0.5025 0.4424 0.4759 -0.1345 0.0409  0.0085  291 ARG A O   
2111 C CB  . ARG A 312 ? 0.4869 0.4742 0.5399 -0.1348 0.0418  -0.0319 291 ARG A CB  
2112 C CG  . ARG A 312 ? 0.5314 0.5409 0.6168 -0.1413 0.0444  -0.0521 291 ARG A CG  
2113 C CD  . ARG A 312 ? 0.4876 0.5082 0.6007 -0.1245 0.0320  -0.0603 291 ARG A CD  
2114 N NE  . ARG A 312 ? 0.5817 0.5895 0.6835 -0.1098 0.0169  -0.0503 291 ARG A NE  
2115 C CZ  . ARG A 312 ? 0.5149 0.5238 0.6289 -0.0918 0.0038  -0.0502 291 ARG A CZ  
2116 N NH1 . ARG A 312 ? 0.6160 0.6371 0.7545 -0.0854 0.0029  -0.0594 291 ARG A NH1 
2117 N NH2 . ARG A 312 ? 0.5547 0.5516 0.6549 -0.0794 -0.0089 -0.0407 291 ARG A NH2 
2118 N N   . TYR A 313 ? 0.4907 0.4469 0.4849 -0.1418 0.0544  -0.0016 292 TYR A N   
2119 C CA  . TYR A 313 ? 0.4863 0.4269 0.4572 -0.1343 0.0513  0.0154  292 TYR A CA  
2120 C C   . TYR A 313 ? 0.4947 0.4192 0.4324 -0.1422 0.0550  0.0271  292 TYR A C   
2121 O O   . TYR A 313 ? 0.4956 0.4062 0.4131 -0.1331 0.0475  0.0411  292 TYR A O   
2122 C CB  . TYR A 313 ? 0.4814 0.4270 0.4596 -0.1358 0.0575  0.0134  292 TYR A CB  
2123 C CG  . TYR A 313 ? 0.4808 0.4115 0.4342 -0.1322 0.0568  0.0301  292 TYR A CG  
2124 C CD1 . TYR A 313 ? 0.4758 0.3997 0.4277 -0.1170 0.0468  0.0413  292 TYR A CD1 
2125 C CD2 . TYR A 313 ? 0.4864 0.4101 0.4177 -0.1441 0.0660  0.0348  292 TYR A CD2 
2126 C CE1 . TYR A 313 ? 0.4752 0.3875 0.4065 -0.1143 0.0464  0.0561  292 TYR A CE1 
2127 C CE2 . TYR A 313 ? 0.4879 0.3994 0.3981 -0.1405 0.0647  0.0492  292 TYR A CE2 
2128 C CZ  . TYR A 313 ? 0.4972 0.4039 0.4085 -0.1259 0.0551  0.0595  292 TYR A CZ  
2129 O OH  . TYR A 313 ? 0.4840 0.3807 0.3763 -0.1228 0.0542  0.0735  292 TYR A OH  
2130 N N   . HIS A 314 ? 0.5023 0.4282 0.4331 -0.1590 0.0667  0.0217  293 HIS A N   
2131 C CA  . HIS A 314 ? 0.5367 0.4455 0.4346 -0.1666 0.0700  0.0328  293 HIS A CA  
2132 C C   . HIS A 314 ? 0.5803 0.4791 0.4677 -0.1635 0.0620  0.0368  293 HIS A C   
2133 O O   . HIS A 314 ? 0.5846 0.4662 0.4440 -0.1614 0.0588  0.0497  293 HIS A O   
2134 C CB  . HIS A 314 ? 0.5446 0.4566 0.4372 -0.1855 0.0843  0.0258  293 HIS A CB  
2135 C CG  . HIS A 314 ? 0.5955 0.5116 0.4873 -0.1885 0.0918  0.0254  293 HIS A CG  
2136 N ND1 . HIS A 314 ? 0.6287 0.5608 0.5386 -0.1983 0.1023  0.0112  293 HIS A ND1 
2137 C CD2 . HIS A 314 ? 0.6071 0.5139 0.4827 -0.1827 0.0900  0.0367  293 HIS A CD2 
2138 C CE1 . HIS A 314 ? 0.6673 0.5987 0.5713 -0.1982 0.1062  0.0138  293 HIS A CE1 
2139 N NE2 . HIS A 314 ? 0.6439 0.5601 0.5277 -0.1891 0.0988  0.0292  293 HIS A NE2 
2140 N N   . ARG A 315 ? 0.5463 0.4558 0.4561 -0.1628 0.0582  0.0255  294 ARG A N   
2141 C CA  . ARG A 315 ? 0.5401 0.4406 0.4420 -0.1587 0.0491  0.0281  294 ARG A CA  
2142 C C   . ARG A 315 ? 0.5500 0.4409 0.4414 -0.1393 0.0361  0.0403  294 ARG A C   
2143 O O   . ARG A 315 ? 0.5981 0.4729 0.4646 -0.1355 0.0308  0.0509  294 ARG A O   
2144 C CB  . ARG A 315 ? 0.5861 0.5026 0.5177 -0.1619 0.0475  0.0118  294 ARG A CB  
2145 C CG  . ARG A 315 ? 0.6404 0.5485 0.5662 -0.1597 0.0383  0.0120  294 ARG A CG  
2146 C CD  . ARG A 315 ? 0.7549 0.6738 0.6985 -0.1755 0.0443  -0.0028 294 ARG A CD  
2147 N NE  . ARG A 315 ? 0.7643 0.7079 0.7428 -0.1785 0.0496  -0.0185 294 ARG A NE  
2148 C CZ  . ARG A 315 ? 0.7063 0.6638 0.7113 -0.1654 0.0402  -0.0268 294 ARG A CZ  
2149 N NH1 . ARG A 315 ? 0.6500 0.5996 0.6502 -0.1484 0.0255  -0.0205 294 ARG A NH1 
2150 N NH2 . ARG A 315 ? 0.6439 0.6240 0.6804 -0.1691 0.0457  -0.0420 294 ARG A NH2 
2151 N N   . PHE A 316 ? 0.5093 0.4099 0.4190 -0.1268 0.0308  0.0391  295 PHE A N   
2152 C CA  . PHE A 316 ? 0.5058 0.3982 0.4055 -0.1087 0.0194  0.0514  295 PHE A CA  
2153 C C   . PHE A 316 ? 0.5140 0.3929 0.3859 -0.1072 0.0219  0.0673  295 PHE A C   
2154 O O   . PHE A 316 ? 0.5103 0.3770 0.3612 -0.0978 0.0148  0.0790  295 PHE A O   
2155 C CB  . PHE A 316 ? 0.5347 0.4390 0.4593 -0.0970 0.0142  0.0472  295 PHE A CB  
2156 C CG  . PHE A 316 ? 0.5237 0.4414 0.4759 -0.0944 0.0087  0.0322  295 PHE A CG  
2157 C CD1 . PHE A 316 ? 0.6195 0.5345 0.5693 -0.0929 0.0017  0.0289  295 PHE A CD1 
2158 C CD2 . PHE A 316 ? 0.4888 0.4220 0.4701 -0.0929 0.0099  0.0208  295 PHE A CD2 
2159 C CE1 . PHE A 316 ? 0.6600 0.5885 0.6364 -0.0903 -0.0041 0.0144  295 PHE A CE1 
2160 C CE2 . PHE A 316 ? 0.4912 0.4379 0.4990 -0.0897 0.0042  0.0064  295 PHE A CE2 
2161 C CZ  . PHE A 316 ? 0.5948 0.5398 0.6007 -0.0886 -0.0028 0.0031  295 PHE A CZ  
2162 N N   . ARG A 317 ? 0.5196 0.4012 0.3912 -0.1160 0.0317  0.0673  296 ARG A N   
2163 C CA  . ARG A 317 ? 0.5673 0.4389 0.4170 -0.1134 0.0333  0.0815  296 ARG A CA  
2164 C C   . ARG A 317 ? 0.5754 0.4317 0.3948 -0.1191 0.0349  0.0895  296 ARG A C   
2165 O O   . ARG A 317 ? 0.6193 0.4657 0.4178 -0.1126 0.0322  0.1027  296 ARG A O   
2166 C CB  . ARG A 317 ? 0.5281 0.4069 0.3866 -0.1215 0.0427  0.0777  296 ARG A CB  
2167 C CG  . ARG A 317 ? 0.5510 0.4216 0.3907 -0.1189 0.0439  0.0911  296 ARG A CG  
2168 C CD  . ARG A 317 ? 0.5538 0.4227 0.3949 -0.1024 0.0346  0.1019  296 ARG A CD  
2169 N NE  . ARG A 317 ? 0.5165 0.3788 0.3406 -0.1002 0.0357  0.1148  296 ARG A NE  
2170 C CZ  . ARG A 317 ? 0.5601 0.4117 0.3584 -0.0975 0.0336  0.1262  296 ARG A CZ  
2171 N NH1 . ARG A 317 ? 0.6312 0.4753 0.4158 -0.0965 0.0300  0.1268  296 ARG A NH1 
2172 N NH2 . ARG A 317 ? 0.5220 0.3703 0.3086 -0.0955 0.0346  0.1367  296 ARG A NH2 
2173 N N   . ASN A 318 ? 0.6219 0.4761 0.4389 -0.1313 0.0391  0.0816  297 ASN A N   
2174 C CA  . ASN A 318 ? 0.6109 0.4485 0.3992 -0.1374 0.0399  0.0884  297 ASN A CA  
2175 C C   . ASN A 318 ? 0.7395 0.5674 0.5176 -0.1270 0.0287  0.0927  297 ASN A C   
2176 O O   . ASN A 318 ? 0.7882 0.6004 0.5416 -0.1297 0.0274  0.0987  297 ASN A O   
2177 C CB  . ASN A 318 ? 0.6531 0.4914 0.4425 -0.1565 0.0501  0.0785  297 ASN A CB  
2178 C CG  . ASN A 318 ? 0.7774 0.5970 0.5345 -0.1649 0.0535  0.0868  297 ASN A CG  
2179 O OD1 . ASN A 318 ? 0.8158 0.6272 0.5533 -0.1610 0.0535  0.0976  297 ASN A OD1 
2180 N ND2 . ASN A 318 ? 0.7908 0.6034 0.5423 -0.1766 0.0561  0.0818  297 ASN A ND2 
2181 N N   . ASP A 319 ? 0.5753 0.4114 0.3710 -0.1148 0.0201  0.0894  298 ASP A N   
2182 C CA  . ASP A 319 ? 0.6215 0.4495 0.4081 -0.1030 0.0086  0.0929  298 ASP A CA  
2183 C C   . ASP A 319 ? 0.6736 0.5013 0.4545 -0.0850 0.0013  0.1045  298 ASP A C   
2184 O O   . ASP A 319 ? 0.6056 0.4426 0.4038 -0.0741 -0.0049 0.1022  298 ASP A O   
2185 C CB  . ASP A 319 ? 0.6127 0.4503 0.4231 -0.1035 0.0039  0.0792  298 ASP A CB  
2186 C CG  . ASP A 319 ? 0.6744 0.5019 0.4734 -0.0946 -0.0075 0.0807  298 ASP A CG  
2187 O OD1 . ASP A 319 ? 0.6854 0.4990 0.4582 -0.0863 -0.0121 0.0926  298 ASP A OD1 
2188 O OD2 . ASP A 319 ? 0.6394 0.4733 0.4559 -0.0956 -0.0122 0.0692  298 ASP A OD2 
2189 N N   . GLU A 320 ? 0.7794 0.4047 0.5129 -0.1089 0.0790  0.0755  299 GLU A N   
2190 C CA  . GLU A 320 ? 0.7746 0.4156 0.5185 -0.0987 0.0727  0.0771  299 GLU A CA  
2191 C C   . GLU A 320 ? 0.7795 0.4032 0.5231 -0.0971 0.0772  0.0694  299 GLU A C   
2192 O O   . GLU A 320 ? 0.7459 0.3841 0.5002 -0.0939 0.0711  0.0646  299 GLU A O   
2193 C CB  . GLU A 320 ? 0.8667 0.5143 0.6085 -0.0837 0.0721  0.0951  299 GLU A CB  
2194 C CG  . GLU A 320 ? 0.9557 0.6377 0.7056 -0.0840 0.0606  0.0997  299 GLU A CG  
2195 C CD  . GLU A 320 ? 1.0948 0.7900 0.8449 -0.0700 0.0587  0.1193  299 GLU A CD  
2196 O OE1 . GLU A 320 ? 1.2973 1.0191 1.0557 -0.0676 0.0496  0.1222  299 GLU A OE1 
2197 O OE2 . GLU A 320 ? 1.2368 0.9165 0.9787 -0.0615 0.0668  0.1328  299 GLU A OE2 
2198 N N   . ALA A 321 ? 0.7517 0.3430 0.4811 -0.1003 0.0885  0.0680  300 ALA A N   
2199 C CA  . ALA A 321 ? 0.6970 0.2692 0.4218 -0.1032 0.0937  0.0588  300 ALA A CA  
2200 C C   . ALA A 321 ? 0.6495 0.2399 0.3851 -0.1181 0.0862  0.0439  300 ALA A C   
2201 O O   . ALA A 321 ? 0.6388 0.2347 0.3805 -0.1175 0.0830  0.0375  300 ALA A O   
2202 C CB  . ALA A 321 ? 0.7455 0.2783 0.4496 -0.1073 0.1083  0.0586  300 ALA A CB  
2203 N N   . PHE A 322 ? 0.7113 0.3125 0.4500 -0.1307 0.0838  0.0395  301 PHE A N   
2204 C CA  . PHE A 322 ? 0.7184 0.3415 0.4702 -0.1430 0.0774  0.0286  301 PHE A CA  
2205 C C   . PHE A 322 ? 0.6349 0.2879 0.4045 -0.1352 0.0674  0.0281  301 PHE A C   
2206 O O   . PHE A 322 ? 0.6313 0.2969 0.4108 -0.1385 0.0633  0.0209  301 PHE A O   
2207 C CB  . PHE A 322 ? 0.7504 0.3806 0.5032 -0.1555 0.0784  0.0269  301 PHE A CB  
2208 C CG  . PHE A 322 ? 0.7516 0.4091 0.5209 -0.1653 0.0729  0.0193  301 PHE A CG  
2209 C CD1 . PHE A 322 ? 0.7531 0.4132 0.5251 -0.1755 0.0725  0.0121  301 PHE A CD1 
2210 C CD2 . PHE A 322 ? 0.7295 0.4102 0.5109 -0.1646 0.0693  0.0206  301 PHE A CD2 
2211 C CE1 . PHE A 322 ? 0.8176 0.5068 0.6070 -0.1832 0.0679  0.0081  301 PHE A CE1 
2212 C CE2 . PHE A 322 ? 0.7435 0.4487 0.5410 -0.1713 0.0667  0.0158  301 PHE A CE2 
2213 C CZ  . PHE A 322 ? 0.7423 0.4538 0.5453 -0.1798 0.0656  0.0106  301 PHE A CZ  
2214 N N   . LEU A 323 ? 0.6298 0.2946 0.4023 -0.1261 0.0637  0.0359  302 LEU A N   
2215 C CA  . LEU A 323 ? 0.6224 0.3131 0.4086 -0.1203 0.0552  0.0351  302 LEU A CA  
2216 C C   . LEU A 323 ? 0.6143 0.3038 0.4037 -0.1106 0.0529  0.0353  302 LEU A C   
2217 O O   . LEU A 323 ? 0.5859 0.2929 0.3873 -0.1101 0.0471  0.0297  302 LEU A O   
2218 C CB  . LEU A 323 ? 0.6305 0.3323 0.4145 -0.1154 0.0521  0.0439  302 LEU A CB  
2219 C CG  . LEU A 323 ? 0.7044 0.4071 0.4835 -0.1247 0.0547  0.0442  302 LEU A CG  
2220 C CD1 . LEU A 323 ? 0.6257 0.3376 0.3985 -0.1210 0.0516  0.0540  302 LEU A CD1 
2221 C CD2 . LEU A 323 ? 0.6412 0.3587 0.4312 -0.1338 0.0540  0.0346  302 LEU A CD2 
2222 N N   . ASN A 324 ? 0.6272 0.2952 0.4057 -0.1021 0.0588  0.0423  303 ASN A N   
2223 C CA  . ASN A 324 ? 0.6658 0.3300 0.4461 -0.0919 0.0587  0.0432  303 ASN A CA  
2224 C C   . ASN A 324 ? 0.6694 0.3281 0.4511 -0.1009 0.0594  0.0309  303 ASN A C   
2225 O O   . ASN A 324 ? 0.6049 0.2755 0.3957 -0.0968 0.0545  0.0274  303 ASN A O   
2226 C CB  . ASN A 324 ? 0.6647 0.3030 0.4317 -0.0801 0.0684  0.0545  303 ASN A CB  
2227 C CG  . ASN A 324 ? 0.7694 0.4242 0.5413 -0.0652 0.0646  0.0697  303 ASN A CG  
2228 O OD1 . ASN A 324 ? 0.7601 0.4443 0.5438 -0.0648 0.0543  0.0701  303 ASN A OD1 
2229 N ND2 . ASN A 324 ? 0.9029 0.5393 0.6653 -0.0534 0.0738  0.0832  303 ASN A ND2 
2230 N N   . GLN A 325 ? 0.6462 0.2883 0.4185 -0.1144 0.0653  0.0246  304 GLN A N   
2231 C CA  . GLN A 325 ? 0.6313 0.2713 0.4034 -0.1261 0.0653  0.0139  304 GLN A CA  
2232 C C   . GLN A 325 ? 0.6310 0.3054 0.4228 -0.1322 0.0555  0.0082  304 GLN A C   
2233 O O   . GLN A 325 ? 0.5668 0.2504 0.3648 -0.1357 0.0521  0.0022  304 GLN A O   
2234 C CB  . GLN A 325 ? 0.6301 0.2455 0.3854 -0.1418 0.0740  0.0095  304 GLN A CB  
2235 C CG  . GLN A 325 ? 0.8682 0.4652 0.6111 -0.1516 0.0789  0.0013  304 GLN A CG  
2236 C CD  . GLN A 325 ? 0.9189 0.4884 0.6489 -0.1374 0.0873  0.0049  304 GLN A CD  
2237 O OE1 . GLN A 325 ? 0.8546 0.4239 0.5852 -0.1356 0.0861  0.0007  304 GLN A OE1 
2238 N NE2 . GLN A 325 ? 1.0939 0.6411 0.8127 -0.1266 0.0965  0.0137  304 GLN A NE2 
2239 N N   . VAL A 326 ? 0.5411 0.2338 0.3421 -0.1334 0.0522  0.0105  305 VAL A N   
2240 C CA  . VAL A 326 ? 0.5750 0.2981 0.3944 -0.1361 0.0457  0.0069  305 VAL A CA  
2241 C C   . VAL A 326 ? 0.4972 0.2340 0.3262 -0.1241 0.0395  0.0077  305 VAL A C   
2242 O O   . VAL A 326 ? 0.4783 0.2326 0.3195 -0.1254 0.0353  0.0033  305 VAL A O   
2243 C CB  . VAL A 326 ? 0.6005 0.3347 0.4243 -0.1392 0.0464  0.0095  305 VAL A CB  
2244 C CG1 . VAL A 326 ? 0.5433 0.3049 0.3844 -0.1375 0.0423  0.0076  305 VAL A CG1 
2245 C CG2 . VAL A 326 ? 0.6878 0.4152 0.5064 -0.1531 0.0517  0.0077  305 VAL A CG2 
2246 N N   . MET A 327 ? 0.5464 0.2775 0.3702 -0.1126 0.0389  0.0146  306 MET A N   
2247 C CA  . MET A 327 ? 0.5055 0.2506 0.3374 -0.1022 0.0330  0.0161  306 MET A CA  
2248 C C   . MET A 327 ? 0.5295 0.2669 0.3610 -0.0988 0.0330  0.0128  306 MET A C   
2249 O O   . MET A 327 ? 0.4805 0.2335 0.3225 -0.0950 0.0277  0.0100  306 MET A O   
2250 C CB  . MET A 327 ? 0.5122 0.2566 0.3383 -0.0924 0.0321  0.0263  306 MET A CB  
2251 C CG  . MET A 327 ? 0.5400 0.2975 0.3665 -0.0963 0.0301  0.0289  306 MET A CG  
2252 S SD  . MET A 327 ? 0.4964 0.2584 0.3150 -0.0876 0.0276  0.0428  306 MET A SD  
2253 C CE  . MET A 327 ? 0.6442 0.3791 0.4505 -0.0821 0.0359  0.0511  306 MET A CE  
2254 N N   . LYS A 328 ? 0.5466 0.2579 0.3643 -0.1002 0.0402  0.0130  307 LYS A N   
2255 C CA  . LYS A 328 ? 0.5294 0.2291 0.3430 -0.0990 0.0422  0.0088  307 LYS A CA  
2256 C C   . LYS A 328 ? 0.5062 0.2210 0.3284 -0.1112 0.0379  -0.0007 307 LYS A C   
2257 O O   . LYS A 328 ? 0.5339 0.2629 0.3658 -0.1075 0.0327  -0.0034 307 LYS A O   
2258 C CB  . LYS A 328 ? 0.5973 0.2606 0.3902 -0.1005 0.0537  0.0101  307 LYS A CB  
2259 C CG  . LYS A 328 ? 0.7125 0.3570 0.4962 -0.0978 0.0588  0.0066  307 LYS A CG  
2260 C CD  . LYS A 328 ? 0.7686 0.3711 0.5280 -0.0996 0.0735  0.0079  307 LYS A CD  
2261 C CE  . LYS A 328 ? 0.8726 0.4516 0.6195 -0.0971 0.0812  0.0041  307 LYS A CE  
2262 N NZ  . LYS A 328 ? 0.8636 0.4440 0.6165 -0.0749 0.0828  0.0144  307 LYS A NZ  
2263 N N   . GLU A 329 ? 0.5349 0.2505 0.3552 -0.1260 0.0396  -0.0044 308 GLU A N   
2264 C CA  . GLU A 329 ? 0.5949 0.3297 0.4247 -0.1386 0.0356  -0.0106 308 GLU A CA  
2265 C C   . GLU A 329 ? 0.5362 0.3036 0.3877 -0.1324 0.0280  -0.0098 308 GLU A C   
2266 O O   . GLU A 329 ? 0.4927 0.2755 0.3534 -0.1338 0.0236  -0.0129 308 GLU A O   
2267 C CB  . GLU A 329 ? 0.6196 0.3546 0.4456 -0.1549 0.0387  -0.0120 308 GLU A CB  
2268 C CG  . GLU A 329 ? 0.8486 0.6112 0.6874 -0.1685 0.0342  -0.0150 308 GLU A CG  
2269 C CD  . GLU A 329 ? 1.0265 0.7996 0.8683 -0.1817 0.0363  -0.0133 308 GLU A CD  
2270 O OE1 . GLU A 329 ? 0.9088 0.6703 0.7453 -0.1788 0.0405  -0.0103 308 GLU A OE1 
2271 O OE2 . GLU A 329 ? 1.0041 0.7993 0.8539 -0.1954 0.0337  -0.0139 308 GLU A OE2 
2272 N N   . GLY A 330 ? 0.5463 0.3230 0.4045 -0.1263 0.0273  -0.0055 309 GLY A N   
2273 C CA  . GLY A 330 ? 0.4871 0.2894 0.3623 -0.1211 0.0230  -0.0050 309 GLY A CA  
2274 C C   . GLY A 330 ? 0.4423 0.2491 0.3215 -0.1104 0.0183  -0.0055 309 GLY A C   
2275 O O   . GLY A 330 ? 0.4622 0.2882 0.3546 -0.1090 0.0149  -0.0073 309 GLY A O   
2276 N N   . ALA A 331 ? 0.4774 0.2675 0.3460 -0.1021 0.0189  -0.0027 310 ALA A N   
2277 C CA  . ALA A 331 ? 0.4890 0.2846 0.3617 -0.0918 0.0147  -0.0022 310 ALA A CA  
2278 C C   . ALA A 331 ? 0.4863 0.2796 0.3595 -0.0946 0.0139  -0.0074 310 ALA A C   
2279 O O   . ALA A 331 ? 0.4563 0.2628 0.3385 -0.0893 0.0094  -0.0089 310 ALA A O   
2280 C CB  . ALA A 331 ? 0.4528 0.2353 0.3159 -0.0813 0.0161  0.0050  310 ALA A CB  
2281 N N   . GLU A 332 ? 0.5039 0.2797 0.3656 -0.1040 0.0186  -0.0105 311 GLU A N   
2282 C CA  . GLU A 332 ? 0.5128 0.2861 0.3717 -0.1102 0.0181  -0.0161 311 GLU A CA  
2283 C C   . GLU A 332 ? 0.4812 0.2841 0.3566 -0.1180 0.0122  -0.0188 311 GLU A C   
2284 O O   . GLU A 332 ? 0.4704 0.2845 0.3523 -0.1164 0.0082  -0.0211 311 GLU A O   
2285 C CB  . GLU A 332 ? 0.5204 0.2661 0.3591 -0.1222 0.0256  -0.0195 311 GLU A CB  
2286 C CG  . GLU A 332 ? 0.6783 0.3949 0.5012 -0.1165 0.0339  -0.0150 311 GLU A CG  
2287 C CD  . GLU A 332 ? 0.8521 0.5334 0.6509 -0.1259 0.0442  -0.0189 311 GLU A CD  
2288 O OE1 . GLU A 332 ? 0.8659 0.5470 0.6582 -0.1446 0.0448  -0.0250 311 GLU A OE1 
2289 O OE2 . GLU A 332 ? 0.8784 0.5322 0.6638 -0.1150 0.0526  -0.0151 311 GLU A OE2 
2290 N N   . LYS A 333 ? 0.5165 0.3333 0.3994 -0.1257 0.0124  -0.0172 312 LYS A N   
2291 C CA  . LYS A 333 ? 0.5099 0.3578 0.4112 -0.1305 0.0085  -0.0165 312 LYS A CA  
2292 C C   . LYS A 333 ? 0.4903 0.3548 0.4062 -0.1172 0.0052  -0.0145 312 LYS A C   
2293 O O   . LYS A 333 ? 0.4901 0.3736 0.4177 -0.1166 0.0016  -0.0147 312 LYS A O   
2294 C CB  . LYS A 333 ? 0.5251 0.3843 0.4324 -0.1388 0.0114  -0.0132 312 LYS A CB  
2295 C CG  . LYS A 333 ? 0.6397 0.4914 0.5356 -0.1564 0.0136  -0.0150 312 LYS A CG  
2296 C CD  . LYS A 333 ? 0.6730 0.5485 0.5817 -0.1654 0.0150  -0.0101 312 LYS A CD  
2297 C CE  . LYS A 333 ? 0.7030 0.5656 0.6069 -0.1625 0.0203  -0.0079 312 LYS A CE  
2298 N NZ  . LYS A 333 ? 0.6657 0.5532 0.5844 -0.1688 0.0228  -0.0022 312 LYS A NZ  
2299 N N   . ALA A 334 ? 0.4610 0.3185 0.3751 -0.1075 0.0066  -0.0123 313 ALA A N   
2300 C CA  . ALA A 334 ? 0.4415 0.3119 0.3656 -0.0974 0.0046  -0.0111 313 ALA A CA  
2301 C C   . ALA A 334 ? 0.4631 0.3330 0.3872 -0.0909 0.0001  -0.0132 313 ALA A C   
2302 O O   . ALA A 334 ? 0.4144 0.3006 0.3501 -0.0871 -0.0023 -0.0135 313 ALA A O   
2303 C CB  . ALA A 334 ? 0.3739 0.2358 0.2915 -0.0920 0.0067  -0.0085 313 ALA A CB  
2304 N N   . SER A 335 ? 0.4644 0.3147 0.3755 -0.0888 0.0003  -0.0140 314 SER A N   
2305 C CA  . SER A 335 ? 0.5157 0.3641 0.4261 -0.0821 -0.0026 -0.0156 314 SER A CA  
2306 C C   . SER A 335 ? 0.4701 0.3280 0.3853 -0.0894 -0.0048 -0.0197 314 SER A C   
2307 O O   . SER A 335 ? 0.4295 0.2970 0.3513 -0.0842 -0.0084 -0.0209 314 SER A O   
2308 C CB  . SER A 335 ? 0.4951 0.3185 0.3900 -0.0772 0.0009  -0.0140 314 SER A CB  
2309 O OG  . SER A 335 ? 0.5869 0.4101 0.4810 -0.0671 0.0004  -0.0080 314 SER A OG  
2310 N N   . ALA A 336 ? 0.4245 0.2816 0.3360 -0.1025 -0.0031 -0.0214 315 ALA A N   
2311 C CA  . ALA A 336 ? 0.4621 0.3315 0.3767 -0.1124 -0.0059 -0.0242 315 ALA A CA  
2312 C C   . ALA A 336 ? 0.4062 0.3074 0.3421 -0.1091 -0.0101 -0.0210 315 ALA A C   
2313 O O   . ALA A 336 ? 0.4693 0.3818 0.4103 -0.1088 -0.0139 -0.0222 315 ALA A O   
2314 C CB  . ALA A 336 ? 0.4597 0.3257 0.3657 -0.1299 -0.0035 -0.0254 315 ALA A CB  
2315 N N   . HIS A 337 ? 0.4071 0.3216 0.3546 -0.1063 -0.0082 -0.0166 316 HIS A N   
2316 C CA  . HIS A 337 ? 0.4280 0.3689 0.3948 -0.1008 -0.0090 -0.0124 316 HIS A CA  
2317 C C   . HIS A 337 ? 0.3641 0.3016 0.3328 -0.0875 -0.0100 -0.0135 316 HIS A C   
2318 O O   . HIS A 337 ? 0.3659 0.3183 0.3448 -0.0833 -0.0124 -0.0127 316 HIS A O   
2319 C CB  . HIS A 337 ? 0.4555 0.4077 0.4321 -0.1014 -0.0036 -0.0069 316 HIS A CB  
2320 C CG  . HIS A 337 ? 0.5603 0.5264 0.5408 -0.1148 -0.0031 -0.0035 316 HIS A CG  
2321 N ND1 . HIS A 337 ? 0.6388 0.5893 0.6063 -0.1245 -0.0013 -0.0054 316 HIS A ND1 
2322 C CD2 . HIS A 337 ? 0.7011 0.6973 0.6971 -0.1209 -0.0043 0.0030  316 HIS A CD2 
2323 C CE1 . HIS A 337 ? 0.6457 0.6157 0.6196 -0.1372 -0.0016 -0.0012 316 HIS A CE1 
2324 N NE2 . HIS A 337 ? 0.6953 0.6952 0.6873 -0.1353 -0.0037 0.0046  316 HIS A NE2 
2325 N N   . ALA A 338 ? 0.3901 0.3096 0.3487 -0.0816 -0.0085 -0.0147 317 ALA A N   
2326 C CA  . ALA A 338 ? 0.3666 0.2855 0.3261 -0.0714 -0.0095 -0.0149 317 ALA A CA  
2327 C C   . ALA A 338 ? 0.3618 0.2800 0.3201 -0.0673 -0.0143 -0.0175 317 ALA A C   
2328 O O   . ALA A 338 ? 0.3256 0.2531 0.2907 -0.0610 -0.0159 -0.0175 317 ALA A O   
2329 C CB  . ALA A 338 ? 0.3277 0.2310 0.2754 -0.0684 -0.0079 -0.0141 317 ALA A CB  
2330 N N   . SER A 339 ? 0.3467 0.2517 0.2949 -0.0711 -0.0154 -0.0199 318 SER A N   
2331 C CA  . SER A 339 ? 0.3292 0.2302 0.2742 -0.0670 -0.0184 -0.0223 318 SER A CA  
2332 C C   . SER A 339 ? 0.3071 0.2277 0.2634 -0.0698 -0.0216 -0.0233 318 SER A C   
2333 O O   . SER A 339 ? 0.3427 0.2671 0.3018 -0.0635 -0.0243 -0.0244 318 SER A O   
2334 C CB  . SER A 339 ? 0.3665 0.2444 0.2951 -0.0711 -0.0157 -0.0247 318 SER A CB  
2335 O OG  . SER A 339 ? 0.5104 0.3884 0.4354 -0.0849 -0.0145 -0.0270 318 SER A OG  
2336 N N   . LYS A 340 ? 0.3564 0.2916 0.3199 -0.0791 -0.0214 -0.0217 319 LYS A N   
2337 C CA  . LYS A 340 ? 0.4116 0.3703 0.3879 -0.0813 -0.0246 -0.0199 319 LYS A CA  
2338 C C   . LYS A 340 ? 0.3775 0.3488 0.3669 -0.0696 -0.0241 -0.0171 319 LYS A C   
2339 O O   . LYS A 340 ? 0.3215 0.3010 0.3157 -0.0655 -0.0271 -0.0176 319 LYS A O   
2340 C CB  . LYS A 340 ? 0.4237 0.4017 0.4081 -0.0927 -0.0241 -0.0155 319 LYS A CB  
2341 C CG  . LYS A 340 ? 0.4722 0.4383 0.4414 -0.1080 -0.0244 -0.0189 319 LYS A CG  
2342 C CD  . LYS A 340 ? 0.5296 0.5215 0.5085 -0.1211 -0.0252 -0.0130 319 LYS A CD  
2343 C CE  . LYS A 340 ? 0.6863 0.6637 0.6471 -0.1386 -0.0243 -0.0169 319 LYS A CE  
2344 N NZ  . LYS A 340 ? 0.7608 0.7687 0.7306 -0.1545 -0.0267 -0.0104 319 LYS A NZ  
2345 N N   . THR A 341 ? 0.3154 0.2858 0.3083 -0.0650 -0.0193 -0.0144 320 THR A N   
2346 C CA  . THR A 341 ? 0.3155 0.2929 0.3167 -0.0557 -0.0165 -0.0125 320 THR A CA  
2347 C C   . THR A 341 ? 0.2635 0.2291 0.2564 -0.0491 -0.0194 -0.0164 320 THR A C   
2348 O O   . THR A 341 ? 0.2701 0.2434 0.2689 -0.0435 -0.0200 -0.0163 320 THR A O   
2349 C CB  . THR A 341 ? 0.3247 0.2993 0.3270 -0.0543 -0.0088 -0.0096 320 THR A CB  
2350 O OG1 . THR A 341 ? 0.3139 0.3047 0.3280 -0.0585 -0.0050 -0.0037 320 THR A OG1 
2351 C CG2 . THR A 341 ? 0.2854 0.2594 0.2898 -0.0464 -0.0037 -0.0091 320 THR A CG2 
2352 N N   . LEU A 342 ? 0.2903 0.2389 0.2702 -0.0493 -0.0208 -0.0187 321 LEU A N   
2353 C CA  . LEU A 342 ? 0.3125 0.2544 0.2862 -0.0427 -0.0236 -0.0199 321 LEU A CA  
2354 C C   . LEU A 342 ? 0.3476 0.2930 0.3234 -0.0401 -0.0278 -0.0220 321 LEU A C   
2355 O O   . LEU A 342 ? 0.2477 0.1976 0.2258 -0.0343 -0.0296 -0.0223 321 LEU A O   
2356 C CB  . LEU A 342 ? 0.3022 0.2285 0.2635 -0.0424 -0.0237 -0.0190 321 LEU A CB  
2357 C CG  . LEU A 342 ? 0.2969 0.2209 0.2532 -0.0354 -0.0265 -0.0173 321 LEU A CG  
2358 C CD1 . LEU A 342 ? 0.3059 0.2365 0.2619 -0.0352 -0.0258 -0.0159 321 LEU A CD1 
2359 C CD2 . LEU A 342 ? 0.3310 0.2414 0.2773 -0.0332 -0.0260 -0.0139 321 LEU A CD2 
2360 N N   . LYS A 343 ? 0.2972 0.2396 0.2703 -0.0458 -0.0290 -0.0238 322 LYS A N   
2361 C CA  . LYS A 343 ? 0.3881 0.3315 0.3603 -0.0449 -0.0321 -0.0263 322 LYS A CA  
2362 C C   . LYS A 343 ? 0.3024 0.2664 0.2880 -0.0436 -0.0341 -0.0252 322 LYS A C   
2363 O O   . LYS A 343 ? 0.3568 0.3238 0.3437 -0.0389 -0.0366 -0.0265 322 LYS A O   
2364 C CB  . LYS A 343 ? 0.3266 0.2597 0.2887 -0.0546 -0.0315 -0.0292 322 LYS A CB  
2365 C CG  . LYS A 343 ? 0.4948 0.4023 0.4412 -0.0534 -0.0276 -0.0301 322 LYS A CG  
2366 C CD  . LYS A 343 ? 0.5257 0.4176 0.4578 -0.0645 -0.0247 -0.0342 322 LYS A CD  
2367 C CE  . LYS A 343 ? 0.6313 0.4945 0.5470 -0.0622 -0.0181 -0.0339 322 LYS A CE  
2368 N NZ  . LYS A 343 ? 0.6023 0.4570 0.5165 -0.0472 -0.0163 -0.0305 322 LYS A NZ  
2369 N N   . ALA A 344 ? 0.3422 0.3212 0.3386 -0.0468 -0.0320 -0.0215 323 ALA A N   
2370 C CA  . ALA A 344 ? 0.3269 0.3258 0.3373 -0.0432 -0.0319 -0.0180 323 ALA A CA  
2371 C C   . ALA A 344 ? 0.3312 0.3269 0.3429 -0.0338 -0.0294 -0.0182 323 ALA A C   
2372 O O   . ALA A 344 ? 0.2973 0.3017 0.3150 -0.0291 -0.0303 -0.0176 323 ALA A O   
2373 C CB  . ALA A 344 ? 0.2788 0.2949 0.3015 -0.0468 -0.0281 -0.0115 323 ALA A CB  
2374 N N   . VAL A 345 ? 0.2441 0.2274 0.2485 -0.0324 -0.0261 -0.0189 324 VAL A N   
2375 C CA  . VAL A 345 ? 0.3223 0.3014 0.3236 -0.0272 -0.0238 -0.0197 324 VAL A CA  
2376 C C   . VAL A 345 ? 0.3147 0.2910 0.3111 -0.0236 -0.0295 -0.0223 324 VAL A C   
2377 O O   . VAL A 345 ? 0.2839 0.2648 0.2826 -0.0197 -0.0295 -0.0227 324 VAL A O   
2378 C CB  . VAL A 345 ? 0.2769 0.2443 0.2686 -0.0295 -0.0197 -0.0197 324 VAL A CB  
2379 C CG1 . VAL A 345 ? 0.2705 0.2332 0.2543 -0.0279 -0.0188 -0.0210 324 VAL A CG1 
2380 C CG2 . VAL A 345 ? 0.2970 0.2670 0.2943 -0.0315 -0.0118 -0.0167 324 VAL A CG2 
2381 N N   . TYR A 346 ? 0.2854 0.2530 0.2743 -0.0244 -0.0333 -0.0235 325 TYR A N   
2382 C CA  . TYR A 346 ? 0.2881 0.2528 0.2728 -0.0196 -0.0371 -0.0244 325 TYR A CA  
2383 C C   . TYR A 346 ? 0.2840 0.2570 0.2750 -0.0181 -0.0396 -0.0262 325 TYR A C   
2384 O O   . TYR A 346 ? 0.2568 0.2324 0.2480 -0.0131 -0.0416 -0.0266 325 TYR A O   
2385 C CB  . TYR A 346 ? 0.2786 0.2296 0.2538 -0.0194 -0.0374 -0.0238 325 TYR A CB  
2386 C CG  . TYR A 346 ? 0.3118 0.2569 0.2802 -0.0183 -0.0363 -0.0200 325 TYR A CG  
2387 C CD1 . TYR A 346 ? 0.3494 0.3003 0.3180 -0.0203 -0.0354 -0.0188 325 TYR A CD1 
2388 C CD2 . TYR A 346 ? 0.3271 0.2601 0.2875 -0.0157 -0.0352 -0.0170 325 TYR A CD2 
2389 C CE1 . TYR A 346 ? 0.2986 0.2464 0.2595 -0.0214 -0.0352 -0.0148 325 TYR A CE1 
2390 C CE2 . TYR A 346 ? 0.3286 0.2596 0.2836 -0.0145 -0.0347 -0.0116 325 TYR A CE2 
2391 C CZ  . TYR A 346 ? 0.2965 0.2365 0.2519 -0.0182 -0.0356 -0.0105 325 TYR A CZ  
2392 O OH  . TYR A 346 ? 0.3173 0.2576 0.2660 -0.0192 -0.0357 -0.0047 325 TYR A OH  
2393 N N   . GLU A 347 ? 0.2687 0.2474 0.2642 -0.0233 -0.0396 -0.0266 326 GLU A N   
2394 C CA  . GLU A 347 ? 0.2912 0.2802 0.2919 -0.0236 -0.0425 -0.0275 326 GLU A CA  
2395 C C   . GLU A 347 ? 0.2752 0.2782 0.2869 -0.0187 -0.0413 -0.0250 326 GLU A C   
2396 O O   . GLU A 347 ? 0.3080 0.3165 0.3221 -0.0153 -0.0437 -0.0258 326 GLU A O   
2397 C CB  . GLU A 347 ? 0.3106 0.3060 0.3125 -0.0332 -0.0434 -0.0271 326 GLU A CB  
2398 C CG  . GLU A 347 ? 0.4619 0.4712 0.4684 -0.0362 -0.0469 -0.0269 326 GLU A CG  
2399 C CD  . GLU A 347 ? 0.5755 0.5723 0.5713 -0.0344 -0.0487 -0.0319 326 GLU A CD  
2400 O OE1 . GLU A 347 ? 0.5301 0.5064 0.5125 -0.0351 -0.0467 -0.0352 326 GLU A OE1 
2401 O OE2 . GLU A 347 ? 0.5957 0.6026 0.5965 -0.0314 -0.0510 -0.0317 326 GLU A OE2 
2402 N N   . ALA A 348 ? 0.2859 0.2928 0.3032 -0.0180 -0.0363 -0.0218 327 ALA A N   
2403 C CA  . ALA A 348 ? 0.2867 0.3017 0.3117 -0.0127 -0.0321 -0.0192 327 ALA A CA  
2404 C C   . ALA A 348 ? 0.3099 0.3162 0.3273 -0.0090 -0.0322 -0.0222 327 ALA A C   
2405 O O   . ALA A 348 ? 0.3110 0.3224 0.3318 -0.0051 -0.0316 -0.0220 327 ALA A O   
2406 C CB  . ALA A 348 ? 0.3652 0.3820 0.3954 -0.0127 -0.0237 -0.0148 327 ALA A CB  
2407 N N   . ILE A 349 ? 0.2696 0.2646 0.2765 -0.0108 -0.0330 -0.0241 328 ILE A N   
2408 C CA  . ILE A 349 ? 0.2549 0.2459 0.2543 -0.0095 -0.0337 -0.0253 328 ILE A CA  
2409 C C   . ILE A 349 ? 0.3104 0.3058 0.3106 -0.0056 -0.0395 -0.0264 328 ILE A C   
2410 O O   . ILE A 349 ? 0.3343 0.3326 0.3329 -0.0039 -0.0399 -0.0267 328 ILE A O   
2411 C CB  . ILE A 349 ? 0.3074 0.2900 0.2963 -0.0132 -0.0340 -0.0248 328 ILE A CB  
2412 C CG1 . ILE A 349 ? 0.3449 0.3216 0.3305 -0.0177 -0.0265 -0.0245 328 ILE A CG1 
2413 C CG2 . ILE A 349 ? 0.3294 0.3138 0.3111 -0.0131 -0.0372 -0.0241 328 ILE A CG2 
2414 C CD1 . ILE A 349 ? 0.3753 0.3446 0.3506 -0.0224 -0.0270 -0.0235 328 ILE A CD1 
2415 N N   . GLY A 350 ? 0.2905 0.2845 0.2912 -0.0048 -0.0432 -0.0270 329 GLY A N   
2416 C CA  . GLY A 350 ? 0.3090 0.3043 0.3091 -0.0007 -0.0469 -0.0279 329 GLY A CA  
2417 C C   . GLY A 350 ? 0.3386 0.3246 0.3311 0.0018  -0.0481 -0.0267 329 GLY A C   
2418 O O   . GLY A 350 ? 0.3206 0.3060 0.3116 0.0066  -0.0494 -0.0264 329 GLY A O   
2419 N N   . PHE A 351 ? 0.2862 0.2643 0.2736 -0.0006 -0.0465 -0.0250 330 PHE A N   
2420 C CA  . PHE A 351 ? 0.3116 0.2791 0.2919 0.0031  -0.0456 -0.0222 330 PHE A CA  
2421 C C   . PHE A 351 ? 0.2595 0.2158 0.2354 0.0027  -0.0437 -0.0255 330 PHE A C   
2422 O O   . PHE A 351 ? 0.2448 0.2013 0.2217 -0.0041 -0.0439 -0.0295 330 PHE A O   
2423 C CB  . PHE A 351 ? 0.2903 0.2508 0.2656 0.0000  -0.0436 -0.0196 330 PHE A CB  
2424 C CG  . PHE A 351 ? 0.2406 0.2094 0.2154 -0.0013 -0.0447 -0.0159 330 PHE A CG  
2425 C CD1 . PHE A 351 ? 0.3079 0.2885 0.2848 -0.0004 -0.0471 -0.0148 330 PHE A CD1 
2426 C CD2 . PHE A 351 ? 0.3105 0.2745 0.2804 -0.0054 -0.0431 -0.0136 330 PHE A CD2 
2427 C CE1 . PHE A 351 ? 0.3275 0.3145 0.2999 -0.0051 -0.0477 -0.0120 330 PHE A CE1 
2428 C CE2 . PHE A 351 ? 0.2835 0.2543 0.2496 -0.0092 -0.0438 -0.0106 330 PHE A CE2 
2429 C CZ  . PHE A 351 ? 0.3035 0.2856 0.2700 -0.0099 -0.0461 -0.0099 330 PHE A CZ  
2430 N N   . VAL A 352 ? 0.2819 0.2284 0.2519 0.0094  -0.0411 -0.0230 331 VAL A N   
2431 C CA  . VAL A 352 ? 0.2708 0.1988 0.2307 0.0078  -0.0363 -0.0263 331 VAL A CA  
2432 C C   . VAL A 352 ? 0.2816 0.1959 0.2338 0.0013  -0.0330 -0.0271 331 VAL A C   
2433 O O   . VAL A 352 ? 0.2893 0.2013 0.2408 0.0043  -0.0316 -0.0220 331 VAL A O   
2434 C CB  . VAL A 352 ? 0.3147 0.2321 0.2691 0.0185  -0.0310 -0.0219 331 VAL A CB  
2435 C CG1 . VAL A 352 ? 0.3632 0.2546 0.3022 0.0159  -0.0230 -0.0262 331 VAL A CG1 
2436 C CG2 . VAL A 352 ? 0.3927 0.3253 0.3550 0.0242  -0.0346 -0.0210 331 VAL A CG2 
2437 N N   . ALA A 353 ? 0.3062 0.2135 0.2525 -0.0090 -0.0320 -0.0330 332 ALA A N   
2438 C CA  . ALA A 353 ? 0.3648 0.2592 0.3027 -0.0172 -0.0287 -0.0343 332 ALA A CA  
2439 C C   . ALA A 353 ? 0.4416 0.3098 0.3653 -0.0116 -0.0200 -0.0316 332 ALA A C   
2440 O O   . ALA A 353 ? 0.3491 0.2022 0.2637 -0.0068 -0.0142 -0.0323 332 ALA A O   
2441 C CB  . ALA A 353 ? 0.4275 0.3219 0.3603 -0.0315 -0.0296 -0.0404 332 ALA A CB  
2442 N N   . LYS A 354 ? 0.3552 0.2172 0.2768 -0.0115 -0.0178 -0.0280 333 LYS A N   
2443 C CA  . LYS A 354 ? 0.4602 0.2966 0.3684 -0.0054 -0.0081 -0.0238 333 LYS A CA  
2444 C C   . LYS A 354 ? 0.4221 0.2309 0.3110 -0.0150 0.0001  -0.0310 333 LYS A C   
2445 O O   . LYS A 354 ? 0.4578 0.2662 0.3422 -0.0300 -0.0019 -0.0370 333 LYS A O   
2446 C CB  . LYS A 354 ? 0.3636 0.1995 0.2726 -0.0058 -0.0078 -0.0189 333 LYS A CB  
2447 C CG  . LYS A 354 ? 0.4337 0.2432 0.3293 0.0012  0.0032  -0.0129 333 LYS A CG  
2448 C CD  . LYS A 354 ? 0.4728 0.2840 0.3695 -0.0002 0.0025  -0.0080 333 LYS A CD  
2449 C CE  . LYS A 354 ? 0.5662 0.3464 0.4467 0.0033  0.0150  -0.0038 333 LYS A CE  
2450 N NZ  . LYS A 354 ? 0.6537 0.4237 0.5315 0.0200  0.0236  0.0059  333 LYS A NZ  
2451 N N   . PRO A 355 ? 0.4899 0.2752 0.3659 -0.0079 0.0102  -0.0303 334 PRO A N   
2452 C CA  . PRO A 355 ? 0.5319 0.2865 0.3845 -0.0197 0.0198  -0.0385 334 PRO A CA  
2453 C C   . PRO A 355 ? 0.6042 0.3302 0.4397 -0.0250 0.0297  -0.0383 334 PRO A C   
2454 O O   . PRO A 355 ? 0.6159 0.3468 0.4588 -0.0185 0.0289  -0.0312 334 PRO A O   
2455 C CB  . PRO A 355 ? 0.5888 0.3257 0.4330 -0.0079 0.0296  -0.0366 334 PRO A CB  
2456 C CG  . PRO A 355 ? 0.5117 0.2631 0.3722 0.0124  0.0289  -0.0239 334 PRO A CG  
2457 C CD  . PRO A 355 ? 0.5217 0.3093 0.4034 0.0101  0.0137  -0.0220 334 PRO A CD  
2458 O OXT . PRO A 355 ? 0.7518 0.4481 0.5638 -0.0373 0.0392  -0.0455 334 PRO A OXT 
2459 N N   . THR B 23  ? 0.7393 0.7952 0.6935 0.1357  0.0226  0.1458  2   THR B N   
2460 C CA  . THR B 23  ? 0.7498 0.8205 0.7017 0.1193  0.0079  0.1303  2   THR B CA  
2461 C C   . THR B 23  ? 0.6998 0.8056 0.6743 0.1207  0.0033  0.1287  2   THR B C   
2462 O O   . THR B 23  ? 0.6866 0.8300 0.6816 0.1305  0.0000  0.1390  2   THR B O   
2463 C CB  . THR B 23  ? 0.8178 0.9092 0.7665 0.1119  -0.0078 0.1292  2   THR B CB  
2464 O OG1 . THR B 23  ? 0.9675 1.0353 0.9017 0.1155  -0.0018 0.1371  2   THR B OG1 
2465 C CG2 . THR B 23  ? 0.7106 0.7975 0.6475 0.0940  -0.0189 0.1112  2   THR B CG2 
2466 N N   . LYS B 24  ? 0.5601 0.6550 0.5308 0.1106  0.0037  0.1159  3   LYS B N   
2467 C CA  . LYS B 24  ? 0.5214 0.6431 0.5121 0.1100  0.0021  0.1131  3   LYS B CA  
2468 C C   . LYS B 24  ? 0.4706 0.6244 0.4714 0.0981  -0.0143 0.1041  3   LYS B C   
2469 O O   . LYS B 24  ? 0.4060 0.5554 0.3947 0.0889  -0.0242 0.0977  3   LYS B O   
2470 C CB  . LYS B 24  ? 0.5436 0.6367 0.5253 0.1054  0.0123  0.1051  3   LYS B CB  
2471 C CG  . LYS B 24  ? 0.5547 0.6174 0.5283 0.1164  0.0297  0.1115  3   LYS B CG  
2472 C CD  . LYS B 24  ? 0.6399 0.6734 0.5996 0.1095  0.0388  0.1014  3   LYS B CD  
2473 C CE  . LYS B 24  ? 0.8906 0.8849 0.8321 0.1142  0.0535  0.1017  3   LYS B CE  
2474 N NZ  . LYS B 24  ? 0.8843 0.8786 0.8372 0.1314  0.0646  0.1153  3   LYS B NZ  
2475 N N   . PRO B 25  ? 0.4901 0.6777 0.5138 0.0977  -0.0170 0.1026  4   PRO B N   
2476 C CA  . PRO B 25  ? 0.4787 0.6933 0.5132 0.0846  -0.0304 0.0912  4   PRO B CA  
2477 C C   . PRO B 25  ? 0.3630 0.5466 0.3805 0.0710  -0.0324 0.0785  4   PRO B C   
2478 O O   . PRO B 25  ? 0.3451 0.5002 0.3529 0.0703  -0.0224 0.0769  4   PRO B O   
2479 C CB  . PRO B 25  ? 0.4447 0.6933 0.5059 0.0863  -0.0278 0.0910  4   PRO B CB  
2480 C CG  . PRO B 25  ? 0.5358 0.7894 0.6031 0.1035  -0.0171 0.1055  4   PRO B CG  
2481 C CD  . PRO B 25  ? 0.5445 0.7494 0.5867 0.1090  -0.0073 0.1105  4   PRO B CD  
2482 N N   . ILE B 26  ? 0.3572 0.5494 0.3716 0.0608  -0.0452 0.0698  5   ILE B N   
2483 C CA  . ILE B 26  ? 0.3444 0.5105 0.3422 0.0492  -0.0485 0.0587  5   ILE B CA  
2484 C C   . ILE B 26  ? 0.2815 0.4638 0.2971 0.0399  -0.0516 0.0494  5   ILE B C   
2485 O O   . ILE B 26  ? 0.2716 0.4904 0.3087 0.0364  -0.0595 0.0454  5   ILE B O   
2486 C CB  . ILE B 26  ? 0.3270 0.4916 0.3105 0.0439  -0.0599 0.0543  5   ILE B CB  
2487 C CG1 . ILE B 26  ? 0.3857 0.5290 0.3506 0.0519  -0.0544 0.0634  5   ILE B CG1 
2488 C CG2 . ILE B 26  ? 0.3423 0.4860 0.3112 0.0327  -0.0643 0.0426  5   ILE B CG2 
2489 C CD1 . ILE B 26  ? 0.3721 0.5226 0.3272 0.0484  -0.0652 0.0621  5   ILE B CD1 
2490 N N   . VAL B 27  ? 0.2699 0.4259 0.2772 0.0357  -0.0445 0.0459  6   VAL B N   
2491 C CA  . VAL B 27  ? 0.3038 0.4672 0.3262 0.0268  -0.0446 0.0383  6   VAL B CA  
2492 C C   . VAL B 27  ? 0.2287 0.3660 0.2328 0.0188  -0.0481 0.0310  6   VAL B C   
2493 O O   . VAL B 27  ? 0.3029 0.4099 0.2832 0.0212  -0.0427 0.0334  6   VAL B O   
2494 C CB  . VAL B 27  ? 0.2868 0.4456 0.3181 0.0303  -0.0313 0.0432  6   VAL B CB  
2495 C CG1 . VAL B 27  ? 0.2863 0.4521 0.3343 0.0202  -0.0303 0.0359  6   VAL B CG1 
2496 C CG2 . VAL B 27  ? 0.3061 0.4912 0.3540 0.0403  -0.0274 0.0513  6   VAL B CG2 
2497 N N   . PHE B 28  ? 0.2218 0.3721 0.2374 0.0096  -0.0565 0.0216  7   PHE B N   
2498 C CA  . PHE B 28  ? 0.2428 0.3720 0.2435 0.0032  -0.0606 0.0149  7   PHE B CA  
2499 C C   . PHE B 28  ? 0.2279 0.3539 0.2433 -0.0034 -0.0555 0.0110  7   PHE B C   
2500 O O   . PHE B 28  ? 0.2807 0.4314 0.3226 -0.0084 -0.0563 0.0061  7   PHE B O   
2501 C CB  . PHE B 28  ? 0.2019 0.3460 0.2018 -0.0016 -0.0748 0.0067  7   PHE B CB  
2502 C CG  . PHE B 28  ? 0.2332 0.3566 0.2159 -0.0064 -0.0794 0.0003  7   PHE B CG  
2503 C CD1 . PHE B 28  ? 0.2466 0.3677 0.2409 -0.0130 -0.0794 -0.0063 7   PHE B CD1 
2504 C CD2 . PHE B 28  ? 0.2948 0.4016 0.2503 -0.0043 -0.0830 0.0010  7   PHE B CD2 
2505 C CE1 . PHE B 28  ? 0.2476 0.3507 0.2264 -0.0155 -0.0832 -0.0108 7   PHE B CE1 
2506 C CE2 . PHE B 28  ? 0.2962 0.3878 0.2358 -0.0080 -0.0874 -0.0049 7   PHE B CE2 
2507 C CZ  . PHE B 28  ? 0.2563 0.3464 0.2075 -0.0127 -0.0877 -0.0101 7   PHE B CZ  
2508 N N   . SER B 29  ? 0.2575 0.3545 0.2558 -0.0035 -0.0496 0.0131  8   SER B N   
2509 C CA  . SER B 29  ? 0.2967 0.3857 0.3063 -0.0090 -0.0436 0.0114  8   SER B CA  
2510 C C   . SER B 29  ? 0.2635 0.3303 0.2539 -0.0106 -0.0467 0.0093  8   SER B C   
2511 O O   . SER B 29  ? 0.3294 0.3792 0.2930 -0.0059 -0.0467 0.0127  8   SER B O   
2512 C CB  . SER B 29  ? 0.3830 0.4618 0.3941 -0.0056 -0.0292 0.0202  8   SER B CB  
2513 O OG  . SER B 29  ? 0.5329 0.6072 0.5590 -0.0118 -0.0228 0.0192  8   SER B OG  
2514 N N   . GLY B 30  ? 0.3160 0.3839 0.3208 -0.0171 -0.0487 0.0030  9   GLY B N   
2515 C CA  . GLY B 30  ? 0.3338 0.3816 0.3236 -0.0173 -0.0504 0.0021  9   GLY B CA  
2516 C C   . GLY B 30  ? 0.3690 0.3966 0.3580 -0.0161 -0.0373 0.0106  9   GLY B C   
2517 O O   . GLY B 30  ? 0.4145 0.4465 0.4249 -0.0196 -0.0285 0.0125  9   GLY B O   
2518 N N   . ALA B 31  ? 0.4010 0.4087 0.3651 -0.0113 -0.0357 0.0160  10  ALA B N   
2519 C CA  . ALA B 31  ? 0.4150 0.4043 0.3735 -0.0084 -0.0233 0.0263  10  ALA B CA  
2520 C C   . ALA B 31  ? 0.4033 0.3796 0.3538 -0.0070 -0.0258 0.0266  10  ALA B C   
2521 O O   . ALA B 31  ? 0.3834 0.3565 0.3101 -0.0027 -0.0329 0.0254  10  ALA B O   
2522 C CB  . ALA B 31  ? 0.3920 0.3734 0.3257 -0.0018 -0.0169 0.0346  10  ALA B CB  
2523 N N   . GLN B 32  ? 0.4201 0.3891 0.3905 -0.0104 -0.0192 0.0282  11  GLN B N   
2524 C CA  . GLN B 32  ? 0.4207 0.3755 0.3860 -0.0076 -0.0195 0.0303  11  GLN B CA  
2525 C C   . GLN B 32  ? 0.4492 0.3901 0.3862 0.0018  -0.0130 0.0439  11  GLN B C   
2526 O O   . GLN B 32  ? 0.4281 0.3643 0.3623 0.0036  -0.0018 0.0540  11  GLN B O   
2527 C CB  . GLN B 32  ? 0.5198 0.4671 0.5151 -0.0136 -0.0106 0.0298  11  GLN B CB  
2528 C CG  . GLN B 32  ? 0.6131 0.5510 0.6141 -0.0133 -0.0142 0.0252  11  GLN B CG  
2529 C CD  . GLN B 32  ? 0.4941 0.4492 0.4978 -0.0168 -0.0300 0.0091  11  GLN B CD  
2530 O OE1 . GLN B 32  ? 0.5769 0.5295 0.5634 -0.0114 -0.0384 0.0073  11  GLN B OE1 
2531 N NE2 . GLN B 32  ? 0.5616 0.5369 0.5869 -0.0258 -0.0342 -0.0025 11  GLN B NE2 
2532 N N   . PRO B 33  ? 0.3975 0.3350 0.3130 0.0079  -0.0197 0.0442  12  PRO B N   
2533 C CA  . PRO B 33  ? 0.4166 0.3460 0.3053 0.0170  -0.0132 0.0570  12  PRO B CA  
2534 C C   . PRO B 33  ? 0.5224 0.4371 0.4202 0.0201  0.0014  0.0716  12  PRO B C   
2535 O O   . PRO B 33  ? 0.5163 0.4286 0.3994 0.0249  0.0107  0.0834  12  PRO B O   
2536 C CB  . PRO B 33  ? 0.4717 0.4035 0.3416 0.0221  -0.0239 0.0528  12  PRO B CB  
2537 C CG  . PRO B 33  ? 0.4222 0.3656 0.3025 0.0152  -0.0372 0.0367  12  PRO B CG  
2538 C CD  . PRO B 33  ? 0.3705 0.3149 0.2839 0.0069  -0.0336 0.0324  12  PRO B CD  
2539 N N   . SER B 34  ? 0.5167 0.4216 0.4387 0.0171  0.0045  0.0710  13  SER B N   
2540 C CA  . SER B 34  ? 0.6381 0.5263 0.5710 0.0193  0.0199  0.0856  13  SER B CA  
2541 C C   . SER B 34  ? 0.6912 0.5795 0.6453 0.0112  0.0306  0.0872  13  SER B C   
2542 O O   . SER B 34  ? 0.7723 0.6479 0.7336 0.0123  0.0449  0.1005  13  SER B O   
2543 C CB  . SER B 34  ? 0.6821 0.5568 0.6340 0.0190  0.0210  0.0837  13  SER B CB  
2544 O OG  . SER B 34  ? 0.9064 0.7823 0.8916 0.0068  0.0222  0.0714  13  SER B OG  
2545 N N   . GLY B 35  ? 0.7644 0.6682 0.7287 0.0035  0.0243  0.0748  14  GLY B N   
2546 C CA  . GLY B 35  ? 0.7575 0.6659 0.7436 -0.0042 0.0334  0.0746  14  GLY B CA  
2547 C C   . GLY B 35  ? 0.8665 0.7696 0.8409 0.0002  0.0465  0.0901  14  GLY B C   
2548 O O   . GLY B 35  ? 0.9536 0.8585 0.8996 0.0083  0.0453  0.0965  14  GLY B O   
2549 N N   . GLU B 36  ? 0.9197 0.8179 0.9161 -0.0058 0.0597  0.0952  15  GLU B N   
2550 C CA  . GLU B 36  ? 0.8691 0.7645 0.8585 -0.0031 0.0732  0.1094  15  GLU B CA  
2551 C C   . GLU B 36  ? 0.8881 0.7994 0.8949 -0.0107 0.0758  0.1024  15  GLU B C   
2552 O O   . GLU B 36  ? 0.8782 0.7926 0.9145 -0.0205 0.0800  0.0959  15  GLU B O   
2553 C CB  . GLU B 36  ? 0.8313 0.7074 0.8313 -0.0031 0.0881  0.1235  15  GLU B CB  
2554 N N   . LEU B 37  ? 0.8146 0.7372 0.8038 -0.0061 0.0738  0.1029  16  LEU B N   
2555 C CA  . LEU B 37  ? 0.7200 0.6587 0.7237 -0.0107 0.0767  0.0978  16  LEU B CA  
2556 C C   . LEU B 37  ? 0.6428 0.5782 0.6570 -0.0135 0.0934  0.1089  16  LEU B C   
2557 O O   . LEU B 37  ? 0.6005 0.5270 0.5964 -0.0075 0.1018  0.1222  16  LEU B O   
2558 C CB  . LEU B 37  ? 0.6695 0.6182 0.6511 -0.0041 0.0707  0.0950  16  LEU B CB  
2559 C CG  . LEU B 37  ? 0.5808 0.5365 0.5552 -0.0028 0.0548  0.0830  16  LEU B CG  
2560 C CD1 . LEU B 37  ? 0.6204 0.5818 0.5732 0.0035  0.0525  0.0818  16  LEU B CD1 
2561 C CD2 . LEU B 37  ? 0.6010 0.5713 0.6040 -0.0106 0.0486  0.0714  16  LEU B CD2 
2562 N N   . THR B 38  ? 0.6610 0.6061 0.7047 -0.0231 0.0984  0.1030  17  THR B N   
2563 C CA  . THR B 38  ? 0.5991 0.5435 0.6557 -0.0276 0.1146  0.1119  17  THR B CA  
2564 C C   . THR B 38  ? 0.6159 0.5792 0.6705 -0.0254 0.1170  0.1109  17  THR B C   
2565 O O   . THR B 38  ? 0.5335 0.5093 0.5799 -0.0209 0.1069  0.1031  17  THR B O   
2566 C CB  . THR B 38  ? 0.6096 0.5551 0.7011 -0.0406 0.1207  0.1051  17  THR B CB  
2567 O OG1 . THR B 38  ? 0.5348 0.5061 0.6458 -0.0466 0.1140  0.0902  17  THR B OG1 
2568 C CG2 . THR B 38  ? 0.6734 0.6015 0.7704 -0.0429 0.1168  0.1021  17  THR B CG2 
2569 N N   . ILE B 39  ? 0.6620 0.6268 0.7251 -0.0287 0.1316  0.1193  18  ILE B N   
2570 C CA  . ILE B 39  ? 0.5734 0.5577 0.6397 -0.0274 0.1357  0.1177  18  ILE B CA  
2571 C C   . ILE B 39  ? 0.5589 0.5658 0.6508 -0.0336 0.1291  0.1032  18  ILE B C   
2572 O O   . ILE B 39  ? 0.4901 0.5150 0.5811 -0.0290 0.1261  0.0989  18  ILE B O   
2573 C CB  . ILE B 39  ? 0.5554 0.5379 0.6276 -0.0309 0.1532  0.1296  18  ILE B CB  
2574 C CG1 . ILE B 39  ? 0.7891 0.7819 0.8434 -0.0226 0.1574  0.1343  18  ILE B CG1 
2575 C CG2 . ILE B 39  ? 0.5461 0.5406 0.6534 -0.0439 0.1610  0.1237  18  ILE B CG2 
2576 C CD1 . ILE B 39  ? 0.8035 0.7841 0.8239 -0.0123 0.1551  0.1421  18  ILE B CD1 
2577 N N   . GLY B 40  ? 0.5604 0.5681 0.6760 -0.0438 0.1274  0.0953  19  GLY B N   
2578 C CA  . GLY B 40  ? 0.5832 0.6169 0.7222 -0.0496 0.1198  0.0804  19  GLY B CA  
2579 C C   . GLY B 40  ? 0.5297 0.5706 0.6549 -0.0416 0.1032  0.0734  19  GLY B C   
2580 O O   . GLY B 40  ? 0.5234 0.5886 0.6557 -0.0390 0.0978  0.0671  19  GLY B O   
2581 N N   . ASN B 41  ? 0.5291 0.5501 0.6346 -0.0372 0.0955  0.0750  20  ASN B N   
2582 C CA  . ASN B 41  ? 0.5677 0.5938 0.6579 -0.0301 0.0805  0.0690  20  ASN B CA  
2583 C C   . ASN B 41  ? 0.5574 0.5882 0.6284 -0.0197 0.0809  0.0737  20  ASN B C   
2584 O O   . ASN B 41  ? 0.5214 0.5652 0.5898 -0.0151 0.0716  0.0679  20  ASN B O   
2585 C CB  . ASN B 41  ? 0.5298 0.5337 0.6002 -0.0271 0.0736  0.0708  20  ASN B CB  
2586 C CG  . ASN B 41  ? 0.5944 0.5944 0.6844 -0.0362 0.0710  0.0633  20  ASN B CG  
2587 O OD1 . ASN B 41  ? 0.6729 0.6517 0.7605 -0.0375 0.0772  0.0698  20  ASN B OD1 
2588 N ND2 . ASN B 41  ? 0.6108 0.6324 0.7210 -0.0422 0.0624  0.0498  20  ASN B ND2 
2589 N N   . TYR B 42  ? 0.4676 0.4882 0.5256 -0.0159 0.0923  0.0841  21  TYR B N   
2590 C CA  . TYR B 42  ? 0.5292 0.5515 0.5676 -0.0062 0.0939  0.0873  21  TYR B CA  
2591 C C   . TYR B 42  ? 0.5781 0.6231 0.6346 -0.0054 0.0990  0.0852  21  TYR B C   
2592 O O   . TYR B 42  ? 0.5018 0.5594 0.5589 0.0002  0.0924  0.0801  21  TYR B O   
2593 C CB  . TYR B 42  ? 0.5041 0.5098 0.5205 -0.0024 0.1039  0.0983  21  TYR B CB  
2594 C CG  . TYR B 42  ? 0.5243 0.5309 0.5197 0.0066  0.1068  0.0997  21  TYR B CG  
2595 C CD1 . TYR B 42  ? 0.5398 0.5420 0.5161 0.0125  0.0974  0.0941  21  TYR B CD1 
2596 C CD2 . TYR B 42  ? 0.5849 0.5965 0.5798 0.0084  0.1197  0.1057  21  TYR B CD2 
2597 C CE1 . TYR B 42  ? 0.4706 0.4719 0.4289 0.0197  0.1016  0.0937  21  TYR B CE1 
2598 C CE2 . TYR B 42  ? 0.5623 0.5747 0.5391 0.0162  0.1233  0.1052  21  TYR B CE2 
2599 C CZ  . TYR B 42  ? 0.5654 0.5717 0.5243 0.0216  0.1146  0.0988  21  TYR B CZ  
2600 O OH  . TYR B 42  ? 0.6159 0.6212 0.5579 0.0284  0.1197  0.0967  21  TYR B OH  
2601 N N   . MET B 43  ? 0.6222 0.6736 0.6942 -0.0106 0.1113  0.0895  22  MET B N   
2602 C CA  . MET B 43  ? 0.6025 0.6772 0.6903 -0.0088 0.1171  0.0880  22  MET B CA  
2603 C C   . MET B 43  ? 0.5030 0.6036 0.6154 -0.0121 0.1086  0.0781  22  MET B C   
2604 O O   . MET B 43  ? 0.5217 0.6433 0.6415 -0.0058 0.1083  0.0762  22  MET B O   
2605 C CB  . MET B 43  ? 0.6223 0.6999 0.7223 -0.0153 0.1321  0.0942  22  MET B CB  
2606 C CG  . MET B 43  ? 0.6031 0.6601 0.6792 -0.0116 0.1412  0.1053  22  MET B CG  
2607 S SD  . MET B 43  ? 0.5792 0.6440 0.6678 -0.0172 0.1598  0.1137  22  MET B SD  
2608 C CE  . MET B 43  ? 0.6856 0.7410 0.7956 -0.0319 0.1640  0.1150  22  MET B CE  
2609 N N   . GLY B 44  ? 0.6235 0.7248 0.7492 -0.0212 0.1023  0.0716  23  GLY B N   
2610 C CA  . GLY B 44  ? 0.5772 0.7069 0.7262 -0.0252 0.0938  0.0610  23  GLY B CA  
2611 C C   . GLY B 44  ? 0.6271 0.7624 0.7639 -0.0155 0.0806  0.0582  23  GLY B C   
2612 O O   . GLY B 44  ? 0.7021 0.8632 0.8489 -0.0097 0.0781  0.0563  23  GLY B O   
2613 N N   . ALA B 45  ? 0.5538 0.6662 0.6693 -0.0132 0.0725  0.0585  24  ALA B N   
2614 C CA  . ALA B 45  ? 0.5345 0.6515 0.6398 -0.0064 0.0596  0.0550  24  ALA B CA  
2615 C C   . ALA B 45  ? 0.5163 0.6097 0.5897 0.0039  0.0593  0.0611  24  ALA B C   
2616 O O   . ALA B 45  ? 0.5180 0.6184 0.5859 0.0131  0.0583  0.0627  24  ALA B O   
2617 C CB  . ALA B 45  ? 0.4924 0.6085 0.6028 -0.0142 0.0486  0.0467  24  ALA B CB  
2618 N N   . LEU B 46  ? 0.5389 0.6427 0.5740 -0.0241 -0.0011 -0.0398 25  LEU B N   
2619 C CA  . LEU B 46  ? 0.5133 0.6000 0.5363 -0.0185 -0.0021 -0.0308 25  LEU B CA  
2620 C C   . LEU B 46  ? 0.4990 0.5881 0.5256 -0.0141 0.0006  -0.0308 25  LEU B C   
2621 O O   . LEU B 46  ? 0.4461 0.5268 0.4658 -0.0067 -0.0016 -0.0251 25  LEU B O   
2622 C CB  . LEU B 46  ? 0.4213 0.4876 0.4318 -0.0253 0.0021  -0.0260 25  LEU B CB  
2623 C CG  . LEU B 46  ? 0.4561 0.5058 0.4544 -0.0207 0.0010  -0.0180 25  LEU B CG  
2624 C CD1 . LEU B 46  ? 0.4891 0.5389 0.4842 -0.0128 -0.0058 -0.0143 25  LEU B CD1 
2625 C CD2 . LEU B 46  ? 0.4324 0.4653 0.4194 -0.0266 0.0040  -0.0146 25  LEU B CD2 
2626 N N   . ARG B 47  ? 0.4555 0.5551 0.4925 -0.0190 0.0060  -0.0376 26  ARG B N   
2627 C CA  . ARG B 47  ? 0.4852 0.5880 0.5265 -0.0148 0.0089  -0.0383 26  ARG B CA  
2628 C C   . ARG B 47  ? 0.4257 0.5426 0.4738 -0.0026 0.0023  -0.0394 26  ARG B C   
2629 O O   . ARG B 47  ? 0.4177 0.5295 0.4625 0.0047  0.0024  -0.0358 26  ARG B O   
2630 C CB  . ARG B 47  ? 0.4401 0.5518 0.4917 -0.0235 0.0170  -0.0464 26  ARG B CB  
2631 C CG  . ARG B 47  ? 0.5213 0.6361 0.5777 -0.0203 0.0212  -0.0478 26  ARG B CG  
2632 C CD  . ARG B 47  ? 0.4545 0.5739 0.5183 -0.0309 0.0310  -0.0554 26  ARG B CD  
2633 N NE  . ARG B 47  ? 0.5578 0.6998 0.6381 -0.0351 0.0314  -0.0662 26  ARG B NE  
2634 C CZ  . ARG B 47  ? 0.4891 0.6395 0.5792 -0.0448 0.0404  -0.0754 26  ARG B CZ  
2635 N NH1 . ARG B 47  ? 0.5499 0.6869 0.6339 -0.0510 0.0499  -0.0745 26  ARG B NH1 
2636 N NH2 . ARG B 47  ? 0.5446 0.7176 0.6508 -0.0488 0.0402  -0.0864 26  ARG B NH2 
2637 N N   . GLN B 48  ? 0.4477 0.5817 0.5041 0.0003  -0.0035 -0.0446 27  GLN B N   
2638 C CA  . GLN B 48  ? 0.5325 0.6786 0.5923 0.0138  -0.0109 -0.0451 27  GLN B CA  
2639 C C   . GLN B 48  ? 0.3890 0.5174 0.4326 0.0217  -0.0157 -0.0353 27  GLN B C   
2640 O O   . GLN B 48  ? 0.4396 0.5642 0.4786 0.0325  -0.0177 -0.0317 27  GLN B O   
2641 C CB  . GLN B 48  ? 0.5552 0.7260 0.6281 0.0149  -0.0162 -0.0542 27  GLN B CB  
2642 N N   . TRP B 49  ? 0.4139 0.5304 0.4483 0.0163  -0.0167 -0.0313 28  TRP B N   
2643 C CA  . TRP B 49  ? 0.4303 0.5303 0.4498 0.0225  -0.0201 -0.0231 28  TRP B CA  
2644 C C   . TRP B 49  ? 0.4540 0.5367 0.4645 0.0251  -0.0159 -0.0170 28  TRP B C   
2645 O O   . TRP B 49  ? 0.4499 0.5228 0.4507 0.0337  -0.0179 -0.0120 28  TRP B O   
2646 C CB  . TRP B 49  ? 0.4701 0.5599 0.4824 0.0147  -0.0205 -0.0206 28  TRP B CB  
2647 C CG  . TRP B 49  ? 0.5274 0.6315 0.5463 0.0121  -0.0246 -0.0262 28  TRP B CG  
2648 C CD1 . TRP B 49  ? 0.5805 0.7064 0.6104 0.0170  -0.0291 -0.0332 28  TRP B CD1 
2649 C CD2 . TRP B 49  ? 0.5622 0.6607 0.5774 0.0040  -0.0244 -0.0260 28  TRP B CD2 
2650 N NE1 . TRP B 49  ? 0.6382 0.7725 0.6715 0.0117  -0.0317 -0.0378 28  TRP B NE1 
2651 C CE2 . TRP B 49  ? 0.5764 0.6932 0.6004 0.0036  -0.0285 -0.0332 28  TRP B CE2 
2652 C CE3 . TRP B 49  ? 0.6212 0.7016 0.6265 -0.0023 -0.0214 -0.0210 28  TRP B CE3 
2653 C CZ2 . TRP B 49  ? 0.5624 0.6784 0.5851 -0.0037 -0.0290 -0.0351 28  TRP B CZ2 
2654 C CZ3 . TRP B 49  ? 0.6209 0.7004 0.6249 -0.0086 -0.0221 -0.0226 28  TRP B CZ3 
2655 C CH2 . TRP B 49  ? 0.5638 0.6602 0.5762 -0.0096 -0.0255 -0.0295 28  TRP B CH2 
2656 N N   . VAL B 50  ? 0.4002 0.4781 0.4127 0.0176  -0.0095 -0.0176 29  VAL B N   
2657 C CA  . VAL B 50  ? 0.3668 0.4297 0.3714 0.0192  -0.0052 -0.0129 29  VAL B CA  
2658 C C   . VAL B 50  ? 0.4087 0.4763 0.4158 0.0299  -0.0057 -0.0133 29  VAL B C   
2659 O O   . VAL B 50  ? 0.3987 0.4524 0.3958 0.0356  -0.0046 -0.0083 29  VAL B O   
2660 C CB  . VAL B 50  ? 0.4114 0.4699 0.4173 0.0096  0.0014  -0.0143 29  VAL B CB  
2661 C CG1 . VAL B 50  ? 0.3471 0.3949 0.3478 0.0119  0.0059  -0.0115 29  VAL B CG1 
2662 C CG2 . VAL B 50  ? 0.3792 0.4270 0.3776 0.0014  0.0019  -0.0119 29  VAL B CG2 
2663 N N   . ASN B 51  ? 0.4353 0.5223 0.4556 0.0329  -0.0069 -0.0197 30  ASN B N   
2664 C CA  . ASN B 51  ? 0.4179 0.5109 0.4414 0.0442  -0.0076 -0.0208 30  ASN B CA  
2665 C C   . ASN B 51  ? 0.4533 0.5457 0.4696 0.0572  -0.0144 -0.0180 30  ASN B C   
2666 O O   . ASN B 51  ? 0.5361 0.6287 0.5508 0.0687  -0.0150 -0.0173 30  ASN B O   
2667 C CB  . ASN B 51  ? 0.4842 0.6004 0.5257 0.0433  -0.0066 -0.0299 30  ASN B CB  
2668 C CG  . ASN B 51  ? 0.6133 0.7267 0.6593 0.0321  0.0018  -0.0323 30  ASN B CG  
2669 O OD1 . ASN B 51  ? 0.6468 0.7430 0.6835 0.0302  0.0066  -0.0274 30  ASN B OD1 
2670 N ND2 . ASN B 51  ? 0.5692 0.6992 0.6288 0.0243  0.0041  -0.0405 30  ASN B ND2 
2671 N N   . MET B 52  ? 0.4771 0.5676 0.4878 0.0562  -0.0191 -0.0161 31  MET B N   
2672 C CA  . MET B 52  ? 0.4728 0.5620 0.4747 0.0683  -0.0256 -0.0135 31  MET B CA  
2673 C C   . MET B 52  ? 0.4768 0.5414 0.4604 0.0681  -0.0243 -0.0054 31  MET B C   
2674 O O   . MET B 52  ? 0.4709 0.5321 0.4454 0.0745  -0.0292 -0.0030 31  MET B O   
2675 C CB  . MET B 52  ? 0.4952 0.6052 0.5062 0.0685  -0.0326 -0.0196 31  MET B CB  
2676 C CG  . MET B 52  ? 0.5516 0.6886 0.5824 0.0688  -0.0336 -0.0295 31  MET B CG  
2677 S SD  . MET B 52  ? 0.8132 0.9775 0.8557 0.0694  -0.0420 -0.0385 31  MET B SD  
2678 C CE  . MET B 52  ? 0.6192 0.7739 0.6594 0.0517  -0.0384 -0.0374 31  MET B CE  
2679 N N   . GLN B 53  ? 0.3586 0.4066 0.3365 0.0606  -0.0177 -0.0017 32  GLN B N   
2680 C CA  . GLN B 53  ? 0.4315 0.4576 0.3936 0.0597  -0.0156 0.0044  32  GLN B CA  
2681 C C   . GLN B 53  ? 0.4514 0.4628 0.4000 0.0715  -0.0142 0.0088  32  GLN B C   
2682 O O   . GLN B 53  ? 0.4680 0.4618 0.4024 0.0723  -0.0125 0.0133  32  GLN B O   
2683 C CB  . GLN B 53  ? 0.3243 0.3394 0.2852 0.0486  -0.0093 0.0057  32  GLN B CB  
2684 C CG  . GLN B 53  ? 0.4317 0.4559 0.4015 0.0374  -0.0099 0.0025  32  GLN B CG  
2685 C CD  . GLN B 53  ? 0.3500 0.3631 0.3167 0.0285  -0.0046 0.0037  32  GLN B CD  
2686 O OE1 . GLN B 53  ? 0.3708 0.3721 0.3292 0.0251  -0.0038 0.0064  32  GLN B OE1 
2687 N NE2 . GLN B 53  ? 0.3566 0.3741 0.3298 0.0251  -0.0009 0.0012  32  GLN B NE2 
2688 N N   . ASP B 54  ? 0.4726 0.4899 0.4248 0.0807  -0.0139 0.0073  33  ASP B N   
2689 C CA  . ASP B 54  ? 0.6028 0.6056 0.5407 0.0941  -0.0128 0.0115  33  ASP B CA  
2690 C C   . ASP B 54  ? 0.6181 0.6284 0.5513 0.1069  -0.0208 0.0115  33  ASP B C   
2691 O O   . ASP B 54  ? 0.5195 0.5129 0.4354 0.1182  -0.0201 0.0163  33  ASP B O   
2692 C CB  . ASP B 54  ? 0.6722 0.6764 0.6148 0.0996  -0.0088 0.0100  33  ASP B CB  
2693 C CG  . ASP B 54  ? 0.7635 0.7532 0.7039 0.0898  0.0001  0.0114  33  ASP B CG  
2694 O OD1 . ASP B 54  ? 0.8159 0.7872 0.7447 0.0840  0.0040  0.0150  33  ASP B OD1 
2695 O OD2 . ASP B 54  ? 1.0310 1.0283 0.9815 0.0879  0.0032  0.0082  33  ASP B OD2 
2696 N N   . ASP B 55  ? 0.5386 0.5729 0.4856 0.1054  -0.0279 0.0060  34  ASP B N   
2697 C CA  . ASP B 55  ? 0.5453 0.5906 0.4893 0.1173  -0.0365 0.0046  34  ASP B CA  
2698 C C   . ASP B 55  ? 0.5282 0.5667 0.4627 0.1131  -0.0395 0.0071  34  ASP B C   
2699 O O   . ASP B 55  ? 0.5798 0.6168 0.5030 0.1244  -0.0452 0.0086  34  ASP B O   
2700 C CB  . ASP B 55  ? 0.5050 0.5829 0.4705 0.1180  -0.0425 -0.0046 34  ASP B CB  
2701 C CG  . ASP B 55  ? 0.6282 0.7151 0.6052 0.1213  -0.0392 -0.0082 34  ASP B CG  
2702 O OD1 . ASP B 55  ? 0.6573 0.7280 0.6229 0.1310  -0.0356 -0.0035 34  ASP B OD1 
2703 O OD2 . ASP B 55  ? 0.6501 0.7592 0.6469 0.1139  -0.0393 -0.0159 34  ASP B OD2 
2704 N N   . TYR B 56  ? 0.4963 0.5304 0.4343 0.0979  -0.0360 0.0074  35  TYR B N   
2705 C CA  . TYR B 56  ? 0.4842 0.5117 0.4144 0.0926  -0.0379 0.0093  35  TYR B CA  
2706 C C   . TYR B 56  ? 0.4558 0.4604 0.3765 0.0832  -0.0301 0.0141  35  TYR B C   
2707 O O   . TYR B 56  ? 0.5053 0.5048 0.4302 0.0772  -0.0242 0.0143  35  TYR B O   
2708 C CB  . TYR B 56  ? 0.4522 0.5010 0.3983 0.0828  -0.0421 0.0030  35  TYR B CB  
2709 C CG  . TYR B 56  ? 0.4530 0.5283 0.4117 0.0897  -0.0495 -0.0041 35  TYR B CG  
2710 C CD1 . TYR B 56  ? 0.4999 0.5916 0.4737 0.0910  -0.0488 -0.0094 35  TYR B CD1 
2711 C CD2 . TYR B 56  ? 0.5160 0.6013 0.4722 0.0944  -0.0570 -0.0064 35  TYR B CD2 
2712 C CE1 . TYR B 56  ? 0.4807 0.5994 0.4680 0.0969  -0.0554 -0.0175 35  TYR B CE1 
2713 C CE2 . TYR B 56  ? 0.6310 0.7433 0.6000 0.1006  -0.0642 -0.0144 35  TYR B CE2 
2714 C CZ  . TYR B 56  ? 0.5154 0.6450 0.5006 0.1017  -0.0633 -0.0203 35  TYR B CZ  
2715 O OH  . TYR B 56  ? 0.6738 0.8327 0.6735 0.1075  -0.0702 -0.0297 35  TYR B OH  
2716 N N   . HIS B 57  ? 0.4312 0.4227 0.3391 0.0820  -0.0302 0.0173  36  HIS B N   
2717 C CA  . HIS B 57  ? 0.4389 0.4142 0.3415 0.0712  -0.0239 0.0197  36  HIS B CA  
2718 C C   . HIS B 57  ? 0.3589 0.3474 0.2736 0.0599  -0.0268 0.0161  36  HIS B C   
2719 O O   . HIS B 57  ? 0.4361 0.4270 0.3479 0.0591  -0.0307 0.0158  36  HIS B O   
2720 C CB  . HIS B 57  ? 0.4437 0.3972 0.3263 0.0751  -0.0212 0.0244  36  HIS B CB  
2721 C CG  . HIS B 57  ? 0.5924 0.5303 0.4705 0.0643  -0.0139 0.0256  36  HIS B CG  
2722 N ND1 . HIS B 57  ? 0.6871 0.6034 0.5479 0.0652  -0.0086 0.0288  36  HIS B ND1 
2723 C CD2 . HIS B 57  ? 0.6761 0.6175 0.5647 0.0529  -0.0109 0.0233  36  HIS B CD2 
2724 C CE1 . HIS B 57  ? 0.5789 0.4883 0.4419 0.0542  -0.0029 0.0276  36  HIS B CE1 
2725 N NE2 . HIS B 57  ? 0.6519 0.5765 0.5312 0.0473  -0.0048 0.0244  36  HIS B NE2 
2726 N N   . CYS B 58  ? 0.3340 0.3299 0.2612 0.0515  -0.0244 0.0135  37  CYS B N   
2727 C CA  . CYS B 58  ? 0.3329 0.3398 0.2706 0.0414  -0.0261 0.0101  37  CYS B CA  
2728 C C   . CYS B 58  ? 0.3873 0.3811 0.3196 0.0330  -0.0224 0.0120  37  CYS B C   
2729 O O   . CYS B 58  ? 0.3644 0.3456 0.2917 0.0313  -0.0171 0.0140  37  CYS B O   
2730 C CB  . CYS B 58  ? 0.3489 0.3683 0.3004 0.0371  -0.0247 0.0063  37  CYS B CB  
2731 S SG  . CYS B 58  ? 0.4250 0.4641 0.3866 0.0462  -0.0288 0.0019  37  CYS B SG  
2732 N N   . ILE B 59  ? 0.3622 0.3600 0.2964 0.0277  -0.0251 0.0106  38  ILE B N   
2733 C CA  . ILE B 59  ? 0.3503 0.3380 0.2802 0.0207  -0.0227 0.0117  38  ILE B CA  
2734 C C   . ILE B 59  ? 0.3451 0.3416 0.2842 0.0127  -0.0237 0.0087  38  ILE B C   
2735 O O   . ILE B 59  ? 0.3532 0.3606 0.2975 0.0119  -0.0274 0.0061  38  ILE B O   
2736 C CB  . ILE B 59  ? 0.3595 0.3396 0.2792 0.0230  -0.0242 0.0133  38  ILE B CB  
2737 C CG1 . ILE B 59  ? 0.4403 0.4082 0.3476 0.0315  -0.0221 0.0167  38  ILE B CG1 
2738 C CG2 . ILE B 59  ? 0.4040 0.3758 0.3213 0.0155  -0.0215 0.0133  38  ILE B CG2 
2739 C CD1 . ILE B 59  ? 0.4209 0.3791 0.3155 0.0345  -0.0228 0.0186  38  ILE B CD1 
2740 N N   . TYR B 60  ? 0.3294 0.3206 0.2695 0.0071  -0.0203 0.0087  39  TYR B N   
2741 C CA  . TYR B 60  ? 0.3091 0.3042 0.2544 0.0003  -0.0203 0.0067  39  TYR B CA  
2742 C C   . TYR B 60  ? 0.2792 0.2653 0.2194 -0.0033 -0.0194 0.0075  39  TYR B C   
2743 O O   . TYR B 60  ? 0.3457 0.3246 0.2827 -0.0038 -0.0166 0.0082  39  TYR B O   
2744 C CB  . TYR B 60  ? 0.3199 0.3172 0.2700 -0.0020 -0.0173 0.0058  39  TYR B CB  
2745 C CG  . TYR B 60  ? 0.3091 0.3170 0.2661 0.0011  -0.0177 0.0039  39  TYR B CG  
2746 C CD1 . TYR B 60  ? 0.3378 0.3448 0.2937 0.0073  -0.0168 0.0051  39  TYR B CD1 
2747 C CD2 . TYR B 60  ? 0.3000 0.3191 0.2649 -0.0023 -0.0185 0.0001  39  TYR B CD2 
2748 C CE1 . TYR B 60  ? 0.3791 0.3974 0.3423 0.0111  -0.0175 0.0028  39  TYR B CE1 
2749 C CE2 . TYR B 60  ? 0.3578 0.3892 0.3309 0.0004  -0.0188 -0.0031 39  TYR B CE2 
2750 C CZ  . TYR B 60  ? 0.4016 0.4333 0.3742 0.0076  -0.0188 -0.0017 39  TYR B CZ  
2751 O OH  . TYR B 60  ? 0.4855 0.5310 0.4672 0.0111  -0.0194 -0.0054 39  TYR B OH  
2752 N N   . CYS B 61  ? 0.3524 0.3400 0.2926 -0.0060 -0.0216 0.0065  40  CYS B N   
2753 C CA  . CYS B 61  ? 0.2916 0.2721 0.2277 -0.0087 -0.0212 0.0065  40  CYS B CA  
2754 C C   . CYS B 61  ? 0.2822 0.2634 0.2205 -0.0131 -0.0210 0.0052  40  CYS B C   
2755 O O   . CYS B 61  ? 0.3113 0.2973 0.2525 -0.0153 -0.0220 0.0038  40  CYS B O   
2756 C CB  . CYS B 61  ? 0.3376 0.3171 0.2699 -0.0075 -0.0232 0.0066  40  CYS B CB  
2757 S SG  . CYS B 61  ? 0.3469 0.3195 0.2756 -0.0109 -0.0225 0.0057  40  CYS B SG  
2758 N N   . ILE B 62  ? 0.3424 0.3183 0.2785 -0.0141 -0.0195 0.0052  41  ILE B N   
2759 C CA  . ILE B 62  ? 0.3539 0.3272 0.2888 -0.0167 -0.0192 0.0046  41  ILE B CA  
2760 C C   . ILE B 62  ? 0.3270 0.2972 0.2594 -0.0173 -0.0207 0.0038  41  ILE B C   
2761 O O   . ILE B 62  ? 0.2980 0.2657 0.2287 -0.0162 -0.0209 0.0031  41  ILE B O   
2762 C CB  . ILE B 62  ? 0.3182 0.2878 0.2506 -0.0160 -0.0177 0.0047  41  ILE B CB  
2763 C CG1 . ILE B 62  ? 0.3014 0.2737 0.2363 -0.0156 -0.0156 0.0053  41  ILE B CG1 
2764 C CG2 . ILE B 62  ? 0.3659 0.3303 0.2939 -0.0171 -0.0174 0.0046  41  ILE B CG2 
2765 C CD1 . ILE B 62  ? 0.3389 0.3077 0.2706 -0.0150 -0.0140 0.0051  41  ILE B CD1 
2766 N N   . VAL B 63  ? 0.3365 0.3076 0.2693 -0.0196 -0.0214 0.0032  42  VAL B N   
2767 C CA  . VAL B 63  ? 0.2983 0.2677 0.2294 -0.0202 -0.0228 0.0023  42  VAL B CA  
2768 C C   . VAL B 63  ? 0.3143 0.2774 0.2417 -0.0204 -0.0224 0.0018  42  VAL B C   
2769 O O   . VAL B 63  ? 0.3648 0.3246 0.2903 -0.0225 -0.0217 0.0012  42  VAL B O   
2770 C CB  . VAL B 63  ? 0.3579 0.3322 0.2911 -0.0223 -0.0238 0.0011  42  VAL B CB  
2771 C CG1 . VAL B 63  ? 0.3292 0.3095 0.2642 -0.0197 -0.0254 0.0016  42  VAL B CG1 
2772 C CG2 . VAL B 63  ? 0.3413 0.3170 0.2765 -0.0258 -0.0219 -0.0002 42  VAL B CG2 
2773 N N   . ASP B 64  ? 0.2856 0.2468 0.2117 -0.0178 -0.0227 0.0013  43  ASP B N   
2774 C CA  . ASP B 64  ? 0.3244 0.2806 0.2466 -0.0161 -0.0233 0.0004  43  ASP B CA  
2775 C C   . ASP B 64  ? 0.3167 0.2719 0.2388 -0.0164 -0.0242 -0.0012 43  ASP B C   
2776 O O   . ASP B 64  ? 0.3247 0.2748 0.2430 -0.0150 -0.0244 -0.0018 43  ASP B O   
2777 C CB  . ASP B 64  ? 0.2878 0.2449 0.2095 -0.0127 -0.0241 -0.0009 43  ASP B CB  
2778 C CG  . ASP B 64  ? 0.2988 0.2609 0.2249 -0.0129 -0.0239 -0.0031 43  ASP B CG  
2779 O OD1 . ASP B 64  ? 0.2934 0.2566 0.2213 -0.0150 -0.0229 -0.0026 43  ASP B OD1 
2780 O OD2 . ASP B 64  ? 0.2801 0.2447 0.2071 -0.0110 -0.0243 -0.0059 43  ASP B OD2 
2781 N N   . GLN B 65  ? 0.2972 0.2558 0.2221 -0.0178 -0.0243 -0.0020 44  GLN B N   
2782 C CA  . GLN B 65  ? 0.3441 0.3013 0.2684 -0.0187 -0.0245 -0.0037 44  GLN B CA  
2783 C C   . GLN B 65  ? 0.2748 0.2299 0.1973 -0.0214 -0.0244 -0.0031 44  GLN B C   
2784 O O   . GLN B 65  ? 0.3474 0.2990 0.2681 -0.0218 -0.0242 -0.0045 44  GLN B O   
2785 C CB  . GLN B 65  ? 0.3330 0.2923 0.2584 -0.0195 -0.0238 -0.0046 44  GLN B CB  
2786 C CG  . GLN B 65  ? 0.2808 0.2415 0.2082 -0.0182 -0.0226 -0.0072 44  GLN B CG  
2787 C CD  . GLN B 65  ? 0.3579 0.3175 0.2842 -0.0197 -0.0200 -0.0078 44  GLN B CD  
2788 O OE1 . GLN B 65  ? 0.4093 0.3679 0.3337 -0.0195 -0.0191 -0.0054 44  GLN B OE1 
2789 N NE2 . GLN B 65  ? 0.3632 0.3219 0.2898 -0.0209 -0.0182 -0.0112 44  GLN B NE2 
2790 N N   . HIS B 66  ? 0.2760 0.2339 0.1998 -0.0234 -0.0241 -0.0019 45  HIS B N   
2791 C CA  . HIS B 66  ? 0.3390 0.2959 0.2620 -0.0270 -0.0232 -0.0028 45  HIS B CA  
2792 C C   . HIS B 66  ? 0.3456 0.2942 0.2643 -0.0273 -0.0208 -0.0025 45  HIS B C   
2793 O O   . HIS B 66  ? 0.3352 0.2787 0.2511 -0.0300 -0.0190 -0.0038 45  HIS B O   
2794 C CB  . HIS B 66  ? 0.2921 0.2568 0.2192 -0.0290 -0.0235 -0.0031 45  HIS B CB  
2795 C CG  . HIS B 66  ? 0.3439 0.3150 0.2724 -0.0281 -0.0260 -0.0036 45  HIS B CG  
2796 N ND1 . HIS B 66  ? 0.2984 0.2705 0.2256 -0.0300 -0.0270 -0.0056 45  HIS B ND1 
2797 C CD2 . HIS B 66  ? 0.3743 0.3494 0.3034 -0.0249 -0.0274 -0.0022 45  HIS B CD2 
2798 C CE1 . HIS B 66  ? 0.3762 0.3527 0.3025 -0.0277 -0.0293 -0.0052 45  HIS B CE1 
2799 N NE2 . HIS B 66  ? 0.3982 0.3759 0.3252 -0.0243 -0.0294 -0.0030 45  HIS B NE2 
2800 N N   . ALA B 67  ? 0.3156 0.2616 0.2324 -0.0244 -0.0205 -0.0009 46  ALA B N   
2801 C CA  . ALA B 67  ? 0.3335 0.2693 0.2432 -0.0238 -0.0178 0.0000  46  ALA B CA  
2802 C C   . ALA B 67  ? 0.3554 0.2827 0.2590 -0.0207 -0.0180 -0.0005 46  ALA B C   
2803 O O   . ALA B 67  ? 0.3490 0.2652 0.2450 -0.0213 -0.0148 -0.0001 46  ALA B O   
2804 C CB  . ALA B 67  ? 0.3437 0.2787 0.2513 -0.0205 -0.0179 0.0017  46  ALA B CB  
2805 N N   . ILE B 68  ? 0.3888 0.3203 0.2952 -0.0172 -0.0211 -0.0017 47  ILE B N   
2806 C CA  . ILE B 68  ? 0.4082 0.3335 0.3100 -0.0130 -0.0217 -0.0028 47  ILE B CA  
2807 C C   . ILE B 68  ? 0.3728 0.2946 0.2739 -0.0163 -0.0201 -0.0042 47  ILE B C   
2808 O O   . ILE B 68  ? 0.3659 0.2829 0.2639 -0.0128 -0.0204 -0.0055 47  ILE B O   
2809 C CB  . ILE B 68  ? 0.3364 0.2693 0.2429 -0.0085 -0.0250 -0.0052 47  ILE B CB  
2810 C CG1 . ILE B 68  ? 0.3666 0.3079 0.2806 -0.0123 -0.0253 -0.0070 47  ILE B CG1 
2811 C CG2 . ILE B 68  ? 0.3465 0.2827 0.2530 -0.0050 -0.0266 -0.0047 47  ILE B CG2 
2812 C CD1 . ILE B 68  ? 0.3174 0.2650 0.2361 -0.0095 -0.0268 -0.0108 47  ILE B CD1 
2813 N N   . THR B 69  ? 0.3431 0.2680 0.2473 -0.0226 -0.0186 -0.0046 48  THR B N   
2814 C CA  . THR B 69  ? 0.3507 0.2708 0.2527 -0.0265 -0.0163 -0.0064 48  THR B CA  
2815 C C   . THR B 69  ? 0.4320 0.3378 0.3248 -0.0268 -0.0119 -0.0057 48  THR B C   
2816 O O   . THR B 69  ? 0.3970 0.2957 0.2861 -0.0293 -0.0091 -0.0074 48  THR B O   
2817 C CB  . THR B 69  ? 0.3183 0.2468 0.2257 -0.0329 -0.0161 -0.0080 48  THR B CB  
2818 O OG1 . THR B 69  ? 0.3762 0.3069 0.2849 -0.0354 -0.0145 -0.0073 48  THR B OG1 
2819 C CG2 . THR B 69  ? 0.3524 0.2911 0.2653 -0.0319 -0.0197 -0.0083 48  THR B CG2 
2820 N N   . VAL B 70  ? 0.4176 0.3177 0.3053 -0.0244 -0.0106 -0.0034 49  VAL B N   
2821 C CA  . VAL B 70  ? 0.4477 0.3306 0.3230 -0.0227 -0.0060 -0.0019 49  VAL B CA  
2822 C C   . VAL B 70  ? 0.4635 0.3421 0.3327 -0.0128 -0.0092 0.0002  49  VAL B C   
2823 O O   . VAL B 70  ? 0.4674 0.3552 0.3412 -0.0102 -0.0127 0.0009  49  VAL B O   
2824 C CB  . VAL B 70  ? 0.4852 0.3636 0.3578 -0.0286 -0.0007 -0.0015 49  VAL B CB  
2825 C CG1 . VAL B 70  ? 0.4946 0.3518 0.3511 -0.0259 0.0050  0.0006  49  VAL B CG1 
2826 C CG2 . VAL B 70  ? 0.4366 0.3215 0.3162 -0.0381 0.0022  -0.0053 49  VAL B CG2 
2827 N N   . ARG B 71  ? 0.5038 0.3689 0.3624 -0.0070 -0.0080 0.0008  50  ARG B N   
2828 C CA  . ARG B 71  ? 0.5794 0.4413 0.4314 0.0039  -0.0118 0.0021  50  ARG B CA  
2829 C C   . ARG B 71  ? 0.5378 0.3973 0.3845 0.0054  -0.0115 0.0047  50  ARG B C   
2830 O O   . ARG B 71  ? 0.5695 0.4173 0.4082 0.0009  -0.0056 0.0066  50  ARG B O   
2831 C CB  . ARG B 71  ? 0.6373 0.4809 0.4748 0.0107  -0.0095 0.0030  50  ARG B CB  
2832 C CG  . ARG B 71  ? 0.6654 0.5136 0.5081 0.0137  -0.0120 -0.0001 50  ARG B CG  
2833 C CD  . ARG B 71  ? 0.5770 0.4406 0.4280 0.0217  -0.0194 -0.0027 50  ARG B CD  
2834 N NE  . ARG B 71  ? 0.5655 0.4332 0.4217 0.0241  -0.0208 -0.0063 50  ARG B NE  
2835 C CZ  . ARG B 71  ? 0.6594 0.5355 0.5260 0.0163  -0.0198 -0.0088 50  ARG B CZ  
2836 N NH1 . ARG B 71  ? 0.6398 0.5221 0.5129 0.0065  -0.0182 -0.0082 50  ARG B NH1 
2837 N NH2 . ARG B 71  ? 0.6417 0.5198 0.5115 0.0189  -0.0205 -0.0123 50  ARG B NH2 
2838 N N   . GLN B 72  ? 0.4876 0.3585 0.3391 0.0110  -0.0172 0.0041  51  GLN B N   
2839 C CA  . GLN B 72  ? 0.4981 0.3699 0.3467 0.0122  -0.0176 0.0059  51  GLN B CA  
2840 C C   . GLN B 72  ? 0.4630 0.3323 0.3029 0.0239  -0.0222 0.0060  51  GLN B C   
2841 O O   . GLN B 72  ? 0.4861 0.3649 0.3315 0.0298  -0.0274 0.0027  51  GLN B O   
2842 C CB  . GLN B 72  ? 0.5257 0.4161 0.3899 0.0067  -0.0201 0.0042  51  GLN B CB  
2843 C CG  . GLN B 72  ? 0.5738 0.4639 0.4380 0.0015  -0.0169 0.0062  51  GLN B CG  
2844 C CD  . GLN B 72  ? 0.5621 0.4506 0.4298 -0.0079 -0.0117 0.0062  51  GLN B CD  
2845 O OE1 . GLN B 72  ? 0.5524 0.4408 0.4230 -0.0110 -0.0109 0.0047  51  GLN B OE1 
2846 N NE2 . GLN B 72  ? 0.6664 0.5549 0.5345 -0.0125 -0.0083 0.0070  51  GLN B NE2 
2847 N N   . ASP B 73  ? 0.4850 0.3419 0.3109 0.0276  -0.0203 0.0091  52  ASP B N   
2848 C CA  . ASP B 73  ? 0.4643 0.3221 0.2824 0.0390  -0.0258 0.0087  52  ASP B CA  
2849 C C   . ASP B 73  ? 0.4599 0.3394 0.2934 0.0373  -0.0307 0.0052  52  ASP B C   
2850 O O   . ASP B 73  ? 0.4016 0.2853 0.2408 0.0296  -0.0280 0.0062  52  ASP B O   
2851 C CB  . ASP B 73  ? 0.5200 0.3580 0.3177 0.0428  -0.0219 0.0131  52  ASP B CB  
2852 C CG  . ASP B 73  ? 0.5408 0.3818 0.3304 0.0544  -0.0283 0.0124  52  ASP B CG  
2853 O OD1 . ASP B 73  ? 0.6192 0.4575 0.4011 0.0661  -0.0330 0.0112  52  ASP B OD1 
2854 O OD2 . ASP B 73  ? 0.5652 0.4123 0.3567 0.0523  -0.0288 0.0124  52  ASP B OD2 
2855 N N   . PRO B 74  ? 0.4509 0.3446 0.2917 0.0438  -0.0372 0.0004  53  PRO B N   
2856 C CA  . PRO B 74  ? 0.4198 0.3333 0.2762 0.0400  -0.0401 -0.0037 53  PRO B CA  
2857 C C   . PRO B 74  ? 0.4113 0.3251 0.2636 0.0395  -0.0399 -0.0023 53  PRO B C   
2858 O O   . PRO B 74  ? 0.3972 0.3196 0.2599 0.0317  -0.0381 -0.0028 53  PRO B O   
2859 C CB  . PRO B 74  ? 0.4810 0.4077 0.3431 0.0482  -0.0465 -0.0102 53  PRO B CB  
2860 C CG  . PRO B 74  ? 0.4541 0.3704 0.3088 0.0538  -0.0464 -0.0093 53  PRO B CG  
2861 C CD  . PRO B 74  ? 0.3872 0.2804 0.2237 0.0543  -0.0416 -0.0022 53  PRO B CD  
2862 N N   . GLN B 75  ? 0.4278 0.3313 0.2641 0.0481  -0.0414 -0.0005 54  GLN B N   
2863 C CA  . GLN B 75  ? 0.4829 0.3863 0.3142 0.0481  -0.0413 0.0005  54  GLN B CA  
2864 C C   . GLN B 75  ? 0.4487 0.3431 0.2790 0.0382  -0.0339 0.0051  54  GLN B C   
2865 O O   . GLN B 75  ? 0.3950 0.2967 0.2316 0.0333  -0.0329 0.0046  54  GLN B O   
2866 C CB  . GLN B 75  ? 0.5673 0.4590 0.3784 0.0604  -0.0443 0.0019  54  GLN B CB  
2867 C CG  . GLN B 75  ? 0.6803 0.5738 0.4856 0.0620  -0.0453 0.0017  54  GLN B CG  
2868 C CD  . GLN B 75  ? 0.8684 0.7398 0.6554 0.0603  -0.0386 0.0084  54  GLN B CD  
2869 O OE1 . GLN B 75  ? 0.7915 0.6563 0.5820 0.0500  -0.0315 0.0115  54  GLN B OE1 
2870 N NE2 . GLN B 75  ? 0.7881 0.6480 0.5549 0.0705  -0.0407 0.0100  54  GLN B NE2 
2871 N N   . ASN B 76  ? 0.4342 0.3133 0.2571 0.0349  -0.0285 0.0090  55  ASN B N   
2872 C CA  . ASN B 76  ? 0.3909 0.2638 0.2147 0.0250  -0.0213 0.0118  55  ASN B CA  
2873 C C   . ASN B 76  ? 0.4003 0.2893 0.2441 0.0159  -0.0210 0.0096  55  ASN B C   
2874 O O   . ASN B 76  ? 0.4016 0.2937 0.2506 0.0094  -0.0176 0.0103  55  ASN B O   
2875 C CB  . ASN B 76  ? 0.4933 0.3460 0.3043 0.0232  -0.0149 0.0150  55  ASN B CB  
2876 C CG  . ASN B 76  ? 0.5912 0.4394 0.4046 0.0123  -0.0070 0.0163  55  ASN B CG  
2877 O OD1 . ASN B 76  ? 0.6571 0.5102 0.4811 0.0045  -0.0044 0.0150  55  ASN B OD1 
2878 N ND2 . ASN B 76  ? 0.6564 0.4964 0.4602 0.0117  -0.0032 0.0181  55  ASN B ND2 
2879 N N   . LEU B 77  ? 0.3894 0.2880 0.2435 0.0159  -0.0243 0.0070  56  LEU B N   
2880 C CA  . LEU B 77  ? 0.3498 0.2619 0.2201 0.0086  -0.0242 0.0052  56  LEU B CA  
2881 C C   . LEU B 77  ? 0.3378 0.2619 0.2159 0.0081  -0.0261 0.0033  56  LEU B C   
2882 O O   . LEU B 77  ? 0.3202 0.2491 0.2054 0.0023  -0.0237 0.0039  56  LEU B O   
2883 C CB  . LEU B 77  ? 0.3478 0.2659 0.2251 0.0093  -0.0268 0.0025  56  LEU B CB  
2884 C CG  . LEU B 77  ? 0.3221 0.2524 0.2135 0.0031  -0.0268 0.0007  56  LEU B CG  
2885 C CD1 . LEU B 77  ? 0.2968 0.2259 0.1910 -0.0041 -0.0229 0.0029  56  LEU B CD1 
2886 C CD2 . LEU B 77  ? 0.4248 0.3577 0.3203 0.0037  -0.0283 -0.0017 56  LEU B CD2 
2887 N N   . ARG B 78  ? 0.3072 0.2366 0.1839 0.0145  -0.0305 0.0003  57  ARG B N   
2888 C CA  . ARG B 78  ? 0.3275 0.2679 0.2112 0.0136  -0.0318 -0.0025 57  ARG B CA  
2889 C C   . ARG B 78  ? 0.3601 0.2951 0.2382 0.0117  -0.0286 0.0004  57  ARG B C   
2890 O O   . ARG B 78  ? 0.3538 0.2949 0.2396 0.0069  -0.0266 0.0000  57  ARG B O   
2891 C CB  . ARG B 78  ? 0.3438 0.2918 0.2267 0.0210  -0.0371 -0.0075 57  ARG B CB  
2892 C CG  . ARG B 78  ? 0.3987 0.3586 0.2890 0.0196  -0.0380 -0.0119 57  ARG B CG  
2893 C CD  . ARG B 78  ? 0.4331 0.4047 0.3264 0.0257  -0.0434 -0.0192 57  ARG B CD  
2894 N NE  . ARG B 78  ? 0.5050 0.4839 0.4080 0.0246  -0.0442 -0.0230 57  ARG B NE  
2895 C CZ  . ARG B 78  ? 0.4857 0.4635 0.3857 0.0306  -0.0473 -0.0242 57  ARG B CZ  
2896 N NH1 . ARG B 78  ? 0.4998 0.4685 0.3862 0.0392  -0.0503 -0.0215 57  ARG B NH1 
2897 N NH2 . ARG B 78  ? 0.3273 0.3121 0.2372 0.0284  -0.0471 -0.0280 57  ARG B NH2 
2898 N N   . LYS B 79  ? 0.3459 0.2679 0.2093 0.0156  -0.0276 0.0033  58  LYS B N   
2899 C CA  . LYS B 79  ? 0.3803 0.2956 0.2371 0.0134  -0.0236 0.0059  58  LYS B CA  
2900 C C   . LYS B 79  ? 0.3715 0.2861 0.2353 0.0048  -0.0180 0.0079  58  LYS B C   
2901 O O   . LYS B 79  ? 0.3383 0.2564 0.2061 0.0011  -0.0155 0.0080  58  LYS B O   
2902 C CB  . LYS B 79  ? 0.4583 0.3565 0.2954 0.0193  -0.0225 0.0088  58  LYS B CB  
2903 C CG  . LYS B 79  ? 0.4819 0.3692 0.3099 0.0157  -0.0163 0.0118  58  LYS B CG  
2904 C CD  . LYS B 79  ? 0.5907 0.4572 0.3961 0.0216  -0.0138 0.0152  58  LYS B CD  
2905 C CE  . LYS B 79  ? 0.7056 0.5572 0.5055 0.0146  -0.0051 0.0181  58  LYS B CE  
2906 N NZ  . LYS B 79  ? 0.6671 0.5222 0.4744 0.0056  0.0009  0.0178  58  LYS B NZ  
2907 N N   . ALA B 80  ? 0.3700 0.2809 0.2355 0.0017  -0.0162 0.0089  59  ALA B N   
2908 C CA  . ALA B 80  ? 0.3555 0.2676 0.2278 -0.0061 -0.0114 0.0096  59  ALA B CA  
2909 C C   . ALA B 80  ? 0.4202 0.3472 0.3077 -0.0092 -0.0131 0.0079  59  ALA B C   
2910 O O   . ALA B 80  ? 0.3444 0.2754 0.2381 -0.0138 -0.0100 0.0079  59  ALA B O   
2911 C CB  . ALA B 80  ? 0.3672 0.2723 0.2374 -0.0087 -0.0091 0.0101  59  ALA B CB  
2912 N N   . THR B 81  ? 0.3005 0.2353 0.1937 -0.0066 -0.0174 0.0059  60  THR B N   
2913 C CA  . THR B 81  ? 0.3449 0.2904 0.2493 -0.0090 -0.0181 0.0046  60  THR B CA  
2914 C C   . THR B 81  ? 0.2980 0.2464 0.2035 -0.0090 -0.0167 0.0043  60  THR B C   
2915 O O   . THR B 81  ? 0.3111 0.2641 0.2232 -0.0118 -0.0148 0.0046  60  THR B O   
2916 C CB  . THR B 81  ? 0.2698 0.2210 0.1784 -0.0068 -0.0215 0.0019  60  THR B CB  
2917 O OG1 . THR B 81  ? 0.3609 0.3095 0.2691 -0.0071 -0.0224 0.0020  60  THR B OG1 
2918 C CG2 . THR B 81  ? 0.2824 0.2411 0.1997 -0.0092 -0.0208 0.0007  60  THR B CG2 
2919 N N   . LEU B 82  ? 0.3076 0.2533 0.2062 -0.0054 -0.0179 0.0034  61  LEU B N   
2920 C CA  . LEU B 82  ? 0.3504 0.2980 0.2489 -0.0056 -0.0163 0.0028  61  LEU B CA  
2921 C C   . LEU B 82  ? 0.3408 0.2828 0.2361 -0.0085 -0.0117 0.0054  61  LEU B C   
2922 O O   . LEU B 82  ? 0.3295 0.2754 0.2298 -0.0107 -0.0092 0.0052  61  LEU B O   
2923 C CB  . LEU B 82  ? 0.3336 0.2807 0.2248 -0.0006 -0.0192 0.0005  61  LEU B CB  
2924 C CG  . LEU B 82  ? 0.3770 0.3323 0.2733 0.0019  -0.0234 -0.0038 61  LEU B CG  
2925 C CD1 . LEU B 82  ? 0.4152 0.3724 0.3046 0.0076  -0.0272 -0.0073 61  LEU B CD1 
2926 C CD2 . LEU B 82  ? 0.3935 0.3569 0.3007 -0.0021 -0.0218 -0.0064 61  LEU B CD2 
2927 N N   . ASP B 83  ? 0.3740 0.3063 0.2608 -0.0088 -0.0097 0.0073  62  ASP B N   
2928 C CA  . ASP B 83  ? 0.3163 0.2434 0.2010 -0.0130 -0.0040 0.0086  62  ASP B CA  
2929 C C   . ASP B 83  ? 0.3387 0.2757 0.2368 -0.0176 -0.0024 0.0077  62  ASP B C   
2930 O O   . ASP B 83  ? 0.3346 0.2750 0.2369 -0.0199 0.0009  0.0072  62  ASP B O   
2931 C CB  . ASP B 83  ? 0.3817 0.2957 0.2555 -0.0138 -0.0009 0.0102  62  ASP B CB  
2932 C CG  . ASP B 83  ? 0.4454 0.3469 0.3024 -0.0078 -0.0020 0.0117  62  ASP B CG  
2933 O OD1 . ASP B 83  ? 0.5047 0.4093 0.3591 -0.0033 -0.0054 0.0109  62  ASP B OD1 
2934 O OD2 . ASP B 83  ? 0.4649 0.3528 0.3104 -0.0072 0.0007  0.0134  62  ASP B OD2 
2935 N N   . THR B 84  ? 0.3074 0.2493 0.2120 -0.0183 -0.0048 0.0073  63  THR B N   
2936 C CA  . THR B 84  ? 0.2668 0.2183 0.1826 -0.0214 -0.0042 0.0062  63  THR B CA  
2937 C C   . THR B 84  ? 0.3004 0.2597 0.2231 -0.0195 -0.0053 0.0058  63  THR B C   
2938 O O   . THR B 84  ? 0.2665 0.2320 0.1958 -0.0207 -0.0033 0.0050  63  THR B O   
2939 C CB  . THR B 84  ? 0.3277 0.2817 0.2468 -0.0219 -0.0070 0.0058  63  THR B CB  
2940 O OG1 . THR B 84  ? 0.4192 0.3653 0.3323 -0.0246 -0.0045 0.0057  63  THR B OG1 
2941 C CG2 . THR B 84  ? 0.3139 0.2789 0.2435 -0.0232 -0.0078 0.0045  63  THR B CG2 
2942 N N   . LEU B 85  ? 0.3067 0.2660 0.2279 -0.0164 -0.0081 0.0057  64  LEU B N   
2943 C CA  . LEU B 85  ? 0.3330 0.2969 0.2588 -0.0150 -0.0078 0.0051  64  LEU B CA  
2944 C C   . LEU B 85  ? 0.2881 0.2513 0.2131 -0.0155 -0.0043 0.0050  64  LEU B C   
2945 O O   . LEU B 85  ? 0.3369 0.3046 0.2676 -0.0154 -0.0025 0.0049  64  LEU B O   
2946 C CB  . LEU B 85  ? 0.3265 0.2898 0.2504 -0.0130 -0.0100 0.0037  64  LEU B CB  
2947 C CG  . LEU B 85  ? 0.3175 0.2828 0.2442 -0.0124 -0.0082 0.0024  64  LEU B CG  
2948 C CD1 . LEU B 85  ? 0.3042 0.2719 0.2359 -0.0119 -0.0072 0.0036  64  LEU B CD1 
2949 C CD2 . LEU B 85  ? 0.3192 0.2849 0.2446 -0.0118 -0.0095 -0.0008 64  LEU B CD2 
2950 N N   . ALA B 86  ? 0.3141 0.2711 0.2310 -0.0154 -0.0034 0.0050  65  ALA B N   
2951 C CA  . ALA B 86  ? 0.2760 0.2313 0.1907 -0.0160 0.0003  0.0048  65  ALA B CA  
2952 C C   . ALA B 86  ? 0.2804 0.2377 0.1995 -0.0192 0.0044  0.0048  65  ALA B C   
2953 O O   . ALA B 86  ? 0.3220 0.2820 0.2446 -0.0196 0.0075  0.0040  65  ALA B O   
2954 C CB  . ALA B 86  ? 0.2924 0.2394 0.1950 -0.0145 0.0002  0.0049  65  ALA B CB  
2955 N N   . LEU B 87  ? 0.3155 0.2719 0.2350 -0.0216 0.0049  0.0050  66  LEU B N   
2956 C CA  . LEU B 87  ? 0.3312 0.2914 0.2564 -0.0256 0.0094  0.0033  66  LEU B CA  
2957 C C   . LEU B 87  ? 0.3487 0.3217 0.2868 -0.0245 0.0081  0.0018  66  LEU B C   
2958 O O   . LEU B 87  ? 0.3058 0.2845 0.2499 -0.0255 0.0115  -0.0002 66  LEU B O   
2959 C CB  . LEU B 87  ? 0.3156 0.2715 0.2379 -0.0293 0.0108  0.0028  66  LEU B CB  
2960 C CG  . LEU B 87  ? 0.3872 0.3474 0.3156 -0.0350 0.0165  -0.0005 66  LEU B CG  
2961 C CD1 . LEU B 87  ? 0.4713 0.4257 0.3948 -0.0373 0.0229  -0.0012 66  LEU B CD1 
2962 C CD2 . LEU B 87  ? 0.4491 0.4032 0.3735 -0.0393 0.0187  -0.0015 66  LEU B CD2 
2963 N N   . TYR B 88  ? 0.3413 0.3186 0.2828 -0.0217 0.0034  0.0025  67  TYR B N   
2964 C CA  . TYR B 88  ? 0.3307 0.3181 0.2814 -0.0188 0.0017  0.0016  67  TYR B CA  
2965 C C   . TYR B 88  ? 0.2785 0.2655 0.2295 -0.0155 0.0032  0.0022  67  TYR B C   
2966 O O   . TYR B 88  ? 0.2388 0.2330 0.1966 -0.0133 0.0043  0.0009  67  TYR B O   
2967 C CB  . TYR B 88  ? 0.3443 0.3330 0.2952 -0.0164 -0.0030 0.0027  67  TYR B CB  
2968 C CG  . TYR B 88  ? 0.3461 0.3400 0.3006 -0.0189 -0.0046 0.0010  67  TYR B CG  
2969 C CD1 . TYR B 88  ? 0.4078 0.3953 0.3572 -0.0228 -0.0040 0.0011  67  TYR B CD1 
2970 C CD2 . TYR B 88  ? 0.3932 0.3985 0.3558 -0.0171 -0.0066 -0.0010 67  TYR B CD2 
2971 C CE1 . TYR B 88  ? 0.4135 0.4050 0.3660 -0.0258 -0.0046 -0.0010 67  TYR B CE1 
2972 C CE2 . TYR B 88  ? 0.4705 0.4818 0.4367 -0.0199 -0.0081 -0.0036 67  TYR B CE2 
2973 C CZ  . TYR B 88  ? 0.4060 0.4101 0.3674 -0.0249 -0.0067 -0.0037 67  TYR B CZ  
2974 O OH  . TYR B 88  ? 0.3708 0.3802 0.3357 -0.0284 -0.0074 -0.0069 67  TYR B OH  
2975 N N   . LEU B 89  ? 0.2792 0.2584 0.2232 -0.0147 0.0033  0.0035  68  LEU B N   
2976 C CA  . LEU B 89  ? 0.2756 0.2530 0.2189 -0.0128 0.0058  0.0034  68  LEU B CA  
2977 C C   . LEU B 89  ? 0.2958 0.2742 0.2404 -0.0148 0.0103  0.0020  68  LEU B C   
2978 O O   . LEU B 89  ? 0.3229 0.3041 0.2714 -0.0128 0.0128  0.0012  68  LEU B O   
2979 C CB  . LEU B 89  ? 0.3357 0.3061 0.2717 -0.0128 0.0052  0.0035  68  LEU B CB  
2980 C CG  . LEU B 89  ? 0.3040 0.2730 0.2387 -0.0115 0.0021  0.0037  68  LEU B CG  
2981 C CD1 . LEU B 89  ? 0.3232 0.2883 0.2521 -0.0122 0.0015  0.0019  68  LEU B CD1 
2982 C CD2 . LEU B 89  ? 0.3682 0.3377 0.3058 -0.0085 0.0030  0.0041  68  LEU B CD2 
2983 N N   . ALA B 90  ? 0.3002 0.2751 0.2406 -0.0187 0.0121  0.0016  69  ALA B N   
2984 C CA  . ALA B 90  ? 0.4061 0.3805 0.3466 -0.0216 0.0176  -0.0001 69  ALA B CA  
2985 C C   . ALA B 90  ? 0.3976 0.3836 0.3503 -0.0221 0.0194  -0.0028 69  ALA B C   
2986 O O   . ALA B 90  ? 0.3566 0.3461 0.3135 -0.0223 0.0235  -0.0049 69  ALA B O   
2987 C CB  . ALA B 90  ? 0.4038 0.3690 0.3346 -0.0256 0.0199  0.0003  69  ALA B CB  
2988 N N   . CYS B 91  ? 0.2998 0.2929 0.2585 -0.0221 0.0162  -0.0037 70  CYS B N   
2989 C CA  . CYS B 91  ? 0.3345 0.3416 0.3057 -0.0217 0.0166  -0.0075 70  CYS B CA  
2990 C C   . CYS B 91  ? 0.3288 0.3425 0.3057 -0.0145 0.0145  -0.0071 70  CYS B C   
2991 O O   . CYS B 91  ? 0.3761 0.4022 0.3633 -0.0125 0.0150  -0.0107 70  CYS B O   
2992 C CB  . CYS B 91  ? 0.3337 0.3469 0.3089 -0.0233 0.0132  -0.0089 70  CYS B CB  
2993 S SG  . CYS B 91  ? 0.4062 0.4113 0.3754 -0.0321 0.0178  -0.0104 70  CYS B SG  
2994 N N   . GLY B 92  ? 0.3108 0.3162 0.2808 -0.0107 0.0126  -0.0035 71  GLY B N   
2995 C CA  . GLY B 92  ? 0.3340 0.3410 0.3061 -0.0039 0.0121  -0.0027 71  GLY B CA  
2996 C C   . GLY B 92  ? 0.3385 0.3438 0.3079 0.0014  0.0075  -0.0002 71  GLY B C   
2997 O O   . GLY B 92  ? 0.3649 0.3701 0.3344 0.0079  0.0074  0.0006  71  GLY B O   
2998 N N   . ILE B 93  ? 0.3642 0.3668 0.3300 -0.0009 0.0042  0.0011  72  ILE B N   
2999 C CA  . ILE B 93  ? 0.3380 0.3368 0.2995 0.0034  0.0008  0.0034  72  ILE B CA  
3000 C C   . ILE B 93  ? 0.3074 0.2945 0.2613 0.0048  0.0036  0.0054  72  ILE B C   
3001 O O   . ILE B 93  ? 0.2671 0.2482 0.2170 0.0004  0.0055  0.0052  72  ILE B O   
3002 C CB  . ILE B 93  ? 0.3443 0.3423 0.3036 -0.0001 -0.0026 0.0039  72  ILE B CB  
3003 C CG1 . ILE B 93  ? 0.3662 0.3757 0.3331 -0.0022 -0.0045 0.0011  72  ILE B CG1 
3004 C CG2 . ILE B 93  ? 0.3215 0.3145 0.2754 0.0039  -0.0051 0.0062  72  ILE B CG2 
3005 C CD1 . ILE B 93  ? 0.3840 0.4052 0.3577 0.0038  -0.0070 -0.0008 72  ILE B CD1 
3006 N N   . ASP B 94  ? 0.3440 0.3276 0.2952 0.0111  0.0041  0.0068  73  ASP B N   
3007 C CA  . ASP B 94  ? 0.3561 0.3280 0.3004 0.0123  0.0085  0.0078  73  ASP B CA  
3008 C C   . ASP B 94  ? 0.3683 0.3311 0.3050 0.0118  0.0080  0.0091  73  ASP B C   
3009 O O   . ASP B 94  ? 0.3457 0.3075 0.2796 0.0165  0.0058  0.0109  73  ASP B O   
3010 C CB  . ASP B 94  ? 0.3483 0.3191 0.2924 0.0200  0.0107  0.0085  73  ASP B CB  
3011 C CG  . ASP B 94  ? 0.3886 0.3461 0.3254 0.0205  0.0168  0.0089  73  ASP B CG  
3012 O OD1 . ASP B 94  ? 0.3460 0.2931 0.2754 0.0179  0.0188  0.0093  73  ASP B OD1 
3013 O OD2 . ASP B 94  ? 0.3602 0.3176 0.2988 0.0232  0.0203  0.0081  73  ASP B OD2 
3014 N N   . PRO B 95  ? 0.2994 0.2562 0.2326 0.0064  0.0101  0.0078  74  PRO B N   
3015 C CA  . PRO B 95  ? 0.3037 0.2536 0.2313 0.0050  0.0101  0.0079  74  PRO B CA  
3016 C C   . PRO B 95  ? 0.3614 0.2996 0.2810 0.0095  0.0142  0.0095  74  PRO B C   
3017 O O   . PRO B 95  ? 0.3032 0.2354 0.2174 0.0094  0.0144  0.0101  74  PRO B O   
3018 C CB  . PRO B 95  ? 0.3536 0.3020 0.2807 -0.0012 0.0119  0.0046  74  PRO B CB  
3019 C CG  . PRO B 95  ? 0.3194 0.2744 0.2509 -0.0029 0.0109  0.0038  74  PRO B CG  
3020 C CD  . PRO B 95  ? 0.3205 0.2778 0.2548 0.0015  0.0122  0.0055  74  PRO B CD  
3021 N N   . GLN B 96  ? 0.3904 0.3238 0.3079 0.0134  0.0183  0.0101  75  GLN B N   
3022 C CA  . GLN B 96  ? 0.4065 0.3255 0.3138 0.0186  0.0231  0.0120  75  GLN B CA  
3023 C C   . GLN B 96  ? 0.4121 0.3326 0.3169 0.0283  0.0194  0.0156  75  GLN B C   
3024 O O   . GLN B 96  ? 0.4826 0.3918 0.3768 0.0327  0.0209  0.0180  75  GLN B O   
3025 C CB  . GLN B 96  ? 0.3624 0.2730 0.2669 0.0187  0.0302  0.0107  75  GLN B CB  
3026 C CG  . GLN B 96  ? 0.3903 0.2988 0.2957 0.0097  0.0343  0.0062  75  GLN B CG  
3027 C CD  . GLN B 96  ? 0.3915 0.3132 0.3061 0.0055  0.0308  0.0039  75  GLN B CD  
3028 O OE1 . GLN B 96  ? 0.3710 0.2990 0.2903 0.0086  0.0294  0.0050  75  GLN B OE1 
3029 N NE2 . GLN B 96  ? 0.4313 0.3569 0.3480 -0.0012 0.0296  0.0004  75  GLN B NE2 
3030 N N   . LYS B 97  ? 0.4459 0.3805 0.3598 0.0318  0.0148  0.0155  76  LYS B N   
3031 C CA  . LYS B 97  ? 0.4122 0.3521 0.3254 0.0413  0.0100  0.0175  76  LYS B CA  
3032 C C   . LYS B 97  ? 0.3887 0.3350 0.3027 0.0399  0.0041  0.0177  76  LYS B C   
3033 O O   . LYS B 97  ? 0.4758 0.4176 0.3816 0.0468  0.0018  0.0200  76  LYS B O   
3034 C CB  . LYS B 97  ? 0.4128 0.3684 0.3376 0.0447  0.0073  0.0155  76  LYS B CB  
3035 C CG  . LYS B 97  ? 0.4762 0.4275 0.4017 0.0460  0.0130  0.0148  76  LYS B CG  
3036 C CD  . LYS B 97  ? 0.4500 0.4175 0.3866 0.0513  0.0100  0.0125  76  LYS B CD  
3037 C CE  . LYS B 97  ? 0.5306 0.4955 0.4696 0.0513  0.0158  0.0112  76  LYS B CE  
3038 N NZ  . LYS B 97  ? 0.6589 0.6401 0.6091 0.0575  0.0134  0.0083  76  LYS B NZ  
3039 N N   . SER B 98  ? 0.3493 0.3051 0.2718 0.0315  0.0016  0.0155  77  SER B N   
3040 C CA  . SER B 98  ? 0.3667 0.3291 0.2910 0.0291  -0.0036 0.0152  77  SER B CA  
3041 C C   . SER B 98  ? 0.3719 0.3248 0.2910 0.0223  -0.0013 0.0151  77  SER B C   
3042 O O   . SER B 98  ? 0.3800 0.3240 0.2959 0.0186  0.0039  0.0144  77  SER B O   
3043 C CB  . SER B 98  ? 0.3355 0.3142 0.2723 0.0247  -0.0073 0.0122  77  SER B CB  
3044 O OG  . SER B 98  ? 0.4138 0.4038 0.3574 0.0305  -0.0092 0.0108  77  SER B OG  
3045 N N   . THR B 99  ? 0.3546 0.3109 0.2736 0.0205  -0.0052 0.0151  78  THR B N   
3046 C CA  . THR B 99  ? 0.3833 0.3333 0.2989 0.0145  -0.0038 0.0143  78  THR B CA  
3047 C C   . THR B 99  ? 0.3693 0.3299 0.2935 0.0087  -0.0076 0.0122  78  THR B C   
3048 O O   . THR B 99  ? 0.4132 0.3811 0.3401 0.0091  -0.0120 0.0121  78  THR B O   
3049 C CB  . THR B 99  ? 0.3529 0.2951 0.2591 0.0176  -0.0043 0.0161  78  THR B CB  
3050 O OG1 . THR B 99  ? 0.4234 0.3542 0.3192 0.0248  -0.0009 0.0186  78  THR B OG1 
3051 C CG2 . THR B 99  ? 0.3845 0.3192 0.2874 0.0112  -0.0012 0.0144  78  THR B CG2 
3052 N N   . ILE B 100 ? 0.3450 0.3058 0.2724 0.0036  -0.0056 0.0104  79  ILE B N   
3053 C CA  . ILE B 100 ? 0.3385 0.3057 0.2710 -0.0011 -0.0083 0.0089  79  ILE B CA  
3054 C C   . ILE B 100 ? 0.3424 0.3048 0.2724 -0.0050 -0.0071 0.0071  79  ILE B C   
3055 O O   . ILE B 100 ? 0.2604 0.2180 0.1884 -0.0060 -0.0035 0.0056  79  ILE B O   
3056 C CB  . ILE B 100 ? 0.3396 0.3120 0.2771 -0.0023 -0.0076 0.0082  79  ILE B CB  
3057 C CG1 . ILE B 100 ? 0.3476 0.3231 0.2871 -0.0067 -0.0093 0.0071  79  ILE B CG1 
3058 C CG2 . ILE B 100 ? 0.3296 0.2968 0.2651 -0.0025 -0.0034 0.0075  79  ILE B CG2 
3059 C CD1 . ILE B 100 ? 0.3481 0.3285 0.2917 -0.0081 -0.0083 0.0064  79  ILE B CD1 
3060 N N   . PHE B 101 ? 0.2706 0.2349 0.2011 -0.0070 -0.0099 0.0065  80  PHE B N   
3061 C CA  . PHE B 101 ? 0.2348 0.1960 0.1636 -0.0097 -0.0093 0.0041  80  PHE B CA  
3062 C C   . PHE B 101 ? 0.2518 0.2165 0.1823 -0.0114 -0.0129 0.0036  80  PHE B C   
3063 O O   . PHE B 101 ? 0.2621 0.2302 0.1942 -0.0112 -0.0152 0.0051  80  PHE B O   
3064 C CB  . PHE B 101 ? 0.2726 0.2272 0.1967 -0.0092 -0.0067 0.0040  80  PHE B CB  
3065 C CG  . PHE B 101 ? 0.2884 0.2431 0.2101 -0.0073 -0.0093 0.0061  80  PHE B CG  
3066 C CD1 . PHE B 101 ? 0.2984 0.2546 0.2189 -0.0029 -0.0108 0.0088  80  PHE B CD1 
3067 C CD2 . PHE B 101 ? 0.3434 0.2977 0.2644 -0.0094 -0.0106 0.0048  80  PHE B CD2 
3068 C CE1 . PHE B 101 ? 0.3041 0.2619 0.2222 -0.0008 -0.0138 0.0100  80  PHE B CE1 
3069 C CE2 . PHE B 101 ? 0.3286 0.2831 0.2468 -0.0079 -0.0130 0.0063  80  PHE B CE2 
3070 C CZ  . PHE B 101 ? 0.2943 0.2507 0.2109 -0.0036 -0.0148 0.0089  80  PHE B CZ  
3071 N N   . VAL B 102 ? 0.2276 0.1918 0.1579 -0.0130 -0.0131 0.0008  81  VAL B N   
3072 C CA  . VAL B 102 ? 0.2658 0.2314 0.1964 -0.0138 -0.0160 0.0001  81  VAL B CA  
3073 C C   . VAL B 102 ? 0.2703 0.2341 0.1998 -0.0145 -0.0159 -0.0005 81  VAL B C   
3074 O O   . VAL B 102 ? 0.2864 0.2475 0.2148 -0.0152 -0.0130 -0.0025 81  VAL B O   
3075 C CB  . VAL B 102 ? 0.2487 0.2156 0.1793 -0.0136 -0.0169 -0.0030 81  VAL B CB  
3076 C CG1 . VAL B 102 ? 0.2629 0.2298 0.1926 -0.0130 -0.0197 -0.0036 81  VAL B CG1 
3077 C CG2 . VAL B 102 ? 0.2696 0.2368 0.1991 -0.0126 -0.0168 -0.0022 81  VAL B CG2 
3078 N N   . GLN B 103 ? 0.2278 0.1924 0.1570 -0.0148 -0.0183 0.0007  82  GLN B N   
3079 C CA  . GLN B 103 ? 0.2498 0.2125 0.1770 -0.0153 -0.0183 0.0005  82  GLN B CA  
3080 C C   . GLN B 103 ? 0.2673 0.2281 0.1944 -0.0167 -0.0166 -0.0031 82  GLN B C   
3081 O O   . GLN B 103 ? 0.2932 0.2499 0.2173 -0.0175 -0.0137 -0.0038 82  GLN B O   
3082 C CB  . GLN B 103 ? 0.2624 0.2271 0.1900 -0.0161 -0.0211 0.0014  82  GLN B CB  
3083 C CG  . GLN B 103 ? 0.2806 0.2440 0.2053 -0.0164 -0.0216 0.0015  82  GLN B CG  
3084 C CD  . GLN B 103 ? 0.3058 0.2715 0.2314 -0.0181 -0.0239 0.0010  82  GLN B CD  
3085 O OE1 . GLN B 103 ? 0.3018 0.2676 0.2291 -0.0193 -0.0242 0.0006  82  GLN B OE1 
3086 N NE2 . GLN B 103 ? 0.3499 0.3161 0.2731 -0.0183 -0.0251 0.0010  82  GLN B NE2 
3087 N N   . SER B 104 ? 0.2436 0.2071 0.1732 -0.0167 -0.0180 -0.0057 83  SER B N   
3088 C CA  . SER B 104 ? 0.2466 0.2113 0.1782 -0.0177 -0.0169 -0.0105 83  SER B CA  
3089 C C   . SER B 104 ? 0.2570 0.2218 0.1899 -0.0193 -0.0127 -0.0141 83  SER B C   
3090 O O   . SER B 104 ? 0.2651 0.2312 0.2002 -0.0213 -0.0104 -0.0191 83  SER B O   
3091 C CB  . SER B 104 ? 0.2700 0.2384 0.2034 -0.0154 -0.0201 -0.0126 83  SER B CB  
3092 O OG  . SER B 104 ? 0.2792 0.2503 0.2133 -0.0137 -0.0208 -0.0133 83  SER B OG  
3093 N N   . HIS B 105 ? 0.2781 0.2415 0.2100 -0.0190 -0.0110 -0.0125 84  HIS B N   
3094 C CA  . HIS B 105 ? 0.2227 0.1845 0.1550 -0.0213 -0.0059 -0.0163 84  HIS B CA  
3095 C C   . HIS B 105 ? 0.3303 0.2830 0.2569 -0.0230 -0.0006 -0.0151 84  HIS B C   
3096 O O   . HIS B 105 ? 0.3681 0.3167 0.2935 -0.0259 0.0054  -0.0188 84  HIS B O   
3097 C CB  . HIS B 105 ? 0.2174 0.1797 0.1497 -0.0202 -0.0055 -0.0149 84  HIS B CB  
3098 C CG  . HIS B 105 ? 0.2235 0.1929 0.1590 -0.0184 -0.0096 -0.0165 84  HIS B CG  
3099 N ND1 . HIS B 105 ? 0.2406 0.2108 0.1757 -0.0175 -0.0096 -0.0157 84  HIS B ND1 
3100 C CD2 . HIS B 105 ? 0.2389 0.2136 0.1764 -0.0167 -0.0138 -0.0188 84  HIS B CD2 
3101 C CE1 . HIS B 105 ? 0.2898 0.2650 0.2256 -0.0152 -0.0135 -0.0172 84  HIS B CE1 
3102 N NE2 . HIS B 105 ? 0.2865 0.2643 0.2235 -0.0143 -0.0163 -0.0190 84  HIS B NE2 
3103 N N   . VAL B 106 ? 0.2548 0.2034 0.1767 -0.0213 -0.0024 -0.0105 85  VAL B N   
3104 C CA  . VAL B 106 ? 0.3188 0.2572 0.2322 -0.0211 0.0018  -0.0083 85  VAL B CA  
3105 C C   . VAL B 106 ? 0.3337 0.2705 0.2451 -0.0227 0.0017  -0.0096 85  VAL B C   
3106 O O   . VAL B 106 ? 0.2901 0.2291 0.2006 -0.0208 -0.0029 -0.0066 85  VAL B O   
3107 C CB  . VAL B 106 ? 0.2898 0.2257 0.1984 -0.0164 -0.0007 -0.0022 85  VAL B CB  
3108 C CG1 . VAL B 106 ? 0.3271 0.2509 0.2243 -0.0144 0.0034  0.0004  85  VAL B CG1 
3109 C CG2 . VAL B 106 ? 0.3583 0.2971 0.2703 -0.0150 -0.0009 -0.0013 85  VAL B CG2 
3110 N N   . PRO B 107 ? 0.3508 0.2843 0.2618 -0.0267 0.0073  -0.0147 86  PRO B N   
3111 C CA  . PRO B 107 ? 0.3511 0.2834 0.2608 -0.0285 0.0076  -0.0165 86  PRO B CA  
3112 C C   . PRO B 107 ? 0.3057 0.2296 0.2048 -0.0260 0.0069  -0.0112 86  PRO B C   
3113 O O   . PRO B 107 ? 0.3121 0.2376 0.2108 -0.0262 0.0043  -0.0111 86  PRO B O   
3114 C CB  . PRO B 107 ? 0.3205 0.2490 0.2305 -0.0339 0.0159  -0.0235 86  PRO B CB  
3115 C CG  . PRO B 107 ? 0.3577 0.2893 0.2724 -0.0353 0.0185  -0.0267 86  PRO B CG  
3116 C CD  . PRO B 107 ? 0.3426 0.2765 0.2573 -0.0306 0.0131  -0.0208 86  PRO B CD  
3117 N N   . GLU B 108 ? 0.3155 0.2304 0.2054 -0.0229 0.0089  -0.0068 87  GLU B N   
3118 C CA  . GLU B 108 ? 0.3610 0.2675 0.2389 -0.0192 0.0082  -0.0023 87  GLU B CA  
3119 C C   . GLU B 108 ? 0.3034 0.2197 0.1850 -0.0165 -0.0002 0.0002  87  GLU B C   
3120 O O   . GLU B 108 ? 0.2949 0.2075 0.1686 -0.0146 -0.0017 0.0020  87  GLU B O   
3121 C CB  . GLU B 108 ? 0.3123 0.2089 0.1801 -0.0143 0.0106  0.0021  87  GLU B CB  
3122 C CG  . GLU B 108 ? 0.3227 0.2042 0.1817 -0.0171 0.0209  0.0001  87  GLU B CG  
3123 C CD  . GLU B 108 ? 0.4057 0.2916 0.2742 -0.0211 0.0244  -0.0041 87  GLU B CD  
3124 O OE1 . GLU B 108 ? 0.3758 0.2752 0.2560 -0.0203 0.0184  -0.0043 87  GLU B OE1 
3125 O OE2 . GLU B 108 ? 0.4570 0.3321 0.3205 -0.0252 0.0337  -0.0077 87  GLU B OE2 
3126 N N   . HIS B 109 ? 0.3033 0.2311 0.1957 -0.0164 -0.0052 0.0000  88  HIS B N   
3127 C CA  . HIS B 109 ? 0.3258 0.2618 0.2216 -0.0151 -0.0117 0.0014  88  HIS B CA  
3128 C C   . HIS B 109 ? 0.3178 0.2545 0.2143 -0.0183 -0.0121 -0.0013 88  HIS B C   
3129 O O   . HIS B 109 ? 0.2730 0.2102 0.1655 -0.0175 -0.0148 -0.0003 88  HIS B O   
3130 C CB  . HIS B 109 ? 0.3415 0.2871 0.2471 -0.0152 -0.0152 0.0014  88  HIS B CB  
3131 C CG  . HIS B 109 ? 0.3542 0.3009 0.2596 -0.0117 -0.0157 0.0041  88  HIS B CG  
3132 N ND1 . HIS B 109 ? 0.2914 0.2447 0.1984 -0.0088 -0.0200 0.0060  88  HIS B ND1 
3133 C CD2 . HIS B 109 ? 0.2810 0.2235 0.1852 -0.0106 -0.0121 0.0046  88  HIS B CD2 
3134 C CE1 . HIS B 109 ? 0.3386 0.2920 0.2457 -0.0056 -0.0192 0.0077  88  HIS B CE1 
3135 N NE2 . HIS B 109 ? 0.3150 0.2609 0.2197 -0.0066 -0.0144 0.0073  88  HIS B NE2 
3136 N N   . ALA B 110 ? 0.3422 0.2797 0.2441 -0.0218 -0.0094 -0.0053 89  ALA B N   
3137 C CA  . ALA B 110 ? 0.2868 0.2248 0.1898 -0.0243 -0.0093 -0.0083 89  ALA B CA  
3138 C C   . ALA B 110 ? 0.2975 0.2260 0.1906 -0.0255 -0.0050 -0.0088 89  ALA B C   
3139 O O   . ALA B 110 ? 0.3154 0.2431 0.2055 -0.0263 -0.0062 -0.0092 89  ALA B O   
3140 C CB  . ALA B 110 ? 0.2955 0.2384 0.2073 -0.0264 -0.0080 -0.0133 89  ALA B CB  
3141 N N   . GLN B 111 ? 0.3302 0.2501 0.2169 -0.0259 0.0008  -0.0088 90  GLN B N   
3142 C CA  . GLN B 111 ? 0.2945 0.2020 0.1689 -0.0270 0.0064  -0.0090 90  GLN B CA  
3143 C C   . GLN B 111 ? 0.3541 0.2579 0.2177 -0.0226 0.0023  -0.0042 90  GLN B C   
3144 O O   . GLN B 111 ? 0.3783 0.2786 0.2358 -0.0236 0.0025  -0.0050 90  GLN B O   
3145 C CB  . GLN B 111 ? 0.3513 0.2476 0.2188 -0.0280 0.0144  -0.0095 90  GLN B CB  
3146 C CG  . GLN B 111 ? 0.2872 0.1876 0.1649 -0.0335 0.0197  -0.0164 90  GLN B CG  
3147 C CD  . GLN B 111 ? 0.3594 0.2491 0.2310 -0.0351 0.0278  -0.0173 90  GLN B CD  
3148 O OE1 . GLN B 111 ? 0.3395 0.2322 0.2146 -0.0332 0.0264  -0.0157 90  GLN B OE1 
3149 N NE2 . GLN B 111 ? 0.3856 0.2617 0.2473 -0.0391 0.0373  -0.0200 90  GLN B NE2 
3150 N N   . LEU B 112 ? 0.3312 0.2368 0.1924 -0.0173 -0.0018 0.0001  91  LEU B N   
3151 C CA  . LEU B 112 ? 0.3219 0.2274 0.1742 -0.0122 -0.0068 0.0035  91  LEU B CA  
3152 C C   . LEU B 112 ? 0.3224 0.2402 0.1831 -0.0139 -0.0131 0.0018  91  LEU B C   
3153 O O   . LEU B 112 ? 0.3519 0.2694 0.2053 -0.0122 -0.0161 0.0022  91  LEU B O   
3154 C CB  . LEU B 112 ? 0.3305 0.2377 0.1806 -0.0057 -0.0100 0.0074  91  LEU B CB  
3155 C CG  . LEU B 112 ? 0.3748 0.2836 0.2155 0.0012  -0.0158 0.0100  91  LEU B CG  
3156 C CD1 . LEU B 112 ? 0.4108 0.3037 0.2325 0.0036  -0.0119 0.0115  91  LEU B CD1 
3157 C CD2 . LEU B 112 ? 0.3511 0.2636 0.1916 0.0084  -0.0190 0.0130  91  LEU B CD2 
3158 N N   . GLY B 113 ? 0.3161 0.2434 0.1905 -0.0171 -0.0149 -0.0004 92  GLY B N   
3159 C CA  . GLY B 113 ? 0.2977 0.2336 0.1786 -0.0193 -0.0192 -0.0022 92  GLY B CA  
3160 C C   . GLY B 113 ? 0.3116 0.2429 0.1882 -0.0225 -0.0171 -0.0048 92  GLY B C   
3161 O O   . GLY B 113 ? 0.2983 0.2326 0.1727 -0.0228 -0.0203 -0.0055 92  GLY B O   
3162 N N   . TRP B 114 ? 0.3731 0.2975 0.2487 -0.0252 -0.0113 -0.0070 93  TRP B N   
3163 C CA  . TRP B 114 ? 0.3806 0.3002 0.2521 -0.0283 -0.0084 -0.0100 93  TRP B CA  
3164 C C   . TRP B 114 ? 0.3688 0.2796 0.2248 -0.0261 -0.0077 -0.0078 93  TRP B C   
3165 O O   . TRP B 114 ? 0.3522 0.2631 0.2040 -0.0271 -0.0094 -0.0090 93  TRP B O   
3166 C CB  . TRP B 114 ? 0.3579 0.2736 0.2328 -0.0319 -0.0016 -0.0140 93  TRP B CB  
3167 C CG  . TRP B 114 ? 0.3831 0.2922 0.2515 -0.0349 0.0024  -0.0169 93  TRP B CG  
3168 C CD1 . TRP B 114 ? 0.3711 0.2678 0.2273 -0.0362 0.0090  -0.0173 93  TRP B CD1 
3169 C CD2 . TRP B 114 ? 0.3235 0.2365 0.1956 -0.0369 0.0005  -0.0195 93  TRP B CD2 
3170 N NE1 . TRP B 114 ? 0.4173 0.3108 0.2699 -0.0392 0.0113  -0.0202 93  TRP B NE1 
3171 C CE2 . TRP B 114 ? 0.3571 0.2610 0.2198 -0.0395 0.0059  -0.0217 93  TRP B CE2 
3172 C CE3 . TRP B 114 ? 0.3849 0.3066 0.2662 -0.0368 -0.0044 -0.0204 93  TRP B CE3 
3173 C CZ2 . TRP B 114 ? 0.4070 0.3116 0.2705 -0.0420 0.0061  -0.0249 93  TRP B CZ2 
3174 C CZ3 . TRP B 114 ? 0.3853 0.3067 0.2667 -0.0390 -0.0040 -0.0234 93  TRP B CZ3 
3175 C CH2 . TRP B 114 ? 0.3398 0.2534 0.2130 -0.0416 0.0010  -0.0257 93  TRP B CH2 
3176 N N   . ALA B 115 ? 0.3245 0.2265 0.1703 -0.0228 -0.0050 -0.0048 94  ALA B N   
3177 C CA  . ALA B 115 ? 0.3148 0.2055 0.1424 -0.0193 -0.0040 -0.0023 94  ALA B CA  
3178 C C   . ALA B 115 ? 0.3428 0.2421 0.1680 -0.0150 -0.0124 -0.0008 94  ALA B C   
3179 O O   . ALA B 115 ? 0.3569 0.2521 0.1710 -0.0140 -0.0134 -0.0011 94  ALA B O   
3180 C CB  . ALA B 115 ? 0.3736 0.2518 0.1896 -0.0151 0.0005  0.0013  94  ALA B CB  
3181 N N   . LEU B 116 ? 0.3357 0.2478 0.1713 -0.0127 -0.0184 0.0000  95  LEU B N   
3182 C CA  . LEU B 116 ? 0.3166 0.2397 0.1524 -0.0094 -0.0262 -0.0003 95  LEU B CA  
3183 C C   . LEU B 116 ? 0.3180 0.2490 0.1615 -0.0151 -0.0282 -0.0045 95  LEU B C   
3184 O O   . LEU B 116 ? 0.3363 0.2754 0.1782 -0.0138 -0.0336 -0.0061 95  LEU B O   
3185 C CB  . LEU B 116 ? 0.3663 0.3010 0.2119 -0.0062 -0.0308 0.0009  95  LEU B CB  
3186 C CG  . LEU B 116 ? 0.3708 0.2989 0.2080 0.0010  -0.0299 0.0051  95  LEU B CG  
3187 C CD1 . LEU B 116 ? 0.3599 0.3008 0.2088 0.0035  -0.0342 0.0053  95  LEU B CD1 
3188 C CD2 . LEU B 116 ? 0.4266 0.3476 0.2454 0.0086  -0.0321 0.0072  95  LEU B CD2 
3189 N N   . ASN B 117 ? 0.3063 0.2355 0.1578 -0.0210 -0.0241 -0.0067 96  ASN B N   
3190 C CA  . ASN B 117 ? 0.3253 0.2582 0.1810 -0.0258 -0.0247 -0.0105 96  ASN B CA  
3191 C C   . ASN B 117 ? 0.3178 0.2441 0.1599 -0.0256 -0.0242 -0.0115 96  ASN B C   
3192 O O   . ASN B 117 ? 0.3553 0.2871 0.1977 -0.0277 -0.0271 -0.0145 96  ASN B O   
3193 C CB  . ASN B 117 ? 0.3419 0.2723 0.2063 -0.0304 -0.0201 -0.0128 96  ASN B CB  
3194 C CG  . ASN B 117 ? 0.3740 0.3127 0.2516 -0.0318 -0.0222 -0.0134 96  ASN B CG  
3195 O OD1 . ASN B 117 ? 0.3693 0.3158 0.2503 -0.0316 -0.0263 -0.0135 96  ASN B OD1 
3196 N ND2 . ASN B 117 ? 0.3934 0.3305 0.2778 -0.0330 -0.0191 -0.0144 96  ASN B ND2 
3197 N N   . CYS B 118 ? 0.3506 0.2642 0.1798 -0.0234 -0.0197 -0.0094 97  CYS B N   
3198 C CA  . CYS B 118 ? 0.3764 0.2808 0.1900 -0.0230 -0.0181 -0.0100 97  CYS B CA  
3199 C C   . CYS B 118 ? 0.3757 0.2830 0.1774 -0.0163 -0.0247 -0.0083 97  CYS B C   
3200 O O   . CYS B 118 ? 0.4103 0.3113 0.1978 -0.0152 -0.0247 -0.0089 97  CYS B O   
3201 C CB  . CYS B 118 ? 0.3798 0.2673 0.1824 -0.0236 -0.0094 -0.0087 97  CYS B CB  
3202 S SG  . CYS B 118 ? 0.3857 0.2734 0.2041 -0.0308 -0.0023 -0.0125 97  CYS B SG  
3203 N N   . TYR B 119 ? 0.3335 0.2510 0.1406 -0.0115 -0.0304 -0.0066 98  TYR B N   
3204 C CA  . TYR B 119 ? 0.3429 0.2677 0.1418 -0.0042 -0.0380 -0.0062 98  TYR B CA  
3205 C C   . TYR B 119 ? 0.3786 0.3242 0.1937 -0.0061 -0.0448 -0.0104 98  TYR B C   
3206 O O   . TYR B 119 ? 0.4104 0.3672 0.2242 -0.0001 -0.0517 -0.0113 98  TYR B O   
3207 C CB  . TYR B 119 ? 0.3972 0.3147 0.1857 0.0047  -0.0382 -0.0011 98  TYR B CB  
3208 C CG  . TYR B 119 ? 0.4510 0.3457 0.2217 0.0057  -0.0298 0.0024  98  TYR B CG  
3209 C CD1 . TYR B 119 ? 0.3947 0.2801 0.1709 0.0004  -0.0215 0.0032  98  TYR B CD1 
3210 C CD2 . TYR B 119 ? 0.4253 0.3074 0.1731 0.0114  -0.0297 0.0042  98  TYR B CD2 
3211 C CE1 . TYR B 119 ? 0.4434 0.3081 0.2041 -0.0003 -0.0125 0.0050  98  TYR B CE1 
3212 C CE2 . TYR B 119 ? 0.5058 0.3647 0.2359 0.0113  -0.0204 0.0070  98  TYR B CE2 
3213 C CZ  . TYR B 119 ? 0.4889 0.3395 0.2263 0.0049  -0.0114 0.0071  98  TYR B CZ  
3214 O OH  . TYR B 119 ? 0.5790 0.4068 0.2997 0.0034  -0.0009 0.0086  98  TYR B OH  
3215 N N   . THR B 120 ? 0.3817 0.3322 0.2116 -0.0143 -0.0425 -0.0134 99  THR B N   
3216 C CA  . THR B 120 ? 0.3402 0.3071 0.1844 -0.0182 -0.0465 -0.0180 99  THR B CA  
3217 C C   . THR B 120 ? 0.3740 0.3410 0.2185 -0.0249 -0.0453 -0.0227 99  THR B C   
3218 O O   . THR B 120 ? 0.3479 0.3036 0.1905 -0.0288 -0.0396 -0.0222 99  THR B O   
3219 C CB  . THR B 120 ? 0.3176 0.2873 0.1767 -0.0216 -0.0440 -0.0171 99  THR B CB  
3220 O OG1 . THR B 120 ? 0.3685 0.3378 0.2270 -0.0156 -0.0448 -0.0130 99  THR B OG1 
3221 C CG2 . THR B 120 ? 0.3518 0.3355 0.2237 -0.0265 -0.0465 -0.0221 99  THR B CG2 
3222 N N   . TYR B 121 ? 0.3684 0.3484 0.2154 -0.0262 -0.0502 -0.0280 100 TYR B N   
3223 C CA  . TYR B 121 ? 0.4444 0.4248 0.2918 -0.0331 -0.0487 -0.0332 100 TYR B CA  
3224 C C   . TYR B 121 ? 0.4529 0.4344 0.3145 -0.0408 -0.0446 -0.0355 100 TYR B C   
3225 O O   . TYR B 121 ? 0.4026 0.3921 0.2750 -0.0417 -0.0454 -0.0360 100 TYR B O   
3226 C CB  . TYR B 121 ? 0.4180 0.4128 0.2629 -0.0322 -0.0553 -0.0392 100 TYR B CB  
3227 C CG  . TYR B 121 ? 0.5607 0.5523 0.3877 -0.0240 -0.0595 -0.0375 100 TYR B CG  
3228 C CD1 . TYR B 121 ? 0.6838 0.6641 0.4972 -0.0253 -0.0571 -0.0379 100 TYR B CD1 
3229 C CD2 . TYR B 121 ? 0.5624 0.5613 0.3847 -0.0144 -0.0657 -0.0356 100 TYR B CD2 
3230 C CE1 . TYR B 121 ? 0.7752 0.7502 0.5694 -0.0174 -0.0604 -0.0360 100 TYR B CE1 
3231 C CE2 . TYR B 121 ? 0.6189 0.6126 0.4219 -0.0055 -0.0695 -0.0336 100 TYR B CE2 
3232 C CZ  . TYR B 121 ? 0.6985 0.6796 0.4867 -0.0071 -0.0668 -0.0336 100 TYR B CZ  
3233 O OH  . TYR B 121 ? 0.7513 0.7248 0.5175 0.0022  -0.0701 -0.0313 100 TYR B OH  
3234 N N   . PHE B 122 ? 0.4394 0.4115 0.2999 -0.0460 -0.0397 -0.0370 101 PHE B N   
3235 C CA  . PHE B 122 ? 0.4925 0.4635 0.3632 -0.0525 -0.0356 -0.0395 101 PHE B CA  
3236 C C   . PHE B 122 ? 0.4648 0.4490 0.3428 -0.0570 -0.0379 -0.0456 101 PHE B C   
3237 O O   . PHE B 122 ? 0.4186 0.4041 0.3058 -0.0607 -0.0354 -0.0466 101 PHE B O   
3238 C CB  . PHE B 122 ? 0.4257 0.3857 0.2922 -0.0564 -0.0307 -0.0413 101 PHE B CB  
3239 C CG  . PHE B 122 ? 0.4450 0.4010 0.3191 -0.0620 -0.0262 -0.0438 101 PHE B CG  
3240 C CD1 . PHE B 122 ? 0.4905 0.4519 0.3675 -0.0680 -0.0258 -0.0498 101 PHE B CD1 
3241 C CD2 . PHE B 122 ? 0.4617 0.4081 0.3391 -0.0609 -0.0219 -0.0408 101 PHE B CD2 
3242 C CE1 . PHE B 122 ? 0.5073 0.4617 0.3887 -0.0729 -0.0204 -0.0518 101 PHE B CE1 
3243 C CE2 . PHE B 122 ? 0.4843 0.4250 0.3660 -0.0644 -0.0178 -0.0426 101 PHE B CE2 
3244 C CZ  . PHE B 122 ? 0.4963 0.4394 0.3790 -0.0704 -0.0166 -0.0477 101 PHE B CZ  
3245 N N   . GLY B 123 ? 0.4133 0.4074 0.2868 -0.0569 -0.0425 -0.0503 102 GLY B N   
3246 C CA  . GLY B 123 ? 0.4612 0.4702 0.3427 -0.0621 -0.0444 -0.0580 102 GLY B CA  
3247 C C   . GLY B 123 ? 0.4050 0.4259 0.2964 -0.0600 -0.0470 -0.0579 102 GLY B C   
3248 O O   . GLY B 123 ? 0.4319 0.4604 0.3335 -0.0664 -0.0448 -0.0633 102 GLY B O   
3249 N N   . GLU B 124 ? 0.4548 0.4767 0.3428 -0.0513 -0.0510 -0.0522 103 GLU B N   
3250 C CA  . GLU B 124 ? 0.4805 0.5134 0.3779 -0.0487 -0.0533 -0.0518 103 GLU B CA  
3251 C C   . GLU B 124 ? 0.4660 0.4912 0.3720 -0.0536 -0.0469 -0.0496 103 GLU B C   
3252 O O   . GLU B 124 ? 0.4744 0.5090 0.3906 -0.0574 -0.0459 -0.0535 103 GLU B O   
3253 C CB  . GLU B 124 ? 0.4266 0.4581 0.3167 -0.0381 -0.0576 -0.0453 103 GLU B CB  
3254 C CG  . GLU B 124 ? 0.5260 0.5662 0.4062 -0.0310 -0.0648 -0.0475 103 GLU B CG  
3255 C CD  . GLU B 124 ? 0.5102 0.5430 0.3792 -0.0200 -0.0674 -0.0400 103 GLU B CD  
3256 O OE1 . GLU B 124 ? 0.4643 0.4790 0.3258 -0.0192 -0.0625 -0.0334 103 GLU B OE1 
3257 O OE2 . GLU B 124 ? 0.5155 0.5605 0.3831 -0.0120 -0.0740 -0.0411 103 GLU B OE2 
3258 N N   . LEU B 125 ? 0.3698 0.3781 0.2713 -0.0533 -0.0424 -0.0439 104 LEU B N   
3259 C CA  . LEU B 125 ? 0.3332 0.3333 0.2407 -0.0564 -0.0370 -0.0415 104 LEU B CA  
3260 C C   . LEU B 125 ? 0.3945 0.3923 0.3057 -0.0651 -0.0320 -0.0471 104 LEU B C   
3261 O O   . LEU B 125 ? 0.4229 0.4178 0.3394 -0.0683 -0.0280 -0.0471 104 LEU B O   
3262 C CB  . LEU B 125 ? 0.3614 0.3464 0.2634 -0.0531 -0.0343 -0.0352 104 LEU B CB  
3263 C CG  . LEU B 125 ? 0.3619 0.3458 0.2600 -0.0456 -0.0369 -0.0297 104 LEU B CG  
3264 C CD1 . LEU B 125 ? 0.3411 0.3117 0.2348 -0.0441 -0.0333 -0.0258 104 LEU B CD1 
3265 C CD2 . LEU B 125 ? 0.3577 0.3476 0.2626 -0.0432 -0.0380 -0.0275 104 LEU B CD2 
3266 N N   . SER B 126 ? 0.4674 0.4650 0.3748 -0.0691 -0.0315 -0.0519 105 SER B N   
3267 C CA  . SER B 126 ? 0.4935 0.4882 0.4036 -0.0780 -0.0260 -0.0581 105 SER B CA  
3268 C C   . SER B 126 ? 0.4716 0.4815 0.3908 -0.0832 -0.0262 -0.0650 105 SER B C   
3269 O O   . SER B 126 ? 0.5234 0.5283 0.4463 -0.0901 -0.0196 -0.0681 105 SER B O   
3270 C CB  . SER B 126 ? 0.5631 0.5554 0.4669 -0.0813 -0.0256 -0.0624 105 SER B CB  
3271 O OG  . SER B 126 ? 0.5811 0.5598 0.4774 -0.0772 -0.0245 -0.0569 105 SER B OG  
3272 N N   . ARG B 127 ? 0.5260 0.5542 0.4484 -0.0798 -0.0332 -0.0680 106 ARG B N   
3273 C CA  . ARG B 127 ? 0.5331 0.5791 0.4662 -0.0842 -0.0339 -0.0758 106 ARG B CA  
3274 C C   . ARG B 127 ? 0.5638 0.6080 0.5034 -0.0837 -0.0308 -0.0724 106 ARG B C   
3275 O O   . ARG B 127 ? 0.6145 0.6692 0.5635 -0.0898 -0.0281 -0.0792 106 ARG B O   
3276 C CB  . ARG B 127 ? 0.4817 0.5487 0.4163 -0.0781 -0.0433 -0.0796 106 ARG B CB  
3277 N N   . MET B 128 ? 0.5439 0.5756 0.4790 -0.0770 -0.0308 -0.0626 107 MET B N   
3278 C CA  . MET B 128 ? 0.5604 0.5877 0.4998 -0.0767 -0.0274 -0.0589 107 MET B CA  
3279 C C   . MET B 128 ? 0.6298 0.6401 0.5670 -0.0835 -0.0183 -0.0589 107 MET B C   
3280 O O   . MET B 128 ? 0.7073 0.7126 0.6467 -0.0842 -0.0144 -0.0566 107 MET B O   
3281 C CB  . MET B 128 ? 0.5788 0.5987 0.5137 -0.0673 -0.0304 -0.0493 107 MET B CB  
3282 C CG  . MET B 128 ? 0.5002 0.5291 0.4318 -0.0591 -0.0381 -0.0472 107 MET B CG  
3283 S SD  . MET B 128 ? 0.6997 0.7514 0.6399 -0.0551 -0.0442 -0.0515 107 MET B SD  
3284 C CE  . MET B 128 ? 0.6055 0.6532 0.5522 -0.0551 -0.0400 -0.0474 107 MET B CE  
3285 N N   . THR B 129 ? 0.8024 0.8028 0.7341 -0.0880 -0.0147 -0.0612 108 THR B N   
3286 C CA  . THR B 129 ? 0.7726 0.7533 0.6990 -0.0926 -0.0060 -0.0602 108 THR B CA  
3287 C C   . THR B 129 ? 0.7503 0.7158 0.6704 -0.0848 -0.0060 -0.0506 108 THR B C   
3288 O O   . THR B 129 ? 0.7502 0.7118 0.6659 -0.0794 -0.0094 -0.0467 108 THR B O   
3289 C CB  . THR B 129 ? 0.8809 0.8613 0.8118 -0.1004 0.0012  -0.0651 108 THR B CB  
3290 O OG1 . THR B 129 ? 0.8371 0.8371 0.7769 -0.1072 0.0001  -0.0753 108 THR B OG1 
3291 C CG2 . THR B 129 ? 0.9086 0.8663 0.8308 -0.1057 0.0111  -0.0653 108 THR B CG2 
3292 N N   . GLU B 140 ? 0.6906 0.5438 0.5577 -0.0668 0.0184  -0.0427 119 GLU B N   
3293 C CA  . GLU B 140 ? 0.5471 0.3888 0.4089 -0.0662 0.0226  -0.0403 119 GLU B CA  
3294 C C   . GLU B 140 ? 0.5992 0.4394 0.4605 -0.0553 0.0187  -0.0343 119 GLU B C   
3295 O O   . GLU B 140 ? 0.5629 0.4141 0.4303 -0.0500 0.0127  -0.0329 119 GLU B O   
3296 C CB  . GLU B 140 ? 0.6305 0.4824 0.4972 -0.0744 0.0229  -0.0425 119 GLU B CB  
3297 C CG  . GLU B 140 ? 0.7926 0.6306 0.6526 -0.0765 0.0296  -0.0415 119 GLU B CG  
3298 C CD  . GLU B 140 ? 0.8545 0.7032 0.7207 -0.0866 0.0316  -0.0462 119 GLU B CD  
3299 O OE1 . GLU B 140 ? 0.8363 0.7057 0.7126 -0.0894 0.0255  -0.0489 119 GLU B OE1 
3300 O OE2 . GLU B 140 ? 0.9593 0.7953 0.8195 -0.0916 0.0397  -0.0476 119 GLU B OE2 
3301 N N   . ASN B 141 ? 0.6220 0.4479 0.4751 -0.0524 0.0226  -0.0313 120 ASN B N   
3302 C CA  . ASN B 141 ? 0.6053 0.4276 0.4555 -0.0413 0.0193  -0.0263 120 ASN B CA  
3303 C C   . ASN B 141 ? 0.5971 0.4317 0.4535 -0.0409 0.0148  -0.0234 120 ASN B C   
3304 O O   . ASN B 141 ? 0.6069 0.4357 0.4585 -0.0335 0.0138  -0.0195 120 ASN B O   
3305 C CB  . ASN B 141 ? 0.6302 0.4277 0.4649 -0.0365 0.0260  -0.0241 120 ASN B CB  
3306 C CG  . ASN B 141 ? 0.5633 0.3460 0.3905 -0.0377 0.0319  -0.0271 120 ASN B CG  
3307 O OD1 . ASN B 141 ? 0.6827 0.4717 0.5148 -0.0351 0.0290  -0.0292 120 ASN B OD1 
3308 N ND2 . ASN B 141 ? 0.6131 0.3751 0.4279 -0.0421 0.0412  -0.0277 120 ASN B ND2 
3309 N N   . ILE B 142 ? 0.4981 0.3494 0.3644 -0.0479 0.0120  -0.0255 121 ILE B N   
3310 C CA  . ILE B 142 ? 0.4796 0.3443 0.3529 -0.0462 0.0069  -0.0228 121 ILE B CA  
3311 C C   . ILE B 142 ? 0.4035 0.2789 0.2830 -0.0397 0.0005  -0.0216 121 ILE B C   
3312 O O   . ILE B 142 ? 0.3999 0.2762 0.2804 -0.0386 -0.0002 -0.0237 121 ILE B O   
3313 C CB  . ILE B 142 ? 0.5280 0.4061 0.4086 -0.0550 0.0063  -0.0257 121 ILE B CB  
3314 C CG1 . ILE B 142 ? 0.4798 0.3688 0.3657 -0.0586 0.0035  -0.0294 121 ILE B CG1 
3315 C CG2 . ILE B 142 ? 0.5753 0.4441 0.4513 -0.0626 0.0136  -0.0285 121 ILE B CG2 
3316 C CD1 . ILE B 142 ? 0.4467 0.3532 0.3406 -0.0626 -0.0006 -0.0311 121 ILE B CD1 
3317 N N   . ASN B 143 ? 0.3989 0.2824 0.2825 -0.0359 -0.0035 -0.0188 122 ASN B N   
3318 C CA  . ASN B 143 ? 0.4039 0.2977 0.2938 -0.0311 -0.0083 -0.0186 122 ASN B CA  
3319 C C   . ASN B 143 ? 0.4020 0.3091 0.2987 -0.0360 -0.0109 -0.0197 122 ASN B C   
3320 O O   . ASN B 143 ? 0.3512 0.2626 0.2492 -0.0414 -0.0106 -0.0201 122 ASN B O   
3321 C CB  . ASN B 143 ? 0.3932 0.2886 0.2836 -0.0242 -0.0111 -0.0158 122 ASN B CB  
3322 C CG  . ASN B 143 ? 0.4046 0.3056 0.2974 -0.0269 -0.0119 -0.0135 122 ASN B CG  
3323 O OD1 . ASN B 143 ? 0.3990 0.3114 0.2983 -0.0295 -0.0144 -0.0137 122 ASN B OD1 
3324 N ND2 . ASN B 143 ? 0.4004 0.2923 0.2869 -0.0255 -0.0096 -0.0113 122 ASN B ND2 
3325 N N   . ALA B 144 ? 0.4308 0.2318 0.3254 -0.0754 -0.0141 -0.0346 123 ALA B N   
3326 C CA  . ALA B 144 ? 0.4199 0.2504 0.3246 -0.0768 -0.0165 -0.0384 123 ALA B CA  
3327 C C   . ALA B 144 ? 0.4403 0.2790 0.3390 -0.0759 -0.0165 -0.0335 123 ALA B C   
3328 O O   . ALA B 144 ? 0.4123 0.2744 0.3185 -0.0786 -0.0160 -0.0372 123 ALA B O   
3329 C CB  . ALA B 144 ? 0.4321 0.2708 0.3433 -0.0697 -0.0240 -0.0375 123 ALA B CB  
3330 N N   . GLY B 145 ? 0.4224 0.2413 0.3057 -0.0704 -0.0176 -0.0256 124 GLY B N   
3331 C CA  . GLY B 145 ? 0.3727 0.1969 0.2478 -0.0682 -0.0168 -0.0213 124 GLY B CA  
3332 C C   . GLY B 145 ? 0.3937 0.2269 0.2740 -0.0765 -0.0049 -0.0238 124 GLY B C   
3333 O O   . GLY B 145 ? 0.3116 0.1656 0.1980 -0.0777 -0.0043 -0.0252 124 GLY B O   
3334 N N   . LEU B 146 ? 0.3821 0.1996 0.2626 -0.0822 0.0050  -0.0241 125 LEU B N   
3335 C CA  . LEU B 146 ? 0.4720 0.2993 0.3659 -0.0919 0.0173  -0.0273 125 LEU B CA  
3336 C C   . LEU B 146 ? 0.4450 0.3042 0.3623 -0.0988 0.0135  -0.0389 125 LEU B C   
3337 O O   . LEU B 146 ? 0.4801 0.3589 0.4104 -0.1033 0.0175  -0.0423 125 LEU B O   
3338 C CB  . LEU B 146 ? 0.4423 0.2459 0.3373 -0.0978 0.0289  -0.0261 125 LEU B CB  
3339 C CG  . LEU B 146 ? 0.5108 0.2845 0.3841 -0.0927 0.0405  -0.0139 125 LEU B CG  
3340 C CD1 . LEU B 146 ? 0.5571 0.3066 0.4337 -0.0987 0.0519  -0.0128 125 LEU B CD1 
3341 C CD2 . LEU B 146 ? 0.5418 0.3266 0.4182 -0.0942 0.0516  -0.0102 125 LEU B CD2 
3342 N N   . PHE B 147 ? 0.3826 0.2471 0.3048 -0.0985 0.0056  -0.0455 126 PHE B N   
3343 C CA  . PHE B 147 ? 0.3390 0.2307 0.2772 -0.1022 0.0009  -0.0571 126 PHE B CA  
3344 C C   . PHE B 147 ? 0.3295 0.2433 0.2646 -0.0956 -0.0059 -0.0553 126 PHE B C   
3345 O O   . PHE B 147 ? 0.3685 0.3060 0.3150 -0.0978 -0.0078 -0.0628 126 PHE B O   
3346 C CB  . PHE B 147 ? 0.3886 0.2768 0.3278 -0.1010 -0.0040 -0.0638 126 PHE B CB  
3347 C CG  . PHE B 147 ? 0.3405 0.2531 0.2899 -0.1019 -0.0095 -0.0764 126 PHE B CG  
3348 C CD1 . PHE B 147 ? 0.3696 0.2902 0.3361 -0.1106 -0.0081 -0.0891 126 PHE B CD1 
3349 C CD2 . PHE B 147 ? 0.4067 0.3330 0.3487 -0.0930 -0.0161 -0.0759 126 PHE B CD2 
3350 C CE1 . PHE B 147 ? 0.4890 0.4308 0.4617 -0.1091 -0.0159 -0.1026 126 PHE B CE1 
3351 C CE2 . PHE B 147 ? 0.4412 0.3872 0.3863 -0.0908 -0.0212 -0.0872 126 PHE B CE2 
3352 C CZ  . PHE B 147 ? 0.3852 0.3389 0.3440 -0.0982 -0.0224 -0.1013 126 PHE B CZ  
3353 N N   . ASP B 148 ? 0.3530 0.2587 0.2742 -0.0871 -0.0104 -0.0458 127 ASP B N   
3354 C CA  . ASP B 148 ? 0.3850 0.3082 0.3041 -0.0803 -0.0169 -0.0433 127 ASP B CA  
3355 C C   . ASP B 148 ? 0.3355 0.2607 0.2485 -0.0771 -0.0161 -0.0369 127 ASP B C   
3356 O O   . ASP B 148 ? 0.3232 0.2636 0.2360 -0.0719 -0.0208 -0.0354 127 ASP B O   
3357 C CB  . ASP B 148 ? 0.3910 0.3059 0.3050 -0.0731 -0.0229 -0.0379 127 ASP B CB  
3358 C CG  . ASP B 148 ? 0.4465 0.3791 0.3616 -0.0667 -0.0274 -0.0353 127 ASP B CG  
3359 O OD1 . ASP B 148 ? 0.3933 0.3448 0.3121 -0.0666 -0.0273 -0.0414 127 ASP B OD1 
3360 O OD2 . ASP B 148 ? 0.4887 0.4149 0.4006 -0.0611 -0.0315 -0.0274 127 ASP B OD2 
3361 N N   . TYR B 149 ? 0.3063 0.2154 0.2130 -0.0788 -0.0092 -0.0327 128 TYR B N   
3362 C CA  . TYR B 149 ? 0.3186 0.2265 0.2154 -0.0732 -0.0082 -0.0264 128 TYR B CA  
3363 C C   . TYR B 149 ? 0.3412 0.2768 0.2499 -0.0743 -0.0072 -0.0305 128 TYR B C   
3364 O O   . TYR B 149 ? 0.3364 0.2751 0.2373 -0.0673 -0.0099 -0.0258 128 TYR B O   
3365 C CB  . TYR B 149 ? 0.3205 0.2045 0.2048 -0.0732 0.0018  -0.0206 128 TYR B CB  
3366 C CG  . TYR B 149 ? 0.3438 0.2355 0.2421 -0.0819 0.0156  -0.0234 128 TYR B CG  
3367 C CD1 . TYR B 149 ? 0.4193 0.3289 0.3254 -0.0816 0.0208  -0.0236 128 TYR B CD1 
3368 C CD2 . TYR B 149 ? 0.3914 0.2719 0.2984 -0.0904 0.0241  -0.0259 128 TYR B CD2 
3369 C CE1 . TYR B 149 ? 0.4276 0.3461 0.3532 -0.0901 0.0342  -0.0264 128 TYR B CE1 
3370 C CE2 . TYR B 149 ? 0.3872 0.2746 0.3133 -0.0995 0.0376  -0.0285 128 TYR B CE2 
3371 C CZ  . TYR B 149 ? 0.4482 0.3556 0.3853 -0.0996 0.0428  -0.0288 128 TYR B CZ  
3372 O OH  . TYR B 149 ? 0.5903 0.5065 0.5529 -0.1092 0.0569  -0.0317 128 TYR B OH  
3373 N N   . PRO B 150 ? 0.3601 0.3157 0.2876 -0.0817 -0.0050 -0.0398 129 PRO B N   
3374 C CA  . PRO B 150 ? 0.3671 0.3502 0.3057 -0.0802 -0.0073 -0.0444 129 PRO B CA  
3375 C C   . PRO B 150 ? 0.3534 0.3467 0.2835 -0.0709 -0.0173 -0.0418 129 PRO B C   
3376 O O   . PRO B 150 ? 0.2993 0.3071 0.2305 -0.0659 -0.0191 -0.0408 129 PRO B O   
3377 C CB  . PRO B 150 ? 0.3176 0.3178 0.2780 -0.0888 -0.0073 -0.0573 129 PRO B CB  
3378 C CG  . PRO B 150 ? 0.3537 0.3328 0.3171 -0.0970 0.0008  -0.0574 129 PRO B CG  
3379 C CD  . PRO B 150 ? 0.3273 0.2808 0.2680 -0.0911 -0.0011 -0.0478 129 PRO B CD  
3380 N N   . VAL B 151 ? 0.3229 0.3086 0.2460 -0.0680 -0.0227 -0.0401 130 VAL B N   
3381 C CA  . VAL B 151 ? 0.3318 0.3242 0.2485 -0.0592 -0.0294 -0.0354 130 VAL B CA  
3382 C C   . VAL B 151 ? 0.3415 0.3197 0.2482 -0.0533 -0.0310 -0.0258 130 VAL B C   
3383 O O   . VAL B 151 ? 0.3127 0.2991 0.2171 -0.0465 -0.0346 -0.0221 130 VAL B O   
3384 C CB  . VAL B 151 ? 0.2846 0.2728 0.1997 -0.0576 -0.0318 -0.0354 130 VAL B CB  
3385 C CG1 . VAL B 151 ? 0.2960 0.2901 0.2066 -0.0484 -0.0354 -0.0286 130 VAL B CG1 
3386 C CG2 . VAL B 151 ? 0.3107 0.3109 0.2322 -0.0617 -0.0315 -0.0467 130 VAL B CG2 
3387 N N   . LEU B 152 ? 0.3530 0.3081 0.2525 -0.0544 -0.0294 -0.0220 131 LEU B N   
3388 C CA  . LEU B 152 ? 0.3874 0.3271 0.2754 -0.0474 -0.0332 -0.0151 131 LEU B CA  
3389 C C   . LEU B 152 ? 0.4074 0.3547 0.2916 -0.0447 -0.0291 -0.0148 131 LEU B C   
3390 O O   . LEU B 152 ? 0.3581 0.3034 0.2359 -0.0371 -0.0338 -0.0110 131 LEU B O   
3391 C CB  . LEU B 152 ? 0.4092 0.3215 0.2865 -0.0469 -0.0337 -0.0125 131 LEU B CB  
3392 C CG  . LEU B 152 ? 0.3954 0.2881 0.2583 -0.0377 -0.0410 -0.0075 131 LEU B CG  
3393 C CD1 . LEU B 152 ? 0.3457 0.2429 0.2172 -0.0330 -0.0509 -0.0053 131 LEU B CD1 
3394 C CD2 . LEU B 152 ? 0.4086 0.2737 0.2585 -0.0353 -0.0435 -0.0061 131 LEU B CD2 
3395 N N   . MET B 153 ? 0.3344 0.2905 0.2252 -0.0508 -0.0200 -0.0190 132 MET B N   
3396 C CA  . MET B 153 ? 0.3525 0.3201 0.2452 -0.0483 -0.0144 -0.0191 132 MET B CA  
3397 C C   . MET B 153 ? 0.3304 0.3214 0.2305 -0.0434 -0.0209 -0.0210 132 MET B C   
3398 O O   . MET B 153 ? 0.3122 0.3052 0.2065 -0.0359 -0.0217 -0.0179 132 MET B O   
3399 C CB  . MET B 153 ? 0.3407 0.3183 0.2490 -0.0574 -0.0028 -0.0243 132 MET B CB  
3400 C CG  . MET B 153 ? 0.5275 0.4806 0.4280 -0.0616 0.0073  -0.0208 132 MET B CG  
3401 S SD  . MET B 153 ? 0.5588 0.5207 0.4784 -0.0696 0.0260  -0.0226 132 MET B SD  
3402 C CE  . MET B 153 ? 0.5194 0.5150 0.4560 -0.0656 0.0243  -0.0268 132 MET B CE  
3403 N N   . ALA B 154 ? 0.3427 0.3503 0.2533 -0.0462 -0.0253 -0.0262 133 ALA B N   
3404 C CA  . ALA B 154 ? 0.3505 0.3779 0.2638 -0.0394 -0.0315 -0.0271 133 ALA B CA  
3405 C C   . ALA B 154 ? 0.2930 0.3078 0.1941 -0.0306 -0.0370 -0.0183 133 ALA B C   
3406 O O   . ALA B 154 ? 0.3327 0.3553 0.2318 -0.0231 -0.0394 -0.0160 133 ALA B O   
3407 C CB  . ALA B 154 ? 0.3605 0.4020 0.2800 -0.0413 -0.0356 -0.0336 133 ALA B CB  
3408 N N   . ALA B 155 ? 0.3337 0.3285 0.2292 -0.0313 -0.0393 -0.0137 134 ALA B N   
3409 C CA  . ALA B 155 ? 0.3296 0.3113 0.2197 -0.0241 -0.0452 -0.0063 134 ALA B CA  
3410 C C   . ALA B 155 ? 0.3492 0.3189 0.2297 -0.0187 -0.0464 -0.0041 134 ALA B C   
3411 O O   . ALA B 155 ? 0.3684 0.3370 0.2465 -0.0112 -0.0508 -0.0005 134 ALA B O   
3412 C CB  . ALA B 155 ? 0.3256 0.2897 0.2176 -0.0266 -0.0480 -0.0034 134 ALA B CB  
3413 N N   . ASP B 156 ? 0.3834 0.3421 0.2565 -0.0213 -0.0415 -0.0060 135 ASP B N   
3414 C CA  . ASP B 156 ? 0.4035 0.3488 0.2625 -0.0141 -0.0410 -0.0042 135 ASP B CA  
3415 C C   . ASP B 156 ? 0.3854 0.3491 0.2476 -0.0083 -0.0395 -0.0046 135 ASP B C   
3416 O O   . ASP B 156 ? 0.4235 0.3780 0.2768 0.0007  -0.0443 -0.0021 135 ASP B O   
3417 C CB  . ASP B 156 ? 0.3784 0.3135 0.2286 -0.0171 -0.0311 -0.0052 135 ASP B CB  
3418 C CG  . ASP B 156 ? 0.4248 0.3369 0.2669 -0.0199 -0.0333 -0.0042 135 ASP B CG  
3419 O OD1 . ASP B 156 ? 0.4241 0.3239 0.2653 -0.0173 -0.0443 -0.0029 135 ASP B OD1 
3420 O OD2 . ASP B 156 ? 0.4591 0.3650 0.2978 -0.0246 -0.0236 -0.0046 135 ASP B OD2 
3421 N N   . ILE B 157 ? 0.3709 0.3603 0.2470 -0.0128 -0.0340 -0.0088 136 ILE B N   
3422 C CA  . ILE B 157 ? 0.4066 0.4159 0.2883 -0.0070 -0.0326 -0.0103 136 ILE B CA  
3423 C C   . ILE B 157 ? 0.3430 0.3598 0.2257 -0.0001 -0.0414 -0.0076 136 ILE B C   
3424 O O   . ILE B 157 ? 0.2759 0.2905 0.1530 0.0092  -0.0442 -0.0047 136 ILE B O   
3425 C CB  . ILE B 157 ? 0.3700 0.4047 0.2705 -0.0141 -0.0255 -0.0175 136 ILE B CB  
3426 C CG1 . ILE B 157 ? 0.4245 0.4492 0.3253 -0.0203 -0.0134 -0.0180 136 ILE B CG1 
3427 C CG2 . ILE B 157 ? 0.3793 0.4383 0.2899 -0.0074 -0.0261 -0.0203 136 ILE B CG2 
3428 C CD1 . ILE B 157 ? 0.4180 0.4609 0.3416 -0.0316 -0.0071 -0.0254 136 ILE B CD1 
3429 N N   . LEU B 158 ? 0.3055 0.3295 0.1939 -0.0035 -0.0447 -0.0079 137 LEU B N   
3430 C CA  . LEU B 158 ? 0.3311 0.3628 0.2191 0.0040  -0.0501 -0.0040 137 LEU B CA  
3431 C C   . LEU B 158 ? 0.3301 0.3398 0.2116 0.0096  -0.0546 0.0043  137 LEU B C   
3432 O O   . LEU B 158 ? 0.3702 0.3826 0.2506 0.0177  -0.0574 0.0093  137 LEU B O   
3433 C CB  . LEU B 158 ? 0.2852 0.3268 0.1769 0.0004  -0.0507 -0.0058 137 LEU B CB  
3434 C CG  . LEU B 158 ? 0.3268 0.3905 0.2277 -0.0048 -0.0492 -0.0163 137 LEU B CG  
3435 C CD1 . LEU B 158 ? 0.3816 0.4507 0.2809 -0.0056 -0.0510 -0.0184 137 LEU B CD1 
3436 C CD2 . LEU B 158 ? 0.3387 0.4254 0.2456 0.0017  -0.0515 -0.0211 137 LEU B CD2 
3437 N N   . LEU B 159 ? 0.3254 0.3127 0.2035 0.0062  -0.0560 0.0055  138 LEU B N   
3438 C CA  . LEU B 159 ? 0.3408 0.3068 0.2177 0.0109  -0.0626 0.0111  138 LEU B CA  
3439 C C   . LEU B 159 ? 0.3834 0.3464 0.2542 0.0208  -0.0656 0.0125  138 LEU B C   
3440 O O   . LEU B 159 ? 0.3913 0.3452 0.2656 0.0262  -0.0703 0.0178  138 LEU B O   
3441 C CB  . LEU B 159 ? 0.3943 0.3373 0.2671 0.0074  -0.0662 0.0093  138 LEU B CB  
3442 C CG  . LEU B 159 ? 0.4086 0.3422 0.2920 0.0016  -0.0689 0.0113  138 LEU B CG  
3443 C CD1 . LEU B 159 ? 0.3688 0.2791 0.2452 0.0013  -0.0751 0.0082  138 LEU B CD1 
3444 C CD2 . LEU B 159 ? 0.3600 0.2901 0.2568 0.0047  -0.0724 0.0180  138 LEU B CD2 
3445 N N   . TYR B 160 ? 0.3667 0.3361 0.2297 0.0237  -0.0619 0.0080  139 TYR B N   
3446 C CA  . TYR B 160 ? 0.3436 0.3064 0.1983 0.0342  -0.0644 0.0083  139 TYR B CA  
3447 C C   . TYR B 160 ? 0.3373 0.3240 0.1964 0.0403  -0.0617 0.0083  139 TYR B C   
3448 O O   . TYR B 160 ? 0.3991 0.3856 0.2523 0.0493  -0.0614 0.0073  139 TYR B O   
3449 C CB  . TYR B 160 ? 0.3199 0.2702 0.1606 0.0361  -0.0610 0.0042  139 TYR B CB  
3450 C CG  . TYR B 160 ? 0.3172 0.2415 0.1504 0.0330  -0.0666 0.0038  139 TYR B CG  
3451 C CD1 . TYR B 160 ? 0.3437 0.2440 0.1726 0.0391  -0.0783 0.0043  139 TYR B CD1 
3452 C CD2 . TYR B 160 ? 0.3611 0.2846 0.1937 0.0243  -0.0616 0.0022  139 TYR B CD2 
3453 C CE1 . TYR B 160 ? 0.3398 0.2176 0.1645 0.0373  -0.0862 0.0025  139 TYR B CE1 
3454 C CE2 . TYR B 160 ? 0.3291 0.2288 0.1547 0.0231  -0.0682 0.0017  139 TYR B CE2 
3455 C CZ  . TYR B 160 ? 0.3070 0.1848 0.1290 0.0300  -0.0812 0.0014  139 TYR B CZ  
3456 O OH  . TYR B 160 ? 0.3505 0.2057 0.1678 0.0300  -0.0904 -0.0007 139 TYR B OH  
3457 N N   . GLN B 161 ? 0.3267 0.3332 0.1948 0.0375  -0.0606 0.0091  140 GLN B N   
3458 C CA  . GLN B 161 ? 0.3680 0.3981 0.2397 0.0449  -0.0604 0.0081  140 GLN B CA  
3459 C C   . GLN B 161 ? 0.3538 0.4007 0.2300 0.0454  -0.0552 0.0008  140 GLN B C   
3460 O O   . GLN B 161 ? 0.3892 0.4481 0.2671 0.0549  -0.0556 -0.0002 140 GLN B O   
3461 C CB  . GLN B 161 ? 0.4184 0.4387 0.2849 0.0567  -0.0653 0.0148  140 GLN B CB  
3462 C CG  . GLN B 161 ? 0.4454 0.4515 0.3126 0.0564  -0.0676 0.0235  140 GLN B CG  
3463 C CD  . GLN B 161 ? 0.4061 0.4302 0.2747 0.0557  -0.0654 0.0250  140 GLN B CD  
3464 O OE1 . GLN B 161 ? 0.3914 0.4346 0.2573 0.0638  -0.0666 0.0237  140 GLN B OE1 
3465 N NE2 . GLN B 161 ? 0.3847 0.4025 0.2565 0.0475  -0.0631 0.0271  140 GLN B NE2 
3466 N N   . THR B 162 ? 0.3443 0.3918 0.2244 0.0353  -0.0491 -0.0037 141 THR B N   
3467 C CA  . THR B 162 ? 0.2907 0.3499 0.1774 0.0345  -0.0404 -0.0089 141 THR B CA  
3468 C C   . THR B 162 ? 0.3447 0.4378 0.2499 0.0371  -0.0405 -0.0148 141 THR B C   
3469 O O   . THR B 162 ? 0.3538 0.4634 0.2682 0.0337  -0.0454 -0.0185 141 THR B O   
3470 C CB  . THR B 162 ? 0.3404 0.3934 0.2298 0.0224  -0.0327 -0.0114 141 THR B CB  
3471 O OG1 . THR B 162 ? 0.3191 0.3404 0.1903 0.0221  -0.0346 -0.0068 141 THR B OG1 
3472 C CG2 . THR B 162 ? 0.3057 0.3702 0.2050 0.0210  -0.0202 -0.0151 141 THR B CG2 
3473 N N   . ASN B 163 ? 0.3289 0.4322 0.2396 0.0445  -0.0355 -0.0166 142 ASN B N   
3474 C CA  . ASN B 163 ? 0.3394 0.4767 0.2726 0.0477  -0.0358 -0.0237 142 ASN B CA  
3475 C C   . ASN B 163 ? 0.3449 0.4994 0.3023 0.0372  -0.0246 -0.0307 142 ASN B C   
3476 O O   . ASN B 163 ? 0.3449 0.5278 0.3271 0.0333  -0.0279 -0.0393 142 ASN B O   
3477 C CB  . ASN B 163 ? 0.4185 0.5598 0.3490 0.0626  -0.0362 -0.0218 142 ASN B CB  
3478 C CG  . ASN B 163 ? 0.4863 0.6085 0.3957 0.0731  -0.0461 -0.0145 142 ASN B CG  
3479 O OD1 . ASN B 163 ? 0.3951 0.4958 0.2893 0.0807  -0.0451 -0.0099 142 ASN B OD1 
3480 N ND2 . ASN B 163 ? 0.5637 0.6921 0.4720 0.0741  -0.0554 -0.0132 142 ASN B ND2 
3481 N N   . GLN B 164 ? 0.3730 0.5098 0.3238 0.0334  -0.0115 -0.0273 143 GLN B N   
3482 C CA  . GLN B 164 ? 0.4246 0.5751 0.3994 0.0243  0.0031  -0.0316 143 GLN B CA  
3483 C C   . GLN B 164 ? 0.3952 0.5171 0.3543 0.0157  0.0133  -0.0265 143 GLN B C   
3484 O O   . GLN B 164 ? 0.3989 0.4901 0.3271 0.0213  0.0122  -0.0197 143 GLN B O   
3485 C CB  . GLN B 164 ? 0.4466 0.6097 0.4327 0.0334  0.0146  -0.0315 143 GLN B CB  
3486 C CG  . GLN B 164 ? 0.4720 0.6676 0.4797 0.0422  0.0051  -0.0378 143 GLN B CG  
3487 C CD  . GLN B 164 ? 0.6774 0.8787 0.6874 0.0554  0.0144  -0.0358 143 GLN B CD  
3488 O OE1 . GLN B 164 ? 0.6864 0.8842 0.7021 0.0543  0.0330  -0.0334 143 GLN B OE1 
3489 N NE2 . GLN B 164 ? 0.6396 0.8479 0.6434 0.0693  0.0025  -0.0360 143 GLN B NE2 
3490 N N   . VAL B 165 ? 0.3568 0.4882 0.3384 0.0026  0.0224  -0.0306 144 VAL B N   
3491 C CA  . VAL B 165 ? 0.4648 0.5699 0.4335 -0.0058 0.0326  -0.0259 144 VAL B CA  
3492 C C   . VAL B 165 ? 0.4622 0.5768 0.4559 -0.0126 0.0535  -0.0263 144 VAL B C   
3493 O O   . VAL B 165 ? 0.4304 0.5747 0.4632 -0.0213 0.0549  -0.0348 144 VAL B O   
3494 C CB  . VAL B 165 ? 0.5158 0.6170 0.4858 -0.0167 0.0225  -0.0294 144 VAL B CB  
3495 C CG1 . VAL B 165 ? 0.5041 0.5764 0.4596 -0.0238 0.0327  -0.0241 144 VAL B CG1 
3496 C CG2 . VAL B 165 ? 0.3886 0.4827 0.3388 -0.0101 0.0046  -0.0279 144 VAL B CG2 
3497 N N   . PRO B 166 ? 0.5466 0.6364 0.5202 -0.0083 0.0706  -0.0176 145 PRO B N   
3498 C CA  . PRO B 166 ? 0.6110 0.7040 0.6072 -0.0165 0.0941  -0.0155 145 PRO B CA  
3499 C C   . PRO B 166 ? 0.6937 0.7733 0.6936 -0.0309 0.0958  -0.0158 145 PRO B C   
3500 O O   . PRO B 166 ? 0.8054 0.8510 0.7704 -0.0288 0.0960  -0.0089 145 PRO B O   
3501 C CB  . PRO B 166 ? 0.5566 0.6214 0.5183 -0.0029 0.1105  -0.0045 145 PRO B CB  
3502 C CG  . PRO B 166 ? 0.5588 0.5952 0.4756 0.0075  0.0929  -0.0017 145 PRO B CG  
3503 C CD  . PRO B 166 ? 0.5452 0.6032 0.4748 0.0062  0.0696  -0.0095 145 PRO B CD  
3504 N N   . VAL B 167 ? 0.7776 0.8837 0.8206 -0.0447 0.0955  -0.0251 146 VAL B N   
3505 C CA  . VAL B 167 ? 0.7894 0.8857 0.8412 -0.0590 0.0957  -0.0277 146 VAL B CA  
3506 C C   . VAL B 167 ? 0.7923 0.8909 0.8759 -0.0692 0.1209  -0.0254 146 VAL B C   
3507 O O   . VAL B 167 ? 0.8025 0.9317 0.9289 -0.0729 0.1287  -0.0311 146 VAL B O   
3508 C CB  . VAL B 167 ? 0.6754 0.7968 0.7505 -0.0665 0.0744  -0.0416 146 VAL B CB  
3509 N N   . GLY B 168 ? 0.8629 0.9288 0.9272 -0.0733 0.1340  -0.0165 147 GLY B N   
3510 C CA  . GLY B 168 ? 1.0375 1.1029 1.1352 -0.0857 0.1576  -0.0143 147 GLY B CA  
3511 C C   . GLY B 168 ? 0.8991 0.9915 1.0470 -0.1027 0.1478  -0.0296 147 GLY B C   
3512 O O   . GLY B 168 ? 0.8562 0.9596 1.0023 -0.1042 0.1231  -0.0404 147 GLY B O   
3513 N N   . GLU B 169 ? 1.0602 1.2168 1.1716 -0.2266 0.1159  0.1945  148 GLU B N   
3514 C CA  . GLU B 169 ? 1.0932 1.2486 1.2611 -0.2372 0.0964  0.1906  148 GLU B CA  
3515 C C   . GLU B 169 ? 1.1161 1.2243 1.2696 -0.2369 0.0692  0.1912  148 GLU B C   
3516 O O   . GLU B 169 ? 0.9554 1.0540 1.1373 -0.2352 0.0477  0.1746  148 GLU B O   
3517 C CB  . GLU B 169 ? 1.0056 1.1803 1.2163 -0.2623 0.1129  0.2119  148 GLU B CB  
3518 N N   . ASP B 170 ? 1.0361 1.1154 1.1452 -0.2380 0.0699  0.2104  149 ASP B N   
3519 C CA  . ASP B 170 ? 0.9106 0.9471 1.0084 -0.2345 0.0462  0.2142  149 ASP B CA  
3520 C C   . ASP B 170 ? 0.8413 0.8695 0.9224 -0.2123 0.0276  0.1885  149 ASP B C   
3521 O O   . ASP B 170 ? 0.7844 0.7822 0.8709 -0.2073 0.0079  0.1848  149 ASP B O   
3522 C CB  . ASP B 170 ? 0.9176 0.9326 0.9719 -0.2395 0.0509  0.2445  149 ASP B CB  
3523 C CG  . ASP B 170 ? 1.0045 1.0382 1.0050 -0.2326 0.0669  0.2458  149 ASP B CG  
3524 O OD1 . ASP B 170 ? 0.9239 0.9787 0.9180 -0.2193 0.0714  0.2209  149 ASP B OD1 
3525 O OD2 . ASP B 170 ? 1.1866 1.2116 1.1488 -0.2412 0.0753  0.2720  149 ASP B OD2 
3526 N N   . GLN B 171 ? 0.8110 0.8636 0.8727 -0.1988 0.0352  0.1714  150 GLN B N   
3527 C CA  . GLN B 171 ? 0.7582 0.8028 0.7997 -0.1791 0.0202  0.1498  150 GLN B CA  
3528 C C   . GLN B 171 ? 0.6717 0.7356 0.7447 -0.1703 0.0145  0.1238  150 GLN B C   
3529 O O   . GLN B 171 ? 0.5763 0.6390 0.6318 -0.1538 0.0067  0.1059  150 GLN B O   
3530 C CB  . GLN B 171 ? 0.8206 0.8705 0.8093 -0.1703 0.0309  0.1497  150 GLN B CB  
3531 C CG  . GLN B 171 ? 0.9941 1.0309 0.9442 -0.1808 0.0368  0.1767  150 GLN B CG  
3532 C CD  . GLN B 171 ? 0.9989 1.0144 0.9105 -0.1724 0.0188  0.1793  150 GLN B CD  
3533 O OE1 . GLN B 171 ? 0.9060 0.9015 0.8344 -0.1679 -0.0011 0.1816  150 GLN B OE1 
3534 N NE2 . GLN B 171 ? 0.9733 0.9936 0.8342 -0.1708 0.0264  0.1783  150 GLN B NE2 
3535 N N   . LYS B 172 ? 0.7461 0.8288 0.8655 -0.1821 0.0169  0.1228  151 LYS B N   
3536 C CA  . LYS B 172 ? 0.6451 0.7517 0.7943 -0.1746 0.0094  0.1010  151 LYS B CA  
3537 C C   . LYS B 172 ? 0.5434 0.6251 0.6873 -0.1644 -0.0147 0.0823  151 LYS B C   
3538 O O   . LYS B 172 ? 0.4315 0.5228 0.5667 -0.1484 -0.0204 0.0648  151 LYS B O   
3539 C CB  . LYS B 172 ? 0.5244 0.6564 0.7278 -0.1934 0.0120  0.1054  151 LYS B CB  
3540 C CG  . LYS B 172 ? 0.7005 0.8700 0.9182 -0.2000 0.0392  0.1199  151 LYS B CG  
3541 C CD  . LYS B 172 ? 0.7855 0.9981 1.0266 -0.1863 0.0453  0.1062  151 LYS B CD  
3542 C CE  . LYS B 172 ? 0.8751 1.1267 1.1349 -0.1907 0.0764  0.1203  151 LYS B CE  
3543 N NZ  . LYS B 172 ? 0.9353 1.2332 1.2329 -0.1772 0.0818  0.1097  151 LYS B NZ  
3544 N N   . GLN B 173 ? 0.5376 0.5855 0.6864 -0.1727 -0.0271 0.0864  152 GLN B N   
3545 C CA  . GLN B 173 ? 0.5244 0.5473 0.6685 -0.1629 -0.0464 0.0676  152 GLN B CA  
3546 C C   . GLN B 173 ? 0.5335 0.5482 0.6378 -0.1425 -0.0481 0.0619  152 GLN B C   
3547 O O   . GLN B 173 ? 0.4662 0.4795 0.5639 -0.1299 -0.0581 0.0426  152 GLN B O   
3548 C CB  . GLN B 173 ? 0.5561 0.5391 0.7115 -0.1734 -0.0550 0.0744  152 GLN B CB  
3549 C CG  . GLN B 173 ? 0.6724 0.6491 0.8633 -0.1884 -0.0660 0.0605  152 GLN B CG  
3550 C CD  . GLN B 173 ? 0.7554 0.6828 0.9460 -0.1884 -0.0771 0.0538  152 GLN B CD  
3551 O OE1 . GLN B 173 ? 0.6536 0.5512 0.8500 -0.1967 -0.0734 0.0722  152 GLN B OE1 
3552 N NE2 . GLN B 173 ? 0.7566 0.6736 0.9394 -0.1782 -0.0894 0.0282  152 GLN B NE2 
3553 N N   . HIS B 174 ? 0.4696 0.4789 0.5456 -0.1409 -0.0391 0.0791  153 HIS B N   
3554 C CA  . HIS B 174 ? 0.5120 0.5145 0.5518 -0.1253 -0.0421 0.0746  153 HIS B CA  
3555 C C   . HIS B 174 ? 0.4837 0.5094 0.5124 -0.1138 -0.0366 0.0579  153 HIS B C   
3556 O O   . HIS B 174 ? 0.4600 0.4795 0.4736 -0.1006 -0.0445 0.0442  153 HIS B O   
3557 C CB  . HIS B 174 ? 0.5467 0.5430 0.5568 -0.1296 -0.0352 0.0972  153 HIS B CB  
3558 C CG  . HIS B 174 ? 0.5697 0.5423 0.5911 -0.1393 -0.0405 0.1183  153 HIS B CG  
3559 N ND1 . HIS B 174 ? 0.7105 0.6828 0.7551 -0.1560 -0.0326 0.1329  153 HIS B ND1 
3560 C CD2 . HIS B 174 ? 0.5803 0.5280 0.5963 -0.1340 -0.0523 0.1290  153 HIS B CD2 
3561 C CE1 . HIS B 174 ? 0.7244 0.6684 0.7744 -0.1606 -0.0393 0.1518  153 HIS B CE1 
3562 N NE2 . HIS B 174 ? 0.5897 0.5192 0.6238 -0.1461 -0.0514 0.1501  153 HIS B NE2 
3563 N N   . LEU B 175 ? 0.4180 0.4703 0.4563 -0.1180 -0.0217 0.0599  154 LEU B N   
3564 C CA  . LEU B 175 ? 0.4854 0.5576 0.5170 -0.1048 -0.0148 0.0459  154 LEU B CA  
3565 C C   . LEU B 175 ? 0.4112 0.4893 0.4656 -0.0971 -0.0296 0.0284  154 LEU B C   
3566 O O   . LEU B 175 ? 0.4274 0.5067 0.4666 -0.0825 -0.0319 0.0162  154 LEU B O   
3567 C CB  . LEU B 175 ? 0.4958 0.5967 0.5396 -0.1091 0.0069  0.0530  154 LEU B CB  
3568 C CG  . LEU B 175 ? 0.5842 0.7002 0.6126 -0.0942 0.0223  0.0435  154 LEU B CG  
3569 C CD1 . LEU B 175 ? 0.5577 0.6957 0.6192 -0.0828 0.0156  0.0308  154 LEU B CD1 
3570 C CD2 . LEU B 175 ? 0.6281 0.7191 0.6069 -0.0850 0.0208  0.0370  154 LEU B CD2 
3571 N N   . GLU B 176 ? 0.3987 0.4787 0.4867 -0.1082 -0.0401 0.0273  155 GLU B N   
3572 C CA  . GLU B 176 ? 0.4176 0.5034 0.5217 -0.1035 -0.0560 0.0102  155 GLU B CA  
3573 C C   . GLU B 176 ? 0.3839 0.4397 0.4629 -0.0939 -0.0688 -0.0015 155 GLU B C   
3574 O O   . GLU B 176 ? 0.4067 0.4662 0.4810 -0.0841 -0.0781 -0.0159 155 GLU B O   
3575 C CB  . GLU B 176 ? 0.4654 0.5596 0.6095 -0.1217 -0.0648 0.0102  155 GLU B CB  
3576 C CG  . GLU B 176 ? 0.5077 0.6384 0.6850 -0.1323 -0.0512 0.0227  155 GLU B CG  
3577 C CD  . GLU B 176 ? 0.6092 0.7740 0.7886 -0.1165 -0.0404 0.0208  155 GLU B CD  
3578 O OE1 . GLU B 176 ? 0.5886 0.7628 0.7690 -0.1045 -0.0526 0.0080  155 GLU B OE1 
3579 O OE2 . GLU B 176 ? 0.6364 0.8161 0.8143 -0.1153 -0.0184 0.0326  155 GLU B OE2 
3580 N N   . LEU B 177 ? 0.3742 0.4020 0.4384 -0.0960 -0.0691 0.0062  156 LEU B N   
3581 C CA  . LEU B 177 ? 0.4172 0.4215 0.4601 -0.0845 -0.0771 -0.0028 156 LEU B CA  
3582 C C   . LEU B 177 ? 0.4425 0.4547 0.4572 -0.0704 -0.0719 -0.0064 156 LEU B C   
3583 O O   . LEU B 177 ? 0.3970 0.4034 0.3998 -0.0597 -0.0780 -0.0191 156 LEU B O   
3584 C CB  . LEU B 177 ? 0.5064 0.4843 0.5458 -0.0880 -0.0779 0.0102  156 LEU B CB  
3585 C CG  . LEU B 177 ? 0.5206 0.4781 0.5447 -0.0752 -0.0840 0.0041  156 LEU B CG  
3586 C CD1 . LEU B 177 ? 0.5236 0.4637 0.5588 -0.0729 -0.0925 -0.0141 156 LEU B CD1 
3587 C CD2 . LEU B 177 ? 0.4877 0.4293 0.5088 -0.0762 -0.0835 0.0238  156 LEU B CD2 
3588 N N   . SER B 178 ? 0.3856 0.4083 0.3867 -0.0713 -0.0594 0.0042  157 SER B N   
3589 C CA  . SER B 178 ? 0.3940 0.4193 0.3671 -0.0603 -0.0533 -0.0006 157 SER B CA  
3590 C C   . SER B 178 ? 0.3931 0.4332 0.3729 -0.0499 -0.0537 -0.0134 157 SER B C   
3591 O O   . SER B 178 ? 0.4525 0.4858 0.4135 -0.0390 -0.0556 -0.0217 157 SER B O   
3592 C CB  . SER B 178 ? 0.4389 0.4702 0.3934 -0.0652 -0.0381 0.0105  157 SER B CB  
3593 O OG  . SER B 178 ? 0.4749 0.4951 0.4231 -0.0758 -0.0396 0.0260  157 SER B OG  
3594 N N   . ARG B 179 ? 0.3085 0.3706 0.3169 -0.0536 -0.0521 -0.0130 158 ARG B N   
3595 C CA  . ARG B 179 ? 0.3098 0.3899 0.3296 -0.0432 -0.0560 -0.0219 158 ARG B CA  
3596 C C   . ARG B 179 ? 0.2847 0.3532 0.3003 -0.0397 -0.0736 -0.0339 158 ARG B C   
3597 O O   . ARG B 179 ? 0.3458 0.4136 0.3467 -0.0272 -0.0764 -0.0406 158 ARG B O   
3598 C CB  . ARG B 179 ? 0.4329 0.5447 0.4917 -0.0499 -0.0536 -0.0169 158 ARG B CB  
3599 C CG  . ARG B 179 ? 0.4847 0.6136 0.5474 -0.0480 -0.0313 -0.0073 158 ARG B CG  
3600 C CD  . ARG B 179 ? 0.4443 0.6089 0.5532 -0.0566 -0.0273 0.0001  158 ARG B CD  
3601 N NE  . ARG B 179 ? 0.6174 0.8050 0.7565 -0.0538 -0.0448 -0.0062 158 ARG B NE  
3602 C CZ  . ARG B 179 ? 0.6199 0.8310 0.7718 -0.0378 -0.0438 -0.0074 158 ARG B CZ  
3603 N NH1 . ARG B 179 ? 0.5789 0.7897 0.7170 -0.0219 -0.0236 -0.0050 158 ARG B NH1 
3604 N NH2 . ARG B 179 ? 0.7323 0.9662 0.9103 -0.0378 -0.0639 -0.0110 158 ARG B NH2 
3605 N N   . ASP B 180 ? 0.3119 0.3681 0.3379 -0.0506 -0.0838 -0.0366 159 ASP B N   
3606 C CA  . ASP B 180 ? 0.3603 0.4037 0.3795 -0.0482 -0.0981 -0.0506 159 ASP B CA  
3607 C C   . ASP B 180 ? 0.3751 0.3974 0.3631 -0.0365 -0.0958 -0.0549 159 ASP B C   
3608 O O   . ASP B 180 ? 0.3747 0.3937 0.3482 -0.0284 -0.1022 -0.0652 159 ASP B O   
3609 C CB  . ASP B 180 ? 0.3913 0.4190 0.4268 -0.0626 -0.1062 -0.0542 159 ASP B CB  
3610 C CG  . ASP B 180 ? 0.4560 0.5061 0.5255 -0.0775 -0.1114 -0.0520 159 ASP B CG  
3611 O OD1 . ASP B 180 ? 0.4683 0.5497 0.5505 -0.0743 -0.1134 -0.0513 159 ASP B OD1 
3612 O OD2 . ASP B 180 ? 0.5912 0.6280 0.6779 -0.0926 -0.1134 -0.0497 159 ASP B OD2 
3613 N N   . VAL B 181 ? 0.4056 0.4155 0.3831 -0.0366 -0.0874 -0.0459 160 VAL B N   
3614 C CA  . VAL B 181 ? 0.4409 0.4359 0.3950 -0.0276 -0.0857 -0.0482 160 VAL B CA  
3615 C C   . VAL B 181 ? 0.4532 0.4560 0.3885 -0.0178 -0.0800 -0.0498 160 VAL B C   
3616 O O   . VAL B 181 ? 0.4294 0.4245 0.3484 -0.0097 -0.0813 -0.0561 160 VAL B O   
3617 C CB  . VAL B 181 ? 0.4413 0.4256 0.3924 -0.0321 -0.0816 -0.0359 160 VAL B CB  
3618 C CG1 . VAL B 181 ? 0.4710 0.4472 0.4032 -0.0244 -0.0803 -0.0368 160 VAL B CG1 
3619 C CG2 . VAL B 181 ? 0.4402 0.4107 0.4109 -0.0391 -0.0868 -0.0331 160 VAL B CG2 
3620 N N   . ALA B 182 ? 0.3691 0.3850 0.3064 -0.0182 -0.0715 -0.0436 161 ALA B N   
3621 C CA  . ALA B 182 ? 0.3839 0.4018 0.3048 -0.0078 -0.0642 -0.0453 161 ALA B CA  
3622 C C   . ALA B 182 ? 0.3599 0.3854 0.2841 0.0016  -0.0721 -0.0520 161 ALA B C   
3623 O O   . ALA B 182 ? 0.4137 0.4299 0.3184 0.0106  -0.0711 -0.0549 161 ALA B O   
3624 C CB  . ALA B 182 ? 0.4255 0.4546 0.3502 -0.0084 -0.0508 -0.0391 161 ALA B CB  
3625 N N   . GLN B 183 ? 0.3408 0.3838 0.2889 -0.0018 -0.0810 -0.0535 162 GLN B N   
3626 C CA  . GLN B 183 ? 0.3846 0.4383 0.3340 0.0055  -0.0922 -0.0585 162 GLN B CA  
3627 C C   . GLN B 183 ? 0.3760 0.4109 0.3026 0.0066  -0.1004 -0.0680 162 GLN B C   
3628 O O   . GLN B 183 ? 0.3813 0.4144 0.2899 0.0161  -0.1036 -0.0698 162 GLN B O   
3629 C CB  . GLN B 183 ? 0.3713 0.4508 0.3531 -0.0023 -0.1028 -0.0581 162 GLN B CB  
3630 C CG  . GLN B 183 ? 0.4721 0.5757 0.4809 -0.0016 -0.0917 -0.0478 162 GLN B CG  
3631 C CD  . GLN B 183 ? 0.5188 0.6550 0.5665 -0.0101 -0.1028 -0.0458 162 GLN B CD  
3632 O OE1 . GLN B 183 ? 0.5287 0.6627 0.5867 -0.0253 -0.1144 -0.0513 162 GLN B OE1 
3633 N NE2 . GLN B 183 ? 0.5682 0.7346 0.6401 -0.0003 -0.0990 -0.0377 162 GLN B NE2 
3634 N N   . ARG B 184 ? 0.4058 0.4258 0.3332 -0.0022 -0.1023 -0.0730 163 ARG B N   
3635 C CA  . ARG B 184 ? 0.4593 0.4609 0.3671 0.0000  -0.1060 -0.0832 163 ARG B CA  
3636 C C   . ARG B 184 ? 0.4165 0.4073 0.3030 0.0087  -0.0942 -0.0786 163 ARG B C   
3637 O O   . ARG B 184 ? 0.4501 0.4364 0.3229 0.0132  -0.0901 -0.0794 163 ARG B O   
3638 C CB  . ARG B 184 ? 0.4433 0.4292 0.3623 -0.0090 -0.1065 -0.0872 163 ARG B CB  
3639 C CG  . ARG B 184 ? 0.5122 0.4774 0.4159 -0.0053 -0.1046 -0.0975 163 ARG B CG  
3640 C CD  . ARG B 184 ? 0.4440 0.3913 0.3642 -0.0120 -0.1047 -0.1001 163 ARG B CD  
3641 N NE  . ARG B 184 ? 0.4473 0.3975 0.3864 -0.0246 -0.1140 -0.1036 163 ARG B NE  
3642 C CZ  . ARG B 184 ? 0.4658 0.4079 0.4278 -0.0340 -0.1133 -0.0970 163 ARG B CZ  
3643 N NH1 . ARG B 184 ? 0.4461 0.3778 0.4144 -0.0311 -0.1052 -0.0852 163 ARG B NH1 
3644 N NH2 . ARG B 184 ? 0.4688 0.4148 0.4489 -0.0477 -0.1218 -0.1006 163 ARG B NH2 
3645 N N   . PHE B 185 ? 0.3791 0.3667 0.2649 0.0082  -0.0867 -0.0716 164 PHE B N   
3646 C CA  . PHE B 185 ? 0.3968 0.3755 0.2655 0.0128  -0.0769 -0.0675 164 PHE B CA  
3647 C C   . PHE B 185 ? 0.4183 0.3997 0.2756 0.0208  -0.0730 -0.0645 164 PHE B C   
3648 O O   . PHE B 185 ? 0.3978 0.3721 0.2439 0.0240  -0.0670 -0.0626 164 PHE B O   
3649 C CB  . PHE B 185 ? 0.4122 0.3883 0.2811 0.0072  -0.0715 -0.0604 164 PHE B CB  
3650 C CG  . PHE B 185 ? 0.3403 0.3078 0.1947 0.0073  -0.0649 -0.0575 164 PHE B CG  
3651 C CD1 . PHE B 185 ? 0.3877 0.3514 0.2294 0.0091  -0.0565 -0.0547 164 PHE B CD1 
3652 C CD2 . PHE B 185 ? 0.3406 0.3043 0.1987 0.0052  -0.0666 -0.0568 164 PHE B CD2 
3653 C CE1 . PHE B 185 ? 0.3662 0.3236 0.1999 0.0054  -0.0504 -0.0518 164 PHE B CE1 
3654 C CE2 . PHE B 185 ? 0.3426 0.3033 0.1917 0.0035  -0.0622 -0.0535 164 PHE B CE2 
3655 C CZ  . PHE B 185 ? 0.3993 0.3576 0.2370 0.0018  -0.0539 -0.0510 164 PHE B CZ  
3656 N N   . ASN B 186 ? 0.4238 0.4163 0.2861 0.0250  -0.0759 -0.0630 165 ASN B N   
3657 C CA  . ASN B 186 ? 0.4604 0.4536 0.3132 0.0362  -0.0731 -0.0590 165 ASN B CA  
3658 C C   . ASN B 186 ? 0.3886 0.3866 0.2338 0.0419  -0.0835 -0.0608 165 ASN B C   
3659 O O   . ASN B 186 ? 0.4294 0.4204 0.2585 0.0508  -0.0808 -0.0558 165 ASN B O   
3660 C CB  . ASN B 186 ? 0.4141 0.4227 0.2867 0.0401  -0.0690 -0.0534 165 ASN B CB  
3661 C CG  . ASN B 186 ? 0.4178 0.4185 0.2892 0.0347  -0.0550 -0.0515 165 ASN B CG  
3662 O OD1 . ASN B 186 ? 0.4401 0.4228 0.2927 0.0292  -0.0495 -0.0528 165 ASN B OD1 
3663 N ND2 . ASN B 186 ? 0.4127 0.4290 0.3039 0.0353  -0.0491 -0.0480 165 ASN B ND2 
3664 N N   . ALA B 187 ? 0.3900 0.3976 0.2477 0.0344  -0.0931 -0.0659 166 ALA B N   
3665 C CA  . ALA B 187 ? 0.4800 0.4910 0.3295 0.0350  -0.1001 -0.0666 166 ALA B CA  
3666 C C   . ALA B 187 ? 0.4206 0.4139 0.2504 0.0343  -0.0893 -0.0667 166 ALA B C   
3667 O O   . ALA B 187 ? 0.5725 0.5655 0.3859 0.0375  -0.0918 -0.0647 166 ALA B O   
3668 C CB  . ALA B 187 ? 0.3613 0.3820 0.2247 0.0240  -0.1117 -0.0745 166 ALA B CB  
3669 N N   . ILE B 188 ? 0.4530 0.4346 0.2846 0.0302  -0.0786 -0.0682 167 ILE B N   
3670 C CA  . ILE B 188 ? 0.4789 0.4494 0.2969 0.0301  -0.0688 -0.0687 167 ILE B CA  
3671 C C   . ILE B 188 ? 0.4787 0.4421 0.2858 0.0348  -0.0601 -0.0603 167 ILE B C   
3672 O O   . ILE B 188 ? 0.4820 0.4399 0.2722 0.0377  -0.0555 -0.0578 167 ILE B O   
3673 C CB  . ILE B 188 ? 0.4601 0.4244 0.2875 0.0252  -0.0648 -0.0747 167 ILE B CB  
3674 C CG1 . ILE B 188 ? 0.4409 0.4047 0.2744 0.0209  -0.0726 -0.0852 167 ILE B CG1 
3675 C CG2 . ILE B 188 ? 0.4604 0.4168 0.2757 0.0275  -0.0545 -0.0756 167 ILE B CG2 
3676 C CD1 . ILE B 188 ? 0.4695 0.4254 0.3165 0.0185  -0.0729 -0.0905 167 ILE B CD1 
3677 N N   . TYR B 189 ? 0.4258 0.3870 0.2391 0.0347  -0.0574 -0.0566 168 TYR B N   
3678 C CA  . TYR B 189 ? 0.4265 0.3758 0.2287 0.0352  -0.0481 -0.0514 168 TYR B CA  
3679 C C   . TYR B 189 ? 0.4373 0.3780 0.2276 0.0444  -0.0476 -0.0468 168 TYR B C   
3680 O O   . TYR B 189 ? 0.4803 0.4039 0.2558 0.0451  -0.0393 -0.0432 168 TYR B O   
3681 C CB  . TYR B 189 ? 0.4278 0.3759 0.2394 0.0260  -0.0440 -0.0524 168 TYR B CB  
3682 C CG  . TYR B 189 ? 0.4358 0.3876 0.2539 0.0220  -0.0442 -0.0562 168 TYR B CG  
3683 C CD1 . TYR B 189 ? 0.4419 0.3892 0.2491 0.0229  -0.0382 -0.0564 168 TYR B CD1 
3684 C CD2 . TYR B 189 ? 0.4292 0.3862 0.2611 0.0194  -0.0505 -0.0603 168 TYR B CD2 
3685 C CE1 . TYR B 189 ? 0.3974 0.3461 0.2070 0.0236  -0.0377 -0.0620 168 TYR B CE1 
3686 C CE2 . TYR B 189 ? 0.4492 0.4045 0.2841 0.0202  -0.0516 -0.0655 168 TYR B CE2 
3687 C CZ  . TYR B 189 ? 0.4130 0.3647 0.2367 0.0236  -0.0449 -0.0672 168 TYR B CZ  
3688 O OH  . TYR B 189 ? 0.4210 0.3726 0.2524 0.0272  -0.0431 -0.0726 168 TYR B OH  
3689 N N   . GLY B 190 ? 0.2952 0.4625 0.3032 0.0958  -0.0983 -0.0141 169 GLY B N   
3690 C CA  . GLY B 190 ? 0.3473 0.5336 0.3681 0.1062  -0.0871 -0.0028 169 GLY B CA  
3691 C C   . GLY B 190 ? 0.3436 0.5227 0.3688 0.0937  -0.0853 -0.0052 169 GLY B C   
3692 O O   . GLY B 190 ? 0.3378 0.4999 0.3572 0.0780  -0.0942 -0.0152 169 GLY B O   
3693 N N   . ASP B 191 ? 0.4377 0.6291 0.4735 0.1023  -0.0711 0.0058  170 ASP B N   
3694 C CA  . ASP B 191 ? 0.4656 0.6536 0.5057 0.0920  -0.0670 0.0055  170 ASP B CA  
3695 C C   . ASP B 191 ? 0.4228 0.5692 0.4515 0.0836  -0.0584 -0.0027 170 ASP B C   
3696 O O   . ASP B 191 ? 0.4676 0.5964 0.4934 0.0892  -0.0383 0.0015  170 ASP B O   
3697 C CB  . ASP B 191 ? 0.4891 0.7029 0.5441 0.1060  -0.0510 0.0226  170 ASP B CB  
3698 C CG  . ASP B 191 ? 0.5349 0.8004 0.6030 0.1106  -0.0621 0.0341  170 ASP B CG  
3699 O OD1 . ASP B 191 ? 0.5358 0.8191 0.6037 0.0937  -0.0803 0.0280  170 ASP B OD1 
3700 O OD2 . ASP B 191 ? 0.6556 0.9453 0.7333 0.1296  -0.0522 0.0501  170 ASP B OD2 
3701 N N   . ILE B 192 ? 0.3042 0.4349 0.3249 0.0684  -0.0725 -0.0137 171 ILE B N   
3702 C CA  . ILE B 192 ? 0.2986 0.3990 0.3094 0.0562  -0.0683 -0.0192 171 ILE B CA  
3703 C C   . ILE B 192 ? 0.2709 0.3696 0.2821 0.0412  -0.0695 -0.0218 171 ILE B C   
3704 O O   . ILE B 192 ? 0.2609 0.3405 0.2637 0.0336  -0.0575 -0.0225 171 ILE B O   
3705 C CB  . ILE B 192 ? 0.3590 0.4469 0.3641 0.0503  -0.0806 -0.0245 171 ILE B CB  
3706 C CG1 . ILE B 192 ? 0.3596 0.4504 0.3644 0.0658  -0.0802 -0.0221 171 ILE B CG1 
3707 C CG2 . ILE B 192 ? 0.2702 0.3353 0.2664 0.0374  -0.0765 -0.0258 171 ILE B CG2 
3708 C CD1 . ILE B 192 ? 0.4080 0.4845 0.4084 0.0744  -0.0644 -0.0181 171 ILE B CD1 
3709 N N   . PHE B 193 ? 0.2988 0.4160 0.3171 0.0351  -0.0829 -0.0237 172 PHE B N   
3710 C CA  . PHE B 193 ? 0.2730 0.3907 0.2932 0.0212  -0.0855 -0.0258 172 PHE B CA  
3711 C C   . PHE B 193 ? 0.2913 0.4347 0.3235 0.0274  -0.0793 -0.0182 172 PHE B C   
3712 O O   . PHE B 193 ? 0.2230 0.3937 0.2641 0.0381  -0.0818 -0.0118 172 PHE B O   
3713 C CB  . PHE B 193 ? 0.2264 0.3454 0.2467 0.0087  -0.1026 -0.0324 172 PHE B CB  
3714 C CG  . PHE B 193 ? 0.2423 0.3404 0.2551 0.0042  -0.1076 -0.0355 172 PHE B CG  
3715 C CD1 . PHE B 193 ? 0.2653 0.3464 0.2719 -0.0043 -0.1031 -0.0342 172 PHE B CD1 
3716 C CD2 . PHE B 193 ? 0.2739 0.3707 0.2850 0.0071  -0.1159 -0.0382 172 PHE B CD2 
3717 C CE1 . PHE B 193 ? 0.2440 0.3138 0.2475 -0.0082 -0.1081 -0.0324 172 PHE B CE1 
3718 C CE2 . PHE B 193 ? 0.2187 0.2981 0.2261 0.0056  -0.1180 -0.0372 172 PHE B CE2 
3719 C CZ  . PHE B 193 ? 0.2509 0.3202 0.2568 -0.0014 -0.1148 -0.0327 172 PHE B CZ  
3720 N N   . LYS B 194 ? 0.2510 0.3880 0.2833 0.0202  -0.0709 -0.0170 173 LYS B N   
3721 C CA  . LYS B 194 ? 0.3233 0.4880 0.3699 0.0217  -0.0693 -0.0092 173 LYS B CA  
3722 C C   . LYS B 194 ? 0.2343 0.4130 0.2846 0.0066  -0.0895 -0.0157 173 LYS B C   
3723 O O   . LYS B 194 ? 0.2896 0.4475 0.3309 -0.0064 -0.0981 -0.0252 173 LYS B O   
3724 C CB  . LYS B 194 ? 0.3349 0.4839 0.3787 0.0193  -0.0509 -0.0058 173 LYS B CB  
3725 C CG  . LYS B 194 ? 0.4643 0.6130 0.5118 0.0380  -0.0252 0.0069  173 LYS B CG  
3726 C CD  . LYS B 194 ? 0.5336 0.6440 0.5616 0.0398  -0.0100 0.0016  173 LYS B CD  
3727 C CE  . LYS B 194 ? 0.5823 0.6841 0.6112 0.0587  0.0211  0.0141  173 LYS B CE  
3728 N NZ  . LYS B 194 ? 0.7295 0.7854 0.7331 0.0538  0.0394  0.0061  173 LYS B NZ  
3729 N N   . VAL B 195 ? 0.2519 0.4672 0.3155 0.0075  -0.0957 -0.0090 174 VAL B N   
3730 C CA  . VAL B 195 ? 0.3192 0.5475 0.3844 -0.0096 -0.1123 -0.0155 174 VAL B CA  
3731 C C   . VAL B 195 ? 0.3312 0.5604 0.4034 -0.0178 -0.1073 -0.0128 174 VAL B C   
3732 O O   . VAL B 195 ? 0.2830 0.5385 0.3696 -0.0103 -0.0984 0.0004  174 VAL B O   
3733 C CB  . VAL B 195 ? 0.3226 0.5930 0.3956 -0.0099 -0.1226 -0.0098 174 VAL B CB  
3734 C CG1 . VAL B 195 ? 0.3339 0.5926 0.4007 -0.0298 -0.1316 -0.0177 174 VAL B CG1 
3735 C CG2 . VAL B 195 ? 0.3482 0.6113 0.4113 -0.0012 -0.1245 -0.0121 174 VAL B CG2 
3736 N N   . PRO B 196 ? 0.3761 0.5793 0.4399 -0.0318 -0.1115 -0.0225 175 PRO B N   
3737 C CA  . PRO B 196 ? 0.3995 0.6004 0.4679 -0.0390 -0.1051 -0.0199 175 PRO B CA  
3738 C C   . PRO B 196 ? 0.4311 0.6660 0.5138 -0.0471 -0.1128 -0.0154 175 PRO B C   
3739 O O   . PRO B 196 ? 0.4524 0.7014 0.5350 -0.0552 -0.1259 -0.0197 175 PRO B O   
3740 C CB  . PRO B 196 ? 0.3407 0.5094 0.3963 -0.0523 -0.1102 -0.0301 175 PRO B CB  
3741 C CG  . PRO B 196 ? 0.3983 0.5627 0.4486 -0.0553 -0.1229 -0.0374 175 PRO B CG  
3742 C CD  . PRO B 196 ? 0.3507 0.5280 0.4019 -0.0409 -0.1212 -0.0339 175 PRO B CD  
3743 N N   . GLU B 197 ? 0.2999 0.5438 0.3926 -0.0459 -0.1022 -0.0066 176 GLU B N   
3744 C CA  . GLU B 197 ? 0.4381 0.7167 0.5467 -0.0544 -0.1081 0.0001  176 GLU B CA  
3745 C C   . GLU B 197 ? 0.4373 0.6973 0.5435 -0.0678 -0.1072 -0.0053 176 GLU B C   
3746 O O   . GLU B 197 ? 0.3786 0.6099 0.4763 -0.0648 -0.0943 -0.0060 176 GLU B O   
3747 C CB  . GLU B 197 ? 0.4176 0.7323 0.5461 -0.0383 -0.0945 0.0209  176 GLU B CB  
3748 C CG  . GLU B 197 ? 0.5373 0.8725 0.6703 -0.0214 -0.0915 0.0305  176 GLU B CG  
3749 C CD  . GLU B 197 ? 0.5779 0.9404 0.7094 -0.0320 -0.1129 0.0255  176 GLU B CD  
3750 O OE1 . GLU B 197 ? 0.5986 0.9593 0.7263 -0.0491 -0.1222 0.0189  176 GLU B OE1 
3751 O OE2 . GLU B 197 ? 0.6176 0.9828 0.7442 -0.0218 -0.1139 0.0263  176 GLU B OE2 
3752 N N   . PRO B 198 ? 0.5308 0.8052 0.6419 -0.0845 -0.1198 -0.0093 177 PRO B N   
3753 C CA  . PRO B 198 ? 0.5541 0.8160 0.6662 -0.0956 -0.1173 -0.0113 177 PRO B CA  
3754 C C   . PRO B 198 ? 0.6028 0.8822 0.7296 -0.0864 -0.1020 0.0038  177 PRO B C   
3755 O O   . PRO B 198 ? 0.5430 0.8574 0.6857 -0.0747 -0.0966 0.0187  177 PRO B O   
3756 C CB  . PRO B 198 ? 0.5694 0.8238 0.6787 -0.1046 -0.1240 -0.0181 177 PRO B CB  
3757 C CG  . PRO B 198 ? 0.5452 0.8236 0.6569 -0.1003 -0.1286 -0.0143 177 PRO B CG  
3758 C CD  . PRO B 198 ? 0.6077 0.8829 0.7143 -0.0879 -0.1274 -0.0138 177 PRO B CD  
3759 N N   . PHE B 199 ? 0.6498 0.9052 0.7712 -0.0912 -0.0933 0.0019  178 PHE B N   
3760 C CA  . PHE B 199 ? 0.7780 1.0362 0.9069 -0.0815 -0.0732 0.0148  178 PHE B CA  
3761 C C   . PHE B 199 ? 0.7526 1.0182 0.8901 -0.0943 -0.0750 0.0164  178 PHE B C   
3762 O O   . PHE B 199 ? 0.6219 0.8699 0.7505 -0.1100 -0.0861 0.0045  178 PHE B O   
3763 C CB  . PHE B 199 ? 0.7188 0.9333 0.8255 -0.0751 -0.0557 0.0103  178 PHE B CB  
3764 C CG  . PHE B 199 ? 0.8174 1.0110 0.9169 -0.0784 -0.0383 0.0129  178 PHE B CG  
3765 C CD1 . PHE B 199 ? 0.8577 1.0660 0.9711 -0.0664 -0.0183 0.0288  178 PHE B CD1 
3766 C CD2 . PHE B 199 ? 0.8128 0.9726 0.8907 -0.0930 -0.0403 0.0012  178 PHE B CD2 
3767 C CE1 . PHE B 199 ? 0.8791 1.0630 0.9823 -0.0696 0.0003  0.0305  178 PHE B CE1 
3768 C CE2 . PHE B 199 ? 0.9292 1.0685 0.9962 -0.0982 -0.0241 0.0027  178 PHE B CE2 
3769 C CZ  . PHE B 199 ? 0.8882 1.0366 0.9664 -0.0867 -0.0032 0.0161  178 PHE B CZ  
3770 N N   . ILE B 200 ? 1.0399 1.3329 1.1965 -0.0862 -0.0626 0.0332  179 ILE B N   
3771 C CA  . ILE B 200 ? 1.0741 1.3843 1.2445 -0.0971 -0.0645 0.0383  179 ILE B CA  
3772 C C   . ILE B 200 ? 1.0662 1.3538 1.2326 -0.0887 -0.0396 0.0460  179 ILE B C   
3773 O O   . ILE B 200 ? 1.0633 1.3345 1.2226 -0.0721 -0.0183 0.0527  179 ILE B O   
3774 C CB  . ILE B 200 ? 1.1065 1.4772 1.3058 -0.0976 -0.0726 0.0546  179 ILE B CB  
3775 C CG1 . ILE B 200 ? 1.1228 1.5208 1.3415 -0.0741 -0.0511 0.0797  179 ILE B CG1 
3776 C CG2 . ILE B 200 ? 1.0291 1.4191 1.2262 -0.1058 -0.0936 0.0469  179 ILE B CG2 
3777 C CD1 . ILE B 200 ? 1.1000 1.5101 1.3356 -0.0698 -0.0340 0.0964  179 ILE B CD1 
3778 N N   . PRO B 201 ? 1.0965 1.3808 1.2658 -0.1000 -0.0391 0.0456  180 PRO B N   
3779 C CA  . PRO B 201 ? 1.0979 1.3554 1.2584 -0.0951 -0.0148 0.0508  180 PRO B CA  
3780 C C   . PRO B 201 ? 1.0920 1.3582 1.2629 -0.0721 0.0132  0.0707  180 PRO B C   
3781 O O   . PRO B 201 ? 1.0330 1.2621 1.1860 -0.0662 0.0390  0.0717  180 PRO B O   
3782 C CB  . PRO B 201 ? 1.0981 1.3741 1.2738 -0.1079 -0.0215 0.0543  180 PRO B CB  
3783 C CG  . PRO B 201 ? 1.0747 1.3629 1.2525 -0.1254 -0.0495 0.0416  180 PRO B CG  
3784 C CD  . PRO B 201 ? 1.0802 1.3872 1.2613 -0.1187 -0.0594 0.0413  180 PRO B CD  
3785 N N   . GLY B 204 ? 0.8189 1.0151 0.9682 -0.0974 0.0664  0.0779  183 GLY B N   
3786 C CA  . GLY B 204 ? 0.7886 1.0080 0.9487 -0.1147 0.0326  0.0676  183 GLY B CA  
3787 C C   . GLY B 204 ? 0.8460 1.0698 1.0134 -0.1278 0.0286  0.0683  183 GLY B C   
3788 O O   . GLY B 204 ? 0.9494 1.2149 1.1466 -0.1313 0.0172  0.0776  183 GLY B O   
3789 N N   . ALA B 205 ? 0.8785 1.0606 1.0174 -0.1370 0.0379  0.0588  184 ALA B N   
3790 C CA  . ALA B 205 ? 0.8415 1.0239 0.9847 -0.1488 0.0361  0.0597  184 ALA B CA  
3791 C C   . ALA B 205 ? 0.8534 1.0547 1.0087 -0.1648 0.0063  0.0508  184 ALA B C   
3792 O O   . ALA B 205 ? 0.8554 1.0433 0.9963 -0.1721 -0.0096 0.0376  184 ALA B O   
3793 C CB  . ALA B 205 ? 0.8551 0.9892 0.9607 -0.1575 0.0509  0.0508  184 ALA B CB  
3794 N N   . ARG B 206 ? 0.8446 1.0752 1.0256 -0.1703 0.0011  0.0590  185 ARG B N   
3795 C CA  . ARG B 206 ? 0.8048 1.0488 0.9957 -0.1871 -0.0223 0.0507  185 ARG B CA  
3796 C C   . ARG B 206 ? 0.7870 1.0023 0.9624 -0.1993 -0.0215 0.0442  185 ARG B C   
3797 O O   . ARG B 206 ? 0.8421 1.0557 1.0212 -0.1992 -0.0079 0.0524  185 ARG B O   
3798 C CB  . ARG B 206 ? 0.8269 1.1196 1.0522 -0.1906 -0.0286 0.0629  185 ARG B CB  
3799 N N   . VAL B 207 ? 0.7592 0.9535 0.9181 -0.2087 -0.0348 0.0316  186 VAL B N   
3800 C CA  . VAL B 207 ? 0.7579 0.9301 0.9043 -0.2201 -0.0361 0.0279  186 VAL B CA  
3801 C C   . VAL B 207 ? 0.8059 0.9797 0.9604 -0.2258 -0.0515 0.0209  186 VAL B C   
3802 O O   . VAL B 207 ? 0.7472 0.9146 0.8958 -0.2194 -0.0605 0.0130  186 VAL B O   
3803 C CB  . VAL B 207 ? 0.7780 0.9182 0.8921 -0.2207 -0.0323 0.0227  186 VAL B CB  
3804 C CG1 . VAL B 207 ? 0.7689 0.8942 0.8726 -0.2325 -0.0346 0.0228  186 VAL B CG1 
3805 C CG2 . VAL B 207 ? 0.6123 0.7390 0.7097 -0.2124 -0.0117 0.0263  186 VAL B CG2 
3806 N N   . MET B 208 ? 0.7752 0.9488 0.9383 -0.2306 -0.0499 0.0229  187 MET B N   
3807 C CA  . MET B 208 ? 0.7767 0.9430 0.9437 -0.2309 -0.0571 0.0156  187 MET B CA  
3808 C C   . MET B 208 ? 0.7467 0.8863 0.9008 -0.2326 -0.0552 0.0146  187 MET B C   
3809 O O   . MET B 208 ? 0.7812 0.9133 0.9264 -0.2356 -0.0487 0.0208  187 MET B O   
3810 C CB  . MET B 208 ? 0.7348 0.9228 0.9226 -0.2372 -0.0561 0.0191  187 MET B CB  
3811 C CG  . MET B 208 ? 0.7778 0.9971 0.9802 -0.2365 -0.0620 0.0200  187 MET B CG  
3812 S SD  . MET B 208 ? 0.9218 1.1352 1.1125 -0.2300 -0.0723 0.0090  187 MET B SD  
3813 C CE  . MET B 208 ? 0.8167 1.0640 1.0182 -0.2230 -0.0708 0.0206  187 MET B CE  
3814 N N   . SER B 209 ? 0.7417 0.8685 0.8947 -0.2322 -0.0595 0.0083  188 SER B N   
3815 C CA  . SER B 209 ? 0.8205 0.9274 0.9670 -0.2347 -0.0565 0.0112  188 SER B CA  
3816 C C   . SER B 209 ? 0.8889 0.9973 1.0437 -0.2420 -0.0496 0.0173  188 SER B C   
3817 O O   . SER B 209 ? 0.8521 0.9719 1.0212 -0.2468 -0.0482 0.0156  188 SER B O   
3818 C CB  . SER B 209 ? 0.8901 0.9835 1.0381 -0.2362 -0.0585 0.0047  188 SER B CB  
3819 O OG  . SER B 209 ? 1.0077 1.1018 1.1497 -0.2297 -0.0646 -0.0017 188 SER B OG  
3820 N N   . LEU B 210 ? 0.8050 0.9039 0.9501 -0.2435 -0.0455 0.0256  189 LEU B N   
3821 C CA  . LEU B 210 ? 0.8223 0.9229 0.9728 -0.2495 -0.0380 0.0327  189 LEU B CA  
3822 C C   . LEU B 210 ? 0.8817 0.9764 1.0468 -0.2552 -0.0346 0.0314  189 LEU B C   
3823 O O   . LEU B 210 ? 0.8798 0.9847 1.0586 -0.2598 -0.0315 0.0304  189 LEU B O   
3824 C CB  . LEU B 210 ? 0.7716 0.8643 0.9051 -0.2512 -0.0350 0.0425  189 LEU B CB  
3825 C CG  . LEU B 210 ? 0.8740 0.9685 0.9876 -0.2507 -0.0345 0.0434  189 LEU B CG  
3826 C CD1 . LEU B 210 ? 0.8134 0.9018 0.9070 -0.2566 -0.0310 0.0530  189 LEU B CD1 
3827 C CD2 . LEU B 210 ? 0.6810 0.7857 0.8012 -0.2525 -0.0279 0.0418  189 LEU B CD2 
3828 N N   . LEU B 211 ? 0.8566 0.9348 1.0194 -0.2562 -0.0335 0.0330  190 LEU B N   
3829 C CA  . LEU B 211 ? 0.8686 0.9344 1.0425 -0.2638 -0.0263 0.0325  190 LEU B CA  
3830 C C   . LEU B 211 ? 0.8372 0.9006 1.0175 -0.2680 -0.0284 0.0192  190 LEU B C   
3831 O O   . LEU B 211 ? 0.8985 0.9470 1.0849 -0.2766 -0.0213 0.0166  190 LEU B O   
3832 C CB  . LEU B 211 ? 0.8468 0.8943 1.0170 -0.2646 -0.0205 0.0435  190 LEU B CB  
3833 C CG  . LEU B 211 ? 0.9570 1.0108 1.1179 -0.2617 -0.0206 0.0594  190 LEU B CG  
3834 C CD1 . LEU B 211 ? 0.8666 0.9077 1.0312 -0.2636 -0.0122 0.0762  190 LEU B CD1 
3835 C CD2 . LEU B 211 ? 0.9596 1.0246 1.1207 -0.2638 -0.0179 0.0616  190 LEU B CD2 
3836 N N   . GLU B 212 ? 0.8663 0.9428 1.0436 -0.2633 -0.0372 0.0115  191 GLU B N   
3837 C CA  . GLU B 212 ? 0.9005 0.9796 1.0812 -0.2686 -0.0408 0.0000  191 GLU B CA  
3838 C C   . GLU B 212 ? 0.8382 0.9440 1.0204 -0.2631 -0.0497 -0.0027 191 GLU B C   
3839 O O   . GLU B 212 ? 0.7916 0.8980 0.9668 -0.2586 -0.0557 -0.0086 191 GLU B O   
3840 C CB  . GLU B 212 ? 0.9006 0.9551 1.0716 -0.2698 -0.0394 -0.0056 191 GLU B CB  
3841 N N   . PRO B 213 ? 0.7785 0.9472 1.2910 -0.1649 -0.0272 0.0619  192 PRO B N   
3842 C CA  . PRO B 213 ? 0.7628 0.9636 1.2504 -0.1686 -0.0258 0.0633  192 PRO B CA  
3843 C C   . PRO B 213 ? 0.7951 1.0065 1.2804 -0.1797 -0.0347 0.0376  192 PRO B C   
3844 O O   . PRO B 213 ? 0.8313 1.0674 1.2928 -0.1825 -0.0361 0.0351  192 PRO B O   
3845 C CB  . PRO B 213 ? 0.7121 0.9187 1.2091 -0.1753 -0.0234 0.0925  192 PRO B CB  
3846 C CG  . PRO B 213 ? 0.7624 0.9417 1.2740 -0.1715 -0.0194 0.1104  192 PRO B CG  
3847 C CD  . PRO B 213 ? 0.7435 0.8972 1.2736 -0.1695 -0.0262 0.0899  192 PRO B CD  
3848 N N   . LYS B 216 ? 0.6505 0.9080 1.0184 -0.1521 -0.0082 -0.0273 195 LYS B N   
3849 C CA  . LYS B 216 ? 0.7987 1.0724 1.1449 -0.1434 -0.0010 -0.0071 195 LYS B CA  
3850 C C   . LYS B 216 ? 0.7864 1.0502 1.1415 -0.1283 0.0085  -0.0063 195 LYS B C   
3851 O O   . LYS B 216 ? 0.6175 0.8718 0.9813 -0.1244 0.0128  -0.0306 195 LYS B O   
3852 C CB  . LYS B 216 ? 0.6609 0.9565 0.9679 -0.1489 0.0006  -0.0173 195 LYS B CB  
3853 N N   . MET B 217 ? 0.6659 0.9318 1.0203 -0.1202 0.0115  0.0211  196 MET B N   
3854 C CA  . MET B 217 ? 0.6848 0.9419 1.0464 -0.1063 0.0177  0.0249  196 MET B CA  
3855 C C   . MET B 217 ? 0.7191 0.9889 1.0623 -0.1017 0.0266  0.0030  196 MET B C   
3856 O O   . MET B 217 ? 0.7568 1.0471 1.0690 -0.1051 0.0307  0.0036  196 MET B O   
3857 C CB  . MET B 217 ? 0.5992 0.8600 0.9526 -0.1008 0.0200  0.0569  196 MET B CB  
3858 C CG  . MET B 217 ? 0.5758 0.8240 0.9385 -0.0878 0.0227  0.0640  196 MET B CG  
3859 S SD  . MET B 217 ? 0.4882 0.7382 0.8355 -0.0832 0.0258  0.0996  196 MET B SD  
3860 C CE  . MET B 217 ? 0.5136 0.7406 0.8822 -0.0909 0.0189  0.1198  196 MET B CE  
3861 N N   . SER B 218 ? 0.8140 1.0712 1.1786 -0.0943 0.0299  -0.0163 197 SER B N   
3862 C CA  . SER B 218 ? 0.9042 1.1722 1.2578 -0.0908 0.0407  -0.0413 197 SER B CA  
3863 C C   . SER B 218 ? 0.8762 1.1360 1.2541 -0.0758 0.0445  -0.0408 197 SER B C   
3864 O O   . SER B 218 ? 0.8651 1.1040 1.2754 -0.0694 0.0368  -0.0324 197 SER B O   
3865 C CB  . SER B 218 ? 0.9153 1.1783 1.2741 -0.0995 0.0426  -0.0762 197 SER B CB  
3866 O OG  . SER B 218 ? 1.0176 1.2564 1.4183 -0.0954 0.0376  -0.0856 197 SER B OG  
3867 N N   . LYS B 219 ? 0.8235 1.0996 1.1860 -0.0708 0.0554  -0.0491 198 LYS B N   
3868 C CA  . LYS B 219 ? 0.7731 1.0444 1.1619 -0.0569 0.0588  -0.0526 198 LYS B CA  
3869 C C   . LYS B 219 ? 1.0895 1.3478 1.5159 -0.0534 0.0616  -0.0839 198 LYS B C   
3870 O O   . LYS B 219 ? 0.8784 1.1277 1.3397 -0.0411 0.0603  -0.0861 198 LYS B O   
3871 C CB  . LYS B 219 ? 1.0431 1.3367 1.4071 -0.0538 0.0708  -0.0545 198 LYS B CB  
3872 N N   . SER B 220 ? 0.8270 1.0838 1.2487 -0.0643 0.0648  -0.1085 199 SER B N   
3873 C CA  . SER B 220 ? 0.7585 1.0022 1.2155 -0.0626 0.0693  -0.1418 199 SER B CA  
3874 C C   . SER B 220 ? 0.7758 0.9922 1.2689 -0.0620 0.0551  -0.1368 199 SER B C   
3875 O O   . SER B 220 ? 0.7461 0.9484 1.2721 -0.0610 0.0574  -0.1643 199 SER B O   
3876 C CB  . SER B 220 ? 0.7767 1.0313 1.2054 -0.0767 0.0812  -0.1739 199 SER B CB  
3877 O OG  . SER B 220 ? 0.9003 1.1561 1.2982 -0.0909 0.0723  -0.1637 199 SER B OG  
3878 N N   . ASP B 221 ? 0.8263 1.0342 1.3148 -0.0631 0.0418  -0.1031 200 ASP B N   
3879 C CA  . ASP B 221 ? 0.7704 0.9522 1.2884 -0.0654 0.0289  -0.0962 200 ASP B CA  
3880 C C   . ASP B 221 ? 0.7818 0.9411 1.3515 -0.0524 0.0244  -0.1043 200 ASP B C   
3881 O O   . ASP B 221 ? 0.6457 0.8036 1.2280 -0.0400 0.0215  -0.0890 200 ASP B O   
3882 C CB  . ASP B 221 ? 0.7872 0.9650 1.2908 -0.0683 0.0184  -0.0564 200 ASP B CB  
3883 C CG  . ASP B 221 ? 0.7904 0.9536 1.3015 -0.0803 0.0093  -0.0519 200 ASP B CG  
3884 O OD1 . ASP B 221 ? 0.7756 0.9167 1.3215 -0.0804 0.0043  -0.0674 200 ASP B OD1 
3885 O OD2 . ASP B 221 ? 0.8804 1.0543 1.3656 -0.0897 0.0072  -0.0334 200 ASP B OD2 
3886 N N   . ASP B 222 ? 0.7652 0.9063 1.3664 -0.0553 0.0227  -0.1288 201 ASP B N   
3887 C CA  . ASP B 222 ? 0.7936 0.9094 1.4502 -0.0432 0.0156  -0.1349 201 ASP B CA  
3888 C C   . ASP B 222 ? 0.8052 0.8962 1.4770 -0.0405 -0.0027 -0.0977 201 ASP B C   
3889 O O   . ASP B 222 ? 0.7353 0.8050 1.4489 -0.0289 -0.0124 -0.0925 201 ASP B O   
3890 C CB  . ASP B 222 ? 0.8338 0.9355 1.5200 -0.0481 0.0196  -0.1726 201 ASP B CB  
3891 N N   . ASN B 223 ? 0.7513 0.8442 1.3911 -0.0516 -0.0076 -0.0718 202 ASN B N   
3892 C CA  . ASN B 223 ? 0.7101 0.7811 1.3559 -0.0521 -0.0219 -0.0349 202 ASN B CA  
3893 C C   . ASN B 223 ? 0.7207 0.8077 1.3304 -0.0492 -0.0206 -0.0046 202 ASN B C   
3894 O O   . ASN B 223 ? 0.6977 0.8069 1.2683 -0.0575 -0.0133 0.0025  202 ASN B O   
3895 C CB  . ASN B 223 ? 0.6949 0.7562 1.3349 -0.0676 -0.0263 -0.0287 202 ASN B CB  
3896 C CG  . ASN B 223 ? 0.7021 0.7320 1.3617 -0.0691 -0.0404 0.0016  202 ASN B CG  
3897 O OD1 . ASN B 223 ? 0.6802 0.7012 1.3371 -0.0618 -0.0467 0.0287  202 ASN B OD1 
3898 N ND2 . ASN B 223 ? 0.6447 0.6564 1.3224 -0.0798 -0.0458 -0.0028 202 ASN B ND2 
3899 N N   . ARG B 224 ? 0.7863 0.8611 1.4104 -0.0376 -0.0288 0.0131  203 ARG B N   
3900 C CA  . ARG B 224 ? 0.6586 0.7478 1.2492 -0.0343 -0.0273 0.0387  203 ARG B CA  
3901 C C   . ARG B 224 ? 0.6048 0.6902 1.1643 -0.0456 -0.0296 0.0710  203 ARG B C   
3902 O O   . ARG B 224 ? 0.5137 0.6202 1.0360 -0.0482 -0.0219 0.0838  203 ARG B O   
3903 C CB  . ARG B 224 ? 0.5760 0.6502 1.1907 -0.0205 -0.0385 0.0504  203 ARG B CB  
3904 N N   . ASN B 225 ? 0.6292 0.6880 1.2049 -0.0528 -0.0389 0.0835  204 ASN B N   
3905 C CA  . ASN B 225 ? 0.5888 0.6417 1.1394 -0.0641 -0.0397 0.1146  204 ASN B CA  
3906 C C   . ASN B 225 ? 0.6006 0.6805 1.1237 -0.0753 -0.0279 0.1100  204 ASN B C   
3907 O O   . ASN B 225 ? 0.5624 0.6449 1.0633 -0.0839 -0.0250 0.1343  204 ASN B O   
3908 C CB  . ASN B 225 ? 0.6168 0.6346 1.1944 -0.0707 -0.0513 0.1262  204 ASN B CB  
3909 C CG  . ASN B 225 ? 0.7053 0.6935 1.3154 -0.0595 -0.0662 0.1303  204 ASN B CG  
3910 O OD1 . ASN B 225 ? 0.6754 0.6479 1.3256 -0.0556 -0.0723 0.1096  204 ASN B OD1 
3911 N ND2 . ASN B 225 ? 0.6373 0.6173 1.2314 -0.0545 -0.0728 0.1565  204 ASN B ND2 
3912 N N   . ASN B 226 ? 0.5455 0.6450 1.0699 -0.0760 -0.0214 0.0797  205 ASN B N   
3913 C CA  . ASN B 226 ? 0.6143 0.7394 1.1135 -0.0866 -0.0134 0.0748  205 ASN B CA  
3914 C C   . ASN B 226 ? 0.6016 0.7544 1.0646 -0.0831 -0.0042 0.0832  205 ASN B C   
3915 O O   . ASN B 226 ? 0.6037 0.7775 1.0456 -0.0913 0.0009  0.0838  205 ASN B O   
3916 C CB  . ASN B 226 ? 0.7146 0.8473 1.2241 -0.0904 -0.0113 0.0390  205 ASN B CB  
3917 C CG  . ASN B 226 ? 0.7316 0.8481 1.2627 -0.1024 -0.0181 0.0337  205 ASN B CG  
3918 O OD1 . ASN B 226 ? 0.7380 0.8449 1.2712 -0.1102 -0.0221 0.0574  205 ASN B OD1 
3919 N ND2 . ASN B 226 ? 0.6349 0.7486 1.1818 -0.1049 -0.0183 0.0012  205 ASN B ND2 
3920 N N   . VAL B 227 ? 0.5458 0.6992 1.0032 -0.0715 -0.0032 0.0898  206 VAL B N   
3921 C CA  . VAL B 227 ? 0.6336 0.8127 1.0594 -0.0677 0.0059  0.0938  206 VAL B CA  
3922 C C   . VAL B 227 ? 0.5245 0.6953 0.9390 -0.0615 0.0038  0.1211  206 VAL B C   
3923 O O   . VAL B 227 ? 0.5335 0.6787 0.9653 -0.0583 -0.0058 0.1337  206 VAL B O   
3924 C CB  . VAL B 227 ? 0.6204 0.8151 1.0476 -0.0603 0.0120  0.0650  206 VAL B CB  
3925 C CG1 . VAL B 227 ? 0.6724 0.8689 1.1115 -0.0671 0.0134  0.0352  206 VAL B CG1 
3926 C CG2 . VAL B 227 ? 0.4642 0.6450 0.9156 -0.0471 0.0073  0.0626  206 VAL B CG2 
3927 N N   . ILE B 228 ? 0.5213 0.7132 0.9052 -0.0606 0.0120  0.1303  207 ILE B N   
3928 C CA  . ILE B 228 ? 0.4802 0.6680 0.8473 -0.0553 0.0117  0.1529  207 ILE B CA  
3929 C C   . ILE B 228 ? 0.5125 0.7218 0.8666 -0.0468 0.0182  0.1412  207 ILE B C   
3930 O O   . ILE B 228 ? 0.4788 0.7119 0.8131 -0.0499 0.0276  0.1338  207 ILE B O   
3931 C CB  . ILE B 228 ? 0.4589 0.6494 0.8011 -0.0642 0.0173  0.1780  207 ILE B CB  
3932 C CG1 . ILE B 228 ? 0.4264 0.5931 0.7827 -0.0734 0.0117  0.1918  207 ILE B CG1 
3933 C CG2 . ILE B 228 ? 0.3891 0.5788 0.7074 -0.0595 0.0193  0.1971  207 ILE B CG2 
3934 C CD1 . ILE B 228 ? 0.4775 0.6532 0.8199 -0.0849 0.0204  0.2063  207 ILE B CD1 
3935 N N   . GLY B 229 ? 0.4564 0.6571 0.8231 -0.0365 0.0122  0.1402  208 GLY B N   
3936 C CA  . GLY B 229 ? 0.4290 0.6495 0.7876 -0.0288 0.0186  0.1289  208 GLY B CA  
3937 C C   . GLY B 229 ? 0.3792 0.6097 0.7043 -0.0292 0.0235  0.1495  208 GLY B C   
3938 O O   . GLY B 229 ? 0.3355 0.5520 0.6469 -0.0330 0.0198  0.1737  208 GLY B O   
3939 N N   . LEU B 230 ? 0.3325 0.5864 0.6434 -0.0262 0.0329  0.1388  209 LEU B N   
3940 C CA  . LEU B 230 ? 0.4050 0.6685 0.6858 -0.0261 0.0382  0.1558  209 LEU B CA  
3941 C C   . LEU B 230 ? 0.3560 0.6042 0.6392 -0.0196 0.0286  0.1705  209 LEU B C   
3942 O O   . LEU B 230 ? 0.3353 0.5819 0.5925 -0.0218 0.0302  0.1898  209 LEU B O   
3943 C CB  . LEU B 230 ? 0.3546 0.6446 0.6215 -0.0246 0.0496  0.1409  209 LEU B CB  
3944 C CG  . LEU B 230 ? 0.3590 0.6664 0.6113 -0.0326 0.0583  0.1317  209 LEU B CG  
3945 C CD1 . LEU B 230 ? 0.4319 0.7612 0.6604 -0.0321 0.0684  0.1289  209 LEU B CD1 
3946 C CD2 . LEU B 230 ? 0.3898 0.6920 0.6326 -0.0410 0.0573  0.1489  209 LEU B CD2 
3947 N N   . LEU B 231 ? 0.3917 0.6281 0.7064 -0.0119 0.0180  0.1611  210 LEU B N   
3948 C CA  . LEU B 231 ? 0.4572 0.6771 0.7784 -0.0058 0.0044  0.1754  210 LEU B CA  
3949 C C   . LEU B 231 ? 0.4983 0.6865 0.8297 -0.0087 -0.0103 0.1927  210 LEU B C   
3950 O O   . LEU B 231 ? 0.5387 0.7088 0.8920 -0.0023 -0.0264 0.1976  210 LEU B O   
3951 C CB  . LEU B 231 ? 0.3656 0.5931 0.7201 0.0053  0.0003  0.1554  210 LEU B CB  
3952 C CG  . LEU B 231 ? 0.4428 0.7005 0.7891 0.0075  0.0154  0.1376  210 LEU B CG  
3953 C CD1 . LEU B 231 ? 0.3688 0.6319 0.7497 0.0182  0.0104  0.1225  210 LEU B CD1 
3954 C CD2 . LEU B 231 ? 0.4174 0.6854 0.7214 0.0028  0.0227  0.1545  210 LEU B CD2 
3955 N N   . GLU B 232 ? 0.4825 0.6635 0.7995 -0.0188 -0.0056 0.2028  211 GLU B N   
3956 C CA  . GLU B 232 ? 0.4995 0.6504 0.8256 -0.0240 -0.0171 0.2184  211 GLU B CA  
3957 C C   . GLU B 232 ? 0.4739 0.6089 0.7651 -0.0309 -0.0198 0.2482  211 GLU B C   
3958 O O   . GLU B 232 ? 0.4767 0.6249 0.7360 -0.0373 -0.0063 0.2560  211 GLU B O   
3959 C CB  . GLU B 232 ? 0.4776 0.6303 0.8102 -0.0325 -0.0095 0.2113  211 GLU B CB  
3960 C CG  . GLU B 232 ? 0.5331 0.6551 0.8854 -0.0373 -0.0212 0.2212  211 GLU B CG  
3961 C CD  . GLU B 232 ? 0.6108 0.7307 1.0030 -0.0339 -0.0246 0.1964  211 GLU B CD  
3962 O OE1 . GLU B 232 ? 0.4760 0.6165 0.8810 -0.0269 -0.0187 0.1709  211 GLU B OE1 
3963 O OE2 . GLU B 232 ? 0.7212 0.8179 1.1312 -0.0391 -0.0322 0.2018  211 GLU B OE2 
3964 N N   . ASP B 233 ? 0.6097 0.7154 0.9069 -0.0303 -0.0374 0.2647  212 ASP B N   
3965 C CA  . ASP B 233 ? 0.6018 0.6888 0.8613 -0.0385 -0.0410 0.2929  212 ASP B CA  
3966 C C   . ASP B 233 ? 0.6484 0.7255 0.8886 -0.0529 -0.0303 0.3070  212 ASP B C   
3967 O O   . ASP B 233 ? 0.7360 0.8117 0.9993 -0.0559 -0.0277 0.2986  212 ASP B O   
3968 C CB  . ASP B 233 ? 0.6285 0.6845 0.8987 -0.0349 -0.0656 0.3076  212 ASP B CB  
3969 C CG  . ASP B 233 ? 0.8013 0.8249 1.0834 -0.0423 -0.0760 0.3214  212 ASP B CG  
3970 O OD1 . ASP B 233 ? 0.8983 0.8918 1.1595 -0.0490 -0.0898 0.3471  212 ASP B OD1 
3971 O OD2 . ASP B 233 ? 0.8398 0.8667 1.1500 -0.0426 -0.0709 0.3071  212 ASP B OD2 
3972 N N   . PRO B 234 ? 0.7075 0.8317 0.6811 -0.0455 0.0444  0.1562  213 PRO B N   
3973 C CA  . PRO B 234 ? 0.7076 0.8521 0.7106 -0.0464 0.0585  0.1635  213 PRO B CA  
3974 C C   . PRO B 234 ? 0.7638 0.9145 0.7782 -0.0567 0.0597  0.1772  213 PRO B C   
3975 O O   . PRO B 234 ? 0.7129 0.8800 0.7618 -0.0596 0.0631  0.1832  213 PRO B O   
3976 C CB  . PRO B 234 ? 0.7037 0.8509 0.6882 -0.0411 0.0790  0.1585  213 PRO B CB  
3977 C CG  . PRO B 234 ? 0.6927 0.8243 0.6497 -0.0346 0.0740  0.1452  213 PRO B CG  
3978 C CD  . PRO B 234 ? 0.6811 0.7972 0.6235 -0.0392 0.0535  0.1460  213 PRO B CD  
3979 N N   . LYS B 235 ? 0.7851 0.9239 0.7729 -0.0622 0.0574  0.1827  214 LYS B N   
3980 C CA  . LYS B 235 ? 0.7512 0.8943 0.7498 -0.0716 0.0603  0.1967  214 LYS B CA  
3981 C C   . LYS B 235 ? 0.8162 0.9607 0.8450 -0.0780 0.0455  0.1997  214 LYS B C   
3982 O O   . LYS B 235 ? 0.7837 0.9403 0.8402 -0.0847 0.0505  0.2083  214 LYS B O   
3983 C CB  . LYS B 235 ? 0.6850 0.8141 0.6483 -0.0751 0.0596  0.2029  214 LYS B CB  
3984 N N   . SER B 236 ? 0.8100 0.9421 0.8337 -0.0768 0.0278  0.1921  215 SER B N   
3985 C CA  . SER B 236 ? 0.8064 0.9386 0.8554 -0.0839 0.0135  0.1934  215 SER B CA  
3986 C C   . SER B 236 ? 0.7173 0.8691 0.8023 -0.0826 0.0131  0.1907  215 SER B C   
3987 O O   . SER B 236 ? 0.6907 0.8516 0.8042 -0.0909 0.0078  0.1949  215 SER B O   
3988 C CB  . SER B 236 ? 0.8500 0.9628 0.8814 -0.0830 -0.0042 0.1854  215 SER B CB  
3989 O OG  . SER B 236 ? 0.7528 0.8650 0.8068 -0.0908 -0.0175 0.1855  215 SER B OG  
3990 N N   . VAL B 237 ? 0.7411 0.9002 0.8265 -0.0724 0.0186  0.1837  216 VAL B N   
3991 C CA  . VAL B 237 ? 0.7424 0.9228 0.8638 -0.0698 0.0199  0.1832  216 VAL B CA  
3992 C C   . VAL B 237 ? 0.6833 0.8828 0.8298 -0.0750 0.0349  0.1928  216 VAL B C   
3993 O O   . VAL B 237 ? 0.6681 0.8849 0.8499 -0.0802 0.0313  0.1963  216 VAL B O   
3994 C CB  . VAL B 237 ? 0.7036 0.8859 0.8199 -0.0567 0.0251  0.1746  216 VAL B CB  
3995 C CG1 . VAL B 237 ? 0.5132 0.7203 0.6686 -0.0529 0.0306  0.1768  216 VAL B CG1 
3996 C CG2 . VAL B 237 ? 0.5641 0.7298 0.6635 -0.0522 0.0089  0.1652  216 VAL B CG2 
3997 N N   . VAL B 238 ? 0.6713 0.8683 0.7996 -0.0741 0.0520  0.1970  217 VAL B N   
3998 C CA  . VAL B 238 ? 0.7067 0.9198 0.8563 -0.0793 0.0681  0.2065  217 VAL B CA  
3999 C C   . VAL B 238 ? 0.6881 0.9017 0.8542 -0.0921 0.0614  0.2148  217 VAL B C   
4000 O O   . VAL B 238 ? 0.6362 0.8680 0.8366 -0.0980 0.0671  0.2204  217 VAL B O   
4001 C CB  . VAL B 238 ? 0.6517 0.8591 0.7719 -0.0768 0.0871  0.2093  217 VAL B CB  
4002 C CG1 . VAL B 238 ? 0.6717 0.8863 0.8023 -0.0857 0.1004  0.2219  217 VAL B CG1 
4003 C CG2 . VAL B 238 ? 0.5702 0.7870 0.6925 -0.0665 0.1013  0.2025  217 VAL B CG2 
4004 N N   . LYS B 239 ? 0.7007 0.8944 0.8442 -0.0967 0.0500  0.2155  218 LYS B N   
4005 C CA  . LYS B 239 ? 0.7450 0.9359 0.9025 -0.1090 0.0456  0.2233  218 LYS B CA  
4006 C C   . LYS B 239 ? 0.7252 0.9264 0.9162 -0.1150 0.0311  0.2189  218 LYS B C   
4007 O O   . LYS B 239 ? 0.7520 0.9633 0.9712 -0.1254 0.0330  0.2244  218 LYS B O   
4008 C CB  . LYS B 239 ? 0.7539 0.9201 0.8784 -0.1112 0.0382  0.2254  218 LYS B CB  
4009 C CG  . LYS B 239 ? 0.7864 0.9466 0.9212 -0.1231 0.0388  0.2357  218 LYS B CG  
4010 C CD  . LYS B 239 ? 0.7884 0.9244 0.8916 -0.1237 0.0316  0.2386  218 LYS B CD  
4011 C CE  . LYS B 239 ? 0.6760 0.8056 0.7425 -0.1164 0.0420  0.2431  218 LYS B CE  
4012 N NZ  . LYS B 239 ? 0.7307 0.8522 0.7876 -0.1221 0.0505  0.2582  218 LYS B NZ  
4013 N N   . LYS B 240 ? 0.6334 0.8325 0.8213 -0.1091 0.0168  0.2090  219 LYS B N   
4014 C CA  . LYS B 240 ? 0.7832 0.9929 0.9996 -0.1148 0.0018  0.2046  219 LYS B CA  
4015 C C   . LYS B 240 ? 0.7129 0.9521 0.9670 -0.1135 0.0073  0.2059  219 LYS B C   
4016 O O   . LYS B 240 ? 0.6611 0.9155 0.9465 -0.1228 0.0001  0.2064  219 LYS B O   
4017 C CB  . LYS B 240 ? 0.7579 0.9550 0.9568 -0.1087 -0.0149 0.1945  219 LYS B CB  
4018 C CG  . LYS B 240 ? 0.7609 0.9307 0.9299 -0.1122 -0.0234 0.1926  219 LYS B CG  
4019 C CD  . LYS B 240 ? 0.6410 0.7986 0.7951 -0.1070 -0.0394 0.1822  219 LYS B CD  
4020 C CE  . LYS B 240 ? 0.8084 0.9404 0.9397 -0.1124 -0.0486 0.1803  219 LYS B CE  
4021 N NZ  . LYS B 240 ? 0.6969 0.8224 0.8306 -0.1151 -0.0661 0.1714  219 LYS B NZ  
4022 N N   . ILE B 241 ? 0.6993 0.9474 0.9521 -0.1025 0.0200  0.2060  220 ILE B N   
4023 C CA  . ILE B 241 ? 0.5808 0.8577 0.8717 -0.1002 0.0270  0.2082  220 ILE B CA  
4024 C C   . ILE B 241 ? 0.6040 0.8936 0.9179 -0.1100 0.0411  0.2171  220 ILE B C   
4025 O O   . ILE B 241 ? 0.6078 0.9205 0.9606 -0.1162 0.0395  0.2192  220 ILE B O   
4026 C CB  . ILE B 241 ? 0.6033 0.8837 0.8863 -0.0854 0.0386  0.2053  220 ILE B CB  
4027 C CG1 . ILE B 241 ? 0.5892 0.8583 0.8545 -0.0760 0.0246  0.1964  220 ILE B CG1 
4028 C CG2 . ILE B 241 ? 0.5140 0.8242 0.8386 -0.0827 0.0486  0.2090  220 ILE B CG2 
4029 C CD1 . ILE B 241 ? 0.5322 0.8154 0.8240 -0.0774 0.0061  0.1942  220 ILE B CD1 
4030 N N   . LYS B 242 ? 0.6370 0.9124 0.9273 -0.1117 0.0553  0.2227  221 LYS B N   
4031 C CA  . LYS B 242 ? 0.6656 0.9502 0.9753 -0.1212 0.0699  0.2320  221 LYS B CA  
4032 C C   . LYS B 242 ? 0.6766 0.9634 1.0090 -0.1356 0.0588  0.2336  221 LYS B C   
4033 O O   . LYS B 242 ? 0.6339 0.9387 1.0005 -0.1441 0.0663  0.2383  221 LYS B O   
4034 C CB  . LYS B 242 ? 0.7459 1.0119 1.0207 -0.1206 0.0847  0.2386  221 LYS B CB  
4035 N N   . ARG B 243 ? 0.7035 0.9722 1.0182 -0.1390 0.0418  0.2289  222 ARG B N   
4036 C CA  . ARG B 243 ? 0.7042 0.9713 1.0368 -0.1534 0.0318  0.2288  222 ARG B CA  
4037 C C   . ARG B 243 ? 0.6946 0.9807 1.0567 -0.1573 0.0152  0.2210  222 ARG B C   
4038 O O   . ARG B 243 ? 0.7123 0.9982 1.0895 -0.1703 0.0058  0.2186  222 ARG B O   
4039 C CB  . ARG B 243 ? 0.7728 1.0098 1.0722 -0.1558 0.0230  0.2278  222 ARG B CB  
4040 N N   . ALA B 244 ? 0.7651 1.0678 1.1361 -0.1468 0.0117  0.2171  223 ALA B N   
4041 C CA  . ALA B 244 ? 0.7941 1.1160 1.1906 -0.1495 -0.0056 0.2109  223 ALA B CA  
4042 C C   . ALA B 244 ? 0.6534 1.0014 1.0940 -0.1627 -0.0034 0.2135  223 ALA B C   
4043 O O   . ALA B 244 ? 0.7693 1.1306 1.2293 -0.1636 0.0136  0.2201  223 ALA B O   
4044 C CB  . ALA B 244 ? 0.6393 0.9747 1.0388 -0.1341 -0.0070 0.2087  223 ALA B CB  
4045 N N   . VAL B 245 ? 0.6697 1.0255 1.1263 -0.1737 -0.0205 0.2075  224 VAL B N   
4046 C CA  . VAL B 245 ? 0.8160 1.1977 1.3150 -0.1879 -0.0198 0.2083  224 VAL B CA  
4047 C C   . VAL B 245 ? 0.8497 1.2655 1.3825 -0.1805 -0.0144 0.2118  224 VAL B C   
4048 O O   . VAL B 245 ? 0.8158 1.2389 1.3441 -0.1664 -0.0194 0.2111  224 VAL B O   
4049 C CB  . VAL B 245 ? 0.6955 1.0815 1.2039 -0.2010 -0.0405 0.1994  224 VAL B CB  
4050 N N   . THR B 246 ? 0.8030 1.2395 1.3715 -0.1900 -0.0028 0.2161  225 THR B N   
4051 C CA  . THR B 246 ? 0.8206 1.2917 1.4274 -0.1848 0.0033  0.2198  225 THR B CA  
4052 C C   . THR B 246 ? 0.7731 1.2688 1.4227 -0.2017 0.0043  0.2191  225 THR B C   
4053 O O   . THR B 246 ? 0.7852 1.2625 1.4253 -0.2142 0.0050  0.2139  225 THR B O   
4054 C CB  . THR B 246 ? 0.8419 1.3084 1.4409 -0.1723 0.0267  0.2273  225 THR B CB  
4055 O OG1 . THR B 246 ? 0.8542 1.3526 1.4875 -0.1637 0.0304  0.2299  225 THR B OG1 
4056 C CG2 . THR B 246 ? 0.8076 1.2664 1.4115 -0.1825 0.0468  0.2332  225 THR B CG2 
4057 N N   . ASP B 247 ? 0.7431 1.2696 1.4263 -0.1974 0.0050  0.2187  226 ASP B N   
4058 C CA  . ASP B 247 ? 0.8292 1.3722 1.5405 -0.2082 0.0047  0.2111  226 ASP B CA  
4059 C C   . ASP B 247 ? 0.9491 1.4988 1.6810 -0.2090 0.0298  0.2180  226 ASP B C   
4060 O O   . ASP B 247 ? 0.8412 1.4021 1.5831 -0.1971 0.0429  0.2267  226 ASP B O   
4061 C CB  . ASP B 247 ? 0.8606 1.4342 1.5956 -0.2035 -0.0121 0.2058  226 ASP B CB  
4062 N N   . SER B 248 ? 0.7632 1.3054 1.5012 -0.2229 0.0375  0.2132  227 SER B N   
4063 C CA  . SER B 248 ? 0.8251 1.3690 1.5785 -0.2252 0.0622  0.2192  227 SER B CA  
4064 C C   . SER B 248 ? 0.7648 1.3425 1.5602 -0.2268 0.0640  0.2151  227 SER B C   
4065 O O   . SER B 248 ? 0.7379 1.3205 1.5510 -0.2391 0.0696  0.2091  227 SER B O   
4066 C CB  . SER B 248 ? 0.8047 1.3215 1.5425 -0.2384 0.0712  0.2171  227 SER B CB  
4067 O OG  . SER B 248 ? 0.7809 1.3010 1.5280 -0.2519 0.0578  0.2036  227 SER B OG  
4068 N N   . ASP B 249 ? 0.8984 1.4996 1.7102 -0.2139 0.0595  0.2184  228 ASP B N   
4069 C CA  . ASP B 249 ? 0.9534 1.5874 1.8057 -0.2126 0.0628  0.2167  228 ASP B CA  
4070 C C   . ASP B 249 ? 0.8705 1.5046 1.7349 -0.2093 0.0911  0.2247  228 ASP B C   
4071 O O   . ASP B 249 ? 0.8662 1.4835 1.7099 -0.2004 0.1059  0.2337  228 ASP B O   
4072 C CB  . ASP B 249 ? 0.6689 1.3263 1.5338 -0.1985 0.0483  0.2181  228 ASP B CB  
4073 N N   . GLU B 250 ? 0.8710 1.5241 1.7675 -0.2169 0.0989  0.2209  229 GLU B N   
4074 C CA  . GLU B 250 ? 0.9011 1.5546 1.8104 -0.2154 0.1260  0.2272  229 GLU B CA  
4075 C C   . GLU B 250 ? 0.8805 1.5677 1.8289 -0.2069 0.1290  0.2278  229 GLU B C   
4076 O O   . GLU B 250 ? 0.8906 1.6032 1.8687 -0.2139 0.1176  0.2203  229 GLU B O   
4077 C CB  . GLU B 250 ? 0.8327 1.4768 1.7460 -0.2323 0.1363  0.2227  229 GLU B CB  
4078 C CG  . GLU B 250 ? 0.8623 1.4691 1.7370 -0.2388 0.1411  0.2250  229 GLU B CG  
4079 C CD  . GLU B 250 ? 0.9032 1.4883 1.7537 -0.2301 0.1642  0.2370  229 GLU B CD  
4080 O OE1 . GLU B 250 ? 0.9089 1.4938 1.7470 -0.2162 0.1648  0.2431  229 GLU B OE1 
4081 O OE2 . GLU B 250 ? 0.7526 1.3210 1.5952 -0.2373 0.1822  0.2402  229 GLU B OE2 
4082 N N   . PRO B 251 ? 0.9126 1.6016 1.8624 -0.1920 0.1444  0.2360  230 PRO B N   
4083 C CA  . PRO B 251 ? 1.1566 1.8198 2.0720 -0.1823 0.1587  0.2443  230 PRO B CA  
4084 C C   . PRO B 251 ? 1.1293 1.7852 2.0212 -0.1737 0.1396  0.2450  230 PRO B C   
4085 O O   . PRO B 251 ? 0.7081 1.3841 1.6163 -0.1693 0.1195  0.2415  230 PRO B O   
4086 C CB  . PRO B 251 ? 0.8608 1.5365 1.7956 -0.1702 0.1804  0.2493  230 PRO B CB  
4087 C CG  . PRO B 251 ? 0.6139 1.3246 1.5908 -0.1670 0.1670  0.2451  230 PRO B CG  
4088 C CD  . PRO B 251 ? 0.6719 1.3912 1.6608 -0.1839 0.1502  0.2368  230 PRO B CD  
4089 N N   . PRO B 252 ? 0.9622 1.5900 1.8150 -0.1711 0.1450  0.2498  231 PRO B N   
4090 C CA  . PRO B 252 ? 0.9161 1.5373 1.7468 -0.1628 0.1276  0.2504  231 PRO B CA  
4091 C C   . PRO B 252 ? 0.9576 1.5956 1.8025 -0.1450 0.1307  0.2537  231 PRO B C   
4092 O O   . PRO B 252 ? 0.9901 1.6245 1.8328 -0.1361 0.1539  0.2586  231 PRO B O   
4093 C CB  . PRO B 252 ? 0.9197 1.5076 1.7070 -0.1643 0.1382  0.2556  231 PRO B CB  
4094 C CG  . PRO B 252 ? 1.0181 1.5937 1.8036 -0.1770 0.1534  0.2562  231 PRO B CG  
4095 C CD  . PRO B 252 ? 0.9885 1.5886 1.8135 -0.1769 0.1652  0.2546  231 PRO B CD  
4096 N N   . VAL B 253 ? 0.7887 1.4437 1.6463 -0.1397 0.1078  0.2505  232 VAL B N   
4097 C CA  . VAL B 253 ? 0.7477 1.4181 1.6196 -0.1220 0.1080  0.2536  232 VAL B CA  
4098 C C   . VAL B 253 ? 0.6773 1.3409 1.5274 -0.1156 0.0863  0.2530  232 VAL B C   
4099 O O   . VAL B 253 ? 0.7319 1.3866 1.5648 -0.1258 0.0665  0.2485  232 VAL B O   
4100 C CB  . VAL B 253 ? 0.6839 1.3867 1.5999 -0.1196 0.1025  0.2516  232 VAL B CB  
4101 N N   . VAL B 254 ? 0.8316 1.4983 1.6821 -0.0984 0.0911  0.2569  233 VAL B N   
4102 C CA  . VAL B 254 ? 0.6788 1.3320 1.5007 -0.0891 0.0733  0.2546  233 VAL B CA  
4103 C C   . VAL B 254 ? 0.8289 1.5114 1.6827 -0.0826 0.0532  0.2556  233 VAL B C   
4104 O O   . VAL B 254 ? 0.6265 1.3259 1.5072 -0.0700 0.0618  0.2589  233 VAL B O   
4105 C CB  . VAL B 254 ? 0.7715 1.3975 1.5587 -0.0728 0.0903  0.2534  233 VAL B CB  
4106 C CG1 . VAL B 254 ? 0.8040 1.4062 1.5504 -0.0656 0.0723  0.2484  233 VAL B CG1 
4107 C CG2 . VAL B 254 ? 0.6993 1.2990 1.4566 -0.0783 0.1134  0.2523  233 VAL B CG2 
4108 N N   . ARG B 255 ? 0.6544 1.3368 1.4972 -0.0907 0.0265  0.2507  234 ARG B N   
4109 C CA  . ARG B 255 ? 0.6978 1.4008 1.5575 -0.0855 0.0050  0.2493  234 ARG B CA  
4110 C C   . ARG B 255 ? 0.7139 1.4037 1.5427 -0.0903 -0.0206 0.2442  234 ARG B C   
4111 O O   . ARG B 255 ? 0.6879 1.3604 1.4940 -0.1050 -0.0260 0.2387  234 ARG B O   
4112 C CB  . ARG B 255 ? 0.6287 1.3562 1.5210 -0.0958 0.0015  0.2458  234 ARG B CB  
4113 N N   . TYR B 256 ? 0.7130 1.4089 1.5399 -0.0777 -0.0354 0.2460  235 TYR B N   
4114 C CA  . TYR B 256 ? 0.7879 1.4702 1.5836 -0.0807 -0.0592 0.2409  235 TYR B CA  
4115 C C   . TYR B 256 ? 0.8128 1.5085 1.6144 -0.0946 -0.0787 0.2330  235 TYR B C   
4116 O O   . TYR B 256 ? 0.7909 1.5130 1.6214 -0.0917 -0.0832 0.2344  235 TYR B O   
4117 C CB  . TYR B 256 ? 0.8253 1.5074 1.6153 -0.0615 -0.0659 0.2460  235 TYR B CB  
4118 N N   . ASP B 257 ? 0.7976 1.4749 1.5719 -0.1099 -0.0894 0.2243  236 ASP B N   
4119 C CA  . ASP B 257 ? 0.7725 1.4594 1.5484 -0.1244 -0.1062 0.2144  236 ASP B CA  
4120 C C   . ASP B 257 ? 0.8435 1.5020 1.5799 -0.1364 -0.1180 0.2048  236 ASP B C   
4121 O O   . ASP B 257 ? 0.9020 1.5449 1.6298 -0.1499 -0.1104 0.2001  236 ASP B O   
4122 C CB  . ASP B 257 ? 0.8292 1.5327 1.6357 -0.1368 -0.0947 0.2117  236 ASP B CB  
4123 C CG  . ASP B 257 ? 0.8733 1.5913 1.6864 -0.1513 -0.1106 0.2005  236 ASP B CG  
4124 O OD1 . ASP B 257 ? 0.8683 1.5800 1.6582 -0.1531 -0.1298 0.1943  236 ASP B OD1 
4125 O OD2 . ASP B 257 ? 0.7983 1.5338 1.6396 -0.1609 -0.1029 0.1974  236 ASP B OD2 
4126 N N   . ALA B 262 ? 0.7263 1.2982 1.3987 -0.1725 -0.0864 0.1968  241 ALA B N   
4127 C CA  . ALA B 262 ? 0.7419 1.2934 1.3805 -0.1657 -0.0988 0.1958  241 ALA B CA  
4128 C C   . ALA B 262 ? 0.6503 1.1812 1.2714 -0.1611 -0.0852 0.2036  241 ALA B C   
4129 O O   . ALA B 262 ? 0.7483 1.2602 1.3396 -0.1486 -0.0893 0.2031  241 ALA B O   
4130 C CB  . ALA B 262 ? 0.7956 1.3278 1.4081 -0.1783 -0.1144 0.1827  241 ALA B CB  
4131 N N   . GLY B 263 ? 0.7394 1.2624 1.3648 -0.1678 -0.0664 0.2065  242 GLY B N   
4132 C CA  . GLY B 263 ? 0.7007 1.1905 1.2905 -0.1586 -0.0496 0.2085  242 GLY B CA  
4133 C C   . GLY B 263 ? 0.6507 1.1493 1.2463 -0.1400 -0.0365 0.2144  242 GLY B C   
4134 O O   . GLY B 263 ? 0.6274 1.1087 1.1948 -0.1259 -0.0378 0.2132  242 GLY B O   
4135 N N   . VAL B 264 ? 0.7619 1.2889 1.3971 -0.1400 -0.0241 0.2202  243 VAL B N   
4136 C CA  . VAL B 264 ? 0.6083 1.1442 1.2529 -0.1230 -0.0088 0.2257  243 VAL B CA  
4137 C C   . VAL B 264 ? 0.6790 1.2222 1.3222 -0.1085 -0.0226 0.2253  243 VAL B C   
4138 O O   . VAL B 264 ? 0.6911 1.2230 1.3189 -0.0925 -0.0125 0.2266  243 VAL B O   
4139 C CB  . VAL B 264 ? 0.5968 1.1668 1.2914 -0.1268 0.0042  0.2317  243 VAL B CB  
4140 C CG1 . VAL B 264 ? 0.8214 1.4037 1.5312 -0.1089 0.0191  0.2370  243 VAL B CG1 
4141 C CG2 . VAL B 264 ? 0.7419 1.3008 1.4347 -0.1393 0.0217  0.2331  243 VAL B CG2 
4142 N N   . SER B 265 ? 0.6483 1.2104 1.3072 -0.1143 -0.0455 0.2235  244 SER B N   
4143 C CA  . SER B 265 ? 0.6234 1.1940 1.2822 -0.1009 -0.0599 0.2247  244 SER B CA  
4144 C C   . SER B 265 ? 0.5875 1.1198 1.1960 -0.0917 -0.0623 0.2196  244 SER B C   
4145 O O   . SER B 265 ? 0.5809 1.1098 1.1829 -0.0748 -0.0599 0.2216  244 SER B O   
4146 C CB  . SER B 265 ? 0.7266 1.3220 1.4052 -0.1112 -0.0848 0.2228  244 SER B CB  
4147 O OG  . SER B 265 ? 0.7228 1.3365 1.4285 -0.1220 -0.0813 0.2202  244 SER B OG  
4148 N N   . ASN B 266 ? 0.6586 1.1619 1.2328 -0.1025 -0.0665 0.2129  245 ASN B N   
4149 C CA  . ASN B 266 ? 0.6992 1.1666 1.2265 -0.0949 -0.0694 0.2075  245 ASN B CA  
4150 C C   . ASN B 266 ? 0.5901 1.0414 1.1007 -0.0798 -0.0483 0.2092  245 ASN B C   
4151 O O   . ASN B 266 ? 0.5694 1.0050 1.0573 -0.0666 -0.0494 0.2069  245 ASN B O   
4152 C CB  . ASN B 266 ? 0.7037 1.1436 1.2014 -0.1094 -0.0740 0.2012  245 ASN B CB  
4153 N N   . LEU B 267 ? 0.6454 1.1003 1.1667 -0.0822 -0.0281 0.2129  246 LEU B N   
4154 C CA  . LEU B 267 ? 0.5628 1.0011 1.0644 -0.0703 -0.0068 0.2133  246 LEU B CA  
4155 C C   . LEU B 267 ? 0.5229 0.9799 1.0485 -0.0541 0.0006  0.2170  246 LEU B C   
4156 O O   . LEU B 267 ? 0.5494 0.9898 1.0540 -0.0414 0.0127  0.2146  246 LEU B O   
4157 C CB  . LEU B 267 ? 0.5683 1.0053 1.0735 -0.0785 0.0130  0.2166  246 LEU B CB  
4158 C CG  . LEU B 267 ? 0.6049 1.0183 1.0826 -0.0922 0.0120  0.2147  246 LEU B CG  
4159 C CD1 . LEU B 267 ? 0.7332 1.1568 1.2284 -0.1074 -0.0057 0.2135  246 LEU B CD1 
4160 C CD2 . LEU B 267 ? 0.5704 0.9835 1.0519 -0.0971 0.0344  0.2199  246 LEU B CD2 
4161 N N   . LEU B 268 ? 0.6206 1.1126 1.1913 -0.0547 -0.0065 0.2226  247 LEU B N   
4162 C CA  . LEU B 268 ? 0.5769 1.0888 1.1750 -0.0387 -0.0016 0.2276  247 LEU B CA  
4163 C C   . LEU B 268 ? 0.5856 1.0866 1.1652 -0.0277 -0.0167 0.2253  247 LEU B C   
4164 O O   . LEU B 268 ? 0.5044 1.0014 1.0835 -0.0116 -0.0066 0.2264  247 LEU B O   
4165 C CB  . LEU B 268 ? 0.7769 1.3315 1.4299 -0.0430 -0.0069 0.2351  247 LEU B CB  
4166 C CG  . LEU B 268 ? 0.7603 1.3296 1.4400 -0.0503 0.0128  0.2386  247 LEU B CG  
4167 C CD1 . LEU B 268 ? 0.7506 1.3632 1.4851 -0.0566 0.0040  0.2449  247 LEU B CD1 
4168 C CD2 . LEU B 268 ? 0.6770 1.2394 1.3564 -0.0366 0.0397  0.2402  247 LEU B CD2 
4169 N N   . ASP B 269 ? 0.7394 1.2350 1.3041 -0.0364 -0.0397 0.2219  248 ASP B N   
4170 C CA  . ASP B 269 ? 0.7181 1.2005 1.2617 -0.0269 -0.0538 0.2195  248 ASP B CA  
4171 C C   . ASP B 269 ? 0.6846 1.1280 1.1828 -0.0190 -0.0426 0.2122  248 ASP B C   
4172 O O   . ASP B 269 ? 0.6913 1.1258 1.1812 -0.0041 -0.0398 0.2118  248 ASP B O   
4173 C CB  . ASP B 269 ? 0.7467 1.2296 1.2811 -0.0399 -0.0794 0.2162  248 ASP B CB  
4174 C CG  . ASP B 269 ? 0.8023 1.3234 1.3785 -0.0517 -0.0909 0.2212  248 ASP B CG  
4175 O OD1 . ASP B 269 ? 0.7894 1.3392 1.4053 -0.0475 -0.0810 0.2285  248 ASP B OD1 
4176 O OD2 . ASP B 269 ? 0.8412 1.3637 1.4112 -0.0656 -0.1095 0.2171  248 ASP B OD2 
4177 N N   . ILE B 270 ? 0.6090 1.0292 1.0784 -0.0289 -0.0358 0.2066  249 ILE B N   
4178 C CA  . ILE B 270 ? 0.6497 1.0342 1.0746 -0.0233 -0.0272 0.1992  249 ILE B CA  
4179 C C   . ILE B 270 ? 0.5889 0.9718 1.0164 -0.0099 -0.0032 0.1998  249 ILE B C   
4180 O O   . ILE B 270 ? 0.4978 0.8626 0.9043 0.0020  0.0017  0.1951  249 ILE B O   
4181 C CB  . ILE B 270 ? 0.5744 0.9381 0.9713 -0.0375 -0.0266 0.1950  249 ILE B CB  
4182 C CG1 . ILE B 270 ? 0.6342 0.9906 1.0199 -0.0488 -0.0498 0.1915  249 ILE B CG1 
4183 C CG2 . ILE B 270 ? 0.5257 0.8585 0.8819 -0.0317 -0.0132 0.1890  249 ILE B CG2 
4184 C CD1 . ILE B 270 ? 0.6983 1.0525 1.0836 -0.0663 -0.0515 0.1916  249 ILE B CD1 
4185 N N   . LEU B 271 ? 0.6138 1.0150 1.0673 -0.0121 0.0130  0.2049  250 LEU B N   
4186 C CA  . LEU B 271 ? 0.5143 0.9142 0.9711 -0.0007 0.0379  0.2048  250 LEU B CA  
4187 C C   . LEU B 271 ? 0.5577 0.9704 1.0386 0.0155  0.0392  0.2077  250 LEU B C   
4188 O O   . LEU B 271 ? 0.4452 0.8424 0.9113 0.0274  0.0537  0.2031  250 LEU B O   
4189 C CB  . LEU B 271 ? 0.5984 1.0176 1.0821 -0.0072 0.0545  0.2104  250 LEU B CB  
4190 C CG  . LEU B 271 ? 0.5710 0.9899 1.0591 0.0024  0.0828  0.2099  250 LEU B CG  
4191 C CD1 . LEU B 271 ? 0.4078 0.7928 0.8462 0.0061  0.0935  0.2006  250 LEU B CD1 
4192 C CD2 . LEU B 271 ? 0.6006 1.0358 1.1111 -0.0066 0.0981  0.2152  250 LEU B CD2 
4193 N N   . SER B 272 ? 0.5184 0.9597 1.0372 0.0162  0.0245  0.2155  251 SER B N   
4194 C CA  . SER B 272 ? 0.5605 1.0161 1.1055 0.0323  0.0249  0.2207  251 SER B CA  
4195 C C   . SER B 272 ? 0.5821 1.0111 1.0939 0.0415  0.0173  0.2148  251 SER B C   
4196 O O   . SER B 272 ? 0.6161 1.0391 1.1310 0.0566  0.0301  0.2145  251 SER B O   
4197 C CB  . SER B 272 ? 0.5804 1.0731 1.1692 0.0297  0.0067  0.2307  251 SER B CB  
4198 O OG  . SER B 272 ? 0.6659 1.1545 1.2376 0.0198  -0.0193 0.2286  251 SER B OG  
4199 N N   . ALA B 273 ? 0.4521 0.8641 0.9329 0.0324  -0.0022 0.2097  252 ALA B N   
4200 C CA  . ALA B 273 ? 0.5564 0.9424 1.0054 0.0402  -0.0096 0.2037  252 ALA B CA  
4201 C C   . ALA B 273 ? 0.5621 0.9187 0.9796 0.0471  0.0113  0.1944  252 ALA B C   
4202 O O   . ALA B 273 ? 0.5410 0.8846 0.9505 0.0602  0.0168  0.1916  252 ALA B O   
4203 C CB  . ALA B 273 ? 0.4198 0.7918 0.8408 0.0273  -0.0322 0.1990  252 ALA B CB  
4204 N N   . VAL B 274 ? 0.5730 0.9191 0.9719 0.0381  0.0234  0.1896  253 VAL B N   
4205 C CA  . VAL B 274 ? 0.5197 0.8392 0.8854 0.0427  0.0421  0.1800  253 VAL B CA  
4206 C C   . VAL B 274 ? 0.5430 0.8708 0.9311 0.0564  0.0656  0.1811  253 VAL B C   
4207 O O   . VAL B 274 ? 0.5403 0.8497 0.9120 0.0669  0.0758  0.1741  253 VAL B O   
4208 C CB  . VAL B 274 ? 0.5485 0.8582 0.8905 0.0294  0.0489  0.1767  253 VAL B CB  
4209 C CG1 . VAL B 274 ? 0.4576 0.7437 0.7658 0.0337  0.0687  0.1670  253 VAL B CG1 
4210 C CG2 . VAL B 274 ? 0.5463 0.8444 0.8658 0.0166  0.0272  0.1751  253 VAL B CG2 
4211 N N   . THR B 275 ? 0.5634 0.9187 0.9907 0.0563  0.0754  0.1895  254 THR B N   
4212 C CA  . THR B 275 ? 0.5698 0.9329 1.0196 0.0678  0.1010  0.1902  254 THR B CA  
4213 C C   . THR B 275 ? 0.5803 0.9617 1.0696 0.0826  0.0991  0.1982  254 THR B C   
4214 O O   . THR B 275 ? 0.5493 0.9347 1.0586 0.0941  0.1210  0.1986  254 THR B O   
4215 C CB  . THR B 275 ? 0.5554 0.9385 1.0288 0.0604  0.1156  0.1951  254 THR B CB  
4216 O OG1 . THR B 275 ? 0.5188 0.9332 1.0330 0.0560  0.1004  0.2064  254 THR B OG1 
4217 C CG2 . THR B 275 ? 0.5096 0.8751 0.9445 0.0463  0.1185  0.1892  254 THR B CG2 
4218 N N   . GLY B 276 ? 0.4972 0.8897 0.9980 0.0826  0.0741  0.2050  255 GLY B N   
4219 C CA  . GLY B 276 ? 0.6170 1.0304 1.1572 0.0966  0.0704  0.2152  255 GLY B CA  
4220 C C   . GLY B 276 ? 0.5700 1.0188 1.1631 0.0996  0.0807  0.2261  255 GLY B C   
4221 O O   . GLY B 276 ? 0.6225 1.0864 1.2506 0.1143  0.0878  0.2340  255 GLY B O   
4222 N N   . GLN B 277 ? 0.5359 0.9985 1.1376 0.0862  0.0821  0.2272  256 GLN B N   
4223 C CA  . GLN B 277 ? 0.5084 1.0050 1.1608 0.0872  0.0925  0.2367  256 GLN B CA  
4224 C C   . GLN B 277 ? 0.5592 1.0884 1.2429 0.0795  0.0670  0.2469  256 GLN B C   
4225 O O   . GLN B 277 ? 0.5118 1.0350 1.1724 0.0681  0.0445  0.2444  256 GLN B O   
4226 C CB  . GLN B 277 ? 0.5144 1.0062 1.1584 0.0770  0.1130  0.2314  256 GLN B CB  
4227 C CG  . GLN B 277 ? 0.5724 1.0344 1.1841 0.0825  0.1390  0.2205  256 GLN B CG  
4228 C CD  . GLN B 277 ? 0.6382 1.0949 1.2359 0.0710  0.1572  0.2159  256 GLN B CD  
4229 O OE1 . GLN B 277 ? 0.6977 1.1592 1.2888 0.0566  0.1463  0.2175  256 GLN B OE1 
4230 N NE2 . GLN B 277 ? 0.7044 1.1510 1.2975 0.0772  0.1859  0.2101  256 GLN B NE2 
4231 N N   . SER B 278 ? 0.6805 1.2453 1.4182 0.0856  0.0712  0.2581  257 SER B N   
4232 C CA  . SER B 278 ? 0.7631 1.3638 1.5352 0.0774  0.0486  0.2675  257 SER B CA  
4233 C C   . SER B 278 ? 0.8921 1.4975 1.6604 0.0578  0.0482  0.2636  257 SER B C   
4234 O O   . SER B 278 ? 0.9291 1.5231 1.6892 0.0541  0.0708  0.2586  257 SER B O   
4235 C CB  . SER B 278 ? 0.6065 1.2455 1.4401 0.0896  0.0545  0.2809  257 SER B CB  
4236 O OG  . SER B 278 ? 0.5688 1.2140 1.4249 0.0904  0.0822  0.2803  257 SER B OG  
4237 N N   . ILE B 279 ? 0.7056 1.3276 1.4793 0.0448  0.0228  0.2658  258 ILE B N   
4238 C CA  . ILE B 279 ? 0.6870 1.3156 1.4623 0.0257  0.0220  0.2628  258 ILE B CA  
4239 C C   . ILE B 279 ? 0.6958 1.3517 1.5174 0.0258  0.0418  0.2686  258 ILE B C   
4240 O O   . ILE B 279 ? 0.7521 1.3957 1.5621 0.0174  0.0598  0.2638  258 ILE B O   
4241 C CB  . ILE B 279 ? 0.7127 1.3581 1.4921 0.0120  -0.0084 0.2639  258 ILE B CB  
4242 N N   . PRO B 280 ? 0.8549 1.5405 1.7204 0.0345  0.0398  0.2767  259 PRO B N   
4243 C CA  . PRO B 280 ? 0.8384 1.5404 1.7379 0.0340  0.0594  0.2785  259 PRO B CA  
4244 C C   . PRO B 280 ? 0.8147 1.5029 1.7134 0.0434  0.0932  0.2774  259 PRO B C   
4245 O O   . PRO B 280 ? 0.8335 1.5245 1.7420 0.0359  0.1122  0.2758  259 PRO B O   
4246 C CB  . PRO B 280 ? 0.8132 1.5368 1.7432 0.0438  0.0479  0.2842  259 PRO B CB  
4247 C CG  . PRO B 280 ? 0.8470 1.5697 1.7577 0.0419  0.0175  0.2844  259 PRO B CG  
4248 C CD  . PRO B 280 ? 0.8866 1.5812 1.7571 0.0424  0.0171  0.2803  259 PRO B CD  
4249 N N   . GLU B 281 ? 0.6844 1.3560 1.5699 0.0594  0.1022  0.2773  260 GLU B N   
4250 C CA  . GLU B 281 ? 0.6468 1.2963 1.5184 0.0667  0.1345  0.2717  260 GLU B CA  
4251 C C   . GLU B 281 ? 0.7233 1.3417 1.5445 0.0526  0.1423  0.2609  260 GLU B C   
4252 O O   . GLU B 281 ? 0.6805 1.2883 1.4950 0.0519  0.1691  0.2568  260 GLU B O   
4253 C CB  . GLU B 281 ? 0.6066 1.2353 1.4615 0.0845  0.1401  0.2696  260 GLU B CB  
4254 N N   . LEU B 282 ? 0.7976 1.4011 1.5831 0.0414  0.1197  0.2566  261 LEU B N   
4255 C CA  . LEU B 282 ? 0.8658 1.4433 1.6081 0.0273  0.1248  0.2487  261 LEU B CA  
4256 C C   . LEU B 282 ? 0.7746 1.3726 1.5437 0.0133  0.1314  0.2525  261 LEU B C   
4257 O O   . LEU B 282 ? 0.7957 1.3793 1.5466 0.0072  0.1516  0.2490  261 LEU B O   
4258 C CB  . LEU B 282 ? 0.8123 1.3699 1.5144 0.0195  0.0988  0.2438  261 LEU B CB  
4259 C CG  . LEU B 282 ? 0.8825 1.4056 1.5383 0.0288  0.0985  0.2359  261 LEU B CG  
4260 C CD1 . LEU B 282 ? 0.9906 1.5042 1.6233 0.0242  0.0693  0.2338  261 LEU B CD1 
4261 C CD2 . LEU B 282 ? 0.7647 1.2569 1.3768 0.0244  0.1176  0.2273  261 LEU B CD2 
4262 N N   . GLU B 283 ? 0.7961 1.4285 1.6087 0.0078  0.1149  0.2598  262 GLU B N   
4263 C CA  . GLU B 283 ? 0.7307 1.3844 1.5730 -0.0059 0.1213  0.2630  262 GLU B CA  
4264 C C   . GLU B 283 ? 0.6295 1.2936 1.5006 0.0005  0.1523  0.2660  262 GLU B C   
4265 O O   . GLU B 283 ? 0.7104 1.3752 1.5852 -0.0102 0.1678  0.2657  262 GLU B O   
4266 C CB  . GLU B 283 ? 0.7027 1.3943 1.5891 -0.0124 0.0973  0.2694  262 GLU B CB  
4267 C CG  . GLU B 283 ? 0.7331 1.4179 1.5957 -0.0160 0.0664  0.2670  262 GLU B CG  
4268 C CD  . GLU B 283 ? 0.7170 1.4219 1.5966 -0.0302 0.0432  0.2657  262 GLU B CD  
4269 O OE1 . GLU B 283 ? 0.6439 1.3715 1.5575 -0.0299 0.0444  0.2671  262 GLU B OE1 
4270 O OE2 . GLU B 283 ? 0.7405 1.4357 1.5960 -0.0419 0.0242  0.2616  262 GLU B OE2 
4271 N N   . GLN B 284 ? 0.5163 1.1881 1.4087 0.0179  0.1627  0.2689  263 GLN B N   
4272 C CA  . GLN B 284 ? 0.5759 1.2485 1.4855 0.0247  0.1938  0.2685  263 GLN B CA  
4273 C C   . GLN B 284 ? 0.6374 1.2790 1.5033 0.0196  0.2174  0.2614  263 GLN B C   
4274 O O   . GLN B 284 ? 0.5979 1.2435 1.4756 0.0147  0.2411  0.2619  263 GLN B O   
4275 C CB  . GLN B 284 ? 0.6164 1.2887 1.5397 0.0447  0.2002  0.2693  263 GLN B CB  
4276 C CG  . GLN B 284 ? 0.6364 1.3334 1.6056 0.0508  0.1982  0.2738  263 GLN B CG  
4277 C CD  . GLN B 284 ? 0.5333 1.2498 1.5195 0.0528  0.1653  0.2794  263 GLN B CD  
4278 O OE1 . GLN B 284 ? 0.4466 1.1856 1.4557 0.0431  0.1501  0.2817  263 GLN B OE1 
4279 N NE2 . GLN B 284 ? 0.5577 1.2648 1.5308 0.0651  0.1550  0.2810  263 GLN B NE2 
4280 N N   . HIS B 285 ? 0.6358 1.2433 1.4459 0.0205  0.2101  0.2538  264 HIS B N   
4281 C CA  . HIS B 285 ? 0.6087 1.1834 1.3684 0.0157  0.2288  0.2458  264 HIS B CA  
4282 C C   . HIS B 285 ? 0.5912 1.1629 1.3375 -0.0025 0.2268  0.2469  264 HIS B C   
4283 O O   . HIS B 285 ? 0.6124 1.1714 1.3398 -0.0076 0.2494  0.2449  264 HIS B O   
4284 C CB  . HIS B 285 ? 0.6813 1.2231 1.3880 0.0211  0.2187  0.2375  264 HIS B CB  
4285 C CG  . HIS B 285 ? 0.7113 1.2205 1.3623 0.0145  0.2319  0.2296  264 HIS B CG  
4286 N ND1 . HIS B 285 ? 0.8232 1.3204 1.4602 0.0190  0.2616  0.2245  264 HIS B ND1 
4287 C CD2 . HIS B 285 ? 0.7733 1.2601 1.3791 0.0038  0.2192  0.2262  264 HIS B CD2 
4288 C CE1 . HIS B 285 ? 0.8476 1.3178 1.4320 0.0111  0.2656  0.2186  264 HIS B CE1 
4289 N NE2 . HIS B 285 ? 0.8261 1.2896 1.3919 0.0023  0.2401  0.2201  264 HIS B NE2 
4290 N N   . PHE B 286 ? 0.6188 1.2017 1.3744 -0.0126 0.2010  0.2501  265 PHE B N   
4291 C CA  . PHE B 286 ? 0.6271 1.2069 1.3732 -0.0301 0.1988  0.2514  265 PHE B CA  
4292 C C   . PHE B 286 ? 0.5730 1.1862 1.3741 -0.0371 0.2077  0.2584  265 PHE B C   
4293 O O   . PHE B 286 ? 0.7060 1.3196 1.5138 -0.0392 0.2338  0.2598  265 PHE B O   
4294 C CB  . PHE B 286 ? 0.5618 1.1343 1.2889 -0.0390 0.1682  0.2498  265 PHE B CB  
4295 C CG  . PHE B 286 ? 0.5964 1.1363 1.2707 -0.0333 0.1584  0.2429  265 PHE B CG  
4296 C CD1 . PHE B 286 ? 0.6050 1.1129 1.2291 -0.0368 0.1693  0.2383  265 PHE B CD1 
4297 C CD2 . PHE B 286 ? 0.6767 1.2185 1.3517 -0.0244 0.1382  0.2413  265 PHE B CD2 
4298 C CE1 . PHE B 286 ? 0.6223 1.1016 1.1997 -0.0319 0.1601  0.2315  265 PHE B CE1 
4299 C CE2 . PHE B 286 ? 0.6119 1.1234 1.2396 -0.0194 0.1300  0.2345  265 PHE B CE2 
4300 C CZ  . PHE B 286 ? 0.6604 1.1410 1.2401 -0.0233 0.1409  0.2292  265 PHE B CZ  
4301 N N   . GLY B 288 ? 0.5542 1.2050 1.4260 -0.0633 0.2376  0.2660  267 GLY B N   
4302 C CA  . GLY B 288 ? 0.5233 1.1580 1.3761 -0.0710 0.2627  0.2662  267 GLY B CA  
4303 C C   . GLY B 288 ? 0.5968 1.2037 1.4005 -0.0789 0.2631  0.2676  267 GLY B C   
4304 O O   . GLY B 288 ? 0.5474 1.1437 1.3381 -0.0913 0.2713  0.2695  267 GLY B O   
4305 N N   . LYS B 289 ? 0.5955 1.1804 1.3585 -0.0705 0.2503  0.2623  268 LYS B N   
4306 C CA  . LYS B 289 ? 0.6164 1.1673 1.3214 -0.0762 0.2436  0.2595  268 LYS B CA  
4307 C C   . LYS B 289 ? 0.5916 1.1443 1.3001 -0.0896 0.2189  0.2606  268 LYS B C   
4308 O O   . LYS B 289 ? 0.6174 1.1955 1.3652 -0.0921 0.2013  0.2614  268 LYS B O   
4309 C CB  . LYS B 289 ? 0.5791 1.1078 1.2435 -0.0636 0.2363  0.2526  268 LYS B CB  
4310 N N   . MET B 290 ? 0.6078 1.1339 1.2751 -0.0985 0.2181  0.2609  269 MET B N   
4311 C CA  . MET B 290 ? 0.5960 1.1193 1.2633 -0.1120 0.1982  0.2615  269 MET B CA  
4312 C C   . MET B 290 ? 0.5808 1.0863 1.2155 -0.1082 0.1728  0.2555  269 MET B C   
4313 O O   . MET B 290 ? 0.5776 1.0725 1.1891 -0.0952 0.1710  0.2512  269 MET B O   
4314 C CB  . MET B 290 ? 0.6746 1.1787 1.3188 -0.1238 0.2116  0.2665  269 MET B CB  
4315 C CG  . MET B 290 ? 0.7491 1.2735 1.4353 -0.1349 0.2278  0.2727  269 MET B CG  
4316 S SD  . MET B 290 ? 0.9972 1.5595 1.7478 -0.1443 0.2095  0.2713  269 MET B SD  
4317 C CE  . MET B 290 ? 0.7671 1.3573 1.5567 -0.1306 0.2216  0.2697  269 MET B CE  
4318 N N   . TYR B 291 ? 0.5943 1.0958 1.2277 -0.1203 0.1540  0.2548  270 TYR B N   
4319 C CA  . TYR B 291 ? 0.5934 1.0762 1.1951 -0.1185 0.1308  0.2490  270 TYR B CA  
4320 C C   . TYR B 291 ? 0.6742 1.1220 1.2191 -0.1129 0.1369  0.2474  270 TYR B C   
4321 O O   . TYR B 291 ? 0.6294 1.0612 1.1459 -0.1068 0.1214  0.2417  270 TYR B O   
4322 C CB  . TYR B 291 ? 0.6042 1.0873 1.2145 -0.1344 0.1132  0.2481  270 TYR B CB  
4323 C CG  . TYR B 291 ? 0.7399 1.2575 1.4015 -0.1410 0.1000  0.2472  270 TYR B CG  
4324 C CD1 . TYR B 291 ? 0.6563 1.2036 1.3542 -0.1315 0.1019  0.2484  270 TYR B CD1 
4325 C CD2 . TYR B 291 ? 0.7239 1.2453 1.3982 -0.1570 0.0857  0.2450  270 TYR B CD2 
4326 C CE1 . TYR B 291 ? 0.7236 1.3051 1.4686 -0.1378 0.0885  0.2483  270 TYR B CE1 
4327 C CE2 . TYR B 291 ? 0.7563 1.3109 1.4760 -0.1644 0.0729  0.2433  270 TYR B CE2 
4328 C CZ  . TYR B 291 ? 0.7716 1.3572 1.5264 -0.1546 0.0735  0.2453  270 TYR B CZ  
4329 O OH  . TYR B 291 ? 0.7378 1.3502 1.5266 -0.1599 0.0586  0.2403  270 TYR B OH  
4330 N N   . GLY B 292 ? 0.5965 1.0326 1.1241 -0.1152 0.1587  0.2523  271 GLY B N   
4331 C CA  . GLY B 292 ? 0.5796 0.9858 1.0537 -0.1096 0.1650  0.2511  271 GLY B CA  
4332 C C   . GLY B 292 ? 0.6220 1.0269 1.0827 -0.0945 0.1742  0.2460  271 GLY B C   
4333 O O   . GLY B 292 ? 0.6111 0.9936 1.0296 -0.0880 0.1704  0.2410  271 GLY B O   
4334 N N   . HIS B 293 ? 0.6673 1.0959 1.1648 -0.0888 0.1873  0.2468  272 HIS B N   
4335 C CA  . HIS B 293 ? 0.5931 1.0223 1.0855 -0.0739 0.1944  0.2411  272 HIS B CA  
4336 C C   . HIS B 293 ? 0.5435 0.9698 1.0318 -0.0669 0.1701  0.2350  272 HIS B C   
4337 O O   . HIS B 293 ? 0.4722 0.8803 0.9275 -0.0575 0.1691  0.2285  272 HIS B O   
4338 C CB  . HIS B 293 ? 0.5404 0.9977 1.0803 -0.0693 0.2117  0.2439  272 HIS B CB  
4339 N N   . LEU B 294 ? 0.4996 0.9435 1.0200 -0.0721 0.1502  0.2365  273 LEU B N   
4340 C CA  . LEU B 294 ? 0.5099 0.9523 1.0272 -0.0660 0.1269  0.2316  273 LEU B CA  
4341 C C   . LEU B 294 ? 0.5565 0.9664 1.0224 -0.0673 0.1151  0.2262  273 LEU B C   
4342 O O   . LEU B 294 ? 0.5727 0.9688 1.0150 -0.0568 0.1103  0.2202  273 LEU B O   
4343 C CB  . LEU B 294 ? 0.4912 0.9585 1.0487 -0.0742 0.1075  0.2343  273 LEU B CB  
4344 C CG  . LEU B 294 ? 0.4089 0.8781 0.9660 -0.0693 0.0822  0.2302  273 LEU B CG  
4345 C CD1 . LEU B 294 ? 0.4038 0.8792 0.9684 -0.0519 0.0869  0.2291  273 LEU B CD1 
4346 C CD2 . LEU B 294 ? 0.5411 1.0374 1.1375 -0.0797 0.0641  0.2327  273 LEU B CD2 
4347 N N   . LYS B 295 ? 0.5076 0.9047 0.9570 -0.0800 0.1111  0.2286  274 LYS B N   
4348 C CA  . LYS B 295 ? 0.5428 0.9108 0.9478 -0.0818 0.0981  0.2242  274 LYS B CA  
4349 C C   . LYS B 295 ? 0.5407 0.8869 0.9035 -0.0724 0.1110  0.2203  274 LYS B C   
4350 O O   . LYS B 295 ? 0.5147 0.8422 0.8472 -0.0668 0.0999  0.2137  274 LYS B O   
4351 C CB  . LYS B 295 ? 0.5815 0.9405 0.9805 -0.0968 0.0950  0.2289  274 LYS B CB  
4352 C CG  . LYS B 295 ? 0.5958 0.9713 1.0290 -0.1074 0.0778  0.2293  274 LYS B CG  
4353 C CD  . LYS B 295 ? 0.6951 1.0619 1.1269 -0.1227 0.0784  0.2339  274 LYS B CD  
4354 C CE  . LYS B 295 ? 0.5976 0.9783 1.0593 -0.1342 0.0602  0.2317  274 LYS B CE  
4355 N NZ  . LYS B 295 ? 0.6153 0.9755 1.0606 -0.1467 0.0541  0.2323  274 LYS B NZ  
4356 N N   . GLY B 296 ? 0.6069 0.9553 0.9667 -0.0712 0.1347  0.2237  275 GLY B N   
4357 C CA  . GLY B 296 ? 0.5537 0.8843 0.8746 -0.0630 0.1480  0.2187  275 GLY B CA  
4358 C C   . GLY B 296 ? 0.5099 0.8423 0.8335 -0.0492 0.1467  0.2105  275 GLY B C   
4359 O O   . GLY B 296 ? 0.4824 0.7949 0.7710 -0.0434 0.1418  0.2030  275 GLY B O   
4360 N N   . GLU B 297 ? 0.4803 0.8370 0.8477 -0.0439 0.1507  0.2123  276 GLU B N   
4361 C CA  . GLU B 297 ? 0.5368 0.8964 0.9117 -0.0299 0.1513  0.2062  276 GLU B CA  
4362 C C   . GLU B 297 ? 0.5289 0.8756 0.8877 -0.0268 0.1269  0.2009  276 GLU B C   
4363 O O   . GLU B 297 ? 0.4496 0.7799 0.7828 -0.0177 0.1276  0.1931  276 GLU B O   
4364 C CB  . GLU B 297 ? 0.4578 0.8486 0.8879 -0.0253 0.1565  0.2113  276 GLU B CB  
4365 C CG  . GLU B 297 ? 0.6158 1.0206 1.0669 -0.0264 0.1834  0.2157  276 GLU B CG  
4366 C CD  . GLU B 297 ? 0.6354 1.0190 1.0443 -0.0268 0.2045  0.2115  276 GLU B CD  
4367 O OE1 . GLU B 297 ? 0.6930 1.0620 1.0770 -0.0175 0.2115  0.2032  276 GLU B OE1 
4368 O OE2 . GLU B 297 ? 0.7125 1.0943 1.1126 -0.0369 0.2142  0.2165  276 GLU B OE2 
4369 N N   . VAL B 298 ? 0.4695 0.8233 0.8430 -0.0350 0.1058  0.2045  277 VAL B N   
4370 C CA  . VAL B 298 ? 0.4603 0.8015 0.8180 -0.0336 0.0825  0.1996  277 VAL B CA  
4371 C C   . VAL B 298 ? 0.4911 0.8006 0.7969 -0.0334 0.0820  0.1927  277 VAL B C   
4372 O O   . VAL B 298 ? 0.4604 0.7561 0.7461 -0.0239 0.0799  0.1853  277 VAL B O   
4373 C CB  . VAL B 298 ? 0.4826 0.8339 0.8588 -0.0460 0.0624  0.2037  277 VAL B CB  
4374 C CG1 . VAL B 298 ? 0.4901 0.8252 0.8449 -0.0460 0.0394  0.1980  277 VAL B CG1 
4375 C CG2 . VAL B 298 ? 0.3973 0.7827 0.8257 -0.0460 0.0605  0.2097  277 VAL B CG2 
4376 N N   . ALA B 299 ? 0.4826 0.7810 0.7675 -0.0439 0.0850  0.1956  278 ALA B N   
4377 C CA  . ALA B 299 ? 0.5032 0.7736 0.7408 -0.0451 0.0813  0.1906  278 ALA B CA  
4378 C C   . ALA B 299 ? 0.4646 0.7233 0.6758 -0.0343 0.0952  0.1827  278 ALA B C   
4379 O O   . ALA B 299 ? 0.4552 0.6936 0.6342 -0.0308 0.0873  0.1750  278 ALA B O   
4380 C CB  . ALA B 299 ? 0.5788 0.8427 0.8023 -0.0565 0.0873  0.1974  278 ALA B CB  
4381 N N   . GLU B 300 ? 0.4641 0.7351 0.6891 -0.0293 0.1168  0.1836  279 GLU B N   
4382 C CA  . GLU B 300 ? 0.5343 0.7944 0.7352 -0.0200 0.1322  0.1747  279 GLU B CA  
4383 C C   . GLU B 300 ? 0.4659 0.7233 0.6739 -0.0085 0.1244  0.1672  279 GLU B C   
4384 O O   . GLU B 300 ? 0.4709 0.7097 0.6479 -0.0031 0.1257  0.1575  279 GLU B O   
4385 C CB  . GLU B 300 ? 0.5421 0.8162 0.7587 -0.0179 0.1587  0.1771  279 GLU B CB  
4386 C CG  . GLU B 300 ? 0.6386 0.9191 0.8563 -0.0290 0.1679  0.1865  279 GLU B CG  
4387 C CD  . GLU B 300 ? 0.9052 1.1797 1.0962 -0.0292 0.1926  0.1842  279 GLU B CD  
4388 O OE1 . GLU B 300 ? 1.0239 1.3082 1.2311 -0.0226 0.2124  0.1810  279 GLU B OE1 
4389 O OE2 . GLU B 300 ? 0.9011 1.1612 1.0548 -0.0360 0.1923  0.1857  279 GLU B OE2 
4390 N N   . ALA B 301 ? 0.4513 0.7277 0.7004 -0.0049 0.1165  0.1719  280 ALA B N   
4391 C CA  . ALA B 301 ? 0.4415 0.7170 0.7004 0.0069  0.1098  0.1670  280 ALA B CA  
4392 C C   . ALA B 301 ? 0.4298 0.6853 0.6616 0.0056  0.0878  0.1617  280 ALA B C   
4393 O O   . ALA B 301 ? 0.4314 0.6703 0.6423 0.0137  0.0884  0.1528  280 ALA B O   
4394 C CB  . ALA B 301 ? 0.4300 0.7334 0.7399 0.0106  0.1052  0.1753  280 ALA B CB  
4395 N N   . VAL B 302 ? 0.4193 0.6754 0.6517 -0.0050 0.0693  0.1664  281 VAL B N   
4396 C CA  . VAL B 302 ? 0.4082 0.6454 0.6167 -0.0070 0.0488  0.1614  281 VAL B CA  
4397 C C   . VAL B 302 ? 0.4738 0.6845 0.6363 -0.0069 0.0536  0.1528  281 VAL B C   
4398 O O   . VAL B 302 ? 0.4302 0.6235 0.5719 -0.0020 0.0452  0.1448  281 VAL B O   
4399 C CB  . VAL B 302 ? 0.4426 0.6846 0.6602 -0.0200 0.0307  0.1674  281 VAL B CB  
4400 C CG1 . VAL B 302 ? 0.4504 0.7150 0.7072 -0.0191 0.0182  0.1724  281 VAL B CG1 
4401 C CG2 . VAL B 302 ? 0.5615 0.8094 0.7813 -0.0305 0.0407  0.1741  281 VAL B CG2 
4402 N N   . SER B 303 ? 0.4941 0.7020 0.6398 -0.0127 0.0669  0.1546  282 SER B N   
4403 C CA  . SER B 303 ? 0.5419 0.7277 0.6437 -0.0130 0.0711  0.1469  282 SER B CA  
4404 C C   . SER B 303 ? 0.4989 0.6784 0.5896 -0.0019 0.0856  0.1365  282 SER B C   
4405 O O   . SER B 303 ? 0.5731 0.7332 0.6312 0.0002  0.0832  0.1268  282 SER B O   
4406 C CB  . SER B 303 ? 0.4946 0.6808 0.5811 -0.0217 0.0818  0.1529  282 SER B CB  
4407 O OG  . SER B 303 ? 0.5297 0.7147 0.6189 -0.0323 0.0676  0.1608  282 SER B OG  
4408 N N   . GLY B 304 ? 0.4599 0.6554 0.5784 0.0051  0.1016  0.1378  283 GLY B N   
4409 C CA  . GLY B 304 ? 0.4691 0.6581 0.5813 0.0159  0.1164  0.1275  283 GLY B CA  
4410 C C   . GLY B 304 ? 0.4970 0.6753 0.6097 0.0239  0.1029  0.1214  283 GLY B C   
4411 O O   . GLY B 304 ? 0.5191 0.6803 0.6079 0.0293  0.1083  0.1099  283 GLY B O   
4412 N N   . MET B 305 ? 0.5004 0.6887 0.6399 0.0242  0.0855  0.1289  284 MET B N   
4413 C CA  . MET B 305 ? 0.4344 0.6133 0.5748 0.0316  0.0720  0.1247  284 MET B CA  
4414 C C   . MET B 305 ? 0.4898 0.6450 0.5932 0.0260  0.0564  0.1178  284 MET B C   
4415 O O   . MET B 305 ? 0.5453 0.6833 0.6314 0.0323  0.0548  0.1084  284 MET B O   
4416 C CB  . MET B 305 ? 0.4101 0.6091 0.5889 0.0324  0.0576  0.1353  284 MET B CB  
4417 C CG  . MET B 305 ? 0.5230 0.7153 0.7059 0.0404  0.0439  0.1333  284 MET B CG  
4418 S SD  . MET B 305 ? 0.5216 0.7348 0.7365 0.0357  0.0198  0.1449  284 MET B SD  
4419 C CE  . MET B 305 ? 0.5040 0.7093 0.6969 0.0179  0.0067  0.1451  284 MET B CE  
4420 N N   . LEU B 306 ? 0.5164 0.6703 0.6089 0.0141  0.0455  0.1225  285 LEU B N   
4421 C CA  . LEU B 306 ? 0.4530 0.5853 0.5131 0.0086  0.0310  0.1169  285 LEU B CA  
4422 C C   . LEU B 306 ? 0.5359 0.6505 0.5594 0.0103  0.0422  0.1061  285 LEU B C   
4423 O O   . LEU B 306 ? 0.5033 0.5987 0.5022 0.0107  0.0330  0.0978  285 LEU B O   
4424 C CB  . LEU B 306 ? 0.4195 0.5546 0.4786 -0.0043 0.0200  0.1251  285 LEU B CB  
4425 C CG  . LEU B 306 ? 0.4732 0.6231 0.5637 -0.0093 0.0053  0.1337  285 LEU B CG  
4426 C CD1 . LEU B 306 ? 0.5353 0.6844 0.6221 -0.0227 -0.0025 0.1402  285 LEU B CD1 
4427 C CD2 . LEU B 306 ? 0.5666 0.7080 0.6580 -0.0053 -0.0113 0.1293  285 LEU B CD2 
4428 N N   . THR B 307 ? 0.4909 0.6124 0.5102 0.0108  0.0621  0.1055  286 THR B N   
4429 C CA  . THR B 307 ? 0.4714 0.5787 0.4546 0.0110  0.0731  0.0947  286 THR B CA  
4430 C C   . THR B 307 ? 0.5181 0.6127 0.4948 0.0210  0.0776  0.0816  286 THR B C   
4431 O O   . THR B 307 ? 0.5406 0.6175 0.4863 0.0203  0.0748  0.0710  286 THR B O   
4432 C CB  . THR B 307 ? 0.5898 0.7086 0.5714 0.0092  0.0949  0.0967  286 THR B CB  
4433 O OG1 . THR B 307 ? 0.5652 0.6925 0.5479 -0.0007 0.0908  0.1086  286 THR B OG1 
4434 C CG2 . THR B 307 ? 0.5233 0.6292 0.4674 0.0094  0.1073  0.0839  286 THR B CG2 
4435 N N   . GLU B 308 ? 0.5299 0.6336 0.5369 0.0304  0.0851  0.0826  287 GLU B N   
4436 C CA  . GLU B 308 ? 0.6155 0.7065 0.6202 0.0406  0.0901  0.0716  287 GLU B CA  
4437 C C   . GLU B 308 ? 0.6112 0.6866 0.6060 0.0407  0.0688  0.0689  287 GLU B C   
4438 O O   . GLU B 308 ? 0.5915 0.6485 0.5656 0.0444  0.0700  0.0567  287 GLU B O   
4439 C CB  . GLU B 308 ? 0.6377 0.7434 0.6813 0.0512  0.1018  0.0763  287 GLU B CB  
4440 C CG  . GLU B 308 ? 0.7571 0.8532 0.7982 0.0612  0.1219  0.0641  287 GLU B CG  
4441 C CD  . GLU B 308 ? 0.8069 0.8844 0.8403 0.0679  0.1128  0.0565  287 GLU B CD  
4442 O OE1 . GLU B 308 ? 0.7811 0.8636 0.8389 0.0737  0.1006  0.0648  287 GLU B OE1 
4443 O OE2 . GLU B 308 ? 0.7823 0.8408 0.7850 0.0670  0.1177  0.0423  287 GLU B OE2 
4444 N N   . LEU B 309 ? 0.4827 0.5651 0.4925 0.0363  0.0499  0.0794  288 LEU B N   
4445 C CA  . LEU B 309 ? 0.4828 0.5502 0.4821 0.0349  0.0298  0.0769  288 LEU B CA  
4446 C C   . LEU B 309 ? 0.4445 0.4936 0.4064 0.0271  0.0237  0.0692  288 LEU B C   
4447 O O   . LEU B 309 ? 0.4151 0.4455 0.3592 0.0290  0.0163  0.0601  288 LEU B O   
4448 C CB  . LEU B 309 ? 0.4726 0.5528 0.4951 0.0296  0.0121  0.0892  288 LEU B CB  
4449 C CG  . LEU B 309 ? 0.5449 0.6329 0.5949 0.0375  0.0047  0.0939  288 LEU B CG  
4450 C CD1 . LEU B 309 ? 0.5479 0.6552 0.6231 0.0304  -0.0095 0.1062  288 LEU B CD1 
4451 C CD2 . LEU B 309 ? 0.5323 0.5985 0.5646 0.0410  -0.0062 0.0858  288 LEU B CD2 
4452 N N   . GLN B 310 ? 0.4884 0.5432 0.4389 0.0186  0.0268  0.0733  289 GLN B N   
4453 C CA  . GLN B 310 ? 0.4493 0.4900 0.3683 0.0107  0.0179  0.0698  289 GLN B CA  
4454 C C   . GLN B 310 ? 0.4485 0.4756 0.3373 0.0134  0.0280  0.0555  289 GLN B C   
4455 O O   . GLN B 310 ? 0.4825 0.4937 0.3480 0.0106  0.0178  0.0486  289 GLN B O   
4456 C CB  . GLN B 310 ? 0.5012 0.5531 0.4190 0.0012  0.0185  0.0807  289 GLN B CB  
4457 C CG  . GLN B 310 ? 0.5210 0.5811 0.4621 -0.0049 0.0041  0.0928  289 GLN B CG  
4458 C CD  . GLN B 310 ? 0.6276 0.6996 0.5721 -0.0135 0.0081  0.1041  289 GLN B CD  
4459 O OE1 . GLN B 310 ? 0.6155 0.6900 0.5438 -0.0146 0.0216  0.1040  289 GLN B OE1 
4460 N NE2 . GLN B 310 ? 0.5797 0.6588 0.5449 -0.0201 -0.0030 0.1137  289 GLN B NE2 
4461 N N   . GLU B 311 ? 0.5384 0.5718 0.4275 0.0182  0.0483  0.0502  290 GLU B N   
4462 C CA  . GLU B 311 ? 0.5615 0.5825 0.4224 0.0199  0.0587  0.0347  290 GLU B CA  
4463 C C   . GLU B 311 ? 0.4754 0.4795 0.3355 0.0269  0.0537  0.0238  290 GLU B C   
4464 O O   . GLU B 311 ? 0.4711 0.4600 0.3051 0.0251  0.0500  0.0122  290 GLU B O   
4465 C CB  . GLU B 311 ? 0.6291 0.6601 0.4921 0.0230  0.0833  0.0304  290 GLU B CB  
4466 C CG  . GLU B 311 ? 0.6721 0.7128 0.5711 0.0326  0.0946  0.0338  290 GLU B CG  
4467 C CD  . GLU B 311 ? 0.7337 0.7619 0.6337 0.0421  0.1053  0.0199  290 GLU B CD  
4468 O OE1 . GLU B 311 ? 0.7020 0.7344 0.6326 0.0513  0.1084  0.0240  290 GLU B OE1 
4469 O OE2 . GLU B 311 ? 0.7782 0.7929 0.6494 0.0403  0.1107  0.0053  290 GLU B OE2 
4470 N N   . ARG B 312 ? 0.4536 0.4607 0.3426 0.0349  0.0530  0.0278  291 ARG B N   
4471 C CA  . ARG B 312 ? 0.4787 0.4692 0.3676 0.0412  0.0461  0.0201  291 ARG B CA  
4472 C C   . ARG B 312 ? 0.4407 0.4189 0.3149 0.0346  0.0241  0.0208  291 ARG B C   
4473 O O   . ARG B 312 ? 0.4315 0.3914 0.2881 0.0356  0.0200  0.0096  291 ARG B O   
4474 C CB  . ARG B 312 ? 0.4359 0.4344 0.3595 0.0506  0.0471  0.0279  291 ARG B CB  
4475 C CG  . ARG B 312 ? 0.5323 0.5384 0.4724 0.0596  0.0704  0.0249  291 ARG B CG  
4476 C CD  . ARG B 312 ? 0.5905 0.6112 0.5695 0.0680  0.0696  0.0375  291 ARG B CD  
4477 N NE  . ARG B 312 ? 0.4828 0.4935 0.4677 0.0727  0.0542  0.0393  291 ARG B NE  
4478 C CZ  . ARG B 312 ? 0.5151 0.5109 0.5000 0.0821  0.0607  0.0315  291 ARG B CZ  
4479 N NH1 . ARG B 312 ? 0.5683 0.5564 0.5477 0.0875  0.0823  0.0198  291 ARG B NH1 
4480 N NH2 . ARG B 312 ? 0.4621 0.4503 0.4526 0.0857  0.0460  0.0352  291 ARG B NH2 
4481 N N   . TYR B 313 ? 0.4237 0.4112 0.3059 0.0274  0.0108  0.0336  292 TYR B N   
4482 C CA  . TYR B 313 ? 0.4150 0.3907 0.2857 0.0206  -0.0090 0.0347  292 TYR B CA  
4483 C C   . TYR B 313 ? 0.4513 0.4139 0.2892 0.0157  -0.0098 0.0248  292 TYR B C   
4484 O O   . TYR B 313 ? 0.4143 0.3597 0.2390 0.0153  -0.0193 0.0168  292 TYR B O   
4485 C CB  . TYR B 313 ? 0.4188 0.4076 0.3037 0.0125  -0.0196 0.0493  292 TYR B CB  
4486 C CG  . TYR B 313 ? 0.4282 0.4046 0.2996 0.0041  -0.0371 0.0504  292 TYR B CG  
4487 C CD1 . TYR B 313 ? 0.3993 0.3655 0.2771 0.0039  -0.0516 0.0497  292 TYR B CD1 
4488 C CD2 . TYR B 313 ? 0.4138 0.3889 0.2662 -0.0035 -0.0384 0.0524  292 TYR B CD2 
4489 C CE1 . TYR B 313 ? 0.3794 0.3335 0.2464 -0.0040 -0.0660 0.0500  292 TYR B CE1 
4490 C CE2 . TYR B 313 ? 0.4891 0.4527 0.3320 -0.0106 -0.0534 0.0540  292 TYR B CE2 
4491 C CZ  . TYR B 313 ? 0.4759 0.4285 0.3267 -0.0109 -0.0666 0.0522  292 TYR B CZ  
4492 O OH  . TYR B 313 ? 0.4284 0.3686 0.2712 -0.0181 -0.0801 0.0531  292 TYR B OH  
4493 N N   . HIS B 314 ? 0.4459 0.4172 0.2702 0.0117  0.0001  0.0255  293 HIS B N   
4494 C CA  . HIS B 314 ? 0.4796 0.4420 0.2727 0.0063  -0.0023 0.0179  293 HIS B CA  
4495 C C   . HIS B 314 ? 0.4526 0.4022 0.2292 0.0112  0.0062  0.0000  293 HIS B C   
4496 O O   . HIS B 314 ? 0.4906 0.4278 0.2462 0.0081  -0.0016 -0.0085 293 HIS B O   
4497 C CB  . HIS B 314 ? 0.5551 0.5317 0.3369 0.0006  0.0063  0.0244  293 HIS B CB  
4498 C CG  . HIS B 314 ? 0.5233 0.5090 0.3161 -0.0061 -0.0033 0.0412  293 HIS B CG  
4499 N ND1 . HIS B 314 ? 0.5483 0.5256 0.3344 -0.0122 -0.0202 0.0463  293 HIS B ND1 
4500 C CD2 . HIS B 314 ? 0.4836 0.4856 0.2953 -0.0079 0.0026  0.0538  293 HIS B CD2 
4501 C CE1 . HIS B 314 ? 0.5143 0.5016 0.3144 -0.0176 -0.0239 0.0610  293 HIS B CE1 
4502 N NE2 . HIS B 314 ? 0.5149 0.5176 0.3305 -0.0153 -0.0105 0.0658  293 HIS B NE2 
4503 N N   . ARG B 315 ? 0.5012 0.4538 0.2885 0.0188  0.0230  -0.0062 294 ARG B N   
4504 C CA  A ARG B 315 ? 0.4981 0.4376 0.2722 0.0233  0.0332  -0.0241 294 ARG B CA  
4505 C CA  B ARG B 315 ? 0.5106 0.4500 0.2847 0.0233  0.0333  -0.0241 294 ARG B CA  
4506 C C   . ARG B 315 ? 0.5195 0.4403 0.2952 0.0265  0.0210  -0.0299 294 ARG B C   
4507 O O   . ARG B 315 ? 0.5882 0.4952 0.3439 0.0252  0.0199  -0.0437 294 ARG B O   
4508 C CB  A ARG B 315 ? 0.5246 0.4703 0.3149 0.0313  0.0548  -0.0281 294 ARG B CB  
4509 C CB  B ARG B 315 ? 0.5246 0.4703 0.3153 0.0314  0.0547  -0.0279 294 ARG B CB  
4510 C CG  A ARG B 315 ? 0.5607 0.4921 0.3403 0.0361  0.0683  -0.0473 294 ARG B CG  
4511 C CG  B ARG B 315 ? 0.5601 0.4918 0.3406 0.0363  0.0686  -0.0470 294 ARG B CG  
4512 C CD  A ARG B 315 ? 0.6319 0.5712 0.4206 0.0410  0.0936  -0.0527 294 ARG B CD  
4513 C CD  B ARG B 315 ? 0.6307 0.5702 0.4243 0.0423  0.0933  -0.0511 294 ARG B CD  
4514 N NE  A ARG B 315 ? 0.5777 0.5284 0.4009 0.0484  0.0983  -0.0391 294 ARG B NE  
4515 N NE  B ARG B 315 ? 0.5773 0.5279 0.4057 0.0496  0.0951  -0.0365 294 ARG B NE  
4516 C CZ  A ARG B 315 ? 0.5756 0.5450 0.4112 0.0460  0.1007  -0.0259 294 ARG B CZ  
4517 C CZ  B ARG B 315 ? 0.5543 0.4988 0.4063 0.0597  0.0973  -0.0353 294 ARG B CZ  
4518 N NH1 A ARG B 315 ? 0.5865 0.5647 0.4023 0.0366  0.0998  -0.0234 294 ARG B NH1 
4519 N NH1 B ARG B 315 ? 0.5153 0.4408 0.3604 0.0641  0.0992  -0.0479 294 ARG B NH1 
4520 N NH2 A ARG B 315 ? 0.5582 0.5385 0.4277 0.0533  0.1043  -0.0144 294 ARG B NH2 
4521 N NH2 B ARG B 315 ? 0.5545 0.5129 0.4382 0.0655  0.0977  -0.0206 294 ARG B NH2 
4522 N N   . PHE B 316 ? 0.4907 0.4115 0.2898 0.0302  0.0116  -0.0198 295 PHE B N   
4523 C CA  . PHE B 316 ? 0.5159 0.4190 0.3155 0.0326  -0.0004 -0.0241 295 PHE B CA  
4524 C C   . PHE B 316 ? 0.5211 0.4163 0.3049 0.0237  -0.0187 -0.0228 295 PHE B C   
4525 O O   . PHE B 316 ? 0.4536 0.3316 0.2241 0.0233  -0.0244 -0.0333 295 PHE B O   
4526 C CB  . PHE B 316 ? 0.4554 0.3627 0.2832 0.0385  -0.0056 -0.0130 295 PHE B CB  
4527 C CG  . PHE B 316 ? 0.4828 0.3970 0.3301 0.0488  0.0116  -0.0130 295 PHE B CG  
4528 C CD1 . PHE B 316 ? 0.5512 0.4563 0.3902 0.0543  0.0292  -0.0273 295 PHE B CD1 
4529 C CD2 . PHE B 316 ? 0.4707 0.4011 0.3463 0.0527  0.0107  0.0011  295 PHE B CD2 
4530 C CE1 . PHE B 316 ? 0.5580 0.4685 0.4174 0.0642  0.0464  -0.0269 295 PHE B CE1 
4531 C CE2 . PHE B 316 ? 0.4630 0.4006 0.3595 0.0629  0.0266  0.0024  295 PHE B CE2 
4532 C CZ  . PHE B 316 ? 0.5533 0.4802 0.4421 0.0689  0.0450  -0.0114 295 PHE B CZ  
4533 N N   . ARG B 317 ? 0.4979 0.4051 0.2842 0.0167  -0.0269 -0.0100 296 ARG B N   
4534 C CA  . ARG B 317 ? 0.4665 0.3663 0.2439 0.0088  -0.0442 -0.0062 296 ARG B CA  
4535 C C   . ARG B 317 ? 0.4997 0.3915 0.2498 0.0047  -0.0450 -0.0165 296 ARG B C   
4536 O O   . ARG B 317 ? 0.5003 0.3785 0.2420 0.0015  -0.0572 -0.0202 296 ARG B O   
4537 C CB  . ARG B 317 ? 0.4030 0.3178 0.1914 0.0024  -0.0502 0.0102  296 ARG B CB  
4538 C CG  . ARG B 317 ? 0.4245 0.3318 0.2068 -0.0058 -0.0664 0.0154  296 ARG B CG  
4539 C CD  . ARG B 317 ? 0.4656 0.3575 0.2557 -0.0054 -0.0786 0.0126  296 ARG B CD  
4540 N NE  . ARG B 317 ? 0.5050 0.3886 0.2909 -0.0135 -0.0926 0.0169  296 ARG B NE  
4541 C CZ  . ARG B 317 ? 0.4928 0.3622 0.2617 -0.0157 -0.0984 0.0091  296 ARG B CZ  
4542 N NH1 . ARG B 317 ? 0.4302 0.2923 0.1829 -0.0113 -0.0920 -0.0042 296 ARG B NH1 
4543 N NH2 . ARG B 317 ? 0.4682 0.3360 0.2492 -0.0218 -0.1049 0.0137  296 ARG B NH2 
4544 N N   . ASN B 318 ? 0.5470 0.4481 0.2833 0.0044  -0.0322 -0.0212 297 ASN B N   
4545 C CA  . ASN B 318 ? 0.4944 0.3917 0.2040 -0.0001 -0.0331 -0.0309 297 ASN B CA  
4546 C C   . ASN B 318 ? 0.5828 0.4651 0.2822 0.0039  -0.0277 -0.0501 297 ASN B C   
4547 O O   . ASN B 318 ? 0.5800 0.4581 0.2586 -0.0001 -0.0307 -0.0598 297 ASN B O   
4548 C CB  . ASN B 318 ? 0.5771 0.4913 0.2735 -0.0032 -0.0215 -0.0286 297 ASN B CB  
4549 C CG  . ASN B 318 ? 0.5679 0.4953 0.2697 -0.0087 -0.0278 -0.0098 297 ASN B CG  
4550 O OD1 . ASN B 318 ? 0.6122 0.5349 0.3170 -0.0128 -0.0431 -0.0012 297 ASN B OD1 
4551 N ND2 . ASN B 318 ? 0.5340 0.4771 0.2380 -0.0089 -0.0149 -0.0036 297 ASN B ND2 
4552 N N   . ASP B 319 ? 0.5419 0.4168 0.2565 0.0117  -0.0197 -0.0554 298 ASP B N   
4553 C CA  . ASP B 319 ? 0.4748 0.3338 0.1824 0.0160  -0.0127 -0.0734 298 ASP B CA  
4554 C C   . ASP B 319 ? 0.5496 0.3909 0.2640 0.0172  -0.0265 -0.0737 298 ASP B C   
4555 O O   . ASP B 319 ? 0.4812 0.3146 0.2119 0.0240  -0.0245 -0.0727 298 ASP B O   
4556 C CB  . ASP B 319 ? 0.5106 0.3713 0.2307 0.0243  0.0069  -0.0787 298 ASP B CB  
4557 C CG  . ASP B 319 ? 0.5764 0.4211 0.2883 0.0280  0.0178  -0.0985 298 ASP B CG  
4558 O OD1 . ASP B 319 ? 0.5862 0.4347 0.3084 0.0218  0.0085  -0.1020 298 ASP B OD1 
4559 O OD2 . ASP B 319 ? 0.5803 0.4251 0.3011 0.0345  0.0361  -0.1047 298 ASP B OD2 
4560 N N   . GLU B 320 ? 0.4506 0.3302 0.3423 0.0774  -0.0447 -0.0008 299 GLU B N   
4561 C CA  . GLU B 320 ? 0.5304 0.4127 0.4313 0.0735  -0.0454 -0.0009 299 GLU B CA  
4562 C C   . GLU B 320 ? 0.5045 0.4034 0.4262 0.0703  -0.0529 -0.0050 299 GLU B C   
4563 O O   . GLU B 320 ? 0.4310 0.3340 0.3632 0.0627  -0.0519 -0.0047 299 GLU B O   
4564 C CB  . GLU B 320 ? 0.5796 0.4526 0.4681 0.0840  -0.0459 -0.0002 299 GLU B CB  
4565 C CG  . GLU B 320 ? 0.7017 0.5519 0.5636 0.0890  -0.0378 0.0042  299 GLU B CG  
4566 C CD  . GLU B 320 ? 0.8228 0.6566 0.6747 0.0811  -0.0283 0.0078  299 GLU B CD  
4567 O OE1 . GLU B 320 ? 0.8658 0.7081 0.7327 0.0712  -0.0284 0.0069  299 GLU B OE1 
4568 O OE2 . GLU B 320 ? 0.7332 0.5435 0.5602 0.0846  -0.0205 0.0113  299 GLU B OE2 
4569 N N   . ALA B 321 ? 0.4030 0.3094 0.3289 0.0753  -0.0598 -0.0090 300 ALA B N   
4570 C CA  . ALA B 321 ? 0.3365 0.2544 0.2788 0.0706  -0.0655 -0.0131 300 ALA B CA  
4571 C C   . ALA B 321 ? 0.3428 0.2619 0.2918 0.0622  -0.0625 -0.0115 300 ALA B C   
4572 O O   . ALA B 321 ? 0.3887 0.3122 0.3487 0.0560  -0.0634 -0.0122 300 ALA B O   
4573 C CB  . ALA B 321 ? 0.4588 0.3815 0.4006 0.0762  -0.0727 -0.0184 300 ALA B CB  
4574 N N   . PHE B 322 ? 0.3402 0.2564 0.2822 0.0628  -0.0586 -0.0092 301 PHE B N   
4575 C CA  . PHE B 322 ? 0.2713 0.1925 0.2195 0.0569  -0.0559 -0.0077 301 PHE B CA  
4576 C C   . PHE B 322 ? 0.3142 0.2367 0.2666 0.0488  -0.0515 -0.0048 301 PHE B C   
4577 O O   . PHE B 322 ? 0.2582 0.1863 0.2195 0.0441  -0.0523 -0.0047 301 PHE B O   
4578 C CB  . PHE B 322 ? 0.3235 0.2455 0.2640 0.0594  -0.0519 -0.0062 301 PHE B CB  
4579 C CG  . PHE B 322 ? 0.2603 0.1921 0.2073 0.0548  -0.0488 -0.0046 301 PHE B CG  
4580 C CD1 . PHE B 322 ? 0.2844 0.2205 0.2382 0.0566  -0.0527 -0.0061 301 PHE B CD1 
4581 C CD2 . PHE B 322 ? 0.2732 0.2099 0.2181 0.0488  -0.0419 -0.0019 301 PHE B CD2 
4582 C CE1 . PHE B 322 ? 0.3454 0.2923 0.3040 0.0552  -0.0505 -0.0046 301 PHE B CE1 
4583 C CE2 . PHE B 322 ? 0.3201 0.2712 0.2724 0.0451  -0.0400 -0.0013 301 PHE B CE2 
4584 C CZ  . PHE B 322 ? 0.4180 0.3750 0.3772 0.0497  -0.0447 -0.0024 301 PHE B CZ  
4585 N N   . LEU B 323 ? 0.2984 0.2135 0.2419 0.0473  -0.0466 -0.0025 302 LEU B N   
4586 C CA  . LEU B 323 ? 0.3002 0.2142 0.2451 0.0388  -0.0420 -0.0004 302 LEU B CA  
4587 C C   . LEU B 323 ? 0.3099 0.2258 0.2643 0.0374  -0.0456 -0.0016 302 LEU B C   
4588 O O   . LEU B 323 ? 0.2604 0.1799 0.2207 0.0304  -0.0442 -0.0008 302 LEU B O   
4589 C CB  . LEU B 323 ? 0.2659 0.1658 0.1951 0.0378  -0.0351 0.0019  302 LEU B CB  
4590 C CG  . LEU B 323 ? 0.3515 0.2471 0.2688 0.0361  -0.0287 0.0035  302 LEU B CG  
4591 C CD1 . LEU B 323 ? 0.4347 0.3096 0.3322 0.0352  -0.0213 0.0059  302 LEU B CD1 
4592 C CD2 . LEU B 323 ? 0.3117 0.2212 0.2368 0.0262  -0.0254 0.0035  302 LEU B CD2 
4593 N N   . ASN B 324 ? 0.3612 0.2763 0.3171 0.0438  -0.0502 -0.0039 303 ASN B N   
4594 C CA  . ASN B 324 ? 0.3531 0.2729 0.3193 0.0417  -0.0532 -0.0057 303 ASN B CA  
4595 C C   . ASN B 324 ? 0.3471 0.2731 0.3236 0.0370  -0.0558 -0.0070 303 ASN B C   
4596 O O   . ASN B 324 ? 0.3464 0.2739 0.3292 0.0315  -0.0550 -0.0065 303 ASN B O   
4597 C CB  . ASN B 324 ? 0.4359 0.3591 0.4034 0.0492  -0.0579 -0.0091 303 ASN B CB  
4598 C CG  . ASN B 324 ? 0.4236 0.3415 0.3832 0.0544  -0.0552 -0.0076 303 ASN B CG  
4599 O OD1 . ASN B 324 ? 0.4899 0.3992 0.4437 0.0506  -0.0494 -0.0044 303 ASN B OD1 
4600 N ND2 . ASN B 324 ? 0.5370 0.4600 0.4952 0.0638  -0.0594 -0.0103 303 ASN B ND2 
4601 N N   . GLN B 325 ? 0.2461 0.1736 0.2222 0.0398  -0.0585 -0.0084 304 GLN B N   
4602 C CA  . GLN B 325 ? 0.2821 0.2110 0.2633 0.0372  -0.0601 -0.0091 304 GLN B CA  
4603 C C   . GLN B 325 ? 0.3238 0.2556 0.3055 0.0330  -0.0565 -0.0055 304 GLN B C   
4604 O O   . GLN B 325 ? 0.2613 0.1930 0.2469 0.0298  -0.0568 -0.0050 304 GLN B O   
4605 C CB  . GLN B 325 ? 0.2584 0.1856 0.2353 0.0427  -0.0629 -0.0111 304 GLN B CB  
4606 C CG  . GLN B 325 ? 0.3530 0.2770 0.3305 0.0422  -0.0640 -0.0116 304 GLN B CG  
4607 C CD  . GLN B 325 ? 0.3075 0.2290 0.2779 0.0492  -0.0649 -0.0125 304 GLN B CD  
4608 O OE1 . GLN B 325 ? 0.3562 0.2734 0.3224 0.0525  -0.0679 -0.0162 304 GLN B OE1 
4609 N NE2 . GLN B 325 ? 0.3628 0.2886 0.3314 0.0520  -0.0625 -0.0095 304 GLN B NE2 
4610 N N   . VAL B 326 ? 0.2522 0.1868 0.2291 0.0326  -0.0528 -0.0034 305 VAL B N   
4611 C CA  . VAL B 326 ? 0.2541 0.1961 0.2325 0.0276  -0.0498 -0.0011 305 VAL B CA  
4612 C C   . VAL B 326 ? 0.2989 0.2387 0.2795 0.0209  -0.0482 -0.0002 305 VAL B C   
4613 O O   . VAL B 326 ? 0.2332 0.1780 0.2170 0.0179  -0.0485 0.0007  305 VAL B O   
4614 C CB  . VAL B 326 ? 0.2786 0.2254 0.2515 0.0259  -0.0452 -0.0001 305 VAL B CB  
4615 C CG1 . VAL B 326 ? 0.3139 0.2722 0.2895 0.0185  -0.0423 0.0010  305 VAL B CG1 
4616 C CG2 . VAL B 326 ? 0.3249 0.2755 0.2956 0.0331  -0.0462 -0.0008 305 VAL B CG2 
4617 N N   . MET B 327 ? 0.2742 0.2062 0.2514 0.0198  -0.0464 -0.0004 306 MET B N   
4618 C CA  . MET B 327 ? 0.3580 0.2864 0.3355 0.0144  -0.0442 0.0004  306 MET B CA  
4619 C C   . MET B 327 ? 0.3075 0.2366 0.2927 0.0144  -0.0473 -0.0005 306 MET B C   
4620 O O   . MET B 327 ? 0.2611 0.1901 0.2475 0.0096  -0.0458 0.0005  306 MET B O   
4621 C CB  . MET B 327 ? 0.2971 0.2154 0.2668 0.0159  -0.0411 0.0005  306 MET B CB  
4622 C CG  . MET B 327 ? 0.2885 0.2002 0.2462 0.0128  -0.0355 0.0019  306 MET B CG  
4623 S SD  . MET B 327 ? 0.2942 0.1871 0.2361 0.0174  -0.0308 0.0028  306 MET B SD  
4624 C CE  . MET B 327 ? 0.3742 0.2705 0.3193 0.0304  -0.0369 0.0013  306 MET B CE  
4625 N N   . LYS B 328 ? 0.3528 0.2819 0.3419 0.0188  -0.0510 -0.0027 307 LYS B N   
4626 C CA  . LYS B 328 ? 0.4348 0.3630 0.4298 0.0167  -0.0527 -0.0041 307 LYS B CA  
4627 C C   . LYS B 328 ? 0.3952 0.3228 0.3889 0.0156  -0.0530 -0.0024 307 LYS B C   
4628 O O   . LYS B 328 ? 0.3278 0.2529 0.3222 0.0119  -0.0517 -0.0012 307 LYS B O   
4629 C CB  . LYS B 328 ? 0.4416 0.3700 0.4398 0.0197  -0.0563 -0.0080 307 LYS B CB  
4630 C CG  . LYS B 328 ? 0.3612 0.2879 0.3647 0.0150  -0.0568 -0.0103 307 LYS B CG  
4631 C CD  . LYS B 328 ? 0.5333 0.4665 0.5433 0.0149  -0.0590 -0.0150 307 LYS B CD  
4632 C CE  . LYS B 328 ? 0.5480 0.4804 0.5634 0.0074  -0.0582 -0.0181 307 LYS B CE  
4633 N NZ  . LYS B 328 ? 0.6271 0.5478 0.6364 0.0054  -0.0590 -0.0190 307 LYS B NZ  
4634 N N   . GLU B 329 ? 0.2757 0.2058 0.2664 0.0201  -0.0545 -0.0019 308 GLU B N   
4635 C CA  . GLU B 329 ? 0.3472 0.2779 0.3350 0.0223  -0.0550 -0.0001 308 GLU B CA  
4636 C C   . GLU B 329 ? 0.3518 0.2898 0.3394 0.0184  -0.0531 0.0024  308 GLU B C   
4637 O O   . GLU B 329 ? 0.2834 0.2195 0.2687 0.0184  -0.0533 0.0039  308 GLU B O   
4638 C CB  . GLU B 329 ? 0.3460 0.2808 0.3304 0.0294  -0.0565 -0.0003 308 GLU B CB  
4639 C CG  . GLU B 329 ? 0.3625 0.3015 0.3430 0.0347  -0.0571 0.0019  308 GLU B CG  
4640 C CD  . GLU B 329 ? 0.4117 0.3512 0.3873 0.0441  -0.0584 0.0013  308 GLU B CD  
4641 O OE1 . GLU B 329 ? 0.3315 0.2729 0.3078 0.0455  -0.0583 -0.0004 308 GLU B OE1 
4642 O OE2 . GLU B 329 ? 0.4088 0.3457 0.3781 0.0514  -0.0592 0.0028  308 GLU B OE2 
4643 N N   . GLY B 330 ? 0.2488 0.1936 0.2367 0.0148  -0.0509 0.0025  309 GLY B N   
4644 C CA  . GLY B 330 ? 0.2576 0.2102 0.2445 0.0093  -0.0491 0.0036  309 GLY B CA  
4645 C C   . GLY B 330 ? 0.2975 0.2425 0.2837 0.0042  -0.0477 0.0041  309 GLY B C   
4646 O O   . GLY B 330 ? 0.3144 0.2629 0.2987 0.0022  -0.0479 0.0052  309 GLY B O   
4647 N N   . ALA B 331 ? 0.2659 0.2016 0.2530 0.0031  -0.0462 0.0032  310 ALA B N   
4648 C CA  . ALA B 331 ? 0.2916 0.2211 0.2781 -0.0010 -0.0439 0.0035  310 ALA B CA  
4649 C C   . ALA B 331 ? 0.3096 0.2354 0.2973 -0.0002 -0.0451 0.0043  310 ALA B C   
4650 O O   . ALA B 331 ? 0.2768 0.2003 0.2614 -0.0034 -0.0435 0.0055  310 ALA B O   
4651 C CB  . ALA B 331 ? 0.2820 0.2058 0.2698 0.0000  -0.0422 0.0021  310 ALA B CB  
4652 N N   . GLU B 332 ? 0.2919 0.2147 0.2816 0.0037  -0.0473 0.0034  311 GLU B N   
4653 C CA  . GLU B 332 ? 0.3159 0.2302 0.3029 0.0037  -0.0471 0.0041  311 GLU B CA  
4654 C C   . GLU B 332 ? 0.3282 0.2433 0.3078 0.0070  -0.0481 0.0070  311 GLU B C   
4655 O O   . GLU B 332 ? 0.2985 0.2069 0.2726 0.0056  -0.0465 0.0089  311 GLU B O   
4656 C CB  . GLU B 332 ? 0.3351 0.2436 0.3233 0.0060  -0.0487 0.0017  311 GLU B CB  
4657 C CG  . GLU B 332 ? 0.4771 0.3851 0.4724 0.0012  -0.0474 -0.0017 311 GLU B CG  
4658 C CD  . GLU B 332 ? 0.5292 0.4461 0.5300 0.0011  -0.0468 -0.0025 311 GLU B CD  
4659 O OE1 . GLU B 332 ? 0.5194 0.4409 0.5217 0.0049  -0.0490 -0.0040 311 GLU B OE1 
4660 O OE2 . GLU B 332 ? 0.5425 0.4598 0.5436 -0.0021 -0.0436 -0.0014 311 GLU B OE2 
4661 N N   . LYS B 333 ? 0.2741 0.1986 0.2528 0.0122  -0.0507 0.0074  312 LYS B N   
4662 C CA  . LYS B 333 ? 0.2923 0.2231 0.2648 0.0170  -0.0524 0.0098  312 LYS B CA  
4663 C C   . LYS B 333 ? 0.3029 0.2415 0.2749 0.0113  -0.0515 0.0104  312 LYS B C   
4664 O O   . LYS B 333 ? 0.2540 0.1920 0.2190 0.0136  -0.0522 0.0124  312 LYS B O   
4665 C CB  . LYS B 333 ? 0.2835 0.2283 0.2575 0.0236  -0.0549 0.0094  312 LYS B CB  
4666 C CG  . LYS B 333 ? 0.3129 0.2707 0.2821 0.0306  -0.0574 0.0112  312 LYS B CG  
4667 C CD  . LYS B 333 ? 0.3442 0.3118 0.3129 0.0409  -0.0595 0.0111  312 LYS B CD  
4668 C CE  . LYS B 333 ? 0.3659 0.3459 0.3433 0.0367  -0.0584 0.0086  312 LYS B CE  
4669 N NZ  . LYS B 333 ? 0.3822 0.3736 0.3591 0.0471  -0.0597 0.0084  312 LYS B NZ  
4670 N N   . ALA B 334 ? 0.2217 0.1654 0.1984 0.0041  -0.0496 0.0086  313 ALA B N   
4671 C CA  . ALA B 334 ? 0.2489 0.1973 0.2228 -0.0027 -0.0482 0.0083  313 ALA B CA  
4672 C C   . ALA B 334 ? 0.2659 0.2013 0.2354 -0.0050 -0.0460 0.0096  313 ALA B C   
4673 O O   . ALA B 334 ? 0.2388 0.1763 0.2021 -0.0060 -0.0465 0.0106  313 ALA B O   
4674 C CB  . ALA B 334 ? 0.2576 0.2075 0.2334 -0.0098 -0.0453 0.0061  313 ALA B CB  
4675 N N   . SER B 335 ? 0.3056 0.2292 0.2781 -0.0057 -0.0434 0.0093  314 SER B N   
4676 C CA  . SER B 335 ? 0.2938 0.2068 0.2632 -0.0087 -0.0400 0.0101  314 SER B CA  
4677 C C   . SER B 335 ? 0.3246 0.2301 0.2861 -0.0050 -0.0405 0.0127  314 SER B C   
4678 O O   . SER B 335 ? 0.3165 0.2158 0.2708 -0.0070 -0.0382 0.0143  314 SER B O   
4679 C CB  . SER B 335 ? 0.3371 0.2444 0.3134 -0.0103 -0.0373 0.0084  314 SER B CB  
4680 O OG  . SER B 335 ? 0.3628 0.2730 0.3417 -0.0125 -0.0355 0.0067  314 SER B OG  
4681 N N   . ALA B 336 ? 0.3021 0.2052 0.2622 0.0012  -0.0430 0.0134  315 ALA B N   
4682 C CA  . ALA B 336 ? 0.3425 0.2340 0.2904 0.0067  -0.0429 0.0164  315 ALA B CA  
4683 C C   . ALA B 336 ? 0.3615 0.2615 0.3010 0.0108  -0.0455 0.0186  315 ALA B C   
4684 O O   . ALA B 336 ? 0.4438 0.3336 0.3718 0.0122  -0.0438 0.0212  315 ALA B O   
4685 C CB  . ALA B 336 ? 0.3275 0.2136 0.2726 0.0141  -0.0449 0.0165  315 ALA B CB  
4686 N N   . HIS B 337 ? 0.3049 0.2249 0.2497 0.0122  -0.0495 0.0172  316 HIS B N   
4687 C CA  . HIS B 337 ? 0.3301 0.2644 0.2692 0.0149  -0.0529 0.0178  316 HIS B CA  
4688 C C   . HIS B 337 ? 0.3697 0.3028 0.3066 0.0058  -0.0505 0.0168  316 HIS B C   
4689 O O   . HIS B 337 ? 0.3245 0.2555 0.2506 0.0080  -0.0512 0.0186  316 HIS B O   
4690 C CB  . HIS B 337 ? 0.3792 0.3380 0.3266 0.0161  -0.0568 0.0153  316 HIS B CB  
4691 C CG  . HIS B 337 ? 0.4071 0.3873 0.3504 0.0201  -0.0614 0.0150  316 HIS B CG  
4692 N ND1 . HIS B 337 ? 0.4975 0.4737 0.4285 0.0247  -0.0628 0.0173  316 HIS B ND1 
4693 C CD2 . HIS B 337 ? 0.4286 0.4368 0.3787 0.0201  -0.0649 0.0122  316 HIS B CD2 
4694 C CE1 . HIS B 337 ? 0.4778 0.4801 0.4085 0.0282  -0.0680 0.0157  316 HIS B CE1 
4695 N NE2 . HIS B 337 ? 0.4324 0.4558 0.3756 0.0247  -0.0691 0.0123  316 HIS B NE2 
4696 N N   . ALA B 338 ? 0.3100 0.2418 0.2548 -0.0034 -0.0473 0.0143  317 ALA B N   
4697 C CA  . ALA B 338 ? 0.3317 0.2612 0.2728 -0.0116 -0.0446 0.0129  317 ALA B CA  
4698 C C   . ALA B 338 ? 0.3457 0.2578 0.2788 -0.0116 -0.0405 0.0152  317 ALA B C   
4699 O O   . ALA B 338 ? 0.3309 0.2413 0.2554 -0.0146 -0.0396 0.0152  317 ALA B O   
4700 C CB  . ALA B 338 ? 0.3348 0.2629 0.2830 -0.0188 -0.0413 0.0101  317 ALA B CB  
4701 N N   . SER B 339 ? 0.3526 0.2520 0.2879 -0.0093 -0.0376 0.0168  318 SER B N   
4702 C CA  . SER B 339 ? 0.3966 0.2800 0.3253 -0.0112 -0.0322 0.0187  318 SER B CA  
4703 C C   . SER B 339 ? 0.4356 0.3122 0.3483 -0.0058 -0.0332 0.0222  318 SER B C   
4704 O O   . SER B 339 ? 0.4073 0.2731 0.3108 -0.0082 -0.0289 0.0236  318 SER B O   
4705 C CB  . SER B 339 ? 0.4412 0.3150 0.3763 -0.0120 -0.0288 0.0185  318 SER B CB  
4706 O OG  . SER B 339 ? 0.5374 0.4077 0.4694 -0.0056 -0.0319 0.0198  318 SER B OG  
4707 N N   . LYS B 340 ? 0.4698 0.3523 0.3776 0.0028  -0.0386 0.0237  319 LYS B N   
4708 C CA  . LYS B 340 ? 0.3869 0.2643 0.2772 0.0107  -0.0404 0.0271  319 LYS B CA  
4709 C C   . LYS B 340 ? 0.4763 0.3638 0.3615 0.0071  -0.0421 0.0258  319 LYS B C   
4710 O O   . LYS B 340 ? 0.4213 0.2969 0.2917 0.0085  -0.0397 0.0283  319 LYS B O   
4711 C CB  . LYS B 340 ? 0.4824 0.3691 0.3691 0.0228  -0.0465 0.0285  319 LYS B CB  
4712 C CG  . LYS B 340 ? 0.5223 0.3936 0.4084 0.0275  -0.0444 0.0299  319 LYS B CG  
4713 C CD  . LYS B 340 ? 0.5843 0.4674 0.4687 0.0401  -0.0503 0.0306  319 LYS B CD  
4714 C CE  . LYS B 340 ? 0.6657 0.5286 0.5456 0.0448  -0.0476 0.0318  319 LYS B CE  
4715 N NZ  . LYS B 340 ? 0.7991 0.6769 0.6831 0.0550  -0.0527 0.0310  319 LYS B NZ  
4716 N N   . THR B 341 ? 0.3546 0.2622 0.2501 0.0014  -0.0455 0.0216  320 THR B N   
4717 C CA  . THR B 341 ? 0.3743 0.2907 0.2636 -0.0040 -0.0470 0.0192  320 THR B CA  
4718 C C   . THR B 341 ? 0.3577 0.2581 0.2444 -0.0126 -0.0400 0.0185  320 THR B C   
4719 O O   . THR B 341 ? 0.3385 0.2336 0.2124 -0.0138 -0.0389 0.0189  320 THR B O   
4720 C CB  . THR B 341 ? 0.3774 0.3178 0.2766 -0.0097 -0.0515 0.0142  320 THR B CB  
4721 O OG1 . THR B 341 ? 0.4469 0.4073 0.3471 -0.0006 -0.0584 0.0145  320 THR B OG1 
4722 C CG2 . THR B 341 ? 0.3916 0.3376 0.2839 -0.0190 -0.0518 0.0103  320 THR B CG2 
4723 N N   . LEU B 342 ? 0.3803 0.2741 0.2784 -0.0176 -0.0351 0.0174  321 LEU B N   
4724 C CA  . LEU B 342 ? 0.3446 0.2262 0.2408 -0.0240 -0.0283 0.0165  321 LEU B CA  
4725 C C   . LEU B 342 ? 0.3581 0.2233 0.2440 -0.0216 -0.0231 0.0201  321 LEU B C   
4726 O O   . LEU B 342 ? 0.3251 0.1826 0.2018 -0.0248 -0.0189 0.0199  321 LEU B O   
4727 C CB  . LEU B 342 ? 0.3308 0.2109 0.2409 -0.0269 -0.0246 0.0148  321 LEU B CB  
4728 C CG  . LEU B 342 ? 0.3680 0.2388 0.2762 -0.0315 -0.0178 0.0133  321 LEU B CG  
4729 C CD1 . LEU B 342 ? 0.3870 0.2598 0.2879 -0.0369 -0.0184 0.0099  321 LEU B CD1 
4730 C CD2 . LEU B 342 ? 0.3743 0.2442 0.2955 -0.0310 -0.0141 0.0125  321 LEU B CD2 
4731 N N   . LYS B 343 ? 0.4053 0.2630 0.2910 -0.0165 -0.0224 0.0233  322 LYS B N   
4732 C CA  . LYS B 343 ? 0.4159 0.2551 0.2900 -0.0159 -0.0158 0.0268  322 LYS B CA  
4733 C C   . LYS B 343 ? 0.4355 0.2698 0.2894 -0.0112 -0.0177 0.0294  322 LYS B C   
4734 O O   . LYS B 343 ? 0.4107 0.2308 0.2527 -0.0130 -0.0113 0.0313  322 LYS B O   
4735 C CB  . LYS B 343 ? 0.4822 0.3112 0.3576 -0.0129 -0.0141 0.0291  322 LYS B CB  
4736 C CG  . LYS B 343 ? 0.6069 0.4312 0.4950 -0.0202 -0.0069 0.0273  322 LYS B CG  
4737 C CD  . LYS B 343 ? 0.6343 0.4742 0.5408 -0.0246 -0.0077 0.0228  322 LYS B CD  
4738 C CE  . LYS B 343 ? 0.6192 0.4705 0.5376 -0.0219 -0.0141 0.0209  322 LYS B CE  
4739 N NZ  . LYS B 343 ? 0.6143 0.4759 0.5482 -0.0252 -0.0134 0.0172  322 LYS B NZ  
4740 N N   . ALA B 344 ? 0.3655 0.2130 0.2150 -0.0049 -0.0262 0.0293  323 ALA B N   
4741 C CA  . ALA B 344 ? 0.4149 0.2629 0.2455 0.0004  -0.0296 0.0307  323 ALA B CA  
4742 C C   . ALA B 344 ? 0.4349 0.2883 0.2633 -0.0078 -0.0289 0.0268  323 ALA B C   
4743 O O   . ALA B 344 ? 0.4358 0.2809 0.2469 -0.0065 -0.0276 0.0282  323 ALA B O   
4744 C CB  . ALA B 344 ? 0.3779 0.2447 0.2069 0.0098  -0.0396 0.0306  323 ALA B CB  
4745 N N   . VAL B 345 ? 0.3517 0.2164 0.1948 -0.0160 -0.0295 0.0220  324 VAL B N   
4746 C CA  . VAL B 345 ? 0.3469 0.2115 0.1855 -0.0244 -0.0274 0.0180  324 VAL B CA  
4747 C C   . VAL B 345 ? 0.4058 0.2502 0.2389 -0.0269 -0.0174 0.0198  324 VAL B C   
4748 O O   . VAL B 345 ? 0.3995 0.2361 0.2179 -0.0287 -0.0149 0.0192  324 VAL B O   
4749 C CB  . VAL B 345 ? 0.3231 0.1991 0.1755 -0.0320 -0.0288 0.0130  324 VAL B CB  
4750 C CG1 . VAL B 345 ? 0.3643 0.2323 0.2092 -0.0406 -0.0242 0.0090  324 VAL B CG1 
4751 C CG2 . VAL B 345 ? 0.3694 0.2684 0.2257 -0.0316 -0.0378 0.0103  324 VAL B CG2 
4752 N N   . TYR B 346 ? 0.3650 0.2027 0.2103 -0.0272 -0.0117 0.0214  325 TYR B N   
4753 C CA  . TYR B 346 ? 0.3835 0.2073 0.2266 -0.0298 -0.0017 0.0224  325 TYR B CA  
4754 C C   . TYR B 346 ? 0.4572 0.2665 0.2823 -0.0263 0.0021  0.0269  325 TYR B C   
4755 O O   . TYR B 346 ? 0.4243 0.2233 0.2390 -0.0285 0.0089  0.0272  325 TYR B O   
4756 C CB  . TYR B 346 ? 0.3741 0.1989 0.2354 -0.0311 0.0027  0.0224  325 TYR B CB  
4757 C CG  . TYR B 346 ? 0.3850 0.2186 0.2601 -0.0339 0.0027  0.0184  325 TYR B CG  
4758 C CD1 . TYR B 346 ? 0.4236 0.2607 0.2936 -0.0364 -0.0005 0.0151  325 TYR B CD1 
4759 C CD2 . TYR B 346 ? 0.4089 0.2462 0.3000 -0.0342 0.0063  0.0175  325 TYR B CD2 
4760 C CE1 . TYR B 346 ? 0.4635 0.3032 0.3415 -0.0381 0.0007  0.0120  325 TYR B CE1 
4761 C CE2 . TYR B 346 ? 0.3562 0.1999 0.2569 -0.0345 0.0064  0.0144  325 TYR B CE2 
4762 C CZ  . TYR B 346 ? 0.4041 0.2469 0.2970 -0.0360 0.0040  0.0120  325 TYR B CZ  
4763 O OH  . TYR B 346 ? 0.3967 0.2408 0.2948 -0.0354 0.0051  0.0094  325 TYR B OH  
4764 N N   . GLU B 347 ? 0.4896 0.2960 0.3085 -0.0200 -0.0017 0.0305  326 GLU B N   
4765 C CA  . GLU B 347 ? 0.5106 0.2997 0.3076 -0.0152 0.0018  0.0354  326 GLU B CA  
4766 C C   . GLU B 347 ? 0.5356 0.3251 0.3144 -0.0137 -0.0010 0.0345  326 GLU B C   
4767 O O   . GLU B 347 ? 0.4484 0.2225 0.2114 -0.0142 0.0060  0.0367  326 GLU B O   
4768 C CB  . GLU B 347 ? 0.5341 0.3194 0.3237 -0.0060 -0.0032 0.0393  326 GLU B CB  
4769 C CG  . GLU B 347 ? 0.7111 0.4770 0.4990 -0.0065 0.0048  0.0429  326 GLU B CG  
4770 C CD  . GLU B 347 ? 0.7878 0.5325 0.5614 -0.0108 0.0164  0.0457  326 GLU B CD  
4771 O OE1 . GLU B 347 ? 0.8833 0.6205 0.6365 -0.0068 0.0167  0.0478  326 GLU B OE1 
4772 O OE2 . GLU B 347 ? 0.8437 0.5806 0.6261 -0.0185 0.0255  0.0454  326 GLU B OE2 
4773 N N   . ALA B 348 ? 0.4686 0.2767 0.2492 -0.0126 -0.0111 0.0309  327 ALA B N   
4774 C CA  . ALA B 348 ? 0.5002 0.3117 0.2631 -0.0119 -0.0154 0.0290  327 ALA B CA  
4775 C C   . ALA B 348 ? 0.4780 0.2828 0.2384 -0.0207 -0.0089 0.0253  327 ALA B C   
4776 O O   . ALA B 348 ? 0.4857 0.2814 0.2264 -0.0201 -0.0071 0.0254  327 ALA B O   
4777 C CB  . ALA B 348 ? 0.4979 0.3349 0.2658 -0.0107 -0.0275 0.0248  327 ALA B CB  
4778 N N   . ILE B 349 ? 0.4675 0.2754 0.2456 -0.0276 -0.0052 0.0221  328 ILE B N   
4779 C CA  . ILE B 349 ? 0.5272 0.3271 0.3013 -0.0340 0.0014  0.0186  328 ILE B CA  
4780 C C   . ILE B 349 ? 0.4664 0.2483 0.2316 -0.0326 0.0125  0.0223  328 ILE B C   
4781 O O   . ILE B 349 ? 0.4857 0.2578 0.2366 -0.0345 0.0174  0.0207  328 ILE B O   
4782 C CB  . ILE B 349 ? 0.4949 0.3008 0.2880 -0.0390 0.0029  0.0150  328 ILE B CB  
4783 C CG1 . ILE B 349 ? 0.5887 0.4067 0.3819 -0.0445 -0.0048 0.0094  328 ILE B CG1 
4784 C CG2 . ILE B 349 ? 0.5640 0.3575 0.3552 -0.0413 0.0133  0.0137  328 ILE B CG2 
4785 C CD1 . ILE B 349 ? 0.5794 0.4139 0.3709 -0.0421 -0.0154 0.0093  328 ILE B CD1 
4786 N N   . GLY B 350 ? 0.4523 0.2294 0.2251 -0.0300 0.0173  0.0268  329 GLY B N   
4787 C CA  . GLY B 350 ? 0.4778 0.2397 0.2436 -0.0304 0.0291  0.0300  329 GLY B CA  
4788 C C   . GLY B 350 ? 0.4769 0.2423 0.2636 -0.0342 0.0372  0.0292  329 GLY B C   
4789 O O   . GLY B 350 ? 0.4808 0.2381 0.2652 -0.0362 0.0481  0.0307  329 GLY B O   
4790 N N   . PHE B 351 ? 0.4422 0.2214 0.2493 -0.0352 0.0322  0.0266  330 PHE B N   
4791 C CA  . PHE B 351 ? 0.4198 0.2058 0.2474 -0.0377 0.0383  0.0255  330 PHE B CA  
4792 C C   . PHE B 351 ? 0.4118 0.1917 0.2415 -0.0395 0.0436  0.0290  330 PHE B C   
4793 O O   . PHE B 351 ? 0.4528 0.2253 0.2734 -0.0370 0.0391  0.0322  330 PHE B O   
4794 C CB  . PHE B 351 ? 0.4181 0.2186 0.2641 -0.0374 0.0309  0.0224  330 PHE B CB  
4795 C CG  . PHE B 351 ? 0.4126 0.2164 0.2571 -0.0374 0.0283  0.0185  330 PHE B CG  
4796 C CD1 . PHE B 351 ? 0.4415 0.2359 0.2709 -0.0378 0.0333  0.0171  330 PHE B CD1 
4797 C CD2 . PHE B 351 ? 0.4699 0.2835 0.3259 -0.0374 0.0217  0.0160  330 PHE B CD2 
4798 C CE1 . PHE B 351 ? 0.4163 0.2091 0.2409 -0.0386 0.0318  0.0132  330 PHE B CE1 
4799 C CE2 . PHE B 351 ? 0.4338 0.2460 0.2852 -0.0385 0.0206  0.0124  330 PHE B CE2 
4800 C CZ  . PHE B 351 ? 0.4562 0.2570 0.2913 -0.0393 0.0258  0.0109  330 PHE B CZ  
4801 N N   . VAL B 352 ? 0.4648 0.2477 0.3054 -0.0437 0.0536  0.0280  331 VAL B N   
4802 C CA  . VAL B 352 ? 0.4445 0.2245 0.2916 -0.0485 0.0587  0.0295  331 VAL B CA  
4803 C C   . VAL B 352 ? 0.5169 0.3068 0.3797 -0.0479 0.0501  0.0280  331 VAL B C   
4804 O O   . VAL B 352 ? 0.5165 0.3227 0.3964 -0.0467 0.0457  0.0242  331 VAL B O   
4805 C CB  . VAL B 352 ? 0.5208 0.3096 0.3808 -0.0545 0.0707  0.0271  331 VAL B CB  
4806 C CG1 . VAL B 352 ? 0.4951 0.2841 0.3649 -0.0624 0.0755  0.0268  331 VAL B CG1 
4807 C CG2 . VAL B 352 ? 0.5569 0.3340 0.3993 -0.0551 0.0807  0.0292  331 VAL B CG2 
4808 N N   . ALA B 353 ? 0.4424 0.2201 0.2967 -0.0476 0.0479  0.0310  332 ALA B N   
4809 C CA  . ALA B 353 ? 0.4417 0.2266 0.3087 -0.0467 0.0405  0.0296  332 ALA B CA  
4810 C C   . ALA B 353 ? 0.4593 0.2577 0.3487 -0.0537 0.0450  0.0253  332 ALA B C   
4811 O O   . ALA B 353 ? 0.4337 0.2292 0.3246 -0.0613 0.0553  0.0247  332 ALA B O   
4812 C CB  . ALA B 353 ? 0.5187 0.2840 0.3684 -0.0440 0.0391  0.0339  332 ALA B CB  
4813 N N   . LYS B 354 ? 0.4920 0.3066 0.3985 -0.0515 0.0375  0.0220  333 LYS B N   
4814 C CA  . LYS B 354 ? 0.4588 0.2896 0.3868 -0.0566 0.0398  0.0173  333 LYS B CA  
4815 C C   . LYS B 354 ? 0.5026 0.3228 0.4288 -0.0644 0.0442  0.0172  333 LYS B C   
4816 O O   . LYS B 354 ? 0.4308 0.2380 0.3478 -0.0618 0.0390  0.0193  333 LYS B O   
4817 C CB  . LYS B 354 ? 0.5139 0.3595 0.4556 -0.0512 0.0300  0.0146  333 LYS B CB  
4818 C CG  . LYS B 354 ? 0.4501 0.3152 0.4135 -0.0542 0.0306  0.0094  333 LYS B CG  
4819 C CD  . LYS B 354 ? 0.5581 0.4329 0.5302 -0.0480 0.0208  0.0077  333 LYS B CD  
4820 C CE  . LYS B 354 ? 0.6081 0.5039 0.6004 -0.0488 0.0203  0.0024  333 LYS B CE  
4821 N NZ  . LYS B 354 ? 0.7654 0.6685 0.7631 -0.0415 0.0116  0.0013  333 LYS B NZ  
4822 N N   . PRO B 355 ? 0.5343 0.3591 0.4679 -0.0743 0.0542  0.0145  334 PRO B N   
4823 C CA  . PRO B 355 ? 0.5216 0.3324 0.4501 -0.0845 0.0600  0.0139  334 PRO B CA  
4824 C C   . PRO B 355 ? 0.6000 0.4232 0.5453 -0.0880 0.0547  0.0086  334 PRO B C   
4825 O O   . PRO B 355 ? 0.6296 0.4756 0.5929 -0.0829 0.0473  0.0052  334 PRO B O   
4826 C CB  . PRO B 355 ? 0.6136 0.4297 0.5461 -0.0953 0.0734  0.0118  334 PRO B CB  
4827 C CG  . PRO B 355 ? 0.6650 0.5102 0.6167 -0.0903 0.0720  0.0085  334 PRO B CG  
4828 C CD  . PRO B 355 ? 0.6072 0.4492 0.5517 -0.0768 0.0618  0.0118  334 PRO B CD  
4829 O OXT . PRO B 355 ? 0.7931 0.6013 0.7317 -0.0961 0.0579  0.0076  334 PRO B OXT 
# 
